data_9CW1
# 
_entry.id   9CW1 
# 
_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   9CW1         pdb_00009cw1 10.2210/pdb9cw1/pdb 
WWPDB D_1000286255 ?            ?                   
# 
_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                        9CW1 
_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'                                                 48996.781 4    1.14.13.39 
'R354A, G357D' ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                              616.487   4    ?          ? ? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                    241.247   4    ?          ? ? ? 
4 non-polymer syn '(6M)-6-{2,3-difluoro-5-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' 277.312   4    ?          ? ? ? 
5 non-polymer syn GLYCEROL                                                                       92.094    6    ?          ? ? ? 
6 non-polymer syn 'ZINC ION'                                                                     65.409    2    ?          ? ? ? 
7 water       nat water                                                                          18.015    1263 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1,bNOS' 
# 
_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       
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVATKDQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKLV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVATKDQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKLV
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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 '(6M)-6-{2,3-difluoro-5-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' A1A0C 
5 GLYCEROL                                                                       GOL   
6 'ZINC ION'                                                                     ZN    
7 water                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  GLU 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  TYR 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  HIS n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  ALA n 
1 47  ARG n 
1 48  ARG 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  ILE 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  GLU 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  ASP n 
1 94  THR 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 PRO 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 GLU 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 ASN 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 LEU n 
1 423 VAL 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                   423 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NOS1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
A1A0C non-polymer         . '(6M)-6-{2,3-difluoro-5-[2-(methylamino)ethyl]phenyl}-4-methylpyridin-2-amine' ? 'C15 H17 F2 N3'    
277.312 
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  
GOL   non-polymer         . GLYCEROL                                                                       
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
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   302 ?   ?   ?   A . n 
A 1 2   PRO 2   303 ?   ?   ?   A . n 
A 1 3   ARG 3   304 ?   ?   ?   A . n 
A 1 4   PHE 4   305 305 PHE PHE A . n 
A 1 5   LEU 5   306 306 LEU LEU A . n 
A 1 6   LYS 6   307 307 LYS LYS A . n 
A 1 7   VAL 7   308 308 VAL VAL A . n 
A 1 8   LYS 8   309 309 LYS LYS A . n 
A 1 9   ASN 9   310 310 ASN ASN A . n 
A 1 10  TRP 10  311 311 TRP TRP A . n 
A 1 11  GLU 11  312 312 GLU GLU A . n 
A 1 12  THR 12  313 313 THR THR A . n 
A 1 13  GLU 13  314 314 GLU GLU A . n 
A 1 14  VAL 14  315 315 VAL VAL A . n 
A 1 15  VAL 15  316 316 VAL VAL A . n 
A 1 16  LEU 16  317 317 LEU LEU A . n 
A 1 17  THR 17  318 318 THR THR A . n 
A 1 18  ASP 18  319 319 ASP ASP A . n 
A 1 19  THR 19  320 320 THR THR A . n 
A 1 20  LEU 20  321 321 LEU LEU A . n 
A 1 21  HIS 21  322 322 HIS HIS A . n 
A 1 22  LEU 22  323 323 LEU LEU A . n 
A 1 23  LYS 23  324 324 LYS LYS A . n 
A 1 24  SER 24  325 325 SER SER A . n 
A 1 25  THR 25  326 326 THR THR A . n 
A 1 26  LEU 26  327 327 LEU LEU A . n 
A 1 27  GLU 27  328 328 GLU GLU A . n 
A 1 28  THR 28  329 329 THR THR A . n 
A 1 29  GLY 29  330 330 GLY GLY A . n 
A 1 30  CYS 30  331 331 CYS CYS A . n 
A 1 31  THR 31  332 332 THR THR A . n 
A 1 32  GLU 32  333 333 GLU GLU A . n 
A 1 33  TYR 33  334 334 TYR TYR A . n 
A 1 34  ILE 34  335 335 ILE ILE A . n 
A 1 35  CYS 35  336 336 CYS CYS A . n 
A 1 36  MET 36  337 337 MET MET A . n 
A 1 37  GLY 37  338 338 GLY GLY A . n 
A 1 38  SER 38  339 339 SER SER A . n 
A 1 39  ILE 39  340 340 ILE ILE A . n 
A 1 40  MET 40  341 341 MET MET A . n 
A 1 41  HIS 41  342 342 HIS HIS A . n 
A 1 42  PRO 42  343 343 PRO PRO A . n 
A 1 43  SER 43  344 344 SER SER A . n 
A 1 44  GLN 44  345 345 GLN GLN A . n 
A 1 45  HIS 45  346 346 HIS HIS A . n 
A 1 46  ALA 46  347 347 ALA ALA A . n 
A 1 47  ARG 47  348 348 ARG ARG A . n 
A 1 48  ARG 48  349 349 ARG ARG A . n 
A 1 49  PRO 49  350 350 PRO PRO A . n 
A 1 50  GLU 50  351 351 GLU GLU A . n 
A 1 51  ASP 51  352 352 ASP ASP A . n 
A 1 52  VAL 52  353 353 VAL VAL A . n 
A 1 53  ALA 53  354 354 ALA ALA A . n 
A 1 54  THR 54  355 355 THR THR A . n 
A 1 55  LYS 55  356 356 LYS LYS A . n 
A 1 56  ASP 56  357 357 ASP ASP A . n 
A 1 57  GLN 57  358 358 GLN GLN A . n 
A 1 58  LEU 58  359 359 LEU LEU A . n 
A 1 59  PHE 59  360 360 PHE PHE A . n 
A 1 60  PRO 60  361 361 PRO PRO A . n 
A 1 61  LEU 61  362 362 LEU LEU A . n 
A 1 62  ALA 62  363 363 ALA ALA A . n 
A 1 63  LYS 63  364 364 LYS LYS A . n 
A 1 64  GLU 64  365 365 GLU GLU A . n 
A 1 65  PHE 65  366 366 PHE PHE A . n 
A 1 66  ILE 66  367 367 ILE ILE A . n 
A 1 67  ASP 67  368 368 ASP ASP A . n 
A 1 68  GLN 68  369 369 GLN GLN A . n 
A 1 69  TYR 69  370 370 TYR TYR A . n 
A 1 70  TYR 70  371 371 TYR TYR A . n 
A 1 71  SER 71  372 372 SER SER A . n 
A 1 72  SER 72  373 373 SER SER A . n 
A 1 73  ILE 73  374 374 ILE ILE A . n 
A 1 74  LYS 74  375 375 LYS LYS A . n 
A 1 75  ARG 75  376 376 ARG ARG A . n 
A 1 76  PHE 76  377 377 PHE PHE A . n 
A 1 77  GLY 77  378 378 GLY GLY A . n 
A 1 78  SER 78  379 379 SER SER A . n 
A 1 79  LYS 79  380 380 LYS LYS A . n 
A 1 80  ALA 80  381 381 ALA ALA A . n 
A 1 81  HIS 81  382 382 HIS HIS A . n 
A 1 82  MET 82  383 383 MET MET A . n 
A 1 83  GLU 83  384 384 GLU GLU A . n 
A 1 84  ARG 84  385 385 ARG ARG A . n 
A 1 85  LEU 85  386 386 LEU LEU A . n 
A 1 86  GLU 86  387 387 GLU GLU A . n 
A 1 87  GLU 87  388 388 GLU GLU A . n 
A 1 88  VAL 88  389 389 VAL VAL A . n 
A 1 89  ASN 89  390 390 ASN ASN A . n 
A 1 90  LYS 90  391 391 LYS LYS A . n 
A 1 91  GLU 91  392 392 GLU GLU A . n 
A 1 92  ILE 92  393 393 ILE ILE A . n 
A 1 93  ASP 93  394 394 ASP ASP A . n 
A 1 94  THR 94  395 395 THR THR A . n 
A 1 95  THR 95  396 396 THR THR A . n 
A 1 96  SER 96  397 397 SER SER A . n 
A 1 97  THR 97  398 398 THR THR A . n 
A 1 98  TYR 98  399 399 TYR TYR A . n 
A 1 99  GLN 99  400 400 GLN GLN A . n 
A 1 100 LEU 100 401 401 LEU LEU A . n 
A 1 101 LYS 101 402 402 LYS LYS A . n 
A 1 102 ASP 102 403 403 ASP ASP A . n 
A 1 103 THR 103 404 404 THR THR A . n 
A 1 104 GLU 104 405 405 GLU GLU A . n 
A 1 105 LEU 105 406 406 LEU LEU A . n 
A 1 106 ILE 106 407 407 ILE ILE A . n 
A 1 107 TYR 107 408 408 TYR TYR A . n 
A 1 108 GLY 108 409 409 GLY GLY A . n 
A 1 109 ALA 109 410 410 ALA ALA A . n 
A 1 110 LYS 110 411 411 LYS LYS A . n 
A 1 111 HIS 111 412 412 HIS HIS A . n 
A 1 112 ALA 112 413 413 ALA ALA A . n 
A 1 113 TRP 113 414 414 TRP TRP A . n 
A 1 114 ARG 114 415 415 ARG ARG A . n 
A 1 115 ASN 115 416 416 ASN ASN A . n 
A 1 116 ALA 116 417 417 ALA ALA A . n 
A 1 117 SER 117 418 418 SER SER A . n 
A 1 118 ARG 118 419 419 ARG ARG A . n 
A 1 119 CYS 119 420 420 CYS CYS A . n 
A 1 120 VAL 120 421 421 VAL VAL A . n 
A 1 121 GLY 121 422 422 GLY GLY A . n 
A 1 122 ARG 122 423 423 ARG ARG A . n 
A 1 123 ILE 123 424 424 ILE ILE A . n 
A 1 124 GLN 124 425 425 GLN GLN A . n 
A 1 125 TRP 125 426 426 TRP TRP A . n 
A 1 126 SER 126 427 427 SER SER A . n 
A 1 127 LYS 127 428 428 LYS LYS A . n 
A 1 128 LEU 128 429 429 LEU LEU A . n 
A 1 129 GLN 129 430 430 GLN GLN A . n 
A 1 130 VAL 130 431 431 VAL VAL A . n 
A 1 131 PHE 131 432 432 PHE PHE A . n 
A 1 132 ASP 132 433 433 ASP ASP A . n 
A 1 133 ALA 133 434 434 ALA ALA A . n 
A 1 134 ARG 134 435 435 ARG ARG A . n 
A 1 135 ASP 135 436 436 ASP ASP A . n 
A 1 136 CYS 136 437 437 CYS CYS A . n 
A 1 137 THR 137 438 438 THR THR A . n 
A 1 138 THR 138 439 439 THR THR A . n 
A 1 139 ALA 139 440 440 ALA ALA A . n 
A 1 140 HIS 140 441 441 HIS HIS A . n 
A 1 141 GLY 141 442 442 GLY GLY A . n 
A 1 142 MET 142 443 443 MET MET A . n 
A 1 143 PHE 143 444 444 PHE PHE A . n 
A 1 144 ASN 144 445 445 ASN ASN A . n 
A 1 145 TYR 145 446 446 TYR TYR A . n 
A 1 146 ILE 146 447 447 ILE ILE A . n 
A 1 147 CYS 147 448 448 CYS CYS A . n 
A 1 148 ASN 148 449 449 ASN ASN A . n 
A 1 149 HIS 149 450 450 HIS HIS A . n 
A 1 150 VAL 150 451 451 VAL VAL A . n 
A 1 151 LYS 151 452 452 LYS LYS A . n 
A 1 152 TYR 152 453 453 TYR TYR A . n 
A 1 153 ALA 153 454 454 ALA ALA A . n 
A 1 154 THR 154 455 455 THR THR A . n 
A 1 155 ASN 155 456 456 ASN ASN A . n 
A 1 156 LYS 156 457 457 LYS LYS A . n 
A 1 157 GLY 157 458 458 GLY GLY A . n 
A 1 158 ASN 158 459 459 ASN ASN A . n 
A 1 159 LEU 159 460 460 LEU LEU A . n 
A 1 160 ARG 160 461 461 ARG ARG A . n 
A 1 161 SER 161 462 462 SER SER A . n 
A 1 162 ALA 162 463 463 ALA ALA A . n 
A 1 163 ILE 163 464 464 ILE ILE A . n 
A 1 164 THR 164 465 465 THR THR A . n 
A 1 165 ILE 165 466 466 ILE ILE A . n 
A 1 166 PHE 166 467 467 PHE PHE A . n 
A 1 167 PRO 167 468 468 PRO PRO A . n 
A 1 168 GLN 168 469 469 GLN GLN A . n 
A 1 169 ARG 169 470 470 ARG ARG A . n 
A 1 170 THR 170 471 471 THR THR A . n 
A 1 171 ASP 171 472 472 ASP ASP A . n 
A 1 172 GLY 172 473 473 GLY GLY A . n 
A 1 173 LYS 173 474 474 LYS LYS A . n 
A 1 174 HIS 174 475 475 HIS HIS A . n 
A 1 175 ASP 175 476 476 ASP ASP A . n 
A 1 176 PHE 176 477 477 PHE PHE A . n 
A 1 177 ARG 177 478 478 ARG ARG A . n 
A 1 178 VAL 178 479 479 VAL VAL A . n 
A 1 179 TRP 179 480 480 TRP TRP A . n 
A 1 180 ASN 180 481 481 ASN ASN A . n 
A 1 181 SER 181 482 482 SER SER A . n 
A 1 182 GLN 182 483 483 GLN GLN A . n 
A 1 183 LEU 183 484 484 LEU LEU A . n 
A 1 184 ILE 184 485 485 ILE ILE A . n 
A 1 185 ARG 185 486 486 ARG ARG A . n 
A 1 186 TYR 186 487 487 TYR TYR A . n 
A 1 187 ALA 187 488 488 ALA ALA A . n 
A 1 188 GLY 188 489 489 GLY GLY A . n 
A 1 189 TYR 189 490 490 TYR TYR A . n 
A 1 190 LYS 190 491 491 LYS LYS A . n 
A 1 191 GLN 191 492 492 GLN GLN A . n 
A 1 192 PRO 192 493 493 PRO PRO A . n 
A 1 193 ASP 193 494 494 ASP ASP A . n 
A 1 194 GLY 194 495 495 GLY GLY A . n 
A 1 195 SER 195 496 496 SER SER A . n 
A 1 196 THR 196 497 497 THR THR A . n 
A 1 197 LEU 197 498 498 LEU LEU A . n 
A 1 198 GLY 198 499 499 GLY GLY A . n 
A 1 199 ASP 199 500 500 ASP ASP A . n 
A 1 200 PRO 200 501 501 PRO PRO A . n 
A 1 201 ALA 201 502 502 ALA ALA A . n 
A 1 202 ASN 202 503 503 ASN ASN A . n 
A 1 203 VAL 203 504 504 VAL VAL A . n 
A 1 204 GLN 204 505 505 GLN GLN A . n 
A 1 205 PHE 205 506 506 PHE PHE A . n 
A 1 206 THR 206 507 507 THR THR A . n 
A 1 207 GLU 207 508 508 GLU GLU A . n 
A 1 208 ILE 208 509 509 ILE ILE A . n 
A 1 209 CYS 209 510 510 CYS CYS A . n 
A 1 210 ILE 210 511 511 ILE ILE A . n 
A 1 211 GLN 211 512 512 GLN GLN A . n 
A 1 212 GLN 212 513 513 GLN GLN A . n 
A 1 213 GLY 213 514 514 GLY GLY A . n 
A 1 214 TRP 214 515 515 TRP TRP A . n 
A 1 215 LYS 215 516 516 LYS LYS A . n 
A 1 216 PRO 216 517 517 PRO PRO A . n 
A 1 217 PRO 217 518 518 PRO PRO A . n 
A 1 218 ARG 218 519 519 ARG ARG A . n 
A 1 219 GLY 219 520 520 GLY GLY A . n 
A 1 220 ARG 220 521 521 ARG ARG A . n 
A 1 221 PHE 221 522 522 PHE PHE A . n 
A 1 222 ASP 222 523 523 ASP ASP A . n 
A 1 223 VAL 223 524 524 VAL VAL A . n 
A 1 224 LEU 224 525 525 LEU LEU A . n 
A 1 225 PRO 225 526 526 PRO PRO A . n 
A 1 226 LEU 226 527 527 LEU LEU A . n 
A 1 227 LEU 227 528 528 LEU LEU A . n 
A 1 228 LEU 228 529 529 LEU LEU A . n 
A 1 229 GLN 229 530 530 GLN GLN A . n 
A 1 230 ALA 230 531 531 ALA ALA A . n 
A 1 231 ASN 231 532 532 ASN ASN A . n 
A 1 232 GLY 232 533 533 GLY GLY A . n 
A 1 233 ASN 233 534 534 ASN ASN A . n 
A 1 234 ASP 234 535 535 ASP ASP A . n 
A 1 235 PRO 235 536 536 PRO PRO A . n 
A 1 236 GLU 236 537 537 GLU GLU A . n 
A 1 237 LEU 237 538 538 LEU LEU A . n 
A 1 238 PHE 238 539 539 PHE PHE A . n 
A 1 239 GLN 239 540 540 GLN GLN A . n 
A 1 240 ILE 240 541 541 ILE ILE A . n 
A 1 241 PRO 241 542 542 PRO PRO A . n 
A 1 242 PRO 242 543 543 PRO PRO A . n 
A 1 243 GLU 243 544 544 GLU GLU A . n 
A 1 244 LEU 244 545 545 LEU LEU A . n 
A 1 245 VAL 245 546 546 VAL VAL A . n 
A 1 246 LEU 246 547 547 LEU LEU A . n 
A 1 247 GLU 247 548 548 GLU GLU A . n 
A 1 248 VAL 248 549 549 VAL VAL A . n 
A 1 249 PRO 249 550 550 PRO PRO A . n 
A 1 250 ILE 250 551 551 ILE ILE A . n 
A 1 251 ARG 251 552 552 ARG ARG A . n 
A 1 252 HIS 252 553 553 HIS HIS A . n 
A 1 253 PRO 253 554 554 PRO PRO A . n 
A 1 254 LYS 254 555 555 LYS LYS A . n 
A 1 255 PHE 255 556 556 PHE PHE A . n 
A 1 256 GLU 256 557 557 GLU GLU A . n 
A 1 257 TRP 257 558 558 TRP TRP A . n 
A 1 258 PHE 258 559 559 PHE PHE A . n 
A 1 259 LYS 259 560 560 LYS LYS A . n 
A 1 260 ASP 260 561 561 ASP ASP A . n 
A 1 261 LEU 261 562 562 LEU LEU A . n 
A 1 262 GLY 262 563 563 GLY GLY A . n 
A 1 263 LEU 263 564 564 LEU LEU A . n 
A 1 264 LYS 264 565 565 LYS LYS A . n 
A 1 265 TRP 265 566 566 TRP TRP A . n 
A 1 266 TYR 266 567 567 TYR TYR A . n 
A 1 267 GLY 267 568 568 GLY GLY A . n 
A 1 268 LEU 268 569 569 LEU LEU A . n 
A 1 269 PRO 269 570 570 PRO PRO A . n 
A 1 270 ALA 270 571 571 ALA ALA A . n 
A 1 271 VAL 271 572 572 VAL VAL A . n 
A 1 272 SER 272 573 573 SER SER A . n 
A 1 273 ASN 273 574 574 ASN ASN A . n 
A 1 274 MET 274 575 575 MET MET A . n 
A 1 275 LEU 275 576 576 LEU LEU A . n 
A 1 276 LEU 276 577 577 LEU LEU A . n 
A 1 277 GLU 277 578 578 GLU GLU A . n 
A 1 278 ILE 278 579 579 ILE ILE A . n 
A 1 279 GLY 279 580 580 GLY GLY A . n 
A 1 280 GLY 280 581 581 GLY GLY A . n 
A 1 281 LEU 281 582 582 LEU LEU A . n 
A 1 282 GLU 282 583 583 GLU GLU A . n 
A 1 283 PHE 283 584 584 PHE PHE A . n 
A 1 284 SER 284 585 585 SER SER A . n 
A 1 285 ALA 285 586 586 ALA ALA A . n 
A 1 286 CYS 286 587 587 CYS CYS A . n 
A 1 287 PRO 287 588 588 PRO PRO A . n 
A 1 288 PHE 288 589 589 PHE PHE A . n 
A 1 289 SER 289 590 590 SER SER A . n 
A 1 290 GLY 290 591 591 GLY GLY A . n 
A 1 291 TRP 291 592 592 TRP TRP A . n 
A 1 292 TYR 292 593 593 TYR TYR A . n 
A 1 293 MET 293 594 594 MET MET A . n 
A 1 294 GLY 294 595 595 GLY GLY A . n 
A 1 295 THR 295 596 596 THR THR A . n 
A 1 296 GLU 296 597 597 GLU GLU A . n 
A 1 297 ILE 297 598 598 ILE ILE A . n 
A 1 298 GLY 298 599 599 GLY GLY A . n 
A 1 299 VAL 299 600 600 VAL VAL A . n 
A 1 300 ARG 300 601 601 ARG ARG A . n 
A 1 301 ASP 301 602 602 ASP ASP A . n 
A 1 302 TYR 302 603 603 TYR TYR A . n 
A 1 303 CYS 303 604 604 CYS CYS A . n 
A 1 304 ASP 304 605 605 ASP ASP A . n 
A 1 305 ASN 305 606 606 ASN ASN A . n 
A 1 306 SER 306 607 607 SER SER A . n 
A 1 307 ARG 307 608 608 ARG ARG A . n 
A 1 308 TYR 308 609 609 TYR TYR A . n 
A 1 309 ASN 309 610 610 ASN ASN A . n 
A 1 310 ILE 310 611 611 ILE ILE A . n 
A 1 311 LEU 311 612 612 LEU LEU A . n 
A 1 312 GLU 312 613 613 GLU GLU A . n 
A 1 313 GLU 313 614 614 GLU GLU A . n 
A 1 314 VAL 314 615 615 VAL VAL A . n 
A 1 315 ALA 315 616 616 ALA ALA A . n 
A 1 316 LYS 316 617 617 LYS LYS A . n 
A 1 317 LYS 317 618 618 LYS LYS A . n 
A 1 318 MET 318 619 619 MET MET A . n 
A 1 319 ASN 319 620 620 ASN ASN A . n 
A 1 320 LEU 320 621 621 LEU LEU A . n 
A 1 321 ASP 321 622 622 ASP ASP A . n 
A 1 322 MET 322 623 623 MET MET A . n 
A 1 323 ARG 323 624 624 ARG ARG A . n 
A 1 324 LYS 324 625 625 LYS LYS A . n 
A 1 325 THR 325 626 626 THR THR A . n 
A 1 326 SER 326 627 627 SER SER A . n 
A 1 327 SER 327 628 628 SER SER A . n 
A 1 328 LEU 328 629 629 LEU LEU A . n 
A 1 329 TRP 329 630 630 TRP TRP A . n 
A 1 330 LYS 330 631 631 LYS LYS A . n 
A 1 331 ASP 331 632 632 ASP ASP A . n 
A 1 332 GLN 332 633 633 GLN GLN A . n 
A 1 333 ALA 333 634 634 ALA ALA A . n 
A 1 334 LEU 334 635 635 LEU LEU A . n 
A 1 335 VAL 335 636 636 VAL VAL A . n 
A 1 336 GLU 336 637 637 GLU GLU A . n 
A 1 337 ILE 337 638 638 ILE ILE A . n 
A 1 338 ASN 338 639 639 ASN ASN A . n 
A 1 339 ILE 339 640 640 ILE ILE A . n 
A 1 340 ALA 340 641 641 ALA ALA A . n 
A 1 341 VAL 341 642 642 VAL VAL A . n 
A 1 342 LEU 342 643 643 LEU LEU A . n 
A 1 343 TYR 343 644 644 TYR TYR A . n 
A 1 344 SER 344 645 645 SER SER A . n 
A 1 345 PHE 345 646 646 PHE PHE A . n 
A 1 346 GLN 346 647 647 GLN GLN A . n 
A 1 347 SER 347 648 648 SER SER A . n 
A 1 348 ASP 348 649 649 ASP ASP A . n 
A 1 349 LYS 349 650 650 LYS LYS A . n 
A 1 350 VAL 350 651 651 VAL VAL A . n 
A 1 351 THR 351 652 652 THR THR A . n 
A 1 352 ILE 352 653 653 ILE ILE A . n 
A 1 353 VAL 353 654 654 VAL VAL A . n 
A 1 354 ASP 354 655 655 ASP ASP A . n 
A 1 355 HIS 355 656 656 HIS HIS A . n 
A 1 356 HIS 356 657 657 HIS HIS A . n 
A 1 357 SER 357 658 658 SER SER A . n 
A 1 358 ALA 358 659 659 ALA ALA A . n 
A 1 359 THR 359 660 660 THR THR A . n 
A 1 360 GLU 360 661 661 GLU GLU A . n 
A 1 361 SER 361 662 662 SER SER A . n 
A 1 362 PHE 362 663 663 PHE PHE A . n 
A 1 363 ILE 363 664 664 ILE ILE A . n 
A 1 364 LYS 364 665 665 LYS LYS A . n 
A 1 365 HIS 365 666 666 HIS HIS A . n 
A 1 366 MET 366 667 667 MET MET A . n 
A 1 367 GLU 367 668 668 GLU GLU A . n 
A 1 368 ASN 368 669 669 ASN ASN A . n 
A 1 369 GLU 369 670 670 GLU GLU A . n 
A 1 370 TYR 370 671 671 TYR TYR A . n 
A 1 371 ARG 371 672 672 ARG ARG A . n 
A 1 372 CYS 372 673 673 CYS CYS A . n 
A 1 373 ARG 373 674 674 ARG ARG A . n 
A 1 374 GLY 374 675 675 GLY GLY A . n 
A 1 375 GLY 375 676 676 GLY GLY A . n 
A 1 376 CYS 376 677 677 CYS CYS A . n 
A 1 377 PRO 377 678 678 PRO PRO A . n 
A 1 378 ALA 378 679 679 ALA ALA A . n 
A 1 379 ASP 379 680 680 ASP ASP A . n 
A 1 380 TRP 380 681 681 TRP TRP A . n 
A 1 381 VAL 381 682 682 VAL VAL A . n 
A 1 382 TRP 382 683 683 TRP TRP A . n 
A 1 383 ILE 383 684 684 ILE ILE A . n 
A 1 384 VAL 384 685 685 VAL VAL A . n 
A 1 385 PRO 385 686 686 PRO PRO A . n 
A 1 386 PRO 386 687 687 PRO PRO A . n 
A 1 387 MET 387 688 688 MET MET A . n 
A 1 388 SER 388 689 689 SER SER A . n 
A 1 389 GLY 389 690 690 GLY GLY A . n 
A 1 390 SER 390 691 691 SER SER A . n 
A 1 391 ILE 391 692 692 ILE ILE A . n 
A 1 392 THR 392 693 693 THR THR A . n 
A 1 393 PRO 393 694 694 PRO PRO A . n 
A 1 394 VAL 394 695 695 VAL VAL A . n 
A 1 395 PHE 395 696 696 PHE PHE A . n 
A 1 396 HIS 396 697 697 HIS HIS A . n 
A 1 397 GLN 397 698 698 GLN GLN A . n 
A 1 398 GLU 398 699 699 GLU GLU A . n 
A 1 399 MET 399 700 700 MET MET A . n 
A 1 400 LEU 400 701 701 LEU LEU A . n 
A 1 401 ASN 401 702 702 ASN ASN A . n 
A 1 402 TYR 402 703 703 TYR TYR A . n 
A 1 403 ARG 403 704 704 ARG ARG A . n 
A 1 404 LEU 404 705 705 LEU LEU A . n 
A 1 405 THR 405 706 706 THR THR A . n 
A 1 406 PRO 406 707 707 PRO PRO A . n 
A 1 407 SER 407 708 708 SER SER A . n 
A 1 408 PHE 408 709 709 PHE PHE A . n 
A 1 409 GLU 409 710 710 GLU GLU A . n 
A 1 410 TYR 410 711 711 TYR TYR A . n 
A 1 411 GLN 411 712 712 GLN GLN A . n 
A 1 412 PRO 412 713 713 PRO PRO A . n 
A 1 413 ASP 413 714 714 ASP ASP A . n 
A 1 414 PRO 414 715 715 PRO PRO A . n 
A 1 415 TRP 415 716 716 TRP TRP A . n 
A 1 416 ASN 416 717 717 ASN ASN A . n 
A 1 417 THR 417 718 718 THR THR A . n 
A 1 418 HIS 418 719 719 HIS HIS A . n 
A 1 419 VAL 419 720 720 VAL VAL A . n 
A 1 420 TRP 420 721 721 TRP TRP A . n 
A 1 421 LYS 421 722 722 LYS LYS A . n 
A 1 422 LEU 422 723 ?   ?   ?   A . n 
A 1 423 VAL 423 724 ?   ?   ?   A . n 
B 1 1   CYS 1   302 ?   ?   ?   B . n 
B 1 2   PRO 2   303 ?   ?   ?   B . n 
B 1 3   ARG 3   304 304 ARG ARG B . n 
B 1 4   PHE 4   305 305 PHE PHE B . n 
B 1 5   LEU 5   306 306 LEU LEU B . n 
B 1 6   LYS 6   307 307 LYS LYS B . n 
B 1 7   VAL 7   308 308 VAL VAL B . n 
B 1 8   LYS 8   309 309 LYS LYS B . n 
B 1 9   ASN 9   310 310 ASN ASN B . n 
B 1 10  TRP 10  311 311 TRP TRP B . n 
B 1 11  GLU 11  312 312 GLU GLU B . n 
B 1 12  THR 12  313 313 THR THR B . n 
B 1 13  GLU 13  314 314 GLU GLU B . n 
B 1 14  VAL 14  315 315 VAL VAL B . n 
B 1 15  VAL 15  316 316 VAL VAL B . n 
B 1 16  LEU 16  317 317 LEU LEU B . n 
B 1 17  THR 17  318 318 THR THR B . n 
B 1 18  ASP 18  319 319 ASP ASP B . n 
B 1 19  THR 19  320 320 THR THR B . n 
B 1 20  LEU 20  321 321 LEU LEU B . n 
B 1 21  HIS 21  322 322 HIS HIS B . n 
B 1 22  LEU 22  323 323 LEU LEU B . n 
B 1 23  LYS 23  324 324 LYS LYS B . n 
B 1 24  SER 24  325 325 SER SER B . n 
B 1 25  THR 25  326 326 THR THR B . n 
B 1 26  LEU 26  327 327 LEU LEU B . n 
B 1 27  GLU 27  328 328 GLU GLU B . n 
B 1 28  THR 28  329 329 THR THR B . n 
B 1 29  GLY 29  330 330 GLY GLY B . n 
B 1 30  CYS 30  331 331 CYS CYS B . n 
B 1 31  THR 31  332 332 THR THR B . n 
B 1 32  GLU 32  333 333 GLU GLU B . n 
B 1 33  TYR 33  334 334 TYR TYR B . n 
B 1 34  ILE 34  335 335 ILE ILE B . n 
B 1 35  CYS 35  336 336 CYS CYS B . n 
B 1 36  MET 36  337 337 MET MET B . n 
B 1 37  GLY 37  338 338 GLY GLY B . n 
B 1 38  SER 38  339 339 SER SER B . n 
B 1 39  ILE 39  340 340 ILE ILE B . n 
B 1 40  MET 40  341 341 MET MET B . n 
B 1 41  HIS 41  342 342 HIS HIS B . n 
B 1 42  PRO 42  343 343 PRO PRO B . n 
B 1 43  SER 43  344 344 SER SER B . n 
B 1 44  GLN 44  345 ?   ?   ?   B . n 
B 1 45  HIS 45  346 ?   ?   ?   B . n 
B 1 46  ALA 46  347 ?   ?   ?   B . n 
B 1 47  ARG 47  348 ?   ?   ?   B . n 
B 1 48  ARG 48  349 ?   ?   ?   B . n 
B 1 49  PRO 49  350 ?   ?   ?   B . n 
B 1 50  GLU 50  351 ?   ?   ?   B . n 
B 1 51  ASP 51  352 352 ASP ASP B . n 
B 1 52  VAL 52  353 353 VAL VAL B . n 
B 1 53  ALA 53  354 354 ALA ALA B . n 
B 1 54  THR 54  355 355 THR THR B . n 
B 1 55  LYS 55  356 356 LYS LYS B . n 
B 1 56  ASP 56  357 357 ASP ASP B . n 
B 1 57  GLN 57  358 358 GLN GLN B . n 
B 1 58  LEU 58  359 359 LEU LEU B . n 
B 1 59  PHE 59  360 360 PHE PHE B . n 
B 1 60  PRO 60  361 361 PRO PRO B . n 
B 1 61  LEU 61  362 362 LEU LEU B . n 
B 1 62  ALA 62  363 363 ALA ALA B . n 
B 1 63  LYS 63  364 364 LYS LYS B . n 
B 1 64  GLU 64  365 365 GLU GLU B . n 
B 1 65  PHE 65  366 366 PHE PHE B . n 
B 1 66  ILE 66  367 367 ILE ILE B . n 
B 1 67  ASP 67  368 368 ASP ASP B . n 
B 1 68  GLN 68  369 369 GLN GLN B . n 
B 1 69  TYR 69  370 370 TYR TYR B . n 
B 1 70  TYR 70  371 371 TYR TYR B . n 
B 1 71  SER 71  372 372 SER SER B . n 
B 1 72  SER 72  373 373 SER SER B . n 
B 1 73  ILE 73  374 374 ILE ILE B . n 
B 1 74  LYS 74  375 375 LYS LYS B . n 
B 1 75  ARG 75  376 376 ARG ARG B . n 
B 1 76  PHE 76  377 377 PHE PHE B . n 
B 1 77  GLY 77  378 378 GLY GLY B . n 
B 1 78  SER 78  379 379 SER SER B . n 
B 1 79  LYS 79  380 380 LYS LYS B . n 
B 1 80  ALA 80  381 381 ALA ALA B . n 
B 1 81  HIS 81  382 382 HIS HIS B . n 
B 1 82  MET 82  383 383 MET MET B . n 
B 1 83  GLU 83  384 384 GLU GLU B . n 
B 1 84  ARG 84  385 385 ARG ARG B . n 
B 1 85  LEU 85  386 386 LEU LEU B . n 
B 1 86  GLU 86  387 387 GLU GLU B . n 
B 1 87  GLU 87  388 388 GLU GLU B . n 
B 1 88  VAL 88  389 389 VAL VAL B . n 
B 1 89  ASN 89  390 390 ASN ASN B . n 
B 1 90  LYS 90  391 391 LYS LYS B . n 
B 1 91  GLU 91  392 392 GLU GLU B . n 
B 1 92  ILE 92  393 393 ILE ILE B . n 
B 1 93  ASP 93  394 394 ASP ASP B . n 
B 1 94  THR 94  395 395 THR THR B . n 
B 1 95  THR 95  396 396 THR THR B . n 
B 1 96  SER 96  397 397 SER SER B . n 
B 1 97  THR 97  398 398 THR THR B . n 
B 1 98  TYR 98  399 399 TYR TYR B . n 
B 1 99  GLN 99  400 400 GLN GLN B . n 
B 1 100 LEU 100 401 401 LEU LEU B . n 
B 1 101 LYS 101 402 402 LYS LYS B . n 
B 1 102 ASP 102 403 403 ASP ASP B . n 
B 1 103 THR 103 404 404 THR THR B . n 
B 1 104 GLU 104 405 405 GLU GLU B . n 
B 1 105 LEU 105 406 406 LEU LEU B . n 
B 1 106 ILE 106 407 407 ILE ILE B . n 
B 1 107 TYR 107 408 408 TYR TYR B . n 
B 1 108 GLY 108 409 409 GLY GLY B . n 
B 1 109 ALA 109 410 410 ALA ALA B . n 
B 1 110 LYS 110 411 411 LYS LYS B . n 
B 1 111 HIS 111 412 412 HIS HIS B . n 
B 1 112 ALA 112 413 413 ALA ALA B . n 
B 1 113 TRP 113 414 414 TRP TRP B . n 
B 1 114 ARG 114 415 415 ARG ARG B . n 
B 1 115 ASN 115 416 416 ASN ASN B . n 
B 1 116 ALA 116 417 417 ALA ALA B . n 
B 1 117 SER 117 418 418 SER SER B . n 
B 1 118 ARG 118 419 419 ARG ARG B . n 
B 1 119 CYS 119 420 420 CYS CYS B . n 
B 1 120 VAL 120 421 421 VAL VAL B . n 
B 1 121 GLY 121 422 422 GLY GLY B . n 
B 1 122 ARG 122 423 423 ARG ARG B . n 
B 1 123 ILE 123 424 424 ILE ILE B . n 
B 1 124 GLN 124 425 425 GLN GLN B . n 
B 1 125 TRP 125 426 426 TRP TRP B . n 
B 1 126 SER 126 427 427 SER SER B . n 
B 1 127 LYS 127 428 428 LYS LYS B . n 
B 1 128 LEU 128 429 429 LEU LEU B . n 
B 1 129 GLN 129 430 430 GLN GLN B . n 
B 1 130 VAL 130 431 431 VAL VAL B . n 
B 1 131 PHE 131 432 432 PHE PHE B . n 
B 1 132 ASP 132 433 433 ASP ASP B . n 
B 1 133 ALA 133 434 434 ALA ALA B . n 
B 1 134 ARG 134 435 435 ARG ARG B . n 
B 1 135 ASP 135 436 436 ASP ASP B . n 
B 1 136 CYS 136 437 437 CYS CYS B . n 
B 1 137 THR 137 438 438 THR THR B . n 
B 1 138 THR 138 439 439 THR THR B . n 
B 1 139 ALA 139 440 440 ALA ALA B . n 
B 1 140 HIS 140 441 441 HIS HIS B . n 
B 1 141 GLY 141 442 442 GLY GLY B . n 
B 1 142 MET 142 443 443 MET MET B . n 
B 1 143 PHE 143 444 444 PHE PHE B . n 
B 1 144 ASN 144 445 445 ASN ASN B . n 
B 1 145 TYR 145 446 446 TYR TYR B . n 
B 1 146 ILE 146 447 447 ILE ILE B . n 
B 1 147 CYS 147 448 448 CYS CYS B . n 
B 1 148 ASN 148 449 449 ASN ASN B . n 
B 1 149 HIS 149 450 450 HIS HIS B . n 
B 1 150 VAL 150 451 451 VAL VAL B . n 
B 1 151 LYS 151 452 452 LYS LYS B . n 
B 1 152 TYR 152 453 453 TYR TYR B . n 
B 1 153 ALA 153 454 454 ALA ALA B . n 
B 1 154 THR 154 455 455 THR THR B . n 
B 1 155 ASN 155 456 456 ASN ASN B . n 
B 1 156 LYS 156 457 457 LYS LYS B . n 
B 1 157 GLY 157 458 458 GLY GLY B . n 
B 1 158 ASN 158 459 459 ASN ASN B . n 
B 1 159 LEU 159 460 460 LEU LEU B . n 
B 1 160 ARG 160 461 461 ARG ARG B . n 
B 1 161 SER 161 462 462 SER SER B . n 
B 1 162 ALA 162 463 463 ALA ALA B . n 
B 1 163 ILE 163 464 464 ILE ILE B . n 
B 1 164 THR 164 465 465 THR THR B . n 
B 1 165 ILE 165 466 466 ILE ILE B . n 
B 1 166 PHE 166 467 467 PHE PHE B . n 
B 1 167 PRO 167 468 468 PRO PRO B . n 
B 1 168 GLN 168 469 469 GLN GLN B . n 
B 1 169 ARG 169 470 470 ARG ARG B . n 
B 1 170 THR 170 471 471 THR THR B . n 
B 1 171 ASP 171 472 472 ASP ASP B . n 
B 1 172 GLY 172 473 473 GLY GLY B . n 
B 1 173 LYS 173 474 474 LYS LYS B . n 
B 1 174 HIS 174 475 475 HIS HIS B . n 
B 1 175 ASP 175 476 476 ASP ASP B . n 
B 1 176 PHE 176 477 477 PHE PHE B . n 
B 1 177 ARG 177 478 478 ARG ARG B . n 
B 1 178 VAL 178 479 479 VAL VAL B . n 
B 1 179 TRP 179 480 480 TRP TRP B . n 
B 1 180 ASN 180 481 481 ASN ASN B . n 
B 1 181 SER 181 482 482 SER SER B . n 
B 1 182 GLN 182 483 483 GLN GLN B . n 
B 1 183 LEU 183 484 484 LEU LEU B . n 
B 1 184 ILE 184 485 485 ILE ILE B . n 
B 1 185 ARG 185 486 486 ARG ARG B . n 
B 1 186 TYR 186 487 487 TYR TYR B . n 
B 1 187 ALA 187 488 488 ALA ALA B . n 
B 1 188 GLY 188 489 489 GLY GLY B . n 
B 1 189 TYR 189 490 490 TYR TYR B . n 
B 1 190 LYS 190 491 491 LYS LYS B . n 
B 1 191 GLN 191 492 492 GLN GLN B . n 
B 1 192 PRO 192 493 493 PRO PRO B . n 
B 1 193 ASP 193 494 494 ASP ASP B . n 
B 1 194 GLY 194 495 495 GLY GLY B . n 
B 1 195 SER 195 496 496 SER SER B . n 
B 1 196 THR 196 497 497 THR THR B . n 
B 1 197 LEU 197 498 498 LEU LEU B . n 
B 1 198 GLY 198 499 499 GLY GLY B . n 
B 1 199 ASP 199 500 500 ASP ASP B . n 
B 1 200 PRO 200 501 501 PRO PRO B . n 
B 1 201 ALA 201 502 502 ALA ALA B . n 
B 1 202 ASN 202 503 503 ASN ASN B . n 
B 1 203 VAL 203 504 504 VAL VAL B . n 
B 1 204 GLN 204 505 505 GLN GLN B . n 
B 1 205 PHE 205 506 506 PHE PHE B . n 
B 1 206 THR 206 507 507 THR THR B . n 
B 1 207 GLU 207 508 508 GLU GLU B . n 
B 1 208 ILE 208 509 509 ILE ILE B . n 
B 1 209 CYS 209 510 510 CYS CYS B . n 
B 1 210 ILE 210 511 511 ILE ILE B . n 
B 1 211 GLN 211 512 512 GLN GLN B . n 
B 1 212 GLN 212 513 513 GLN GLN B . n 
B 1 213 GLY 213 514 514 GLY GLY B . n 
B 1 214 TRP 214 515 515 TRP TRP B . n 
B 1 215 LYS 215 516 516 LYS LYS B . n 
B 1 216 PRO 216 517 517 PRO PRO B . n 
B 1 217 PRO 217 518 518 PRO PRO B . n 
B 1 218 ARG 218 519 519 ARG ARG B . n 
B 1 219 GLY 219 520 520 GLY GLY B . n 
B 1 220 ARG 220 521 521 ARG ARG B . n 
B 1 221 PHE 221 522 522 PHE PHE B . n 
B 1 222 ASP 222 523 523 ASP ASP B . n 
B 1 223 VAL 223 524 524 VAL VAL B . n 
B 1 224 LEU 224 525 525 LEU LEU B . n 
B 1 225 PRO 225 526 526 PRO PRO B . n 
B 1 226 LEU 226 527 527 LEU LEU B . n 
B 1 227 LEU 227 528 528 LEU LEU B . n 
B 1 228 LEU 228 529 529 LEU LEU B . n 
B 1 229 GLN 229 530 530 GLN GLN B . n 
B 1 230 ALA 230 531 531 ALA ALA B . n 
B 1 231 ASN 231 532 532 ASN ASN B . n 
B 1 232 GLY 232 533 533 GLY GLY B . n 
B 1 233 ASN 233 534 534 ASN ASN B . n 
B 1 234 ASP 234 535 535 ASP ASP B . n 
B 1 235 PRO 235 536 536 PRO PRO B . n 
B 1 236 GLU 236 537 537 GLU GLU B . n 
B 1 237 LEU 237 538 538 LEU LEU B . n 
B 1 238 PHE 238 539 539 PHE PHE B . n 
B 1 239 GLN 239 540 540 GLN GLN B . n 
B 1 240 ILE 240 541 541 ILE ILE B . n 
B 1 241 PRO 241 542 542 PRO PRO B . n 
B 1 242 PRO 242 543 543 PRO PRO B . n 
B 1 243 GLU 243 544 544 GLU GLU B . n 
B 1 244 LEU 244 545 545 LEU LEU B . n 
B 1 245 VAL 245 546 546 VAL VAL B . n 
B 1 246 LEU 246 547 547 LEU LEU B . n 
B 1 247 GLU 247 548 548 GLU GLU B . n 
B 1 248 VAL 248 549 549 VAL VAL B . n 
B 1 249 PRO 249 550 550 PRO PRO B . n 
B 1 250 ILE 250 551 551 ILE ILE B . n 
B 1 251 ARG 251 552 552 ARG ARG B . n 
B 1 252 HIS 252 553 553 HIS HIS B . n 
B 1 253 PRO 253 554 554 PRO PRO B . n 
B 1 254 LYS 254 555 555 LYS LYS B . n 
B 1 255 PHE 255 556 556 PHE PHE B . n 
B 1 256 GLU 256 557 557 GLU GLU B . n 
B 1 257 TRP 257 558 558 TRP TRP B . n 
B 1 258 PHE 258 559 559 PHE PHE B . n 
B 1 259 LYS 259 560 560 LYS LYS B . n 
B 1 260 ASP 260 561 561 ASP ASP B . n 
B 1 261 LEU 261 562 562 LEU LEU B . n 
B 1 262 GLY 262 563 563 GLY GLY B . n 
B 1 263 LEU 263 564 564 LEU LEU B . n 
B 1 264 LYS 264 565 565 LYS LYS B . n 
B 1 265 TRP 265 566 566 TRP TRP B . n 
B 1 266 TYR 266 567 567 TYR TYR B . n 
B 1 267 GLY 267 568 568 GLY GLY B . n 
B 1 268 LEU 268 569 569 LEU LEU B . n 
B 1 269 PRO 269 570 570 PRO PRO B . n 
B 1 270 ALA 270 571 571 ALA ALA B . n 
B 1 271 VAL 271 572 572 VAL VAL B . n 
B 1 272 SER 272 573 573 SER SER B . n 
B 1 273 ASN 273 574 574 ASN ASN B . n 
B 1 274 MET 274 575 575 MET MET B . n 
B 1 275 LEU 275 576 576 LEU LEU B . n 
B 1 276 LEU 276 577 577 LEU LEU B . n 
B 1 277 GLU 277 578 578 GLU GLU B . n 
B 1 278 ILE 278 579 579 ILE ILE B . n 
B 1 279 GLY 279 580 580 GLY GLY B . n 
B 1 280 GLY 280 581 581 GLY GLY B . n 
B 1 281 LEU 281 582 582 LEU LEU B . n 
B 1 282 GLU 282 583 583 GLU GLU B . n 
B 1 283 PHE 283 584 584 PHE PHE B . n 
B 1 284 SER 284 585 585 SER SER B . n 
B 1 285 ALA 285 586 586 ALA ALA B . n 
B 1 286 CYS 286 587 587 CYS CYS B . n 
B 1 287 PRO 287 588 588 PRO PRO B . n 
B 1 288 PHE 288 589 589 PHE PHE B . n 
B 1 289 SER 289 590 590 SER SER B . n 
B 1 290 GLY 290 591 591 GLY GLY B . n 
B 1 291 TRP 291 592 592 TRP TRP B . n 
B 1 292 TYR 292 593 593 TYR TYR B . n 
B 1 293 MET 293 594 594 MET MET B . n 
B 1 294 GLY 294 595 595 GLY GLY B . n 
B 1 295 THR 295 596 596 THR THR B . n 
B 1 296 GLU 296 597 597 GLU GLU B . n 
B 1 297 ILE 297 598 598 ILE ILE B . n 
B 1 298 GLY 298 599 599 GLY GLY B . n 
B 1 299 VAL 299 600 600 VAL VAL B . n 
B 1 300 ARG 300 601 601 ARG ARG B . n 
B 1 301 ASP 301 602 602 ASP ASP B . n 
B 1 302 TYR 302 603 603 TYR TYR B . n 
B 1 303 CYS 303 604 604 CYS CYS B . n 
B 1 304 ASP 304 605 605 ASP ASP B . n 
B 1 305 ASN 305 606 606 ASN ASN B . n 
B 1 306 SER 306 607 607 SER SER B . n 
B 1 307 ARG 307 608 608 ARG ARG B . n 
B 1 308 TYR 308 609 609 TYR TYR B . n 
B 1 309 ASN 309 610 610 ASN ASN B . n 
B 1 310 ILE 310 611 611 ILE ILE B . n 
B 1 311 LEU 311 612 612 LEU LEU B . n 
B 1 312 GLU 312 613 613 GLU GLU B . n 
B 1 313 GLU 313 614 614 GLU GLU B . n 
B 1 314 VAL 314 615 615 VAL VAL B . n 
B 1 315 ALA 315 616 616 ALA ALA B . n 
B 1 316 LYS 316 617 617 LYS LYS B . n 
B 1 317 LYS 317 618 618 LYS LYS B . n 
B 1 318 MET 318 619 619 MET MET B . n 
B 1 319 ASN 319 620 620 ASN ASN B . n 
B 1 320 LEU 320 621 621 LEU LEU B . n 
B 1 321 ASP 321 622 622 ASP ASP B . n 
B 1 322 MET 322 623 623 MET MET B . n 
B 1 323 ARG 323 624 624 ARG ARG B . n 
B 1 324 LYS 324 625 625 LYS LYS B . n 
B 1 325 THR 325 626 626 THR THR B . n 
B 1 326 SER 326 627 627 SER SER B . n 
B 1 327 SER 327 628 628 SER SER B . n 
B 1 328 LEU 328 629 629 LEU LEU B . n 
B 1 329 TRP 329 630 630 TRP TRP B . n 
B 1 330 LYS 330 631 631 LYS LYS B . n 
B 1 331 ASP 331 632 632 ASP ASP B . n 
B 1 332 GLN 332 633 633 GLN GLN B . n 
B 1 333 ALA 333 634 634 ALA ALA B . n 
B 1 334 LEU 334 635 635 LEU LEU B . n 
B 1 335 VAL 335 636 636 VAL VAL B . n 
B 1 336 GLU 336 637 637 GLU GLU B . n 
B 1 337 ILE 337 638 638 ILE ILE B . n 
B 1 338 ASN 338 639 639 ASN ASN B . n 
B 1 339 ILE 339 640 640 ILE ILE B . n 
B 1 340 ALA 340 641 641 ALA ALA B . n 
B 1 341 VAL 341 642 642 VAL VAL B . n 
B 1 342 LEU 342 643 643 LEU LEU B . n 
B 1 343 TYR 343 644 644 TYR TYR B . n 
B 1 344 SER 344 645 645 SER SER B . n 
B 1 345 PHE 345 646 646 PHE PHE B . n 
B 1 346 GLN 346 647 647 GLN GLN B . n 
B 1 347 SER 347 648 648 SER SER B . n 
B 1 348 ASP 348 649 649 ASP ASP B . n 
B 1 349 LYS 349 650 650 LYS LYS B . n 
B 1 350 VAL 350 651 651 VAL VAL B . n 
B 1 351 THR 351 652 652 THR THR B . n 
B 1 352 ILE 352 653 653 ILE ILE B . n 
B 1 353 VAL 353 654 654 VAL VAL B . n 
B 1 354 ASP 354 655 655 ASP ASP B . n 
B 1 355 HIS 355 656 656 HIS HIS B . n 
B 1 356 HIS 356 657 657 HIS HIS B . n 
B 1 357 SER 357 658 658 SER SER B . n 
B 1 358 ALA 358 659 659 ALA ALA B . n 
B 1 359 THR 359 660 660 THR THR B . n 
B 1 360 GLU 360 661 661 GLU GLU B . n 
B 1 361 SER 361 662 662 SER SER B . n 
B 1 362 PHE 362 663 663 PHE PHE B . n 
B 1 363 ILE 363 664 664 ILE ILE B . n 
B 1 364 LYS 364 665 665 LYS LYS B . n 
B 1 365 HIS 365 666 666 HIS HIS B . n 
B 1 366 MET 366 667 667 MET MET B . n 
B 1 367 GLU 367 668 668 GLU GLU B . n 
B 1 368 ASN 368 669 669 ASN ASN B . n 
B 1 369 GLU 369 670 670 GLU GLU B . n 
B 1 370 TYR 370 671 671 TYR TYR B . n 
B 1 371 ARG 371 672 672 ARG ARG B . n 
B 1 372 CYS 372 673 673 CYS CYS B . n 
B 1 373 ARG 373 674 674 ARG ARG B . n 
B 1 374 GLY 374 675 675 GLY GLY B . n 
B 1 375 GLY 375 676 676 GLY GLY B . n 
B 1 376 CYS 376 677 677 CYS CYS B . n 
B 1 377 PRO 377 678 678 PRO PRO B . n 
B 1 378 ALA 378 679 679 ALA ALA B . n 
B 1 379 ASP 379 680 680 ASP ASP B . n 
B 1 380 TRP 380 681 681 TRP TRP B . n 
B 1 381 VAL 381 682 682 VAL VAL B . n 
B 1 382 TRP 382 683 683 TRP TRP B . n 
B 1 383 ILE 383 684 684 ILE ILE B . n 
B 1 384 VAL 384 685 685 VAL VAL B . n 
B 1 385 PRO 385 686 686 PRO PRO B . n 
B 1 386 PRO 386 687 687 PRO PRO B . n 
B 1 387 MET 387 688 688 MET MET B . n 
B 1 388 SER 388 689 689 SER SER B . n 
B 1 389 GLY 389 690 690 GLY GLY B . n 
B 1 390 SER 390 691 691 SER SER B . n 
B 1 391 ILE 391 692 692 ILE ILE B . n 
B 1 392 THR 392 693 693 THR THR B . n 
B 1 393 PRO 393 694 694 PRO PRO B . n 
B 1 394 VAL 394 695 695 VAL VAL B . n 
B 1 395 PHE 395 696 696 PHE PHE B . n 
B 1 396 HIS 396 697 697 HIS HIS B . n 
B 1 397 GLN 397 698 698 GLN GLN B . n 
B 1 398 GLU 398 699 699 GLU GLU B . n 
B 1 399 MET 399 700 700 MET MET B . n 
B 1 400 LEU 400 701 701 LEU LEU B . n 
B 1 401 ASN 401 702 702 ASN ASN B . n 
B 1 402 TYR 402 703 703 TYR TYR B . n 
B 1 403 ARG 403 704 704 ARG ARG B . n 
B 1 404 LEU 404 705 705 LEU LEU B . n 
B 1 405 THR 405 706 706 THR THR B . n 
B 1 406 PRO 406 707 707 PRO PRO B . n 
B 1 407 SER 407 708 708 SER SER B . n 
B 1 408 PHE 408 709 709 PHE PHE B . n 
B 1 409 GLU 409 710 710 GLU GLU B . n 
B 1 410 TYR 410 711 711 TYR TYR B . n 
B 1 411 GLN 411 712 712 GLN GLN B . n 
B 1 412 PRO 412 713 713 PRO PRO B . n 
B 1 413 ASP 413 714 714 ASP ASP B . n 
B 1 414 PRO 414 715 715 PRO PRO B . n 
B 1 415 TRP 415 716 716 TRP TRP B . n 
B 1 416 ASN 416 717 717 ASN ASN B . n 
B 1 417 THR 417 718 718 THR THR B . n 
B 1 418 HIS 418 719 719 HIS HIS B . n 
B 1 419 VAL 419 720 720 VAL VAL B . n 
B 1 420 TRP 420 721 721 TRP TRP B . n 
B 1 421 LYS 421 722 722 LYS LYS B . n 
B 1 422 LEU 422 723 723 LEU LEU B . n 
B 1 423 VAL 423 724 724 VAL VAL B . n 
C 1 1   CYS 1   302 ?   ?   ?   C . n 
C 1 2   PRO 2   303 ?   ?   ?   C . n 
C 1 3   ARG 3   304 304 ARG ARG C . n 
C 1 4   PHE 4   305 305 PHE PHE C . n 
C 1 5   LEU 5   306 306 LEU LEU C . n 
C 1 6   LYS 6   307 307 LYS LYS C . n 
C 1 7   VAL 7   308 308 VAL VAL C . n 
C 1 8   LYS 8   309 309 LYS LYS C . n 
C 1 9   ASN 9   310 310 ASN ASN C . n 
C 1 10  TRP 10  311 311 TRP TRP C . n 
C 1 11  GLU 11  312 312 GLU GLU C . n 
C 1 12  THR 12  313 313 THR THR C . n 
C 1 13  GLU 13  314 314 GLU GLU C . n 
C 1 14  VAL 14  315 315 VAL VAL C . n 
C 1 15  VAL 15  316 316 VAL VAL C . n 
C 1 16  LEU 16  317 317 LEU LEU C . n 
C 1 17  THR 17  318 318 THR THR C . n 
C 1 18  ASP 18  319 319 ASP ASP C . n 
C 1 19  THR 19  320 320 THR THR C . n 
C 1 20  LEU 20  321 321 LEU LEU C . n 
C 1 21  HIS 21  322 322 HIS HIS C . n 
C 1 22  LEU 22  323 323 LEU LEU C . n 
C 1 23  LYS 23  324 324 LYS LYS C . n 
C 1 24  SER 24  325 325 SER SER C . n 
C 1 25  THR 25  326 326 THR THR C . n 
C 1 26  LEU 26  327 327 LEU LEU C . n 
C 1 27  GLU 27  328 328 GLU GLU C . n 
C 1 28  THR 28  329 329 THR THR C . n 
C 1 29  GLY 29  330 330 GLY GLY C . n 
C 1 30  CYS 30  331 331 CYS CYS C . n 
C 1 31  THR 31  332 332 THR THR C . n 
C 1 32  GLU 32  333 333 GLU GLU C . n 
C 1 33  TYR 33  334 334 TYR TYR C . n 
C 1 34  ILE 34  335 335 ILE ILE C . n 
C 1 35  CYS 35  336 336 CYS CYS C . n 
C 1 36  MET 36  337 337 MET MET C . n 
C 1 37  GLY 37  338 338 GLY GLY C . n 
C 1 38  SER 38  339 339 SER SER C . n 
C 1 39  ILE 39  340 340 ILE ILE C . n 
C 1 40  MET 40  341 341 MET MET C . n 
C 1 41  HIS 41  342 342 HIS HIS C . n 
C 1 42  PRO 42  343 343 PRO PRO C . n 
C 1 43  SER 43  344 ?   ?   ?   C . n 
C 1 44  GLN 44  345 ?   ?   ?   C . n 
C 1 45  HIS 45  346 ?   ?   ?   C . n 
C 1 46  ALA 46  347 ?   ?   ?   C . n 
C 1 47  ARG 47  348 ?   ?   ?   C . n 
C 1 48  ARG 48  349 ?   ?   ?   C . n 
C 1 49  PRO 49  350 ?   ?   ?   C . n 
C 1 50  GLU 50  351 ?   ?   ?   C . n 
C 1 51  ASP 51  352 352 ASP ASP C . n 
C 1 52  VAL 52  353 353 VAL VAL C . n 
C 1 53  ALA 53  354 354 ALA ALA C . n 
C 1 54  THR 54  355 355 THR THR C . n 
C 1 55  LYS 55  356 356 LYS LYS C . n 
C 1 56  ASP 56  357 357 ASP ASP C . n 
C 1 57  GLN 57  358 358 GLN GLN C . n 
C 1 58  LEU 58  359 359 LEU LEU C . n 
C 1 59  PHE 59  360 360 PHE PHE C . n 
C 1 60  PRO 60  361 361 PRO PRO C . n 
C 1 61  LEU 61  362 362 LEU LEU C . n 
C 1 62  ALA 62  363 363 ALA ALA C . n 
C 1 63  LYS 63  364 364 LYS LYS C . n 
C 1 64  GLU 64  365 365 GLU GLU C . n 
C 1 65  PHE 65  366 366 PHE PHE C . n 
C 1 66  ILE 66  367 367 ILE ILE C . n 
C 1 67  ASP 67  368 368 ASP ASP C . n 
C 1 68  GLN 68  369 369 GLN GLN C . n 
C 1 69  TYR 69  370 370 TYR TYR C . n 
C 1 70  TYR 70  371 371 TYR TYR C . n 
C 1 71  SER 71  372 372 SER SER C . n 
C 1 72  SER 72  373 373 SER SER C . n 
C 1 73  ILE 73  374 374 ILE ILE C . n 
C 1 74  LYS 74  375 375 LYS LYS C . n 
C 1 75  ARG 75  376 376 ARG ARG C . n 
C 1 76  PHE 76  377 377 PHE PHE C . n 
C 1 77  GLY 77  378 378 GLY GLY C . n 
C 1 78  SER 78  379 379 SER SER C . n 
C 1 79  LYS 79  380 380 LYS LYS C . n 
C 1 80  ALA 80  381 381 ALA ALA C . n 
C 1 81  HIS 81  382 382 HIS HIS C . n 
C 1 82  MET 82  383 383 MET MET C . n 
C 1 83  GLU 83  384 384 GLU GLU C . n 
C 1 84  ARG 84  385 385 ARG ARG C . n 
C 1 85  LEU 85  386 386 LEU LEU C . n 
C 1 86  GLU 86  387 387 GLU GLU C . n 
C 1 87  GLU 87  388 388 GLU GLU C . n 
C 1 88  VAL 88  389 389 VAL VAL C . n 
C 1 89  ASN 89  390 390 ASN ASN C . n 
C 1 90  LYS 90  391 391 LYS LYS C . n 
C 1 91  GLU 91  392 392 GLU GLU C . n 
C 1 92  ILE 92  393 393 ILE ILE C . n 
C 1 93  ASP 93  394 394 ASP ASP C . n 
C 1 94  THR 94  395 395 THR THR C . n 
C 1 95  THR 95  396 396 THR THR C . n 
C 1 96  SER 96  397 397 SER SER C . n 
C 1 97  THR 97  398 398 THR THR C . n 
C 1 98  TYR 98  399 399 TYR TYR C . n 
C 1 99  GLN 99  400 400 GLN GLN C . n 
C 1 100 LEU 100 401 401 LEU LEU C . n 
C 1 101 LYS 101 402 402 LYS LYS C . n 
C 1 102 ASP 102 403 403 ASP ASP C . n 
C 1 103 THR 103 404 404 THR THR C . n 
C 1 104 GLU 104 405 405 GLU GLU C . n 
C 1 105 LEU 105 406 406 LEU LEU C . n 
C 1 106 ILE 106 407 407 ILE ILE C . n 
C 1 107 TYR 107 408 408 TYR TYR C . n 
C 1 108 GLY 108 409 409 GLY GLY C . n 
C 1 109 ALA 109 410 410 ALA ALA C . n 
C 1 110 LYS 110 411 411 LYS LYS C . n 
C 1 111 HIS 111 412 412 HIS HIS C . n 
C 1 112 ALA 112 413 413 ALA ALA C . n 
C 1 113 TRP 113 414 414 TRP TRP C . n 
C 1 114 ARG 114 415 415 ARG ARG C . n 
C 1 115 ASN 115 416 416 ASN ASN C . n 
C 1 116 ALA 116 417 417 ALA ALA C . n 
C 1 117 SER 117 418 418 SER SER C . n 
C 1 118 ARG 118 419 419 ARG ARG C . n 
C 1 119 CYS 119 420 420 CYS CYS C . n 
C 1 120 VAL 120 421 421 VAL VAL C . n 
C 1 121 GLY 121 422 422 GLY GLY C . n 
C 1 122 ARG 122 423 423 ARG ARG C . n 
C 1 123 ILE 123 424 424 ILE ILE C . n 
C 1 124 GLN 124 425 425 GLN GLN C . n 
C 1 125 TRP 125 426 426 TRP TRP C . n 
C 1 126 SER 126 427 427 SER SER C . n 
C 1 127 LYS 127 428 428 LYS LYS C . n 
C 1 128 LEU 128 429 429 LEU LEU C . n 
C 1 129 GLN 129 430 430 GLN GLN C . n 
C 1 130 VAL 130 431 431 VAL VAL C . n 
C 1 131 PHE 131 432 432 PHE PHE C . n 
C 1 132 ASP 132 433 433 ASP ASP C . n 
C 1 133 ALA 133 434 434 ALA ALA C . n 
C 1 134 ARG 134 435 435 ARG ARG C . n 
C 1 135 ASP 135 436 436 ASP ASP C . n 
C 1 136 CYS 136 437 437 CYS CYS C . n 
C 1 137 THR 137 438 438 THR THR C . n 
C 1 138 THR 138 439 439 THR THR C . n 
C 1 139 ALA 139 440 440 ALA ALA C . n 
C 1 140 HIS 140 441 441 HIS HIS C . n 
C 1 141 GLY 141 442 442 GLY GLY C . n 
C 1 142 MET 142 443 443 MET MET C . n 
C 1 143 PHE 143 444 444 PHE PHE C . n 
C 1 144 ASN 144 445 445 ASN ASN C . n 
C 1 145 TYR 145 446 446 TYR TYR C . n 
C 1 146 ILE 146 447 447 ILE ILE C . n 
C 1 147 CYS 147 448 448 CYS CYS C . n 
C 1 148 ASN 148 449 449 ASN ASN C . n 
C 1 149 HIS 149 450 450 HIS HIS C . n 
C 1 150 VAL 150 451 451 VAL VAL C . n 
C 1 151 LYS 151 452 452 LYS LYS C . n 
C 1 152 TYR 152 453 453 TYR TYR C . n 
C 1 153 ALA 153 454 454 ALA ALA C . n 
C 1 154 THR 154 455 455 THR THR C . n 
C 1 155 ASN 155 456 456 ASN ASN C . n 
C 1 156 LYS 156 457 457 LYS LYS C . n 
C 1 157 GLY 157 458 458 GLY GLY C . n 
C 1 158 ASN 158 459 459 ASN ASN C . n 
C 1 159 LEU 159 460 460 LEU LEU C . n 
C 1 160 ARG 160 461 461 ARG ARG C . n 
C 1 161 SER 161 462 462 SER SER C . n 
C 1 162 ALA 162 463 463 ALA ALA C . n 
C 1 163 ILE 163 464 464 ILE ILE C . n 
C 1 164 THR 164 465 465 THR THR C . n 
C 1 165 ILE 165 466 466 ILE ILE C . n 
C 1 166 PHE 166 467 467 PHE PHE C . n 
C 1 167 PRO 167 468 468 PRO PRO C . n 
C 1 168 GLN 168 469 469 GLN GLN C . n 
C 1 169 ARG 169 470 470 ARG ARG C . n 
C 1 170 THR 170 471 471 THR THR C . n 
C 1 171 ASP 171 472 472 ASP ASP C . n 
C 1 172 GLY 172 473 473 GLY GLY C . n 
C 1 173 LYS 173 474 474 LYS LYS C . n 
C 1 174 HIS 174 475 475 HIS HIS C . n 
C 1 175 ASP 175 476 476 ASP ASP C . n 
C 1 176 PHE 176 477 477 PHE PHE C . n 
C 1 177 ARG 177 478 478 ARG ARG C . n 
C 1 178 VAL 178 479 479 VAL VAL C . n 
C 1 179 TRP 179 480 480 TRP TRP C . n 
C 1 180 ASN 180 481 481 ASN ASN C . n 
C 1 181 SER 181 482 482 SER SER C . n 
C 1 182 GLN 182 483 483 GLN GLN C . n 
C 1 183 LEU 183 484 484 LEU LEU C . n 
C 1 184 ILE 184 485 485 ILE ILE C . n 
C 1 185 ARG 185 486 486 ARG ARG C . n 
C 1 186 TYR 186 487 487 TYR TYR C . n 
C 1 187 ALA 187 488 488 ALA ALA C . n 
C 1 188 GLY 188 489 489 GLY GLY C . n 
C 1 189 TYR 189 490 490 TYR TYR C . n 
C 1 190 LYS 190 491 491 LYS LYS C . n 
C 1 191 GLN 191 492 492 GLN GLN C . n 
C 1 192 PRO 192 493 493 PRO PRO C . n 
C 1 193 ASP 193 494 494 ASP ASP C . n 
C 1 194 GLY 194 495 495 GLY GLY C . n 
C 1 195 SER 195 496 496 SER SER C . n 
C 1 196 THR 196 497 497 THR THR C . n 
C 1 197 LEU 197 498 498 LEU LEU C . n 
C 1 198 GLY 198 499 499 GLY GLY C . n 
C 1 199 ASP 199 500 500 ASP ASP C . n 
C 1 200 PRO 200 501 501 PRO PRO C . n 
C 1 201 ALA 201 502 502 ALA ALA C . n 
C 1 202 ASN 202 503 503 ASN ASN C . n 
C 1 203 VAL 203 504 504 VAL VAL C . n 
C 1 204 GLN 204 505 505 GLN GLN C . n 
C 1 205 PHE 205 506 506 PHE PHE C . n 
C 1 206 THR 206 507 507 THR THR C . n 
C 1 207 GLU 207 508 508 GLU GLU C . n 
C 1 208 ILE 208 509 509 ILE ILE C . n 
C 1 209 CYS 209 510 510 CYS CYS C . n 
C 1 210 ILE 210 511 511 ILE ILE C . n 
C 1 211 GLN 211 512 512 GLN GLN C . n 
C 1 212 GLN 212 513 513 GLN GLN C . n 
C 1 213 GLY 213 514 514 GLY GLY C . n 
C 1 214 TRP 214 515 515 TRP TRP C . n 
C 1 215 LYS 215 516 516 LYS LYS C . n 
C 1 216 PRO 216 517 517 PRO PRO C . n 
C 1 217 PRO 217 518 518 PRO PRO C . n 
C 1 218 ARG 218 519 519 ARG ARG C . n 
C 1 219 GLY 219 520 520 GLY GLY C . n 
C 1 220 ARG 220 521 521 ARG ARG C . n 
C 1 221 PHE 221 522 522 PHE PHE C . n 
C 1 222 ASP 222 523 523 ASP ASP C . n 
C 1 223 VAL 223 524 524 VAL VAL C . n 
C 1 224 LEU 224 525 525 LEU LEU C . n 
C 1 225 PRO 225 526 526 PRO PRO C . n 
C 1 226 LEU 226 527 527 LEU LEU C . n 
C 1 227 LEU 227 528 528 LEU LEU C . n 
C 1 228 LEU 228 529 529 LEU LEU C . n 
C 1 229 GLN 229 530 530 GLN GLN C . n 
C 1 230 ALA 230 531 531 ALA ALA C . n 
C 1 231 ASN 231 532 532 ASN ASN C . n 
C 1 232 GLY 232 533 533 GLY GLY C . n 
C 1 233 ASN 233 534 534 ASN ASN C . n 
C 1 234 ASP 234 535 535 ASP ASP C . n 
C 1 235 PRO 235 536 536 PRO PRO C . n 
C 1 236 GLU 236 537 537 GLU GLU C . n 
C 1 237 LEU 237 538 538 LEU LEU C . n 
C 1 238 PHE 238 539 539 PHE PHE C . n 
C 1 239 GLN 239 540 540 GLN GLN C . n 
C 1 240 ILE 240 541 541 ILE ILE C . n 
C 1 241 PRO 241 542 542 PRO PRO C . n 
C 1 242 PRO 242 543 543 PRO PRO C . n 
C 1 243 GLU 243 544 544 GLU GLU C . n 
C 1 244 LEU 244 545 545 LEU LEU C . n 
C 1 245 VAL 245 546 546 VAL VAL C . n 
C 1 246 LEU 246 547 547 LEU LEU C . n 
C 1 247 GLU 247 548 548 GLU GLU C . n 
C 1 248 VAL 248 549 549 VAL VAL C . n 
C 1 249 PRO 249 550 550 PRO PRO C . n 
C 1 250 ILE 250 551 551 ILE ILE C . n 
C 1 251 ARG 251 552 552 ARG ARG C . n 
C 1 252 HIS 252 553 553 HIS HIS C . n 
C 1 253 PRO 253 554 554 PRO PRO C . n 
C 1 254 LYS 254 555 555 LYS LYS C . n 
C 1 255 PHE 255 556 556 PHE PHE C . n 
C 1 256 GLU 256 557 557 GLU GLU C . n 
C 1 257 TRP 257 558 558 TRP TRP C . n 
C 1 258 PHE 258 559 559 PHE PHE C . n 
C 1 259 LYS 259 560 560 LYS LYS C . n 
C 1 260 ASP 260 561 561 ASP ASP C . n 
C 1 261 LEU 261 562 562 LEU LEU C . n 
C 1 262 GLY 262 563 563 GLY GLY C . n 
C 1 263 LEU 263 564 564 LEU LEU C . n 
C 1 264 LYS 264 565 565 LYS LYS C . n 
C 1 265 TRP 265 566 566 TRP TRP C . n 
C 1 266 TYR 266 567 567 TYR TYR C . n 
C 1 267 GLY 267 568 568 GLY GLY C . n 
C 1 268 LEU 268 569 569 LEU LEU C . n 
C 1 269 PRO 269 570 570 PRO PRO C . n 
C 1 270 ALA 270 571 571 ALA ALA C . n 
C 1 271 VAL 271 572 572 VAL VAL C . n 
C 1 272 SER 272 573 573 SER SER C . n 
C 1 273 ASN 273 574 574 ASN ASN C . n 
C 1 274 MET 274 575 575 MET MET C . n 
C 1 275 LEU 275 576 576 LEU LEU C . n 
C 1 276 LEU 276 577 577 LEU LEU C . n 
C 1 277 GLU 277 578 578 GLU GLU C . n 
C 1 278 ILE 278 579 579 ILE ILE C . n 
C 1 279 GLY 279 580 580 GLY GLY C . n 
C 1 280 GLY 280 581 581 GLY GLY C . n 
C 1 281 LEU 281 582 582 LEU LEU C . n 
C 1 282 GLU 282 583 583 GLU GLU C . n 
C 1 283 PHE 283 584 584 PHE PHE C . n 
C 1 284 SER 284 585 585 SER SER C . n 
C 1 285 ALA 285 586 586 ALA ALA C . n 
C 1 286 CYS 286 587 587 CYS CYS C . n 
C 1 287 PRO 287 588 588 PRO PRO C . n 
C 1 288 PHE 288 589 589 PHE PHE C . n 
C 1 289 SER 289 590 590 SER SER C . n 
C 1 290 GLY 290 591 591 GLY GLY C . n 
C 1 291 TRP 291 592 592 TRP TRP C . n 
C 1 292 TYR 292 593 593 TYR TYR C . n 
C 1 293 MET 293 594 594 MET MET C . n 
C 1 294 GLY 294 595 595 GLY GLY C . n 
C 1 295 THR 295 596 596 THR THR C . n 
C 1 296 GLU 296 597 597 GLU GLU C . n 
C 1 297 ILE 297 598 598 ILE ILE C . n 
C 1 298 GLY 298 599 599 GLY GLY C . n 
C 1 299 VAL 299 600 600 VAL VAL C . n 
C 1 300 ARG 300 601 601 ARG ARG C . n 
C 1 301 ASP 301 602 602 ASP ASP C . n 
C 1 302 TYR 302 603 603 TYR TYR C . n 
C 1 303 CYS 303 604 604 CYS CYS C . n 
C 1 304 ASP 304 605 605 ASP ASP C . n 
C 1 305 ASN 305 606 606 ASN ASN C . n 
C 1 306 SER 306 607 607 SER SER C . n 
C 1 307 ARG 307 608 608 ARG ARG C . n 
C 1 308 TYR 308 609 609 TYR TYR C . n 
C 1 309 ASN 309 610 610 ASN ASN C . n 
C 1 310 ILE 310 611 611 ILE ILE C . n 
C 1 311 LEU 311 612 612 LEU LEU C . n 
C 1 312 GLU 312 613 613 GLU GLU C . n 
C 1 313 GLU 313 614 614 GLU GLU C . n 
C 1 314 VAL 314 615 615 VAL VAL C . n 
C 1 315 ALA 315 616 616 ALA ALA C . n 
C 1 316 LYS 316 617 617 LYS LYS C . n 
C 1 317 LYS 317 618 618 LYS LYS C . n 
C 1 318 MET 318 619 619 MET MET C . n 
C 1 319 ASN 319 620 620 ASN ASN C . n 
C 1 320 LEU 320 621 621 LEU LEU C . n 
C 1 321 ASP 321 622 622 ASP ASP C . n 
C 1 322 MET 322 623 623 MET MET C . n 
C 1 323 ARG 323 624 624 ARG ARG C . n 
C 1 324 LYS 324 625 625 LYS LYS C . n 
C 1 325 THR 325 626 626 THR THR C . n 
C 1 326 SER 326 627 627 SER SER C . n 
C 1 327 SER 327 628 628 SER SER C . n 
C 1 328 LEU 328 629 629 LEU LEU C . n 
C 1 329 TRP 329 630 630 TRP TRP C . n 
C 1 330 LYS 330 631 631 LYS LYS C . n 
C 1 331 ASP 331 632 632 ASP ASP C . n 
C 1 332 GLN 332 633 633 GLN GLN C . n 
C 1 333 ALA 333 634 634 ALA ALA C . n 
C 1 334 LEU 334 635 635 LEU LEU C . n 
C 1 335 VAL 335 636 636 VAL VAL C . n 
C 1 336 GLU 336 637 637 GLU GLU C . n 
C 1 337 ILE 337 638 638 ILE ILE C . n 
C 1 338 ASN 338 639 639 ASN ASN C . n 
C 1 339 ILE 339 640 640 ILE ILE C . n 
C 1 340 ALA 340 641 641 ALA ALA C . n 
C 1 341 VAL 341 642 642 VAL VAL C . n 
C 1 342 LEU 342 643 643 LEU LEU C . n 
C 1 343 TYR 343 644 644 TYR TYR C . n 
C 1 344 SER 344 645 645 SER SER C . n 
C 1 345 PHE 345 646 646 PHE PHE C . n 
C 1 346 GLN 346 647 647 GLN GLN C . n 
C 1 347 SER 347 648 648 SER SER C . n 
C 1 348 ASP 348 649 649 ASP ASP C . n 
C 1 349 LYS 349 650 650 LYS LYS C . n 
C 1 350 VAL 350 651 651 VAL VAL C . n 
C 1 351 THR 351 652 652 THR THR C . n 
C 1 352 ILE 352 653 653 ILE ILE C . n 
C 1 353 VAL 353 654 654 VAL VAL C . n 
C 1 354 ASP 354 655 655 ASP ASP C . n 
C 1 355 HIS 355 656 656 HIS HIS C . n 
C 1 356 HIS 356 657 657 HIS HIS C . n 
C 1 357 SER 357 658 658 SER SER C . n 
C 1 358 ALA 358 659 659 ALA ALA C . n 
C 1 359 THR 359 660 660 THR THR C . n 
C 1 360 GLU 360 661 661 GLU GLU C . n 
C 1 361 SER 361 662 662 SER SER C . n 
C 1 362 PHE 362 663 663 PHE PHE C . n 
C 1 363 ILE 363 664 664 ILE ILE C . n 
C 1 364 LYS 364 665 665 LYS LYS C . n 
C 1 365 HIS 365 666 666 HIS HIS C . n 
C 1 366 MET 366 667 667 MET MET C . n 
C 1 367 GLU 367 668 668 GLU GLU C . n 
C 1 368 ASN 368 669 669 ASN ASN C . n 
C 1 369 GLU 369 670 670 GLU GLU C . n 
C 1 370 TYR 370 671 671 TYR TYR C . n 
C 1 371 ARG 371 672 672 ARG ARG C . n 
C 1 372 CYS 372 673 673 CYS CYS C . n 
C 1 373 ARG 373 674 674 ARG ARG C . n 
C 1 374 GLY 374 675 675 GLY GLY C . n 
C 1 375 GLY 375 676 676 GLY GLY C . n 
C 1 376 CYS 376 677 677 CYS CYS C . n 
C 1 377 PRO 377 678 678 PRO PRO C . n 
C 1 378 ALA 378 679 679 ALA ALA C . n 
C 1 379 ASP 379 680 680 ASP ASP C . n 
C 1 380 TRP 380 681 681 TRP TRP C . n 
C 1 381 VAL 381 682 682 VAL VAL C . n 
C 1 382 TRP 382 683 683 TRP TRP C . n 
C 1 383 ILE 383 684 684 ILE ILE C . n 
C 1 384 VAL 384 685 685 VAL VAL C . n 
C 1 385 PRO 385 686 686 PRO PRO C . n 
C 1 386 PRO 386 687 687 PRO PRO C . n 
C 1 387 MET 387 688 688 MET MET C . n 
C 1 388 SER 388 689 689 SER SER C . n 
C 1 389 GLY 389 690 690 GLY GLY C . n 
C 1 390 SER 390 691 691 SER SER C . n 
C 1 391 ILE 391 692 692 ILE ILE C . n 
C 1 392 THR 392 693 693 THR THR C . n 
C 1 393 PRO 393 694 694 PRO PRO C . n 
C 1 394 VAL 394 695 695 VAL VAL C . n 
C 1 395 PHE 395 696 696 PHE PHE C . n 
C 1 396 HIS 396 697 697 HIS HIS C . n 
C 1 397 GLN 397 698 698 GLN GLN C . n 
C 1 398 GLU 398 699 699 GLU GLU C . n 
C 1 399 MET 399 700 700 MET MET C . n 
C 1 400 LEU 400 701 701 LEU LEU C . n 
C 1 401 ASN 401 702 702 ASN ASN C . n 
C 1 402 TYR 402 703 703 TYR TYR C . n 
C 1 403 ARG 403 704 704 ARG ARG C . n 
C 1 404 LEU 404 705 705 LEU LEU C . n 
C 1 405 THR 405 706 706 THR THR C . n 
C 1 406 PRO 406 707 707 PRO PRO C . n 
C 1 407 SER 407 708 708 SER SER C . n 
C 1 408 PHE 408 709 709 PHE PHE C . n 
C 1 409 GLU 409 710 710 GLU GLU C . n 
C 1 410 TYR 410 711 711 TYR TYR C . n 
C 1 411 GLN 411 712 712 GLN GLN C . n 
C 1 412 PRO 412 713 713 PRO PRO C . n 
C 1 413 ASP 413 714 714 ASP ASP C . n 
C 1 414 PRO 414 715 715 PRO PRO C . n 
C 1 415 TRP 415 716 716 TRP TRP C . n 
C 1 416 ASN 416 717 717 ASN ASN C . n 
C 1 417 THR 417 718 718 THR THR C . n 
C 1 418 HIS 418 719 719 HIS HIS C . n 
C 1 419 VAL 419 720 720 VAL VAL C . n 
C 1 420 TRP 420 721 721 TRP TRP C . n 
C 1 421 LYS 421 722 722 LYS LYS C . n 
C 1 422 LEU 422 723 723 LEU LEU C . n 
C 1 423 VAL 423 724 724 VAL VAL C . n 
D 1 1   CYS 1   302 ?   ?   ?   D . n 
D 1 2   PRO 2   303 ?   ?   ?   D . n 
D 1 3   ARG 3   304 ?   ?   ?   D . n 
D 1 4   PHE 4   305 305 PHE PHE D . n 
D 1 5   LEU 5   306 306 LEU LEU D . n 
D 1 6   LYS 6   307 307 LYS LYS D . n 
D 1 7   VAL 7   308 308 VAL VAL D . n 
D 1 8   LYS 8   309 309 LYS LYS D . n 
D 1 9   ASN 9   310 310 ASN ASN D . n 
D 1 10  TRP 10  311 311 TRP TRP D . n 
D 1 11  GLU 11  312 312 GLU GLU D . n 
D 1 12  THR 12  313 313 THR THR D . n 
D 1 13  GLU 13  314 314 GLU GLU D . n 
D 1 14  VAL 14  315 315 VAL VAL D . n 
D 1 15  VAL 15  316 316 VAL VAL D . n 
D 1 16  LEU 16  317 317 LEU LEU D . n 
D 1 17  THR 17  318 318 THR THR D . n 
D 1 18  ASP 18  319 319 ASP ASP D . n 
D 1 19  THR 19  320 320 THR THR D . n 
D 1 20  LEU 20  321 321 LEU LEU D . n 
D 1 21  HIS 21  322 322 HIS HIS D . n 
D 1 22  LEU 22  323 323 LEU LEU D . n 
D 1 23  LYS 23  324 324 LYS LYS D . n 
D 1 24  SER 24  325 325 SER SER D . n 
D 1 25  THR 25  326 326 THR THR D . n 
D 1 26  LEU 26  327 327 LEU LEU D . n 
D 1 27  GLU 27  328 328 GLU GLU D . n 
D 1 28  THR 28  329 329 THR THR D . n 
D 1 29  GLY 29  330 330 GLY GLY D . n 
D 1 30  CYS 30  331 331 CYS CYS D . n 
D 1 31  THR 31  332 332 THR THR D . n 
D 1 32  GLU 32  333 333 GLU GLU D . n 
D 1 33  TYR 33  334 334 TYR TYR D . n 
D 1 34  ILE 34  335 335 ILE ILE D . n 
D 1 35  CYS 35  336 336 CYS CYS D . n 
D 1 36  MET 36  337 337 MET MET D . n 
D 1 37  GLY 37  338 338 GLY GLY D . n 
D 1 38  SER 38  339 339 SER SER D . n 
D 1 39  ILE 39  340 340 ILE ILE D . n 
D 1 40  MET 40  341 341 MET MET D . n 
D 1 41  HIS 41  342 342 HIS HIS D . n 
D 1 42  PRO 42  343 343 PRO PRO D . n 
D 1 43  SER 43  344 344 SER SER D . n 
D 1 44  GLN 44  345 345 GLN GLN D . n 
D 1 45  HIS 45  346 346 HIS HIS D . n 
D 1 46  ALA 46  347 347 ALA ALA D . n 
D 1 47  ARG 47  348 348 ARG ARG D . n 
D 1 48  ARG 48  349 349 ARG ARG D . n 
D 1 49  PRO 49  350 350 PRO PRO D . n 
D 1 50  GLU 50  351 351 GLU GLU D . n 
D 1 51  ASP 51  352 352 ASP ASP D . n 
D 1 52  VAL 52  353 353 VAL VAL D . n 
D 1 53  ALA 53  354 354 ALA ALA D . n 
D 1 54  THR 54  355 355 THR THR D . n 
D 1 55  LYS 55  356 356 LYS LYS D . n 
D 1 56  ASP 56  357 357 ASP ASP D . n 
D 1 57  GLN 57  358 358 GLN GLN D . n 
D 1 58  LEU 58  359 359 LEU LEU D . n 
D 1 59  PHE 59  360 360 PHE PHE D . n 
D 1 60  PRO 60  361 361 PRO PRO D . n 
D 1 61  LEU 61  362 362 LEU LEU D . n 
D 1 62  ALA 62  363 363 ALA ALA D . n 
D 1 63  LYS 63  364 364 LYS LYS D . n 
D 1 64  GLU 64  365 365 GLU GLU D . n 
D 1 65  PHE 65  366 366 PHE PHE D . n 
D 1 66  ILE 66  367 367 ILE ILE D . n 
D 1 67  ASP 67  368 368 ASP ASP D . n 
D 1 68  GLN 68  369 369 GLN GLN D . n 
D 1 69  TYR 69  370 370 TYR TYR D . n 
D 1 70  TYR 70  371 371 TYR TYR D . n 
D 1 71  SER 71  372 372 SER SER D . n 
D 1 72  SER 72  373 373 SER SER D . n 
D 1 73  ILE 73  374 374 ILE ILE D . n 
D 1 74  LYS 74  375 375 LYS LYS D . n 
D 1 75  ARG 75  376 376 ARG ARG D . n 
D 1 76  PHE 76  377 377 PHE PHE D . n 
D 1 77  GLY 77  378 378 GLY GLY D . n 
D 1 78  SER 78  379 379 SER SER D . n 
D 1 79  LYS 79  380 380 LYS LYS D . n 
D 1 80  ALA 80  381 381 ALA ALA D . n 
D 1 81  HIS 81  382 382 HIS HIS D . n 
D 1 82  MET 82  383 383 MET MET D . n 
D 1 83  GLU 83  384 384 GLU GLU D . n 
D 1 84  ARG 84  385 385 ARG ARG D . n 
D 1 85  LEU 85  386 386 LEU LEU D . n 
D 1 86  GLU 86  387 387 GLU GLU D . n 
D 1 87  GLU 87  388 388 GLU GLU D . n 
D 1 88  VAL 88  389 389 VAL VAL D . n 
D 1 89  ASN 89  390 390 ASN ASN D . n 
D 1 90  LYS 90  391 391 LYS LYS D . n 
D 1 91  GLU 91  392 392 GLU GLU D . n 
D 1 92  ILE 92  393 393 ILE ILE D . n 
D 1 93  ASP 93  394 394 ASP ASP D . n 
D 1 94  THR 94  395 395 THR THR D . n 
D 1 95  THR 95  396 396 THR THR D . n 
D 1 96  SER 96  397 397 SER SER D . n 
D 1 97  THR 97  398 398 THR THR D . n 
D 1 98  TYR 98  399 399 TYR TYR D . n 
D 1 99  GLN 99  400 400 GLN GLN D . n 
D 1 100 LEU 100 401 401 LEU LEU D . n 
D 1 101 LYS 101 402 402 LYS LYS D . n 
D 1 102 ASP 102 403 403 ASP ASP D . n 
D 1 103 THR 103 404 404 THR THR D . n 
D 1 104 GLU 104 405 405 GLU GLU D . n 
D 1 105 LEU 105 406 406 LEU LEU D . n 
D 1 106 ILE 106 407 407 ILE ILE D . n 
D 1 107 TYR 107 408 408 TYR TYR D . n 
D 1 108 GLY 108 409 409 GLY GLY D . n 
D 1 109 ALA 109 410 410 ALA ALA D . n 
D 1 110 LYS 110 411 411 LYS LYS D . n 
D 1 111 HIS 111 412 412 HIS HIS D . n 
D 1 112 ALA 112 413 413 ALA ALA D . n 
D 1 113 TRP 113 414 414 TRP TRP D . n 
D 1 114 ARG 114 415 415 ARG ARG D . n 
D 1 115 ASN 115 416 416 ASN ASN D . n 
D 1 116 ALA 116 417 417 ALA ALA D . n 
D 1 117 SER 117 418 418 SER SER D . n 
D 1 118 ARG 118 419 419 ARG ARG D . n 
D 1 119 CYS 119 420 420 CYS CYS D . n 
D 1 120 VAL 120 421 421 VAL VAL D . n 
D 1 121 GLY 121 422 422 GLY GLY D . n 
D 1 122 ARG 122 423 423 ARG ARG D . n 
D 1 123 ILE 123 424 424 ILE ILE D . n 
D 1 124 GLN 124 425 425 GLN GLN D . n 
D 1 125 TRP 125 426 426 TRP TRP D . n 
D 1 126 SER 126 427 427 SER SER D . n 
D 1 127 LYS 127 428 428 LYS LYS D . n 
D 1 128 LEU 128 429 429 LEU LEU D . n 
D 1 129 GLN 129 430 430 GLN GLN D . n 
D 1 130 VAL 130 431 431 VAL VAL D . n 
D 1 131 PHE 131 432 432 PHE PHE D . n 
D 1 132 ASP 132 433 433 ASP ASP D . n 
D 1 133 ALA 133 434 434 ALA ALA D . n 
D 1 134 ARG 134 435 435 ARG ARG D . n 
D 1 135 ASP 135 436 436 ASP ASP D . n 
D 1 136 CYS 136 437 437 CYS CYS D . n 
D 1 137 THR 137 438 438 THR THR D . n 
D 1 138 THR 138 439 439 THR THR D . n 
D 1 139 ALA 139 440 440 ALA ALA D . n 
D 1 140 HIS 140 441 441 HIS HIS D . n 
D 1 141 GLY 141 442 442 GLY GLY D . n 
D 1 142 MET 142 443 443 MET MET D . n 
D 1 143 PHE 143 444 444 PHE PHE D . n 
D 1 144 ASN 144 445 445 ASN ASN D . n 
D 1 145 TYR 145 446 446 TYR TYR D . n 
D 1 146 ILE 146 447 447 ILE ILE D . n 
D 1 147 CYS 147 448 448 CYS CYS D . n 
D 1 148 ASN 148 449 449 ASN ASN D . n 
D 1 149 HIS 149 450 450 HIS HIS D . n 
D 1 150 VAL 150 451 451 VAL VAL D . n 
D 1 151 LYS 151 452 452 LYS LYS D . n 
D 1 152 TYR 152 453 453 TYR TYR D . n 
D 1 153 ALA 153 454 454 ALA ALA D . n 
D 1 154 THR 154 455 455 THR THR D . n 
D 1 155 ASN 155 456 456 ASN ASN D . n 
D 1 156 LYS 156 457 457 LYS LYS D . n 
D 1 157 GLY 157 458 458 GLY GLY D . n 
D 1 158 ASN 158 459 459 ASN ASN D . n 
D 1 159 LEU 159 460 460 LEU LEU D . n 
D 1 160 ARG 160 461 461 ARG ARG D . n 
D 1 161 SER 161 462 462 SER SER D . n 
D 1 162 ALA 162 463 463 ALA ALA D . n 
D 1 163 ILE 163 464 464 ILE ILE D . n 
D 1 164 THR 164 465 465 THR THR D . n 
D 1 165 ILE 165 466 466 ILE ILE D . n 
D 1 166 PHE 166 467 467 PHE PHE D . n 
D 1 167 PRO 167 468 468 PRO PRO D . n 
D 1 168 GLN 168 469 469 GLN GLN D . n 
D 1 169 ARG 169 470 470 ARG ARG D . n 
D 1 170 THR 170 471 471 THR THR D . n 
D 1 171 ASP 171 472 472 ASP ASP D . n 
D 1 172 GLY 172 473 473 GLY GLY D . n 
D 1 173 LYS 173 474 474 LYS LYS D . n 
D 1 174 HIS 174 475 475 HIS HIS D . n 
D 1 175 ASP 175 476 476 ASP ASP D . n 
D 1 176 PHE 176 477 477 PHE PHE D . n 
D 1 177 ARG 177 478 478 ARG ARG D . n 
D 1 178 VAL 178 479 479 VAL VAL D . n 
D 1 179 TRP 179 480 480 TRP TRP D . n 
D 1 180 ASN 180 481 481 ASN ASN D . n 
D 1 181 SER 181 482 482 SER SER D . n 
D 1 182 GLN 182 483 483 GLN GLN D . n 
D 1 183 LEU 183 484 484 LEU LEU D . n 
D 1 184 ILE 184 485 485 ILE ILE D . n 
D 1 185 ARG 185 486 486 ARG ARG D . n 
D 1 186 TYR 186 487 487 TYR TYR D . n 
D 1 187 ALA 187 488 488 ALA ALA D . n 
D 1 188 GLY 188 489 489 GLY GLY D . n 
D 1 189 TYR 189 490 490 TYR TYR D . n 
D 1 190 LYS 190 491 491 LYS LYS D . n 
D 1 191 GLN 191 492 492 GLN GLN D . n 
D 1 192 PRO 192 493 493 PRO PRO D . n 
D 1 193 ASP 193 494 494 ASP ASP D . n 
D 1 194 GLY 194 495 495 GLY GLY D . n 
D 1 195 SER 195 496 496 SER SER D . n 
D 1 196 THR 196 497 497 THR THR D . n 
D 1 197 LEU 197 498 498 LEU LEU D . n 
D 1 198 GLY 198 499 499 GLY GLY D . n 
D 1 199 ASP 199 500 500 ASP ASP D . n 
D 1 200 PRO 200 501 501 PRO PRO D . n 
D 1 201 ALA 201 502 502 ALA ALA D . n 
D 1 202 ASN 202 503 503 ASN ASN D . n 
D 1 203 VAL 203 504 504 VAL VAL D . n 
D 1 204 GLN 204 505 505 GLN GLN D . n 
D 1 205 PHE 205 506 506 PHE PHE D . n 
D 1 206 THR 206 507 507 THR THR D . n 
D 1 207 GLU 207 508 508 GLU GLU D . n 
D 1 208 ILE 208 509 509 ILE ILE D . n 
D 1 209 CYS 209 510 510 CYS CYS D . n 
D 1 210 ILE 210 511 511 ILE ILE D . n 
D 1 211 GLN 211 512 512 GLN GLN D . n 
D 1 212 GLN 212 513 513 GLN GLN D . n 
D 1 213 GLY 213 514 514 GLY GLY D . n 
D 1 214 TRP 214 515 515 TRP TRP D . n 
D 1 215 LYS 215 516 516 LYS LYS D . n 
D 1 216 PRO 216 517 517 PRO PRO D . n 
D 1 217 PRO 217 518 518 PRO PRO D . n 
D 1 218 ARG 218 519 519 ARG ARG D . n 
D 1 219 GLY 219 520 520 GLY GLY D . n 
D 1 220 ARG 220 521 521 ARG ARG D . n 
D 1 221 PHE 221 522 522 PHE PHE D . n 
D 1 222 ASP 222 523 523 ASP ASP D . n 
D 1 223 VAL 223 524 524 VAL VAL D . n 
D 1 224 LEU 224 525 525 LEU LEU D . n 
D 1 225 PRO 225 526 526 PRO PRO D . n 
D 1 226 LEU 226 527 527 LEU LEU D . n 
D 1 227 LEU 227 528 528 LEU LEU D . n 
D 1 228 LEU 228 529 529 LEU LEU D . n 
D 1 229 GLN 229 530 530 GLN GLN D . n 
D 1 230 ALA 230 531 531 ALA ALA D . n 
D 1 231 ASN 231 532 532 ASN ASN D . n 
D 1 232 GLY 232 533 533 GLY GLY D . n 
D 1 233 ASN 233 534 534 ASN ASN D . n 
D 1 234 ASP 234 535 535 ASP ASP D . n 
D 1 235 PRO 235 536 536 PRO PRO D . n 
D 1 236 GLU 236 537 537 GLU GLU D . n 
D 1 237 LEU 237 538 538 LEU LEU D . n 
D 1 238 PHE 238 539 539 PHE PHE D . n 
D 1 239 GLN 239 540 540 GLN GLN D . n 
D 1 240 ILE 240 541 541 ILE ILE D . n 
D 1 241 PRO 241 542 542 PRO PRO D . n 
D 1 242 PRO 242 543 543 PRO PRO D . n 
D 1 243 GLU 243 544 544 GLU GLU D . n 
D 1 244 LEU 244 545 545 LEU LEU D . n 
D 1 245 VAL 245 546 546 VAL VAL D . n 
D 1 246 LEU 246 547 547 LEU LEU D . n 
D 1 247 GLU 247 548 548 GLU GLU D . n 
D 1 248 VAL 248 549 549 VAL VAL D . n 
D 1 249 PRO 249 550 550 PRO PRO D . n 
D 1 250 ILE 250 551 551 ILE ILE D . n 
D 1 251 ARG 251 552 552 ARG ARG D . n 
D 1 252 HIS 252 553 553 HIS HIS D . n 
D 1 253 PRO 253 554 554 PRO PRO D . n 
D 1 254 LYS 254 555 555 LYS LYS D . n 
D 1 255 PHE 255 556 556 PHE PHE D . n 
D 1 256 GLU 256 557 557 GLU GLU D . n 
D 1 257 TRP 257 558 558 TRP TRP D . n 
D 1 258 PHE 258 559 559 PHE PHE D . n 
D 1 259 LYS 259 560 560 LYS LYS D . n 
D 1 260 ASP 260 561 561 ASP ASP D . n 
D 1 261 LEU 261 562 562 LEU LEU D . n 
D 1 262 GLY 262 563 563 GLY GLY D . n 
D 1 263 LEU 263 564 564 LEU LEU D . n 
D 1 264 LYS 264 565 565 LYS LYS D . n 
D 1 265 TRP 265 566 566 TRP TRP D . n 
D 1 266 TYR 266 567 567 TYR TYR D . n 
D 1 267 GLY 267 568 568 GLY GLY D . n 
D 1 268 LEU 268 569 569 LEU LEU D . n 
D 1 269 PRO 269 570 570 PRO PRO D . n 
D 1 270 ALA 270 571 571 ALA ALA D . n 
D 1 271 VAL 271 572 572 VAL VAL D . n 
D 1 272 SER 272 573 573 SER SER D . n 
D 1 273 ASN 273 574 574 ASN ASN D . n 
D 1 274 MET 274 575 575 MET MET D . n 
D 1 275 LEU 275 576 576 LEU LEU D . n 
D 1 276 LEU 276 577 577 LEU LEU D . n 
D 1 277 GLU 277 578 578 GLU GLU D . n 
D 1 278 ILE 278 579 579 ILE ILE D . n 
D 1 279 GLY 279 580 580 GLY GLY D . n 
D 1 280 GLY 280 581 581 GLY GLY D . n 
D 1 281 LEU 281 582 582 LEU LEU D . n 
D 1 282 GLU 282 583 583 GLU GLU D . n 
D 1 283 PHE 283 584 584 PHE PHE D . n 
D 1 284 SER 284 585 585 SER SER D . n 
D 1 285 ALA 285 586 586 ALA ALA D . n 
D 1 286 CYS 286 587 587 CYS CYS D . n 
D 1 287 PRO 287 588 588 PRO PRO D . n 
D 1 288 PHE 288 589 589 PHE PHE D . n 
D 1 289 SER 289 590 590 SER SER D . n 
D 1 290 GLY 290 591 591 GLY GLY D . n 
D 1 291 TRP 291 592 592 TRP TRP D . n 
D 1 292 TYR 292 593 593 TYR TYR D . n 
D 1 293 MET 293 594 594 MET MET D . n 
D 1 294 GLY 294 595 595 GLY GLY D . n 
D 1 295 THR 295 596 596 THR THR D . n 
D 1 296 GLU 296 597 597 GLU GLU D . n 
D 1 297 ILE 297 598 598 ILE ILE D . n 
D 1 298 GLY 298 599 599 GLY GLY D . n 
D 1 299 VAL 299 600 600 VAL VAL D . n 
D 1 300 ARG 300 601 601 ARG ARG D . n 
D 1 301 ASP 301 602 602 ASP ASP D . n 
D 1 302 TYR 302 603 603 TYR TYR D . n 
D 1 303 CYS 303 604 604 CYS CYS D . n 
D 1 304 ASP 304 605 605 ASP ASP D . n 
D 1 305 ASN 305 606 606 ASN ASN D . n 
D 1 306 SER 306 607 607 SER SER D . n 
D 1 307 ARG 307 608 608 ARG ARG D . n 
D 1 308 TYR 308 609 609 TYR TYR D . n 
D 1 309 ASN 309 610 610 ASN ASN D . n 
D 1 310 ILE 310 611 611 ILE ILE D . n 
D 1 311 LEU 311 612 612 LEU LEU D . n 
D 1 312 GLU 312 613 613 GLU GLU D . n 
D 1 313 GLU 313 614 614 GLU GLU D . n 
D 1 314 VAL 314 615 615 VAL VAL D . n 
D 1 315 ALA 315 616 616 ALA ALA D . n 
D 1 316 LYS 316 617 617 LYS LYS D . n 
D 1 317 LYS 317 618 618 LYS LYS D . n 
D 1 318 MET 318 619 619 MET MET D . n 
D 1 319 ASN 319 620 620 ASN ASN D . n 
D 1 320 LEU 320 621 621 LEU LEU D . n 
D 1 321 ASP 321 622 622 ASP ASP D . n 
D 1 322 MET 322 623 623 MET MET D . n 
D 1 323 ARG 323 624 624 ARG ARG D . n 
D 1 324 LYS 324 625 625 LYS LYS D . n 
D 1 325 THR 325 626 626 THR THR D . n 
D 1 326 SER 326 627 627 SER SER D . n 
D 1 327 SER 327 628 628 SER SER D . n 
D 1 328 LEU 328 629 629 LEU LEU D . n 
D 1 329 TRP 329 630 630 TRP TRP D . n 
D 1 330 LYS 330 631 631 LYS LYS D . n 
D 1 331 ASP 331 632 632 ASP ASP D . n 
D 1 332 GLN 332 633 633 GLN GLN D . n 
D 1 333 ALA 333 634 634 ALA ALA D . n 
D 1 334 LEU 334 635 635 LEU LEU D . n 
D 1 335 VAL 335 636 636 VAL VAL D . n 
D 1 336 GLU 336 637 637 GLU GLU D . n 
D 1 337 ILE 337 638 638 ILE ILE D . n 
D 1 338 ASN 338 639 639 ASN ASN D . n 
D 1 339 ILE 339 640 640 ILE ILE D . n 
D 1 340 ALA 340 641 641 ALA ALA D . n 
D 1 341 VAL 341 642 642 VAL VAL D . n 
D 1 342 LEU 342 643 643 LEU LEU D . n 
D 1 343 TYR 343 644 644 TYR TYR D . n 
D 1 344 SER 344 645 645 SER SER D . n 
D 1 345 PHE 345 646 646 PHE PHE D . n 
D 1 346 GLN 346 647 647 GLN GLN D . n 
D 1 347 SER 347 648 648 SER SER D . n 
D 1 348 ASP 348 649 649 ASP ASP D . n 
D 1 349 LYS 349 650 650 LYS LYS D . n 
D 1 350 VAL 350 651 651 VAL VAL D . n 
D 1 351 THR 351 652 652 THR THR D . n 
D 1 352 ILE 352 653 653 ILE ILE D . n 
D 1 353 VAL 353 654 654 VAL VAL D . n 
D 1 354 ASP 354 655 655 ASP ASP D . n 
D 1 355 HIS 355 656 656 HIS HIS D . n 
D 1 356 HIS 356 657 657 HIS HIS D . n 
D 1 357 SER 357 658 658 SER SER D . n 
D 1 358 ALA 358 659 659 ALA ALA D . n 
D 1 359 THR 359 660 660 THR THR D . n 
D 1 360 GLU 360 661 661 GLU GLU D . n 
D 1 361 SER 361 662 662 SER SER D . n 
D 1 362 PHE 362 663 663 PHE PHE D . n 
D 1 363 ILE 363 664 664 ILE ILE D . n 
D 1 364 LYS 364 665 665 LYS LYS D . n 
D 1 365 HIS 365 666 666 HIS HIS D . n 
D 1 366 MET 366 667 667 MET MET D . n 
D 1 367 GLU 367 668 668 GLU GLU D . n 
D 1 368 ASN 368 669 669 ASN ASN D . n 
D 1 369 GLU 369 670 670 GLU GLU D . n 
D 1 370 TYR 370 671 671 TYR TYR D . n 
D 1 371 ARG 371 672 672 ARG ARG D . n 
D 1 372 CYS 372 673 673 CYS CYS D . n 
D 1 373 ARG 373 674 674 ARG ARG D . n 
D 1 374 GLY 374 675 675 GLY GLY D . n 
D 1 375 GLY 375 676 676 GLY GLY D . n 
D 1 376 CYS 376 677 677 CYS CYS D . n 
D 1 377 PRO 377 678 678 PRO PRO D . n 
D 1 378 ALA 378 679 679 ALA ALA D . n 
D 1 379 ASP 379 680 680 ASP ASP D . n 
D 1 380 TRP 380 681 681 TRP TRP D . n 
D 1 381 VAL 381 682 682 VAL VAL D . n 
D 1 382 TRP 382 683 683 TRP TRP D . n 
D 1 383 ILE 383 684 684 ILE ILE D . n 
D 1 384 VAL 384 685 685 VAL VAL D . n 
D 1 385 PRO 385 686 686 PRO PRO D . n 
D 1 386 PRO 386 687 687 PRO PRO D . n 
D 1 387 MET 387 688 688 MET MET D . n 
D 1 388 SER 388 689 689 SER SER D . n 
D 1 389 GLY 389 690 690 GLY GLY D . n 
D 1 390 SER 390 691 691 SER SER D . n 
D 1 391 ILE 391 692 692 ILE ILE D . n 
D 1 392 THR 392 693 693 THR THR D . n 
D 1 393 PRO 393 694 694 PRO PRO D . n 
D 1 394 VAL 394 695 695 VAL VAL D . n 
D 1 395 PHE 395 696 696 PHE PHE D . n 
D 1 396 HIS 396 697 697 HIS HIS D . n 
D 1 397 GLN 397 698 698 GLN GLN D . n 
D 1 398 GLU 398 699 699 GLU GLU D . n 
D 1 399 MET 399 700 700 MET MET D . n 
D 1 400 LEU 400 701 701 LEU LEU D . n 
D 1 401 ASN 401 702 702 ASN ASN D . n 
D 1 402 TYR 402 703 703 TYR TYR D . n 
D 1 403 ARG 403 704 704 ARG ARG D . n 
D 1 404 LEU 404 705 705 LEU LEU D . n 
D 1 405 THR 405 706 706 THR THR D . n 
D 1 406 PRO 406 707 707 PRO PRO D . n 
D 1 407 SER 407 708 708 SER SER D . n 
D 1 408 PHE 408 709 709 PHE PHE D . n 
D 1 409 GLU 409 710 710 GLU GLU D . n 
D 1 410 TYR 410 711 711 TYR TYR D . n 
D 1 411 GLN 411 712 712 GLN GLN D . n 
D 1 412 PRO 412 713 713 PRO PRO D . n 
D 1 413 ASP 413 714 714 ASP ASP D . n 
D 1 414 PRO 414 715 715 PRO PRO D . n 
D 1 415 TRP 415 716 716 TRP TRP D . n 
D 1 416 ASN 416 717 717 ASN ASN D . n 
D 1 417 THR 417 718 718 THR THR D . n 
D 1 418 HIS 418 719 719 HIS HIS D . n 
D 1 419 VAL 419 720 720 VAL VAL D . n 
D 1 420 TRP 420 721 721 TRP TRP D . n 
D 1 421 LYS 421 722 722 LYS LYS D . n 
D 1 422 LEU 422 723 ?   ?   ?   D . n 
D 1 423 VAL 423 724 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0C 
_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 
E  2 HEM   1   801  750  HEM   HEM A . 
F  3 H4B   1   802  760  H4B   BH4 A . 
G  4 A1A0C 1   803  800  A1A0C 4V7 A . 
H  5 GOL   1   804  882  GOL   GOL A . 
I  6 ZN    1   805  900  ZN    ZN  A . 
J  5 GOL   1   806  881  GOL   GOL A . 
K  2 HEM   1   801  750  HEM   HEM B . 
L  3 H4B   1   802  760  H4B   BH4 B . 
M  4 A1A0C 1   803  800  A1A0C 4V7 B . 
N  5 GOL   1   804  881  GOL   GOL B . 
O  2 HEM   1   801  750  HEM   HEM C . 
P  3 H4B   1   802  760  H4B   BH4 C . 
Q  4 A1A0C 1   803  800  A1A0C 4V7 C . 
R  5 GOL   1   804  881  GOL   GOL C . 
S  5 GOL   1   805  882  GOL   GOL C . 
T  6 ZN    1   806  900  ZN    ZN  C . 
U  2 HEM   1   801  750  HEM   HEM D . 
V  3 H4B   1   802  760  H4B   BH4 D . 
W  4 A1A0C 1   803  800  A1A0C 4V7 D . 
X  5 GOL   1   804  880  GOL   GOL D . 
Y  7 HOH   1   901  962  HOH   HOH A . 
Y  7 HOH   2   902  1007 HOH   HOH A . 
Y  7 HOH   3   903  1071 HOH   HOH A . 
Y  7 HOH   4   904  510  HOH   HOH A . 
Y  7 HOH   5   905  1048 HOH   HOH A . 
Y  7 HOH   6   906  420  HOH   HOH A . 
Y  7 HOH   7   907  1006 HOH   HOH A . 
Y  7 HOH   8   908  1051 HOH   HOH A . 
Y  7 HOH   9   909  181  HOH   HOH A . 
Y  7 HOH   10  910  661  HOH   HOH A . 
Y  7 HOH   11  911  992  HOH   HOH A . 
Y  7 HOH   12  912  1005 HOH   HOH A . 
Y  7 HOH   13  913  397  HOH   HOH A . 
Y  7 HOH   14  914  13   HOH   HOH A . 
Y  7 HOH   15  915  956  HOH   HOH A . 
Y  7 HOH   16  916  1004 HOH   HOH A . 
Y  7 HOH   17  917  1043 HOH   HOH A . 
Y  7 HOH   18  918  1073 HOH   HOH A . 
Y  7 HOH   19  919  985  HOH   HOH A . 
Y  7 HOH   20  920  585  HOH   HOH A . 
Y  7 HOH   21  921  701  HOH   HOH A . 
Y  7 HOH   22  922  334  HOH   HOH A . 
Y  7 HOH   23  923  12   HOH   HOH A . 
Y  7 HOH   24  924  1028 HOH   HOH A . 
Y  7 HOH   25  925  202  HOH   HOH A . 
Y  7 HOH   26  926  326  HOH   HOH A . 
Y  7 HOH   27  927  19   HOH   HOH A . 
Y  7 HOH   28  928  1042 HOH   HOH A . 
Y  7 HOH   29  929  629  HOH   HOH A . 
Y  7 HOH   30  930  706  HOH   HOH A . 
Y  7 HOH   31  931  110  HOH   HOH A . 
Y  7 HOH   32  932  647  HOH   HOH A . 
Y  7 HOH   33  933  959  HOH   HOH A . 
Y  7 HOH   34  934  795  HOH   HOH A . 
Y  7 HOH   35  935  1059 HOH   HOH A . 
Y  7 HOH   36  936  1013 HOH   HOH A . 
Y  7 HOH   37  937  119  HOH   HOH A . 
Y  7 HOH   38  938  220  HOH   HOH A . 
Y  7 HOH   39  939  751  HOH   HOH A . 
Y  7 HOH   40  940  379  HOH   HOH A . 
Y  7 HOH   41  941  33   HOH   HOH A . 
Y  7 HOH   42  942  502  HOH   HOH A . 
Y  7 HOH   43  943  437  HOH   HOH A . 
Y  7 HOH   44  944  98   HOH   HOH A . 
Y  7 HOH   45  945  335  HOH   HOH A . 
Y  7 HOH   46  946  814  HOH   HOH A . 
Y  7 HOH   47  947  41   HOH   HOH A . 
Y  7 HOH   48  948  983  HOH   HOH A . 
Y  7 HOH   49  949  7    HOH   HOH A . 
Y  7 HOH   50  950  707  HOH   HOH A . 
Y  7 HOH   51  951  122  HOH   HOH A . 
Y  7 HOH   52  952  388  HOH   HOH A . 
Y  7 HOH   53  953  832  HOH   HOH A . 
Y  7 HOH   54  954  380  HOH   HOH A . 
Y  7 HOH   55  955  465  HOH   HOH A . 
Y  7 HOH   56  956  672  HOH   HOH A . 
Y  7 HOH   57  957  799  HOH   HOH A . 
Y  7 HOH   58  958  961  HOH   HOH A . 
Y  7 HOH   59  959  285  HOH   HOH A . 
Y  7 HOH   60  960  652  HOH   HOH A . 
Y  7 HOH   61  961  1021 HOH   HOH A . 
Y  7 HOH   62  962  129  HOH   HOH A . 
Y  7 HOH   63  963  30   HOH   HOH A . 
Y  7 HOH   64  964  731  HOH   HOH A . 
Y  7 HOH   65  965  1008 HOH   HOH A . 
Y  7 HOH   66  966  413  HOH   HOH A . 
Y  7 HOH   67  967  586  HOH   HOH A . 
Y  7 HOH   68  968  186  HOH   HOH A . 
Y  7 HOH   69  969  387  HOH   HOH A . 
Y  7 HOH   70  970  1061 HOH   HOH A . 
Y  7 HOH   71  971  255  HOH   HOH A . 
Y  7 HOH   72  972  73   HOH   HOH A . 
Y  7 HOH   73  973  118  HOH   HOH A . 
Y  7 HOH   74  974  475  HOH   HOH A . 
Y  7 HOH   75  975  310  HOH   HOH A . 
Y  7 HOH   76  976  1038 HOH   HOH A . 
Y  7 HOH   77  977  367  HOH   HOH A . 
Y  7 HOH   78  978  718  HOH   HOH A . 
Y  7 HOH   79  979  481  HOH   HOH A . 
Y  7 HOH   80  980  104  HOH   HOH A . 
Y  7 HOH   81  981  473  HOH   HOH A . 
Y  7 HOH   82  982  1131 HOH   HOH A . 
Y  7 HOH   83  983  522  HOH   HOH A . 
Y  7 HOH   84  984  333  HOH   HOH A . 
Y  7 HOH   85  985  167  HOH   HOH A . 
Y  7 HOH   86  986  627  HOH   HOH A . 
Y  7 HOH   87  987  891  HOH   HOH A . 
Y  7 HOH   88  988  360  HOH   HOH A . 
Y  7 HOH   89  989  750  HOH   HOH A . 
Y  7 HOH   90  990  713  HOH   HOH A . 
Y  7 HOH   91  991  61   HOH   HOH A . 
Y  7 HOH   92  992  1027 HOH   HOH A . 
Y  7 HOH   93  993  785  HOH   HOH A . 
Y  7 HOH   94  994  756  HOH   HOH A . 
Y  7 HOH   95  995  182  HOH   HOH A . 
Y  7 HOH   96  996  618  HOH   HOH A . 
Y  7 HOH   97  997  995  HOH   HOH A . 
Y  7 HOH   98  998  1053 HOH   HOH A . 
Y  7 HOH   99  999  219  HOH   HOH A . 
Y  7 HOH   100 1000 974  HOH   HOH A . 
Y  7 HOH   101 1001 489  HOH   HOH A . 
Y  7 HOH   102 1002 24   HOH   HOH A . 
Y  7 HOH   103 1003 351  HOH   HOH A . 
Y  7 HOH   104 1004 843  HOH   HOH A . 
Y  7 HOH   105 1005 158  HOH   HOH A . 
Y  7 HOH   106 1006 192  HOH   HOH A . 
Y  7 HOH   107 1007 221  HOH   HOH A . 
Y  7 HOH   108 1008 70   HOH   HOH A . 
Y  7 HOH   109 1009 205  HOH   HOH A . 
Y  7 HOH   110 1010 499  HOH   HOH A . 
Y  7 HOH   111 1011 217  HOH   HOH A . 
Y  7 HOH   112 1012 1020 HOH   HOH A . 
Y  7 HOH   113 1013 521  HOH   HOH A . 
Y  7 HOH   114 1014 209  HOH   HOH A . 
Y  7 HOH   115 1015 141  HOH   HOH A . 
Y  7 HOH   116 1016 1137 HOH   HOH A . 
Y  7 HOH   117 1017 10   HOH   HOH A . 
Y  7 HOH   118 1018 280  HOH   HOH A . 
Y  7 HOH   119 1019 253  HOH   HOH A . 
Y  7 HOH   120 1020 1047 HOH   HOH A . 
Y  7 HOH   121 1021 478  HOH   HOH A . 
Y  7 HOH   122 1022 1025 HOH   HOH A . 
Y  7 HOH   123 1023 214  HOH   HOH A . 
Y  7 HOH   124 1024 997  HOH   HOH A . 
Y  7 HOH   125 1025 247  HOH   HOH A . 
Y  7 HOH   126 1026 391  HOH   HOH A . 
Y  7 HOH   127 1027 340  HOH   HOH A . 
Y  7 HOH   128 1028 40   HOH   HOH A . 
Y  7 HOH   129 1029 903  HOH   HOH A . 
Y  7 HOH   130 1030 405  HOH   HOH A . 
Y  7 HOH   131 1031 330  HOH   HOH A . 
Y  7 HOH   132 1032 96   HOH   HOH A . 
Y  7 HOH   133 1033 1040 HOH   HOH A . 
Y  7 HOH   134 1034 393  HOH   HOH A . 
Y  7 HOH   135 1035 590  HOH   HOH A . 
Y  7 HOH   136 1036 1019 HOH   HOH A . 
Y  7 HOH   137 1037 354  HOH   HOH A . 
Y  7 HOH   138 1038 189  HOH   HOH A . 
Y  7 HOH   139 1039 782  HOH   HOH A . 
Y  7 HOH   140 1040 1014 HOH   HOH A . 
Y  7 HOH   141 1041 80   HOH   HOH A . 
Y  7 HOH   142 1042 1050 HOH   HOH A . 
Y  7 HOH   143 1043 275  HOH   HOH A . 
Y  7 HOH   144 1044 852  HOH   HOH A . 
Y  7 HOH   145 1045 343  HOH   HOH A . 
Y  7 HOH   146 1046 1024 HOH   HOH A . 
Y  7 HOH   147 1047 591  HOH   HOH A . 
Y  7 HOH   148 1048 784  HOH   HOH A . 
Y  7 HOH   149 1049 998  HOH   HOH A . 
Y  7 HOH   150 1050 895  HOH   HOH A . 
Y  7 HOH   151 1051 788  HOH   HOH A . 
Y  7 HOH   152 1052 298  HOH   HOH A . 
Y  7 HOH   153 1053 736  HOH   HOH A . 
Y  7 HOH   154 1054 1056 HOH   HOH A . 
Y  7 HOH   155 1055 314  HOH   HOH A . 
Y  7 HOH   156 1056 994  HOH   HOH A . 
Y  7 HOH   157 1057 993  HOH   HOH A . 
Y  7 HOH   158 1058 1037 HOH   HOH A . 
Y  7 HOH   159 1059 744  HOH   HOH A . 
Y  7 HOH   160 1060 361  HOH   HOH A . 
Y  7 HOH   161 1061 999  HOH   HOH A . 
Y  7 HOH   162 1062 344  HOH   HOH A . 
Y  7 HOH   163 1063 282  HOH   HOH A . 
Y  7 HOH   164 1064 69   HOH   HOH A . 
Y  7 HOH   165 1065 174  HOH   HOH A . 
Y  7 HOH   166 1066 187  HOH   HOH A . 
Y  7 HOH   167 1067 1009 HOH   HOH A . 
Y  7 HOH   168 1068 687  HOH   HOH A . 
Y  7 HOH   169 1069 548  HOH   HOH A . 
Y  7 HOH   170 1070 1054 HOH   HOH A . 
Y  7 HOH   171 1071 488  HOH   HOH A . 
Y  7 HOH   172 1072 154  HOH   HOH A . 
Y  7 HOH   173 1073 455  HOH   HOH A . 
Y  7 HOH   174 1074 81   HOH   HOH A . 
Y  7 HOH   175 1075 638  HOH   HOH A . 
Y  7 HOH   176 1076 138  HOH   HOH A . 
Y  7 HOH   177 1077 1017 HOH   HOH A . 
Y  7 HOH   178 1078 215  HOH   HOH A . 
Y  7 HOH   179 1079 721  HOH   HOH A . 
Y  7 HOH   180 1080 1023 HOH   HOH A . 
Y  7 HOH   181 1081 954  HOH   HOH A . 
Y  7 HOH   182 1082 980  HOH   HOH A . 
Y  7 HOH   183 1083 749  HOH   HOH A . 
Y  7 HOH   184 1084 264  HOH   HOH A . 
Y  7 HOH   185 1085 740  HOH   HOH A . 
Y  7 HOH   186 1086 937  HOH   HOH A . 
Y  7 HOH   187 1087 349  HOH   HOH A . 
Y  7 HOH   188 1088 831  HOH   HOH A . 
Y  7 HOH   189 1089 176  HOH   HOH A . 
Y  7 HOH   190 1090 34   HOH   HOH A . 
Y  7 HOH   191 1091 356  HOH   HOH A . 
Y  7 HOH   192 1092 1134 HOH   HOH A . 
Y  7 HOH   193 1093 1035 HOH   HOH A . 
Y  7 HOH   194 1094 1057 HOH   HOH A . 
Y  7 HOH   195 1095 724  HOH   HOH A . 
Y  7 HOH   196 1096 909  HOH   HOH A . 
Y  7 HOH   197 1097 1036 HOH   HOH A . 
Y  7 HOH   198 1098 466  HOH   HOH A . 
Y  7 HOH   199 1099 1046 HOH   HOH A . 
Y  7 HOH   200 1100 922  HOH   HOH A . 
Y  7 HOH   201 1101 1064 HOH   HOH A . 
Y  7 HOH   202 1102 523  HOH   HOH A . 
Y  7 HOH   203 1103 431  HOH   HOH A . 
Y  7 HOH   204 1104 1031 HOH   HOH A . 
Y  7 HOH   205 1105 262  HOH   HOH A . 
Y  7 HOH   206 1106 644  HOH   HOH A . 
Y  7 HOH   207 1107 520  HOH   HOH A . 
Y  7 HOH   208 1108 241  HOH   HOH A . 
Y  7 HOH   209 1109 1045 HOH   HOH A . 
Y  7 HOH   210 1110 810  HOH   HOH A . 
Y  7 HOH   211 1111 1000 HOH   HOH A . 
Y  7 HOH   212 1112 143  HOH   HOH A . 
Y  7 HOH   213 1113 39   HOH   HOH A . 
Y  7 HOH   214 1114 525  HOH   HOH A . 
Y  7 HOH   215 1115 1052 HOH   HOH A . 
Y  7 HOH   216 1116 878  HOH   HOH A . 
Y  7 HOH   217 1117 757  HOH   HOH A . 
Y  7 HOH   218 1118 568  HOH   HOH A . 
Y  7 HOH   219 1119 1133 HOH   HOH A . 
Y  7 HOH   220 1120 781  HOH   HOH A . 
Y  7 HOH   221 1121 1041 HOH   HOH A . 
Y  7 HOH   222 1122 958  HOH   HOH A . 
Y  7 HOH   223 1123 1217 HOH   HOH A . 
Y  7 HOH   224 1124 218  HOH   HOH A . 
Y  7 HOH   225 1125 1063 HOH   HOH A . 
Y  7 HOH   226 1126 869  HOH   HOH A . 
Y  7 HOH   227 1127 254  HOH   HOH A . 
Y  7 HOH   228 1128 867  HOH   HOH A . 
Y  7 HOH   229 1129 1066 HOH   HOH A . 
Y  7 HOH   230 1130 684  HOH   HOH A . 
Y  7 HOH   231 1131 901  HOH   HOH A . 
Y  7 HOH   232 1132 1049 HOH   HOH A . 
Y  7 HOH   233 1133 605  HOH   HOH A . 
Y  7 HOH   234 1134 996  HOH   HOH A . 
Y  7 HOH   235 1135 384  HOH   HOH A . 
Y  7 HOH   236 1136 1044 HOH   HOH A . 
Y  7 HOH   237 1137 503  HOH   HOH A . 
Y  7 HOH   238 1138 621  HOH   HOH A . 
Y  7 HOH   239 1139 313  HOH   HOH A . 
Y  7 HOH   240 1140 774  HOH   HOH A . 
Y  7 HOH   241 1141 981  HOH   HOH A . 
Y  7 HOH   242 1142 550  HOH   HOH A . 
Y  7 HOH   243 1143 904  HOH   HOH A . 
Y  7 HOH   244 1144 544  HOH   HOH A . 
Y  7 HOH   245 1145 1062 HOH   HOH A . 
Y  7 HOH   246 1146 445  HOH   HOH A . 
Y  7 HOH   247 1147 779  HOH   HOH A . 
Y  7 HOH   248 1148 587  HOH   HOH A . 
Y  7 HOH   249 1149 414  HOH   HOH A . 
Y  7 HOH   250 1150 875  HOH   HOH A . 
Y  7 HOH   251 1151 827  HOH   HOH A . 
Y  7 HOH   252 1152 630  HOH   HOH A . 
Y  7 HOH   253 1153 469  HOH   HOH A . 
Y  7 HOH   254 1154 645  HOH   HOH A . 
Y  7 HOH   255 1155 592  HOH   HOH A . 
Y  7 HOH   256 1156 982  HOH   HOH A . 
Y  7 HOH   257 1157 571  HOH   HOH A . 
Y  7 HOH   258 1158 628  HOH   HOH A . 
Y  7 HOH   259 1159 596  HOH   HOH A . 
Y  7 HOH   260 1160 412  HOH   HOH A . 
Y  7 HOH   261 1161 1018 HOH   HOH A . 
Y  7 HOH   262 1162 874  HOH   HOH A . 
Y  7 HOH   263 1163 231  HOH   HOH A . 
Y  7 HOH   264 1164 480  HOH   HOH A . 
Y  7 HOH   265 1165 1033 HOH   HOH A . 
Y  7 HOH   266 1166 476  HOH   HOH A . 
Y  7 HOH   267 1167 1015 HOH   HOH A . 
Y  7 HOH   268 1168 916  HOH   HOH A . 
Y  7 HOH   269 1169 764  HOH   HOH A . 
Y  7 HOH   270 1170 955  HOH   HOH A . 
Y  7 HOH   271 1171 429  HOH   HOH A . 
Y  7 HOH   272 1172 912  HOH   HOH A . 
Y  7 HOH   273 1173 1016 HOH   HOH A . 
Y  7 HOH   274 1174 667  HOH   HOH A . 
Y  7 HOH   275 1175 673  HOH   HOH A . 
Y  7 HOH   276 1176 840  HOH   HOH A . 
Y  7 HOH   277 1177 1132 HOH   HOH A . 
Y  7 HOH   278 1178 612  HOH   HOH A . 
Y  7 HOH   279 1179 1060 HOH   HOH A . 
Y  7 HOH   280 1180 325  HOH   HOH A . 
Y  7 HOH   281 1181 1039 HOH   HOH A . 
Y  7 HOH   282 1182 404  HOH   HOH A . 
Y  7 HOH   283 1183 988  HOH   HOH A . 
Y  7 HOH   284 1184 1012 HOH   HOH A . 
Y  7 HOH   285 1185 1072 HOH   HOH A . 
Y  7 HOH   286 1186 650  HOH   HOH A . 
Y  7 HOH   287 1187 1032 HOH   HOH A . 
Y  7 HOH   288 1188 538  HOH   HOH A . 
Y  7 HOH   289 1189 1135 HOH   HOH A . 
Y  7 HOH   290 1190 452  HOH   HOH A . 
Y  7 HOH   291 1191 859  HOH   HOH A . 
Y  7 HOH   292 1192 1034 HOH   HOH A . 
Y  7 HOH   293 1193 564  HOH   HOH A . 
Y  7 HOH   294 1194 386  HOH   HOH A . 
Y  7 HOH   295 1195 440  HOH   HOH A . 
Y  7 HOH   296 1196 300  HOH   HOH A . 
Y  7 HOH   297 1197 841  HOH   HOH A . 
Y  7 HOH   298 1198 493  HOH   HOH A . 
Y  7 HOH   299 1199 960  HOH   HOH A . 
Y  7 HOH   300 1200 1011 HOH   HOH A . 
Y  7 HOH   301 1201 834  HOH   HOH A . 
Y  7 HOH   302 1202 1029 HOH   HOH A . 
Y  7 HOH   303 1203 1065 HOH   HOH A . 
Y  7 HOH   304 1204 1022 HOH   HOH A . 
Y  7 HOH   305 1205 662  HOH   HOH A . 
Y  7 HOH   306 1206 753  HOH   HOH A . 
Y  7 HOH   307 1207 807  HOH   HOH A . 
Y  7 HOH   308 1208 829  HOH   HOH A . 
Y  7 HOH   309 1209 668  HOH   HOH A . 
Y  7 HOH   310 1210 979  HOH   HOH A . 
Y  7 HOH   311 1211 839  HOH   HOH A . 
Y  7 HOH   312 1212 957  HOH   HOH A . 
Y  7 HOH   313 1213 836  HOH   HOH A . 
Y  7 HOH   314 1214 1067 HOH   HOH A . 
Y  7 HOH   315 1215 552  HOH   HOH A . 
Y  7 HOH   316 1216 446  HOH   HOH A . 
Y  7 HOH   317 1217 972  HOH   HOH A . 
Y  7 HOH   318 1218 1136 HOH   HOH A . 
Y  7 HOH   319 1219 1068 HOH   HOH A . 
Y  7 HOH   320 1220 925  HOH   HOH A . 
Y  7 HOH   321 1221 676  HOH   HOH A . 
Y  7 HOH   322 1222 615  HOH   HOH A . 
Z  7 HOH   1   901  1089 HOH   HOH B . 
Z  7 HOH   2   902  1080 HOH   HOH B . 
Z  7 HOH   3   903  1092 HOH   HOH B . 
Z  7 HOH   4   904  976  HOH   HOH B . 
Z  7 HOH   5   905  1077 HOH   HOH B . 
Z  7 HOH   6   906  1121 HOH   HOH B . 
Z  7 HOH   7   907  963  HOH   HOH B . 
Z  7 HOH   8   908  1091 HOH   HOH B . 
Z  7 HOH   9   909  1083 HOH   HOH B . 
Z  7 HOH   10  910  967  HOH   HOH B . 
Z  7 HOH   11  911  303  HOH   HOH B . 
Z  7 HOH   12  912  1130 HOH   HOH B . 
Z  7 HOH   13  913  164  HOH   HOH B . 
Z  7 HOH   14  914  794  HOH   HOH B . 
Z  7 HOH   15  915  318  HOH   HOH B . 
Z  7 HOH   16  916  722  HOH   HOH B . 
Z  7 HOH   17  917  232  HOH   HOH B . 
Z  7 HOH   18  918  719  HOH   HOH B . 
Z  7 HOH   19  919  987  HOH   HOH B . 
Z  7 HOH   20  920  1123 HOH   HOH B . 
Z  7 HOH   21  921  216  HOH   HOH B . 
Z  7 HOH   22  922  1058 HOH   HOH B . 
Z  7 HOH   23  923  541  HOH   HOH B . 
Z  7 HOH   24  924  130  HOH   HOH B . 
Z  7 HOH   25  925  100  HOH   HOH B . 
Z  7 HOH   26  926  206  HOH   HOH B . 
Z  7 HOH   27  927  11   HOH   HOH B . 
Z  7 HOH   28  928  633  HOH   HOH B . 
Z  7 HOH   29  929  1098 HOH   HOH B . 
Z  7 HOH   30  930  933  HOH   HOH B . 
Z  7 HOH   31  931  86   HOH   HOH B . 
Z  7 HOH   32  932  708  HOH   HOH B . 
Z  7 HOH   33  933  1070 HOH   HOH B . 
Z  7 HOH   34  934  695  HOH   HOH B . 
Z  7 HOH   35  935  52   HOH   HOH B . 
Z  7 HOH   36  936  322  HOH   HOH B . 
Z  7 HOH   37  937  107  HOH   HOH B . 
Z  7 HOH   38  938  79   HOH   HOH B . 
Z  7 HOH   39  939  53   HOH   HOH B . 
Z  7 HOH   40  940  171  HOH   HOH B . 
Z  7 HOH   41  941  165  HOH   HOH B . 
Z  7 HOH   42  942  1081 HOH   HOH B . 
Z  7 HOH   43  943  135  HOH   HOH B . 
Z  7 HOH   44  944  805  HOH   HOH B . 
Z  7 HOH   45  945  112  HOH   HOH B . 
Z  7 HOH   46  946  20   HOH   HOH B . 
Z  7 HOH   47  947  990  HOH   HOH B . 
Z  7 HOH   48  948  1115 HOH   HOH B . 
Z  7 HOH   49  949  286  HOH   HOH B . 
Z  7 HOH   50  950  77   HOH   HOH B . 
Z  7 HOH   51  951  159  HOH   HOH B . 
Z  7 HOH   52  952  278  HOH   HOH B . 
Z  7 HOH   53  953  257  HOH   HOH B . 
Z  7 HOH   54  954  796  HOH   HOH B . 
Z  7 HOH   55  955  696  HOH   HOH B . 
Z  7 HOH   56  956  419  HOH   HOH B . 
Z  7 HOH   57  957  63   HOH   HOH B . 
Z  7 HOH   58  958  292  HOH   HOH B . 
Z  7 HOH   59  959  457  HOH   HOH B . 
Z  7 HOH   60  960  147  HOH   HOH B . 
Z  7 HOH   61  961  1103 HOH   HOH B . 
Z  7 HOH   62  962  975  HOH   HOH B . 
Z  7 HOH   63  963  259  HOH   HOH B . 
Z  7 HOH   64  964  747  HOH   HOH B . 
Z  7 HOH   65  965  665  HOH   HOH B . 
Z  7 HOH   66  966  666  HOH   HOH B . 
Z  7 HOH   67  967  545  HOH   HOH B . 
Z  7 HOH   68  968  377  HOH   HOH B . 
Z  7 HOH   69  969  991  HOH   HOH B . 
Z  7 HOH   70  970  37   HOH   HOH B . 
Z  7 HOH   71  971  15   HOH   HOH B . 
Z  7 HOH   72  972  108  HOH   HOH B . 
Z  7 HOH   73  973  227  HOH   HOH B . 
Z  7 HOH   74  974  409  HOH   HOH B . 
Z  7 HOH   75  975  358  HOH   HOH B . 
Z  7 HOH   76  976  4    HOH   HOH B . 
Z  7 HOH   77  977  250  HOH   HOH B . 
Z  7 HOH   78  978  191  HOH   HOH B . 
Z  7 HOH   79  979  179  HOH   HOH B . 
Z  7 HOH   80  980  524  HOH   HOH B . 
Z  7 HOH   81  981  745  HOH   HOH B . 
Z  7 HOH   82  982  1118 HOH   HOH B . 
Z  7 HOH   83  983  47   HOH   HOH B . 
Z  7 HOH   84  984  273  HOH   HOH B . 
Z  7 HOH   85  985  204  HOH   HOH B . 
Z  7 HOH   86  986  125  HOH   HOH B . 
Z  7 HOH   87  987  230  HOH   HOH B . 
Z  7 HOH   88  988  533  HOH   HOH B . 
Z  7 HOH   89  989  3    HOH   HOH B . 
Z  7 HOH   90  990  196  HOH   HOH B . 
Z  7 HOH   91  991  258  HOH   HOH B . 
Z  7 HOH   92  992  461  HOH   HOH B . 
Z  7 HOH   93  993  797  HOH   HOH B . 
Z  7 HOH   94  994  984  HOH   HOH B . 
Z  7 HOH   95  995  136  HOH   HOH B . 
Z  7 HOH   96  996  1110 HOH   HOH B . 
Z  7 HOH   97  997  399  HOH   HOH B . 
Z  7 HOH   98  998  683  HOH   HOH B . 
Z  7 HOH   99  999  197  HOH   HOH B . 
Z  7 HOH   100 1000 580  HOH   HOH B . 
Z  7 HOH   101 1001 599  HOH   HOH B . 
Z  7 HOH   102 1002 426  HOH   HOH B . 
Z  7 HOH   103 1003 38   HOH   HOH B . 
Z  7 HOH   104 1004 279  HOH   HOH B . 
Z  7 HOH   105 1005 50   HOH   HOH B . 
Z  7 HOH   106 1006 1078 HOH   HOH B . 
Z  7 HOH   107 1007 528  HOH   HOH B . 
Z  7 HOH   108 1008 95   HOH   HOH B . 
Z  7 HOH   109 1009 16   HOH   HOH B . 
Z  7 HOH   110 1010 894  HOH   HOH B . 
Z  7 HOH   111 1011 66   HOH   HOH B . 
Z  7 HOH   112 1012 157  HOH   HOH B . 
Z  7 HOH   113 1013 654  HOH   HOH B . 
Z  7 HOH   114 1014 375  HOH   HOH B . 
Z  7 HOH   115 1015 464  HOH   HOH B . 
Z  7 HOH   116 1016 114  HOH   HOH B . 
Z  7 HOH   117 1017 126  HOH   HOH B . 
Z  7 HOH   118 1018 801  HOH   HOH B . 
Z  7 HOH   119 1019 786  HOH   HOH B . 
Z  7 HOH   120 1020 48   HOH   HOH B . 
Z  7 HOH   121 1021 149  HOH   HOH B . 
Z  7 HOH   122 1022 235  HOH   HOH B . 
Z  7 HOH   123 1023 406  HOH   HOH B . 
Z  7 HOH   124 1024 94   HOH   HOH B . 
Z  7 HOH   125 1025 887  HOH   HOH B . 
Z  7 HOH   126 1026 551  HOH   HOH B . 
Z  7 HOH   127 1027 1097 HOH   HOH B . 
Z  7 HOH   128 1028 472  HOH   HOH B . 
Z  7 HOH   129 1029 283  HOH   HOH B . 
Z  7 HOH   130 1030 177  HOH   HOH B . 
Z  7 HOH   131 1031 306  HOH   HOH B . 
Z  7 HOH   132 1032 1107 HOH   HOH B . 
Z  7 HOH   133 1033 302  HOH   HOH B . 
Z  7 HOH   134 1034 725  HOH   HOH B . 
Z  7 HOH   135 1035 133  HOH   HOH B . 
Z  7 HOH   136 1036 323  HOH   HOH B . 
Z  7 HOH   137 1037 735  HOH   HOH B . 
Z  7 HOH   138 1038 103  HOH   HOH B . 
Z  7 HOH   139 1039 151  HOH   HOH B . 
Z  7 HOH   140 1040 802  HOH   HOH B . 
Z  7 HOH   141 1041 348  HOH   HOH B . 
Z  7 HOH   142 1042 845  HOH   HOH B . 
Z  7 HOH   143 1043 90   HOH   HOH B . 
Z  7 HOH   144 1044 249  HOH   HOH B . 
Z  7 HOH   145 1045 88   HOH   HOH B . 
Z  7 HOH   146 1046 261  HOH   HOH B . 
Z  7 HOH   147 1047 846  HOH   HOH B . 
Z  7 HOH   148 1048 730  HOH   HOH B . 
Z  7 HOH   149 1049 583  HOH   HOH B . 
Z  7 HOH   150 1050 1125 HOH   HOH B . 
Z  7 HOH   151 1051 540  HOH   HOH B . 
Z  7 HOH   152 1052 1090 HOH   HOH B . 
Z  7 HOH   153 1053 185  HOH   HOH B . 
Z  7 HOH   154 1054 861  HOH   HOH B . 
Z  7 HOH   155 1055 102  HOH   HOH B . 
Z  7 HOH   156 1056 212  HOH   HOH B . 
Z  7 HOH   157 1057 459  HOH   HOH B . 
Z  7 HOH   158 1058 1094 HOH   HOH B . 
Z  7 HOH   159 1059 964  HOH   HOH B . 
Z  7 HOH   160 1060 1055 HOH   HOH B . 
Z  7 HOH   161 1061 428  HOH   HOH B . 
Z  7 HOH   162 1062 664  HOH   HOH B . 
Z  7 HOH   163 1063 433  HOH   HOH B . 
Z  7 HOH   164 1064 582  HOH   HOH B . 
Z  7 HOH   165 1065 436  HOH   HOH B . 
Z  7 HOH   166 1066 411  HOH   HOH B . 
Z  7 HOH   167 1067 17   HOH   HOH B . 
Z  7 HOH   168 1068 659  HOH   HOH B . 
Z  7 HOH   169 1069 758  HOH   HOH B . 
Z  7 HOH   170 1070 365  HOH   HOH B . 
Z  7 HOH   171 1071 763  HOH   HOH B . 
Z  7 HOH   172 1072 853  HOH   HOH B . 
Z  7 HOH   173 1073 860  HOH   HOH B . 
Z  7 HOH   174 1074 194  HOH   HOH B . 
Z  7 HOH   175 1075 692  HOH   HOH B . 
Z  7 HOH   176 1076 402  HOH   HOH B . 
Z  7 HOH   177 1077 873  HOH   HOH B . 
Z  7 HOH   178 1078 820  HOH   HOH B . 
Z  7 HOH   179 1079 600  HOH   HOH B . 
Z  7 HOH   180 1080 374  HOH   HOH B . 
Z  7 HOH   181 1081 74   HOH   HOH B . 
Z  7 HOH   182 1082 792  HOH   HOH B . 
Z  7 HOH   183 1083 674  HOH   HOH B . 
Z  7 HOH   184 1084 1112 HOH   HOH B . 
Z  7 HOH   185 1085 1122 HOH   HOH B . 
Z  7 HOH   186 1086 588  HOH   HOH B . 
Z  7 HOH   187 1087 248  HOH   HOH B . 
Z  7 HOH   188 1088 410  HOH   HOH B . 
Z  7 HOH   189 1089 632  HOH   HOH B . 
Z  7 HOH   190 1090 359  HOH   HOH B . 
Z  7 HOH   191 1091 449  HOH   HOH B . 
Z  7 HOH   192 1092 989  HOH   HOH B . 
Z  7 HOH   193 1093 562  HOH   HOH B . 
Z  7 HOH   194 1094 84   HOH   HOH B . 
Z  7 HOH   195 1095 106  HOH   HOH B . 
Z  7 HOH   196 1096 198  HOH   HOH B . 
Z  7 HOH   197 1097 709  HOH   HOH B . 
Z  7 HOH   198 1098 1105 HOH   HOH B . 
Z  7 HOH   199 1099 573  HOH   HOH B . 
Z  7 HOH   200 1100 635  HOH   HOH B . 
Z  7 HOH   201 1101 462  HOH   HOH B . 
Z  7 HOH   202 1102 626  HOH   HOH B . 
Z  7 HOH   203 1103 934  HOH   HOH B . 
Z  7 HOH   204 1104 971  HOH   HOH B . 
Z  7 HOH   205 1105 378  HOH   HOH B . 
Z  7 HOH   206 1106 175  HOH   HOH B . 
Z  7 HOH   207 1107 570  HOH   HOH B . 
Z  7 HOH   208 1108 49   HOH   HOH B . 
Z  7 HOH   209 1109 1082 HOH   HOH B . 
Z  7 HOH   210 1110 203  HOH   HOH B . 
Z  7 HOH   211 1111 546  HOH   HOH B . 
Z  7 HOH   212 1112 529  HOH   HOH B . 
Z  7 HOH   213 1113 927  HOH   HOH B . 
Z  7 HOH   214 1114 1108 HOH   HOH B . 
Z  7 HOH   215 1115 407  HOH   HOH B . 
Z  7 HOH   216 1116 166  HOH   HOH B . 
Z  7 HOH   217 1117 1076 HOH   HOH B . 
Z  7 HOH   218 1118 648  HOH   HOH B . 
Z  7 HOH   219 1119 1074 HOH   HOH B . 
Z  7 HOH   220 1120 1129 HOH   HOH B . 
Z  7 HOH   221 1121 905  HOH   HOH B . 
Z  7 HOH   222 1122 352  HOH   HOH B . 
Z  7 HOH   223 1123 1119 HOH   HOH B . 
Z  7 HOH   224 1124 539  HOH   HOH B . 
Z  7 HOH   225 1125 225  HOH   HOH B . 
Z  7 HOH   226 1126 819  HOH   HOH B . 
Z  7 HOH   227 1127 1117 HOH   HOH B . 
Z  7 HOH   228 1128 1084 HOH   HOH B . 
Z  7 HOH   229 1129 345  HOH   HOH B . 
Z  7 HOH   230 1130 1111 HOH   HOH B . 
Z  7 HOH   231 1131 498  HOH   HOH B . 
Z  7 HOH   232 1132 812  HOH   HOH B . 
Z  7 HOH   233 1133 851  HOH   HOH B . 
Z  7 HOH   234 1134 1069 HOH   HOH B . 
Z  7 HOH   235 1135 610  HOH   HOH B . 
Z  7 HOH   236 1136 969  HOH   HOH B . 
Z  7 HOH   237 1137 914  HOH   HOH B . 
Z  7 HOH   238 1138 1093 HOH   HOH B . 
Z  7 HOH   239 1139 973  HOH   HOH B . 
Z  7 HOH   240 1140 607  HOH   HOH B . 
Z  7 HOH   241 1141 1114 HOH   HOH B . 
Z  7 HOH   242 1142 970  HOH   HOH B . 
Z  7 HOH   243 1143 1127 HOH   HOH B . 
Z  7 HOH   244 1144 775  HOH   HOH B . 
Z  7 HOH   245 1145 1116 HOH   HOH B . 
Z  7 HOH   246 1146 930  HOH   HOH B . 
Z  7 HOH   247 1147 246  HOH   HOH B . 
Z  7 HOH   248 1148 965  HOH   HOH B . 
Z  7 HOH   249 1149 729  HOH   HOH B . 
Z  7 HOH   250 1150 694  HOH   HOH B . 
Z  7 HOH   251 1151 1102 HOH   HOH B . 
Z  7 HOH   252 1152 703  HOH   HOH B . 
Z  7 HOH   253 1153 813  HOH   HOH B . 
Z  7 HOH   254 1154 450  HOH   HOH B . 
Z  7 HOH   255 1155 537  HOH   HOH B . 
Z  7 HOH   256 1156 267  HOH   HOH B . 
Z  7 HOH   257 1157 689  HOH   HOH B . 
Z  7 HOH   258 1158 336  HOH   HOH B . 
Z  7 HOH   259 1159 1087 HOH   HOH B . 
Z  7 HOH   260 1160 543  HOH   HOH B . 
Z  7 HOH   261 1161 301  HOH   HOH B . 
Z  7 HOH   262 1162 968  HOH   HOH B . 
Z  7 HOH   263 1163 611  HOH   HOH B . 
Z  7 HOH   264 1164 936  HOH   HOH B . 
Z  7 HOH   265 1165 1124 HOH   HOH B . 
Z  7 HOH   266 1166 742  HOH   HOH B . 
Z  7 HOH   267 1167 339  HOH   HOH B . 
Z  7 HOH   268 1168 886  HOH   HOH B . 
Z  7 HOH   269 1169 1079 HOH   HOH B . 
Z  7 HOH   270 1170 685  HOH   HOH B . 
Z  7 HOH   271 1171 808  HOH   HOH B . 
Z  7 HOH   272 1172 892  HOH   HOH B . 
Z  7 HOH   273 1173 783  HOH   HOH B . 
Z  7 HOH   274 1174 977  HOH   HOH B . 
Z  7 HOH   275 1175 738  HOH   HOH B . 
Z  7 HOH   276 1176 593  HOH   HOH B . 
Z  7 HOH   277 1177 604  HOH   HOH B . 
Z  7 HOH   278 1178 752  HOH   HOH B . 
Z  7 HOH   279 1179 448  HOH   HOH B . 
Z  7 HOH   280 1180 1095 HOH   HOH B . 
Z  7 HOH   281 1181 1085 HOH   HOH B . 
Z  7 HOH   282 1182 1104 HOH   HOH B . 
Z  7 HOH   283 1183 773  HOH   HOH B . 
Z  7 HOH   284 1184 403  HOH   HOH B . 
Z  7 HOH   285 1185 434  HOH   HOH B . 
Z  7 HOH   286 1186 966  HOH   HOH B . 
Z  7 HOH   287 1187 616  HOH   HOH B . 
Z  7 HOH   288 1188 1088 HOH   HOH B . 
Z  7 HOH   289 1189 849  HOH   HOH B . 
Z  7 HOH   290 1190 928  HOH   HOH B . 
Z  7 HOH   291 1191 460  HOH   HOH B . 
Z  7 HOH   292 1192 921  HOH   HOH B . 
Z  7 HOH   293 1193 716  HOH   HOH B . 
Z  7 HOH   294 1194 1128 HOH   HOH B . 
Z  7 HOH   295 1195 720  HOH   HOH B . 
Z  7 HOH   296 1196 1075 HOH   HOH B . 
Z  7 HOH   297 1197 1126 HOH   HOH B . 
Z  7 HOH   298 1198 1096 HOH   HOH B . 
Z  7 HOH   299 1199 678  HOH   HOH B . 
Z  7 HOH   300 1200 515  HOH   HOH B . 
Z  7 HOH   301 1201 660  HOH   HOH B . 
Z  7 HOH   302 1202 690  HOH   HOH B . 
Z  7 HOH   303 1203 1113 HOH   HOH B . 
Z  7 HOH   304 1204 715  HOH   HOH B . 
Z  7 HOH   305 1205 634  HOH   HOH B . 
Z  7 HOH   306 1206 1086 HOH   HOH B . 
Z  7 HOH   307 1207 408  HOH   HOH B . 
Z  7 HOH   308 1208 733  HOH   HOH B . 
Z  7 HOH   309 1209 467  HOH   HOH B . 
Z  7 HOH   310 1210 321  HOH   HOH B . 
Z  7 HOH   311 1211 623  HOH   HOH B . 
Z  7 HOH   312 1212 1120 HOH   HOH B . 
Z  7 HOH   313 1213 679  HOH   HOH B . 
Z  7 HOH   314 1214 1109 HOH   HOH B . 
Z  7 HOH   315 1215 1106 HOH   HOH B . 
Z  7 HOH   316 1216 822  HOH   HOH B . 
Z  7 HOH   317 1217 508  HOH   HOH B . 
Z  7 HOH   318 1218 663  HOH   HOH B . 
Z  7 HOH   319 1219 569  HOH   HOH B . 
Z  7 HOH   320 1220 572  HOH   HOH B . 
AA 7 HOH   1   901  1157 HOH   HOH C . 
AA 7 HOH   2   902  1174 HOH   HOH C . 
AA 7 HOH   3   903  948  HOH   HOH C . 
AA 7 HOH   4   904  1199 HOH   HOH C . 
AA 7 HOH   5   905  702  HOH   HOH C . 
AA 7 HOH   6   906  1207 HOH   HOH C . 
AA 7 HOH   7   907  1158 HOH   HOH C . 
AA 7 HOH   8   908  950  HOH   HOH C . 
AA 7 HOH   9   909  691  HOH   HOH C . 
AA 7 HOH   10  910  856  HOH   HOH C . 
AA 7 HOH   11  911  36   HOH   HOH C . 
AA 7 HOH   12  912  697  HOH   HOH C . 
AA 7 HOH   13  913  734  HOH   HOH C . 
AA 7 HOH   14  914  1156 HOH   HOH C . 
AA 7 HOH   15  915  233  HOH   HOH C . 
AA 7 HOH   16  916  688  HOH   HOH C . 
AA 7 HOH   17  917  479  HOH   HOH C . 
AA 7 HOH   18  918  947  HOH   HOH C . 
AA 7 HOH   19  919  631  HOH   HOH C . 
AA 7 HOH   20  920  193  HOH   HOH C . 
AA 7 HOH   21  921  762  HOH   HOH C . 
AA 7 HOH   22  922  329  HOH   HOH C . 
AA 7 HOH   23  923  315  HOH   HOH C . 
AA 7 HOH   24  924  1146 HOH   HOH C . 
AA 7 HOH   25  925  1194 HOH   HOH C . 
AA 7 HOH   26  926  139  HOH   HOH C . 
AA 7 HOH   27  927  245  HOH   HOH C . 
AA 7 HOH   28  928  8    HOH   HOH C . 
AA 7 HOH   29  929  116  HOH   HOH C . 
AA 7 HOH   30  930  1189 HOH   HOH C . 
AA 7 HOH   31  931  153  HOH   HOH C . 
AA 7 HOH   32  932  92   HOH   HOH C . 
AA 7 HOH   33  933  686  HOH   HOH C . 
AA 7 HOH   34  934  150  HOH   HOH C . 
AA 7 HOH   35  935  454  HOH   HOH C . 
AA 7 HOH   36  936  121  HOH   HOH C . 
AA 7 HOH   37  937  381  HOH   HOH C . 
AA 7 HOH   38  938  2    HOH   HOH C . 
AA 7 HOH   39  939  54   HOH   HOH C . 
AA 7 HOH   40  940  57   HOH   HOH C . 
AA 7 HOH   41  941  312  HOH   HOH C . 
AA 7 HOH   42  942  453  HOH   HOH C . 
AA 7 HOH   43  943  337  HOH   HOH C . 
AA 7 HOH   44  944  513  HOH   HOH C . 
AA 7 HOH   45  945  45   HOH   HOH C . 
AA 7 HOH   46  946  547  HOH   HOH C . 
AA 7 HOH   47  947  75   HOH   HOH C . 
AA 7 HOH   48  948  256  HOH   HOH C . 
AA 7 HOH   49  949  727  HOH   HOH C . 
AA 7 HOH   50  950  291  HOH   HOH C . 
AA 7 HOH   51  951  737  HOH   HOH C . 
AA 7 HOH   52  952  210  HOH   HOH C . 
AA 7 HOH   53  953  755  HOH   HOH C . 
AA 7 HOH   54  954  51   HOH   HOH C . 
AA 7 HOH   55  955  268  HOH   HOH C . 
AA 7 HOH   56  956  516  HOH   HOH C . 
AA 7 HOH   57  957  180  HOH   HOH C . 
AA 7 HOH   58  958  142  HOH   HOH C . 
AA 7 HOH   59  959  373  HOH   HOH C . 
AA 7 HOH   60  960  919  HOH   HOH C . 
AA 7 HOH   61  961  889  HOH   HOH C . 
AA 7 HOH   62  962  195  HOH   HOH C . 
AA 7 HOH   63  963  21   HOH   HOH C . 
AA 7 HOH   64  964  311  HOH   HOH C . 
AA 7 HOH   65  965  242  HOH   HOH C . 
AA 7 HOH   66  966  485  HOH   HOH C . 
AA 7 HOH   67  967  642  HOH   HOH C . 
AA 7 HOH   68  968  140  HOH   HOH C . 
AA 7 HOH   69  969  276  HOH   HOH C . 
AA 7 HOH   70  970  23   HOH   HOH C . 
AA 7 HOH   71  971  169  HOH   HOH C . 
AA 7 HOH   72  972  584  HOH   HOH C . 
AA 7 HOH   73  973  5    HOH   HOH C . 
AA 7 HOH   74  974  714  HOH   HOH C . 
AA 7 HOH   75  975  29   HOH   HOH C . 
AA 7 HOH   76  976  514  HOH   HOH C . 
AA 7 HOH   77  977  732  HOH   HOH C . 
AA 7 HOH   78  978  470  HOH   HOH C . 
AA 7 HOH   79  979  155  HOH   HOH C . 
AA 7 HOH   80  980  444  HOH   HOH C . 
AA 7 HOH   81  981  137  HOH   HOH C . 
AA 7 HOH   82  982  760  HOH   HOH C . 
AA 7 HOH   83  983  68   HOH   HOH C . 
AA 7 HOH   84  984  1010 HOH   HOH C . 
AA 7 HOH   85  985  207  HOH   HOH C . 
AA 7 HOH   86  986  438  HOH   HOH C . 
AA 7 HOH   87  987  606  HOH   HOH C . 
AA 7 HOH   88  988  240  HOH   HOH C . 
AA 7 HOH   89  989  190  HOH   HOH C . 
AA 7 HOH   90  990  1173 HOH   HOH C . 
AA 7 HOH   91  991  327  HOH   HOH C . 
AA 7 HOH   92  992  28   HOH   HOH C . 
AA 7 HOH   93  993  468  HOH   HOH C . 
AA 7 HOH   94  994  237  HOH   HOH C . 
AA 7 HOH   95  995  484  HOH   HOH C . 
AA 7 HOH   96  996  32   HOH   HOH C . 
AA 7 HOH   97  997  183  HOH   HOH C . 
AA 7 HOH   98  998  622  HOH   HOH C . 
AA 7 HOH   99  999  698  HOH   HOH C . 
AA 7 HOH   100 1000 1185 HOH   HOH C . 
AA 7 HOH   101 1001 97   HOH   HOH C . 
AA 7 HOH   102 1002 99   HOH   HOH C . 
AA 7 HOH   103 1003 1186 HOH   HOH C . 
AA 7 HOH   104 1004 1182 HOH   HOH C . 
AA 7 HOH   105 1005 1167 HOH   HOH C . 
AA 7 HOH   106 1006 85   HOH   HOH C . 
AA 7 HOH   107 1007 857  HOH   HOH C . 
AA 7 HOH   108 1008 244  HOH   HOH C . 
AA 7 HOH   109 1009 396  HOH   HOH C . 
AA 7 HOH   110 1010 156  HOH   HOH C . 
AA 7 HOH   111 1011 1026 HOH   HOH C . 
AA 7 HOH   112 1012 1147 HOH   HOH C . 
AA 7 HOH   113 1013 27   HOH   HOH C . 
AA 7 HOH   114 1014 120  HOH   HOH C . 
AA 7 HOH   115 1015 578  HOH   HOH C . 
AA 7 HOH   116 1016 1179 HOH   HOH C . 
AA 7 HOH   117 1017 290  HOH   HOH C . 
AA 7 HOH   118 1018 643  HOH   HOH C . 
AA 7 HOH   119 1019 293  HOH   HOH C . 
AA 7 HOH   120 1020 872  HOH   HOH C . 
AA 7 HOH   121 1021 14   HOH   HOH C . 
AA 7 HOH   122 1022 347  HOH   HOH C . 
AA 7 HOH   123 1023 811  HOH   HOH C . 
AA 7 HOH   124 1024 658  HOH   HOH C . 
AA 7 HOH   125 1025 87   HOH   HOH C . 
AA 7 HOH   126 1026 456  HOH   HOH C . 
AA 7 HOH   127 1027 1172 HOH   HOH C . 
AA 7 HOH   128 1028 765  HOH   HOH C . 
AA 7 HOH   129 1029 421  HOH   HOH C . 
AA 7 HOH   130 1030 91   HOH   HOH C . 
AA 7 HOH   131 1031 1175 HOH   HOH C . 
AA 7 HOH   132 1032 442  HOH   HOH C . 
AA 7 HOH   133 1033 362  HOH   HOH C . 
AA 7 HOH   134 1034 791  HOH   HOH C . 
AA 7 HOH   135 1035 76   HOH   HOH C . 
AA 7 HOH   136 1036 1190 HOH   HOH C . 
AA 7 HOH   137 1037 364  HOH   HOH C . 
AA 7 HOH   138 1038 64   HOH   HOH C . 
AA 7 HOH   139 1039 67   HOH   HOH C . 
AA 7 HOH   140 1040 653  HOH   HOH C . 
AA 7 HOH   141 1041 184  HOH   HOH C . 
AA 7 HOH   142 1042 793  HOH   HOH C . 
AA 7 HOH   143 1043 371  HOH   HOH C . 
AA 7 HOH   144 1044 25   HOH   HOH C . 
AA 7 HOH   145 1045 597  HOH   HOH C . 
AA 7 HOH   146 1046 238  HOH   HOH C . 
AA 7 HOH   147 1047 59   HOH   HOH C . 
AA 7 HOH   148 1048 500  HOH   HOH C . 
AA 7 HOH   149 1049 837  HOH   HOH C . 
AA 7 HOH   150 1050 439  HOH   HOH C . 
AA 7 HOH   151 1051 78   HOH   HOH C . 
AA 7 HOH   152 1052 277  HOH   HOH C . 
AA 7 HOH   153 1053 494  HOH   HOH C . 
AA 7 HOH   154 1054 463  HOH   HOH C . 
AA 7 HOH   155 1055 296  HOH   HOH C . 
AA 7 HOH   156 1056 305  HOH   HOH C . 
AA 7 HOH   157 1057 884  HOH   HOH C . 
AA 7 HOH   158 1058 55   HOH   HOH C . 
AA 7 HOH   159 1059 93   HOH   HOH C . 
AA 7 HOH   160 1060 168  HOH   HOH C . 
AA 7 HOH   161 1061 778  HOH   HOH C . 
AA 7 HOH   162 1062 637  HOH   HOH C . 
AA 7 HOH   163 1063 320  HOH   HOH C . 
AA 7 HOH   164 1064 1211 HOH   HOH C . 
AA 7 HOH   165 1065 896  HOH   HOH C . 
AA 7 HOH   166 1066 1181 HOH   HOH C . 
AA 7 HOH   167 1067 222  HOH   HOH C . 
AA 7 HOH   168 1068 299  HOH   HOH C . 
AA 7 HOH   169 1069 501  HOH   HOH C . 
AA 7 HOH   170 1070 526  HOH   HOH C . 
AA 7 HOH   171 1071 833  HOH   HOH C . 
AA 7 HOH   172 1072 945  HOH   HOH C . 
AA 7 HOH   173 1073 161  HOH   HOH C . 
AA 7 HOH   174 1074 200  HOH   HOH C . 
AA 7 HOH   175 1075 363  HOH   HOH C . 
AA 7 HOH   176 1076 1209 HOH   HOH C . 
AA 7 HOH   177 1077 509  HOH   HOH C . 
AA 7 HOH   178 1078 58   HOH   HOH C . 
AA 7 HOH   179 1079 949  HOH   HOH C . 
AA 7 HOH   180 1080 640  HOH   HOH C . 
AA 7 HOH   181 1081 417  HOH   HOH C . 
AA 7 HOH   182 1082 115  HOH   HOH C . 
AA 7 HOH   183 1083 641  HOH   HOH C . 
AA 7 HOH   184 1084 926  HOH   HOH C . 
AA 7 HOH   185 1085 798  HOH   HOH C . 
AA 7 HOH   186 1086 576  HOH   HOH C . 
AA 7 HOH   187 1087 776  HOH   HOH C . 
AA 7 HOH   188 1088 1166 HOH   HOH C . 
AA 7 HOH   189 1089 131  HOH   HOH C . 
AA 7 HOH   190 1090 1204 HOH   HOH C . 
AA 7 HOH   191 1091 208  HOH   HOH C . 
AA 7 HOH   192 1092 1159 HOH   HOH C . 
AA 7 HOH   193 1093 72   HOH   HOH C . 
AA 7 HOH   194 1094 447  HOH   HOH C . 
AA 7 HOH   195 1095 368  HOH   HOH C . 
AA 7 HOH   196 1096 876  HOH   HOH C . 
AA 7 HOH   197 1097 427  HOH   HOH C . 
AA 7 HOH   198 1098 871  HOH   HOH C . 
AA 7 HOH   199 1099 1188 HOH   HOH C . 
AA 7 HOH   200 1100 613  HOH   HOH C . 
AA 7 HOH   201 1101 577  HOH   HOH C . 
AA 7 HOH   202 1102 425  HOH   HOH C . 
AA 7 HOH   203 1103 527  HOH   HOH C . 
AA 7 HOH   204 1104 850  HOH   HOH C . 
AA 7 HOH   205 1105 535  HOH   HOH C . 
AA 7 HOH   206 1106 341  HOH   HOH C . 
AA 7 HOH   207 1107 803  HOH   HOH C . 
AA 7 HOH   208 1108 675  HOH   HOH C . 
AA 7 HOH   209 1109 319  HOH   HOH C . 
AA 7 HOH   210 1110 682  HOH   HOH C . 
AA 7 HOH   211 1111 1141 HOH   HOH C . 
AA 7 HOH   212 1112 422  HOH   HOH C . 
AA 7 HOH   213 1113 471  HOH   HOH C . 
AA 7 HOH   214 1114 173  HOH   HOH C . 
AA 7 HOH   215 1115 589  HOH   HOH C . 
AA 7 HOH   216 1116 389  HOH   HOH C . 
AA 7 HOH   217 1117 712  HOH   HOH C . 
AA 7 HOH   218 1118 766  HOH   HOH C . 
AA 7 HOH   219 1119 46   HOH   HOH C . 
AA 7 HOH   220 1120 1162 HOH   HOH C . 
AA 7 HOH   221 1121 560  HOH   HOH C . 
AA 7 HOH   222 1122 383  HOH   HOH C . 
AA 7 HOH   223 1123 170  HOH   HOH C . 
AA 7 HOH   224 1124 835  HOH   HOH C . 
AA 7 HOH   225 1125 858  HOH   HOH C . 
AA 7 HOH   226 1126 443  HOH   HOH C . 
AA 7 HOH   227 1127 251  HOH   HOH C . 
AA 7 HOH   228 1128 239  HOH   HOH C . 
AA 7 HOH   229 1129 902  HOH   HOH C . 
AA 7 HOH   230 1130 700  HOH   HOH C . 
AA 7 HOH   231 1131 910  HOH   HOH C . 
AA 7 HOH   232 1132 1202 HOH   HOH C . 
AA 7 HOH   233 1133 1168 HOH   HOH C . 
AA 7 HOH   234 1134 1193 HOH   HOH C . 
AA 7 HOH   235 1135 423  HOH   HOH C . 
AA 7 HOH   236 1136 134  HOH   HOH C . 
AA 7 HOH   237 1137 1160 HOH   HOH C . 
AA 7 HOH   238 1138 1208 HOH   HOH C . 
AA 7 HOH   239 1139 441  HOH   HOH C . 
AA 7 HOH   240 1140 646  HOH   HOH C . 
AA 7 HOH   241 1141 1198 HOH   HOH C . 
AA 7 HOH   242 1142 603  HOH   HOH C . 
AA 7 HOH   243 1143 549  HOH   HOH C . 
AA 7 HOH   244 1144 669  HOH   HOH C . 
AA 7 HOH   245 1145 951  HOH   HOH C . 
AA 7 HOH   246 1146 825  HOH   HOH C . 
AA 7 HOH   247 1147 826  HOH   HOH C . 
AA 7 HOH   248 1148 370  HOH   HOH C . 
AA 7 HOH   249 1149 1180 HOH   HOH C . 
AA 7 HOH   250 1150 271  HOH   HOH C . 
AA 7 HOH   251 1151 1191 HOH   HOH C . 
AA 7 HOH   252 1152 608  HOH   HOH C . 
AA 7 HOH   253 1153 866  HOH   HOH C . 
AA 7 HOH   254 1154 868  HOH   HOH C . 
AA 7 HOH   255 1155 953  HOH   HOH C . 
AA 7 HOH   256 1156 804  HOH   HOH C . 
AA 7 HOH   257 1157 946  HOH   HOH C . 
AA 7 HOH   258 1158 625  HOH   HOH C . 
AA 7 HOH   259 1159 1143 HOH   HOH C . 
AA 7 HOH   260 1160 1183 HOH   HOH C . 
AA 7 HOH   261 1161 881  HOH   HOH C . 
AA 7 HOH   262 1162 681  HOH   HOH C . 
AA 7 HOH   263 1163 823  HOH   HOH C . 
AA 7 HOH   264 1164 1171 HOH   HOH C . 
AA 7 HOH   265 1165 201  HOH   HOH C . 
AA 7 HOH   266 1166 863  HOH   HOH C . 
AA 7 HOH   267 1167 877  HOH   HOH C . 
AA 7 HOH   268 1168 517  HOH   HOH C . 
AA 7 HOH   269 1169 1030 HOH   HOH C . 
AA 7 HOH   270 1170 939  HOH   HOH C . 
AA 7 HOH   271 1171 1200 HOH   HOH C . 
AA 7 HOH   272 1172 899  HOH   HOH C . 
AA 7 HOH   273 1173 595  HOH   HOH C . 
AA 7 HOH   274 1174 566  HOH   HOH C . 
AA 7 HOH   275 1175 931  HOH   HOH C . 
AA 7 HOH   276 1176 924  HOH   HOH C . 
AA 7 HOH   277 1177 1187 HOH   HOH C . 
AA 7 HOH   278 1178 598  HOH   HOH C . 
AA 7 HOH   279 1179 1192 HOH   HOH C . 
AA 7 HOH   280 1180 1197 HOH   HOH C . 
AA 7 HOH   281 1181 1206 HOH   HOH C . 
AA 7 HOH   282 1182 771  HOH   HOH C . 
AA 7 HOH   283 1183 1169 HOH   HOH C . 
AA 7 HOH   284 1184 1144 HOH   HOH C . 
AA 7 HOH   285 1185 911  HOH   HOH C . 
AA 7 HOH   286 1186 558  HOH   HOH C . 
AA 7 HOH   287 1187 338  HOH   HOH C . 
AA 7 HOH   288 1188 559  HOH   HOH C . 
AA 7 HOH   289 1189 620  HOH   HOH C . 
AA 7 HOH   290 1190 495  HOH   HOH C . 
AA 7 HOH   291 1191 882  HOH   HOH C . 
AA 7 HOH   292 1192 1161 HOH   HOH C . 
AA 7 HOH   293 1193 767  HOH   HOH C . 
AA 7 HOH   294 1194 655  HOH   HOH C . 
AA 7 HOH   295 1195 1163 HOH   HOH C . 
AA 7 HOH   296 1196 739  HOH   HOH C . 
AA 7 HOH   297 1197 574  HOH   HOH C . 
AA 7 HOH   298 1198 532  HOH   HOH C . 
AA 7 HOH   299 1199 1165 HOH   HOH C . 
AA 7 HOH   300 1200 401  HOH   HOH C . 
AA 7 HOH   301 1201 1205 HOH   HOH C . 
AA 7 HOH   302 1202 1178 HOH   HOH C . 
AA 7 HOH   303 1203 1203 HOH   HOH C . 
AA 7 HOH   304 1204 938  HOH   HOH C . 
AA 7 HOH   305 1205 818  HOH   HOH C . 
AA 7 HOH   306 1206 1184 HOH   HOH C . 
AA 7 HOH   307 1207 929  HOH   HOH C . 
AA 7 HOH   308 1208 769  HOH   HOH C . 
AA 7 HOH   309 1209 952  HOH   HOH C . 
AA 7 HOH   310 1210 1145 HOH   HOH C . 
AA 7 HOH   311 1211 656  HOH   HOH C . 
AA 7 HOH   312 1212 705  HOH   HOH C . 
AA 7 HOH   313 1213 636  HOH   HOH C . 
AA 7 HOH   314 1214 1177 HOH   HOH C . 
AA 7 HOH   315 1215 817  HOH   HOH C . 
AA 7 HOH   316 1216 918  HOH   HOH C . 
AA 7 HOH   317 1217 1164 HOH   HOH C . 
AA 7 HOH   318 1218 1212 HOH   HOH C . 
AA 7 HOH   319 1219 534  HOH   HOH C . 
AA 7 HOH   320 1220 847  HOH   HOH C . 
AA 7 HOH   321 1221 743  HOH   HOH C . 
AA 7 HOH   322 1222 907  HOH   HOH C . 
AA 7 HOH   323 1223 864  HOH   HOH C . 
AA 7 HOH   324 1224 1170 HOH   HOH C . 
AA 7 HOH   325 1225 1142 HOH   HOH C . 
AA 7 HOH   326 1226 844  HOH   HOH C . 
AA 7 HOH   327 1227 1176 HOH   HOH C . 
BA 7 HOH   1   901  1148 HOH   HOH D . 
BA 7 HOH   2   902  1251 HOH   HOH D . 
BA 7 HOH   3   903  1243 HOH   HOH D . 
BA 7 HOH   4   904  1257 HOH   HOH D . 
BA 7 HOH   5   905  940  HOH   HOH D . 
BA 7 HOH   6   906  1252 HOH   HOH D . 
BA 7 HOH   7   907  1101 HOH   HOH D . 
BA 7 HOH   8   908  1245 HOH   HOH D . 
BA 7 HOH   9   909  761  HOH   HOH D . 
BA 7 HOH   10  910  266  HOH   HOH D . 
BA 7 HOH   11  911  432  HOH   HOH D . 
BA 7 HOH   12  912  693  HOH   HOH D . 
BA 7 HOH   13  913  542  HOH   HOH D . 
BA 7 HOH   14  914  506  HOH   HOH D . 
BA 7 HOH   15  915  1231 HOH   HOH D . 
BA 7 HOH   16  916  1196 HOH   HOH D . 
BA 7 HOH   17  917  132  HOH   HOH D . 
BA 7 HOH   18  918  726  HOH   HOH D . 
BA 7 HOH   19  919  1099 HOH   HOH D . 
BA 7 HOH   20  920  885  HOH   HOH D . 
BA 7 HOH   21  921  105  HOH   HOH D . 
BA 7 HOH   22  922  372  HOH   HOH D . 
BA 7 HOH   23  923  699  HOH   HOH D . 
BA 7 HOH   24  924  680  HOH   HOH D . 
BA 7 HOH   25  925  1    HOH   HOH D . 
BA 7 HOH   26  926  435  HOH   HOH D . 
BA 7 HOH   27  927  26   HOH   HOH D . 
BA 7 HOH   28  928  109  HOH   HOH D . 
BA 7 HOH   29  929  376  HOH   HOH D . 
BA 7 HOH   30  930  519  HOH   HOH D . 
BA 7 HOH   31  931  18   HOH   HOH D . 
BA 7 HOH   32  932  944  HOH   HOH D . 
BA 7 HOH   33  933  717  HOH   HOH D . 
BA 7 HOH   34  934  416  HOH   HOH D . 
BA 7 HOH   35  935  123  HOH   HOH D . 
BA 7 HOH   36  936  492  HOH   HOH D . 
BA 7 HOH   37  937  382  HOH   HOH D . 
BA 7 HOH   38  938  35   HOH   HOH D . 
BA 7 HOH   39  939  639  HOH   HOH D . 
BA 7 HOH   40  940  770  HOH   HOH D . 
BA 7 HOH   41  941  392  HOH   HOH D . 
BA 7 HOH   42  942  451  HOH   HOH D . 
BA 7 HOH   43  943  800  HOH   HOH D . 
BA 7 HOH   44  944  430  HOH   HOH D . 
BA 7 HOH   45  945  234  HOH   HOH D . 
BA 7 HOH   46  946  1232 HOH   HOH D . 
BA 7 HOH   47  947  148  HOH   HOH D . 
BA 7 HOH   48  948  1259 HOH   HOH D . 
BA 7 HOH   49  949  111  HOH   HOH D . 
BA 7 HOH   50  950  42   HOH   HOH D . 
BA 7 HOH   51  951  226  HOH   HOH D . 
BA 7 HOH   52  952  43   HOH   HOH D . 
BA 7 HOH   53  953  288  HOH   HOH D . 
BA 7 HOH   54  954  287  HOH   HOH D . 
BA 7 HOH   55  955  228  HOH   HOH D . 
BA 7 HOH   56  956  651  HOH   HOH D . 
BA 7 HOH   57  957  531  HOH   HOH D . 
BA 7 HOH   58  958  1002 HOH   HOH D . 
BA 7 HOH   59  959  490  HOH   HOH D . 
BA 7 HOH   60  960  565  HOH   HOH D . 
BA 7 HOH   61  961  601  HOH   HOH D . 
BA 7 HOH   62  962  71   HOH   HOH D . 
BA 7 HOH   63  963  575  HOH   HOH D . 
BA 7 HOH   64  964  366  HOH   HOH D . 
BA 7 HOH   65  965  556  HOH   HOH D . 
BA 7 HOH   66  966  1240 HOH   HOH D . 
BA 7 HOH   67  967  265  HOH   HOH D . 
BA 7 HOH   68  968  62   HOH   HOH D . 
BA 7 HOH   69  969  243  HOH   HOH D . 
BA 7 HOH   70  970  830  HOH   HOH D . 
BA 7 HOH   71  971  504  HOH   HOH D . 
BA 7 HOH   72  972  458  HOH   HOH D . 
BA 7 HOH   73  973  815  HOH   HOH D . 
BA 7 HOH   74  974  160  HOH   HOH D . 
BA 7 HOH   75  975  65   HOH   HOH D . 
BA 7 HOH   76  976  346  HOH   HOH D . 
BA 7 HOH   77  977  400  HOH   HOH D . 
BA 7 HOH   78  978  316  HOH   HOH D . 
BA 7 HOH   79  979  609  HOH   HOH D . 
BA 7 HOH   80  980  117  HOH   HOH D . 
BA 7 HOH   81  981  415  HOH   HOH D . 
BA 7 HOH   82  982  260  HOH   HOH D . 
BA 7 HOH   83  983  113  HOH   HOH D . 
BA 7 HOH   84  984  127  HOH   HOH D . 
BA 7 HOH   85  985  56   HOH   HOH D . 
BA 7 HOH   86  986  9    HOH   HOH D . 
BA 7 HOH   87  987  82   HOH   HOH D . 
BA 7 HOH   88  988  483  HOH   HOH D . 
BA 7 HOH   89  989  553  HOH   HOH D . 
BA 7 HOH   90  990  342  HOH   HOH D . 
BA 7 HOH   91  991  294  HOH   HOH D . 
BA 7 HOH   92  992  754  HOH   HOH D . 
BA 7 HOH   93  993  821  HOH   HOH D . 
BA 7 HOH   94  994  152  HOH   HOH D . 
BA 7 HOH   95  995  6    HOH   HOH D . 
BA 7 HOH   96  996  272  HOH   HOH D . 
BA 7 HOH   97  997  1219 HOH   HOH D . 
BA 7 HOH   98  998  308  HOH   HOH D . 
BA 7 HOH   99  999  223  HOH   HOH D . 
BA 7 HOH   100 1000 711  HOH   HOH D . 
BA 7 HOH   101 1001 284  HOH   HOH D . 
BA 7 HOH   102 1002 172  HOH   HOH D . 
BA 7 HOH   103 1003 511  HOH   HOH D . 
BA 7 HOH   104 1004 281  HOH   HOH D . 
BA 7 HOH   105 1005 162  HOH   HOH D . 
BA 7 HOH   106 1006 309  HOH   HOH D . 
BA 7 HOH   107 1007 704  HOH   HOH D . 
BA 7 HOH   108 1008 482  HOH   HOH D . 
BA 7 HOH   109 1009 163  HOH   HOH D . 
BA 7 HOH   110 1010 178  HOH   HOH D . 
BA 7 HOH   111 1011 768  HOH   HOH D . 
BA 7 HOH   112 1012 1201 HOH   HOH D . 
BA 7 HOH   113 1013 22   HOH   HOH D . 
BA 7 HOH   114 1014 915  HOH   HOH D . 
BA 7 HOH   115 1015 1227 HOH   HOH D . 
BA 7 HOH   116 1016 1152 HOH   HOH D . 
BA 7 HOH   117 1017 144  HOH   HOH D . 
BA 7 HOH   118 1018 789  HOH   HOH D . 
BA 7 HOH   119 1019 941  HOH   HOH D . 
BA 7 HOH   120 1020 1149 HOH   HOH D . 
BA 7 HOH   121 1021 317  HOH   HOH D . 
BA 7 HOH   122 1022 491  HOH   HOH D . 
BA 7 HOH   123 1023 213  HOH   HOH D . 
BA 7 HOH   124 1024 60   HOH   HOH D . 
BA 7 HOH   125 1025 923  HOH   HOH D . 
BA 7 HOH   126 1026 297  HOH   HOH D . 
BA 7 HOH   127 1027 1220 HOH   HOH D . 
BA 7 HOH   128 1028 780  HOH   HOH D . 
BA 7 HOH   129 1029 263  HOH   HOH D . 
BA 7 HOH   130 1030 1228 HOH   HOH D . 
BA 7 HOH   131 1031 274  HOH   HOH D . 
BA 7 HOH   132 1032 89   HOH   HOH D . 
BA 7 HOH   133 1033 1151 HOH   HOH D . 
BA 7 HOH   134 1034 353  HOH   HOH D . 
BA 7 HOH   135 1035 124  HOH   HOH D . 
BA 7 HOH   136 1036 824  HOH   HOH D . 
BA 7 HOH   137 1037 561  HOH   HOH D . 
BA 7 HOH   138 1038 350  HOH   HOH D . 
BA 7 HOH   139 1039 83   HOH   HOH D . 
BA 7 HOH   140 1040 146  HOH   HOH D . 
BA 7 HOH   141 1041 594  HOH   HOH D . 
BA 7 HOH   142 1042 31   HOH   HOH D . 
BA 7 HOH   143 1043 295  HOH   HOH D . 
BA 7 HOH   144 1044 188  HOH   HOH D . 
BA 7 HOH   145 1045 790  HOH   HOH D . 
BA 7 HOH   146 1046 806  HOH   HOH D . 
BA 7 HOH   147 1047 1258 HOH   HOH D . 
BA 7 HOH   148 1048 855  HOH   HOH D . 
BA 7 HOH   149 1049 1138 HOH   HOH D . 
BA 7 HOH   150 1050 787  HOH   HOH D . 
BA 7 HOH   151 1051 145  HOH   HOH D . 
BA 7 HOH   152 1052 1229 HOH   HOH D . 
BA 7 HOH   153 1053 920  HOH   HOH D . 
BA 7 HOH   154 1054 44   HOH   HOH D . 
BA 7 HOH   155 1055 879  HOH   HOH D . 
BA 7 HOH   156 1056 211  HOH   HOH D . 
BA 7 HOH   157 1057 1239 HOH   HOH D . 
BA 7 HOH   158 1058 424  HOH   HOH D . 
BA 7 HOH   159 1059 579  HOH   HOH D . 
BA 7 HOH   160 1060 1222 HOH   HOH D . 
BA 7 HOH   161 1061 304  HOH   HOH D . 
BA 7 HOH   162 1062 710  HOH   HOH D . 
BA 7 HOH   163 1063 332  HOH   HOH D . 
BA 7 HOH   164 1064 1214 HOH   HOH D . 
BA 7 HOH   165 1065 828  HOH   HOH D . 
BA 7 HOH   166 1066 307  HOH   HOH D . 
BA 7 HOH   167 1067 390  HOH   HOH D . 
BA 7 HOH   168 1068 897  HOH   HOH D . 
BA 7 HOH   169 1069 1244 HOH   HOH D . 
BA 7 HOH   170 1070 1253 HOH   HOH D . 
BA 7 HOH   171 1071 809  HOH   HOH D . 
BA 7 HOH   172 1072 870  HOH   HOH D . 
BA 7 HOH   173 1073 497  HOH   HOH D . 
BA 7 HOH   174 1074 199  HOH   HOH D . 
BA 7 HOH   175 1075 848  HOH   HOH D . 
BA 7 HOH   176 1076 512  HOH   HOH D . 
BA 7 HOH   177 1077 394  HOH   HOH D . 
BA 7 HOH   178 1078 1256 HOH   HOH D . 
BA 7 HOH   179 1079 748  HOH   HOH D . 
BA 7 HOH   180 1080 1247 HOH   HOH D . 
BA 7 HOH   181 1081 555  HOH   HOH D . 
BA 7 HOH   182 1082 1001 HOH   HOH D . 
BA 7 HOH   183 1083 507  HOH   HOH D . 
BA 7 HOH   184 1084 518  HOH   HOH D . 
BA 7 HOH   185 1085 236  HOH   HOH D . 
BA 7 HOH   186 1086 289  HOH   HOH D . 
BA 7 HOH   187 1087 1260 HOH   HOH D . 
BA 7 HOH   188 1088 746  HOH   HOH D . 
BA 7 HOH   189 1089 1249 HOH   HOH D . 
BA 7 HOH   190 1090 252  HOH   HOH D . 
BA 7 HOH   191 1091 1263 HOH   HOH D . 
BA 7 HOH   192 1092 614  HOH   HOH D . 
BA 7 HOH   193 1093 1210 HOH   HOH D . 
BA 7 HOH   194 1094 563  HOH   HOH D . 
BA 7 HOH   195 1095 880  HOH   HOH D . 
BA 7 HOH   196 1096 355  HOH   HOH D . 
BA 7 HOH   197 1097 1254 HOH   HOH D . 
BA 7 HOH   198 1098 530  HOH   HOH D . 
BA 7 HOH   199 1099 677  HOH   HOH D . 
BA 7 HOH   200 1100 101  HOH   HOH D . 
BA 7 HOH   201 1101 1224 HOH   HOH D . 
BA 7 HOH   202 1102 1248 HOH   HOH D . 
BA 7 HOH   203 1103 486  HOH   HOH D . 
BA 7 HOH   204 1104 505  HOH   HOH D . 
BA 7 HOH   205 1105 554  HOH   HOH D . 
BA 7 HOH   206 1106 900  HOH   HOH D . 
BA 7 HOH   207 1107 1223 HOH   HOH D . 
BA 7 HOH   208 1108 1233 HOH   HOH D . 
BA 7 HOH   209 1109 1246 HOH   HOH D . 
BA 7 HOH   210 1110 854  HOH   HOH D . 
BA 7 HOH   211 1111 619  HOH   HOH D . 
BA 7 HOH   212 1112 324  HOH   HOH D . 
BA 7 HOH   213 1113 128  HOH   HOH D . 
BA 7 HOH   214 1114 224  HOH   HOH D . 
BA 7 HOH   215 1115 1140 HOH   HOH D . 
BA 7 HOH   216 1116 772  HOH   HOH D . 
BA 7 HOH   217 1117 1218 HOH   HOH D . 
BA 7 HOH   218 1118 229  HOH   HOH D . 
BA 7 HOH   219 1119 1241 HOH   HOH D . 
BA 7 HOH   220 1120 917  HOH   HOH D . 
BA 7 HOH   221 1121 1250 HOH   HOH D . 
BA 7 HOH   222 1122 1213 HOH   HOH D . 
BA 7 HOH   223 1123 1139 HOH   HOH D . 
BA 7 HOH   224 1124 328  HOH   HOH D . 
BA 7 HOH   225 1125 624  HOH   HOH D . 
BA 7 HOH   226 1126 890  HOH   HOH D . 
BA 7 HOH   227 1127 1225 HOH   HOH D . 
BA 7 HOH   228 1128 270  HOH   HOH D . 
BA 7 HOH   229 1129 1215 HOH   HOH D . 
BA 7 HOH   230 1130 602  HOH   HOH D . 
BA 7 HOH   231 1131 1262 HOH   HOH D . 
BA 7 HOH   232 1132 1216 HOH   HOH D . 
BA 7 HOH   233 1133 759  HOH   HOH D . 
BA 7 HOH   234 1134 1153 HOH   HOH D . 
BA 7 HOH   235 1135 671  HOH   HOH D . 
BA 7 HOH   236 1136 1255 HOH   HOH D . 
BA 7 HOH   237 1137 862  HOH   HOH D . 
BA 7 HOH   238 1138 1100 HOH   HOH D . 
BA 7 HOH   239 1139 913  HOH   HOH D . 
BA 7 HOH   240 1140 978  HOH   HOH D . 
BA 7 HOH   241 1141 1236 HOH   HOH D . 
BA 7 HOH   242 1142 369  HOH   HOH D . 
BA 7 HOH   243 1143 1150 HOH   HOH D . 
BA 7 HOH   244 1144 865  HOH   HOH D . 
BA 7 HOH   245 1145 1230 HOH   HOH D . 
BA 7 HOH   246 1146 1003 HOH   HOH D . 
BA 7 HOH   247 1147 1221 HOH   HOH D . 
BA 7 HOH   248 1148 723  HOH   HOH D . 
BA 7 HOH   249 1149 385  HOH   HOH D . 
BA 7 HOH   250 1150 269  HOH   HOH D . 
BA 7 HOH   251 1151 986  HOH   HOH D . 
BA 7 HOH   252 1152 357  HOH   HOH D . 
BA 7 HOH   253 1153 1195 HOH   HOH D . 
BA 7 HOH   254 1154 893  HOH   HOH D . 
BA 7 HOH   255 1155 1261 HOH   HOH D . 
BA 7 HOH   256 1156 1154 HOH   HOH D . 
BA 7 HOH   257 1157 943  HOH   HOH D . 
BA 7 HOH   258 1158 1234 HOH   HOH D . 
BA 7 HOH   259 1159 1155 HOH   HOH D . 
BA 7 HOH   260 1160 842  HOH   HOH D . 
BA 7 HOH   261 1161 536  HOH   HOH D . 
BA 7 HOH   262 1162 1237 HOH   HOH D . 
BA 7 HOH   263 1163 395  HOH   HOH D . 
BA 7 HOH   264 1164 496  HOH   HOH D . 
BA 7 HOH   265 1165 728  HOH   HOH D . 
BA 7 HOH   266 1166 932  HOH   HOH D . 
BA 7 HOH   267 1167 398  HOH   HOH D . 
BA 7 HOH   268 1168 777  HOH   HOH D . 
BA 7 HOH   269 1169 657  HOH   HOH D . 
BA 7 HOH   270 1170 898  HOH   HOH D . 
BA 7 HOH   271 1171 474  HOH   HOH D . 
BA 7 HOH   272 1172 1242 HOH   HOH D . 
BA 7 HOH   273 1173 1238 HOH   HOH D . 
BA 7 HOH   274 1174 567  HOH   HOH D . 
BA 7 HOH   275 1175 908  HOH   HOH D . 
BA 7 HOH   276 1176 741  HOH   HOH D . 
BA 7 HOH   277 1177 942  HOH   HOH D . 
BA 7 HOH   278 1178 816  HOH   HOH D . 
BA 7 HOH   279 1179 581  HOH   HOH D . 
BA 7 HOH   280 1180 477  HOH   HOH D . 
BA 7 HOH   281 1181 888  HOH   HOH D . 
BA 7 HOH   282 1182 649  HOH   HOH D . 
BA 7 HOH   283 1183 1226 HOH   HOH D . 
BA 7 HOH   284 1184 487  HOH   HOH D . 
BA 7 HOH   285 1185 557  HOH   HOH D . 
BA 7 HOH   286 1186 838  HOH   HOH D . 
BA 7 HOH   287 1187 331  HOH   HOH D . 
BA 7 HOH   288 1188 883  HOH   HOH D . 
BA 7 HOH   289 1189 1235 HOH   HOH D . 
BA 7 HOH   290 1190 617  HOH   HOH D . 
BA 7 HOH   291 1191 670  HOH   HOH D . 
BA 7 HOH   292 1192 906  HOH   HOH D . 
BA 7 HOH   293 1193 418  HOH   HOH D . 
BA 7 HOH   294 1194 935  HOH   HOH D . 
# 
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                   90.04 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CW1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.562 
_cell.length_a_esd                 ? 
_cell.length_b                     116.068 
_cell.length_b_esd                 ? 
_cell.length_c                     163.034 
_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                         9CW1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9CW1 
_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             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.2 
_exptl_crystal.description                  plates 
_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              7.2 
_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    '8% PEG3350, 35 mM citric acid, 65 mM Bis-Tris propane, 10% glycerol, 5 mM TCEP' 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-03-24 
_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 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CW1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               49.15 
_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                                     150418 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.5 
_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                                0.142 
_reflns.pdbx_Rpim_I_all                                0.077 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       494643 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.118 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.90 
_reflns_shell.d_res_low                                     1.93 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           24753 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7402 
_reflns_shell.percent_possible_obs                          99.8 
_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                               3.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               1.804 
_reflns_shell.pdbx_Rpim_I_all                               0.981 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.341 
_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                                  1.506 
_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                                 9CW1 
_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                            1.900 
_refine.ls_d_res_low                             49.15 
_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                     149322 
_refine.ls_number_reflns_R_free                  14572 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.52 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1773 
_refine.ls_R_factor_R_free                       0.2195 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1751 
_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                          0.66 
_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                 23.92 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.27 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13558 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         358 
_refine_hist.number_atoms_solvent             1263 
_refine_hist.number_atoms_total               15179 
_refine_hist.d_res_high                       1.900 
_refine_hist.d_res_low                        49.15 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 14435 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.950  ? 19662 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.477 ? 8436  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051  ? 2030  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 2486  ? 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' 1.9000 1.9216 . . 447 8156 86.00 . . . . 0.3631 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 1.9216 1.9442 . . 473 8642 93.00 . . . . 0.3410 . . . . . . . . . . . 0.3878 
'X-RAY DIFFRACTION' 1.9442 1.9679 . . 537 9074 96.00 . . . . 0.3312 . . . . . . . . . . . 0.3794 
'X-RAY DIFFRACTION' 1.9679 1.9928 . . 547 9189 98.00 . . . . 0.2917 . . . . . . . . . . . 0.2967 
'X-RAY DIFFRACTION' 1.9928 2.0190 . . 509 9080 98.00 . . . . 0.2676 . . . . . . . . . . . 0.2960 
'X-RAY DIFFRACTION' 2.0190 2.0467 . . 430 9311 97.00 . . . . 0.2690 . . . . . . . . . . . 0.2934 
'X-RAY DIFFRACTION' 2.0467 2.0759 . . 478 9170 97.00 . . . . 0.2712 . . . . . . . . . . . 0.3061 
'X-RAY DIFFRACTION' 2.0759 2.1069 . . 509 9157 98.00 . . . . 0.2487 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 2.1069 2.1399 . . 496 9191 97.00 . . . . 0.2480 . . . . . . . . . . . 0.3060 
'X-RAY DIFFRACTION' 2.1399 2.1749 . . 466 9210 97.00 . . . . 0.2261 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 2.1749 2.2124 . . 519 9032 97.00 . . . . 0.2160 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 2.2124 2.2527 . . 479 9250 97.00 . . . . 0.2239 . . . . . . . . . . . 0.2868 
'X-RAY DIFFRACTION' 2.2527 2.2960 . . 525 9088 97.00 . . . . 0.2073 . . . . . . . . . . . 0.2444 
'X-RAY DIFFRACTION' 2.2960 2.3429 . . 477 9254 97.00 . . . . 0.2015 . . . . . . . . . . . 0.2630 
'X-RAY DIFFRACTION' 2.3429 2.3938 . . 489 9026 97.00 . . . . 0.1898 . . . . . . . . . . . 0.2281 
'X-RAY DIFFRACTION' 2.3938 2.4495 . . 486 8931 94.00 . . . . 0.1892 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 2.4495 2.5107 . . 460 8783 94.00 . . . . 0.1824 . . . . . . . . . . . 0.2362 
'X-RAY DIFFRACTION' 2.5107 2.5786 . . 528 9224 97.00 . . . . 0.1712 . . . . . . . . . . . 0.2397 
'X-RAY DIFFRACTION' 2.5786 2.6545 . . 486 8816 95.00 . . . . 0.1828 . . . . . . . . . . . 0.2333 
'X-RAY DIFFRACTION' 2.6545 2.7402 . . 437 9243 98.00 . . . . 0.1811 . . . . . . . . . . . 0.2241 
'X-RAY DIFFRACTION' 2.7402 2.8381 . . 499 9310 98.00 . . . . 0.1670 . . . . . . . . . . . 0.2211 
'X-RAY DIFFRACTION' 2.8381 2.9517 . . 450 9252 98.00 . . . . 0.1632 . . . . . . . . . . . 0.1985 
'X-RAY DIFFRACTION' 2.9517 3.0860 . . 451 9377 98.00 . . . . 0.1694 . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 3.0860 3.2487 . . 457 9269 98.00 . . . . 0.1564 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 3.2487 3.4522 . . 555 9202 98.00 . . . . 0.1521 . . . . . . . . . . . 0.2028 
'X-RAY DIFFRACTION' 3.4522 3.7187 . . 493 9261 98.00 . . . . 0.1350 . . . . . . . . . . . 0.1808 
'X-RAY DIFFRACTION' 3.7187 4.0927 . . 519 9099 97.00 . . . . 0.1287 . . . . . . . . . . . 0.1680 
'X-RAY DIFFRACTION' 4.0927 4.6846 . . 457 8900 94.00 . . . . 0.1208 . . . . . . . . . . . 0.1469 
'X-RAY DIFFRACTION' 4.6846 5.9005 . . 453 9100 97.00 . . . . 0.1352 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 5.9005 49.15  . . 460 9339 99.00 . . . . 0.1560 . . . . . . . . . . . 0.1795 
# 
_struct.entry_id                     9CW1 
_struct.title                        
;Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain bound with 6-(2,3-difluoro-5-(2-(methylamino)ethyl)phenyl)-4-methylpyridin-2-amine dihydrochloride
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CW1 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
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 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 5 ? 
I  N N 6 ? 
J  N N 5 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 6 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 7 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_HUMAN 
_struct_ref.pdbx_db_accession          P29475 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKA
HMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWK
;
_struct_ref.pdbx_align_begin           302 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CW1 A 1 ? 421 ? P29475 302 ? 722 ? 302 722 
2 1 9CW1 B 1 ? 421 ? P29475 302 ? 722 ? 302 722 
3 1 9CW1 C 1 ? 421 ? P29475 302 ? 722 ? 302 722 
4 1 9CW1 D 1 ? 421 ? P29475 302 ? 722 ? 302 722 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CW1 ALA A 53  ? UNP P29475 ARG 354 'engineered mutation' 354 1  
1 9CW1 ASP A 56  ? UNP P29475 GLY 357 'engineered mutation' 357 2  
1 9CW1 LEU A 422 ? UNP P29475 ?   ?   'expression tag'      723 3  
1 9CW1 VAL A 423 ? UNP P29475 ?   ?   'expression tag'      724 4  
2 9CW1 ALA B 53  ? UNP P29475 ARG 354 'engineered mutation' 354 5  
2 9CW1 ASP B 56  ? UNP P29475 GLY 357 'engineered mutation' 357 6  
2 9CW1 LEU B 422 ? UNP P29475 ?   ?   'expression tag'      723 7  
2 9CW1 VAL B 423 ? UNP P29475 ?   ?   'expression tag'      724 8  
3 9CW1 ALA C 53  ? UNP P29475 ARG 354 'engineered mutation' 354 9  
3 9CW1 ASP C 56  ? UNP P29475 GLY 357 'engineered mutation' 357 10 
3 9CW1 LEU C 422 ? UNP P29475 ?   ?   'expression tag'      723 11 
3 9CW1 VAL C 423 ? UNP P29475 ?   ?   'expression tag'      724 12 
4 9CW1 ALA D 53  ? UNP P29475 ARG 354 'engineered mutation' 354 13 
4 9CW1 ASP D 56  ? UNP P29475 GLY 357 'engineered mutation' 357 14 
4 9CW1 LEU D 422 ? UNP P29475 ?   ?   'expression tag'      723 15 
4 9CW1 VAL D 423 ? UNP P29475 ?   ?   'expression tag'      724 16 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9710  ? 
1 MORE         -80   ? 
1 'SSA (A^2)'  33250 ? 
2 'ABSA (A^2)' 9860  ? 
2 MORE         -80   ? 
2 'SSA (A^2)'  33140 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,Y,Z   
2 1 C,D,O,P,Q,R,S,T,U,V,W,X,AA,BA 
# 
_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 320 SER A 325 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 355 ILE A 374 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? SER A 96  ? SER A 379 SER A 397 1 ? 19 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 402 ASN A 416 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 422 TRP A 426 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 439 ASN A 456 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 457 ASN A 459 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 503 GLN A 513 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 542 VAL A 546 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 255 ? GLY A 262 ? PHE A 556 GLY A 563 5 ? 8  
HELX_P HELX_P11 AB2 GLY A 294 ? VAL A 299 ? GLY A 595 VAL A 600 1 ? 6  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 600 ASP A 605 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? MET A 318 ? ILE A 611 MET A 619 1 ? 9  
HELX_P HELX_P14 AB5 LYS A 324 ? SER A 327 ? LYS A 625 SER A 628 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? ASP A 348 ? LEU A 629 ASP A 649 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 354 ? GLY A 374 ? ASP A 655 GLY A 675 1 ? 21 
HELX_P HELX_P17 AB8 ASP A 379 ? VAL A 384 ? ASP A 680 VAL A 685 1 ? 6  
HELX_P HELX_P18 AB9 SER A 388 ? GLN A 397 ? SER A 689 GLN A 698 5 ? 10 
HELX_P HELX_P19 AC1 ASP A 413 ? HIS A 418 ? ASP A 714 HIS A 719 1 ? 6  
HELX_P HELX_P20 AC2 THR B 19  ? SER B 24  ? THR B 320 SER B 325 5 ? 6  
HELX_P HELX_P21 AC3 THR B 54  ? ILE B 73  ? THR B 355 ILE B 374 1 ? 20 
HELX_P HELX_P22 AC4 SER B 78  ? SER B 96  ? SER B 379 SER B 397 1 ? 19 
HELX_P HELX_P23 AC5 LYS B 101 ? ASN B 115 ? LYS B 402 ASN B 416 1 ? 15 
HELX_P HELX_P24 AC6 GLY B 121 ? TRP B 125 ? GLY B 422 TRP B 426 5 ? 5  
HELX_P HELX_P25 AC7 THR B 138 ? ASN B 155 ? THR B 439 ASN B 456 1 ? 18 
HELX_P HELX_P26 AC8 LYS B 156 ? ASN B 158 ? LYS B 457 ASN B 459 5 ? 3  
HELX_P HELX_P27 AC9 ASN B 202 ? GLN B 212 ? ASN B 503 GLN B 513 1 ? 11 
HELX_P HELX_P28 AD1 PRO B 241 ? VAL B 245 ? PRO B 542 VAL B 546 5 ? 5  
HELX_P HELX_P29 AD2 PHE B 255 ? GLY B 262 ? PHE B 556 GLY B 563 5 ? 8  
HELX_P HELX_P30 AD3 GLY B 294 ? VAL B 299 ? GLY B 595 VAL B 600 1 ? 6  
HELX_P HELX_P31 AD4 VAL B 299 ? ASP B 304 ? VAL B 600 ASP B 605 1 ? 6  
HELX_P HELX_P32 AD5 ILE B 310 ? MET B 318 ? ILE B 611 MET B 619 1 ? 9  
HELX_P HELX_P33 AD6 LYS B 324 ? SER B 327 ? LYS B 625 SER B 628 5 ? 4  
HELX_P HELX_P34 AD7 LEU B 328 ? ASP B 348 ? LEU B 629 ASP B 649 1 ? 21 
HELX_P HELX_P35 AD8 ASP B 354 ? GLY B 374 ? ASP B 655 GLY B 675 1 ? 21 
HELX_P HELX_P36 AD9 ASP B 379 ? VAL B 384 ? ASP B 680 VAL B 685 1 ? 6  
HELX_P HELX_P37 AE1 SER B 388 ? GLN B 397 ? SER B 689 GLN B 698 5 ? 10 
HELX_P HELX_P38 AE2 ASP B 413 ? HIS B 418 ? ASP B 714 HIS B 719 1 ? 6  
HELX_P HELX_P39 AE3 THR C 19  ? SER C 24  ? THR C 320 SER C 325 5 ? 6  
HELX_P HELX_P40 AE4 THR C 54  ? ILE C 73  ? THR C 355 ILE C 374 1 ? 20 
HELX_P HELX_P41 AE5 SER C 78  ? SER C 96  ? SER C 379 SER C 397 1 ? 19 
HELX_P HELX_P42 AE6 LYS C 101 ? ASN C 115 ? LYS C 402 ASN C 416 1 ? 15 
HELX_P HELX_P43 AE7 GLY C 121 ? TRP C 125 ? GLY C 422 TRP C 426 5 ? 5  
HELX_P HELX_P44 AE8 THR C 138 ? ASN C 155 ? THR C 439 ASN C 456 1 ? 18 
HELX_P HELX_P45 AE9 LYS C 156 ? ASN C 158 ? LYS C 457 ASN C 459 5 ? 3  
HELX_P HELX_P46 AF1 ASN C 202 ? GLN C 212 ? ASN C 503 GLN C 513 1 ? 11 
HELX_P HELX_P47 AF2 PRO C 241 ? VAL C 245 ? PRO C 542 VAL C 546 5 ? 5  
HELX_P HELX_P48 AF3 PHE C 255 ? GLY C 262 ? PHE C 556 GLY C 563 5 ? 8  
HELX_P HELX_P49 AF4 GLY C 294 ? VAL C 299 ? GLY C 595 VAL C 600 1 ? 6  
HELX_P HELX_P50 AF5 VAL C 299 ? ASP C 304 ? VAL C 600 ASP C 605 1 ? 6  
HELX_P HELX_P51 AF6 ILE C 310 ? MET C 318 ? ILE C 611 MET C 619 1 ? 9  
HELX_P HELX_P52 AF7 LYS C 324 ? SER C 327 ? LYS C 625 SER C 628 5 ? 4  
HELX_P HELX_P53 AF8 LEU C 328 ? ASP C 348 ? LEU C 629 ASP C 649 1 ? 21 
HELX_P HELX_P54 AF9 ASP C 354 ? GLY C 374 ? ASP C 655 GLY C 675 1 ? 21 
HELX_P HELX_P55 AG1 ASP C 379 ? VAL C 384 ? ASP C 680 VAL C 685 1 ? 6  
HELX_P HELX_P56 AG2 SER C 388 ? GLN C 397 ? SER C 689 GLN C 698 5 ? 10 
HELX_P HELX_P57 AG3 ASP C 413 ? HIS C 418 ? ASP C 714 HIS C 719 1 ? 6  
HELX_P HELX_P58 AG4 THR D 19  ? SER D 24  ? THR D 320 SER D 325 5 ? 6  
HELX_P HELX_P59 AG5 THR D 54  ? ILE D 73  ? THR D 355 ILE D 374 1 ? 20 
HELX_P HELX_P60 AG6 SER D 78  ? SER D 96  ? SER D 379 SER D 397 1 ? 19 
HELX_P HELX_P61 AG7 LYS D 101 ? ASN D 115 ? LYS D 402 ASN D 416 1 ? 15 
HELX_P HELX_P62 AG8 GLY D 121 ? TRP D 125 ? GLY D 422 TRP D 426 5 ? 5  
HELX_P HELX_P63 AG9 THR D 138 ? ASN D 155 ? THR D 439 ASN D 456 1 ? 18 
HELX_P HELX_P64 AH1 LYS D 156 ? ASN D 158 ? LYS D 457 ASN D 459 5 ? 3  
HELX_P HELX_P65 AH2 ASN D 202 ? GLN D 212 ? ASN D 503 GLN D 513 1 ? 11 
HELX_P HELX_P66 AH3 PRO D 241 ? VAL D 245 ? PRO D 542 VAL D 546 5 ? 5  
HELX_P HELX_P67 AH4 PHE D 255 ? GLY D 262 ? PHE D 556 GLY D 563 5 ? 8  
HELX_P HELX_P68 AH5 GLY D 294 ? VAL D 299 ? GLY D 595 VAL D 600 1 ? 6  
HELX_P HELX_P69 AH6 VAL D 299 ? ASP D 304 ? VAL D 600 ASP D 605 1 ? 6  
HELX_P HELX_P70 AH7 ILE D 310 ? MET D 318 ? ILE D 611 MET D 619 1 ? 9  
HELX_P HELX_P71 AH8 LYS D 324 ? SER D 327 ? LYS D 625 SER D 628 5 ? 4  
HELX_P HELX_P72 AH9 LEU D 328 ? ASP D 348 ? LEU D 629 ASP D 649 1 ? 21 
HELX_P HELX_P73 AI1 ASP D 354 ? GLY D 374 ? ASP D 655 GLY D 675 1 ? 21 
HELX_P HELX_P74 AI2 ASP D 379 ? VAL D 384 ? ASP D 680 VAL D 685 1 ? 6  
HELX_P HELX_P75 AI3 SER D 388 ? GLN D 397 ? SER D 689 GLN D 698 5 ? 10 
HELX_P HELX_P76 AI4 ASP D 413 ? HIS D 418 ? ASP D 714 HIS D 719 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 I ZN  .  ZN ? ? A CYS 331 A ZN  805 1_555 ? ? ? ? ? ? ? 2.305 ? ? 
metalc2  metalc ? ? A CYS 35  SG ? ? ? 1_555 I ZN  .  ZN ? ? A CYS 336 A ZN  805 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc3  metalc ? ? A CYS 119 SG ? ? ? 1_555 E HEM .  FE ? ? A CYS 420 A HEM 801 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc4  metalc ? ? I ZN  .   ZN ? ? ? 1_555 B CYS 30 SG ? ? A ZN  805 B CYS 331 1_555 ? ? ? ? ? ? ? 2.310 ? ? 
metalc5  metalc ? ? I ZN  .   ZN ? ? ? 1_555 B CYS 35 SG ? ? A ZN  805 B CYS 336 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc6  metalc ? ? B CYS 119 SG ? ? ? 1_555 K HEM .  FE ? ? B CYS 420 B HEM 801 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc7  metalc ? ? C CYS 30  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 331 C ZN  806 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc8  metalc ? ? C CYS 35  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 336 C ZN  806 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc9  metalc ? ? C CYS 119 SG ? ? ? 1_555 O HEM .  FE ? ? C CYS 420 C HEM 801 1_555 ? ? ? ? ? ? ? 2.353 ? ? 
metalc10 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 30 SG ? ? C ZN  806 D CYS 331 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc11 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 35 SG ? ? C ZN  806 D CYS 336 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc12 metalc ? ? D CYS 119 SG ? ? ? 1_555 U HEM .  FE ? ? D CYS 420 D HEM 801 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
# 
_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 331 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 336 ? 1_555 113.1 ? 
2  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 119.9 ? 
3  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 104.8 ? 
4  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 103.5 ? 
5  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 100.4 ? 
6  SG ? B CYS 30  ? B CYS 331 ? 1_555 ZN ? I ZN  . ? A ZN  805 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 113.6 ? 
7  SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NA ? E HEM .  ? A HEM 801 ? 1_555 101.2 ? 
8  SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NB ? E HEM .  ? A HEM 801 ? 1_555 97.6  ? 
9  NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NB ? E HEM .  ? A HEM 801 ? 1_555 85.7  ? 
10 SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 96.0  ? 
11 NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 162.7 ? 
12 NB ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 90.0  ? 
13 SG ? A CYS 119 ? A CYS 420 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 102.7 ? 
14 NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 90.5  ? 
15 NB ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 159.6 ? 
16 NC ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 87.8  ? 
17 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NA ? K HEM .  ? B HEM 801 ? 1_555 102.5 ? 
18 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NB ? K HEM .  ? B HEM 801 ? 1_555 100.1 ? 
19 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NB ? K HEM .  ? B HEM 801 ? 1_555 84.8  ? 
20 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 97.4  ? 
21 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 160.1 ? 
22 NB ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 NC ? K HEM .  ? B HEM 801 ? 1_555 90.9  ? 
23 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 104.0 ? 
24 NA ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 90.5  ? 
25 NB ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 155.8 ? 
26 NC ? K HEM .   ? B HEM 801 ? 1_555 FE ? K HEM . ? B HEM 801 ? 1_555 ND ? K HEM .  ? B HEM 801 ? 1_555 85.5  ? 
27 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? C CYS 35 ? C CYS 336 ? 1_555 113.9 ? 
28 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 30 ? D CYS 331 ? 1_555 118.1 ? 
29 SG ? C CYS 35  ? C CYS 336 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 30 ? D CYS 331 ? 1_555 105.0 ? 
30 SG ? C CYS 30  ? C CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 103.6 ? 
31 SG ? C CYS 35  ? C CYS 336 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 102.6 ? 
32 SG ? D CYS 30  ? D CYS 331 ? 1_555 ZN ? T ZN  . ? C ZN  806 ? 1_555 SG ? D CYS 35 ? D CYS 336 ? 1_555 112.7 ? 
33 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NA ? O HEM .  ? C HEM 801 ? 1_555 101.5 ? 
34 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NB ? O HEM .  ? C HEM 801 ? 1_555 98.7  ? 
35 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NB ? O HEM .  ? C HEM 801 ? 1_555 86.3  ? 
36 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 95.6  ? 
37 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 162.9 ? 
38 NB ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 91.1  ? 
39 SG ? C CYS 119 ? C CYS 420 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 102.7 ? 
40 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 89.7  ? 
41 NB ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 158.5 ? 
42 NC ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 86.6  ? 
43 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NA ? U HEM .  ? D HEM 801 ? 1_555 100.8 ? 
44 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NB ? U HEM .  ? D HEM 801 ? 1_555 97.7  ? 
45 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NB ? U HEM .  ? D HEM 801 ? 1_555 87.3  ? 
46 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 96.6  ? 
47 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 162.6 ? 
48 NB ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 89.8  ? 
49 SG ? D CYS 119 ? D CYS 420 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 101.7 ? 
50 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 89.0  ? 
51 NB ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 160.6 ? 
52 NC ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 88.2  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 405 A . ? THR 706 A PRO 406 A ? PRO 707 A 1 -2.80 
2 THR 405 B . ? THR 706 B PRO 406 B ? PRO 707 B 1 1.13  
3 THR 405 C . ? THR 706 C PRO 406 C ? PRO 707 C 1 -0.95 
4 THR 405 C . ? THR 706 C PRO 406 C ? PRO 707 C 1 -3.05 
5 THR 405 D . ? THR 706 D PRO 406 D ? PRO 707 D 1 -1.43 
# 
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 ? 
AA8 ? 2 ? 
AA9 ? 4 ? 
AB1 ? 3 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 2 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 3 ? 
AB9 ? 2 ? 
AC1 ? 2 ? 
AC2 ? 3 ? 
AC3 ? 2 ? 
AC4 ? 2 ? 
AC5 ? 4 ? 
AC6 ? 3 ? 
AC7 ? 2 ? 
AC8 ? 2 ? 
AC9 ? 3 ? 
AD1 ? 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      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? parallel      
AB6 1 2 ? anti-parallel 
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC3 1 2 ? parallel      
AC4 1 2 ? anti-parallel 
AC5 1 2 ? parallel      
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC9 1 2 ? anti-parallel 
AC9 2 3 ? anti-parallel 
AD1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 5   ? LYS A 8   ? LEU A 306 LYS A 309 
AA1 2 VAL A 15  ? ASP A 18  ? VAL A 316 ASP A 319 
AA2 1 GLN A 129 ? ASP A 132 ? GLN A 430 ASP A 433 
AA2 2 ALA A 162 ? ILE A 165 ? ALA A 463 ILE A 466 
AA2 3 PHE A 288 ? SER A 289 ? PHE A 589 SER A 590 
AA2 4 ALA A 270 ? VAL A 271 ? ALA A 571 VAL A 572 
AA3 1 ARG A 177 ? VAL A 178 ? ARG A 478 VAL A 479 
AA3 2 LEU A 226 ? GLN A 229 ? LEU A 527 GLN A 530 
AA3 3 GLU A 236 ? PHE A 238 ? GLU A 537 PHE A 539 
AA4 1 GLY A 188 ? LYS A 190 ? GLY A 489 LYS A 491 
AA4 2 THR A 196 ? GLY A 198 ? THR A 497 GLY A 499 
AA5 1 GLU A 247 ? PRO A 249 ? GLU A 548 PRO A 550 
AA5 2 LYS A 264 ? TYR A 266 ? LYS A 565 TYR A 567 
AA6 1 LEU A 281 ? PHE A 283 ? LEU A 582 PHE A 584 
AA6 2 LEU A 275 ? ILE A 278 ? LEU A 576 ILE A 579 
AA6 3 SER A 407 ? GLU A 409 ? SER A 708 GLU A 710 
AA7 1 TYR A 292 ? MET A 293 ? TYR A 593 MET A 594 
AA7 2 ILE A 352 ? VAL A 353 ? ILE A 653 VAL A 654 
AA8 1 LEU B 5   ? LYS B 8   ? LEU B 306 LYS B 309 
AA8 2 VAL B 15  ? ASP B 18  ? VAL B 316 ASP B 319 
AA9 1 GLN B 129 ? ASP B 132 ? GLN B 430 ASP B 433 
AA9 2 ALA B 162 ? ILE B 165 ? ALA B 463 ILE B 466 
AA9 3 PHE B 288 ? SER B 289 ? PHE B 589 SER B 590 
AA9 4 ALA B 270 ? VAL B 271 ? ALA B 571 VAL B 572 
AB1 1 ARG B 177 ? VAL B 178 ? ARG B 478 VAL B 479 
AB1 2 LEU B 226 ? GLN B 229 ? LEU B 527 GLN B 530 
AB1 3 GLU B 236 ? PHE B 238 ? GLU B 537 PHE B 539 
AB2 1 GLY B 188 ? LYS B 190 ? GLY B 489 LYS B 491 
AB2 2 THR B 196 ? GLY B 198 ? THR B 497 GLY B 499 
AB3 1 GLU B 247 ? PRO B 249 ? GLU B 548 PRO B 550 
AB3 2 LYS B 264 ? TYR B 266 ? LYS B 565 TYR B 567 
AB4 1 LEU B 281 ? PHE B 283 ? LEU B 582 PHE B 584 
AB4 2 LEU B 275 ? ILE B 278 ? LEU B 576 ILE B 579 
AB4 3 SER B 407 ? GLU B 409 ? SER B 708 GLU B 710 
AB5 1 TYR B 292 ? MET B 293 ? TYR B 593 MET B 594 
AB5 2 ILE B 352 ? VAL B 353 ? ILE B 653 VAL B 654 
AB6 1 LEU C 5   ? LYS C 8   ? LEU C 306 LYS C 309 
AB6 2 VAL C 15  ? ASP C 18  ? VAL C 316 ASP C 319 
AB7 1 GLN C 129 ? ASP C 132 ? GLN C 430 ASP C 433 
AB7 2 ALA C 162 ? ILE C 165 ? ALA C 463 ILE C 466 
AB7 3 PHE C 288 ? SER C 289 ? PHE C 589 SER C 590 
AB7 4 ALA C 270 ? VAL C 271 ? ALA C 571 VAL C 572 
AB8 1 ARG C 177 ? VAL C 178 ? ARG C 478 VAL C 479 
AB8 2 LEU C 226 ? GLN C 229 ? LEU C 527 GLN C 530 
AB8 3 GLU C 236 ? PHE C 238 ? GLU C 537 PHE C 539 
AB9 1 GLY C 188 ? LYS C 190 ? GLY C 489 LYS C 491 
AB9 2 THR C 196 ? GLY C 198 ? THR C 497 GLY C 499 
AC1 1 GLU C 247 ? PRO C 249 ? GLU C 548 PRO C 550 
AC1 2 LYS C 264 ? TYR C 266 ? LYS C 565 TYR C 567 
AC2 1 LEU C 281 ? PHE C 283 ? LEU C 582 PHE C 584 
AC2 2 LEU C 275 ? ILE C 278 ? LEU C 576 ILE C 579 
AC2 3 SER C 407 ? GLU C 409 ? SER C 708 GLU C 710 
AC3 1 TYR C 292 ? MET C 293 ? TYR C 593 MET C 594 
AC3 2 ILE C 352 ? VAL C 353 ? ILE C 653 VAL C 654 
AC4 1 LEU D 5   ? LYS D 8   ? LEU D 306 LYS D 309 
AC4 2 VAL D 15  ? ASP D 18  ? VAL D 316 ASP D 319 
AC5 1 GLN D 129 ? ASP D 132 ? GLN D 430 ASP D 433 
AC5 2 ALA D 162 ? ILE D 165 ? ALA D 463 ILE D 466 
AC5 3 PHE D 288 ? SER D 289 ? PHE D 589 SER D 590 
AC5 4 ALA D 270 ? VAL D 271 ? ALA D 571 VAL D 572 
AC6 1 ARG D 177 ? VAL D 178 ? ARG D 478 VAL D 479 
AC6 2 LEU D 226 ? GLN D 229 ? LEU D 527 GLN D 530 
AC6 3 GLU D 236 ? PHE D 238 ? GLU D 537 PHE D 539 
AC7 1 GLY D 188 ? LYS D 190 ? GLY D 489 LYS D 491 
AC7 2 THR D 196 ? GLY D 198 ? THR D 497 GLY D 499 
AC8 1 GLU D 247 ? PRO D 249 ? GLU D 548 PRO D 550 
AC8 2 LYS D 264 ? TYR D 266 ? LYS D 565 TYR D 567 
AC9 1 LEU D 281 ? PHE D 283 ? LEU D 582 PHE D 584 
AC9 2 LEU D 275 ? ILE D 278 ? LEU D 576 ILE D 579 
AC9 3 SER D 407 ? GLU D 409 ? SER D 708 GLU D 710 
AD1 1 TYR D 292 ? MET D 293 ? TYR D 593 MET D 594 
AD1 2 ILE D 352 ? VAL D 353 ? ILE D 653 VAL D 654 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 5   ? N LEU A 306 O ASP A 18  ? O ASP A 319 
AA2 1 2 N PHE A 131 ? N PHE A 432 O ILE A 163 ? O ILE A 464 
AA2 2 3 N ALA A 162 ? N ALA A 463 O SER A 289 ? O SER A 590 
AA2 3 4 O PHE A 288 ? O PHE A 589 N VAL A 271 ? N VAL A 572 
AA3 1 2 N ARG A 177 ? N ARG A 478 O GLN A 229 ? O GLN A 530 
AA3 2 3 N LEU A 226 ? N LEU A 527 O PHE A 238 ? O PHE A 539 
AA4 1 2 N TYR A 189 ? N TYR A 490 O LEU A 197 ? O LEU A 498 
AA5 1 2 N VAL A 248 ? N VAL A 549 O TRP A 265 ? O TRP A 566 
AA6 1 2 O PHE A 283 ? O PHE A 584 N LEU A 276 ? N LEU A 577 
AA6 2 3 N LEU A 275 ? N LEU A 576 O GLU A 409 ? O GLU A 710 
AA7 1 2 N TYR A 292 ? N TYR A 593 O VAL A 353 ? O VAL A 654 
AA8 1 2 N LEU B 5   ? N LEU B 306 O ASP B 18  ? O ASP B 319 
AA9 1 2 N PHE B 131 ? N PHE B 432 O ILE B 163 ? O ILE B 464 
AA9 2 3 N ALA B 162 ? N ALA B 463 O SER B 289 ? O SER B 590 
AA9 3 4 O PHE B 288 ? O PHE B 589 N VAL B 271 ? N VAL B 572 
AB1 1 2 N ARG B 177 ? N ARG B 478 O GLN B 229 ? O GLN B 530 
AB1 2 3 N LEU B 226 ? N LEU B 527 O PHE B 238 ? O PHE B 539 
AB2 1 2 N TYR B 189 ? N TYR B 490 O LEU B 197 ? O LEU B 498 
AB3 1 2 N VAL B 248 ? N VAL B 549 O TRP B 265 ? O TRP B 566 
AB4 1 2 O PHE B 283 ? O PHE B 584 N LEU B 276 ? N LEU B 577 
AB4 2 3 N LEU B 275 ? N LEU B 576 O GLU B 409 ? O GLU B 710 
AB5 1 2 N TYR B 292 ? N TYR B 593 O VAL B 353 ? O VAL B 654 
AB6 1 2 N LEU C 5   ? N LEU C 306 O ASP C 18  ? O ASP C 319 
AB7 1 2 N PHE C 131 ? N PHE C 432 O ILE C 163 ? O ILE C 464 
AB7 2 3 N ALA C 162 ? N ALA C 463 O SER C 289 ? O SER C 590 
AB7 3 4 O PHE C 288 ? O PHE C 589 N VAL C 271 ? N VAL C 572 
AB8 1 2 N ARG C 177 ? N ARG C 478 O GLN C 229 ? O GLN C 530 
AB8 2 3 N LEU C 226 ? N LEU C 527 O PHE C 238 ? O PHE C 539 
AB9 1 2 N TYR C 189 ? N TYR C 490 O LEU C 197 ? O LEU C 498 
AC1 1 2 N VAL C 248 ? N VAL C 549 O TRP C 265 ? O TRP C 566 
AC2 1 2 O PHE C 283 ? O PHE C 584 N LEU C 276 ? N LEU C 577 
AC2 2 3 N LEU C 275 ? N LEU C 576 O GLU C 409 ? O GLU C 710 
AC3 1 2 N TYR C 292 ? N TYR C 593 O VAL C 353 ? O VAL C 654 
AC4 1 2 N LEU D 5   ? N LEU D 306 O ASP D 18  ? O ASP D 319 
AC5 1 2 N PHE D 131 ? N PHE D 432 O ILE D 163 ? O ILE D 464 
AC5 2 3 N ALA D 162 ? N ALA D 463 O SER D 289 ? O SER D 590 
AC5 3 4 O PHE D 288 ? O PHE D 589 N VAL D 271 ? N VAL D 572 
AC6 1 2 N ARG D 177 ? N ARG D 478 O GLN D 229 ? O GLN D 530 
AC6 2 3 N LEU D 226 ? N LEU D 527 O PHE D 238 ? O PHE D 539 
AC7 1 2 N TYR D 189 ? N TYR D 490 O LEU D 197 ? O LEU D 498 
AC8 1 2 N VAL D 248 ? N VAL D 549 O TRP D 265 ? O TRP D 566 
AC9 1 2 O PHE D 283 ? O PHE D 584 N LEU D 276 ? N LEU D 577 
AC9 2 3 N LEU D 275 ? N LEU D 576 O GLU D 409 ? O GLU D 710 
AD1 1 2 N TYR D 292 ? N TYR D 593 O VAL D 353 ? O VAL D 654 
# 
_pdbx_entry_details.entry_id                   9CW1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 C GLU 578  ? ? O   C HOH 901  ? ? 2.05 
2 1 OG  B SER 662  ? B O   B HOH 901  ? ? 2.07 
3 1 NH1 A ARG 348  ? ? OE2 A GLU 365  ? ? 2.15 
4 1 OG  D SER 325  ? ? O   D HOH 901  ? ? 2.15 
5 1 NE2 A GLN 483  ? ? O   A HOH 901  ? ? 2.17 
6 1 O   B HOH 1180 ? ? O   B HOH 1198 ? ? 2.18 
7 1 OE2 B GLU 578  ? ? O   B HOH 902  ? ? 2.18 
8 1 NE2 D GLN 540  ? ? O   D HOH 902  ? ? 2.19 
9 1 O   C HOH 1134 ? ? O   C HOH 1179 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     929 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    D 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     919 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.13 
# 
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 ASP A 352 ? ? -120.64 -160.02 
2  1 VAL A 353 ? ? -49.44  105.54  
3  1 THR A 471 ? ? -110.47 -80.78  
4  1 CYS A 587 ? ? -150.98 57.44   
5  1 ARG A 608 ? ? -116.22 -133.33 
6  1 THR B 326 ? ? -126.91 -57.93  
7  1 LYS B 428 ? ? -104.63 75.08   
8  1 THR B 471 ? ? -113.07 -88.07  
9  1 CYS B 587 ? ? -151.08 53.74   
10 1 ARG B 608 ? ? -111.22 -135.45 
11 1 CYS B 677 ? ? -160.18 102.52  
12 1 THR C 326 ? ? -134.67 -58.74  
13 1 LYS C 428 ? ? -104.73 73.78   
14 1 THR C 471 ? ? -113.69 -87.72  
15 1 CYS C 587 ? ? -151.36 55.15   
16 1 ARG C 608 ? ? -110.88 -136.17 
17 1 GLU D 351 ? ? -40.21  -73.07  
18 1 ASP D 352 ? ? -102.64 -158.47 
19 1 SER D 397 ? ? 67.74   -0.81   
20 1 THR D 471 ? ? -110.94 -80.35  
21 1 CYS D 587 ? ? -147.29 59.58   
22 1 ARG D 608 ? ? -116.92 -133.13 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -10.7921 -4.3938  -39.8062 0.1675 ? -0.0025 ? -0.0237 ? 0.1987 ? 0.0014  ? 0.1857 ? 0.4563 ? 
-0.1293 ? -0.0713 ? 0.7470 ? 0.0269  ? 2.3169 ? 0.0242 ? 0.0584  ? 0.0062  ? 0.0149  ? -0.0496 ? -0.0677 ? -0.0538 ? 0.1113  ? 
0.0240 ? 
2 'X-RAY DIFFRACTION' ? refined -12.8273 -4.1290  -2.6812  0.2181 ? -0.0152 ? -0.0340 ? 0.2049 ? -0.0257 ? 0.2120 ? 0.4925 ? 
-0.1100 ? -0.1236 ? 0.6099 ? 0.0301  ? 1.3825 ? 0.0156 ? -0.0284 ? -0.0321 ? -0.0246 ? -0.0194 ? 0.0227  ? -0.0307 ? -0.0060 ? 
0.0040 ? 
3 'X-RAY DIFFRACTION' ? refined 13.0070  -53.2000 -78.8151 0.2085 ? 0.0068  ? 0.0388  ? 0.2031 ? -0.0255 ? 0.2165 ? 0.4551 ? 
0.1513  ? 0.1284  ? 0.6819 ? -0.0260 ? 1.4808 ? 0.0133 ? 0.0223  ? 0.0297  ? 0.0268  ? -0.0176 ? 0.0269  ? 0.0336  ? -0.0159 ? 
0.0048 ? 
4 'X-RAY DIFFRACTION' ? refined 14.9934  -52.8861 -41.7197 0.1671 ? 0.0042  ? 0.0265  ? 0.2091 ? 0.0031  ? 0.1900 ? 0.4065 ? 
0.1213  ? 0.0452  ? 0.7882 ? -0.0223 ? 2.3068 ? 0.0214 ? -0.0639 ? -0.0012 ? -0.0060 ? -0.0426 ? -0.0445 ? 0.0457  ? 0.1211  ? 
0.0239 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '(chain A and resid 302:722)' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '(chain B and resid 304:722)' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? '(chain C and resid 302:722)' 
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? '(chain D and resid 304:724)' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 1219 ? 6.03 . 
2 1 O ? B HOH 1220 ? 6.16 . 
3 1 O ? C HOH 1227 ? 5.98 . 
4 1 O ? D HOH 1194 ? 7.14 . 
# 
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 302 ? A CYS 1   
2  1 Y 1 A PRO 303 ? A PRO 2   
3  1 Y 1 A ARG 304 ? A ARG 3   
4  1 Y 1 A LEU 723 ? A LEU 422 
5  1 Y 1 A VAL 724 ? A VAL 423 
6  1 Y 1 B CYS 302 ? B CYS 1   
7  1 Y 1 B PRO 303 ? B PRO 2   
8  1 Y 1 B GLN 345 ? B GLN 44  
9  1 Y 1 B HIS 346 ? B HIS 45  
10 1 Y 1 B ALA 347 ? B ALA 46  
11 1 Y 1 B ARG 348 ? B ARG 47  
12 1 Y 1 B ARG 349 ? B ARG 48  
13 1 Y 1 B PRO 350 ? B PRO 49  
14 1 Y 1 B GLU 351 ? B GLU 50  
15 1 Y 1 C CYS 302 ? C CYS 1   
16 1 Y 1 C PRO 303 ? C PRO 2   
17 1 Y 1 C SER 344 ? C SER 43  
18 1 Y 1 C GLN 345 ? C GLN 44  
19 1 Y 1 C HIS 346 ? C HIS 45  
20 1 Y 1 C ALA 347 ? C ALA 46  
21 1 Y 1 C ARG 348 ? C ARG 47  
22 1 Y 1 C ARG 349 ? C ARG 48  
23 1 Y 1 C PRO 350 ? C PRO 49  
24 1 Y 1 C GLU 351 ? C GLU 50  
25 1 Y 1 D CYS 302 ? D CYS 1   
26 1 Y 1 D PRO 303 ? D PRO 2   
27 1 Y 1 D ARG 304 ? D ARG 3   
28 1 Y 1 D LEU 723 ? D LEU 422 
29 1 Y 1 D VAL 724 ? D VAL 423 
# 
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 
A1A0C C11  C  Y N 1   
A1A0C C12  C  Y N 2   
A1A0C C17  C  N N 3   
A1A0C C16  C  Y N 4   
A1A0C C15  C  Y N 5   
A1A0C C14  C  Y N 6   
A1A0C C13  C  Y N 7   
A1A0C C18  C  N N 8   
A1A0C C20  C  N N 9   
A1A0C C02  C  Y N 10  
A1A0C C03  C  Y N 11  
A1A0C C04  C  Y N 12  
A1A0C C05  C  Y N 13  
A1A0C C06  C  Y N 14  
A1A0C C07  C  N N 15  
A1A0C F12  F  N N 16  
A1A0C F13  F  N N 17  
A1A0C N01  N  Y N 18  
A1A0C N02  N  N N 19  
A1A0C N19  N  N N 20  
A1A0C H1   H  N N 21  
A1A0C H2   H  N N 22  
A1A0C H3   H  N N 23  
A1A0C H4   H  N N 24  
A1A0C H5   H  N N 25  
A1A0C H6   H  N N 26  
A1A0C H7   H  N N 27  
A1A0C H8   H  N N 28  
A1A0C H9   H  N N 29  
A1A0C H10  H  N N 30  
A1A0C H11  H  N N 31  
A1A0C H12  H  N N 32  
A1A0C H13  H  N N 33  
A1A0C H14  H  N N 34  
A1A0C H15  H  N N 35  
A1A0C H16  H  N N 36  
A1A0C H17  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
GOL   C1   C  N N 174 
GOL   O1   O  N N 175 
GOL   C2   C  N N 176 
GOL   O2   O  N N 177 
GOL   C3   C  N N 178 
GOL   O3   O  N N 179 
GOL   H11  H  N N 180 
GOL   H12  H  N N 181 
GOL   HO1  H  N N 182 
GOL   H2   H  N N 183 
GOL   HO2  H  N N 184 
GOL   H31  H  N N 185 
GOL   H32  H  N N 186 
GOL   HO3  H  N N 187 
H4B   N1   N  Y N 188 
H4B   C2   C  Y N 189 
H4B   N2   N  N N 190 
H4B   N3   N  Y N 191 
H4B   C4   C  Y N 192 
H4B   O4   O  N N 193 
H4B   C4A  C  Y N 194 
H4B   C8A  C  Y N 195 
H4B   N5   N  N N 196 
H4B   N8   N  N N 197 
H4B   C6   C  N R 198 
H4B   C7   C  N N 199 
H4B   C9   C  N R 200 
H4B   O9   O  N N 201 
H4B   C10  C  N S 202 
H4B   C11  C  N N 203 
H4B   O10  O  N N 204 
H4B   HN21 H  N N 205 
H4B   HN22 H  N N 206 
H4B   HN3  H  N N 207 
H4B   HN5  H  N N 208 
H4B   HN8  H  N N 209 
H4B   H6   H  N N 210 
H4B   H71  H  N N 211 
H4B   H72  H  N N 212 
H4B   H9   H  N N 213 
H4B   HO9  H  N N 214 
H4B   H10  H  N N 215 
H4B   H111 H  N N 216 
H4B   H112 H  N N 217 
H4B   H113 H  N N 218 
H4B   HO0  H  N N 219 
HEM   CHA  C  N N 220 
HEM   CHB  C  N N 221 
HEM   CHC  C  N N 222 
HEM   CHD  C  N N 223 
HEM   C1A  C  Y N 224 
HEM   C2A  C  Y N 225 
HEM   C3A  C  Y N 226 
HEM   C4A  C  Y N 227 
HEM   CMA  C  N N 228 
HEM   CAA  C  N N 229 
HEM   CBA  C  N N 230 
HEM   CGA  C  N N 231 
HEM   O1A  O  N N 232 
HEM   O2A  O  N N 233 
HEM   C1B  C  N N 234 
HEM   C2B  C  N N 235 
HEM   C3B  C  N N 236 
HEM   C4B  C  N N 237 
HEM   CMB  C  N N 238 
HEM   CAB  C  N N 239 
HEM   CBB  C  N N 240 
HEM   C1C  C  Y N 241 
HEM   C2C  C  Y N 242 
HEM   C3C  C  Y N 243 
HEM   C4C  C  Y N 244 
HEM   CMC  C  N N 245 
HEM   CAC  C  N N 246 
HEM   CBC  C  N N 247 
HEM   C1D  C  N N 248 
HEM   C2D  C  N N 249 
HEM   C3D  C  N N 250 
HEM   C4D  C  N N 251 
HEM   CMD  C  N N 252 
HEM   CAD  C  N N 253 
HEM   CBD  C  N N 254 
HEM   CGD  C  N N 255 
HEM   O1D  O  N N 256 
HEM   O2D  O  N N 257 
HEM   NA   N  Y N 258 
HEM   NB   N  N N 259 
HEM   NC   N  Y N 260 
HEM   ND   N  N N 261 
HEM   FE   FE N N 262 
HEM   HHB  H  N N 263 
HEM   HHC  H  N N 264 
HEM   HHD  H  N N 265 
HEM   HMA  H  N N 266 
HEM   HMAA H  N N 267 
HEM   HMAB H  N N 268 
HEM   HAA  H  N N 269 
HEM   HAAA H  N N 270 
HEM   HBA  H  N N 271 
HEM   HBAA H  N N 272 
HEM   HMB  H  N N 273 
HEM   HMBA H  N N 274 
HEM   HMBB H  N N 275 
HEM   HAB  H  N N 276 
HEM   HBB  H  N N 277 
HEM   HBBA H  N N 278 
HEM   HMC  H  N N 279 
HEM   HMCA H  N N 280 
HEM   HMCB H  N N 281 
HEM   HAC  H  N N 282 
HEM   HBC  H  N N 283 
HEM   HBCA H  N N 284 
HEM   HMD  H  N N 285 
HEM   HMDA H  N N 286 
HEM   HMDB H  N N 287 
HEM   HAD  H  N N 288 
HEM   HADA H  N N 289 
HEM   HBD  H  N N 290 
HEM   HBDA H  N N 291 
HEM   H2A  H  N N 292 
HEM   H2D  H  N N 293 
HEM   HHA  H  N N 294 
HIS   N    N  N N 295 
HIS   CA   C  N S 296 
HIS   C    C  N N 297 
HIS   O    O  N N 298 
HIS   CB   C  N N 299 
HIS   CG   C  Y N 300 
HIS   ND1  N  Y N 301 
HIS   CD2  C  Y N 302 
HIS   CE1  C  Y N 303 
HIS   NE2  N  Y N 304 
HIS   OXT  O  N N 305 
HIS   H    H  N N 306 
HIS   H2   H  N N 307 
HIS   HA   H  N N 308 
HIS   HB2  H  N N 309 
HIS   HB3  H  N N 310 
HIS   HD1  H  N N 311 
HIS   HD2  H  N N 312 
HIS   HE1  H  N N 313 
HIS   HE2  H  N N 314 
HIS   HXT  H  N N 315 
HOH   O    O  N N 316 
HOH   H1   H  N N 317 
HOH   H2   H  N N 318 
ILE   N    N  N N 319 
ILE   CA   C  N S 320 
ILE   C    C  N N 321 
ILE   O    O  N N 322 
ILE   CB   C  N S 323 
ILE   CG1  C  N N 324 
ILE   CG2  C  N N 325 
ILE   CD1  C  N N 326 
ILE   OXT  O  N N 327 
ILE   H    H  N N 328 
ILE   H2   H  N N 329 
ILE   HA   H  N N 330 
ILE   HB   H  N N 331 
ILE   HG12 H  N N 332 
ILE   HG13 H  N N 333 
ILE   HG21 H  N N 334 
ILE   HG22 H  N N 335 
ILE   HG23 H  N N 336 
ILE   HD11 H  N N 337 
ILE   HD12 H  N N 338 
ILE   HD13 H  N N 339 
ILE   HXT  H  N N 340 
LEU   N    N  N N 341 
LEU   CA   C  N S 342 
LEU   C    C  N N 343 
LEU   O    O  N N 344 
LEU   CB   C  N N 345 
LEU   CG   C  N N 346 
LEU   CD1  C  N N 347 
LEU   CD2  C  N N 348 
LEU   OXT  O  N N 349 
LEU   H    H  N N 350 
LEU   H2   H  N N 351 
LEU   HA   H  N N 352 
LEU   HB2  H  N N 353 
LEU   HB3  H  N N 354 
LEU   HG   H  N N 355 
LEU   HD11 H  N N 356 
LEU   HD12 H  N N 357 
LEU   HD13 H  N N 358 
LEU   HD21 H  N N 359 
LEU   HD22 H  N N 360 
LEU   HD23 H  N N 361 
LEU   HXT  H  N N 362 
LYS   N    N  N N 363 
LYS   CA   C  N S 364 
LYS   C    C  N N 365 
LYS   O    O  N N 366 
LYS   CB   C  N N 367 
LYS   CG   C  N N 368 
LYS   CD   C  N N 369 
LYS   CE   C  N N 370 
LYS   NZ   N  N N 371 
LYS   OXT  O  N N 372 
LYS   H    H  N N 373 
LYS   H2   H  N N 374 
LYS   HA   H  N N 375 
LYS   HB2  H  N N 376 
LYS   HB3  H  N N 377 
LYS   HG2  H  N N 378 
LYS   HG3  H  N N 379 
LYS   HD2  H  N N 380 
LYS   HD3  H  N N 381 
LYS   HE2  H  N N 382 
LYS   HE3  H  N N 383 
LYS   HZ1  H  N N 384 
LYS   HZ2  H  N N 385 
LYS   HZ3  H  N N 386 
LYS   HXT  H  N N 387 
MET   N    N  N N 388 
MET   CA   C  N S 389 
MET   C    C  N N 390 
MET   O    O  N N 391 
MET   CB   C  N N 392 
MET   CG   C  N N 393 
MET   SD   S  N N 394 
MET   CE   C  N N 395 
MET   OXT  O  N N 396 
MET   H    H  N N 397 
MET   H2   H  N N 398 
MET   HA   H  N N 399 
MET   HB2  H  N N 400 
MET   HB3  H  N N 401 
MET   HG2  H  N N 402 
MET   HG3  H  N N 403 
MET   HE1  H  N N 404 
MET   HE2  H  N N 405 
MET   HE3  H  N N 406 
MET   HXT  H  N N 407 
PHE   N    N  N N 408 
PHE   CA   C  N S 409 
PHE   C    C  N N 410 
PHE   O    O  N N 411 
PHE   CB   C  N N 412 
PHE   CG   C  Y N 413 
PHE   CD1  C  Y N 414 
PHE   CD2  C  Y N 415 
PHE   CE1  C  Y N 416 
PHE   CE2  C  Y N 417 
PHE   CZ   C  Y N 418 
PHE   OXT  O  N N 419 
PHE   H    H  N N 420 
PHE   H2   H  N N 421 
PHE   HA   H  N N 422 
PHE   HB2  H  N N 423 
PHE   HB3  H  N N 424 
PHE   HD1  H  N N 425 
PHE   HD2  H  N N 426 
PHE   HE1  H  N N 427 
PHE   HE2  H  N N 428 
PHE   HZ   H  N N 429 
PHE   HXT  H  N N 430 
PRO   N    N  N N 431 
PRO   CA   C  N S 432 
PRO   C    C  N N 433 
PRO   O    O  N N 434 
PRO   CB   C  N N 435 
PRO   CG   C  N N 436 
PRO   CD   C  N N 437 
PRO   OXT  O  N N 438 
PRO   H    H  N N 439 
PRO   HA   H  N N 440 
PRO   HB2  H  N N 441 
PRO   HB3  H  N N 442 
PRO   HG2  H  N N 443 
PRO   HG3  H  N N 444 
PRO   HD2  H  N N 445 
PRO   HD3  H  N N 446 
PRO   HXT  H  N N 447 
SER   N    N  N N 448 
SER   CA   C  N S 449 
SER   C    C  N N 450 
SER   O    O  N N 451 
SER   CB   C  N N 452 
SER   OG   O  N N 453 
SER   OXT  O  N N 454 
SER   H    H  N N 455 
SER   H2   H  N N 456 
SER   HA   H  N N 457 
SER   HB2  H  N N 458 
SER   HB3  H  N N 459 
SER   HG   H  N N 460 
SER   HXT  H  N N 461 
THR   N    N  N N 462 
THR   CA   C  N S 463 
THR   C    C  N N 464 
THR   O    O  N N 465 
THR   CB   C  N R 466 
THR   OG1  O  N N 467 
THR   CG2  C  N N 468 
THR   OXT  O  N N 469 
THR   H    H  N N 470 
THR   H2   H  N N 471 
THR   HA   H  N N 472 
THR   HB   H  N N 473 
THR   HG1  H  N N 474 
THR   HG21 H  N N 475 
THR   HG22 H  N N 476 
THR   HG23 H  N N 477 
THR   HXT  H  N N 478 
TRP   N    N  N N 479 
TRP   CA   C  N S 480 
TRP   C    C  N N 481 
TRP   O    O  N N 482 
TRP   CB   C  N N 483 
TRP   CG   C  Y N 484 
TRP   CD1  C  Y N 485 
TRP   CD2  C  Y N 486 
TRP   NE1  N  Y N 487 
TRP   CE2  C  Y N 488 
TRP   CE3  C  Y N 489 
TRP   CZ2  C  Y N 490 
TRP   CZ3  C  Y N 491 
TRP   CH2  C  Y N 492 
TRP   OXT  O  N N 493 
TRP   H    H  N N 494 
TRP   H2   H  N N 495 
TRP   HA   H  N N 496 
TRP   HB2  H  N N 497 
TRP   HB3  H  N N 498 
TRP   HD1  H  N N 499 
TRP   HE1  H  N N 500 
TRP   HE3  H  N N 501 
TRP   HZ2  H  N N 502 
TRP   HZ3  H  N N 503 
TRP   HH2  H  N N 504 
TRP   HXT  H  N N 505 
TYR   N    N  N N 506 
TYR   CA   C  N S 507 
TYR   C    C  N N 508 
TYR   O    O  N N 509 
TYR   CB   C  N N 510 
TYR   CG   C  Y N 511 
TYR   CD1  C  Y N 512 
TYR   CD2  C  Y N 513 
TYR   CE1  C  Y N 514 
TYR   CE2  C  Y N 515 
TYR   CZ   C  Y N 516 
TYR   OH   O  N N 517 
TYR   OXT  O  N N 518 
TYR   H    H  N N 519 
TYR   H2   H  N N 520 
TYR   HA   H  N N 521 
TYR   HB2  H  N N 522 
TYR   HB3  H  N N 523 
TYR   HD1  H  N N 524 
TYR   HD2  H  N N 525 
TYR   HE1  H  N N 526 
TYR   HE2  H  N N 527 
TYR   HH   H  N N 528 
TYR   HXT  H  N N 529 
VAL   N    N  N N 530 
VAL   CA   C  N S 531 
VAL   C    C  N N 532 
VAL   O    O  N N 533 
VAL   CB   C  N N 534 
VAL   CG1  C  N N 535 
VAL   CG2  C  N N 536 
VAL   OXT  O  N N 537 
VAL   H    H  N N 538 
VAL   H2   H  N N 539 
VAL   HA   H  N N 540 
VAL   HB   H  N N 541 
VAL   HG11 H  N N 542 
VAL   HG12 H  N N 543 
VAL   HG13 H  N N 544 
VAL   HG21 H  N N 545 
VAL   HG22 H  N N 546 
VAL   HG23 H  N N 547 
VAL   HXT  H  N N 548 
ZN    ZN   ZN N N 549 
# 
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 
A1A0C C07 C04  sing N N 1   
A1A0C C04 C03  doub Y N 2   
A1A0C C04 C05  sing Y N 3   
A1A0C C03 C02  sing Y N 4   
A1A0C C05 C06  doub Y N 5   
A1A0C F12 C12  sing N N 6   
A1A0C C02 N01  doub Y N 7   
A1A0C C02 N02  sing N N 8   
A1A0C C06 N01  sing Y N 9   
A1A0C C06 C11  sing N N 10  
A1A0C C12 C11  doub Y N 11  
A1A0C C12 C13  sing Y N 12  
A1A0C C11 C16  sing Y N 13  
A1A0C F13 C13  sing N N 14  
A1A0C C13 C14  doub Y N 15  
A1A0C C20 N19  sing N N 16  
A1A0C C16 C15  doub Y N 17  
A1A0C C14 C15  sing Y N 18  
A1A0C C18 N19  sing N N 19  
A1A0C C18 C17  sing N N 20  
A1A0C C15 C17  sing N N 21  
A1A0C C17 H1   sing N N 22  
A1A0C C17 H2   sing N N 23  
A1A0C C16 H3   sing N N 24  
A1A0C C14 H4   sing N N 25  
A1A0C C18 H5   sing N N 26  
A1A0C C18 H6   sing N N 27  
A1A0C C20 H7   sing N N 28  
A1A0C C20 H8   sing N N 29  
A1A0C C20 H9   sing N N 30  
A1A0C C03 H10  sing N N 31  
A1A0C C05 H11  sing N N 32  
A1A0C C07 H12  sing N N 33  
A1A0C C07 H13  sing N N 34  
A1A0C C07 H14  sing N N 35  
A1A0C N02 H15  sing N N 36  
A1A0C N02 H16  sing N N 37  
A1A0C N19 H17  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
GOL   C1  O1   sing N N 167 
GOL   C1  C2   sing N N 168 
GOL   C1  H11  sing N N 169 
GOL   C1  H12  sing N N 170 
GOL   O1  HO1  sing N N 171 
GOL   C2  O2   sing N N 172 
GOL   C2  C3   sing N N 173 
GOL   C2  H2   sing N N 174 
GOL   O2  HO2  sing N N 175 
GOL   C3  O3   sing N N 176 
GOL   C3  H31  sing N N 177 
GOL   C3  H32  sing N N 178 
GOL   O3  HO3  sing N N 179 
H4B   N1  C2   doub Y N 180 
H4B   N1  C8A  sing Y N 181 
H4B   C2  N2   sing N N 182 
H4B   C2  N3   sing Y N 183 
H4B   N2  HN21 sing N N 184 
H4B   N2  HN22 sing N N 185 
H4B   N3  C4   sing Y N 186 
H4B   N3  HN3  sing N N 187 
H4B   C4  O4   doub N N 188 
H4B   C4  C4A  sing Y N 189 
H4B   C4A C8A  doub Y N 190 
H4B   C4A N5   sing N N 191 
H4B   C8A N8   sing N N 192 
H4B   N5  C6   sing N N 193 
H4B   N5  HN5  sing N N 194 
H4B   N8  C7   sing N N 195 
H4B   N8  HN8  sing N N 196 
H4B   C6  C7   sing N N 197 
H4B   C6  C9   sing N N 198 
H4B   C6  H6   sing N N 199 
H4B   C7  H71  sing N N 200 
H4B   C7  H72  sing N N 201 
H4B   C9  O9   sing N N 202 
H4B   C9  C10  sing N N 203 
H4B   C9  H9   sing N N 204 
H4B   O9  HO9  sing N N 205 
H4B   C10 C11  sing N N 206 
H4B   C10 O10  sing N N 207 
H4B   C10 H10  sing N N 208 
H4B   C11 H111 sing N N 209 
H4B   C11 H112 sing N N 210 
H4B   C11 H113 sing N N 211 
H4B   O10 HO0  sing N N 212 
HEM   CHA C1A  sing N N 213 
HEM   CHA C4D  doub N N 214 
HEM   CHA HHA  sing N N 215 
HEM   CHB C4A  sing N N 216 
HEM   CHB C1B  doub N N 217 
HEM   CHB HHB  sing N N 218 
HEM   CHC C4B  sing N N 219 
HEM   CHC C1C  doub N N 220 
HEM   CHC HHC  sing N N 221 
HEM   CHD C4C  doub N N 222 
HEM   CHD C1D  sing N N 223 
HEM   CHD HHD  sing N N 224 
HEM   C1A C2A  doub Y N 225 
HEM   C1A NA   sing Y N 226 
HEM   C2A C3A  sing Y N 227 
HEM   C2A CAA  sing N N 228 
HEM   C3A C4A  doub Y N 229 
HEM   C3A CMA  sing N N 230 
HEM   C4A NA   sing Y N 231 
HEM   CMA HMA  sing N N 232 
HEM   CMA HMAA sing N N 233 
HEM   CMA HMAB sing N N 234 
HEM   CAA CBA  sing N N 235 
HEM   CAA HAA  sing N N 236 
HEM   CAA HAAA sing N N 237 
HEM   CBA CGA  sing N N 238 
HEM   CBA HBA  sing N N 239 
HEM   CBA HBAA sing N N 240 
HEM   CGA O1A  doub N N 241 
HEM   CGA O2A  sing N N 242 
HEM   C1B C2B  sing N N 243 
HEM   C1B NB   sing N N 244 
HEM   C2B C3B  doub N N 245 
HEM   C2B CMB  sing N N 246 
HEM   C3B C4B  sing N N 247 
HEM   C3B CAB  sing N N 248 
HEM   C4B NB   doub N N 249 
HEM   CMB HMB  sing N N 250 
HEM   CMB HMBA sing N N 251 
HEM   CMB HMBB sing N N 252 
HEM   CAB CBB  doub N N 253 
HEM   CAB HAB  sing N N 254 
HEM   CBB HBB  sing N N 255 
HEM   CBB HBBA sing N N 256 
HEM   C1C C2C  sing Y N 257 
HEM   C1C NC   sing Y N 258 
HEM   C2C C3C  doub Y N 259 
HEM   C2C CMC  sing N N 260 
HEM   C3C C4C  sing Y N 261 
HEM   C3C CAC  sing N N 262 
HEM   C4C NC   sing Y N 263 
HEM   CMC HMC  sing N N 264 
HEM   CMC HMCA sing N N 265 
HEM   CMC HMCB sing N N 266 
HEM   CAC CBC  doub N N 267 
HEM   CAC HAC  sing N N 268 
HEM   CBC HBC  sing N N 269 
HEM   CBC HBCA sing N N 270 
HEM   C1D C2D  sing N N 271 
HEM   C1D ND   doub N N 272 
HEM   C2D C3D  doub N N 273 
HEM   C2D CMD  sing N N 274 
HEM   C3D C4D  sing N N 275 
HEM   C3D CAD  sing N N 276 
HEM   C4D ND   sing N N 277 
HEM   CMD HMD  sing N N 278 
HEM   CMD HMDA sing N N 279 
HEM   CMD HMDB sing N N 280 
HEM   CAD CBD  sing N N 281 
HEM   CAD HAD  sing N N 282 
HEM   CAD HADA sing N N 283 
HEM   CBD CGD  sing N N 284 
HEM   CBD HBD  sing N N 285 
HEM   CBD HBDA sing N N 286 
HEM   CGD O1D  doub N N 287 
HEM   CGD O2D  sing N N 288 
HEM   O2A H2A  sing N N 289 
HEM   O2D H2D  sing N N 290 
HEM   FE  NA   sing N N 291 
HEM   FE  NB   sing N N 292 
HEM   FE  NC   sing N N 293 
HEM   FE  ND   sing N N 294 
HIS   N   CA   sing N N 295 
HIS   N   H    sing N N 296 
HIS   N   H2   sing N N 297 
HIS   CA  C    sing N N 298 
HIS   CA  CB   sing N N 299 
HIS   CA  HA   sing N N 300 
HIS   C   O    doub N N 301 
HIS   C   OXT  sing N N 302 
HIS   CB  CG   sing N N 303 
HIS   CB  HB2  sing N N 304 
HIS   CB  HB3  sing N N 305 
HIS   CG  ND1  sing Y N 306 
HIS   CG  CD2  doub Y N 307 
HIS   ND1 CE1  doub Y N 308 
HIS   ND1 HD1  sing N N 309 
HIS   CD2 NE2  sing Y N 310 
HIS   CD2 HD2  sing N N 311 
HIS   CE1 NE2  sing Y N 312 
HIS   CE1 HE1  sing N N 313 
HIS   NE2 HE2  sing N N 314 
HIS   OXT HXT  sing N N 315 
HOH   O   H1   sing N N 316 
HOH   O   H2   sing N N 317 
ILE   N   CA   sing N N 318 
ILE   N   H    sing N N 319 
ILE   N   H2   sing N N 320 
ILE   CA  C    sing N N 321 
ILE   CA  CB   sing N N 322 
ILE   CA  HA   sing N N 323 
ILE   C   O    doub N N 324 
ILE   C   OXT  sing N N 325 
ILE   CB  CG1  sing N N 326 
ILE   CB  CG2  sing N N 327 
ILE   CB  HB   sing N N 328 
ILE   CG1 CD1  sing N N 329 
ILE   CG1 HG12 sing N N 330 
ILE   CG1 HG13 sing N N 331 
ILE   CG2 HG21 sing N N 332 
ILE   CG2 HG22 sing N N 333 
ILE   CG2 HG23 sing N N 334 
ILE   CD1 HD11 sing N N 335 
ILE   CD1 HD12 sing N N 336 
ILE   CD1 HD13 sing N N 337 
ILE   OXT HXT  sing N N 338 
LEU   N   CA   sing N N 339 
LEU   N   H    sing N N 340 
LEU   N   H2   sing N N 341 
LEU   CA  C    sing N N 342 
LEU   CA  CB   sing N N 343 
LEU   CA  HA   sing N N 344 
LEU   C   O    doub N N 345 
LEU   C   OXT  sing N N 346 
LEU   CB  CG   sing N N 347 
LEU   CB  HB2  sing N N 348 
LEU   CB  HB3  sing N N 349 
LEU   CG  CD1  sing N N 350 
LEU   CG  CD2  sing N N 351 
LEU   CG  HG   sing N N 352 
LEU   CD1 HD11 sing N N 353 
LEU   CD1 HD12 sing N N 354 
LEU   CD1 HD13 sing N N 355 
LEU   CD2 HD21 sing N N 356 
LEU   CD2 HD22 sing N N 357 
LEU   CD2 HD23 sing N N 358 
LEU   OXT HXT  sing N N 359 
LYS   N   CA   sing N N 360 
LYS   N   H    sing N N 361 
LYS   N   H2   sing N N 362 
LYS   CA  C    sing N N 363 
LYS   CA  CB   sing N N 364 
LYS   CA  HA   sing N N 365 
LYS   C   O    doub N N 366 
LYS   C   OXT  sing N N 367 
LYS   CB  CG   sing N N 368 
LYS   CB  HB2  sing N N 369 
LYS   CB  HB3  sing N N 370 
LYS   CG  CD   sing N N 371 
LYS   CG  HG2  sing N N 372 
LYS   CG  HG3  sing N N 373 
LYS   CD  CE   sing N N 374 
LYS   CD  HD2  sing N N 375 
LYS   CD  HD3  sing N N 376 
LYS   CE  NZ   sing N N 377 
LYS   CE  HE2  sing N N 378 
LYS   CE  HE3  sing N N 379 
LYS   NZ  HZ1  sing N N 380 
LYS   NZ  HZ2  sing N N 381 
LYS   NZ  HZ3  sing N N 382 
LYS   OXT HXT  sing N N 383 
MET   N   CA   sing N N 384 
MET   N   H    sing N N 385 
MET   N   H2   sing N N 386 
MET   CA  C    sing N N 387 
MET   CA  CB   sing N N 388 
MET   CA  HA   sing N N 389 
MET   C   O    doub N N 390 
MET   C   OXT  sing N N 391 
MET   CB  CG   sing N N 392 
MET   CB  HB2  sing N N 393 
MET   CB  HB3  sing N N 394 
MET   CG  SD   sing N N 395 
MET   CG  HG2  sing N N 396 
MET   CG  HG3  sing N N 397 
MET   SD  CE   sing N N 398 
MET   CE  HE1  sing N N 399 
MET   CE  HE2  sing N N 400 
MET   CE  HE3  sing N N 401 
MET   OXT HXT  sing N N 402 
PHE   N   CA   sing N N 403 
PHE   N   H    sing N N 404 
PHE   N   H2   sing N N 405 
PHE   CA  C    sing N N 406 
PHE   CA  CB   sing N N 407 
PHE   CA  HA   sing N N 408 
PHE   C   O    doub N N 409 
PHE   C   OXT  sing N N 410 
PHE   CB  CG   sing N N 411 
PHE   CB  HB2  sing N N 412 
PHE   CB  HB3  sing N N 413 
PHE   CG  CD1  doub Y N 414 
PHE   CG  CD2  sing Y N 415 
PHE   CD1 CE1  sing Y N 416 
PHE   CD1 HD1  sing N N 417 
PHE   CD2 CE2  doub Y N 418 
PHE   CD2 HD2  sing N N 419 
PHE   CE1 CZ   doub Y N 420 
PHE   CE1 HE1  sing N N 421 
PHE   CE2 CZ   sing Y N 422 
PHE   CE2 HE2  sing N N 423 
PHE   CZ  HZ   sing N N 424 
PHE   OXT HXT  sing N N 425 
PRO   N   CA   sing N N 426 
PRO   N   CD   sing N N 427 
PRO   N   H    sing N N 428 
PRO   CA  C    sing N N 429 
PRO   CA  CB   sing N N 430 
PRO   CA  HA   sing N N 431 
PRO   C   O    doub N N 432 
PRO   C   OXT  sing N N 433 
PRO   CB  CG   sing N N 434 
PRO   CB  HB2  sing N N 435 
PRO   CB  HB3  sing N N 436 
PRO   CG  CD   sing N N 437 
PRO   CG  HG2  sing N N 438 
PRO   CG  HG3  sing N N 439 
PRO   CD  HD2  sing N N 440 
PRO   CD  HD3  sing N N 441 
PRO   OXT HXT  sing N N 442 
SER   N   CA   sing N N 443 
SER   N   H    sing N N 444 
SER   N   H2   sing N N 445 
SER   CA  C    sing N N 446 
SER   CA  CB   sing N N 447 
SER   CA  HA   sing N N 448 
SER   C   O    doub N N 449 
SER   C   OXT  sing N N 450 
SER   CB  OG   sing N N 451 
SER   CB  HB2  sing N N 452 
SER   CB  HB3  sing N N 453 
SER   OG  HG   sing N N 454 
SER   OXT HXT  sing N N 455 
THR   N   CA   sing N N 456 
THR   N   H    sing N N 457 
THR   N   H2   sing N N 458 
THR   CA  C    sing N N 459 
THR   CA  CB   sing N N 460 
THR   CA  HA   sing N N 461 
THR   C   O    doub N N 462 
THR   C   OXT  sing N N 463 
THR   CB  OG1  sing N N 464 
THR   CB  CG2  sing N N 465 
THR   CB  HB   sing N N 466 
THR   OG1 HG1  sing N N 467 
THR   CG2 HG21 sing N N 468 
THR   CG2 HG22 sing N N 469 
THR   CG2 HG23 sing N N 470 
THR   OXT HXT  sing N N 471 
TRP   N   CA   sing N N 472 
TRP   N   H    sing N N 473 
TRP   N   H2   sing N N 474 
TRP   CA  C    sing N N 475 
TRP   CA  CB   sing N N 476 
TRP   CA  HA   sing N N 477 
TRP   C   O    doub N N 478 
TRP   C   OXT  sing N N 479 
TRP   CB  CG   sing N N 480 
TRP   CB  HB2  sing N N 481 
TRP   CB  HB3  sing N N 482 
TRP   CG  CD1  doub Y N 483 
TRP   CG  CD2  sing Y N 484 
TRP   CD1 NE1  sing Y N 485 
TRP   CD1 HD1  sing N N 486 
TRP   CD2 CE2  doub Y N 487 
TRP   CD2 CE3  sing Y N 488 
TRP   NE1 CE2  sing Y N 489 
TRP   NE1 HE1  sing N N 490 
TRP   CE2 CZ2  sing Y N 491 
TRP   CE3 CZ3  doub Y N 492 
TRP   CE3 HE3  sing N N 493 
TRP   CZ2 CH2  doub Y N 494 
TRP   CZ2 HZ2  sing N N 495 
TRP   CZ3 CH2  sing Y N 496 
TRP   CZ3 HZ3  sing N N 497 
TRP   CH2 HH2  sing N N 498 
TRP   OXT HXT  sing N N 499 
TYR   N   CA   sing N N 500 
TYR   N   H    sing N N 501 
TYR   N   H2   sing N N 502 
TYR   CA  C    sing N N 503 
TYR   CA  CB   sing N N 504 
TYR   CA  HA   sing N N 505 
TYR   C   O    doub N N 506 
TYR   C   OXT  sing N N 507 
TYR   CB  CG   sing N N 508 
TYR   CB  HB2  sing N N 509 
TYR   CB  HB3  sing N N 510 
TYR   CG  CD1  doub Y N 511 
TYR   CG  CD2  sing Y N 512 
TYR   CD1 CE1  sing Y N 513 
TYR   CD1 HD1  sing N N 514 
TYR   CD2 CE2  doub Y N 515 
TYR   CD2 HD2  sing N N 516 
TYR   CE1 CZ   doub Y N 517 
TYR   CE1 HE1  sing N N 518 
TYR   CE2 CZ   sing Y N 519 
TYR   CE2 HE2  sing N N 520 
TYR   CZ  OH   sing N N 521 
TYR   OH  HH   sing N N 522 
TYR   OXT HXT  sing N N 523 
VAL   N   CA   sing N N 524 
VAL   N   H    sing N N 525 
VAL   N   H2   sing N N 526 
VAL   CA  C    sing N N 527 
VAL   CA  CB   sing N N 528 
VAL   CA  HA   sing N N 529 
VAL   C   O    doub N N 530 
VAL   C   OXT  sing N N 531 
VAL   CB  CG1  sing N N 532 
VAL   CB  CG2  sing N N 533 
VAL   CB  HB   sing N N 534 
VAL   CG1 HG11 sing N N 535 
VAL   CG1 HG12 sing N N 536 
VAL   CG1 HG13 sing N N 537 
VAL   CG2 HG21 sing N N 538 
VAL   CG2 HG22 sing N N 539 
VAL   CG2 HG23 sing N N 540 
VAL   OXT HXT  sing N N 541 
# 
_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   7TS7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CW1 
_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]   0.019394 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000012 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008616 
_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]   0.006134 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . PHE   A  1 4   ? -22.776 -25.966 -22.265  1.00 57.87  ? 305  PHE   A N   1 
ATOM   2     C  CA  . PHE   A  1 4   ? -23.435 -24.667 -22.245  1.00 57.50  ? 305  PHE   A CA  1 
ATOM   3     C  C   . PHE   A  1 4   ? -22.713 -23.680 -21.324  1.00 55.94  ? 305  PHE   A C   1 
ATOM   4     O  O   . PHE   A  1 4   ? -22.221 -24.045 -20.261  1.00 60.82  ? 305  PHE   A O   1 
ATOM   5     C  CB  . PHE   A  1 4   ? -24.901 -24.816 -21.812  1.00 71.23  ? 305  PHE   A CB  1 
ATOM   6     C  CG  . PHE   A  1 4   ? -25.109 -24.819 -20.312  1.00 84.29  ? 305  PHE   A CG  1 
ATOM   7     C  CD1 . PHE   A  1 4   ? -25.562 -23.679 -19.654  1.00 83.70  ? 305  PHE   A CD1 1 
ATOM   8     C  CD2 . PHE   A  1 4   ? -24.857 -25.962 -19.562  1.00 90.19  ? 305  PHE   A CD2 1 
ATOM   9     C  CE1 . PHE   A  1 4   ? -25.756 -23.681 -18.281  1.00 81.41  ? 305  PHE   A CE1 1 
ATOM   10    C  CE2 . PHE   A  1 4   ? -25.048 -25.968 -18.187  1.00 87.44  ? 305  PHE   A CE2 1 
ATOM   11    C  CZ  . PHE   A  1 4   ? -25.497 -24.827 -17.548  1.00 85.15  ? 305  PHE   A CZ  1 
ATOM   12    N  N   . LEU   A  1 5   ? -22.653 -22.421 -21.740  1.00 43.44  ? 306  LEU   A N   1 
ATOM   13    C  CA  . LEU   A  1 5   ? -22.111 -21.350 -20.920  1.00 41.56  ? 306  LEU   A CA  1 
ATOM   14    C  C   . LEU   A  1 5   ? -23.079 -20.184 -20.971  1.00 35.94  ? 306  LEU   A C   1 
ATOM   15    O  O   . LEU   A  1 5   ? -23.648 -19.889 -22.025  1.00 41.99  ? 306  LEU   A O   1 
ATOM   16    C  CB  . LEU   A  1 5   ? -20.725 -20.910 -21.405  1.00 38.20  ? 306  LEU   A CB  1 
ATOM   17    C  CG  . LEU   A  1 5   ? -19.591 -21.942 -21.429  1.00 39.42  ? 306  LEU   A CG  1 
ATOM   18    C  CD1 . LEU   A  1 5   ? -18.407 -21.426 -22.238  1.00 34.47  ? 306  LEU   A CD1 1 
ATOM   19    C  CD2 . LEU   A  1 5   ? -19.159 -22.273 -20.010  1.00 33.50  ? 306  LEU   A CD2 1 
ATOM   20    N  N   . LYS   A  1 6   ? -23.273 -19.520 -19.840  1.00 30.54  ? 307  LYS   A N   1 
ATOM   21    C  CA  . LYS   A  1 6   ? -24.209 -18.408 -19.750  1.00 31.90  ? 307  LYS   A CA  1 
ATOM   22    C  C   . LYS   A  1 6   ? -23.460 -17.087 -19.711  1.00 30.26  ? 307  LYS   A C   1 
ATOM   23    O  O   . LYS   A  1 6   ? -22.396 -16.979 -19.098  1.00 37.45  ? 307  LYS   A O   1 
ATOM   24    C  CB  . LYS   A  1 6   ? -25.097 -18.523 -18.505  1.00 37.19  ? 307  LYS   A CB  1 
ATOM   25    C  CG  . LYS   A  1 6   ? -26.121 -19.642 -18.572  1.00 49.19  ? 307  LYS   A CG  1 
ATOM   26    C  CD  . LYS   A  1 6   ? -26.986 -19.682 -17.313  1.00 54.39  ? 307  LYS   A CD  1 
ATOM   27    C  CE  . LYS   A  1 6   ? -27.928 -20.882 -17.324  1.00 60.07  ? 307  LYS   A CE  1 
ATOM   28    N  NZ  . LYS   A  1 6   ? -28.704 -20.980 -18.599  1.00 62.96  ? 307  LYS   A NZ  1 
ATOM   29    N  N   . VAL   A  1 7   ? -24.019 -16.078 -20.353  1.00 24.30  ? 308  VAL   A N   1 
ATOM   30    C  CA  . VAL   A  1 7   ? -23.535 -14.713 -20.213  1.00 28.08  ? 308  VAL   A CA  1 
ATOM   31    C  C   . VAL   A  1 7   ? -24.689 -13.877 -19.698  1.00 34.55  ? 308  VAL   A C   1 
ATOM   32    O  O   . VAL   A  1 7   ? -25.837 -14.038 -20.131  1.00 35.56  ? 308  VAL   A O   1 
ATOM   33    C  CB  . VAL   A  1 7   ? -22.975 -14.122 -21.525  1.00 34.80  ? 308  VAL   A CB  1 
ATOM   34    C  CG1 . VAL   A  1 7   ? -21.699 -14.840 -21.932  1.00 41.86  ? 308  VAL   A CG1 1 
ATOM   35    C  CG2 . VAL   A  1 7   ? -24.014 -14.191 -22.630  1.00 32.16  ? 308  VAL   A CG2 1 
ATOM   36    N  N   . LYS   A  1 8   ? -24.383 -13.001 -18.756  1.00 35.08  ? 309  LYS   A N   1 
ATOM   37    C  CA  . LYS   A  1 8   ? -25.373 -12.162 -18.117  1.00 27.72  ? 309  LYS   A CA  1 
ATOM   38    C  C   . LYS   A  1 8   ? -25.119 -10.719 -18.503  1.00 21.43  ? 309  LYS   A C   1 
ATOM   39    O  O   . LYS   A  1 8   ? -23.971 -10.274 -18.552  1.00 23.86  ? 309  LYS   A O   1 
ATOM   40    C  CB  . LYS   A  1 8   ? -25.323 -12.311 -16.582  1.00 27.18  ? 309  LYS   A CB  1 
ATOM   41    C  CG  . LYS   A  1 8   ? -26.289 -11.416 -15.840  1.00 28.78  ? 309  LYS   A CG  1 
ATOM   42    C  CD  . LYS   A  1 8   ? -26.406 -11.852 -14.378  1.00 38.63  ? 309  LYS   A CD  1 
ATOM   43    C  CE  . LYS   A  1 8   ? -27.213 -10.869 -13.556  1.00 40.06  ? 309  LYS   A CE  1 
ATOM   44    N  NZ  . LYS   A  1 8   ? -27.280 -11.309 -12.147  1.00 41.63  ? 309  LYS   A NZ  1 
ATOM   45    N  N   . ASN   A  1 9   ? -26.191 -9.994  -18.770  1.00 27.08  ? 310  ASN   A N   1 
ATOM   46    C  CA  . ASN   A  1 9   ? -26.124 -8.547  -18.838  1.00 28.50  ? 310  ASN   A CA  1 
ATOM   47    C  C   . ASN   A  1 9   ? -26.491 -8.000  -17.464  1.00 25.49  ? 310  ASN   A C   1 
ATOM   48    O  O   . ASN   A  1 9   ? -27.581 -8.279  -16.952  1.00 29.83  ? 310  ASN   A O   1 
ATOM   49    C  CB  . ASN   A  1 9   ? -27.055 -8.001  -19.915  1.00 30.41  ? 310  ASN   A CB  1 
ATOM   50    C  CG  . ASN   A  1 9   ? -26.881 -6.533  -20.096  1.00 35.04  ? 310  ASN   A CG  1 
ATOM   51    O  OD1 . ASN   A  1 9   ? -27.307 -5.739  -19.254  1.00 37.91  ? 310  ASN   A OD1 1 
ATOM   52    N  ND2 . ASN   A  1 9   ? -26.203 -6.150  -21.162  1.00 31.90  ? 310  ASN   A ND2 1 
ATOM   53    N  N   . TRP   A  1 10  ? -25.581 -7.244  -16.860  1.00 21.38  ? 311  TRP   A N   1 
ATOM   54    C  CA  . TRP   A  1 10  ? -25.785 -6.847  -15.471  1.00 33.12  ? 311  TRP   A CA  1 
ATOM   55    C  C   . TRP   A  1 10  ? -26.666 -5.623  -15.337  1.00 37.97  ? 311  TRP   A C   1 
ATOM   56    O  O   . TRP   A  1 10  ? -27.070 -5.285  -14.223  1.00 37.94  ? 311  TRP   A O   1 
ATOM   57    C  CB  . TRP   A  1 10  ? -24.439 -6.613  -14.784  1.00 27.73  ? 311  TRP   A CB  1 
ATOM   58    C  CG  . TRP   A  1 10  ? -23.756 -7.916  -14.535  1.00 27.55  ? 311  TRP   A CG  1 
ATOM   59    C  CD1 . TRP   A  1 10  ? -22.894 -8.567  -15.368  1.00 27.69  ? 311  TRP   A CD1 1 
ATOM   60    C  CD2 . TRP   A  1 10  ? -23.921 -8.754  -13.389  1.00 34.88  ? 311  TRP   A CD2 1 
ATOM   61    N  NE1 . TRP   A  1 10  ? -22.492 -9.756  -14.796  1.00 25.56  ? 311  TRP   A NE1 1 
ATOM   62    C  CE2 . TRP   A  1 10  ? -23.113 -9.896  -13.584  1.00 31.76  ? 311  TRP   A CE2 1 
ATOM   63    C  CE3 . TRP   A  1 10  ? -24.659 -8.643  -12.205  1.00 34.99  ? 311  TRP   A CE3 1 
ATOM   64    C  CZ2 . TRP   A  1 10  ? -23.025 -10.919 -12.643  1.00 35.15  ? 311  TRP   A CZ2 1 
ATOM   65    C  CZ3 . TRP   A  1 10  ? -24.573 -9.662  -11.273  1.00 39.83  ? 311  TRP   A CZ3 1 
ATOM   66    C  CH2 . TRP   A  1 10  ? -23.761 -10.786 -11.499  1.00 45.96  ? 311  TRP   A CH2 1 
ATOM   67    N  N   . GLU   A  1 11  ? -26.972 -4.959  -16.439  1.00 31.17  ? 312  GLU   A N   1 
ATOM   68    C  CA  . GLU   A  1 11  ? -27.951 -3.888  -16.424  1.00 34.51  ? 312  GLU   A CA  1 
ATOM   69    C  C   . GLU   A  1 11  ? -29.361 -4.432  -16.587  1.00 39.73  ? 312  GLU   A C   1 
ATOM   70    O  O   . GLU   A  1 11  ? -30.273 -4.030  -15.859  1.00 42.42  ? 312  GLU   A O   1 
ATOM   71    C  CB  . GLU   A  1 11  ? -27.624 -2.889  -17.530  1.00 35.37  ? 312  GLU   A CB  1 
ATOM   72    C  CG  . GLU   A  1 11  ? -28.485 -1.660  -17.556  1.00 53.30  ? 312  GLU   A CG  1 
ATOM   73    C  CD  . GLU   A  1 11  ? -28.133 -0.746  -18.718  1.00 60.78  ? 312  GLU   A CD  1 
ATOM   74    O  OE1 . GLU   A  1 11  ? -27.122 -1.017  -19.407  1.00 44.98  ? 312  GLU   A OE1 1 
ATOM   75    O  OE2 . GLU   A  1 11  ? -28.875 0.238   -18.942  1.00 73.16  ? 312  GLU   A OE2 1 
ATOM   76    N  N   . THR   A  1 12  ? -29.551 -5.380  -17.500  1.00 33.63  ? 313  THR   A N   1 
ATOM   77    C  CA  . THR   A  1 12  ? -30.885 -5.854  -17.832  1.00 35.13  ? 313  THR   A CA  1 
ATOM   78    C  C   . THR   A  1 12  ? -31.235 -7.173  -17.169  1.00 36.75  ? 313  THR   A C   1 
ATOM   79    O  O   . THR   A  1 12  ? -32.412 -7.543  -17.150  1.00 36.91  ? 313  THR   A O   1 
ATOM   80    C  CB  . THR   A  1 12  ? -31.013 -6.014  -19.348  1.00 40.32  ? 313  THR   A CB  1 
ATOM   81    O  OG1 . THR   A  1 12  ? -30.078 -7.003  -19.793  1.00 45.04  ? 313  THR   A OG1 1 
ATOM   82    C  CG2 . THR   A  1 12  ? -30.693 -4.697  -20.043  1.00 40.01  ? 313  THR   A CG2 1 
ATOM   83    N  N   . GLU   A  1 13  ? -30.243 -7.892  -16.649  1.00 34.52  ? 314  GLU   A N   1 
ATOM   84    C  CA  . GLU   A  1 13  ? -30.372 -9.245  -16.120  1.00 40.72  ? 314  GLU   A CA  1 
ATOM   85    C  C   . GLU   A  1 13  ? -30.718 -10.266 -17.195  1.00 37.16  ? 314  GLU   A C   1 
ATOM   86    O  O   . GLU   A  1 13  ? -30.987 -11.426 -16.873  1.00 41.31  ? 314  GLU   A O   1 
ATOM   87    C  CB  . GLU   A  1 13  ? -31.385 -9.308  -14.975  1.00 51.73  ? 314  GLU   A CB  1 
ATOM   88    C  CG  . GLU   A  1 13  ? -31.144 -8.237  -13.926  1.00 61.72  ? 314  GLU   A CG  1 
ATOM   89    C  CD  . GLU   A  1 13  ? -31.351 -8.748  -12.521  1.00 75.27  ? 314  GLU   A CD  1 
ATOM   90    O  OE1 . GLU   A  1 13  ? -30.680 -9.734  -12.137  1.00 82.45  ? 314  GLU   A OE1 1 
ATOM   91    O  OE2 . GLU   A  1 13  ? -32.190 -8.167  -11.805  1.00 77.90  ? 314  GLU   A OE2 1 
ATOM   92    N  N   . VAL   A  1 14  ? -30.696 -9.877  -18.469  1.00 39.44  ? 315  VAL   A N   1 
ATOM   93    C  CA  . VAL   A  1 14  ? -30.818 -10.865 -19.532  1.00 41.29  ? 315  VAL   A CA  1 
ATOM   94    C  C   . VAL   A  1 14  ? -29.647 -11.833 -19.453  1.00 38.32  ? 315  VAL   A C   1 
ATOM   95    O  O   . VAL   A  1 14  ? -28.483 -11.428 -19.307  1.00 34.18  ? 315  VAL   A O   1 
ATOM   96    C  CB  . VAL   A  1 14  ? -30.898 -10.171 -20.896  1.00 43.33  ? 315  VAL   A CB  1 
ATOM   97    C  CG1 . VAL   A  1 14  ? -30.766 -11.189 -22.036  1.00 41.72  ? 315  VAL   A CG1 1 
ATOM   98    C  CG2 . VAL   A  1 14  ? -32.200 -9.397  -21.006  1.00 46.04  ? 315  VAL   A CG2 1 
ATOM   99    N  N   . VAL   A  1 15  ? -29.959 -13.126 -19.490  1.00 32.41  ? 316  VAL   A N   1 
ATOM   100   C  CA  . VAL   A  1 15  ? -28.960 -14.183 -19.537  1.00 32.25  ? 316  VAL   A CA  1 
ATOM   101   C  C   . VAL   A  1 15  ? -29.097 -14.898 -20.874  1.00 31.88  ? 316  VAL   A C   1 
ATOM   102   O  O   . VAL   A  1 15  ? -30.200 -15.314 -21.250  1.00 36.10  ? 316  VAL   A O   1 
ATOM   103   C  CB  . VAL   A  1 15  ? -29.109 -15.185 -18.380  1.00 30.25  ? 316  VAL   A CB  1 
ATOM   104   C  CG1 . VAL   A  1 15  ? -28.071 -16.293 -18.526  1.00 29.46  ? 316  VAL   A CG1 1 
ATOM   105   C  CG2 . VAL   A  1 15  ? -28.980 -14.493 -17.023  1.00 28.20  ? 316  VAL   A CG2 1 
ATOM   106   N  N   . LEU   A  1 16  ? -27.980 -15.043 -21.579  1.00 32.88  ? 317  LEU   A N   1 
ATOM   107   C  CA  . LEU   A  1 16  ? -27.919 -15.769 -22.841  1.00 34.38  ? 317  LEU   A CA  1 
ATOM   108   C  C   . LEU   A  1 16  ? -27.065 -17.013 -22.646  1.00 39.00  ? 317  LEU   A C   1 
ATOM   109   O  O   . LEU   A  1 16  ? -26.086 -16.993 -21.893  1.00 43.51  ? 317  LEU   A O   1 
ATOM   110   C  CB  . LEU   A  1 16  ? -27.340 -14.897 -23.954  1.00 31.84  ? 317  LEU   A CB  1 
ATOM   111   C  CG  . LEU   A  1 16  ? -28.092 -13.580 -24.136  1.00 36.31  ? 317  LEU   A CG  1 
ATOM   112   C  CD1 . LEU   A  1 16  ? -27.408 -12.716 -25.145  1.00 32.85  ? 317  LEU   A CD1 1 
ATOM   113   C  CD2 . LEU   A  1 16  ? -29.556 -13.834 -24.505  1.00 34.61  ? 317  LEU   A CD2 1 
ATOM   114   N  N   . THR   A  1 17  ? -27.452 -18.096 -23.310  1.00 33.75  ? 318  THR   A N   1 
ATOM   115   C  CA  . THR   A  1 17  ? -26.814 -19.390 -23.138  1.00 37.64  ? 318  THR   A CA  1 
ATOM   116   C  C   . THR   A  1 17  ? -26.074 -19.729 -24.419  1.00 31.24  ? 318  THR   A C   1 
ATOM   117   O  O   . THR   A  1 17  ? -26.688 -19.815 -25.484  1.00 32.58  ? 318  THR   A O   1 
ATOM   118   C  CB  . THR   A  1 17  ? -27.842 -20.470 -22.810  1.00 41.14  ? 318  THR   A CB  1 
ATOM   119   O  OG1 . THR   A  1 17  ? -28.718 -19.997 -21.778  1.00 44.50  ? 318  THR   A OG1 1 
ATOM   120   C  CG2 . THR   A  1 17  ? -27.140 -21.735 -22.333  1.00 43.95  ? 318  THR   A CG2 1 
ATOM   121   N  N   . ASP   A  1 18  ? -24.767 -19.942 -24.312  1.00 26.23  ? 319  ASP   A N   1 
ATOM   122   C  CA  . ASP   A  1 18  ? -23.912 -20.119 -25.472  1.00 22.95  ? 319  ASP   A CA  1 
ATOM   123   C  C   . ASP   A  1 18  ? -23.635 -21.599 -25.696  1.00 37.40  ? 319  ASP   A C   1 
ATOM   124   O  O   . ASP   A  1 18  ? -23.117 -22.281 -24.805  1.00 33.41  ? 319  ASP   A O   1 
ATOM   125   C  CB  . ASP   A  1 18  ? -22.604 -19.360 -25.283  1.00 28.85  ? 319  ASP   A CB  1 
ATOM   126   C  CG  . ASP   A  1 18  ? -21.788 -19.297 -26.550  1.00 28.76  ? 319  ASP   A CG  1 
ATOM   127   O  OD1 . ASP   A  1 18  ? -21.379 -20.357 -27.056  1.00 31.14  ? 319  ASP   A OD1 1 
ATOM   128   O  OD2 . ASP   A  1 18  ? -21.568 -18.180 -27.047  1.00 30.05  ? 319  ASP   A OD2 1 
ATOM   129   N  N   . THR   A  1 19  ? -23.988 -22.090 -26.884  1.00 32.53  ? 320  THR   A N   1 
ATOM   130   C  CA  . THR   A  1 19  ? -23.533 -23.386 -27.368  1.00 26.53  ? 320  THR   A CA  1 
ATOM   131   C  C   . THR   A  1 19  ? -22.656 -23.269 -28.603  1.00 29.38  ? 320  THR   A C   1 
ATOM   132   O  O   . THR   A  1 19  ? -21.969 -24.234 -28.949  1.00 32.55  ? 320  THR   A O   1 
ATOM   133   C  CB  . THR   A  1 19  ? -24.723 -24.297 -27.713  1.00 28.72  ? 320  THR   A CB  1 
ATOM   134   O  OG1 . THR   A  1 19  ? -25.606 -23.612 -28.609  1.00 33.60  ? 320  THR   A OG1 1 
ATOM   135   C  CG2 . THR   A  1 19  ? -25.487 -24.716 -26.469  1.00 35.18  ? 320  THR   A CG2 1 
ATOM   136   N  N   . LEU   A  1 20  ? -22.665 -22.117 -29.275  1.00 29.55  ? 321  LEU   A N   1 
ATOM   137   C  CA  . LEU   A  1 20  ? -21.845 -21.967 -30.470  1.00 31.55  ? 321  LEU   A CA  1 
ATOM   138   C  C   . LEU   A  1 20  ? -20.372 -22.234 -30.176  1.00 36.75  ? 321  LEU   A C   1 
ATOM   139   O  O   . LEU   A  1 20  ? -19.672 -22.782 -31.031  1.00 26.52  ? 321  LEU   A O   1 
ATOM   140   C  CB  . LEU   A  1 20  ? -22.034 -20.571 -31.062  1.00 22.48  ? 321  LEU   A CB  1 
ATOM   141   C  CG  . LEU   A  1 20  ? -21.356 -20.266 -32.397  1.00 25.82  ? 321  LEU   A CG  1 
ATOM   142   C  CD1 . LEU   A  1 20  ? -21.874 -21.182 -33.500  1.00 29.92  ? 321  LEU   A CD1 1 
ATOM   143   C  CD2 . LEU   A  1 20  ? -21.613 -18.823 -32.739  1.00 19.94  ? 321  LEU   A CD2 1 
ATOM   144   N  N   . HIS   A  1 21  ? -19.897 -21.909 -28.959  1.00 25.60  ? 322  HIS   A N   1 
ATOM   145   C  CA  . HIS   A  1 21  ? -18.472 -22.046 -28.656  1.00 25.24  ? 322  HIS   A CA  1 
ATOM   146   C  C   . HIS   A  1 21  ? -17.978 -23.478 -28.801  1.00 30.70  ? 322  HIS   A C   1 
ATOM   147   O  O   . HIS   A  1 21  ? -16.763 -23.700 -28.865  1.00 28.61  ? 322  HIS   A O   1 
ATOM   148   C  CB  . HIS   A  1 21  ? -18.166 -21.583 -27.234  1.00 24.86  ? 322  HIS   A CB  1 
ATOM   149   C  CG  . HIS   A  1 21  ? -18.675 -22.527 -26.194  1.00 27.80  ? 322  HIS   A CG  1 
ATOM   150   N  ND1 . HIS   A  1 21  ? -19.958 -22.457 -25.699  1.00 27.48  ? 322  HIS   A ND1 1 
ATOM   151   C  CD2 . HIS   A  1 21  ? -18.098 -23.597 -25.602  1.00 30.80  ? 322  HIS   A CD2 1 
ATOM   152   C  CE1 . HIS   A  1 21  ? -20.143 -23.431 -24.828  1.00 38.02  ? 322  HIS   A CE1 1 
ATOM   153   N  NE2 . HIS   A  1 21  ? -19.031 -24.140 -24.754  1.00 34.77  ? 322  HIS   A NE2 1 
ATOM   154   N  N   . LEU   A  1 22  ? -18.879 -24.461 -28.821  1.00 28.80  ? 323  LEU   A N   1 
ATOM   155   C  CA  . LEU   A  1 22  ? -18.437 -25.834 -29.020  1.00 36.67  ? 323  LEU   A CA  1 
ATOM   156   C  C   . LEU   A  1 22  ? -17.818 -26.027 -30.389  1.00 40.78  ? 323  LEU   A C   1 
ATOM   157   O  O   . LEU   A  1 22  ? -17.124 -27.023 -30.607  1.00 48.23  ? 323  LEU   A O   1 
ATOM   158   C  CB  . LEU   A  1 22  ? -19.599 -26.807 -28.842  1.00 43.92  ? 323  LEU   A CB  1 
ATOM   159   C  CG  . LEU   A  1 22  ? -20.299 -26.848 -27.483  1.00 45.03  ? 323  LEU   A CG  1 
ATOM   160   C  CD1 . LEU   A  1 22  ? -21.432 -27.843 -27.551  1.00 52.50  ? 323  LEU   A CD1 1 
ATOM   161   C  CD2 . LEU   A  1 22  ? -19.345 -27.211 -26.351  1.00 43.22  ? 323  LEU   A CD2 1 
ATOM   162   N  N   . LYS   A  1 23  ? -18.052 -25.096 -31.308  1.00 31.15  ? 324  LYS   A N   1 
ATOM   163   C  CA  . LYS   A  1 23  ? -17.492 -25.138 -32.648  1.00 35.88  ? 324  LYS   A CA  1 
ATOM   164   C  C   . LYS   A  1 23  ? -16.215 -24.334 -32.785  1.00 41.34  ? 324  LYS   A C   1 
ATOM   165   O  O   . LYS   A  1 23  ? -15.760 -24.123 -33.914  1.00 46.90  ? 324  LYS   A O   1 
ATOM   166   C  CB  . LYS   A  1 23  ? -18.499 -24.605 -33.666  1.00 31.88  ? 324  LYS   A CB  1 
ATOM   167   C  CG  . LYS   A  1 23  ? -19.694 -25.476 -33.862  1.00 45.31  ? 324  LYS   A CG  1 
ATOM   168   C  CD  . LYS   A  1 23  ? -19.878 -25.790 -35.329  1.00 55.40  ? 324  LYS   A CD  1 
ATOM   169   C  CE  . LYS   A  1 23  ? -19.405 -27.192 -35.644  1.00 64.10  ? 324  LYS   A CE  1 
ATOM   170   N  NZ  . LYS   A  1 23  ? -20.459 -27.977 -36.353  1.00 64.69  ? 324  LYS   A NZ  1 
ATOM   171   N  N   . SER   A  1 24  ? -15.648 -23.840 -31.690  1.00 30.89  ? 325  SER   A N   1 
ATOM   172   C  CA  . SER   A  1 24  ? -14.449 -23.029 -31.827  1.00 36.80  ? 325  SER   A CA  1 
ATOM   173   C  C   . SER   A  1 24  ? -13.284 -23.902 -32.283  1.00 42.37  ? 325  SER   A C   1 
ATOM   174   O  O   . SER   A  1 24  ? -13.229 -25.097 -31.992  1.00 42.53  ? 325  SER   A O   1 
ATOM   175   C  CB  . SER   A  1 24  ? -14.115 -22.332 -30.509  1.00 36.52  ? 325  SER   A CB  1 
ATOM   176   O  OG  . SER   A  1 24  ? -13.506 -23.240 -29.617  1.00 50.97  ? 325  SER   A OG  1 
ATOM   177   N  N   . THR   A  1 25  ? -12.346 -23.297 -33.010  1.00 46.80  ? 326  THR   A N   1 
ATOM   178   C  CA  . THR   A  1 25  ? -11.276 -24.067 -33.629  1.00 52.96  ? 326  THR   A CA  1 
ATOM   179   C  C   . THR   A  1 25  ? -9.884  -23.699 -33.138  1.00 52.72  ? 326  THR   A C   1 
ATOM   180   O  O   . THR   A  1 25  ? -9.074  -24.593 -32.879  1.00 62.34  ? 326  THR   A O   1 
ATOM   181   C  CB  . THR   A  1 25  ? -11.363 -23.921 -35.158  1.00 60.67  ? 326  THR   A CB  1 
ATOM   182   O  OG1 . THR   A  1 25  ? -11.935 -22.650 -35.480  1.00 59.54  ? 326  THR   A OG1 1 
ATOM   183   C  CG2 . THR   A  1 25  ? -12.252 -25.017 -35.750  1.00 63.49  ? 326  THR   A CG2 1 
ATOM   184   N  N   . LEU   A  1 26  ? -9.584  -22.416 -32.975  1.00 42.40  ? 327  LEU   A N   1 
ATOM   185   C  CA  . LEU   A  1 26  ? -8.262  -21.971 -32.561  1.00 45.37  ? 327  LEU   A CA  1 
ATOM   186   C  C   . LEU   A  1 26  ? -8.217  -21.660 -31.067  1.00 46.35  ? 327  LEU   A C   1 
ATOM   187   O  O   . LEU   A  1 26  ? -9.213  -21.252 -30.462  1.00 34.91  ? 327  LEU   A O   1 
ATOM   188   C  CB  . LEU   A  1 26  ? -7.831  -20.729 -33.348  1.00 56.91  ? 327  LEU   A CB  1 
ATOM   189   C  CG  . LEU   A  1 26  ? -7.469  -20.902 -34.831  1.00 57.94  ? 327  LEU   A CG  1 
ATOM   190   C  CD1 . LEU   A  1 26  ? -6.723  -22.221 -35.051  1.00 52.73  ? 327  LEU   A CD1 1 
ATOM   191   C  CD2 . LEU   A  1 26  ? -8.693  -20.789 -35.736  1.00 58.24  ? 327  LEU   A CD2 1 
ATOM   192   N  N   . GLU   A  1 27  ? -7.038  -21.863 -30.482  1.00 40.28  ? 328  GLU   A N   1 
ATOM   193   C  CA  . GLU   A  1 27  ? -6.787  -21.424 -29.118  1.00 37.26  ? 328  GLU   A CA  1 
ATOM   194   C  C   . GLU   A  1 27  ? -6.974  -19.918 -29.005  1.00 37.28  ? 328  GLU   A C   1 
ATOM   195   O  O   . GLU   A  1 27  ? -6.605  -19.158 -29.904  1.00 34.25  ? 328  GLU   A O   1 
ATOM   196   C  CB  . GLU   A  1 27  ? -5.372  -21.819 -28.693  1.00 33.30  ? 328  GLU   A CB  1 
ATOM   197   C  CG  . GLU   A  1 27  ? -5.152  -23.327 -28.606  1.00 32.18  ? 328  GLU   A CG  1 
ATOM   198   C  CD  . GLU   A  1 27  ? -3.758  -23.693 -28.135  1.00 43.11  ? 328  GLU   A CD  1 
ATOM   199   O  OE1 . GLU   A  1 27  ? -2.900  -22.787 -28.065  1.00 42.12  ? 328  GLU   A OE1 1 
ATOM   200   O  OE2 . GLU   A  1 27  ? -3.517  -24.885 -27.833  1.00 45.76  ? 328  GLU   A OE2 1 
ATOM   201   N  N   . THR   A  1 28  ? -7.585  -19.488 -27.903  1.00 30.64  ? 329  THR   A N   1 
ATOM   202   C  CA  . THR   A  1 28  ? -7.674  -18.066 -27.609  1.00 22.54  ? 329  THR   A CA  1 
ATOM   203   C  C   . THR   A  1 28  ? -6.361  -17.508 -27.102  1.00 24.81  ? 329  THR   A C   1 
ATOM   204   O  O   . THR   A  1 28  ? -6.170  -16.290 -27.137  1.00 30.77  ? 329  THR   A O   1 
ATOM   205   C  CB  . THR   A  1 28  ? -8.736  -17.795 -26.543  1.00 33.19  ? 329  THR   A CB  1 
ATOM   206   O  OG1 . THR   A  1 28  ? -8.390  -18.511 -25.335  1.00 28.89  ? 329  THR   A OG1 1 
ATOM   207   C  CG2 . THR   A  1 28  ? -10.120 -18.207 -27.032  1.00 30.14  ? 329  THR   A CG2 1 
ATOM   208   N  N   . GLY   A  1 29  ? -5.470  -18.365 -26.616  1.00 26.82  ? 330  GLY   A N   1 
ATOM   209   C  CA  . GLY   A  1 29  ? -4.328  -17.946 -25.847  1.00 33.84  ? 330  GLY   A CA  1 
ATOM   210   C  C   . GLY   A  1 29  ? -4.507  -18.106 -24.350  1.00 34.85  ? 330  GLY   A C   1 
ATOM   211   O  O   . GLY   A  1 29  ? -3.511  -18.242 -23.630  1.00 37.08  ? 330  GLY   A O   1 
ATOM   212   N  N   . CYS   A  1 30  ? -5.746  -18.116 -23.867  1.00 34.43  ? 331  CYS   A N   1 
ATOM   213   C  CA  . CYS   A  1 30  ? -5.995  -18.325 -22.447  1.00 27.97  ? 331  CYS   A CA  1 
ATOM   214   C  C   . CYS   A  1 30  ? -5.826  -19.789 -22.083  1.00 29.96  ? 331  CYS   A C   1 
ATOM   215   O  O   . CYS   A  1 30  ? -5.832  -20.677 -22.937  1.00 29.93  ? 331  CYS   A O   1 
ATOM   216   C  CB  . CYS   A  1 30  ? -7.406  -17.878 -22.060  1.00 23.18  ? 331  CYS   A CB  1 
ATOM   217   S  SG  . CYS   A  1 30  ? -7.754  -16.185 -22.509  1.00 27.70  ? 331  CYS   A SG  1 
ATOM   218   N  N   . THR   A  1 31  ? -5.671  -20.029 -20.786  1.00 27.35  ? 332  THR   A N   1 
ATOM   219   C  CA  . THR   A  1 31  ? -5.788  -21.352 -20.201  1.00 30.27  ? 332  THR   A CA  1 
ATOM   220   C  C   . THR   A  1 31  ? -6.652  -21.234 -18.956  1.00 29.03  ? 332  THR   A C   1 
ATOM   221   O  O   . THR   A  1 31  ? -7.046  -20.142 -18.547  1.00 35.51  ? 332  THR   A O   1 
ATOM   222   C  CB  . THR   A  1 31  ? -4.423  -21.946 -19.836  1.00 32.99  ? 332  THR   A CB  1 
ATOM   223   O  OG1 . THR   A  1 31  ? -3.892  -21.249 -18.698  1.00 32.48  ? 332  THR   A OG1 1 
ATOM   224   C  CG2 . THR   A  1 31  ? -3.451  -21.836 -20.994  1.00 31.04  ? 332  THR   A CG2 1 
ATOM   225   N  N   . GLU   A  1 32  ? -6.947  -22.366 -18.334  1.00 33.24  ? 333  GLU   A N   1 
ATOM   226   C  CA  . GLU   A  1 32  ? -7.644  -22.275 -17.063  1.00 38.38  ? 333  GLU   A CA  1 
ATOM   227   C  C   . GLU   A  1 32  ? -6.816  -21.554 -16.009  1.00 33.90  ? 333  GLU   A C   1 
ATOM   228   O  O   . GLU   A  1 32  ? -7.379  -21.121 -15.007  1.00 35.20  ? 333  GLU   A O   1 
ATOM   229   C  CB  . GLU   A  1 32  ? -8.059  -23.669 -16.577  1.00 48.95  ? 333  GLU   A CB  1 
ATOM   230   C  CG  . GLU   A  1 32  ? -6.990  -24.725 -16.686  1.00 66.14  ? 333  GLU   A CG  1 
ATOM   231   C  CD  . GLU   A  1 32  ? -7.194  -25.618 -17.897  1.00 83.87  ? 333  GLU   A CD  1 
ATOM   232   O  OE1 . GLU   A  1 32  ? -7.142  -25.107 -19.043  1.00 78.58  ? 333  GLU   A OE1 1 
ATOM   233   O  OE2 . GLU   A  1 32  ? -7.426  -26.831 -17.694  1.00 95.43  ? 333  GLU   A OE2 1 
ATOM   234   N  N   . TYR   A  1 33  ? -5.512  -21.371 -16.227  1.00 30.54  ? 334  TYR   A N   1 
ATOM   235   C  CA  . TYR   A  1 33  ? -4.653  -20.700 -15.259  1.00 28.61  ? 334  TYR   A CA  1 
ATOM   236   C  C   . TYR   A  1 33  ? -4.272  -19.276 -15.651  1.00 30.92  ? 334  TYR   A C   1 
ATOM   237   O  O   . TYR   A  1 33  ? -3.839  -18.510 -14.787  1.00 31.66  ? 334  TYR   A O   1 
ATOM   238   C  CB  . TYR   A  1 33  ? -3.382  -21.523 -15.043  1.00 35.47  ? 334  TYR   A CB  1 
ATOM   239   C  CG  . TYR   A  1 33  ? -3.676  -22.851 -14.396  1.00 46.41  ? 334  TYR   A CG  1 
ATOM   240   C  CD1 . TYR   A  1 33  ? -4.224  -22.904 -13.119  1.00 61.45  ? 334  TYR   A CD1 1 
ATOM   241   C  CD2 . TYR   A  1 33  ? -3.416  -24.048 -15.048  1.00 49.00  ? 334  TYR   A CD2 1 
ATOM   242   C  CE1 . TYR   A  1 33  ? -4.506  -24.109 -12.510  1.00 69.19  ? 334  TYR   A CE1 1 
ATOM   243   C  CE2 . TYR   A  1 33  ? -3.695  -25.267 -14.439  1.00 60.67  ? 334  TYR   A CE2 1 
ATOM   244   C  CZ  . TYR   A  1 33  ? -4.237  -25.287 -13.167  1.00 71.89  ? 334  TYR   A CZ  1 
ATOM   245   O  OH  . TYR   A  1 33  ? -4.520  -26.481 -12.538  1.00 81.85  ? 334  TYR   A OH  1 
ATOM   246   N  N   . ILE   A  1 34  ? -4.423  -18.887 -16.911  1.00 30.61  ? 335  ILE   A N   1 
ATOM   247   C  CA  . ILE   A  1 34  ? -4.033  -17.548 -17.333  1.00 30.99  ? 335  ILE   A CA  1 
ATOM   248   C  C   . ILE   A  1 34  ? -5.044  -17.016 -18.340  1.00 34.47  ? 335  ILE   A C   1 
ATOM   249   O  O   . ILE   A  1 34  ? -5.483  -17.733 -19.244  1.00 38.87  ? 335  ILE   A O   1 
ATOM   250   C  CB  . ILE   A  1 34  ? -2.609  -17.543 -17.917  1.00 35.85  ? 335  ILE   A CB  1 
ATOM   251   C  CG1 . ILE   A  1 34  ? -2.119  -16.117 -18.098  1.00 33.61  ? 335  ILE   A CG1 1 
ATOM   252   C  CG2 . ILE   A  1 34  ? -2.566  -18.258 -19.267  1.00 45.60  ? 335  ILE   A CG2 1 
ATOM   253   C  CD1 . ILE   A  1 34  ? -0.649  -16.000 -17.879  1.00 31.10  ? 335  ILE   A CD1 1 
ATOM   254   N  N   . CYS   A  1 35  ? -5.437  -15.764 -18.179  1.00 26.87  ? 336  CYS   A N   1 
ATOM   255   C  CA  . CYS   A  1 35  ? -6.302  -15.130 -19.155  1.00 22.20  ? 336  CYS   A CA  1 
ATOM   256   C  C   . CYS   A  1 35  ? -5.482  -14.123 -19.941  1.00 26.81  ? 336  CYS   A C   1 
ATOM   257   O  O   . CYS   A  1 35  ? -4.758  -13.312 -19.356  1.00 27.20  ? 336  CYS   A O   1 
ATOM   258   C  CB  . CYS   A  1 35  ? -7.508  -14.450 -18.514  1.00 23.81  ? 336  CYS   A CB  1 
ATOM   259   S  SG  . CYS   A  1 35  ? -8.446  -13.509 -19.750  1.00 26.75  ? 336  CYS   A SG  1 
ATOM   260   N  N   . MET   A  1 36  ? -5.560  -14.214 -21.269  1.00 24.68  ? 337  MET   A N   1 
ATOM   261   C  CA  . MET   A  1 36  ? -4.835  -13.315 -22.148  1.00 22.43  ? 337  MET   A CA  1 
ATOM   262   C  C   . MET   A  1 36  ? -5.781  -12.376 -22.883  1.00 20.12  ? 337  MET   A C   1 
ATOM   263   O  O   . MET   A  1 36  ? -5.464  -11.892 -23.974  1.00 24.01  ? 337  MET   A O   1 
ATOM   264   C  CB  . MET   A  1 36  ? -3.989  -14.120 -23.129  1.00 31.97  ? 337  MET   A CB  1 
ATOM   265   C  CG  . MET   A  1 36  ? -2.887  -14.881 -22.433  1.00 41.02  ? 337  MET   A CG  1 
ATOM   266   S  SD  . MET   A  1 36  ? -1.658  -15.363 -23.635  1.00 54.86  ? 337  MET   A SD  1 
ATOM   267   C  CE  . MET   A  1 36  ? -0.170  -14.867 -22.783  1.00 61.21  ? 337  MET   A CE  1 
ATOM   268   N  N   . GLY   A  1 37  ? -6.940  -12.102 -22.278  1.00 27.50  ? 338  GLY   A N   1 
ATOM   269   C  CA  . GLY   A  1 37  ? -7.987  -11.348 -22.944  1.00 22.63  ? 338  GLY   A CA  1 
ATOM   270   C  C   . GLY   A  1 37  ? -7.592  -9.953  -23.398  1.00 23.60  ? 338  GLY   A C   1 
ATOM   271   O  O   . GLY   A  1 37  ? -8.221  -9.420  -24.311  1.00 23.98  ? 338  GLY   A O   1 
ATOM   272   N  N   . SER   A  1 38  ? -6.576  -9.338  -22.774  1.00 23.71  ? 339  SER   A N   1 
ATOM   273   C  CA  . SER   A  1 38  ? -6.138  -8.010  -23.201  1.00 28.07  ? 339  SER   A CA  1 
ATOM   274   C  C   . SER   A  1 38  ? -4.852  -8.028  -24.023  1.00 29.57  ? 339  SER   A C   1 
ATOM   275   O  O   . SER   A  1 38  ? -4.321  -6.961  -24.345  1.00 27.80  ? 339  SER   A O   1 
ATOM   276   C  CB  . SER   A  1 38  ? -5.973  -7.076  -21.993  1.00 22.83  ? 339  SER   A CB  1 
ATOM   277   O  OG  . SER   A  1 38  ? -4.886  -7.426  -21.150  1.00 24.88  ? 339  SER   A OG  1 
ATOM   278   N  N   . ILE   A  1 39  ? -4.338  -9.207  -24.358  1.00 28.37  ? 340  ILE   A N   1 
ATOM   279   C  CA  . ILE   A  1 39  ? -3.209  -9.322  -25.271  1.00 25.14  ? 340  ILE   A CA  1 
ATOM   280   C  C   . ILE   A  1 39  ? -3.699  -9.084  -26.693  1.00 23.69  ? 340  ILE   A C   1 
ATOM   281   O  O   . ILE   A  1 39  ? -4.707  -9.660  -27.112  1.00 23.86  ? 340  ILE   A O   1 
ATOM   282   C  CB  . ILE   A  1 39  ? -2.554  -10.706 -25.148  1.00 32.49  ? 340  ILE   A CB  1 
ATOM   283   C  CG1 . ILE   A  1 39  ? -2.162  -10.991 -23.697  1.00 36.19  ? 340  ILE   A CG1 1 
ATOM   284   C  CG2 . ILE   A  1 39  ? -1.353  -10.799 -26.073  1.00 33.59  ? 340  ILE   A CG2 1 
ATOM   285   C  CD1 . ILE   A  1 39  ? -0.980  -10.211 -23.240  1.00 39.39  ? 340  ILE   A CD1 1 
ATOM   286   N  N   . MET   A  1 40  ? -2.975  -8.245  -27.441  1.00 22.55  ? 341  MET   A N   1 
ATOM   287   C  CA  . MET   A  1 40  ? -3.407  -7.863  -28.785  1.00 28.43  ? 341  MET   A CA  1 
ATOM   288   C  C   . MET   A  1 40  ? -3.391  -9.057  -29.740  1.00 30.25  ? 341  MET   A C   1 
ATOM   289   O  O   . MET   A  1 40  ? -4.342  -9.265  -30.505  1.00 26.70  ? 341  MET   A O   1 
ATOM   290   C  CB  . MET   A  1 40  ? -2.510  -6.743  -29.306  1.00 36.70  ? 341  MET   A CB  1 
ATOM   291   C  CG  . MET   A  1 40  ? -2.881  -6.239  -30.689  1.00 54.00  ? 341  MET   A CG  1 
ATOM   292   S  SD  . MET   A  1 40  ? -4.112  -4.934  -30.618  1.00 58.08  ? 341  MET   A SD  1 
ATOM   293   C  CE  . MET   A  1 40  ? -3.259  -3.721  -29.592  1.00 35.11  ? 341  MET   A CE  1 
ATOM   294   N  N   . HIS   A  1 41  ? -2.304  -9.836  -29.732  1.00 30.87  ? 342  HIS   A N   1 
ATOM   295   C  CA  A HIS   A  1 41  ? -2.172  -11.055 -30.530  0.47 36.05  ? 342  HIS   A CA  1 
ATOM   296   C  CA  B HIS   A  1 41  ? -2.181  -11.057 -30.532  0.53 36.16  ? 342  HIS   A CA  1 
ATOM   297   C  C   . HIS   A  1 41  ? -1.848  -12.195 -29.571  1.00 32.03  ? 342  HIS   A C   1 
ATOM   298   O  O   . HIS   A  1 41  ? -0.680  -12.585 -29.427  1.00 28.63  ? 342  HIS   A O   1 
ATOM   299   C  CB  A HIS   A  1 41  ? -1.081  -10.933 -31.592  0.47 37.45  ? 342  HIS   A CB  1 
ATOM   300   C  CB  B HIS   A  1 41  ? -1.122  -10.908 -31.628  0.53 37.44  ? 342  HIS   A CB  1 
ATOM   301   C  CG  A HIS   A  1 41  ? -0.893  -9.551  -32.127  0.47 36.28  ? 342  HIS   A CG  1 
ATOM   302   C  CG  B HIS   A  1 41  ? -1.172  -11.979 -32.683  0.53 42.83  ? 342  HIS   A CG  1 
ATOM   303   N  ND1 A HIS   A  1 41  ? -1.755  -8.979  -33.038  0.47 39.14  ? 342  HIS   A ND1 1 
ATOM   304   N  ND1 B HIS   A  1 41  ? -0.041  -12.462 -33.307  0.53 44.03  ? 342  HIS   A ND1 1 
ATOM   305   C  CD2 A HIS   A  1 41  ? 0.080   -8.636  -31.904  0.47 40.26  ? 342  HIS   A CD2 1 
ATOM   306   C  CD2 B HIS   A  1 41  ? -2.216  -12.648 -33.232  0.53 40.10  ? 342  HIS   A CD2 1 
ATOM   307   C  CE1 A HIS   A  1 41  ? -1.328  -7.767  -33.344  0.47 36.87  ? 342  HIS   A CE1 1 
ATOM   308   C  CE1 B HIS   A  1 41  ? -0.384  -13.387 -34.185  0.53 43.92  ? 342  HIS   A CE1 1 
ATOM   309   N  NE2 A HIS   A  1 41  ? -0.217  -7.534  -32.670  0.47 38.26  ? 342  HIS   A NE2 1 
ATOM   310   N  NE2 B HIS   A  1 41  ? -1.698  -13.519 -34.159  0.53 41.05  ? 342  HIS   A NE2 1 
ATOM   311   N  N   . PRO   A  1 42  ? -2.849  -12.745 -28.879  1.00 39.53  ? 343  PRO   A N   1 
ATOM   312   C  CA  . PRO   A  1 42  ? -2.536  -13.725 -27.826  1.00 40.14  ? 343  PRO   A CA  1 
ATOM   313   C  C   . PRO   A  1 42  ? -2.063  -15.067 -28.349  1.00 42.07  ? 343  PRO   A C   1 
ATOM   314   O  O   . PRO   A  1 42  ? -1.403  -15.796 -27.605  1.00 36.63  ? 343  PRO   A O   1 
ATOM   315   C  CB  . PRO   A  1 42  ? -3.862  -13.860 -27.062  1.00 36.14  ? 343  PRO   A CB  1 
ATOM   316   C  CG  . PRO   A  1 42  ? -4.905  -13.501 -28.048  1.00 37.92  ? 343  PRO   A CG  1 
ATOM   317   C  CD  . PRO   A  1 42  ? -4.291  -12.447 -28.954  1.00 38.71  ? 343  PRO   A CD  1 
ATOM   318   N  N   . SER   A  1 43  ? -2.364  -15.422 -29.593  1.00 34.36  ? 344  SER   A N   1 
ATOM   319   C  CA  . SER   A  1 43  ? -2.164  -16.793 -30.025  1.00 42.33  ? 344  SER   A CA  1 
ATOM   320   C  C   . SER   A  1 43  ? -1.602  -16.805 -31.439  1.00 44.28  ? 344  SER   A C   1 
ATOM   321   O  O   . SER   A  1 43  ? -1.952  -15.958 -32.264  1.00 38.66  ? 344  SER   A O   1 
ATOM   322   C  CB  . SER   A  1 43  ? -3.488  -17.579 -29.942  1.00 37.88  ? 344  SER   A CB  1 
ATOM   323   O  OG  . SER   A  1 43  ? -3.355  -18.899 -30.455  1.00 40.01  ? 344  SER   A OG  1 
ATOM   324   N  N   . GLN   A  1 44  ? -0.698  -17.747 -31.699  1.00 45.96  ? 345  GLN   A N   1 
ATOM   325   C  CA  . GLN   A  1 44  ? -0.218  -18.011 -33.048  1.00 51.85  ? 345  GLN   A CA  1 
ATOM   326   C  C   . GLN   A  1 44  ? -0.761  -19.326 -33.590  1.00 54.14  ? 345  GLN   A C   1 
ATOM   327   O  O   . GLN   A  1 44  ? -0.222  -19.865 -34.561  1.00 55.15  ? 345  GLN   A O   1 
ATOM   328   C  CB  . GLN   A  1 44  ? 1.309   -18.012 -33.083  1.00 52.39  ? 345  GLN   A CB  1 
ATOM   329   C  CG  . GLN   A  1 44  ? 1.945   -16.835 -32.375  1.00 60.99  ? 345  GLN   A CG  1 
ATOM   330   C  CD  . GLN   A  1 44  ? 3.440   -17.011 -32.210  1.00 62.89  ? 345  GLN   A CD  1 
ATOM   331   O  OE1 . GLN   A  1 44  ? 4.194   -16.946 -33.184  1.00 60.87  ? 345  GLN   A OE1 1 
ATOM   332   N  NE2 . GLN   A  1 44  ? 3.880   -17.255 -30.973  1.00 60.19  ? 345  GLN   A NE2 1 
ATOM   333   N  N   . HIS   A  1 45  ? -1.813  -19.859 -32.970  1.00 48.31  ? 346  HIS   A N   1 
ATOM   334   C  CA  . HIS   A  1 45  ? -2.426  -21.099 -33.431  1.00 52.55  ? 346  HIS   A CA  1 
ATOM   335   C  C   . HIS   A  1 45  ? -3.071  -20.858 -34.787  1.00 54.76  ? 346  HIS   A C   1 
ATOM   336   O  O   . HIS   A  1 45  ? -4.072  -20.141 -34.883  1.00 57.16  ? 346  HIS   A O   1 
ATOM   337   C  CB  . HIS   A  1 45  ? -3.452  -21.593 -32.416  1.00 53.09  ? 346  HIS   A CB  1 
ATOM   338   C  CG  . HIS   A  1 45  ? -3.902  -23.002 -32.643  1.00 53.81  ? 346  HIS   A CG  1 
ATOM   339   N  ND1 . HIS   A  1 45  ? -5.078  -23.500 -32.124  1.00 52.55  ? 346  HIS   A ND1 1 
ATOM   340   C  CD2 . HIS   A  1 45  ? -3.329  -24.025 -33.324  1.00 52.43  ? 346  HIS   A CD2 1 
ATOM   341   C  CE1 . HIS   A  1 45  ? -5.214  -24.767 -32.479  1.00 53.37  ? 346  HIS   A CE1 1 
ATOM   342   N  NE2 . HIS   A  1 45  ? -4.166  -25.110 -33.207  1.00 48.95  ? 346  HIS   A NE2 1 
ATOM   343   N  N   . ALA   A  1 46  ? -2.484  -21.430 -35.836  1.00 56.11  ? 347  ALA   A N   1 
ATOM   344   C  CA  . ALA   A  1 46  ? -3.026  -21.390 -37.186  1.00 46.91  ? 347  ALA   A CA  1 
ATOM   345   C  C   . ALA   A  1 46  ? -3.560  -22.766 -37.549  1.00 49.11  ? 347  ALA   A C   1 
ATOM   346   O  O   . ALA   A  1 46  ? -3.167  -23.784 -36.973  1.00 53.06  ? 347  ALA   A O   1 
ATOM   347   C  CB  . ALA   A  1 46  ? -1.969  -20.947 -38.205  1.00 41.61  ? 347  ALA   A CB  1 
ATOM   348   N  N   . ARG   A  1 47  ? -4.465  -22.799 -38.518  1.00 56.35  ? 348  ARG   A N   1 
ATOM   349   C  CA  . ARG   A  1 47  ? -5.096  -24.069 -38.842  1.00 60.38  ? 348  ARG   A CA  1 
ATOM   350   C  C   . ARG   A  1 47  ? -4.257  -24.933 -39.780  1.00 54.40  ? 348  ARG   A C   1 
ATOM   351   O  O   . ARG   A  1 47  ? -4.437  -26.155 -39.795  1.00 60.42  ? 348  ARG   A O   1 
ATOM   352   C  CB  . ARG   A  1 47  ? -6.483  -23.803 -39.416  1.00 57.50  ? 348  ARG   A CB  1 
ATOM   353   C  CG  . ARG   A  1 47  ? -7.328  -22.975 -38.474  1.00 57.69  ? 348  ARG   A CG  1 
ATOM   354   C  CD  . ARG   A  1 47  ? -8.767  -23.340 -38.603  1.00 62.01  ? 348  ARG   A CD  1 
ATOM   355   N  NE  . ARG   A  1 47  ? -9.212  -23.144 -39.969  1.00 72.41  ? 348  ARG   A NE  1 
ATOM   356   C  CZ  . ARG   A  1 47  ? -10.270 -23.752 -40.482  1.00 74.78  ? 348  ARG   A CZ  1 
ATOM   357   N  NH1 . ARG   A  1 47  ? -10.964 -24.586 -39.721  1.00 82.15  ? 348  ARG   A NH1 1 
ATOM   358   N  NH2 . ARG   A  1 47  ? -10.626 -23.534 -41.741  1.00 58.30  ? 348  ARG   A NH2 1 
ATOM   359   N  N   . ARG   A  1 48  ? -3.331  -24.341 -40.530  1.00 53.39  ? 349  ARG   A N   1 
ATOM   360   C  CA  . ARG   A  1 48  ? -2.403  -25.067 -41.388  1.00 60.08  ? 349  ARG   A CA  1 
ATOM   361   C  C   . ARG   A  1 48  ? -1.035  -24.406 -41.309  1.00 61.79  ? 349  ARG   A C   1 
ATOM   362   O  O   . ARG   A  1 48  ? -0.945  -23.193 -41.083  1.00 63.98  ? 349  ARG   A O   1 
ATOM   363   C  CB  . ARG   A  1 48  ? -2.890  -25.107 -42.850  1.00 57.84  ? 349  ARG   A CB  1 
ATOM   364   C  CG  . ARG   A  1 48  ? -3.799  -23.945 -43.275  1.00 54.45  ? 349  ARG   A CG  1 
ATOM   365   C  CD  . ARG   A  1 48  ? -3.010  -22.705 -43.644  1.00 55.25  ? 349  ARG   A CD  1 
ATOM   366   N  NE  . ARG   A  1 48  ? -1.803  -23.067 -44.377  1.00 65.71  ? 349  ARG   A NE  1 
ATOM   367   C  CZ  . ARG   A  1 48  ? -1.770  -23.412 -45.662  1.00 69.16  ? 349  ARG   A CZ  1 
ATOM   368   N  NH1 . ARG   A  1 48  ? -2.883  -23.441 -46.386  1.00 64.91  ? 349  ARG   A NH1 1 
ATOM   369   N  NH2 . ARG   A  1 48  ? -0.613  -23.730 -46.227  1.00 75.47  ? 349  ARG   A NH2 1 
ATOM   370   N  N   . PRO   A  1 49  ? 0.044   -25.169 -41.490  1.00 65.66  ? 350  PRO   A N   1 
ATOM   371   C  CA  . PRO   A  1 49  ? 1.389   -24.596 -41.354  1.00 72.29  ? 350  PRO   A CA  1 
ATOM   372   C  C   . PRO   A  1 49  ? 1.620   -23.454 -42.333  1.00 80.44  ? 350  PRO   A C   1 
ATOM   373   O  O   . PRO   A  1 49  ? 0.845   -23.216 -43.262  1.00 81.47  ? 350  PRO   A O   1 
ATOM   374   C  CB  . PRO   A  1 49  ? 2.325   -25.782 -41.630  1.00 71.17  ? 350  PRO   A CB  1 
ATOM   375   C  CG  . PRO   A  1 49  ? 1.481   -26.794 -42.317  1.00 71.93  ? 350  PRO   A CG  1 
ATOM   376   C  CD  . PRO   A  1 49  ? 0.090   -26.609 -41.790  1.00 70.42  ? 350  PRO   A CD  1 
ATOM   377   N  N   . GLU   A  1 50  ? 2.736   -22.750 -42.114  1.00 93.89  ? 351  GLU   A N   1 
ATOM   378   C  CA  . GLU   A  1 50  ? 2.924   -21.419 -42.695  1.00 102.73 ? 351  GLU   A CA  1 
ATOM   379   C  C   . GLU   A  1 50  ? 2.859   -21.432 -44.221  1.00 103.28 ? 351  GLU   A C   1 
ATOM   380   O  O   . GLU   A  1 50  ? 2.254   -20.535 -44.823  1.00 101.86 ? 351  GLU   A O   1 
ATOM   381   C  CB  . GLU   A  1 50  ? 4.249   -20.823 -42.212  1.00 108.69 ? 351  GLU   A CB  1 
ATOM   382   C  CG  . GLU   A  1 50  ? 4.211   -20.342 -40.765  1.00 109.99 ? 351  GLU   A CG  1 
ATOM   383   C  CD  . GLU   A  1 50  ? 5.495   -20.641 -40.015  1.00 112.35 ? 351  GLU   A CD  1 
ATOM   384   O  OE1 . GLU   A  1 50  ? 6.501   -21.005 -40.663  1.00 112.28 ? 351  GLU   A OE1 1 
ATOM   385   O  OE2 . GLU   A  1 50  ? 5.491   -20.519 -38.770  1.00 113.11 ? 351  GLU   A OE2 1 
ATOM   386   N  N   . ASP   A  1 51  ? 3.469   -22.424 -44.868  1.00 103.01 ? 352  ASP   A N   1 
ATOM   387   C  CA  . ASP   A  1 51  ? 3.410   -22.467 -46.326  1.00 100.79 ? 352  ASP   A CA  1 
ATOM   388   C  C   . ASP   A  1 51  ? 2.762   -23.758 -46.813  1.00 95.61  ? 352  ASP   A C   1 
ATOM   389   O  O   . ASP   A  1 51  ? 2.075   -24.443 -46.046  1.00 98.15  ? 352  ASP   A O   1 
ATOM   390   C  CB  . ASP   A  1 51  ? 4.805   -22.293 -46.919  1.00 103.26 ? 352  ASP   A CB  1 
ATOM   391   C  CG  . ASP   A  1 51  ? 5.674   -23.505 -46.722  1.00 108.05 ? 352  ASP   A CG  1 
ATOM   392   O  OD1 . ASP   A  1 51  ? 5.566   -24.155 -45.659  1.00 108.86 ? 352  ASP   A OD1 1 
ATOM   393   O  OD2 . ASP   A  1 51  ? 6.448   -23.819 -47.646  1.00 110.11 ? 352  ASP   A OD2 1 
ATOM   394   N  N   . VAL   A  1 52  ? 3.014   -24.108 -48.081  1.00 86.78  ? 353  VAL   A N   1 
ATOM   395   C  CA  . VAL   A  1 52  ? 2.204   -25.063 -48.836  1.00 77.70  ? 353  VAL   A CA  1 
ATOM   396   C  C   . VAL   A  1 52  ? 1.965   -26.351 -48.053  1.00 70.17  ? 353  VAL   A C   1 
ATOM   397   O  O   . VAL   A  1 52  ? 2.862   -27.188 -47.887  1.00 62.04  ? 353  VAL   A O   1 
ATOM   398   C  CB  . VAL   A  1 52  ? 2.822   -25.347 -50.224  1.00 69.47  ? 353  VAL   A CB  1 
ATOM   399   C  CG1 . VAL   A  1 52  ? 4.315   -25.581 -50.130  1.00 74.19  ? 353  VAL   A CG1 1 
ATOM   400   C  CG2 . VAL   A  1 52  ? 2.116   -26.528 -50.917  1.00 66.36  ? 353  VAL   A CG2 1 
ATOM   401   N  N   . ALA   A  1 53  ? 0.742   -26.493 -47.551  1.00 64.38  ? 354  ALA   A N   1 
ATOM   402   C  CA  . ALA   A  1 53  ? 0.370   -27.643 -46.754  1.00 52.77  ? 354  ALA   A CA  1 
ATOM   403   C  C   . ALA   A  1 53  ? 0.369   -28.901 -47.607  1.00 51.62  ? 354  ALA   A C   1 
ATOM   404   O  O   . ALA   A  1 53  ? 0.100   -28.867 -48.812  1.00 49.92  ? 354  ALA   A O   1 
ATOM   405   C  CB  . ALA   A  1 53  ? -1.011  -27.430 -46.129  1.00 50.25  ? 354  ALA   A CB  1 
ATOM   406   N  N   . THR   A  1 54  ? 0.708   -30.018 -46.975  1.00 47.66  ? 355  THR   A N   1 
ATOM   407   C  CA  . THR   A  1 54  ? 0.456   -31.306 -47.588  1.00 46.55  ? 355  THR   A CA  1 
ATOM   408   C  C   . THR   A  1 54  ? -1.047  -31.559 -47.646  1.00 42.19  ? 355  THR   A C   1 
ATOM   409   O  O   . THR   A  1 54  ? -1.856  -30.842 -47.045  1.00 39.91  ? 355  THR   A O   1 
ATOM   410   C  CB  . THR   A  1 54  ? 1.136   -32.422 -46.800  1.00 48.12  ? 355  THR   A CB  1 
ATOM   411   O  OG1 . THR   A  1 54  ? 0.726   -32.338 -45.431  1.00 48.30  ? 355  THR   A OG1 1 
ATOM   412   C  CG2 . THR   A  1 54  ? 2.641   -32.293 -46.885  1.00 45.10  ? 355  THR   A CG2 1 
ATOM   413   N  N   . LYS   A  1 55  ? -1.412  -32.624 -48.355  1.00 40.18  ? 356  LYS   A N   1 
ATOM   414   C  CA  . LYS   A  1 55  ? -2.822  -32.940 -48.560  1.00 44.97  ? 356  LYS   A CA  1 
ATOM   415   C  C   . LYS   A  1 55  ? -3.539  -33.196 -47.236  1.00 34.11  ? 356  LYS   A C   1 
ATOM   416   O  O   . LYS   A  1 55  ? -4.617  -32.646 -46.990  1.00 33.41  ? 356  LYS   A O   1 
ATOM   417   C  CB  . LYS   A  1 55  ? -2.947  -34.146 -49.489  1.00 49.30  ? 356  LYS   A CB  1 
ATOM   418   C  CG  . LYS   A  1 55  ? -4.365  -34.491 -49.850  1.00 49.34  ? 356  LYS   A CG  1 
ATOM   419   C  CD  . LYS   A  1 55  ? -4.420  -35.660 -50.812  1.00 61.82  ? 356  LYS   A CD  1 
ATOM   420   C  CE  . LYS   A  1 55  ? -5.818  -35.788 -51.357  1.00 67.09  ? 356  LYS   A CE  1 
ATOM   421   N  NZ  . LYS   A  1 55  ? -6.812  -35.372 -50.328  1.00 72.02  ? 356  LYS   A NZ  1 
ATOM   422   N  N   . ASP   A  1 56  ? -2.964  -34.037 -46.373  1.00 37.18  ? 357  ASP   A N   1 
ATOM   423   C  CA  . ASP   A  1 56  ? -3.611  -34.318 -45.094  1.00 41.55  ? 357  ASP   A CA  1 
ATOM   424   C  C   . ASP   A  1 56  ? -3.638  -33.111 -44.171  1.00 41.34  ? 357  ASP   A C   1 
ATOM   425   O  O   . ASP   A  1 56  ? -4.302  -33.168 -43.130  1.00 44.86  ? 357  ASP   A O   1 
ATOM   426   C  CB  . ASP   A  1 56  ? -2.939  -35.498 -44.380  1.00 51.29  ? 357  ASP   A CB  1 
ATOM   427   C  CG  . ASP   A  1 56  ? -1.440  -35.317 -44.210  1.00 65.08  ? 357  ASP   A CG  1 
ATOM   428   O  OD1 . ASP   A  1 56  ? -0.878  -35.892 -43.254  1.00 73.92  ? 357  ASP   A OD1 1 
ATOM   429   O  OD2 . ASP   A  1 56  ? -0.821  -34.608 -45.028  1.00 74.19  ? 357  ASP   A OD2 1 
ATOM   430   N  N   . GLN   A  1 57  ? -2.951  -32.024 -44.523  1.00 34.52  ? 358  GLN   A N   1 
ATOM   431   C  CA  . GLN   A  1 57  ? -3.050  -30.803 -43.736  1.00 39.63  ? 358  GLN   A CA  1 
ATOM   432   C  C   . GLN   A  1 57  ? -4.140  -29.882 -44.257  1.00 40.24  ? 358  GLN   A C   1 
ATOM   433   O  O   . GLN   A  1 57  ? -4.844  -29.240 -43.470  1.00 37.41  ? 358  GLN   A O   1 
ATOM   434   C  CB  . GLN   A  1 57  ? -1.707  -30.069 -43.723  1.00 41.38  ? 358  GLN   A CB  1 
ATOM   435   C  CG  . GLN   A  1 57  ? -0.670  -30.727 -42.821  1.00 52.30  ? 358  GLN   A CG  1 
ATOM   436   C  CD  . GLN   A  1 57  ? 0.745   -30.286 -43.136  1.00 54.08  ? 358  GLN   A CD  1 
ATOM   437   O  OE1 . GLN   A  1 57  ? 0.975   -29.485 -44.045  1.00 53.91  ? 358  GLN   A OE1 1 
ATOM   438   N  NE2 . GLN   A  1 57  ? 1.702   -30.817 -42.390  1.00 53.24  ? 358  GLN   A NE2 1 
ATOM   439   N  N   . LEU   A  1 58  ? -4.298  -29.809 -45.570  1.00 40.02  ? 359  LEU   A N   1 
ATOM   440   C  CA  . LEU   A  1 58  ? -5.262  -28.880 -46.136  1.00 37.77  ? 359  LEU   A CA  1 
ATOM   441   C  C   . LEU   A  1 58  ? -6.639  -29.507 -46.306  1.00 33.27  ? 359  LEU   A C   1 
ATOM   442   O  O   . LEU   A  1 58  ? -7.644  -28.871 -45.981  1.00 30.45  ? 359  LEU   A O   1 
ATOM   443   C  CB  . LEU   A  1 58  ? -4.758  -28.353 -47.485  1.00 33.96  ? 359  LEU   A CB  1 
ATOM   444   C  CG  . LEU   A  1 58  ? -5.645  -27.314 -48.172  1.00 39.09  ? 359  LEU   A CG  1 
ATOM   445   C  CD1 . LEU   A  1 58  ? -5.841  -26.100 -47.263  1.00 35.56  ? 359  LEU   A CD1 1 
ATOM   446   C  CD2 . LEU   A  1 58  ? -5.099  -26.901 -49.561  1.00 34.44  ? 359  LEU   A CD2 1 
ATOM   447   N  N   . PHE   A  1 59  ? -6.715  -30.738 -46.811  1.00 35.31  ? 360  PHE   A N   1 
ATOM   448   C  CA  . PHE   A  1 59  ? -8.035  -31.302 -47.086  1.00 37.45  ? 360  PHE   A CA  1 
ATOM   449   C  C   . PHE   A  1 59  ? -8.957  -31.294 -45.872  1.00 34.56  ? 360  PHE   A C   1 
ATOM   450   O  O   . PHE   A  1 59  ? -10.128 -30.902 -46.025  1.00 36.63  ? 360  PHE   A O   1 
ATOM   451   C  CB  . PHE   A  1 59  ? -7.931  -32.719 -47.654  1.00 34.48  ? 360  PHE   A CB  1 
ATOM   452   C  CG  . PHE   A  1 59  ? -9.265  -33.275 -48.041  1.00 41.32  ? 360  PHE   A CG  1 
ATOM   453   C  CD1 . PHE   A  1 59  ? -9.858  -32.893 -49.242  1.00 44.05  ? 360  PHE   A CD1 1 
ATOM   454   C  CD2 . PHE   A  1 59  ? -9.960  -34.121 -47.189  1.00 37.28  ? 360  PHE   A CD2 1 
ATOM   455   C  CE1 . PHE   A  1 59  ? -11.097 -33.372 -49.597  1.00 48.48  ? 360  PHE   A CE1 1 
ATOM   456   C  CE2 . PHE   A  1 59  ? -11.200 -34.601 -47.534  1.00 42.17  ? 360  PHE   A CE2 1 
ATOM   457   C  CZ  . PHE   A  1 59  ? -11.773 -34.230 -48.741  1.00 52.98  ? 360  PHE   A CZ  1 
ATOM   458   N  N   . PRO   A  1 60  ? -8.530  -31.706 -44.666  1.00 38.50  ? 361  PRO   A N   1 
ATOM   459   C  CA  . PRO   A  1 60  ? -9.451  -31.629 -43.516  1.00 30.74  ? 361  PRO   A CA  1 
ATOM   460   C  C   . PRO   A  1 60  ? -10.037 -30.247 -43.301  1.00 32.10  ? 361  PRO   A C   1 
ATOM   461   O  O   . PRO   A  1 60  ? -11.217 -30.128 -42.945  1.00 34.76  ? 361  PRO   A O   1 
ATOM   462   C  CB  . PRO   A  1 60  ? -8.571  -32.064 -42.335  1.00 36.06  ? 361  PRO   A CB  1 
ATOM   463   C  CG  . PRO   A  1 60  ? -7.521  -32.927 -42.954  1.00 39.82  ? 361  PRO   A CG  1 
ATOM   464   C  CD  . PRO   A  1 60  ? -7.230  -32.287 -44.278  1.00 41.29  ? 361  PRO   A CD  1 
ATOM   465   N  N   . LEU   A  1 61  ? -9.252  -29.190 -43.526  1.00 32.29  ? 362  LEU   A N   1 
ATOM   466   C  CA  . LEU   A  1 61  ? -9.783  -27.840 -43.361  1.00 34.54  ? 362  LEU   A CA  1 
ATOM   467   C  C   . LEU   A  1 61  ? -10.788 -27.513 -44.452  1.00 40.08  ? 362  LEU   A C   1 
ATOM   468   O  O   . LEU   A  1 61  ? -11.817 -26.879 -44.185  1.00 34.08  ? 362  LEU   A O   1 
ATOM   469   C  CB  . LEU   A  1 61  ? -8.649  -26.821 -43.368  1.00 29.65  ? 362  LEU   A CB  1 
ATOM   470   C  CG  . LEU   A  1 61  ? -7.617  -27.072 -42.272  1.00 37.01  ? 362  LEU   A CG  1 
ATOM   471   C  CD1 . LEU   A  1 61  ? -6.436  -26.148 -42.435  1.00 31.71  ? 362  LEU   A CD1 1 
ATOM   472   C  CD2 . LEU   A  1 61  ? -8.250  -26.888 -40.896  1.00 37.85  ? 362  LEU   A CD2 1 
ATOM   473   N  N   . ALA   A  1 62  ? -10.498 -27.935 -45.687  1.00 35.53  ? 363  ALA   A N   1 
ATOM   474   C  CA  . ALA   A  1 62  ? -11.418 -27.696 -46.794  1.00 37.65  ? 363  ALA   A CA  1 
ATOM   475   C  C   . ALA   A  1 62  ? -12.724 -28.439 -46.574  1.00 39.07  ? 363  ALA   A C   1 
ATOM   476   O  O   . ALA   A  1 62  ? -13.813 -27.869 -46.721  1.00 31.42  ? 363  ALA   A O   1 
ATOM   477   C  CB  . ALA   A  1 62  ? -10.771 -28.135 -48.109  1.00 32.73  ? 363  ALA   A CB  1 
ATOM   478   N  N   . LYS   A  1 63  ? -12.624 -29.726 -46.232  1.00 35.00  ? 364  LYS   A N   1 
ATOM   479   C  CA  . LYS   A  1 63  ? -13.804 -30.527 -45.937  1.00 37.60  ? 364  LYS   A CA  1 
ATOM   480   C  C   . LYS   A  1 63  ? -14.658 -29.850 -44.879  1.00 40.11  ? 364  LYS   A C   1 
ATOM   481   O  O   . LYS   A  1 63  ? -15.872 -29.693 -45.050  1.00 41.31  ? 364  LYS   A O   1 
ATOM   482   C  CB  . LYS   A  1 63  ? -13.382 -31.921 -45.474  1.00 40.08  ? 364  LYS   A CB  1 
ATOM   483   C  CG  . LYS   A  1 63  ? -14.547 -32.893 -45.317  1.00 54.51  ? 364  LYS   A CG  1 
ATOM   484   C  CD  . LYS   A  1 63  ? -14.114 -34.207 -44.679  1.00 59.63  ? 364  LYS   A CD  1 
ATOM   485   C  CE  . LYS   A  1 63  ? -15.297 -35.143 -44.480  1.00 56.87  ? 364  LYS   A CE  1 
ATOM   486   N  NZ  . LYS   A  1 63  ? -16.414 -34.465 -43.769  1.00 50.95  ? 364  LYS   A NZ  1 
ATOM   487   N  N   . GLU   A  1 64  ? -14.018 -29.416 -43.789  1.00 37.96  ? 365  GLU   A N   1 
ATOM   488   C  CA  . GLU   A  1 64  ? -14.721 -28.728 -42.714  1.00 42.10  ? 365  GLU   A CA  1 
ATOM   489   C  C   . GLU   A  1 64  ? -15.496 -27.529 -43.247  1.00 35.95  ? 365  GLU   A C   1 
ATOM   490   O  O   . GLU   A  1 64  ? -16.685 -27.352 -42.950  1.00 34.04  ? 365  GLU   A O   1 
ATOM   491   C  CB  . GLU   A  1 64  ? -13.713 -28.299 -41.637  1.00 44.57  ? 365  GLU   A CB  1 
ATOM   492   C  CG  . GLU   A  1 64  ? -14.256 -27.353 -40.575  1.00 61.86  ? 365  GLU   A CG  1 
ATOM   493   C  CD  . GLU   A  1 64  ? -13.157 -26.785 -39.682  1.00 79.74  ? 365  GLU   A CD  1 
ATOM   494   O  OE1 . GLU   A  1 64  ? -13.297 -26.826 -38.438  1.00 82.95  ? 365  GLU   A OE1 1 
ATOM   495   O  OE2 . GLU   A  1 64  ? -12.144 -26.303 -40.233  1.00 83.02  ? 365  GLU   A OE2 1 
ATOM   496   N  N   . PHE   A  1 65  ? -14.837 -26.688 -44.037  1.00 28.09  ? 366  PHE   A N   1 
ATOM   497   C  CA  . PHE   A  1 65  ? -15.524 -25.512 -44.554  1.00 30.38  ? 366  PHE   A CA  1 
ATOM   498   C  C   . PHE   A  1 65  ? -16.633 -25.891 -45.528  1.00 33.40  ? 366  PHE   A C   1 
ATOM   499   O  O   . PHE   A  1 65  ? -17.739 -25.339 -45.467  1.00 31.46  ? 366  PHE   A O   1 
ATOM   500   C  CB  . PHE   A  1 65  ? -14.546 -24.569 -45.236  1.00 32.15  ? 366  PHE   A CB  1 
ATOM   501   C  CG  . PHE   A  1 65  ? -15.231 -23.486 -45.986  1.00 37.66  ? 366  PHE   A CG  1 
ATOM   502   C  CD1 . PHE   A  1 65  ? -15.833 -22.433 -45.299  1.00 33.60  ? 366  PHE   A CD1 1 
ATOM   503   C  CD2 . PHE   A  1 65  ? -15.333 -23.539 -47.368  1.00 33.76  ? 366  PHE   A CD2 1 
ATOM   504   C  CE1 . PHE   A  1 65  ? -16.503 -21.434 -45.987  1.00 35.99  ? 366  PHE   A CE1 1 
ATOM   505   C  CE2 . PHE   A  1 65  ? -15.990 -22.539 -48.060  1.00 37.76  ? 366  PHE   A CE2 1 
ATOM   506   C  CZ  . PHE   A  1 65  ? -16.578 -21.486 -47.375  1.00 32.62  ? 366  PHE   A CZ  1 
ATOM   507   N  N   . ILE   A  1 66  ? -16.350 -26.803 -46.459  1.00 33.41  ? 367  ILE   A N   1 
ATOM   508   C  CA  . ILE   A  1 66  ? -17.383 -27.190 -47.416  1.00 40.75  ? 367  ILE   A CA  1 
ATOM   509   C  C   . ILE   A  1 66  ? -18.562 -27.799 -46.669  1.00 37.44  ? 367  ILE   A C   1 
ATOM   510   O  O   . ILE   A  1 66  ? -19.722 -27.435 -46.897  1.00 34.72  ? 367  ILE   A O   1 
ATOM   511   C  CB  . ILE   A  1 66  ? -16.819 -28.155 -48.477  1.00 38.10  ? 367  ILE   A CB  1 
ATOM   512   C  CG1 . ILE   A  1 66  ? -15.626 -27.543 -49.227  1.00 37.78  ? 367  ILE   A CG1 1 
ATOM   513   C  CG2 . ILE   A  1 66  ? -17.912 -28.569 -49.443  1.00 37.74  ? 367  ILE   A CG2 1 
ATOM   514   C  CD1 . ILE   A  1 66  ? -15.946 -26.287 -50.016  1.00 40.19  ? 367  ILE   A CD1 1 
ATOM   515   N  N   . ASP   A  1 67  ? -18.269 -28.717 -45.739  1.00 37.72  ? 368  ASP   A N   1 
ATOM   516   C  CA  . ASP   A  1 67  ? -19.290 -29.256 -44.841  1.00 41.93  ? 368  ASP   A CA  1 
ATOM   517   C  C   . ASP   A  1 67  ? -20.123 -28.144 -44.223  1.00 37.70  ? 368  ASP   A C   1 
ATOM   518   O  O   . ASP   A  1 67  ? -21.357 -28.180 -44.263  1.00 36.93  ? 368  ASP   A O   1 
ATOM   519   C  CB  . ASP   A  1 67  ? -18.638 -30.088 -43.732  1.00 44.73  ? 368  ASP   A CB  1 
ATOM   520   C  CG  . ASP   A  1 67  ? -18.202 -31.453 -44.204  1.00 48.84  ? 368  ASP   A CG  1 
ATOM   521   O  OD1 . ASP   A  1 67  ? -18.421 -31.779 -45.388  1.00 47.82  ? 368  ASP   A OD1 1 
ATOM   522   O  OD2 . ASP   A  1 67  ? -17.636 -32.200 -43.385  1.00 49.44  ? 368  ASP   A OD2 1 
ATOM   523   N  N   . GLN   A  1 68  ? -19.451 -27.142 -43.647  1.00 33.77  ? 369  GLN   A N   1 
ATOM   524   C  CA  . GLN   A  1 68  ? -20.146 -26.031 -43.017  1.00 31.15  ? 369  GLN   A CA  1 
ATOM   525   C  C   . GLN   A  1 68  ? -20.987 -25.264 -44.027  1.00 37.25  ? 369  GLN   A C   1 
ATOM   526   O  O   . GLN   A  1 68  ? -22.158 -24.957 -43.772  1.00 39.75  ? 369  GLN   A O   1 
ATOM   527   C  CB  . GLN   A  1 68  ? -19.130 -25.107 -42.353  1.00 32.97  ? 369  GLN   A CB  1 
ATOM   528   C  CG  . GLN   A  1 68  ? -19.746 -23.895 -41.689  1.00 42.88  ? 369  GLN   A CG  1 
ATOM   529   C  CD  . GLN   A  1 68  ? -18.706 -22.850 -41.303  1.00 53.50  ? 369  GLN   A CD  1 
ATOM   530   O  OE1 . GLN   A  1 68  ? -18.910 -21.650 -41.505  1.00 52.38  ? 369  GLN   A OE1 1 
ATOM   531   N  NE2 . GLN   A  1 68  ? -17.587 -23.303 -40.742  1.00 56.44  ? 369  GLN   A NE2 1 
ATOM   532   N  N   . TYR   A  1 69  ? -20.401 -24.937 -45.184  1.00 33.55  ? 370  TYR   A N   1 
ATOM   533   C  CA  . TYR   A  1 69  ? -21.162 -24.258 -46.229  1.00 38.74  ? 370  TYR   A CA  1 
ATOM   534   C  C   . TYR   A  1 69  ? -22.373 -25.080 -46.651  1.00 35.16  ? 370  TYR   A C   1 
ATOM   535   O  O   . TYR   A  1 69  ? -23.486 -24.554 -46.771  1.00 35.19  ? 370  TYR   A O   1 
ATOM   536   C  CB  . TYR   A  1 69  ? -20.287 -23.977 -47.451  1.00 40.47  ? 370  TYR   A CB  1 
ATOM   537   C  CG  . TYR   A  1 69  ? -21.113 -23.466 -48.605  1.00 35.34  ? 370  TYR   A CG  1 
ATOM   538   C  CD1 . TYR   A  1 69  ? -21.653 -22.189 -48.570  1.00 33.40  ? 370  TYR   A CD1 1 
ATOM   539   C  CD2 . TYR   A  1 69  ? -21.390 -24.270 -49.706  1.00 37.27  ? 370  TYR   A CD2 1 
ATOM   540   C  CE1 . TYR   A  1 69  ? -22.428 -21.716 -49.603  1.00 35.89  ? 370  TYR   A CE1 1 
ATOM   541   C  CE2 . TYR   A  1 69  ? -22.163 -23.801 -50.753  1.00 40.21  ? 370  TYR   A CE2 1 
ATOM   542   C  CZ  . TYR   A  1 69  ? -22.675 -22.523 -50.694  1.00 40.17  ? 370  TYR   A CZ  1 
ATOM   543   O  OH  . TYR   A  1 69  ? -23.451 -22.046 -51.717  1.00 40.00  ? 370  TYR   A OH  1 
ATOM   544   N  N   . TYR   A  1 70  ? -22.180 -26.374 -46.900  1.00 29.25  ? 371  TYR   A N   1 
ATOM   545   C  CA  . TYR   A  1 70  ? -23.321 -27.129 -47.390  1.00 35.34  ? 371  TYR   A CA  1 
ATOM   546   C  C   . TYR   A  1 70  ? -24.342 -27.366 -46.293  1.00 35.63  ? 371  TYR   A C   1 
ATOM   547   O  O   . TYR   A  1 70  ? -25.537 -27.463 -46.586  1.00 41.91  ? 371  TYR   A O   1 
ATOM   548   C  CB  . TYR   A  1 70  ? -22.870 -28.431 -48.047  1.00 40.00  ? 371  TYR   A CB  1 
ATOM   549   C  CG  . TYR   A  1 70  ? -22.600 -28.181 -49.512  1.00 39.30  ? 371  TYR   A CG  1 
ATOM   550   C  CD1 . TYR   A  1 70  ? -21.328 -27.857 -49.954  1.00 34.77  ? 371  TYR   A CD1 1 
ATOM   551   C  CD2 . TYR   A  1 70  ? -23.637 -28.189 -50.439  1.00 37.03  ? 371  TYR   A CD2 1 
ATOM   552   C  CE1 . TYR   A  1 70  ? -21.084 -27.593 -51.302  1.00 35.80  ? 371  TYR   A CE1 1 
ATOM   553   C  CE2 . TYR   A  1 70  ? -23.403 -27.917 -51.792  1.00 35.71  ? 371  TYR   A CE2 1 
ATOM   554   C  CZ  . TYR   A  1 70  ? -22.125 -27.624 -52.211  1.00 35.66  ? 371  TYR   A CZ  1 
ATOM   555   O  OH  . TYR   A  1 70  ? -21.883 -27.357 -53.536  1.00 36.64  ? 371  TYR   A OH  1 
ATOM   556   N  N   . SER   A  1 71  ? -23.898 -27.434 -45.033  1.00 39.79  ? 372  SER   A N   1 
ATOM   557   C  CA  . SER   A  1 71  ? -24.838 -27.428 -43.914  1.00 46.46  ? 372  SER   A CA  1 
ATOM   558   C  C   . SER   A  1 71  ? -25.623 -26.127 -43.871  1.00 41.76  ? 372  SER   A C   1 
ATOM   559   O  O   . SER   A  1 71  ? -26.837 -26.132 -43.639  1.00 43.29  ? 372  SER   A O   1 
ATOM   560   C  CB  . SER   A  1 71  ? -24.098 -27.629 -42.587  1.00 50.14  ? 372  SER   A CB  1 
ATOM   561   O  OG  . SER   A  1 71  ? -23.486 -28.906 -42.516  1.00 56.98  ? 372  SER   A OG  1 
ATOM   562   N  N   . SER   A  1 72  ? -24.944 -25.000 -44.106  1.00 39.58  ? 373  SER   A N   1 
ATOM   563   C  CA  . SER   A  1 72  ? -25.599 -23.702 -44.010  1.00 39.27  ? 373  SER   A CA  1 
ATOM   564   C  C   . SER   A  1 72  ? -26.749 -23.565 -45.000  1.00 44.99  ? 373  SER   A C   1 
ATOM   565   O  O   . SER   A  1 72  ? -27.703 -22.826 -44.730  1.00 44.55  ? 373  SER   A O   1 
ATOM   566   C  CB  . SER   A  1 72  ? -24.581 -22.582 -44.220  1.00 36.85  ? 373  SER   A CB  1 
ATOM   567   O  OG  . SER   A  1 72  ? -24.314 -22.374 -45.596  1.00 42.91  ? 373  SER   A OG  1 
ATOM   568   N  N   . ILE   A  1 73  ? -26.693 -24.259 -46.139  1.00 39.39  ? 374  ILE   A N   1 
ATOM   569   C  CA  . ILE   A  1 73  ? -27.767 -24.187 -47.124  1.00 38.98  ? 374  ILE   A CA  1 
ATOM   570   C  C   . ILE   A  1 73  ? -28.627 -25.454 -47.112  1.00 37.23  ? 374  ILE   A C   1 
ATOM   571   O  O   . ILE   A  1 73  ? -29.328 -25.729 -48.078  1.00 43.70  ? 374  ILE   A O   1 
ATOM   572   C  CB  . ILE   A  1 73  ? -27.231 -23.880 -48.540  1.00 42.53  ? 374  ILE   A CB  1 
ATOM   573   C  CG1 . ILE   A  1 73  ? -26.354 -25.024 -49.068  1.00 36.02  ? 374  ILE   A CG1 1 
ATOM   574   C  CG2 . ILE   A  1 73  ? -26.444 -22.568 -48.542  1.00 43.26  ? 374  ILE   A CG2 1 
ATOM   575   C  CD1 . ILE   A  1 73  ? -25.981 -24.904 -50.538  1.00 36.03  ? 374  ILE   A CD1 1 
ATOM   576   N  N   . LYS   A  1 74  ? -28.611 -26.212 -46.017  1.00 41.08  ? 375  LYS   A N   1 
ATOM   577   C  CA  . LYS   A  1 74  ? -29.509 -27.362 -45.835  1.00 49.48  ? 375  LYS   A CA  1 
ATOM   578   C  C   . LYS   A  1 74  ? -29.274 -28.417 -46.915  1.00 46.49  ? 375  LYS   A C   1 
ATOM   579   O  O   . LYS   A  1 74  ? -30.206 -29.060 -47.404  1.00 47.48  ? 375  LYS   A O   1 
ATOM   580   C  CB  . LYS   A  1 74  ? -30.982 -26.929 -45.812  1.00 51.43  ? 375  LYS   A CB  1 
ATOM   581   C  CG  . LYS   A  1 74  ? -31.279 -25.677 -44.984  1.00 49.23  ? 375  LYS   A CG  1 
ATOM   582   C  CD  . LYS   A  1 74  ? -31.184 -25.953 -43.482  1.00 57.39  ? 375  LYS   A CD  1 
ATOM   583   C  CE  . LYS   A  1 74  ? -31.124 -24.657 -42.666  1.00 53.78  ? 375  LYS   A CE  1 
ATOM   584   N  NZ  . LYS   A  1 74  ? -30.247 -24.803 -41.462  1.00 42.31  ? 375  LYS   A NZ  1 
ATOM   585   N  N   . ARG   A  1 75  ? -28.010 -28.594 -47.290  1.00 42.22  ? 376  ARG   A N   1 
ATOM   586   C  CA  . ARG   A  1 75  ? -27.632 -29.513 -48.356  1.00 43.89  ? 376  ARG   A CA  1 
ATOM   587   C  C   . ARG   A  1 75  ? -26.513 -30.441 -47.906  1.00 46.86  ? 376  ARG   A C   1 
ATOM   588   O  O   . ARG   A  1 75  ? -25.696 -30.879 -48.725  1.00 38.16  ? 376  ARG   A O   1 
ATOM   589   C  CB  . ARG   A  1 75  ? -27.220 -28.746 -49.611  1.00 42.79  ? 376  ARG   A CB  1 
ATOM   590   C  CG  . ARG   A  1 75  ? -28.348 -27.994 -50.271  1.00 46.72  ? 376  ARG   A CG  1 
ATOM   591   C  CD  . ARG   A  1 75  ? -29.351 -28.952 -50.896  1.00 63.30  ? 376  ARG   A CD  1 
ATOM   592   N  NE  . ARG   A  1 75  ? -30.449 -28.226 -51.525  1.00 75.74  ? 376  ARG   A NE  1 
ATOM   593   C  CZ  . ARG   A  1 75  ? -31.520 -27.793 -50.868  1.00 80.83  ? 376  ARG   A CZ  1 
ATOM   594   N  NH1 . ARG   A  1 75  ? -32.476 -27.131 -51.507  1.00 74.75  ? 376  ARG   A NH1 1 
ATOM   595   N  NH2 . ARG   A  1 75  ? -31.634 -28.022 -49.563  1.00 86.41  ? 376  ARG   A NH2 1 
ATOM   596   N  N   . PHE   A  1 76  ? -26.448 -30.739 -46.608  1.00 44.08  ? 377  PHE   A N   1 
ATOM   597   C  CA  . PHE   A  1 76  ? -25.395 -31.613 -46.116  1.00 50.95  ? 377  PHE   A CA  1 
ATOM   598   C  C   . PHE   A  1 76  ? -25.578 -33.015 -46.687  1.00 52.25  ? 377  PHE   A C   1 
ATOM   599   O  O   . PHE   A  1 76  ? -26.655 -33.608 -46.584  1.00 51.45  ? 377  PHE   A O   1 
ATOM   600   C  CB  . PHE   A  1 76  ? -25.375 -31.658 -44.584  1.00 54.50  ? 377  PHE   A CB  1 
ATOM   601   C  CG  . PHE   A  1 76  ? -24.237 -32.467 -44.036  1.00 60.47  ? 377  PHE   A CG  1 
ATOM   602   C  CD1 . PHE   A  1 76  ? -23.032 -31.864 -43.717  1.00 63.44  ? 377  PHE   A CD1 1 
ATOM   603   C  CD2 . PHE   A  1 76  ? -24.354 -33.841 -43.890  1.00 62.63  ? 377  PHE   A CD2 1 
ATOM   604   C  CE1 . PHE   A  1 76  ? -21.976 -32.614 -43.243  1.00 61.29  ? 377  PHE   A CE1 1 
ATOM   605   C  CE2 . PHE   A  1 76  ? -23.303 -34.596 -43.422  1.00 62.87  ? 377  PHE   A CE2 1 
ATOM   606   C  CZ  . PHE   A  1 76  ? -22.116 -33.984 -43.098  1.00 62.67  ? 377  PHE   A CZ  1 
ATOM   607   N  N   . GLY   A  1 77  ? -24.514 -33.545 -47.289  1.00 51.30  ? 378  GLY   A N   1 
ATOM   608   C  CA  . GLY   A  1 77  ? -24.540 -34.854 -47.896  1.00 49.78  ? 378  GLY   A CA  1 
ATOM   609   C  C   . GLY   A  1 77  ? -25.205 -34.902 -49.250  1.00 48.73  ? 378  GLY   A C   1 
ATOM   610   O  O   . GLY   A  1 77  ? -25.265 -35.980 -49.854  1.00 49.61  ? 378  GLY   A O   1 
ATOM   611   N  N   . SER   A  1 78  ? -25.706 -33.771 -49.739  1.00 43.33  ? 379  SER   A N   1 
ATOM   612   C  CA  . SER   A  1 78  ? -26.356 -33.702 -51.031  1.00 38.07  ? 379  SER   A CA  1 
ATOM   613   C  C   . SER   A  1 78  ? -25.394 -34.123 -52.131  1.00 49.52  ? 379  SER   A C   1 
ATOM   614   O  O   . SER   A  1 78  ? -24.179 -34.218 -51.942  1.00 46.98  ? 379  SER   A O   1 
ATOM   615   C  CB  . SER   A  1 78  ? -26.845 -32.284 -51.306  1.00 42.45  ? 379  SER   A CB  1 
ATOM   616   O  OG  . SER   A  1 78  ? -25.742 -31.391 -51.381  1.00 39.67  ? 379  SER   A OG  1 
ATOM   617   N  N   . LYS   A  1 79  ? -25.965 -34.354 -53.309  1.00 39.29  ? 380  LYS   A N   1 
ATOM   618   C  CA  . LYS   A  1 79  ? -25.149 -34.645 -54.472  1.00 49.20  ? 380  LYS   A CA  1 
ATOM   619   C  C   . LYS   A  1 79  ? -24.082 -33.571 -54.669  1.00 44.07  ? 380  LYS   A C   1 
ATOM   620   O  O   . LYS   A  1 79  ? -22.888 -33.877 -54.744  1.00 48.44  ? 380  LYS   A O   1 
ATOM   621   C  CB  . LYS   A  1 79  ? -26.052 -34.785 -55.700  1.00 51.89  ? 380  LYS   A CB  1 
ATOM   622   C  CG  . LYS   A  1 79  ? -25.360 -35.354 -56.910  1.00 54.24  ? 380  LYS   A CG  1 
ATOM   623   C  CD  . LYS   A  1 79  ? -26.354 -35.580 -58.031  1.00 60.88  ? 380  LYS   A CD  1 
ATOM   624   C  CE  . LYS   A  1 79  ? -27.502 -36.456 -57.557  1.00 62.40  ? 380  LYS   A CE  1 
ATOM   625   N  NZ  . LYS   A  1 79  ? -27.062 -37.854 -57.290  1.00 58.68  ? 380  LYS   A NZ  1 
ATOM   626   N  N   . ALA   A  1 80  ? -24.492 -32.299 -54.688  1.00 43.94  ? 381  ALA   A N   1 
ATOM   627   C  CA  . ALA   A  1 80  ? -23.537 -31.213 -54.904  1.00 44.09  ? 381  ALA   A CA  1 
ATOM   628   C  C   . ALA   A  1 80  ? -22.462 -31.181 -53.823  1.00 45.51  ? 381  ALA   A C   1 
ATOM   629   O  O   . ALA   A  1 80  ? -21.289 -30.909 -54.110  1.00 43.30  ? 381  ALA   A O   1 
ATOM   630   C  CB  . ALA   A  1 80  ? -24.272 -29.873 -54.961  1.00 42.25  ? 381  ALA   A CB  1 
ATOM   631   N  N   . HIS   A  1 81  ? -22.846 -31.439 -52.572  1.00 46.36  ? 382  HIS   A N   1 
ATOM   632   C  CA  . HIS   A  1 81  ? -21.878 -31.462 -51.480  1.00 43.32  ? 382  HIS   A CA  1 
ATOM   633   C  C   . HIS   A  1 81  ? -20.814 -32.532 -51.708  1.00 44.32  ? 382  HIS   A C   1 
ATOM   634   O  O   . HIS   A  1 81  ? -19.610 -32.260 -51.609  1.00 39.43  ? 382  HIS   A O   1 
ATOM   635   C  CB  . HIS   A  1 81  ? -22.612 -31.695 -50.161  1.00 43.38  ? 382  HIS   A CB  1 
ATOM   636   C  CG  . HIS   A  1 81  ? -21.728 -31.669 -48.956  1.00 47.46  ? 382  HIS   A CG  1 
ATOM   637   N  ND1 . HIS   A  1 81  ? -22.194 -31.965 -47.694  1.00 51.18  ? 382  HIS   A ND1 1 
ATOM   638   C  CD2 . HIS   A  1 81  ? -20.414 -31.375 -48.812  1.00 49.08  ? 382  HIS   A CD2 1 
ATOM   639   C  CE1 . HIS   A  1 81  ? -21.206 -31.858 -46.823  1.00 48.74  ? 382  HIS   A CE1 1 
ATOM   640   N  NE2 . HIS   A  1 81  ? -20.113 -31.503 -47.476  1.00 48.90  ? 382  HIS   A NE2 1 
ATOM   641   N  N   . MET   A  1 82  ? -21.241 -33.758 -52.022  1.00 38.77  ? 383  MET   A N   1 
ATOM   642   C  CA  . MET   A  1 82  ? -20.286 -34.848 -52.191  1.00 37.87  ? 383  MET   A CA  1 
ATOM   643   C  C   . MET   A  1 82  ? -19.427 -34.631 -53.424  1.00 43.98  ? 383  MET   A C   1 
ATOM   644   O  O   . MET   A  1 82  ? -18.225 -34.921 -53.411  1.00 49.72  ? 383  MET   A O   1 
ATOM   645   C  CB  . MET   A  1 82  ? -21.020 -36.191 -52.284  1.00 47.47  ? 383  MET   A CB  1 
ATOM   646   C  CG  . MET   A  1 82  ? -21.857 -36.498 -51.075  1.00 48.93  ? 383  MET   A CG  1 
ATOM   647   S  SD  . MET   A  1 82  ? -20.900 -36.221 -49.576  1.00 57.47  ? 383  MET   A SD  1 
ATOM   648   C  CE  . MET   A  1 82  ? -19.650 -37.490 -49.754  1.00 63.69  ? 383  MET   A CE  1 
ATOM   649   N  N   . GLU   A  1 83  ? -20.030 -34.128 -54.502  1.00 43.04  ? 384  GLU   A N   1 
ATOM   650   C  CA  . GLU   A  1 83  ? -19.249 -33.797 -55.684  1.00 44.38  ? 384  GLU   A CA  1 
ATOM   651   C  C   . GLU   A  1 83  ? -18.203 -32.752 -55.343  1.00 40.40  ? 384  GLU   A C   1 
ATOM   652   O  O   . GLU   A  1 83  ? -17.029 -32.894 -55.701  1.00 42.21  ? 384  GLU   A O   1 
ATOM   653   C  CB  . GLU   A  1 83  ? -20.167 -33.316 -56.811  1.00 51.67  ? 384  GLU   A CB  1 
ATOM   654   C  CG  . GLU   A  1 83  ? -21.049 -34.413 -57.392  1.00 62.23  ? 384  GLU   A CG  1 
ATOM   655   C  CD  . GLU   A  1 83  ? -21.906 -33.930 -58.546  1.00 71.61  ? 384  GLU   A CD  1 
ATOM   656   O  OE1 . GLU   A  1 83  ? -21.654 -32.813 -59.048  1.00 74.34  ? 384  GLU   A OE1 1 
ATOM   657   O  OE2 . GLU   A  1 83  ? -22.833 -34.667 -58.951  1.00 76.48  ? 384  GLU   A OE2 1 
ATOM   658   N  N   . ARG   A  1 84  ? -18.609 -31.712 -54.609  1.00 41.87  ? 385  ARG   A N   1 
ATOM   659   C  CA  . ARG   A  1 84  ? -17.673 -30.661 -54.223  1.00 42.72  ? 385  ARG   A CA  1 
ATOM   660   C  C   . ARG   A  1 84  ? -16.491 -31.231 -53.449  1.00 40.61  ? 385  ARG   A C   1 
ATOM   661   O  O   . ARG   A  1 84  ? -15.335 -30.890 -53.725  1.00 44.32  ? 385  ARG   A O   1 
ATOM   662   C  CB  . ARG   A  1 84  ? -18.393 -29.598 -53.402  1.00 41.93  ? 385  ARG   A CB  1 
ATOM   663   C  CG  . ARG   A  1 84  ? -17.559 -28.369 -53.145  1.00 37.69  ? 385  ARG   A CG  1 
ATOM   664   C  CD  . ARG   A  1 84  ? -17.398 -27.494 -54.384  1.00 37.62  ? 385  ARG   A CD  1 
ATOM   665   N  NE  . ARG   A  1 84  ? -16.529 -26.379 -54.034  1.00 37.20  ? 385  ARG   A NE  1 
ATOM   666   C  CZ  . ARG   A  1 84  ? -15.306 -26.189 -54.514  1.00 43.65  ? 385  ARG   A CZ  1 
ATOM   667   N  NH1 . ARG   A  1 84  ? -14.794 -27.006 -55.435  1.00 49.75  ? 385  ARG   A NH1 1 
ATOM   668   N  NH2 . ARG   A  1 84  ? -14.608 -25.152 -54.089  1.00 34.09  ? 385  ARG   A NH2 1 
ATOM   669   N  N   . LEU   A  1 85  ? -16.760 -32.116 -52.489  1.00 39.46  ? 386  LEU   A N   1 
ATOM   670   C  CA  . LEU   A  1 85  ? -15.680 -32.790 -51.780  1.00 37.36  ? 386  LEU   A CA  1 
ATOM   671   C  C   . LEU   A  1 85  ? -14.730 -33.482 -52.746  1.00 39.18  ? 386  LEU   A C   1 
ATOM   672   O  O   . LEU   A  1 85  ? -13.511 -33.285 -52.678  1.00 38.92  ? 386  LEU   A O   1 
ATOM   673   C  CB  . LEU   A  1 85  ? -16.259 -33.783 -50.777  1.00 42.30  ? 386  LEU   A CB  1 
ATOM   674   C  CG  . LEU   A  1 85  ? -16.918 -33.077 -49.589  1.00 42.14  ? 386  LEU   A CG  1 
ATOM   675   C  CD1 . LEU   A  1 85  ? -17.320 -34.084 -48.527  1.00 46.98  ? 386  LEU   A CD1 1 
ATOM   676   C  CD2 . LEU   A  1 85  ? -15.984 -32.017 -48.998  1.00 34.96  ? 386  LEU   A CD2 1 
ATOM   677   N  N   . GLU   A  1 86  ? -15.280 -34.283 -53.668  1.00 42.25  ? 387  GLU   A N   1 
ATOM   678   C  CA  . GLU   A  1 86  ? -14.463 -34.963 -54.665  1.00 44.68  ? 387  GLU   A CA  1 
ATOM   679   C  C   . GLU   A  1 86  ? -13.678 -33.968 -55.501  1.00 43.86  ? 387  GLU   A C   1 
ATOM   680   O  O   . GLU   A  1 86  ? -12.514 -34.206 -55.842  1.00 48.67  ? 387  GLU   A O   1 
ATOM   681   C  CB  . GLU   A  1 86  ? -15.346 -35.820 -55.573  1.00 56.37  ? 387  GLU   A CB  1 
ATOM   682   C  CG  . GLU   A  1 86  ? -15.627 -37.211 -55.050  1.00 73.42  ? 387  GLU   A CG  1 
ATOM   683   C  CD  . GLU   A  1 86  ? -14.357 -37.994 -54.792  1.00 84.64  ? 387  GLU   A CD  1 
ATOM   684   O  OE1 . GLU   A  1 86  ? -14.240 -38.602 -53.705  1.00 83.31  ? 387  GLU   A OE1 1 
ATOM   685   O  OE2 . GLU   A  1 86  ? -13.470 -37.989 -55.673  1.00 92.21  ? 387  GLU   A OE2 1 
ATOM   686   N  N   . GLU   A  1 87  ? -14.310 -32.852 -55.851  1.00 36.16  ? 388  GLU   A N   1 
ATOM   687   C  CA  . GLU   A  1 87  ? -13.643 -31.835 -56.646  1.00 34.98  ? 388  GLU   A CA  1 
ATOM   688   C  C   . GLU   A  1 87  ? -12.494 -31.217 -55.863  1.00 37.79  ? 388  GLU   A C   1 
ATOM   689   O  O   . GLU   A  1 87  ? -11.368 -31.109 -56.366  1.00 37.72  ? 388  GLU   A O   1 
ATOM   690   C  CB  . GLU   A  1 87  ? -14.668 -30.781 -57.068  1.00 38.18  ? 388  GLU   A CB  1 
ATOM   691   C  CG  . GLU   A  1 87  ? -14.178 -29.741 -58.049  1.00 46.20  ? 388  GLU   A CG  1 
ATOM   692   C  CD  . GLU   A  1 87  ? -15.288 -28.787 -58.449  1.00 55.99  ? 388  GLU   A CD  1 
ATOM   693   O  OE1 . GLU   A  1 87  ? -16.210 -28.580 -57.627  1.00 47.10  ? 388  GLU   A OE1 1 
ATOM   694   O  OE2 . GLU   A  1 87  ? -15.249 -28.257 -59.585  1.00 59.24  ? 388  GLU   A OE2 1 
ATOM   695   N  N   . VAL   A  1 88  ? -12.755 -30.821 -54.618  1.00 39.35  ? 389  VAL   A N   1 
ATOM   696   C  CA  . VAL   A  1 88  ? -11.695 -30.238 -53.807  1.00 39.53  ? 389  VAL   A CA  1 
ATOM   697   C  C   . VAL   A  1 88  ? -10.567 -31.241 -53.617  1.00 35.53  ? 389  VAL   A C   1 
ATOM   698   O  O   . VAL   A  1 88  ? -9.383  -30.900 -53.726  1.00 33.96  ? 389  VAL   A O   1 
ATOM   699   C  CB  . VAL   A  1 88  ? -12.269 -29.738 -52.474  1.00 38.56  ? 389  VAL   A CB  1 
ATOM   700   C  CG1 . VAL   A  1 88  ? -11.139 -29.303 -51.535  1.00 32.95  ? 389  VAL   A CG1 1 
ATOM   701   C  CG2 . VAL   A  1 88  ? -13.232 -28.586 -52.768  1.00 33.77  ? 389  VAL   A CG2 1 
ATOM   702   N  N   . ASN   A  1 89  ? -10.912 -32.507 -53.416  1.00 35.87  ? 390  ASN   A N   1 
ATOM   703   C  CA  . ASN   A  1 89  ? -9.878  -33.525 -53.284  1.00 41.42  ? 390  ASN   A CA  1 
ATOM   704   C  C   . ASN   A  1 89  ? -8.993  -33.597 -54.526  1.00 49.14  ? 390  ASN   A C   1 
ATOM   705   O  O   . ASN   A  1 89  ? -7.770  -33.733 -54.407  1.00 42.78  ? 390  ASN   A O   1 
ATOM   706   C  CB  . ASN   A  1 89  ? -10.511 -34.882 -52.999  1.00 45.63  ? 390  ASN   A CB  1 
ATOM   707   C  CG  . ASN   A  1 89  ? -9.507  -36.005 -53.074  1.00 59.26  ? 390  ASN   A CG  1 
ATOM   708   O  OD1 . ASN   A  1 89  ? -8.739  -36.222 -52.139  1.00 51.98  ? 390  ASN   A OD1 1 
ATOM   709   N  ND2 . ASN   A  1 89  ? -9.496  -36.724 -54.200  1.00 63.99  ? 390  ASN   A ND2 1 
ATOM   710   N  N   . LYS   A  1 90  ? -9.588  -33.513 -55.728  1.00 45.73  ? 391  LYS   A N   1 
ATOM   711   C  CA  . LYS   A  1 90  ? -8.797  -33.576 -56.955  1.00 41.89  ? 391  LYS   A CA  1 
ATOM   712   C  C   . LYS   A  1 90  ? -7.929  -32.337 -57.110  1.00 38.96  ? 391  LYS   A C   1 
ATOM   713   O  O   . LYS   A  1 90  ? -6.754  -32.430 -57.485  1.00 44.73  ? 391  LYS   A O   1 
ATOM   714   C  CB  . LYS   A  1 90  ? -9.702  -33.725 -58.184  1.00 53.68  ? 391  LYS   A CB  1 
ATOM   715   C  CG  . LYS   A  1 90  ? -10.599 -34.955 -58.199  1.00 72.19  ? 391  LYS   A CG  1 
ATOM   716   C  CD  . LYS   A  1 90  ? -9.812  -36.252 -58.045  1.00 76.55  ? 391  LYS   A CD  1 
ATOM   717   C  CE  . LYS   A  1 90  ? -10.737 -37.458 -57.975  1.00 71.84  ? 391  LYS   A CE  1 
ATOM   718   N  NZ  . LYS   A  1 90  ? -10.103 -38.583 -57.234  1.00 70.80  ? 391  LYS   A NZ  1 
ATOM   719   N  N   . GLU   A  1 91  ? -8.505  -31.161 -56.862  1.00 37.61  ? 392  GLU   A N   1 
ATOM   720   C  CA  . GLU   A  1 91  ? -7.741  -29.924 -56.950  1.00 41.45  ? 392  GLU   A CA  1 
ATOM   721   C  C   . GLU   A  1 91  ? -6.514  -29.976 -56.051  1.00 43.32  ? 392  GLU   A C   1 
ATOM   722   O  O   . GLU   A  1 91  ? -5.398  -29.662 -56.481  1.00 42.60  ? 392  GLU   A O   1 
ATOM   723   C  CB  . GLU   A  1 91  ? -8.626  -28.736 -56.575  1.00 39.91  ? 392  GLU   A CB  1 
ATOM   724   C  CG  . GLU   A  1 91  ? -9.730  -28.427 -57.569  1.00 46.78  ? 392  GLU   A CG  1 
ATOM   725   C  CD  . GLU   A  1 91  ? -10.383 -27.096 -57.285  1.00 58.48  ? 392  GLU   A CD  1 
ATOM   726   O  OE1 . GLU   A  1 91  ? -9.659  -26.079 -57.243  1.00 66.84  ? 392  GLU   A OE1 1 
ATOM   727   O  OE2 . GLU   A  1 91  ? -11.613 -27.066 -57.082  1.00 66.35  ? 392  GLU   A OE2 1 
ATOM   728   N  N   . ILE   A  1 92  ? -6.706  -30.369 -54.792  1.00 38.52  ? 393  ILE   A N   1 
ATOM   729   C  CA  . ILE   A  1 92  ? -5.580  -30.485 -53.872  1.00 44.66  ? 393  ILE   A CA  1 
ATOM   730   C  C   . ILE   A  1 92  ? -4.595  -31.529 -54.384  1.00 41.69  ? 393  ILE   A C   1 
ATOM   731   O  O   . ILE   A  1 92  ? -3.384  -31.292 -54.432  1.00 43.26  ? 393  ILE   A O   1 
ATOM   732   C  CB  . ILE   A  1 92  ? -6.088  -30.801 -52.453  1.00 41.90  ? 393  ILE   A CB  1 
ATOM   733   C  CG1 . ILE   A  1 92  ? -6.859  -29.591 -51.914  1.00 37.55  ? 393  ILE   A CG1 1 
ATOM   734   C  CG2 . ILE   A  1 92  ? -4.931  -31.184 -51.533  1.00 44.50  ? 393  ILE   A CG2 1 
ATOM   735   C  CD1 . ILE   A  1 92  ? -7.602  -29.834 -50.610  1.00 39.52  ? 393  ILE   A CD1 1 
ATOM   736   N  N   . ASP   A  1 93  ? -5.111  -32.676 -54.831  1.00 44.43  ? 394  ASP   A N   1 
ATOM   737   C  CA  . ASP   A  1 93  ? -4.266  -33.715 -55.423  1.00 54.36  ? 394  ASP   A CA  1 
ATOM   738   C  C   . ASP   A  1 93  ? -3.388  -33.180 -56.547  1.00 55.75  ? 394  ASP   A C   1 
ATOM   739   O  O   . ASP   A  1 93  ? -2.232  -33.593 -56.687  1.00 64.51  ? 394  ASP   A O   1 
ATOM   740   C  CB  . ASP   A  1 93  ? -5.125  -34.858 -55.965  1.00 61.49  ? 394  ASP   A CB  1 
ATOM   741   C  CG  . ASP   A  1 93  ? -5.500  -35.854 -54.905  1.00 71.98  ? 394  ASP   A CG  1 
ATOM   742   O  OD1 . ASP   A  1 93  ? -6.670  -36.291 -54.894  1.00 75.28  ? 394  ASP   A OD1 1 
ATOM   743   O  OD2 . ASP   A  1 93  ? -4.625  -36.194 -54.081  1.00 78.97  ? 394  ASP   A OD2 1 
ATOM   744   N  N   . THR   A  1 94  ? -3.916  -32.270 -57.366  1.00 43.05  ? 395  THR   A N   1 
ATOM   745   C  CA  . THR   A  1 94  ? -3.221  -31.868 -58.581  1.00 50.34  ? 395  THR   A CA  1 
ATOM   746   C  C   . THR   A  1 94  ? -2.566  -30.496 -58.494  1.00 55.08  ? 395  THR   A C   1 
ATOM   747   O  O   . THR   A  1 94  ? -1.709  -30.186 -59.328  1.00 54.98  ? 395  THR   A O   1 
ATOM   748   C  CB  . THR   A  1 94  ? -4.188  -31.887 -59.774  1.00 50.74  ? 395  THR   A CB  1 
ATOM   749   O  OG1 . THR   A  1 94  ? -5.274  -30.993 -59.519  1.00 56.80  ? 395  THR   A OG1 1 
ATOM   750   C  CG2 . THR   A  1 94  ? -4.742  -33.281 -59.984  1.00 53.07  ? 395  THR   A CG2 1 
ATOM   751   N  N   . THR   A  1 95  ? -2.948  -29.662 -57.525  1.00 49.47  ? 396  THR   A N   1 
ATOM   752   C  CA  . THR   A  1 95  ? -2.395  -28.320 -57.414  1.00 47.23  ? 396  THR   A CA  1 
ATOM   753   C  C   . THR   A  1 95  ? -1.932  -27.962 -56.005  1.00 43.10  ? 396  THR   A C   1 
ATOM   754   O  O   . THR   A  1 95  ? -1.434  -26.848 -55.806  1.00 49.39  ? 396  THR   A O   1 
ATOM   755   C  CB  . THR   A  1 95  ? -3.421  -27.263 -57.875  1.00 42.07  ? 396  THR   A CB  1 
ATOM   756   O  OG1 . THR   A  1 95  ? -4.449  -27.122 -56.883  1.00 41.72  ? 396  THR   A OG1 1 
ATOM   757   C  CG2 . THR   A  1 95  ? -4.058  -27.651 -59.202  1.00 36.92  ? 396  THR   A CG2 1 
ATOM   758   N  N   . SER   A  1 96  ? -2.089  -28.855 -55.027  1.00 34.94  ? 397  SER   A N   1 
ATOM   759   C  CA  . SER   A  1 96  ? -1.783  -28.599 -53.615  1.00 42.36  ? 397  SER   A CA  1 
ATOM   760   C  C   . SER   A  1 96  ? -2.686  -27.539 -53.006  1.00 43.60  ? 397  SER   A C   1 
ATOM   761   O  O   . SER   A  1 96  ? -2.453  -27.109 -51.866  1.00 44.10  ? 397  SER   A O   1 
ATOM   762   C  CB  . SER   A  1 96  ? -0.319  -28.194 -53.391  1.00 46.57  ? 397  SER   A CB  1 
ATOM   763   O  OG  . SER   A  1 96  ? 0.548   -29.316 -53.424  1.00 48.48  ? 397  SER   A OG  1 
ATOM   764   N  N   . THR   A  1 97  ? -3.714  -27.105 -53.723  1.00 40.02  ? 398  THR   A N   1 
ATOM   765   C  CA  . THR   A  1 97  ? -4.660  -26.141 -53.186  1.00 36.22  ? 398  THR   A CA  1 
ATOM   766   C  C   . THR   A  1 97  ? -6.019  -26.430 -53.813  1.00 34.75  ? 398  THR   A C   1 
ATOM   767   O  O   . THR   A  1 97  ? -6.204  -27.450 -54.483  1.00 34.86  ? 398  THR   A O   1 
ATOM   768   C  CB  . THR   A  1 97  ? -4.155  -24.714 -53.439  1.00 30.83  ? 398  THR   A CB  1 
ATOM   769   O  OG1 . THR   A  1 97  ? -4.922  -23.784 -52.666  1.00 33.28  ? 398  THR   A OG1 1 
ATOM   770   C  CG2 . THR   A  1 97  ? -4.242  -24.359 -54.925  1.00 29.77  ? 398  THR   A CG2 1 
ATOM   771   N  N   . TYR   A  1 98  ? -6.988  -25.557 -53.563  1.00 34.51  ? 399  TYR   A N   1 
ATOM   772   C  CA  . TYR   A  1 98  ? -8.258  -25.636 -54.273  1.00 31.87  ? 399  TYR   A CA  1 
ATOM   773   C  C   . TYR   A  1 98  ? -8.823  -24.234 -54.390  1.00 29.80  ? 399  TYR   A C   1 
ATOM   774   O  O   . TYR   A  1 98  ? -8.321  -23.288 -53.777  1.00 29.68  ? 399  TYR   A O   1 
ATOM   775   C  CB  . TYR   A  1 98  ? -9.251  -26.581 -53.589  1.00 32.63  ? 399  TYR   A CB  1 
ATOM   776   C  CG  . TYR   A  1 98  ? -9.778  -26.084 -52.262  1.00 33.21  ? 399  TYR   A CG  1 
ATOM   777   C  CD1 . TYR   A  1 98  ? -11.074 -25.611 -52.146  1.00 32.56  ? 399  TYR   A CD1 1 
ATOM   778   C  CD2 . TYR   A  1 98  ? -8.981  -26.103 -51.125  1.00 29.59  ? 399  TYR   A CD2 1 
ATOM   779   C  CE1 . TYR   A  1 98  ? -11.557 -25.173 -50.942  1.00 30.81  ? 399  TYR   A CE1 1 
ATOM   780   C  CE2 . TYR   A  1 98  ? -9.453  -25.663 -49.924  1.00 32.58  ? 399  TYR   A CE2 1 
ATOM   781   C  CZ  . TYR   A  1 98  ? -10.745 -25.201 -49.833  1.00 33.44  ? 399  TYR   A CZ  1 
ATOM   782   O  OH  . TYR   A  1 98  ? -11.220 -24.761 -48.618  1.00 33.77  ? 399  TYR   A OH  1 
ATOM   783   N  N   . GLN   A  1 99  ? -9.864  -24.102 -55.209  1.00 33.51  ? 400  GLN   A N   1 
ATOM   784   C  CA  . GLN   A  1 99  ? -10.457 -22.806 -55.515  1.00 30.20  ? 400  GLN   A CA  1 
ATOM   785   C  C   . GLN   A  1 99  ? -11.887 -22.779 -55.004  1.00 30.67  ? 400  GLN   A C   1 
ATOM   786   O  O   . GLN   A  1 99  ? -12.650 -23.727 -55.226  1.00 31.64  ? 400  GLN   A O   1 
ATOM   787   C  CB  . GLN   A  1 99  ? -10.426 -22.524 -57.029  1.00 29.94  ? 400  GLN   A CB  1 
ATOM   788   C  CG  . GLN   A  1 99  ? -9.032  -22.531 -57.632  1.00 32.72  ? 400  GLN   A CG  1 
ATOM   789   C  CD  . GLN   A  1 99  ? -8.095  -21.542 -56.951  1.00 38.84  ? 400  GLN   A CD  1 
ATOM   790   O  OE1 . GLN   A  1 99  ? -8.443  -20.374 -56.743  1.00 41.64  ? 400  GLN   A OE1 1 
ATOM   791   N  NE2 . GLN   A  1 99  ? -6.901  -22.013 -56.584  1.00 38.30  ? 400  GLN   A NE2 1 
ATOM   792   N  N   . LEU   A  1 100 ? -12.248 -21.692 -54.335  1.00 29.23  ? 401  LEU   A N   1 
ATOM   793   C  CA  . LEU   A  1 100 ? -13.601 -21.526 -53.834  1.00 33.00  ? 401  LEU   A CA  1 
ATOM   794   C  C   . LEU   A  1 100 ? -14.554 -21.168 -54.961  1.00 31.30  ? 401  LEU   A C   1 
ATOM   795   O  O   . LEU   A  1 100 ? -14.226 -20.360 -55.835  1.00 33.82  ? 401  LEU   A O   1 
ATOM   796   C  CB  . LEU   A  1 100 ? -13.636 -20.426 -52.769  1.00 26.05  ? 401  LEU   A CB  1 
ATOM   797   C  CG  . LEU   A  1 100 ? -12.871 -20.777 -51.502  1.00 24.60  ? 401  LEU   A CG  1 
ATOM   798   C  CD1 . LEU   A  1 100 ? -12.973 -19.638 -50.509  1.00 25.06  ? 401  LEU   A CD1 1 
ATOM   799   C  CD2 . LEU   A  1 100 ? -13.475 -22.032 -50.925  1.00 21.89  ? 401  LEU   A CD2 1 
ATOM   800   N  N   . LYS   A  1 101 ? -15.739 -21.775 -54.938  1.00 26.87  ? 402  LYS   A N   1 
ATOM   801   C  CA  . LYS   A  1 101 ? -16.849 -21.244 -55.712  1.00 28.13  ? 402  LYS   A CA  1 
ATOM   802   C  C   . LYS   A  1 101 ? -17.178 -19.829 -55.248  1.00 26.28  ? 402  LYS   A C   1 
ATOM   803   O  O   . LYS   A  1 101 ? -16.943 -19.465 -54.090  1.00 26.13  ? 402  LYS   A O   1 
ATOM   804   C  CB  . LYS   A  1 101 ? -18.083 -22.132 -55.560  1.00 28.94  ? 402  LYS   A CB  1 
ATOM   805   C  CG  . LYS   A  1 101 ? -17.850 -23.549 -55.982  1.00 34.77  ? 402  LYS   A CG  1 
ATOM   806   C  CD  . LYS   A  1 101 ? -17.517 -23.598 -57.463  1.00 39.92  ? 402  LYS   A CD  1 
ATOM   807   C  CE  . LYS   A  1 101 ? -16.368 -24.555 -57.740  1.00 49.55  ? 402  LYS   A CE  1 
ATOM   808   N  NZ  . LYS   A  1 101 ? -16.466 -25.201 -59.081  1.00 47.36  ? 402  LYS   A NZ  1 
ATOM   809   N  N   . ASP   A  1 102 ? -17.741 -19.034 -56.167  1.00 27.13  ? 403  ASP   A N   1 
ATOM   810   C  CA  . ASP   A  1 102 ? -18.163 -17.672 -55.842  1.00 27.28  ? 403  ASP   A CA  1 
ATOM   811   C  C   . ASP   A  1 102 ? -19.082 -17.648 -54.630  1.00 27.25  ? 403  ASP   A C   1 
ATOM   812   O  O   . ASP   A  1 102 ? -18.938 -16.800 -53.747  1.00 28.40  ? 403  ASP   A O   1 
ATOM   813   C  CB  . ASP   A  1 102 ? -18.875 -17.035 -57.032  1.00 29.00  ? 403  ASP   A CB  1 
ATOM   814   C  CG  . ASP   A  1 102 ? -17.992 -16.950 -58.263  1.00 52.00  ? 403  ASP   A CG  1 
ATOM   815   O  OD1 . ASP   A  1 102 ? -16.852 -17.465 -58.211  1.00 58.92  ? 403  ASP   A OD1 1 
ATOM   816   O  OD2 . ASP   A  1 102 ? -18.436 -16.367 -59.282  1.00 54.45  ? 403  ASP   A OD2 1 
ATOM   817   N  N   . THR   A  1 103 ? -20.059 -18.555 -54.600  1.00 28.95  ? 404  THR   A N   1 
ATOM   818   C  CA  . THR   A  1 103 ? -20.967 -18.640 -53.466  1.00 30.62  ? 404  THR   A CA  1 
ATOM   819   C  C   . THR   A  1 103 ? -20.207 -18.945 -52.182  1.00 32.00  ? 404  THR   A C   1 
ATOM   820   O  O   . THR   A  1 103 ? -20.473 -18.337 -51.143  1.00 26.99  ? 404  THR   A O   1 
ATOM   821   C  CB  . THR   A  1 103 ? -22.034 -19.709 -53.712  1.00 34.85  ? 404  THR   A CB  1 
ATOM   822   O  OG1 . THR   A  1 103 ? -21.402 -20.981 -53.923  1.00 39.95  ? 404  THR   A OG1 1 
ATOM   823   C  CG2 . THR   A  1 103 ? -22.882 -19.363 -54.923  1.00 34.92  ? 404  THR   A CG2 1 
ATOM   824   N  N   . GLU   A  1 104 ? -19.248 -19.873 -52.240  1.00 30.82  ? 405  GLU   A N   1 
ATOM   825   C  CA  . GLU   A  1 104 ? -18.475 -20.203 -51.047  1.00 26.52  ? 405  GLU   A CA  1 
ATOM   826   C  C   . GLU   A  1 104 ? -17.612 -19.026 -50.617  1.00 28.96  ? 405  GLU   A C   1 
ATOM   827   O  O   . GLU   A  1 104 ? -17.452 -18.769 -49.417  1.00 28.12  ? 405  GLU   A O   1 
ATOM   828   C  CB  . GLU   A  1 104 ? -17.600 -21.429 -51.315  1.00 25.37  ? 405  GLU   A CB  1 
ATOM   829   C  CG  . GLU   A  1 104 ? -18.367 -22.673 -51.711  1.00 32.43  ? 405  GLU   A CG  1 
ATOM   830   C  CD  . GLU   A  1 104 ? -17.486 -23.701 -52.410  1.00 35.48  ? 405  GLU   A CD  1 
ATOM   831   O  OE1 . GLU   A  1 104 ? -17.961 -24.833 -52.625  1.00 30.85  ? 405  GLU   A OE1 1 
ATOM   832   O  OE2 . GLU   A  1 104 ? -16.323 -23.378 -52.740  1.00 37.08  ? 405  GLU   A OE2 1 
ATOM   833   N  N   . LEU   A  1 105 ? -17.011 -18.334 -51.588  1.00 29.43  ? 406  LEU   A N   1 
ATOM   834   C  CA  . LEU   A  1 105 ? -16.236 -17.137 -51.294  1.00 25.29  ? 406  LEU   A CA  1 
ATOM   835   C  C   . LEU   A  1 105 ? -17.093 -16.123 -50.562  1.00 27.62  ? 406  LEU   A C   1 
ATOM   836   O  O   . LEU   A  1 105 ? -16.672 -15.543 -49.554  1.00 30.23  ? 406  LEU   A O   1 
ATOM   837   C  CB  . LEU   A  1 105 ? -15.694 -16.525 -52.586  1.00 27.50  ? 406  LEU   A CB  1 
ATOM   838   C  CG  . LEU   A  1 105 ? -14.786 -15.309 -52.411  1.00 28.43  ? 406  LEU   A CG  1 
ATOM   839   C  CD1 . LEU   A  1 105 ? -13.512 -15.745 -51.698  1.00 32.28  ? 406  LEU   A CD1 1 
ATOM   840   C  CD2 . LEU   A  1 105 ? -14.464 -14.645 -53.767  1.00 26.77  ? 406  LEU   A CD2 1 
ATOM   841   N  N   . ILE   A  1 106 ? -18.304 -15.898 -51.059  1.00 25.37  ? 407  ILE   A N   1 
ATOM   842   C  CA  . ILE   A  1 106 ? -19.163 -14.889 -50.461  1.00 23.63  ? 407  ILE   A CA  1 
ATOM   843   C  C   . ILE   A  1 106 ? -19.579 -15.318 -49.063  1.00 30.87  ? 407  ILE   A C   1 
ATOM   844   O  O   . ILE   A  1 106 ? -19.486 -14.543 -48.105  1.00 31.39  ? 407  ILE   A O   1 
ATOM   845   C  CB  . ILE   A  1 106 ? -20.383 -14.637 -51.357  1.00 21.65  ? 407  ILE   A CB  1 
ATOM   846   C  CG1 . ILE   A  1 106 ? -19.950 -13.911 -52.632  1.00 22.54  ? 407  ILE   A CG1 1 
ATOM   847   C  CG2 . ILE   A  1 106 ? -21.450 -13.869 -50.579  1.00 23.00  ? 407  ILE   A CG2 1 
ATOM   848   C  CD1 . ILE   A  1 106 ? -20.987 -13.976 -53.733  1.00 28.34  ? 407  ILE   A CD1 1 
ATOM   849   N  N   . TYR   A  1 107 ? -20.052 -16.561 -48.937  1.00 30.42  ? 408  TYR   A N   1 
ATOM   850   C  CA  . TYR   A  1 107 ? -20.382 -17.126 -47.636  1.00 31.13  ? 408  TYR   A CA  1 
ATOM   851   C  C   . TYR   A  1 107 ? -19.217 -16.994 -46.665  1.00 28.82  ? 408  TYR   A C   1 
ATOM   852   O  O   . TYR   A  1 107 ? -19.391 -16.582 -45.510  1.00 24.61  ? 408  TYR   A O   1 
ATOM   853   C  CB  . TYR   A  1 107 ? -20.770 -18.597 -47.803  1.00 28.95  ? 408  TYR   A CB  1 
ATOM   854   C  CG  . TYR   A  1 107 ? -20.904 -19.327 -46.484  1.00 29.86  ? 408  TYR   A CG  1 
ATOM   855   C  CD1 . TYR   A  1 107 ? -22.076 -19.257 -45.752  1.00 24.81  ? 408  TYR   A CD1 1 
ATOM   856   C  CD2 . TYR   A  1 107 ? -19.853 -20.080 -45.971  1.00 30.97  ? 408  TYR   A CD2 1 
ATOM   857   C  CE1 . TYR   A  1 107 ? -22.207 -19.930 -44.537  1.00 26.65  ? 408  TYR   A CE1 1 
ATOM   858   C  CE2 . TYR   A  1 107 ? -19.970 -20.748 -44.768  1.00 34.98  ? 408  TYR   A CE2 1 
ATOM   859   C  CZ  . TYR   A  1 107 ? -21.148 -20.672 -44.055  1.00 35.40  ? 408  TYR   A CZ  1 
ATOM   860   O  OH  . TYR   A  1 107 ? -21.258 -21.332 -42.855  1.00 43.81  ? 408  TYR   A OH  1 
ATOM   861   N  N   . GLY   A  1 108 ? -18.015 -17.345 -47.122  1.00 25.10  ? 409  GLY   A N   1 
ATOM   862   C  CA  . GLY   A  1 108 ? -16.869 -17.331 -46.236  1.00 23.64  ? 409  GLY   A CA  1 
ATOM   863   C  C   . GLY   A  1 108 ? -16.514 -15.938 -45.755  1.00 30.65  ? 409  GLY   A C   1 
ATOM   864   O  O   . GLY   A  1 108 ? -16.183 -15.743 -44.578  1.00 23.73  ? 409  GLY   A O   1 
ATOM   865   N  N   . ALA   A  1 109 ? -16.566 -14.955 -46.661  1.00 21.15  ? 410  ALA   A N   1 
ATOM   866   C  CA  . ALA   A  1 109 ? -16.240 -13.583 -46.296  1.00 22.88  ? 410  ALA   A CA  1 
ATOM   867   C  C   . ALA   A  1 109 ? -17.258 -13.033 -45.310  1.00 21.94  ? 410  ALA   A C   1 
ATOM   868   O  O   . ALA   A  1 109 ? -16.893 -12.440 -44.291  1.00 27.67  ? 410  ALA   A O   1 
ATOM   869   C  CB  . ALA   A  1 109 ? -16.162 -12.703 -47.556  1.00 20.22  ? 410  ALA   A CB  1 
ATOM   870   N  N   . LYS   A  1 110 ? -18.545 -13.224 -45.595  1.00 21.53  ? 411  LYS   A N   1 
ATOM   871   C  CA  . LYS   A  1 110 ? -19.562 -12.761 -44.661  1.00 25.10  ? 411  LYS   A CA  1 
ATOM   872   C  C   . LYS   A  1 110 ? -19.403 -13.434 -43.305  1.00 27.83  ? 411  LYS   A C   1 
ATOM   873   O  O   . LYS   A  1 110 ? -19.568 -12.792 -42.269  1.00 24.19  ? 411  LYS   A O   1 
ATOM   874   C  CB  . LYS   A  1 110 ? -20.960 -13.006 -45.222  1.00 21.07  ? 411  LYS   A CB  1 
ATOM   875   C  CG  . LYS   A  1 110 ? -21.279 -12.135 -46.439  1.00 22.88  ? 411  LYS   A CG  1 
ATOM   876   C  CD  . LYS   A  1 110 ? -22.682 -12.364 -46.955  1.00 22.09  ? 411  LYS   A CD  1 
ATOM   877   C  CE  . LYS   A  1 110 ? -22.946 -11.531 -48.215  1.00 22.60  ? 411  LYS   A CE  1 
ATOM   878   N  NZ  . LYS   A  1 110 ? -24.401 -11.589 -48.496  1.00 28.25  ? 411  LYS   A NZ  1 
ATOM   879   N  N   . HIS   A  1 111 ? -19.043 -14.712 -43.290  1.00 26.55  ? 412  HIS   A N   1 
ATOM   880   C  CA  . HIS   A  1 111 ? -18.920 -15.406 -42.017  1.00 21.73  ? 412  HIS   A CA  1 
ATOM   881   C  C   . HIS   A  1 111 ? -17.659 -15.046 -41.265  1.00 29.64  ? 412  HIS   A C   1 
ATOM   882   O  O   . HIS   A  1 111 ? -17.681 -15.003 -40.024  1.00 23.78  ? 412  HIS   A O   1 
ATOM   883   C  CB  . HIS   A  1 111 ? -19.050 -16.891 -42.229  1.00 24.26  ? 412  HIS   A CB  1 
ATOM   884   C  CG  . HIS   A  1 111 ? -20.479 -17.279 -42.270  1.00 29.78  ? 412  HIS   A CG  1 
ATOM   885   N  ND1 . HIS   A  1 111 ? -21.130 -17.827 -41.190  1.00 33.04  ? 412  HIS   A ND1 1 
ATOM   886   C  CD2 . HIS   A  1 111 ? -21.429 -17.015 -43.190  1.00 28.38  ? 412  HIS   A CD2 1 
ATOM   887   C  CE1 . HIS   A  1 111 ? -22.410 -17.973 -41.484  1.00 29.82  ? 412  HIS   A CE1 1 
ATOM   888   N  NE2 . HIS   A  1 111 ? -22.616 -17.482 -42.689  1.00 31.54  ? 412  HIS   A NE2 1 
ATOM   889   N  N   . ALA   A  1 112 ? -16.595 -14.696 -41.979  1.00 21.79  ? 413  ALA   A N   1 
ATOM   890   C  CA  . ALA   A  1 112 ? -15.424 -14.163 -41.301  1.00 21.91  ? 413  ALA   A CA  1 
ATOM   891   C  C   . ALA   A  1 112 ? -15.767 -12.870 -40.580  1.00 24.15  ? 413  ALA   A C   1 
ATOM   892   O  O   . ALA   A  1 112 ? -15.322 -12.640 -39.451  1.00 22.40  ? 413  ALA   A O   1 
ATOM   893   C  CB  . ALA   A  1 112 ? -14.311 -13.939 -42.303  1.00 19.77  ? 413  ALA   A CB  1 
ATOM   894   N  N   . TRP   A  1 113 ? -16.575 -12.021 -41.217  1.00 19.77  ? 414  TRP   A N   1 
ATOM   895   C  CA  . TRP   A  1 113 ? -17.045 -10.820 -40.551  1.00 19.57  ? 414  TRP   A CA  1 
ATOM   896   C  C   . TRP   A  1 113 ? -17.947 -11.177 -39.383  1.00 20.16  ? 414  TRP   A C   1 
ATOM   897   O  O   . TRP   A  1 113 ? -17.781 -10.653 -38.283  1.00 23.23  ? 414  TRP   A O   1 
ATOM   898   C  CB  . TRP   A  1 113 ? -17.775 -9.919  -41.545  1.00 15.79  ? 414  TRP   A CB  1 
ATOM   899   C  CG  . TRP   A  1 113 ? -18.217 -8.623  -40.959  1.00 20.91  ? 414  TRP   A CG  1 
ATOM   900   C  CD1 . TRP   A  1 113 ? -17.893 -8.118  -39.733  1.00 21.83  ? 414  TRP   A CD1 1 
ATOM   901   C  CD2 . TRP   A  1 113 ? -19.072 -7.657  -41.577  1.00 23.15  ? 414  TRP   A CD2 1 
ATOM   902   N  NE1 . TRP   A  1 113 ? -18.504 -6.905  -39.544  1.00 21.37  ? 414  TRP   A NE1 1 
ATOM   903   C  CE2 . TRP   A  1 113 ? -19.229 -6.595  -40.667  1.00 23.87  ? 414  TRP   A CE2 1 
ATOM   904   C  CE3 . TRP   A  1 113 ? -19.719 -7.586  -42.818  1.00 22.44  ? 414  TRP   A CE3 1 
ATOM   905   C  CZ2 . TRP   A  1 113 ? -20.014 -5.474  -40.955  1.00 20.12  ? 414  TRP   A CZ2 1 
ATOM   906   C  CZ3 . TRP   A  1 113 ? -20.497 -6.470  -43.101  1.00 26.37  ? 414  TRP   A CZ3 1 
ATOM   907   C  CH2 . TRP   A  1 113 ? -20.634 -5.430  -42.174  1.00 26.13  ? 414  TRP   A CH2 1 
ATOM   908   N  N   . ARG   A  1 114 ? -18.929 -12.047 -39.618  1.00 22.22  ? 415  ARG   A N   1 
ATOM   909   C  CA  . ARG   A  1 114 ? -19.832 -12.466 -38.556  1.00 22.57  ? 415  ARG   A CA  1 
ATOM   910   C  C   . ARG   A  1 114 ? -19.079 -13.030 -37.365  1.00 25.40  ? 415  ARG   A C   1 
ATOM   911   O  O   . ARG   A  1 114 ? -19.504 -12.854 -36.214  1.00 26.12  ? 415  ARG   A O   1 
ATOM   912   C  CB  . ARG   A  1 114 ? -20.797 -13.508 -39.106  1.00 24.23  ? 415  ARG   A CB  1 
ATOM   913   C  CG  . ARG   A  1 114 ? -21.926 -13.843 -38.195  1.00 22.91  ? 415  ARG   A CG  1 
ATOM   914   C  CD  . ARG   A  1 114 ? -22.690 -15.020 -38.740  1.00 23.16  ? 415  ARG   A CD  1 
ATOM   915   N  NE  . ARG   A  1 114 ? -23.979 -15.119 -38.085  1.00 21.71  ? 415  ARG   A NE  1 
ATOM   916   C  CZ  . ARG   A  1 114 ? -24.898 -16.018 -38.387  1.00 26.80  ? 415  ARG   A CZ  1 
ATOM   917   N  NH1 . ARG   A  1 114 ? -26.047 -16.008 -37.732  1.00 25.57  ? 415  ARG   A NH1 1 
ATOM   918   N  NH2 . ARG   A  1 114 ? -24.671 -16.901 -39.362  1.00 26.01  ? 415  ARG   A NH2 1 
ATOM   919   N  N   . ASN   A  1 115 ? -17.961 -13.695 -37.615  1.00 18.08  ? 416  ASN   A N   1 
ATOM   920   C  CA  . ASN   A  1 115 ? -17.179 -14.333 -36.575  1.00 24.11  ? 416  ASN   A CA  1 
ATOM   921   C  C   . ASN   A  1 115 ? -16.165 -13.393 -35.944  1.00 27.50  ? 416  ASN   A C   1 
ATOM   922   O  O   . ASN   A  1 115 ? -15.407 -13.829 -35.074  1.00 23.04  ? 416  ASN   A O   1 
ATOM   923   C  CB  . ASN   A  1 115 ? -16.446 -15.554 -37.143  1.00 21.57  ? 416  ASN   A CB  1 
ATOM   924   C  CG  . ASN   A  1 115 ? -17.384 -16.648 -37.583  1.00 25.63  ? 416  ASN   A CG  1 
ATOM   925   O  OD1 . ASN   A  1 115 ? -18.551 -16.670 -37.193  1.00 21.97  ? 416  ASN   A OD1 1 
ATOM   926   N  ND2 . ASN   A  1 115 ? -16.880 -17.568 -38.411  1.00 23.65  ? 416  ASN   A ND2 1 
ATOM   927   N  N   . ALA   A  1 116 ? -16.102 -12.135 -36.376  1.00 19.33  ? 417  ALA   A N   1 
ATOM   928   C  CA  . ALA   A  1 116 ? -15.044 -11.239 -35.912  1.00 20.62  ? 417  ALA   A CA  1 
ATOM   929   C  C   . ALA   A  1 116 ? -15.429 -10.716 -34.525  1.00 19.06  ? 417  ALA   A C   1 
ATOM   930   O  O   . ALA   A  1 116 ? -16.223 -9.782  -34.392  1.00 18.43  ? 417  ALA   A O   1 
ATOM   931   C  CB  . ALA   A  1 116 ? -14.820 -10.108 -36.908  1.00 16.15  ? 417  ALA   A CB  1 
ATOM   932   N  N   . SER   A  1 117 ? -14.854 -11.321 -33.491  1.00 18.51  ? 418  SER   A N   1 
ATOM   933   C  CA  A SER   A  1 117 ? -15.288 -11.031 -32.127  0.75 19.31  ? 418  SER   A CA  1 
ATOM   934   C  CA  B SER   A  1 117 ? -15.271 -11.038 -32.121  0.25 19.39  ? 418  SER   A CA  1 
ATOM   935   C  C   . SER   A  1 117 ? -14.999 -9.602  -31.703  1.00 23.63  ? 418  SER   A C   1 
ATOM   936   O  O   . SER   A  1 117 ? -15.657 -9.102  -30.785  1.00 23.77  ? 418  SER   A O   1 
ATOM   937   C  CB  A SER   A  1 117 ? -14.604 -11.969 -31.150  0.75 18.47  ? 418  SER   A CB  1 
ATOM   938   C  CB  B SER   A  1 117 ? -14.560 -11.983 -31.157  0.25 18.88  ? 418  SER   A CB  1 
ATOM   939   O  OG  A SER   A  1 117 ? -13.226 -11.677 -31.136  0.75 22.83  ? 418  SER   A OG  1 
ATOM   940   O  OG  B SER   A  1 117 ? -14.665 -13.331 -31.583  0.25 17.07  ? 418  SER   A OG  1 
ATOM   941   N  N   . ARG   A  1 118 ? -14.033 -8.939  -32.334  1.00 21.57  ? 419  ARG   A N   1 
ATOM   942   C  CA  . ARG   A  1 118 ? -13.686 -7.584  -31.950  1.00 21.21  ? 419  ARG   A CA  1 
ATOM   943   C  C   . ARG   A  1 118 ? -14.529 -6.524  -32.629  1.00 26.83  ? 419  ARG   A C   1 
ATOM   944   O  O   . ARG   A  1 118 ? -14.344 -5.343  -32.329  1.00 20.82  ? 419  ARG   A O   1 
ATOM   945   C  CB  . ARG   A  1 118 ? -12.209 -7.321  -32.238  1.00 19.27  ? 419  ARG   A CB  1 
ATOM   946   C  CG  . ARG   A  1 118 ? -11.301 -8.158  -31.365  1.00 19.63  ? 419  ARG   A CG  1 
ATOM   947   C  CD  . ARG   A  1 118 ? -9.853  -7.987  -31.764  1.00 19.38  ? 419  ARG   A CD  1 
ATOM   948   N  NE  . ARG   A  1 118 ? -8.973  -8.469  -30.712  1.00 23.03  ? 419  ARG   A NE  1 
ATOM   949   C  CZ  . ARG   A  1 118 ? -7.653  -8.533  -30.832  1.00 31.06  ? 419  ARG   A CZ  1 
ATOM   950   N  NH1 . ARG   A  1 118 ? -7.077  -8.151  -31.970  1.00 24.98  ? 419  ARG   A NH1 1 
ATOM   951   N  NH2 . ARG   A  1 118 ? -6.910  -8.981  -29.829  1.00 33.04  ? 419  ARG   A NH2 1 
ATOM   952   N  N   . CYS   A  1 119 ? -15.441 -6.901  -33.527  1.00 23.44  ? 420  CYS   A N   1 
ATOM   953   C  CA  . CYS   A  1 119 ? -16.143 -5.935  -34.354  1.00 15.86  ? 420  CYS   A CA  1 
ATOM   954   C  C   . CYS   A  1 119 ? -17.516 -5.669  -33.771  1.00 16.64  ? 420  CYS   A C   1 
ATOM   955   O  O   . CYS   A  1 119 ? -18.348 -6.580  -33.687  1.00 17.67  ? 420  CYS   A O   1 
ATOM   956   C  CB  . CYS   A  1 119 ? -16.271 -6.429  -35.805  1.00 20.71  ? 420  CYS   A CB  1 
ATOM   957   S  SG  . CYS   A  1 119 ? -17.269 -5.338  -36.852  1.00 22.96  ? 420  CYS   A SG  1 
ATOM   958   N  N   . VAL   A  1 120 ? -17.753 -4.414  -33.387  1.00 19.03  ? 421  VAL   A N   1 
ATOM   959   C  CA  . VAL   A  1 120 ? -19.048 -3.998  -32.855  1.00 23.22  ? 421  VAL   A CA  1 
ATOM   960   C  C   . VAL   A  1 120 ? -20.077 -3.787  -33.946  1.00 25.28  ? 421  VAL   A C   1 
ATOM   961   O  O   . VAL   A  1 120 ? -21.274 -3.671  -33.643  1.00 24.45  ? 421  VAL   A O   1 
ATOM   962   C  CB  . VAL   A  1 120 ? -18.860 -2.714  -32.018  1.00 22.77  ? 421  VAL   A CB  1 
ATOM   963   C  CG1 . VAL   A  1 120 ? -18.599 -1.529  -32.909  1.00 20.37  ? 421  VAL   A CG1 1 
ATOM   964   C  CG2 . VAL   A  1 120 ? -20.063 -2.449  -31.105  1.00 22.99  ? 421  VAL   A CG2 1 
ATOM   965   N  N   . GLY   A  1 121 ? -19.651 -3.749  -35.209  1.00 25.93  ? 422  GLY   A N   1 
ATOM   966   C  CA  . GLY   A  1 121 ? -20.533 -3.465  -36.325  1.00 24.34  ? 422  GLY   A CA  1 
ATOM   967   C  C   . GLY   A  1 121 ? -21.226 -4.662  -36.942  1.00 29.84  ? 422  GLY   A C   1 
ATOM   968   O  O   . GLY   A  1 121 ? -21.896 -4.506  -37.966  1.00 26.69  ? 422  GLY   A O   1 
ATOM   969   N  N   . ARG   A  1 122 ? -21.129 -5.843  -36.331  1.00 27.00  ? 423  ARG   A N   1 
ATOM   970   C  CA  . ARG   A  1 122 ? -21.504 -7.076  -37.012  1.00 24.84  ? 423  ARG   A CA  1 
ATOM   971   C  C   . ARG   A  1 122 ? -22.996 -7.263  -37.210  1.00 24.23  ? 423  ARG   A C   1 
ATOM   972   O  O   . ARG   A  1 122 ? -23.379 -8.247  -37.849  1.00 22.80  ? 423  ARG   A O   1 
ATOM   973   C  CB  . ARG   A  1 122 ? -20.967 -8.289  -36.253  1.00 20.77  ? 423  ARG   A CB  1 
ATOM   974   C  CG  . ARG   A  1 122 ? -19.482 -8.518  -36.461  1.00 20.13  ? 423  ARG   A CG  1 
ATOM   975   C  CD  . ARG   A  1 122 ? -19.061 -9.681  -35.632  1.00 20.81  ? 423  ARG   A CD  1 
ATOM   976   N  NE  . ARG   A  1 122 ? -18.881 -9.335  -34.216  1.00 21.00  ? 423  ARG   A NE  1 
ATOM   977   C  CZ  . ARG   A  1 122 ? -18.831 -10.237 -33.250  1.00 18.91  ? 423  ARG   A CZ  1 
ATOM   978   N  NH1 . ARG   A  1 122 ? -18.974 -11.517 -33.561  1.00 18.37  ? 423  ARG   A NH1 1 
ATOM   979   N  NH2 . ARG   A  1 122 ? -18.627 -9.868  -31.974  1.00 19.14  ? 423  ARG   A NH2 1 
ATOM   980   N  N   . ILE   A  1 123 ? -23.858 -6.383  -36.693  1.00 19.72  ? 424  ILE   A N   1 
ATOM   981   C  CA  . ILE   A  1 123 ? -25.271 -6.548  -37.010  1.00 24.07  ? 424  ILE   A CA  1 
ATOM   982   C  C   . ILE   A  1 123 ? -25.484 -6.456  -38.524  1.00 29.55  ? 424  ILE   A C   1 
ATOM   983   O  O   . ILE   A  1 123 ? -26.468 -6.982  -39.060  1.00 21.60  ? 424  ILE   A O   1 
ATOM   984   C  CB  . ILE   A  1 123 ? -26.120 -5.510  -36.258  1.00 25.88  ? 424  ILE   A CB  1 
ATOM   985   C  CG1 . ILE   A  1 123 ? -27.575 -5.973  -36.212  1.00 28.62  ? 424  ILE   A CG1 1 
ATOM   986   C  CG2 . ILE   A  1 123 ? -25.989 -4.133  -36.911  1.00 23.86  ? 424  ILE   A CG2 1 
ATOM   987   C  CD1 . ILE   A  1 123 ? -28.397 -5.208  -35.225  1.00 31.52  ? 424  ILE   A CD1 1 
ATOM   988   N  N   . GLN   A  1 124 ? -24.536 -5.850  -39.223  1.00 27.05  ? 425  GLN   A N   1 
ATOM   989   C  CA  . GLN   A  1 124 ? -24.550 -5.636  -40.660  1.00 32.61  ? 425  GLN   A CA  1 
ATOM   990   C  C   . GLN   A  1 124 ? -23.958 -6.793  -41.464  1.00 26.27  ? 425  GLN   A C   1 
ATOM   991   O  O   . GLN   A  1 124 ? -23.879 -6.681  -42.693  1.00 27.37  ? 425  GLN   A O   1 
ATOM   992   C  CB  . GLN   A  1 124 ? -23.765 -4.349  -40.968  1.00 31.47  ? 425  GLN   A CB  1 
ATOM   993   C  CG  . GLN   A  1 124 ? -24.401 -3.089  -40.423  1.00 33.74  ? 425  GLN   A CG  1 
ATOM   994   C  CD  . GLN   A  1 124 ? -25.555 -2.655  -41.294  1.00 44.23  ? 425  GLN   A CD  1 
ATOM   995   O  OE1 . GLN   A  1 124 ? -25.536 -2.881  -42.503  1.00 42.94  ? 425  GLN   A OE1 1 
ATOM   996   N  NE2 . GLN   A  1 124 ? -26.570 -2.045  -40.691  1.00 46.19  ? 425  GLN   A NE2 1 
ATOM   997   N  N   . TRP   A  1 125 ? -23.557 -7.891  -40.812  1.00 26.02  ? 426  TRP   A N   1 
ATOM   998   C  CA  . TRP   A  1 125 ? -22.604 -8.828  -41.407  1.00 18.53  ? 426  TRP   A CA  1 
ATOM   999   C  C   . TRP   A  1 125 ? -23.113 -9.431  -42.717  1.00 20.76  ? 426  TRP   A C   1 
ATOM   1000  O  O   . TRP   A  1 125 ? -22.321 -9.697  -43.622  1.00 26.97  ? 426  TRP   A O   1 
ATOM   1001  C  CB  . TRP   A  1 125 ? -22.270 -9.952  -40.423  1.00 20.85  ? 426  TRP   A CB  1 
ATOM   1002  C  CG  . TRP   A  1 125 ? -23.423 -10.893 -40.193  1.00 20.48  ? 426  TRP   A CG  1 
ATOM   1003  C  CD1 . TRP   A  1 125 ? -24.405 -10.758 -39.253  1.00 23.31  ? 426  TRP   A CD1 1 
ATOM   1004  C  CD2 . TRP   A  1 125 ? -23.715 -12.105 -40.910  1.00 17.67  ? 426  TRP   A CD2 1 
ATOM   1005  N  NE1 . TRP   A  1 125 ? -25.286 -11.808 -39.342  1.00 30.32  ? 426  TRP   A NE1 1 
ATOM   1006  C  CE2 . TRP   A  1 125 ? -24.892 -12.641 -40.356  1.00 27.20  ? 426  TRP   A CE2 1 
ATOM   1007  C  CE3 . TRP   A  1 125 ? -23.103 -12.781 -41.972  1.00 20.69  ? 426  TRP   A CE3 1 
ATOM   1008  C  CZ2 . TRP   A  1 125 ? -25.460 -13.825 -40.817  1.00 26.13  ? 426  TRP   A CZ2 1 
ATOM   1009  C  CZ3 . TRP   A  1 125 ? -23.672 -13.961 -42.432  1.00 27.00  ? 426  TRP   A CZ3 1 
ATOM   1010  C  CH2 . TRP   A  1 125 ? -24.844 -14.463 -41.864  1.00 25.43  ? 426  TRP   A CH2 1 
ATOM   1011  N  N   . SER   A  1 126 ? -24.412 -9.700  -42.831  1.00 25.51  ? 427  SER   A N   1 
ATOM   1012  C  CA  . SER   A  1 126 ? -24.858 -10.346 -44.055  1.00 32.43  ? 427  SER   A CA  1 
ATOM   1013  C  C   . SER   A  1 126 ? -25.032 -9.355  -45.198  1.00 27.80  ? 427  SER   A C   1 
ATOM   1014  O  O   . SER   A  1 126 ? -25.214 -9.778  -46.346  1.00 34.94  ? 427  SER   A O   1 
ATOM   1015  C  CB  . SER   A  1 126 ? -26.157 -11.114 -43.813  1.00 36.90  ? 427  SER   A CB  1 
ATOM   1016  O  OG  . SER   A  1 126 ? -27.224 -10.217 -43.586  1.00 40.27  ? 427  SER   A OG  1 
ATOM   1017  N  N   . LYS   A  1 127 ? -24.978 -8.055  -44.906  1.00 28.35  ? 428  LYS   A N   1 
ATOM   1018  C  CA  . LYS   A  1 127 ? -24.983 -7.007  -45.930  1.00 34.02  ? 428  LYS   A CA  1 
ATOM   1019  C  C   . LYS   A  1 127 ? -23.540 -6.608  -46.230  1.00 43.59  ? 428  LYS   A C   1 
ATOM   1020  O  O   . LYS   A  1 127 ? -23.024 -5.588  -45.769  1.00 51.42  ? 428  LYS   A O   1 
ATOM   1021  C  CB  . LYS   A  1 127 ? -25.786 -5.803  -45.466  1.00 34.30  ? 428  LYS   A CB  1 
ATOM   1022  C  CG  . LYS   A  1 127 ? -27.282 -5.895  -45.581  1.00 55.21  ? 428  LYS   A CG  1 
ATOM   1023  C  CD  . LYS   A  1 127 ? -27.860 -4.475  -45.524  1.00 71.62  ? 428  LYS   A CD  1 
ATOM   1024  C  CE  . LYS   A  1 127 ? -27.130 -3.538  -46.510  1.00 73.05  ? 428  LYS   A CE  1 
ATOM   1025  N  NZ  . LYS   A  1 127 ? -27.830 -2.237  -46.727  1.00 70.43  ? 428  LYS   A NZ  1 
ATOM   1026  N  N   . LEU   A  1 128 ? -22.874 -7.459  -46.990  1.00 31.24  ? 429  LEU   A N   1 
ATOM   1027  C  CA  . LEU   A  1 128 ? -21.464 -7.289  -47.302  1.00 19.14  ? 429  LEU   A CA  1 
ATOM   1028  C  C   . LEU   A  1 128 ? -21.326 -7.481  -48.794  1.00 23.82  ? 429  LEU   A C   1 
ATOM   1029  O  O   . LEU   A  1 128 ? -21.699 -8.537  -49.308  1.00 25.29  ? 429  LEU   A O   1 
ATOM   1030  C  CB  . LEU   A  1 128 ? -20.591 -8.304  -46.569  1.00 17.46  ? 429  LEU   A CB  1 
ATOM   1031  C  CG  . LEU   A  1 128 ? -19.138 -8.173  -47.032  1.00 19.77  ? 429  LEU   A CG  1 
ATOM   1032  C  CD1 . LEU   A  1 128 ? -18.629 -6.800  -46.635  1.00 19.73  ? 429  LEU   A CD1 1 
ATOM   1033  C  CD2 . LEU   A  1 128 ? -18.251 -9.265  -46.454  1.00 19.86  ? 429  LEU   A CD2 1 
ATOM   1034  N  N   . GLN   A  1 129 ? -20.829 -6.470  -49.492  1.00 22.04  ? 430  GLN   A N   1 
ATOM   1035  C  CA  . GLN   A  1 129 ? -20.618 -6.618  -50.924  1.00 20.23  ? 430  GLN   A CA  1 
ATOM   1036  C  C   . GLN   A  1 129 ? -19.254 -7.258  -51.127  1.00 23.45  ? 430  GLN   A C   1 
ATOM   1037  O  O   . GLN   A  1 129 ? -18.255 -6.749  -50.619  1.00 25.18  ? 430  GLN   A O   1 
ATOM   1038  C  CB  . GLN   A  1 129 ? -20.713 -5.262  -51.619  1.00 22.63  ? 430  GLN   A CB  1 
ATOM   1039  C  CG  . GLN   A  1 129 ? -20.474 -5.325  -53.111  1.00 30.28  ? 430  GLN   A CG  1 
ATOM   1040  C  CD  . GLN   A  1 129 ? -21.514 -6.137  -53.821  1.00 34.93  ? 430  GLN   A CD  1 
ATOM   1041  O  OE1 . GLN   A  1 129 ? -22.651 -6.238  -53.369  1.00 36.85  ? 430  GLN   A OE1 1 
ATOM   1042  N  NE2 . GLN   A  1 129 ? -21.127 -6.739  -54.936  1.00 47.90  ? 430  GLN   A NE2 1 
ATOM   1043  N  N   . VAL   A  1 130 ? -19.207 -8.388  -51.827  1.00 22.80  ? 431  VAL   A N   1 
ATOM   1044  C  CA  . VAL   A  1 130 ? -17.961 -9.124  -52.015  1.00 21.80  ? 431  VAL   A CA  1 
ATOM   1045  C  C   . VAL   A  1 130 ? -17.506 -8.953  -53.458  1.00 25.60  ? 431  VAL   A C   1 
ATOM   1046  O  O   . VAL   A  1 130 ? -18.195 -9.374  -54.393  1.00 26.91  ? 431  VAL   A O   1 
ATOM   1047  C  CB  . VAL   A  1 130 ? -18.110 -10.610 -51.662  1.00 22.92  ? 431  VAL   A CB  1 
ATOM   1048  C  CG1 . VAL   A  1 130 ? -16.777 -11.330 -51.868  1.00 25.52  ? 431  VAL   A CG1 1 
ATOM   1049  C  CG2 . VAL   A  1 130 ? -18.603 -10.757 -50.210  1.00 17.44  ? 431  VAL   A CG2 1 
ATOM   1050  N  N   . PHE   A  1 131 ? -16.328 -8.372  -53.630  1.00 27.17  ? 432  PHE   A N   1 
ATOM   1051  C  CA  . PHE   A  1 131 ? -15.712 -8.217  -54.930  1.00 25.90  ? 432  PHE   A CA  1 
ATOM   1052  C  C   . PHE   A  1 131 ? -14.664 -9.299  -55.102  1.00 27.31  ? 432  PHE   A C   1 
ATOM   1053  O  O   . PHE   A  1 131 ? -13.679 -9.340  -54.363  1.00 25.21  ? 432  PHE   A O   1 
ATOM   1054  C  CB  . PHE   A  1 131 ? -15.098 -6.833  -55.071  1.00 22.08  ? 432  PHE   A CB  1 
ATOM   1055  C  CG  . PHE   A  1 131 ? -16.105 -5.746  -55.048  1.00 31.37  ? 432  PHE   A CG  1 
ATOM   1056  C  CD1 . PHE   A  1 131 ? -17.071 -5.664  -56.042  1.00 31.54  ? 432  PHE   A CD1 1 
ATOM   1057  C  CD2 . PHE   A  1 131 ? -16.102 -4.806  -54.033  1.00 26.09  ? 432  PHE   A CD2 1 
ATOM   1058  C  CE1 . PHE   A  1 131 ? -18.017 -4.655  -56.021  1.00 34.77  ? 432  PHE   A CE1 1 
ATOM   1059  C  CE2 . PHE   A  1 131 ? -17.037 -3.796  -54.009  1.00 30.51  ? 432  PHE   A CE2 1 
ATOM   1060  C  CZ  . PHE   A  1 131 ? -17.998 -3.715  -54.995  1.00 29.98  ? 432  PHE   A CZ  1 
ATOM   1061  N  N   . ASP   A  1 132 ? -14.886 -10.171 -56.077  1.00 28.30  ? 433  ASP   A N   1 
ATOM   1062  C  CA  . ASP   A  1 132 ? -13.978 -11.274 -56.356  1.00 27.79  ? 433  ASP   A CA  1 
ATOM   1063  C  C   . ASP   A  1 132 ? -12.866 -10.748 -57.251  1.00 33.40  ? 433  ASP   A C   1 
ATOM   1064  O  O   . ASP   A  1 132 ? -13.086 -10.469 -58.430  1.00 27.27  ? 433  ASP   A O   1 
ATOM   1065  C  CB  . ASP   A  1 132 ? -14.744 -12.410 -57.024  1.00 24.86  ? 433  ASP   A CB  1 
ATOM   1066  C  CG  . ASP   A  1 132 ? -13.901 -13.629 -57.267  1.00 24.83  ? 433  ASP   A CG  1 
ATOM   1067  O  OD1 . ASP   A  1 132 ? -14.489 -14.647 -57.685  1.00 33.13  ? 433  ASP   A OD1 1 
ATOM   1068  O  OD2 . ASP   A  1 132 ? -12.675 -13.588 -57.039  1.00 24.68  ? 433  ASP   A OD2 1 
ATOM   1069  N  N   . ALA   A  1 133 ? -11.672 -10.597 -56.696  1.00 32.42  ? 434  ALA   A N   1 
ATOM   1070  C  CA  . ALA   A  1 133 ? -10.525 -10.127 -57.459  1.00 25.34  ? 434  ALA   A CA  1 
ATOM   1071  C  C   . ALA   A  1 133 ? -9.488  -11.231 -57.617  1.00 26.60  ? 434  ALA   A C   1 
ATOM   1072  O  O   . ALA   A  1 133 ? -8.285  -10.965 -57.718  1.00 23.80  ? 434  ALA   A O   1 
ATOM   1073  C  CB  . ALA   A  1 133 ? -9.912  -8.888  -56.800  1.00 20.03  ? 434  ALA   A CB  1 
ATOM   1074  N  N   . ARG   A  1 134 ? -9.945  -12.482 -57.630  1.00 22.39  ? 435  ARG   A N   1 
ATOM   1075  C  CA  . ARG   A  1 134 ? -9.012  -13.591 -57.725  1.00 24.69  ? 435  ARG   A CA  1 
ATOM   1076  C  C   . ARG   A  1 134 ? -8.421  -13.764 -59.121  1.00 24.79  ? 435  ARG   A C   1 
ATOM   1077  O  O   . ARG   A  1 134 ? -7.504  -14.574 -59.287  1.00 27.87  ? 435  ARG   A O   1 
ATOM   1078  C  CB  . ARG   A  1 134 ? -9.707  -14.864 -57.269  1.00 26.73  ? 435  ARG   A CB  1 
ATOM   1079  C  CG  . ARG   A  1 134 ? -9.958  -14.846 -55.756  1.00 22.42  ? 435  ARG   A CG  1 
ATOM   1080  C  CD  . ARG   A  1 134 ? -10.754 -16.055 -55.334  1.00 27.06  ? 435  ARG   A CD  1 
ATOM   1081  N  NE  . ARG   A  1 134 ? -12.072 -16.087 -55.960  1.00 26.17  ? 435  ARG   A NE  1 
ATOM   1082  C  CZ  . ARG   A  1 134 ? -12.829 -17.178 -56.021  1.00 27.68  ? 435  ARG   A CZ  1 
ATOM   1083  N  NH1 . ARG   A  1 134 ? -12.385 -18.318 -55.502  1.00 30.64  ? 435  ARG   A NH1 1 
ATOM   1084  N  NH2 . ARG   A  1 134 ? -14.018 -17.139 -56.610  1.00 26.16  ? 435  ARG   A NH2 1 
ATOM   1085  N  N   . ASP   A  1 135 ? -8.892  -13.017 -60.114  1.00 25.42  ? 436  ASP   A N   1 
ATOM   1086  C  CA  . ASP   A  1 135 ? -8.294  -13.068 -61.444  1.00 26.98  ? 436  ASP   A CA  1 
ATOM   1087  C  C   . ASP   A  1 135 ? -7.172  -12.051 -61.600  1.00 32.39  ? 436  ASP   A C   1 
ATOM   1088  O  O   . ASP   A  1 135 ? -6.528  -12.002 -62.654  1.00 32.74  ? 436  ASP   A O   1 
ATOM   1089  C  CB  . ASP   A  1 135 ? -9.370  -12.850 -62.501  1.00 23.96  ? 436  ASP   A CB  1 
ATOM   1090  C  CG  . ASP   A  1 135 ? -9.945  -11.450 -62.458  1.00 39.81  ? 436  ASP   A CG  1 
ATOM   1091  O  OD1 . ASP   A  1 135 ? -10.599 -11.048 -63.443  1.00 36.95  ? 436  ASP   A OD1 1 
ATOM   1092  O  OD2 . ASP   A  1 135 ? -9.734  -10.746 -61.442  1.00 39.75  ? 436  ASP   A OD2 1 
ATOM   1093  N  N   . CYS   A  1 136 ? -6.919  -11.259 -60.558  1.00 27.34  ? 437  CYS   A N   1 
ATOM   1094  C  CA  . CYS   A  1 136 ? -5.921  -10.202 -60.613  1.00 27.68  ? 437  CYS   A CA  1 
ATOM   1095  C  C   . CYS   A  1 136 ? -4.516  -10.794 -60.695  1.00 31.08  ? 437  CYS   A C   1 
ATOM   1096  O  O   . CYS   A  1 136 ? -4.230  -11.851 -60.126  1.00 34.54  ? 437  CYS   A O   1 
ATOM   1097  C  CB  . CYS   A  1 136 ? -6.062  -9.301  -59.381  1.00 25.12  ? 437  CYS   A CB  1 
ATOM   1098  S  SG  . CYS   A  1 136 ? -4.991  -7.869  -59.380  1.00 31.12  ? 437  CYS   A SG  1 
ATOM   1099  N  N   . THR   A  1 137 ? -3.634  -10.121 -61.439  1.00 29.03  ? 438  THR   A N   1 
ATOM   1100  C  CA  . THR   A  1 137 ? -2.279  -10.621 -61.637  1.00 23.31  ? 438  THR   A CA  1 
ATOM   1101  C  C   . THR   A  1 137 ? -1.176  -9.595  -61.426  1.00 26.23  ? 438  THR   A C   1 
ATOM   1102  O  O   . THR   A  1 137 ? -0.008  -9.989  -61.392  1.00 30.42  ? 438  THR   A O   1 
ATOM   1103  C  CB  . THR   A  1 137 ? -2.100  -11.193 -63.060  1.00 31.30  ? 438  THR   A CB  1 
ATOM   1104  O  OG1 . THR   A  1 137 ? -2.013  -10.118 -64.009  1.00 32.09  ? 438  THR   A OG1 1 
ATOM   1105  C  CG2 . THR   A  1 137 ? -3.255  -12.125 -63.446  1.00 30.81  ? 438  THR   A CG2 1 
ATOM   1106  N  N   . THR   A  1 138 ? -1.484  -8.304  -61.323  1.00 24.32  ? 439  THR   A N   1 
ATOM   1107  C  CA  . THR   A  1 138 ? -0.452  -7.274  -61.227  1.00 23.82  ? 439  THR   A CA  1 
ATOM   1108  C  C   . THR   A  1 138 ? -0.891  -6.221  -60.215  1.00 24.62  ? 439  THR   A C   1 
ATOM   1109  O  O   . THR   A  1 138 ? -2.080  -6.082  -59.911  1.00 25.33  ? 439  THR   A O   1 
ATOM   1110  C  CB  . THR   A  1 138 ? -0.188  -6.583  -62.581  1.00 30.32  ? 439  THR   A CB  1 
ATOM   1111  O  OG1 . THR   A  1 138 ? -1.370  -5.878  -62.973  1.00 29.30  ? 439  THR   A OG1 1 
ATOM   1112  C  CG2 . THR   A  1 138 ? 0.182   -7.585  -63.674  1.00 28.75  ? 439  THR   A CG2 1 
ATOM   1113  N  N   . ALA   A  1 139 ? 0.081   -5.467  -59.693  1.00 31.93  ? 440  ALA   A N   1 
ATOM   1114  C  CA  . ALA   A  1 139 ? -0.259  -4.367  -58.795  1.00 28.54  ? 440  ALA   A CA  1 
ATOM   1115  C  C   . ALA   A  1 139 ? -1.180  -3.356  -59.476  1.00 24.59  ? 440  ALA   A C   1 
ATOM   1116  O  O   . ALA   A  1 139 ? -2.047  -2.764  -58.820  1.00 22.77  ? 440  ALA   A O   1 
ATOM   1117  C  CB  . ALA   A  1 139 ? 1.012   -3.683  -58.285  1.00 24.80  ? 440  ALA   A CB  1 
ATOM   1118  N  N   . HIS   A  1 140 ? -1.015  -3.153  -60.791  1.00 24.90  ? 441  HIS   A N   1 
ATOM   1119  C  CA  . HIS   A  1 140 ? -1.931  -2.285  -61.535  1.00 28.56  ? 441  HIS   A CA  1 
ATOM   1120  C  C   . HIS   A  1 140 ? -3.364  -2.797  -61.466  1.00 24.09  ? 441  HIS   A C   1 
ATOM   1121  O  O   . HIS   A  1 140 ? -4.299  -2.024  -61.232  1.00 29.84  ? 441  HIS   A O   1 
ATOM   1122  C  CB  . HIS   A  1 140 ? -1.485  -2.169  -63.001  1.00 24.35  ? 441  HIS   A CB  1 
ATOM   1123  C  CG  . HIS   A  1 140 ? -0.477  -1.093  -63.246  1.00 27.61  ? 441  HIS   A CG  1 
ATOM   1124  N  ND1 . HIS   A  1 140 ? 0.878   -1.290  -63.104  1.00 30.59  ? 441  HIS   A ND1 1 
ATOM   1125  C  CD2 . HIS   A  1 140 ? -0.629  0.190   -63.657  1.00 31.87  ? 441  HIS   A CD2 1 
ATOM   1126  C  CE1 . HIS   A  1 140 ? 1.518   -0.173  -63.402  1.00 32.91  ? 441  HIS   A CE1 1 
ATOM   1127  N  NE2 . HIS   A  1 140 ? 0.626   0.740   -63.743  1.00 32.40  ? 441  HIS   A NE2 1 
ATOM   1128  N  N   . GLY   A  1 141 ? -3.562  -4.096  -61.701  1.00 23.39  ? 442  GLY   A N   1 
ATOM   1129  C  CA  . GLY   A  1 141 ? -4.888  -4.670  -61.527  1.00 21.60  ? 442  GLY   A CA  1 
ATOM   1130  C  C   . GLY   A  1 141 ? -5.402  -4.543  -60.098  1.00 25.18  ? 442  GLY   A C   1 
ATOM   1131  O  O   . GLY   A  1 141 ? -6.599  -4.343  -59.873  1.00 26.88  ? 442  GLY   A O   1 
ATOM   1132  N  N   . MET   A  1 142 ? -4.508  -4.662  -59.114  1.00 25.02  ? 443  MET   A N   1 
ATOM   1133  C  CA  . MET   A  1 142 ? -4.923  -4.483  -57.720  1.00 23.55  ? 443  MET   A CA  1 
ATOM   1134  C  C   . MET   A  1 142 ? -5.373  -3.056  -57.475  1.00 23.11  ? 443  MET   A C   1 
ATOM   1135  O  O   . MET   A  1 142 ? -6.346  -2.816  -56.757  1.00 23.10  ? 443  MET   A O   1 
ATOM   1136  C  CB  . MET   A  1 142 ? -3.781  -4.820  -56.773  1.00 23.96  ? 443  MET   A CB  1 
ATOM   1137  C  CG  . MET   A  1 142 ? -3.380  -6.266  -56.748  1.00 28.34  ? 443  MET   A CG  1 
ATOM   1138  S  SD  . MET   A  1 142 ? -1.958  -6.495  -55.664  1.00 31.64  ? 443  MET   A SD  1 
ATOM   1139  C  CE  . MET   A  1 142 ? -2.641  -6.164  -54.041  1.00 27.33  ? 443  MET   A CE  1 
ATOM   1140  N  N   . PHE   A  1 143 ? -4.667  -2.094  -58.066  1.00 27.64  ? 444  PHE   A N   1 
ATOM   1141  C  CA  . PHE   A  1 143 ? -5.053  -0.696  -57.951  1.00 22.53  ? 444  PHE   A CA  1 
ATOM   1142  C  C   . PHE   A  1 143 ? -6.441  -0.459  -58.529  1.00 26.82  ? 444  PHE   A C   1 
ATOM   1143  O  O   . PHE   A  1 143 ? -7.285  0.197   -57.907  1.00 25.73  ? 444  PHE   A O   1 
ATOM   1144  C  CB  . PHE   A  1 143 ? -4.013  0.165   -58.664  1.00 21.62  ? 444  PHE   A CB  1 
ATOM   1145  C  CG  . PHE   A  1 143 ? -4.386  1.599   -58.742  1.00 32.85  ? 444  PHE   A CG  1 
ATOM   1146  C  CD1 . PHE   A  1 143 ? -4.705  2.175   -59.959  1.00 26.20  ? 444  PHE   A CD1 1 
ATOM   1147  C  CD2 . PHE   A  1 143 ? -4.454  2.370   -57.592  1.00 31.81  ? 444  PHE   A CD2 1 
ATOM   1148  C  CE1 . PHE   A  1 143 ? -5.060  3.509   -60.039  1.00 30.93  ? 444  PHE   A CE1 1 
ATOM   1149  C  CE2 . PHE   A  1 143 ? -4.795  3.698   -57.662  1.00 31.76  ? 444  PHE   A CE2 1 
ATOM   1150  C  CZ  . PHE   A  1 143 ? -5.105  4.270   -58.885  1.00 35.21  ? 444  PHE   A CZ  1 
ATOM   1151  N  N   . ASN   A  1 144 ? -6.676  -0.955  -59.746  1.00 20.94  ? 445  ASN   A N   1 
ATOM   1152  C  CA  . ASN   A  1 144 ? -8.000  -0.881  -60.365  1.00 22.10  ? 445  ASN   A CA  1 
ATOM   1153  C  C   . ASN   A  1 144 ? -9.082  -1.452  -59.446  1.00 19.73  ? 445  ASN   A C   1 
ATOM   1154  O  O   . ASN   A  1 144 ? -10.116 -0.815  -59.198  1.00 25.60  ? 445  ASN   A O   1 
ATOM   1155  C  CB  . ASN   A  1 144 ? -7.970  -1.642  -61.699  1.00 29.87  ? 445  ASN   A CB  1 
ATOM   1156  C  CG  . ASN   A  1 144 ? -9.207  -1.403  -62.537  1.00 38.71  ? 445  ASN   A CG  1 
ATOM   1157  O  OD1 . ASN   A  1 144 ? -9.692  -0.278  -62.619  1.00 43.42  ? 445  ASN   A OD1 1 
ATOM   1158  N  ND2 . ASN   A  1 144 ? -9.719  -2.455  -63.171  1.00 37.10  ? 445  ASN   A ND2 1 
ATOM   1159  N  N   . TYR   A  1 145 ? -8.862  -2.672  -58.950  1.00 20.26  ? 446  TYR   A N   1 
ATOM   1160  C  CA  . TYR   A  1 145 ? -9.824  -3.293  -58.042  1.00 28.17  ? 446  TYR   A CA  1 
ATOM   1161  C  C   . TYR   A  1 145 ? -10.033 -2.458  -56.786  1.00 27.77  ? 446  TYR   A C   1 
ATOM   1162  O  O   . TYR   A  1 145 ? -11.165 -2.308  -56.305  1.00 21.58  ? 446  TYR   A O   1 
ATOM   1163  C  CB  . TYR   A  1 145 ? -9.346  -4.691  -57.660  1.00 25.83  ? 446  TYR   A CB  1 
ATOM   1164  C  CG  . TYR   A  1 145 ? -9.860  -5.768  -58.569  1.00 25.22  ? 446  TYR   A CG  1 
ATOM   1165  C  CD1 . TYR   A  1 145 ? -8.996  -6.497  -59.368  1.00 24.35  ? 446  TYR   A CD1 1 
ATOM   1166  C  CD2 . TYR   A  1 145 ? -11.209 -6.062  -58.623  1.00 26.94  ? 446  TYR   A CD2 1 
ATOM   1167  C  CE1 . TYR   A  1 145 ? -9.465  -7.506  -60.199  1.00 23.35  ? 446  TYR   A CE1 1 
ATOM   1168  C  CE2 . TYR   A  1 145 ? -11.692 -7.059  -59.456  1.00 25.53  ? 446  TYR   A CE2 1 
ATOM   1169  C  CZ  . TYR   A  1 145 ? -10.820 -7.779  -60.232  1.00 25.38  ? 446  TYR   A CZ  1 
ATOM   1170  O  OH  . TYR   A  1 145 ? -11.308 -8.772  -61.051  1.00 31.42  ? 446  TYR   A OH  1 
ATOM   1171  N  N   . ILE   A  1 146 ? -8.953  -1.919  -56.233  1.00 25.21  ? 447  ILE   A N   1 
ATOM   1172  C  CA  . ILE   A  1 146 ? -9.080  -1.153  -55.001  1.00 28.16  ? 447  ILE   A CA  1 
ATOM   1173  C  C   . ILE   A  1 146 ? -9.816  0.152   -55.261  1.00 28.00  ? 447  ILE   A C   1 
ATOM   1174  O  O   . ILE   A  1 146 ? -10.683 0.553   -54.480  1.00 24.26  ? 447  ILE   A O   1 
ATOM   1175  C  CB  . ILE   A  1 146 ? -7.694  -0.931  -54.379  1.00 27.88  ? 447  ILE   A CB  1 
ATOM   1176  C  CG1 . ILE   A  1 146 ? -7.224  -2.252  -53.759  1.00 24.55  ? 447  ILE   A CG1 1 
ATOM   1177  C  CG2 . ILE   A  1 146 ? -7.744  0.192   -53.342  1.00 27.56  ? 447  ILE   A CG2 1 
ATOM   1178  C  CD1 . ILE   A  1 146 ? -5.772  -2.280  -53.414  1.00 22.99  ? 447  ILE   A CD1 1 
ATOM   1179  N  N   . CYS   A  1 147 ? -9.522  0.810   -56.386  1.00 24.42  ? 448  CYS   A N   1 
ATOM   1180  C  CA  . CYS   A  1 147 ? -10.242 2.031   -56.722  1.00 23.91  ? 448  CYS   A CA  1 
ATOM   1181  C  C   . CYS   A  1 147 ? -11.727 1.768   -56.863  1.00 26.97  ? 448  CYS   A C   1 
ATOM   1182  O  O   . CYS   A  1 147 ? -12.552 2.557   -56.391  1.00 27.31  ? 448  CYS   A O   1 
ATOM   1183  C  CB  . CYS   A  1 147 ? -9.698  2.630   -58.014  1.00 27.31  ? 448  CYS   A CB  1 
ATOM   1184  S  SG  . CYS   A  1 147 ? -8.122  3.391   -57.772  1.00 33.75  ? 448  CYS   A SG  1 
ATOM   1185  N  N   . ASN   A  1 148 ? -12.084 0.676   -57.540  1.00 22.40  ? 449  ASN   A N   1 
ATOM   1186  C  CA  . ASN   A  1 148 ? -13.487 0.325   -57.682  1.00 22.60  ? 449  ASN   A CA  1 
ATOM   1187  C  C   . ASN   A  1 148 ? -14.119 0.055   -56.323  1.00 18.29  ? 449  ASN   A C   1 
ATOM   1188  O  O   . ASN   A  1 148 ? -15.247 0.485   -56.057  1.00 23.06  ? 449  ASN   A O   1 
ATOM   1189  C  CB  . ASN   A  1 148 ? -13.616 -0.875  -58.613  1.00 18.96  ? 449  ASN   A CB  1 
ATOM   1190  C  CG  . ASN   A  1 148 ? -13.192 -0.537  -60.044  1.00 28.49  ? 449  ASN   A CG  1 
ATOM   1191  O  OD1 . ASN   A  1 148 ? -13.103 0.638   -60.416  1.00 24.59  ? 449  ASN   A OD1 1 
ATOM   1192  N  ND2 . ASN   A  1 148 ? -12.935 -1.559  -60.846  1.00 26.88  ? 449  ASN   A ND2 1 
ATOM   1193  N  N   . HIS   A  1 149 ? -13.403 -0.660  -55.456  1.00 19.87  ? 450  HIS   A N   1 
ATOM   1194  C  CA  . HIS   A  1 149 ? -13.872 -0.889  -54.092  1.00 24.77  ? 450  HIS   A CA  1 
ATOM   1195  C  C   . HIS   A  1 149 ? -14.135 0.434   -53.383  1.00 21.96  ? 450  HIS   A C   1 
ATOM   1196  O  O   . HIS   A  1 149 ? -15.246 0.691   -52.904  1.00 22.42  ? 450  HIS   A O   1 
ATOM   1197  C  CB  . HIS   A  1 149 ? -12.825 -1.723  -53.349  1.00 21.93  ? 450  HIS   A CB  1 
ATOM   1198  C  CG  . HIS   A  1 149 ? -13.161 -2.013  -51.915  1.00 25.98  ? 450  HIS   A CG  1 
ATOM   1199  N  ND1 . HIS   A  1 149 ? -13.036 -3.271  -51.374  1.00 22.56  ? 450  HIS   A ND1 1 
ATOM   1200  C  CD2 . HIS   A  1 149 ? -13.586 -1.213  -50.906  1.00 23.15  ? 450  HIS   A CD2 1 
ATOM   1201  C  CE1 . HIS   A  1 149 ? -13.374 -3.237  -50.094  1.00 27.14  ? 450  HIS   A CE1 1 
ATOM   1202  N  NE2 . HIS   A  1 149 ? -13.721 -2.001  -49.789  1.00 23.47  ? 450  HIS   A NE2 1 
ATOM   1203  N  N   . VAL   A  1 150 ? -13.122 1.298   -53.336  1.00 18.81  ? 451  VAL   A N   1 
ATOM   1204  C  CA  . VAL   A  1 150 ? -13.251 2.575   -52.640  1.00 19.61  ? 451  VAL   A CA  1 
ATOM   1205  C  C   . VAL   A  1 150 ? -14.421 3.376   -53.191  1.00 27.05  ? 451  VAL   A C   1 
ATOM   1206  O  O   . VAL   A  1 150 ? -15.189 3.983   -52.435  1.00 18.78  ? 451  VAL   A O   1 
ATOM   1207  C  CB  . VAL   A  1 150 ? -11.931 3.361   -52.743  1.00 23.21  ? 451  VAL   A CB  1 
ATOM   1208  C  CG1 . VAL   A  1 150 ? -12.121 4.811   -52.273  1.00 18.78  ? 451  VAL   A CG1 1 
ATOM   1209  C  CG2 . VAL   A  1 150 ? -10.855 2.648   -51.940  1.00 21.51  ? 451  VAL   A CG2 1 
ATOM   1210  N  N   . LYS   A  1 151 ? -14.582 3.392   -54.522  1.00 27.45  ? 452  LYS   A N   1 
ATOM   1211  C  CA  . LYS   A  1 151 ? -15.668 4.169   -55.104  1.00 25.63  ? 452  LYS   A CA  1 
ATOM   1212  C  C   . LYS   A  1 151 ? -17.020 3.559   -54.766  1.00 21.96  ? 452  LYS   A C   1 
ATOM   1213  O  O   . LYS   A  1 151 ? -17.955 4.280   -54.403  1.00 20.88  ? 452  LYS   A O   1 
ATOM   1214  C  CB  . LYS   A  1 151 ? -15.494 4.275   -56.618  1.00 31.07  ? 452  LYS   A CB  1 
ATOM   1215  C  CG  . LYS   A  1 151 ? -16.476 5.202   -57.287  1.00 26.71  ? 452  LYS   A CG  1 
ATOM   1216  C  CD  . LYS   A  1 151 ? -16.152 5.287   -58.804  1.00 30.64  ? 452  LYS   A CD  1 
ATOM   1217  C  CE  . LYS   A  1 151 ? -16.859 6.457   -59.443  1.00 34.40  ? 452  LYS   A CE  1 
ATOM   1218  N  NZ  . LYS   A  1 151 ? -16.410 6.699   -60.850  1.00 33.61  ? 452  LYS   A NZ  1 
ATOM   1219  N  N   . TYR   A  1 152 ? -17.137 2.235   -54.886  1.00 19.65  ? 453  TYR   A N   1 
ATOM   1220  C  CA  . TYR   A  1 152 ? -18.368 1.560   -54.500  1.00 26.76  ? 453  TYR   A CA  1 
ATOM   1221  C  C   . TYR   A  1 152 ? -18.663 1.782   -53.028  1.00 18.21  ? 453  TYR   A C   1 
ATOM   1222  O  O   . TYR   A  1 152 ? -19.781 2.154   -52.653  1.00 25.42  ? 453  TYR   A O   1 
ATOM   1223  C  CB  . TYR   A  1 152 ? -18.271 0.057   -54.773  1.00 19.23  ? 453  TYR   A CB  1 
ATOM   1224  C  CG  . TYR   A  1 152 ? -19.498 -0.662  -54.278  1.00 27.26  ? 453  TYR   A CG  1 
ATOM   1225  C  CD1 . TYR   A  1 152 ? -20.612 -0.797  -55.096  1.00 29.81  ? 453  TYR   A CD1 1 
ATOM   1226  C  CD2 . TYR   A  1 152 ? -19.564 -1.172  -52.981  1.00 23.18  ? 453  TYR   A CD2 1 
ATOM   1227  C  CE1 . TYR   A  1 152 ? -21.743 -1.425  -54.646  1.00 32.60  ? 453  TYR   A CE1 1 
ATOM   1228  C  CE2 . TYR   A  1 152 ? -20.699 -1.793  -52.527  1.00 26.36  ? 453  TYR   A CE2 1 
ATOM   1229  C  CZ  . TYR   A  1 152 ? -21.778 -1.919  -53.363  1.00 32.35  ? 453  TYR   A CZ  1 
ATOM   1230  O  OH  . TYR   A  1 152 ? -22.907 -2.548  -52.913  1.00 43.34  ? 453  TYR   A OH  1 
ATOM   1231  N  N   . ALA   A  1 153 ? -17.670 1.513   -52.182  1.00 21.34  ? 454  ALA   A N   1 
ATOM   1232  C  CA  . ALA   A  1 153 ? -17.866 1.600   -50.734  1.00 22.41  ? 454  ALA   A CA  1 
ATOM   1233  C  C   . ALA   A  1 153 ? -18.220 3.016   -50.307  1.00 22.49  ? 454  ALA   A C   1 
ATOM   1234  O  O   . ALA   A  1 153 ? -19.039 3.215   -49.406  1.00 29.69  ? 454  ALA   A O   1 
ATOM   1235  C  CB  . ALA   A  1 153 ? -16.601 1.143   -50.005  1.00 16.82  ? 454  ALA   A CB  1 
ATOM   1236  N  N   . THR   A  1 154 ? -17.596 4.014   -50.931  1.00 27.89  ? 455  THR   A N   1 
ATOM   1237  C  CA  . THR   A  1 154 ? -17.837 5.392   -50.523  1.00 27.37  ? 455  THR   A CA  1 
ATOM   1238  C  C   . THR   A  1 154 ? -19.236 5.833   -50.915  1.00 30.39  ? 455  THR   A C   1 
ATOM   1239  O  O   . THR   A  1 154 ? -20.005 6.304   -50.067  1.00 23.85  ? 455  THR   A O   1 
ATOM   1240  C  CB  . THR   A  1 154 ? -16.777 6.311   -51.129  1.00 28.88  ? 455  THR   A CB  1 
ATOM   1241  O  OG1 . THR   A  1 154 ? -15.492 5.954   -50.591  1.00 23.77  ? 455  THR   A OG1 1 
ATOM   1242  C  CG2 . THR   A  1 154 ? -17.082 7.777   -50.822  1.00 23.28  ? 455  THR   A CG2 1 
ATOM   1243  N  N   . ASN   A  1 155 ? -19.589 5.682   -52.201  1.00 28.17  ? 456  ASN   A N   1 
ATOM   1244  C  CA  . ASN   A  1 155 ? -20.967 5.882   -52.637  1.00 28.57  ? 456  ASN   A CA  1 
ATOM   1245  C  C   . ASN   A  1 155 ? -21.441 7.279   -52.253  1.00 29.58  ? 456  ASN   A C   1 
ATOM   1246  O  O   . ASN   A  1 155 ? -22.534 7.462   -51.707  1.00 28.58  ? 456  ASN   A O   1 
ATOM   1247  C  CB  . ASN   A  1 155 ? -21.877 4.796   -52.048  1.00 30.29  ? 456  ASN   A CB  1 
ATOM   1248  C  CG  . ASN   A  1 155 ? -23.284 4.817   -52.625  1.00 36.00  ? 456  ASN   A CG  1 
ATOM   1249  O  OD1 . ASN   A  1 155 ? -23.486 5.129   -53.794  1.00 34.60  ? 456  ASN   A OD1 1 
ATOM   1250  N  ND2 . ASN   A  1 155 ? -24.263 4.481   -51.797  1.00 26.33  ? 456  ASN   A ND2 1 
ATOM   1251  N  N   . LYS   A  1 156 ? -20.566 8.259   -52.479  1.00 24.45  ? 457  LYS   A N   1 
ATOM   1252  C  CA  . LYS   A  1 156 ? -20.849 9.670   -52.232  1.00 26.35  ? 457  LYS   A CA  1 
ATOM   1253  C  C   . LYS   A  1 156 ? -21.300 9.923   -50.794  1.00 28.46  ? 457  LYS   A C   1 
ATOM   1254  O  O   . LYS   A  1 156 ? -22.125 10.803  -50.537  1.00 33.69  ? 457  LYS   A O   1 
ATOM   1255  C  CB  . LYS   A  1 156 ? -21.885 10.202  -53.228  1.00 25.85  ? 457  LYS   A CB  1 
ATOM   1256  C  CG  . LYS   A  1 156 ? -21.472 10.020  -54.682  1.00 32.88  ? 457  LYS   A CG  1 
ATOM   1257  C  CD  . LYS   A  1 156 ? -22.562 10.524  -55.619  1.00 40.00  ? 457  LYS   A CD  1 
ATOM   1258  C  CE  . LYS   A  1 156 ? -22.097 10.535  -57.070  1.00 49.30  ? 457  LYS   A CE  1 
ATOM   1259  N  NZ  . LYS   A  1 156 ? -20.765 11.200  -57.179  1.00 50.06  ? 457  LYS   A NZ  1 
ATOM   1260  N  N   . GLY   A  1 157 ? -20.762 9.153   -49.843  1.00 29.82  ? 458  GLY   A N   1 
ATOM   1261  C  CA  . GLY   A  1 157 ? -21.015 9.359   -48.430  1.00 26.29  ? 458  GLY   A CA  1 
ATOM   1262  C  C   . GLY   A  1 157 ? -22.041 8.425   -47.836  1.00 29.23  ? 458  GLY   A C   1 
ATOM   1263  O  O   . GLY   A  1 157 ? -22.151 8.337   -46.604  1.00 30.48  ? 458  GLY   A O   1 
ATOM   1264  N  N   . ASN   A  1 158 ? -22.807 7.739   -48.675  1.00 26.74  ? 459  ASN   A N   1 
ATOM   1265  C  CA  . ASN   A  1 158 ? -23.720 6.705   -48.210  1.00 28.89  ? 459  ASN   A CA  1 
ATOM   1266  C  C   . ASN   A  1 158 ? -22.953 5.381   -48.197  1.00 31.20  ? 459  ASN   A C   1 
ATOM   1267  O  O   . ASN   A  1 158 ? -23.128 4.519   -49.058  1.00 31.96  ? 459  ASN   A O   1 
ATOM   1268  C  CB  . ASN   A  1 158 ? -24.948 6.656   -49.107  1.00 27.85  ? 459  ASN   A CB  1 
ATOM   1269  C  CG  . ASN   A  1 158 ? -26.024 5.753   -48.552  1.00 40.40  ? 459  ASN   A CG  1 
ATOM   1270  O  OD1 . ASN   A  1 158 ? -26.031 5.453   -47.359  1.00 37.01  ? 459  ASN   A OD1 1 
ATOM   1271  N  ND2 . ASN   A  1 158 ? -26.941 5.316   -49.411  1.00 45.35  ? 459  ASN   A ND2 1 
ATOM   1272  N  N   . LEU   A  1 159 ? -22.077 5.227   -47.198  1.00 23.81  ? 460  LEU   A N   1 
ATOM   1273  C  CA  . LEU   A  1 159 ? -21.081 4.158   -47.234  1.00 26.23  ? 460  LEU   A CA  1 
ATOM   1274  C  C   . LEU   A  1 159 ? -21.740 2.783   -47.266  1.00 23.55  ? 460  LEU   A C   1 
ATOM   1275  O  O   . LEU   A  1 159 ? -22.803 2.557   -46.683  1.00 27.31  ? 460  LEU   A O   1 
ATOM   1276  C  CB  . LEU   A  1 159 ? -20.130 4.224   -46.032  1.00 22.50  ? 460  LEU   A CB  1 
ATOM   1277  C  CG  . LEU   A  1 159 ? -19.418 5.544   -45.752  1.00 39.93  ? 460  LEU   A CG  1 
ATOM   1278  C  CD1 . LEU   A  1 159 ? -18.197 5.335   -44.877  1.00 41.65  ? 460  LEU   A CD1 1 
ATOM   1279  C  CD2 . LEU   A  1 159 ? -19.023 6.191   -47.028  1.00 31.53  ? 460  LEU   A CD2 1 
ATOM   1280  N  N   . ARG   A  1 160 ? -21.082 1.858   -47.958  1.00 21.00  ? 461  ARG   A N   1 
ATOM   1281  C  CA  . ARG   A  1 160 ? -21.570 0.502   -48.124  1.00 19.38  ? 461  ARG   A CA  1 
ATOM   1282  C  C   . ARG   A  1 160 ? -20.423 -0.427  -47.800  1.00 25.31  ? 461  ARG   A C   1 
ATOM   1283  O  O   . ARG   A  1 160 ? -19.299 -0.194  -48.253  1.00 22.88  ? 461  ARG   A O   1 
ATOM   1284  C  CB  . ARG   A  1 160 ? -22.057 0.264   -49.560  1.00 23.57  ? 461  ARG   A CB  1 
ATOM   1285  C  CG  . ARG   A  1 160 ? -23.280 1.067   -49.948  1.00 30.80  ? 461  ARG   A CG  1 
ATOM   1286  C  CD  . ARG   A  1 160 ? -23.723 0.708   -51.375  1.00 29.43  ? 461  ARG   A CD  1 
ATOM   1287  N  NE  . ARG   A  1 160 ? -22.869 1.323   -52.384  1.00 27.18  ? 461  ARG   A NE  1 
ATOM   1288  C  CZ  . ARG   A  1 160 ? -23.231 1.468   -53.652  1.00 32.24  ? 461  ARG   A CZ  1 
ATOM   1289  N  NH1 . ARG   A  1 160 ? -24.417 1.023   -54.047  1.00 31.24  ? 461  ARG   A NH1 1 
ATOM   1290  N  NH2 . ARG   A  1 160 ? -22.418 2.053   -54.519  1.00 22.55  ? 461  ARG   A NH2 1 
ATOM   1291  N  N   . SER   A  1 161 ? -20.688 -1.455  -47.000  1.00 22.77  ? 462  SER   A N   1 
ATOM   1292  C  CA  A SER   A  1 161 ? -19.627 -2.370  -46.611  0.50 24.83  ? 462  SER   A CA  1 
ATOM   1293  C  CA  B SER   A  1 161 ? -19.627 -2.370  -46.612  0.50 24.87  ? 462  SER   A CA  1 
ATOM   1294  C  C   . SER   A  1 161 ? -19.192 -3.206  -47.807  1.00 26.22  ? 462  SER   A C   1 
ATOM   1295  O  O   . SER   A  1 161 ? -20.015 -3.670  -48.597  1.00 22.00  ? 462  SER   A O   1 
ATOM   1296  C  CB  A SER   A  1 161 ? -20.096 -3.277  -45.476  0.50 21.56  ? 462  SER   A CB  1 
ATOM   1297  C  CB  B SER   A  1 161 ? -20.093 -3.276  -45.472  0.50 21.56  ? 462  SER   A CB  1 
ATOM   1298  O  OG  A SER   A  1 161 ? -21.182 -4.073  -45.904  0.50 18.07  ? 462  SER   A OG  1 
ATOM   1299  O  OG  B SER   A  1 161 ? -20.614 -2.505  -44.410  0.50 17.17  ? 462  SER   A OG  1 
ATOM   1300  N  N   . ALA   A  1 162 ? -17.885 -3.406  -47.939  1.00 20.39  ? 463  ALA   A N   1 
ATOM   1301  C  CA  . ALA   A  1 162 ? -17.402 -4.176  -49.065  1.00 18.78  ? 463  ALA   A CA  1 
ATOM   1302  C  C   . ALA   A  1 162 ? -16.096 -4.843  -48.700  1.00 24.33  ? 463  ALA   A C   1 
ATOM   1303  O  O   . ALA   A  1 162 ? -15.384 -4.405  -47.792  1.00 18.45  ? 463  ALA   A O   1 
ATOM   1304  C  CB  . ALA   A  1 162 ? -17.191 -3.287  -50.301  1.00 19.49  ? 463  ALA   A CB  1 
ATOM   1305  N  N   . ILE   A  1 163 ? -15.784 -5.901  -49.435  1.00 18.56  ? 464  ILE   A N   1 
ATOM   1306  C  CA  . ILE   A  1 163 ? -14.491 -6.562  -49.325  1.00 18.86  ? 464  ILE   A CA  1 
ATOM   1307  C  C   . ILE   A  1 163 ? -14.067 -6.934  -50.734  1.00 25.03  ? 464  ILE   A C   1 
ATOM   1308  O  O   . ILE   A  1 163 ? -14.890 -7.366  -51.548  1.00 20.76  ? 464  ILE   A O   1 
ATOM   1309  C  CB  . ILE   A  1 163 ? -14.538 -7.804  -48.402  1.00 16.37  ? 464  ILE   A CB  1 
ATOM   1310  C  CG1 . ILE   A  1 163 ? -13.153 -8.430  -48.282  1.00 15.47  ? 464  ILE   A CG1 1 
ATOM   1311  C  CG2 . ILE   A  1 163 ? -15.548 -8.845  -48.928  1.00 15.74  ? 464  ILE   A CG2 1 
ATOM   1312  C  CD1 . ILE   A  1 163 ? -13.013 -9.435  -47.097  1.00 17.02  ? 464  ILE   A CD1 1 
ATOM   1313  N  N   . THR   A  1 164 ? -12.790 -6.735  -51.031  1.00 20.32  ? 465  THR   A N   1 
ATOM   1314  C  CA  . THR   A  1 164 ? -12.208 -7.153  -52.293  1.00 22.99  ? 465  THR   A CA  1 
ATOM   1315  C  C   . THR   A  1 164 ? -11.173 -8.221  -51.991  1.00 25.34  ? 465  THR   A C   1 
ATOM   1316  O  O   . THR   A  1 164 ? -10.283 -8.003  -51.163  1.00 23.82  ? 465  THR   A O   1 
ATOM   1317  C  CB  . THR   A  1 164 ? -11.577 -5.966  -53.023  1.00 21.94  ? 465  THR   A CB  1 
ATOM   1318  O  OG1 . THR   A  1 164 ? -12.601 -5.008  -53.296  1.00 22.28  ? 465  THR   A OG1 1 
ATOM   1319  C  CG2 . THR   A  1 164 ? -10.918 -6.424  -54.322  1.00 22.80  ? 465  THR   A CG2 1 
ATOM   1320  N  N   . ILE   A  1 165 ? -11.297 -9.372  -52.647  1.00 18.75  ? 466  ILE   A N   1 
ATOM   1321  C  CA  . ILE   A  1 165 ? -10.528 -10.553 -52.291  1.00 22.57  ? 466  ILE   A CA  1 
ATOM   1322  C  C   . ILE   A  1 165 ? -9.611  -10.911 -53.453  1.00 20.24  ? 466  ILE   A C   1 
ATOM   1323  O  O   . ILE   A  1 165 ? -10.066 -11.348 -54.522  1.00 25.70  ? 466  ILE   A O   1 
ATOM   1324  C  CB  . ILE   A  1 165 ? -11.435 -11.724 -51.894  1.00 29.81  ? 466  ILE   A CB  1 
ATOM   1325  C  CG1 . ILE   A  1 165 ? -12.282 -11.337 -50.673  1.00 23.49  ? 466  ILE   A CG1 1 
ATOM   1326  C  CG2 . ILE   A  1 165 ? -10.603 -12.922 -51.518  1.00 29.50  ? 466  ILE   A CG2 1 
ATOM   1327  C  CD1 . ILE   A  1 165 ? -13.344 -12.348 -50.330  1.00 20.78  ? 466  ILE   A CD1 1 
ATOM   1328  N  N   . PHE   A  1 166 ? -8.323  -10.714 -53.246  1.00 25.81  ? 467  PHE   A N   1 
ATOM   1329  C  CA  . PHE   A  1 166 ? -7.298  -10.997 -54.236  1.00 22.92  ? 467  PHE   A CA  1 
ATOM   1330  C  C   . PHE   A  1 166 ? -6.882  -12.455 -54.145  1.00 25.89  ? 467  PHE   A C   1 
ATOM   1331  O  O   . PHE   A  1 166 ? -7.348  -13.180 -53.269  1.00 27.28  ? 467  PHE   A O   1 
ATOM   1332  C  CB  . PHE   A  1 166 ? -6.132  -10.041 -54.018  1.00 26.86  ? 467  PHE   A CB  1 
ATOM   1333  C  CG  . PHE   A  1 166 ? -6.474  -8.621  -54.348  1.00 29.43  ? 467  PHE   A CG  1 
ATOM   1334  C  CD1 . PHE   A  1 166 ? -6.566  -8.216  -55.663  1.00 26.04  ? 467  PHE   A CD1 1 
ATOM   1335  C  CD2 . PHE   A  1 166 ? -6.724  -7.702  -53.347  1.00 27.99  ? 467  PHE   A CD2 1 
ATOM   1336  C  CE1 . PHE   A  1 166 ? -6.887  -6.923  -55.979  1.00 29.56  ? 467  PHE   A CE1 1 
ATOM   1337  C  CE2 . PHE   A  1 166 ? -7.045  -6.394  -53.658  1.00 29.63  ? 467  PHE   A CE2 1 
ATOM   1338  C  CZ  . PHE   A  1 166 ? -7.125  -6.003  -54.976  1.00 24.40  ? 467  PHE   A CZ  1 
ATOM   1339  N  N   . PRO   A  1 167 ? -6.046  -12.937 -55.073  1.00 28.08  ? 468  PRO   A N   1 
ATOM   1340  C  CA  . PRO   A  1 167 ? -5.728  -14.369 -55.097  1.00 28.41  ? 468  PRO   A CA  1 
ATOM   1341  C  C   . PRO   A  1 167 ? -5.158  -14.871 -53.780  1.00 25.37  ? 468  PRO   A C   1 
ATOM   1342  O  O   . PRO   A  1 167 ? -4.335  -14.214 -53.140  1.00 25.40  ? 468  PRO   A O   1 
ATOM   1343  C  CB  . PRO   A  1 167 ? -4.697  -14.478 -56.216  1.00 29.99  ? 468  PRO   A CB  1 
ATOM   1344  C  CG  . PRO   A  1 167 ? -5.083  -13.402 -57.158  1.00 26.25  ? 468  PRO   A CG  1 
ATOM   1345  C  CD  . PRO   A  1 167 ? -5.582  -12.269 -56.306  1.00 26.33  ? 468  PRO   A CD  1 
ATOM   1346  N  N   . GLN   A  1 168 ? -5.596  -16.064 -53.393  1.00 27.69  ? 469  GLN   A N   1 
ATOM   1347  C  CA  . GLN   A  1 168 ? -5.142  -16.670 -52.155  1.00 28.40  ? 469  GLN   A CA  1 
ATOM   1348  C  C   . GLN   A  1 168 ? -3.650  -16.945 -52.209  1.00 34.48  ? 469  GLN   A C   1 
ATOM   1349  O  O   . GLN   A  1 168 ? -3.035  -16.992 -53.281  1.00 26.39  ? 469  GLN   A O   1 
ATOM   1350  C  CB  . GLN   A  1 168 ? -5.867  -17.978 -51.908  1.00 24.13  ? 469  GLN   A CB  1 
ATOM   1351  C  CG  . GLN   A  1 168 ? -5.616  -18.984 -52.991  1.00 26.36  ? 469  GLN   A CG  1 
ATOM   1352  C  CD  . GLN   A  1 168 ? -6.797  -19.895 -53.183  1.00 27.05  ? 469  GLN   A CD  1 
ATOM   1353  O  OE1 . GLN   A  1 168 ? -7.941  -19.442 -53.219  1.00 31.69  ? 469  GLN   A OE1 1 
ATOM   1354  N  NE2 . GLN   A  1 168 ? -6.534  -21.191 -53.280  1.00 27.85  ? 469  GLN   A NE2 1 
ATOM   1355  N  N   . ARG   A  1 169 ? -3.072  -17.143 -51.028  1.00 33.57  ? 470  ARG   A N   1 
ATOM   1356  C  CA  . ARG   A  1 169 ? -1.675  -17.541 -50.935  1.00 32.70  ? 470  ARG   A CA  1 
ATOM   1357  C  C   . ARG   A  1 169 ? -1.490  -18.923 -51.549  1.00 32.57  ? 470  ARG   A C   1 
ATOM   1358  O  O   . ARG   A  1 169 ? -2.364  -19.786 -51.445  1.00 33.65  ? 470  ARG   A O   1 
ATOM   1359  C  CB  . ARG   A  1 169 ? -1.226  -17.523 -49.468  1.00 44.60  ? 470  ARG   A CB  1 
ATOM   1360  C  CG  . ARG   A  1 169 ? 0.073   -18.265 -49.201  1.00 54.10  ? 470  ARG   A CG  1 
ATOM   1361  C  CD  . ARG   A  1 169 ? 0.580   -18.041 -47.785  1.00 56.15  ? 470  ARG   A CD  1 
ATOM   1362  N  NE  . ARG   A  1 169 ? 0.864   -16.637 -47.531  1.00 51.29  ? 470  ARG   A NE  1 
ATOM   1363  C  CZ  . ARG   A  1 169 ? 0.367   -15.953 -46.512  1.00 57.63  ? 470  ARG   A CZ  1 
ATOM   1364  N  NH1 . ARG   A  1 169 ? -0.433  -16.553 -45.641  1.00 58.24  ? 470  ARG   A NH1 1 
ATOM   1365  N  NH2 . ARG   A  1 169 ? 0.681   -14.675 -46.358  1.00 64.05  ? 470  ARG   A NH2 1 
ATOM   1366  N  N   . THR   A  1 170 ? -0.354  -19.121 -52.225  1.00 35.66  ? 471  THR   A N   1 
ATOM   1367  C  CA  . THR   A  1 170 ? -0.052  -20.408 -52.837  1.00 38.47  ? 471  THR   A CA  1 
ATOM   1368  C  C   . THR   A  1 170 ? 1.094   -21.095 -52.104  1.00 45.22  ? 471  THR   A C   1 
ATOM   1369  O  O   . THR   A  1 170 ? 0.864   -21.976 -51.271  1.00 50.06  ? 471  THR   A O   1 
ATOM   1370  C  CB  . THR   A  1 170 ? 0.287   -20.234 -54.317  1.00 41.28  ? 471  THR   A CB  1 
ATOM   1371  O  OG1 . THR   A  1 170 ? 1.317   -19.247 -54.458  1.00 44.38  ? 471  THR   A OG1 1 
ATOM   1372  C  CG2 . THR   A  1 170 ? -0.945  -19.800 -55.092  1.00 37.98  ? 471  THR   A CG2 1 
ATOM   1373  N  N   . ASP   A  1 171 ? 2.332   -20.704 -52.404  1.00 52.59  ? 472  ASP   A N   1 
ATOM   1374  C  CA  . ASP   A  1 171 ? 3.493   -21.225 -51.697  1.00 56.37  ? 472  ASP   A CA  1 
ATOM   1375  C  C   . ASP   A  1 171 ? 4.028   -20.262 -50.646  1.00 60.98  ? 472  ASP   A C   1 
ATOM   1376  O  O   . ASP   A  1 171 ? 4.880   -20.657 -49.843  1.00 66.88  ? 472  ASP   A O   1 
ATOM   1377  C  CB  . ASP   A  1 171 ? 4.614   -21.573 -52.685  1.00 59.45  ? 472  ASP   A CB  1 
ATOM   1378  C  CG  . ASP   A  1 171 ? 5.100   -20.368 -53.476  1.00 62.11  ? 472  ASP   A CG  1 
ATOM   1379  O  OD1 . ASP   A  1 171 ? 4.569   -19.254 -53.279  1.00 58.56  ? 472  ASP   A OD1 1 
ATOM   1380  O  OD2 . ASP   A  1 171 ? 6.018   -20.537 -54.303  1.00 62.79  ? 472  ASP   A OD2 1 
ATOM   1381  N  N   . GLY   A  1 172 ? 3.548   -19.020 -50.625  1.00 49.12  ? 473  GLY   A N   1 
ATOM   1382  C  CA  . GLY   A  1 172 ? 4.044   -18.021 -49.708  1.00 45.52  ? 473  GLY   A CA  1 
ATOM   1383  C  C   . GLY   A  1 172 ? 5.087   -17.104 -50.301  1.00 44.34  ? 473  GLY   A C   1 
ATOM   1384  O  O   . GLY   A  1 172 ? 5.409   -16.082 -49.690  1.00 49.50  ? 473  GLY   A O   1 
ATOM   1385  N  N   . LYS   A  1 173 ? 5.634   -17.446 -51.459  1.00 49.36  ? 474  LYS   A N   1 
ATOM   1386  C  CA  . LYS   A  1 173 ? 6.549   -16.567 -52.170  1.00 59.31  ? 474  LYS   A CA  1 
ATOM   1387  C  C   . LYS   A  1 173 ? 5.840   -15.711 -53.208  1.00 58.86  ? 474  LYS   A C   1 
ATOM   1388  O  O   . LYS   A  1 173 ? 6.464   -14.818 -53.791  1.00 56.75  ? 474  LYS   A O   1 
ATOM   1389  C  CB  . LYS   A  1 173 ? 7.654   -17.384 -52.852  1.00 67.78  ? 474  LYS   A CB  1 
ATOM   1390  C  CG  . LYS   A  1 173 ? 8.704   -17.956 -51.907  1.00 77.76  ? 474  LYS   A CG  1 
ATOM   1391  C  CD  . LYS   A  1 173 ? 10.066  -18.025 -52.597  1.00 86.48  ? 474  LYS   A CD  1 
ATOM   1392  C  CE  . LYS   A  1 173 ? 11.035  -18.944 -51.862  1.00 90.08  ? 474  LYS   A CE  1 
ATOM   1393  N  NZ  . LYS   A  1 173 ? 10.646  -20.378 -51.991  1.00 90.19  ? 474  LYS   A NZ  1 
ATOM   1394  N  N   . HIS   A  1 174 ? 4.556   -15.956 -53.444  1.00 52.35  ? 475  HIS   A N   1 
ATOM   1395  C  CA  . HIS   A  1 174 ? 3.803   -15.245 -54.460  1.00 48.04  ? 475  HIS   A CA  1 
ATOM   1396  C  C   . HIS   A  1 174 ? 2.634   -14.494 -53.840  1.00 41.65  ? 475  HIS   A C   1 
ATOM   1397  O  O   . HIS   A  1 174 ? 1.570   -14.374 -54.448  1.00 44.24  ? 475  HIS   A O   1 
ATOM   1398  C  CB  . HIS   A  1 174 ? 3.321   -16.213 -55.539  1.00 53.43  ? 475  HIS   A CB  1 
ATOM   1399  C  CG  . HIS   A  1 174 ? 4.433   -16.865 -56.304  1.00 63.96  ? 475  HIS   A CG  1 
ATOM   1400  N  ND1 . HIS   A  1 174 ? 5.358   -17.702 -55.713  1.00 65.49  ? 475  HIS   A ND1 1 
ATOM   1401  C  CD2 . HIS   A  1 174 ? 4.763   -16.809 -57.616  1.00 62.64  ? 475  HIS   A CD2 1 
ATOM   1402  C  CE1 . HIS   A  1 174 ? 6.211   -18.128 -56.628  1.00 62.67  ? 475  HIS   A CE1 1 
ATOM   1403  N  NE2 . HIS   A  1 174 ? 5.873   -17.600 -57.791  1.00 64.77  ? 475  HIS   A NE2 1 
ATOM   1404  N  N   . ASP   A  1 175 ? 2.824   -13.977 -52.629  1.00 35.29  ? 476  ASP   A N   1 
ATOM   1405  C  CA  . ASP   A  1 175 ? 1.720   -13.357 -51.913  1.00 30.13  ? 476  ASP   A CA  1 
ATOM   1406  C  C   . ASP   A  1 175 ? 1.239   -12.100 -52.615  1.00 31.71  ? 476  ASP   A C   1 
ATOM   1407  O  O   . ASP   A  1 175 ? 2.031   -11.326 -53.161  1.00 36.31  ? 476  ASP   A O   1 
ATOM   1408  C  CB  . ASP   A  1 175 ? 2.122   -12.997 -50.483  1.00 34.11  ? 476  ASP   A CB  1 
ATOM   1409  C  CG  . ASP   A  1 175 ? 2.151   -14.195 -49.559  1.00 35.07  ? 476  ASP   A CG  1 
ATOM   1410  O  OD1 . ASP   A  1 175 ? 1.981   -15.334 -50.045  1.00 37.43  ? 476  ASP   A OD1 1 
ATOM   1411  O  OD2 . ASP   A  1 175 ? 2.353   -13.987 -48.347  1.00 41.92  ? 476  ASP   A OD2 1 
ATOM   1412  N  N   . PHE   A  1 176 ? -0.076  -11.910 -52.597  1.00 25.08  ? 477  PHE   A N   1 
ATOM   1413  C  CA  . PHE   A  1 176 ? -0.680  -10.612 -52.842  1.00 25.60  ? 477  PHE   A CA  1 
ATOM   1414  C  C   . PHE   A  1 176 ? -0.779  -9.870  -51.516  1.00 28.43  ? 477  PHE   A C   1 
ATOM   1415  O  O   . PHE   A  1 176 ? -1.302  -10.417 -50.542  1.00 28.85  ? 477  PHE   A O   1 
ATOM   1416  C  CB  . PHE   A  1 176 ? -2.057  -10.786 -53.471  1.00 21.27  ? 477  PHE   A CB  1 
ATOM   1417  C  CG  . PHE   A  1 176 ? -1.993  -11.148 -54.931  1.00 21.70  ? 477  PHE   A CG  1 
ATOM   1418  C  CD1 . PHE   A  1 176 ? -1.558  -12.411 -55.328  1.00 26.54  ? 477  PHE   A CD1 1 
ATOM   1419  C  CD2 . PHE   A  1 176 ? -2.314  -10.214 -55.898  1.00 23.79  ? 477  PHE   A CD2 1 
ATOM   1420  C  CE1 . PHE   A  1 176 ? -1.471  -12.745 -56.667  1.00 31.49  ? 477  PHE   A CE1 1 
ATOM   1421  C  CE2 . PHE   A  1 176 ? -2.225  -10.543 -57.252  1.00 31.97  ? 477  PHE   A CE2 1 
ATOM   1422  C  CZ  . PHE   A  1 176 ? -1.806  -11.809 -57.630  1.00 34.07  ? 477  PHE   A CZ  1 
ATOM   1423  N  N   . ARG   A  1 177 ? -0.274  -8.635  -51.471  1.00 24.23  ? 478  ARG   A N   1 
ATOM   1424  C  CA  . ARG   A  1 177 ? -0.372  -7.851  -50.245  1.00 34.19  ? 478  ARG   A CA  1 
ATOM   1425  C  C   . ARG   A  1 177 ? -0.690  -6.402  -50.564  1.00 29.97  ? 478  ARG   A C   1 
ATOM   1426  O  O   . ARG   A  1 177 ? -0.102  -5.811  -51.471  1.00 33.34  ? 478  ARG   A O   1 
ATOM   1427  C  CB  . ARG   A  1 177 ? 0.926   -7.893  -49.423  1.00 28.64  ? 478  ARG   A CB  1 
ATOM   1428  C  CG  . ARG   A  1 177 ? 1.284   -9.260  -48.875  1.00 29.45  ? 478  ARG   A CG  1 
ATOM   1429  C  CD  . ARG   A  1 177 ? 0.228   -9.735  -47.894  1.00 32.54  ? 478  ARG   A CD  1 
ATOM   1430  N  NE  . ARG   A  1 177 ? 0.052   -8.831  -46.765  1.00 29.63  ? 478  ARG   A NE  1 
ATOM   1431  C  CZ  . ARG   A  1 177 ? 0.781   -8.865  -45.646  1.00 36.22  ? 478  ARG   A CZ  1 
ATOM   1432  N  NH1 . ARG   A  1 177 ? 1.759   -9.749  -45.498  1.00 32.01  ? 478  ARG   A NH1 1 
ATOM   1433  N  NH2 . ARG   A  1 177 ? 0.530   -8.005  -44.668  1.00 28.84  ? 478  ARG   A NH2 1 
ATOM   1434  N  N   . VAL   A  1 178 ? -1.599  -5.827  -49.796  1.00 24.07  ? 479  VAL   A N   1 
ATOM   1435  C  CA  . VAL   A  1 178 ? -1.705  -4.381  -49.693  1.00 27.20  ? 479  VAL   A CA  1 
ATOM   1436  C  C   . VAL   A  1 178 ? -0.792  -3.994  -48.541  1.00 31.64  ? 479  VAL   A C   1 
ATOM   1437  O  O   . VAL   A  1 178 ? -1.047  -4.363  -47.395  1.00 29.72  ? 479  VAL   A O   1 
ATOM   1438  C  CB  . VAL   A  1 178 ? -3.148  -3.933  -49.449  1.00 22.53  ? 479  VAL   A CB  1 
ATOM   1439  C  CG1 . VAL   A  1 178 ? -3.199  -2.434  -49.297  1.00 20.57  ? 479  VAL   A CG1 1 
ATOM   1440  C  CG2 . VAL   A  1 178 ? -4.048  -4.416  -50.580  1.00 23.05  ? 479  VAL   A CG2 1 
ATOM   1441  N  N   . TRP   A  1 179 ? 0.313   -3.314  -48.844  1.00 29.20  ? 480  TRP   A N   1 
ATOM   1442  C  CA  . TRP   A  1 179 ? 1.241   -2.972  -47.781  1.00 26.86  ? 480  TRP   A CA  1 
ATOM   1443  C  C   . TRP   A  1 179 ? 0.665   -1.917  -46.854  1.00 30.09  ? 480  TRP   A C   1 
ATOM   1444  O  O   . TRP   A  1 179 ? 1.096   -1.821  -45.706  1.00 30.02  ? 480  TRP   A O   1 
ATOM   1445  C  CB  . TRP   A  1 179 ? 2.575   -2.506  -48.365  1.00 28.49  ? 480  TRP   A CB  1 
ATOM   1446  C  CG  . TRP   A  1 179 ? 3.413   -3.623  -48.875  1.00 28.72  ? 480  TRP   A CG  1 
ATOM   1447  C  CD1 . TRP   A  1 179 ? 2.980   -4.757  -49.514  1.00 22.56  ? 480  TRP   A CD1 1 
ATOM   1448  C  CD2 . TRP   A  1 179 ? 4.842   -3.735  -48.779  1.00 27.48  ? 480  TRP   A CD2 1 
ATOM   1449  N  NE1 . TRP   A  1 179 ? 4.057   -5.552  -49.839  1.00 34.00  ? 480  TRP   A NE1 1 
ATOM   1450  C  CE2 . TRP   A  1 179 ? 5.208   -4.954  -49.388  1.00 25.79  ? 480  TRP   A CE2 1 
ATOM   1451  C  CE3 . TRP   A  1 179 ? 5.842   -2.924  -48.235  1.00 35.38  ? 480  TRP   A CE3 1 
ATOM   1452  C  CZ2 . TRP   A  1 179 ? 6.535   -5.380  -49.469  1.00 27.88  ? 480  TRP   A CZ2 1 
ATOM   1453  C  CZ3 . TRP   A  1 179 ? 7.162   -3.348  -48.315  1.00 33.03  ? 480  TRP   A CZ3 1 
ATOM   1454  C  CH2 . TRP   A  1 179 ? 7.494   -4.563  -48.929  1.00 33.98  ? 480  TRP   A CH2 1 
ATOM   1455  N  N   . ASN   A  1 180 ? -0.313  -1.147  -47.320  1.00 28.42  ? 481  ASN   A N   1 
ATOM   1456  C  CA  . ASN   A  1 180 ? -1.007  -0.209  -46.457  1.00 28.32  ? 481  ASN   A CA  1 
ATOM   1457  C  C   . ASN   A  1 180 ? -1.765  -0.950  -45.375  1.00 32.19  ? 481  ASN   A C   1 
ATOM   1458  O  O   . ASN   A  1 180 ? -2.365  -1.999  -45.624  1.00 28.84  ? 481  ASN   A O   1 
ATOM   1459  C  CB  . ASN   A  1 180 ? -1.979  0.625   -47.273  1.00 28.12  ? 481  ASN   A CB  1 
ATOM   1460  C  CG  . ASN   A  1 180 ? -1.310  1.279   -48.454  1.00 25.35  ? 481  ASN   A CG  1 
ATOM   1461  O  OD1 . ASN   A  1 180 ? -0.936  0.611   -49.423  1.00 32.88  ? 481  ASN   A OD1 1 
ATOM   1462  N  ND2 . ASN   A  1 180 ? -1.158  2.588   -48.387  1.00 27.86  ? 481  ASN   A ND2 1 
ATOM   1463  N  N   . SER   A  1 181 ? -1.763  -0.387  -44.166  1.00 19.95  ? 482  SER   A N   1 
ATOM   1464  C  CA  . SER   A  1 181 ? -2.557  -1.008  -43.109  1.00 24.55  ? 482  SER   A CA  1 
ATOM   1465  C  C   . SER   A  1 181 ? -4.037  -0.752  -43.341  1.00 20.15  ? 482  SER   A C   1 
ATOM   1466  O  O   . SER   A  1 181 ? -4.876  -1.616  -43.068  1.00 21.03  ? 482  SER   A O   1 
ATOM   1467  C  CB  . SER   A  1 181 ? -2.106  -0.494  -41.741  1.00 21.44  ? 482  SER   A CB  1 
ATOM   1468  O  OG  . SER   A  1 181 ? -2.091  0.922   -41.737  1.00 26.69  ? 482  SER   A OG  1 
ATOM   1469  N  N   . GLN   A  1 182 ? -4.372  0.434   -43.849  1.00 18.82  ? 483  GLN   A N   1 
ATOM   1470  C  CA  . GLN   A  1 182 ? -5.703  0.742   -44.341  1.00 22.77  ? 483  GLN   A CA  1 
ATOM   1471  C  C   . GLN   A  1 182 ? -5.552  1.434   -45.693  1.00 27.17  ? 483  GLN   A C   1 
ATOM   1472  O  O   . GLN   A  1 182 ? -4.540  2.090   -45.961  1.00 26.39  ? 483  GLN   A O   1 
ATOM   1473  C  CB  . GLN   A  1 182 ? -6.497  1.624   -43.366  1.00 18.48  ? 483  GLN   A CB  1 
ATOM   1474  C  CG  . GLN   A  1 182 ? -6.802  0.931   -42.017  1.00 25.68  ? 483  GLN   A CG  1 
ATOM   1475  C  CD  . GLN   A  1 182 ? -6.370  1.748   -40.795  1.00 37.07  ? 483  GLN   A CD  1 
ATOM   1476  O  OE1 . GLN   A  1 182 ? -5.690  1.238   -39.900  1.00 44.75  ? 483  GLN   A OE1 1 
ATOM   1477  N  NE2 . GLN   A  1 182 ? -6.785  2.999   -40.744  1.00 34.13  ? 483  GLN   A NE2 1 
ATOM   1478  N  N   . LEU   A  1 183 ? -6.575  1.296   -46.535  1.00 23.93  ? 484  LEU   A N   1 
ATOM   1479  C  CA  . LEU   A  1 183 ? -6.491  1.841   -47.885  1.00 23.87  ? 484  LEU   A CA  1 
ATOM   1480  C  C   . LEU   A  1 183 ? -6.235  3.333   -47.855  1.00 27.94  ? 484  LEU   A C   1 
ATOM   1481  O  O   . LEU   A  1 183 ? -5.450  3.854   -48.655  1.00 25.56  ? 484  LEU   A O   1 
ATOM   1482  C  CB  . LEU   A  1 183 ? -7.780  1.542   -48.646  1.00 21.23  ? 484  LEU   A CB  1 
ATOM   1483  C  CG  . LEU   A  1 183 ? -8.061  0.056   -48.882  1.00 21.32  ? 484  LEU   A CG  1 
ATOM   1484  C  CD1 . LEU   A  1 183 ? -9.315  -0.100  -49.727  1.00 24.27  ? 484  LEU   A CD1 1 
ATOM   1485  C  CD2 . LEU   A  1 183 ? -6.877  -0.641  -49.541  1.00 19.52  ? 484  LEU   A CD2 1 
ATOM   1486  N  N   . ILE   A  1 184 ? -6.871  4.031   -46.919  1.00 25.98  ? 485  ILE   A N   1 
ATOM   1487  C  CA  . ILE   A  1 184 ? -6.751  5.475   -46.790  1.00 24.20  ? 485  ILE   A CA  1 
ATOM   1488  C  C   . ILE   A  1 184 ? -6.248  5.777   -45.387  1.00 31.71  ? 485  ILE   A C   1 
ATOM   1489  O  O   . ILE   A  1 184 ? -6.918  5.455   -44.396  1.00 24.06  ? 485  ILE   A O   1 
ATOM   1490  C  CB  . ILE   A  1 184 ? -8.082  6.182   -47.079  1.00 24.42  ? 485  ILE   A CB  1 
ATOM   1491  C  CG1 . ILE   A  1 184 ? -8.475  5.929   -48.548  1.00 30.90  ? 485  ILE   A CG1 1 
ATOM   1492  C  CG2 . ILE   A  1 184 ? -7.943  7.677   -46.869  1.00 21.68  ? 485  ILE   A CG2 1 
ATOM   1493  C  CD1 . ILE   A  1 184 ? -9.923  6.109   -48.825  1.00 28.07  ? 485  ILE   A CD1 1 
ATOM   1494  N  N   . ARG   A  1 185 ? -5.045  6.342   -45.309  1.00 27.08  ? 486  ARG   A N   1 
ATOM   1495  C  CA  . ARG   A  1 185 ? -4.465  6.823   -44.062  1.00 30.85  ? 486  ARG   A CA  1 
ATOM   1496  C  C   . ARG   A  1 185 ? -3.608  8.026   -44.410  1.00 30.38  ? 486  ARG   A C   1 
ATOM   1497  O  O   . ARG   A  1 185 ? -3.286  8.254   -45.579  1.00 27.72  ? 486  ARG   A O   1 
ATOM   1498  C  CB  . ARG   A  1 185 ? -3.613  5.759   -43.347  1.00 26.29  ? 486  ARG   A CB  1 
ATOM   1499  C  CG  . ARG   A  1 185 ? -4.371  4.512   -42.921  1.00 24.69  ? 486  ARG   A CG  1 
ATOM   1500  C  CD  . ARG   A  1 185 ? -3.610  3.713   -41.881  1.00 27.61  ? 486  ARG   A CD  1 
ATOM   1501  N  NE  . ARG   A  1 185 ? -3.499  4.454   -40.627  1.00 30.98  ? 486  ARG   A NE  1 
ATOM   1502  C  CZ  . ARG   A  1 185 ? -2.970  3.976   -39.505  1.00 33.56  ? 486  ARG   A CZ  1 
ATOM   1503  N  NH1 . ARG   A  1 185 ? -2.492  2.738   -39.446  1.00 26.27  ? 486  ARG   A NH1 1 
ATOM   1504  N  NH2 . ARG   A  1 185 ? -2.926  4.744   -38.432  1.00 28.85  ? 486  ARG   A NH2 1 
ATOM   1505  N  N   . TYR   A  1 186 ? -3.246  8.799   -43.396  1.00 22.66  ? 487  TYR   A N   1 
ATOM   1506  C  CA  . TYR   A  1 186 ? -2.434  9.984   -43.609  1.00 24.16  ? 487  TYR   A CA  1 
ATOM   1507  C  C   . TYR   A  1 186 ? -0.981  9.690   -43.279  1.00 24.36  ? 487  TYR   A C   1 
ATOM   1508  O  O   . TYR   A  1 186 ? -0.677  8.909   -42.375  1.00 34.46  ? 487  TYR   A O   1 
ATOM   1509  C  CB  . TYR   A  1 186 ? -2.933  11.152  -42.759  1.00 24.01  ? 487  TYR   A CB  1 
ATOM   1510  C  CG  . TYR   A  1 186 ? -4.333  11.588  -43.097  1.00 31.77  ? 487  TYR   A CG  1 
ATOM   1511  C  CD1 . TYR   A  1 186 ? -5.359  11.488  -42.162  1.00 26.15  ? 487  TYR   A CD1 1 
ATOM   1512  C  CD2 . TYR   A  1 186 ? -4.633  12.097  -44.359  1.00 28.97  ? 487  TYR   A CD2 1 
ATOM   1513  C  CE1 . TYR   A  1 186 ? -6.655  11.900  -42.476  1.00 31.31  ? 487  TYR   A CE1 1 
ATOM   1514  C  CE2 . TYR   A  1 186 ? -5.907  12.511  -44.680  1.00 29.20  ? 487  TYR   A CE2 1 
ATOM   1515  C  CZ  . TYR   A  1 186 ? -6.921  12.413  -43.742  1.00 32.10  ? 487  TYR   A CZ  1 
ATOM   1516  O  OH  . TYR   A  1 186 ? -8.193  12.836  -44.078  1.00 29.50  ? 487  TYR   A OH  1 
ATOM   1517  N  N   . ALA   A  1 187 ? -0.083  10.332  -44.014  1.00 32.53  ? 488  ALA   A N   1 
ATOM   1518  C  CA  . ALA   A  1 187 ? 1.341   10.138  -43.802  1.00 28.38  ? 488  ALA   A CA  1 
ATOM   1519  C  C   . ALA   A  1 187 ? 1.779   10.705  -42.453  1.00 36.74  ? 488  ALA   A C   1 
ATOM   1520  O  O   . ALA   A  1 187 ? 1.087   11.505  -41.820  1.00 32.66  ? 488  ALA   A O   1 
ATOM   1521  C  CB  . ALA   A  1 187 ? 2.152   10.808  -44.910  1.00 28.72  ? 488  ALA   A CB  1 
ATOM   1522  N  N   . GLY   A  1 188 ? 2.958   10.283  -42.027  1.00 36.49  ? 489  GLY   A N   1 
ATOM   1523  C  CA  . GLY   A  1 188 ? 3.581   10.829  -40.845  1.00 31.57  ? 489  GLY   A CA  1 
ATOM   1524  C  C   . GLY   A  1 188 ? 5.042   11.073  -41.130  1.00 31.55  ? 489  GLY   A C   1 
ATOM   1525  O  O   . GLY   A  1 188 ? 5.692   10.262  -41.797  1.00 38.18  ? 489  GLY   A O   1 
ATOM   1526  N  N   . TYR   A  1 189 ? 5.567   12.189  -40.648  1.00 31.41  ? 490  TYR   A N   1 
ATOM   1527  C  CA  . TYR   A  1 189 ? 6.919   12.604  -40.989  1.00 44.55  ? 490  TYR   A CA  1 
ATOM   1528  C  C   . TYR   A  1 189 ? 7.678   12.923  -39.714  1.00 45.57  ? 490  TYR   A C   1 
ATOM   1529  O  O   . TYR   A  1 189 ? 7.149   13.609  -38.835  1.00 50.93  ? 490  TYR   A O   1 
ATOM   1530  C  CB  . TYR   A  1 189 ? 6.904   13.828  -41.908  1.00 44.70  ? 490  TYR   A CB  1 
ATOM   1531  C  CG  . TYR   A  1 189 ? 5.999   13.706  -43.113  1.00 46.11  ? 490  TYR   A CG  1 
ATOM   1532  C  CD1 . TYR   A  1 189 ? 4.721   14.255  -43.105  1.00 43.27  ? 490  TYR   A CD1 1 
ATOM   1533  C  CD2 . TYR   A  1 189 ? 6.428   13.058  -44.265  1.00 46.25  ? 490  TYR   A CD2 1 
ATOM   1534  C  CE1 . TYR   A  1 189 ? 3.899   14.162  -44.207  1.00 44.85  ? 490  TYR   A CE1 1 
ATOM   1535  C  CE2 . TYR   A  1 189 ? 5.611   12.954  -45.371  1.00 46.24  ? 490  TYR   A CE2 1 
ATOM   1536  C  CZ  . TYR   A  1 189 ? 4.349   13.509  -45.341  1.00 48.28  ? 490  TYR   A CZ  1 
ATOM   1537  O  OH  . TYR   A  1 189 ? 3.534   13.406  -46.447  1.00 43.87  ? 490  TYR   A OH  1 
ATOM   1538  N  N   . LYS   A  1 190 ? 8.910   12.429  -39.617  1.00 50.34  ? 491  LYS   A N   1 
ATOM   1539  C  CA  . LYS   A  1 190 ? 9.814   12.843  -38.549  1.00 59.57  ? 491  LYS   A CA  1 
ATOM   1540  C  C   . LYS   A  1 190 ? 10.348  14.234  -38.869  1.00 58.72  ? 491  LYS   A C   1 
ATOM   1541  O  O   . LYS   A  1 190 ? 10.934  14.452  -39.935  1.00 58.28  ? 491  LYS   A O   1 
ATOM   1542  C  CB  . LYS   A  1 190 ? 10.959  11.845  -38.383  1.00 65.49  ? 491  LYS   A CB  1 
ATOM   1543  C  CG  . LYS   A  1 190 ? 10.511  10.456  -37.959  1.00 71.30  ? 491  LYS   A CG  1 
ATOM   1544  C  CD  . LYS   A  1 190 ? 11.296  9.942   -36.759  1.00 77.98  ? 491  LYS   A CD  1 
ATOM   1545  C  CE  . LYS   A  1 190 ? 12.522  9.144   -37.187  1.00 80.81  ? 491  LYS   A CE  1 
ATOM   1546  N  NZ  . LYS   A  1 190 ? 12.143  7.913   -37.945  1.00 77.97  ? 491  LYS   A NZ  1 
ATOM   1547  N  N   . GLN   A  1 191 ? 10.134  15.162  -37.967  1.00 62.38  ? 492  GLN   A N   1 
ATOM   1548  C  CA  . GLN   A  1 191 ? 10.590  16.534  -38.130  1.00 68.76  ? 492  GLN   A CA  1 
ATOM   1549  C  C   . GLN   A  1 191 ? 12.033  16.684  -37.652  1.00 72.65  ? 492  GLN   A C   1 
ATOM   1550  O  O   . GLN   A  1 191 ? 12.488  15.931  -36.784  1.00 63.35  ? 492  GLN   A O   1 
ATOM   1551  C  CB  . GLN   A  1 191 ? 9.688   17.493  -37.354  1.00 64.59  ? 492  GLN   A CB  1 
ATOM   1552  C  CG  . GLN   A  1 191 ? 8.254   17.571  -37.860  1.00 63.01  ? 492  GLN   A CG  1 
ATOM   1553  C  CD  . GLN   A  1 191 ? 8.136   18.172  -39.250  1.00 64.87  ? 492  GLN   A CD  1 
ATOM   1554  O  OE1 . GLN   A  1 191 ? 8.581   17.589  -40.237  1.00 65.38  ? 492  GLN   A OE1 1 
ATOM   1555  N  NE2 . GLN   A  1 191 ? 7.523   19.343  -39.333  1.00 67.55  ? 492  GLN   A NE2 1 
ATOM   1556  N  N   . PRO   A  1 192 ? 12.769  17.654  -38.209  1.00 80.20  ? 493  PRO   A N   1 
ATOM   1557  C  CA  . PRO   A  1 192 ? 14.165  17.842  -37.779  1.00 79.73  ? 493  PRO   A CA  1 
ATOM   1558  C  C   . PRO   A  1 192 ? 14.310  17.985  -36.274  1.00 80.84  ? 493  PRO   A C   1 
ATOM   1559  O  O   . PRO   A  1 192 ? 15.199  17.367  -35.677  1.00 81.13  ? 493  PRO   A O   1 
ATOM   1560  C  CB  . PRO   A  1 192 ? 14.584  19.123  -38.516  1.00 78.52  ? 493  PRO   A CB  1 
ATOM   1561  C  CG  . PRO   A  1 192 ? 13.653  19.232  -39.670  1.00 76.22  ? 493  PRO   A CG  1 
ATOM   1562  C  CD  . PRO   A  1 192 ? 12.354  18.655  -39.208  1.00 77.90  ? 493  PRO   A CD  1 
ATOM   1563  N  N   . ASP   A  1 193 ? 13.428  18.762  -35.640  1.00 78.42  ? 494  ASP   A N   1 
ATOM   1564  C  CA  . ASP   A  1 193 ? 13.522  18.972  -34.199  1.00 71.22  ? 494  ASP   A CA  1 
ATOM   1565  C  C   . ASP   A  1 193 ? 13.244  17.696  -33.414  1.00 66.54  ? 494  ASP   A C   1 
ATOM   1566  O  O   . ASP   A  1 193 ? 13.701  17.562  -32.274  1.00 72.87  ? 494  ASP   A O   1 
ATOM   1567  C  CB  . ASP   A  1 193 ? 12.568  20.090  -33.770  1.00 74.41  ? 494  ASP   A CB  1 
ATOM   1568  C  CG  . ASP   A  1 193 ? 11.222  20.008  -34.458  1.00 82.17  ? 494  ASP   A CG  1 
ATOM   1569  O  OD1 . ASP   A  1 193 ? 10.239  19.620  -33.791  1.00 81.00  ? 494  ASP   A OD1 1 
ATOM   1570  O  OD2 . ASP   A  1 193 ? 11.148  20.326  -35.669  1.00 88.87  ? 494  ASP   A OD2 1 
ATOM   1571  N  N   . GLY   A  1 194 ? 12.513  16.752  -33.994  1.00 60.01  ? 495  GLY   A N   1 
ATOM   1572  C  CA  . GLY   A  1 194 ? 12.218  15.491  -33.337  1.00 54.55  ? 495  GLY   A CA  1 
ATOM   1573  C  C   . GLY   A  1 194 ? 10.746  15.212  -33.121  1.00 55.08  ? 495  GLY   A C   1 
ATOM   1574  O  O   . GLY   A  1 194 ? 10.394  14.080  -32.752  1.00 54.77  ? 495  GLY   A O   1 
ATOM   1575  N  N   . SER   A  1 195 ? 9.867   16.187  -33.326  1.00 52.33  ? 496  SER   A N   1 
ATOM   1576  C  CA  . SER   A  1 195 ? 8.431   15.964  -33.232  1.00 56.79  ? 496  SER   A CA  1 
ATOM   1577  C  C   . SER   A  1 195 ? 7.971   15.184  -34.468  1.00 53.25  ? 496  SER   A C   1 
ATOM   1578  O  O   . SER   A  1 195 ? 8.775   14.715  -35.277  1.00 46.54  ? 496  SER   A O   1 
ATOM   1579  C  CB  . SER   A  1 195 ? 7.701   17.295  -33.080  1.00 60.49  ? 496  SER   A CB  1 
ATOM   1580  O  OG  . SER   A  1 195 ? 7.966   18.148  -34.185  1.00 67.06  ? 496  SER   A OG  1 
ATOM   1581  N  N   . THR   A  1 196 ? 6.658   15.036  -34.626  1.00 45.29  ? 497  THR   A N   1 
ATOM   1582  C  CA  . THR   A  1 196 ? 6.092   14.295  -35.745  1.00 42.63  ? 497  THR   A CA  1 
ATOM   1583  C  C   . THR   A  1 196 ? 4.992   15.114  -36.399  1.00 42.71  ? 497  THR   A C   1 
ATOM   1584  O  O   . THR   A  1 196 ? 4.108   15.632  -35.709  1.00 45.49  ? 497  THR   A O   1 
ATOM   1585  C  CB  . THR   A  1 196 ? 5.526   12.942  -35.297  1.00 45.48  ? 497  THR   A CB  1 
ATOM   1586  O  OG1 . THR   A  1 196 ? 6.588   12.106  -34.813  1.00 51.47  ? 497  THR   A OG1 1 
ATOM   1587  C  CG2 . THR   A  1 196 ? 4.813   12.248  -36.465  1.00 40.96  ? 497  THR   A CG2 1 
ATOM   1588  N  N   . LEU   A  1 197 ? 5.040   15.210  -37.725  1.00 41.37  ? 498  LEU   A N   1 
ATOM   1589  C  CA  . LEU   A  1 197 ? 4.004   15.860  -38.513  1.00 45.20  ? 498  LEU   A CA  1 
ATOM   1590  C  C   . LEU   A  1 197 ? 3.098   14.795  -39.124  1.00 45.78  ? 498  LEU   A C   1 
ATOM   1591  O  O   . LEU   A  1 197 ? 3.580   13.789  -39.655  1.00 42.76  ? 498  LEU   A O   1 
ATOM   1592  C  CB  . LEU   A  1 197 ? 4.627   16.734  -39.601  1.00 43.29  ? 498  LEU   A CB  1 
ATOM   1593  C  CG  . LEU   A  1 197 ? 3.657   17.320  -40.626  1.00 49.50  ? 498  LEU   A CG  1 
ATOM   1594  C  CD1 . LEU   A  1 197 ? 2.710   18.302  -39.964  1.00 51.63  ? 498  LEU   A CD1 1 
ATOM   1595  C  CD2 . LEU   A  1 197 ? 4.412   17.986  -41.764  1.00 44.83  ? 498  LEU   A CD2 1 
ATOM   1596  N  N   . GLY   A  1 198 ? 1.788   15.012  -39.039  1.00 42.31  ? 499  GLY   A N   1 
ATOM   1597  C  CA  . GLY   A  1 198 ? 0.846   14.024  -39.528  1.00 33.89  ? 499  GLY   A CA  1 
ATOM   1598  C  C   . GLY   A  1 198 ? 0.568   12.907  -38.540  1.00 38.72  ? 499  GLY   A C   1 
ATOM   1599  O  O   . GLY   A  1 198 ? 0.553   13.134  -37.328  1.00 40.94  ? 499  GLY   A O   1 
ATOM   1600  N  N   . ASP   A  1 199 ? 0.355   11.689  -39.046  1.00 38.08  ? 500  ASP   A N   1 
ATOM   1601  C  CA  . ASP   A  1 199 ? -0.018  10.555  -38.207  1.00 27.58  ? 500  ASP   A CA  1 
ATOM   1602  C  C   . ASP   A  1 199 ? 1.238   9.815   -37.768  1.00 32.52  ? 500  ASP   A C   1 
ATOM   1603  O  O   . ASP   A  1 199 ? 1.899   9.189   -38.613  1.00 30.02  ? 500  ASP   A O   1 
ATOM   1604  C  CB  . ASP   A  1 199 ? -0.944  9.618   -38.972  1.00 30.02  ? 500  ASP   A CB  1 
ATOM   1605  C  CG  . ASP   A  1 199 ? -1.620  8.603   -38.074  1.00 32.63  ? 500  ASP   A CG  1 
ATOM   1606  O  OD1 . ASP   A  1 199 ? -1.071  8.301   -36.995  1.00 35.09  ? 500  ASP   A OD1 1 
ATOM   1607  O  OD2 . ASP   A  1 199 ? -2.703  8.100   -38.448  1.00 32.10  ? 500  ASP   A OD2 1 
ATOM   1608  N  N   . PRO   A  1 200 ? 1.600   9.833   -36.476  1.00 35.74  ? 501  PRO   A N   1 
ATOM   1609  C  CA  . PRO   A  1 200 ? 2.835   9.140   -36.056  1.00 29.39  ? 501  PRO   A CA  1 
ATOM   1610  C  C   . PRO   A  1 200 ? 2.795   7.642   -36.287  1.00 30.17  ? 501  PRO   A C   1 
ATOM   1611  O  O   . PRO   A  1 200 ? 3.850   7.030   -36.497  1.00 33.98  ? 501  PRO   A O   1 
ATOM   1612  C  CB  . PRO   A  1 200 ? 2.949   9.489   -34.558  1.00 28.57  ? 501  PRO   A CB  1 
ATOM   1613  C  CG  . PRO   A  1 200 ? 2.176   10.771  -34.422  1.00 37.90  ? 501  PRO   A CG  1 
ATOM   1614  C  CD  . PRO   A  1 200 ? 1.020   10.638  -35.387  1.00 30.15  ? 501  PRO   A CD  1 
ATOM   1615  N  N   . ALA   A  1 201 ? 1.609   7.028   -36.268  1.00 28.63  ? 502  ALA   A N   1 
ATOM   1616  C  CA  . ALA   A  1 201 ? 1.525   5.597   -36.544  1.00 32.05  ? 502  ALA   A CA  1 
ATOM   1617  C  C   . ALA   A  1 201 ? 2.102   5.253   -37.912  1.00 40.52  ? 502  ALA   A C   1 
ATOM   1618  O  O   . ALA   A  1 201 ? 2.659   4.163   -38.099  1.00 37.31  ? 502  ALA   A O   1 
ATOM   1619  C  CB  . ALA   A  1 201 ? 0.072   5.129   -36.454  1.00 33.59  ? 502  ALA   A CB  1 
ATOM   1620  N  N   . ASN   A  1 202 ? 2.004   6.170   -38.872  1.00 35.67  ? 503  ASN   A N   1 
ATOM   1621  C  CA  . ASN   A  1 202 ? 2.384   5.870   -40.243  1.00 31.17  ? 503  ASN   A CA  1 
ATOM   1622  C  C   . ASN   A  1 202 ? 3.750   6.419   -40.614  1.00 36.51  ? 503  ASN   A C   1 
ATOM   1623  O  O   . ASN   A  1 202 ? 4.063   6.523   -41.804  1.00 37.96  ? 503  ASN   A O   1 
ATOM   1624  C  CB  . ASN   A  1 202 ? 1.309   6.383   -41.192  1.00 24.80  ? 503  ASN   A CB  1 
ATOM   1625  C  CG  . ASN   A  1 202 ? -0.000  5.678   -40.966  1.00 27.17  ? 503  ASN   A CG  1 
ATOM   1626  O  OD1 . ASN   A  1 202 ? -0.010  4.480   -40.660  1.00 32.02  ? 503  ASN   A OD1 1 
ATOM   1627  N  ND2 . ASN   A  1 202 ? -1.109  6.407   -41.066  1.00 23.03  ? 503  ASN   A ND2 1 
ATOM   1628  N  N   . VAL   A  1 203 ? 4.585   6.744   -39.629  1.00 35.20  ? 504  VAL   A N   1 
ATOM   1629  C  CA  . VAL   A  1 203 ? 5.906   7.272   -39.958  1.00 39.62  ? 504  VAL   A CA  1 
ATOM   1630  C  C   . VAL   A  1 203 ? 6.713   6.235   -40.728  1.00 41.16  ? 504  VAL   A C   1 
ATOM   1631  O  O   . VAL   A  1 203 ? 7.299   6.536   -41.775  1.00 42.63  ? 504  VAL   A O   1 
ATOM   1632  C  CB  . VAL   A  1 203 ? 6.640   7.740   -38.692  1.00 38.01  ? 504  VAL   A CB  1 
ATOM   1633  C  CG1 . VAL   A  1 203 ? 8.119   7.930   -38.993  1.00 32.16  ? 504  VAL   A CG1 1 
ATOM   1634  C  CG2 . VAL   A  1 203 ? 6.024   9.034   -38.195  1.00 38.40  ? 504  VAL   A CG2 1 
ATOM   1635  N  N   . GLN   A  1 204 ? 6.735   4.994   -40.237  1.00 32.07  ? 505  GLN   A N   1 
ATOM   1636  C  CA  . GLN   A  1 204 ? 7.516   3.961   -40.912  1.00 35.15  ? 505  GLN   A CA  1 
ATOM   1637  C  C   . GLN   A  1 204 ? 6.979   3.694   -42.314  1.00 37.69  ? 505  GLN   A C   1 
ATOM   1638  O  O   . GLN   A  1 204 ? 7.742   3.639   -43.286  1.00 34.94  ? 505  GLN   A O   1 
ATOM   1639  C  CB  . GLN   A  1 204 ? 7.520   2.668   -40.103  1.00 34.41  ? 505  GLN   A CB  1 
ATOM   1640  C  CG  . GLN   A  1 204 ? 8.451   1.630   -40.706  1.00 48.52  ? 505  GLN   A CG  1 
ATOM   1641  C  CD  . GLN   A  1 204 ? 8.359   0.279   -40.036  1.00 52.78  ? 505  GLN   A CD  1 
ATOM   1642  O  OE1 . GLN   A  1 204 ? 7.332   -0.070  -39.449  1.00 54.83  ? 505  GLN   A OE1 1 
ATOM   1643  N  NE2 . GLN   A  1 204 ? 9.440   -0.496  -40.120  1.00 52.20  ? 505  GLN   A NE2 1 
ATOM   1644  N  N   . PHE   A  1 205 ? 5.667   3.500   -42.439  1.00 35.32  ? 506  PHE   A N   1 
ATOM   1645  C  CA  . PHE   A  1 205 ? 5.103   3.262   -43.759  1.00 34.29  ? 506  PHE   A CA  1 
ATOM   1646  C  C   . PHE   A  1 205 ? 5.378   4.437   -44.690  1.00 37.81  ? 506  PHE   A C   1 
ATOM   1647  O  O   . PHE   A  1 205 ? 5.780   4.246   -45.848  1.00 32.02  ? 506  PHE   A O   1 
ATOM   1648  C  CB  . PHE   A  1 205 ? 3.604   2.988   -43.657  1.00 35.40  ? 506  PHE   A CB  1 
ATOM   1649  C  CG  . PHE   A  1 205 ? 2.992   2.621   -44.971  1.00 35.43  ? 506  PHE   A CG  1 
ATOM   1650  C  CD1 . PHE   A  1 205 ? 3.172   1.348   -45.494  1.00 34.21  ? 506  PHE   A CD1 1 
ATOM   1651  C  CD2 . PHE   A  1 205 ? 2.278   3.559   -45.708  1.00 31.12  ? 506  PHE   A CD2 1 
ATOM   1652  C  CE1 . PHE   A  1 205 ? 2.629   1.002   -46.727  1.00 34.99  ? 506  PHE   A CE1 1 
ATOM   1653  C  CE2 . PHE   A  1 205 ? 1.723   3.222   -46.944  1.00 37.31  ? 506  PHE   A CE2 1 
ATOM   1654  C  CZ  . PHE   A  1 205 ? 1.902   1.944   -47.454  1.00 35.64  ? 506  PHE   A CZ  1 
ATOM   1655  N  N   . THR   A  1 206 ? 5.200   5.663   -44.189  1.00 26.87  ? 507  THR   A N   1 
ATOM   1656  C  CA  . THR   A  1 206 ? 5.518   6.843   -44.982  1.00 38.08  ? 507  THR   A CA  1 
ATOM   1657  C  C   . THR   A  1 206 ? 6.966   6.817   -45.458  1.00 42.23  ? 507  THR   A C   1 
ATOM   1658  O  O   . THR   A  1 206 ? 7.252   7.140   -46.617  1.00 41.00  ? 507  THR   A O   1 
ATOM   1659  C  CB  . THR   A  1 206 ? 5.237   8.108   -44.172  1.00 34.64  ? 507  THR   A CB  1 
ATOM   1660  O  OG1 . THR   A  1 206 ? 3.855   8.120   -43.779  1.00 34.26  ? 507  THR   A OG1 1 
ATOM   1661  C  CG2 . THR   A  1 206 ? 5.539   9.353   -44.989  1.00 29.59  ? 507  THR   A CG2 1 
ATOM   1662  N  N   . GLU   A  1 207 ? 7.894   6.412   -44.589  1.00 38.88  ? 508  GLU   A N   1 
ATOM   1663  C  CA  . GLU   A  1 207 ? 9.295   6.385   -45.003  1.00 36.66  ? 508  GLU   A CA  1 
ATOM   1664  C  C   . GLU   A  1 207 ? 9.522   5.365   -46.112  1.00 34.07  ? 508  GLU   A C   1 
ATOM   1665  O  O   . GLU   A  1 207 ? 10.297  5.617   -47.041  1.00 33.42  ? 508  GLU   A O   1 
ATOM   1666  C  CB  . GLU   A  1 207 ? 10.194  6.106   -43.799  1.00 46.27  ? 508  GLU   A CB  1 
ATOM   1667  C  CG  . GLU   A  1 207 ? 10.284  7.295   -42.845  1.00 63.85  ? 508  GLU   A CG  1 
ATOM   1668  C  CD  . GLU   A  1 207 ? 11.094  7.018   -41.577  1.00 72.74  ? 508  GLU   A CD  1 
ATOM   1669  O  OE1 . GLU   A  1 207 ? 11.256  5.835   -41.196  1.00 72.29  ? 508  GLU   A OE1 1 
ATOM   1670  O  OE2 . GLU   A  1 207 ? 11.561  8.002   -40.960  1.00 74.05  ? 508  GLU   A OE2 1 
ATOM   1671  N  N   . ILE   A  1 208 ? 8.852   4.213   -46.035  1.00 40.39  ? 509  ILE   A N   1 
ATOM   1672  C  CA  . ILE   A  1 208 ? 8.946   3.226   -47.108  1.00 38.35  ? 509  ILE   A CA  1 
ATOM   1673  C  C   . ILE   A  1 208 ? 8.456   3.830   -48.417  1.00 38.85  ? 509  ILE   A C   1 
ATOM   1674  O  O   . ILE   A  1 208 ? 9.111   3.721   -49.462  1.00 38.99  ? 509  ILE   A O   1 
ATOM   1675  C  CB  . ILE   A  1 208 ? 8.148   1.961   -46.747  1.00 39.09  ? 509  ILE   A CB  1 
ATOM   1676  C  CG1 . ILE   A  1 208 ? 8.791   1.237   -45.563  1.00 41.67  ? 509  ILE   A CG1 1 
ATOM   1677  C  CG2 . ILE   A  1 208 ? 8.072   1.044   -47.946  1.00 35.81  ? 509  ILE   A CG2 1 
ATOM   1678  C  CD1 . ILE   A  1 208 ? 7.839   0.292   -44.835  1.00 43.88  ? 509  ILE   A CD1 1 
ATOM   1679  N  N   . CYS   A  1 209 ? 7.303   4.499   -48.369  1.00 38.05  ? 510  CYS   A N   1 
ATOM   1680  C  CA  . CYS   A  1 209 ? 6.765   5.152   -49.559  1.00 37.79  ? 510  CYS   A CA  1 
ATOM   1681  C  C   . CYS   A  1 209 ? 7.745   6.160   -50.128  1.00 37.31  ? 510  CYS   A C   1 
ATOM   1682  O  O   . CYS   A  1 209 ? 8.033   6.147   -51.331  1.00 38.91  ? 510  CYS   A O   1 
ATOM   1683  C  CB  . CYS   A  1 209 ? 5.444   5.836   -49.227  1.00 36.44  ? 510  CYS   A CB  1 
ATOM   1684  S  SG  . CYS   A  1 209 ? 4.141   4.654   -48.883  1.00 36.35  ? 510  CYS   A SG  1 
ATOM   1685  N  N   . ILE   A  1 210 ? 8.246   7.062   -49.278  1.00 34.09  ? 511  ILE   A N   1 
ATOM   1686  C  CA  . ILE   A  1 210 ? 9.190   8.073   -49.739  1.00 35.98  ? 511  ILE   A CA  1 
ATOM   1687  C  C   . ILE   A  1 210 ? 10.401  7.402   -50.362  1.00 39.55  ? 511  ILE   A C   1 
ATOM   1688  O  O   . ILE   A  1 210 ? 10.866  7.783   -51.445  1.00 43.98  ? 511  ILE   A O   1 
ATOM   1689  C  CB  . ILE   A  1 210 ? 9.593   9.001   -48.580  1.00 40.94  ? 511  ILE   A CB  1 
ATOM   1690  C  CG1 . ILE   A  1 210 ? 8.374   9.769   -48.078  1.00 45.10  ? 511  ILE   A CG1 1 
ATOM   1691  C  CG2 . ILE   A  1 210 ? 10.697  9.968   -49.031  1.00 36.44  ? 511  ILE   A CG2 1 
ATOM   1692  C  CD1 . ILE   A  1 210 ? 8.647   10.601  -46.844  1.00 49.42  ? 511  ILE   A CD1 1 
ATOM   1693  N  N   . GLN   A  1 211 ? 10.903  6.363   -49.699  1.00 37.03  ? 512  GLN   A N   1 
ATOM   1694  C  CA  . GLN   A  1 211 ? 12.042  5.618   -50.206  1.00 42.56  ? 512  GLN   A CA  1 
ATOM   1695  C  C   . GLN   A  1 211 ? 11.713  4.902   -51.509  1.00 45.47  ? 512  GLN   A C   1 
ATOM   1696  O  O   . GLN   A  1 211 ? 12.612  4.657   -52.317  1.00 50.13  ? 512  GLN   A O   1 
ATOM   1697  C  CB  . GLN   A  1 211 ? 12.503  4.644   -49.121  1.00 53.88  ? 512  GLN   A CB  1 
ATOM   1698  C  CG  . GLN   A  1 211 ? 13.680  3.790   -49.486  1.00 67.12  ? 512  GLN   A CG  1 
ATOM   1699  C  CD  . GLN   A  1 211 ? 13.280  2.345   -49.668  1.00 80.79  ? 512  GLN   A CD  1 
ATOM   1700  O  OE1 . GLN   A  1 211 ? 13.497  1.758   -50.730  1.00 81.53  ? 512  GLN   A OE1 1 
ATOM   1701  N  NE2 . GLN   A  1 211 ? 12.687  1.758   -48.628  1.00 82.61  ? 512  GLN   A NE2 1 
ATOM   1702  N  N   . GLN   A  1 212 ? 10.443  4.593   -51.749  1.00 41.37  ? 513  GLN   A N   1 
ATOM   1703  C  CA  . GLN   A  1 212 ? 10.017  3.979   -52.994  1.00 42.58  ? 513  GLN   A CA  1 
ATOM   1704  C  C   . GLN   A  1 212 ? 9.759   5.001   -54.087  1.00 51.12  ? 513  GLN   A C   1 
ATOM   1705  O  O   . GLN   A  1 212 ? 9.279   4.632   -55.164  1.00 53.84  ? 513  GLN   A O   1 
ATOM   1706  C  CB  . GLN   A  1 212 ? 8.763   3.131   -52.764  1.00 48.62  ? 513  GLN   A CB  1 
ATOM   1707  C  CG  . GLN   A  1 212 ? 9.056   1.768   -52.166  1.00 52.13  ? 513  GLN   A CG  1 
ATOM   1708  C  CD  . GLN   A  1 212 ? 10.210  1.076   -52.870  1.00 55.83  ? 513  GLN   A CD  1 
ATOM   1709  O  OE1 . GLN   A  1 212 ? 11.316  0.999   -52.338  1.00 58.62  ? 513  GLN   A OE1 1 
ATOM   1710  N  NE2 . GLN   A  1 212 ? 9.959   0.578   -54.075  1.00 55.14  ? 513  GLN   A NE2 1 
ATOM   1711  N  N   . GLY   A  1 213 ? 10.068  6.268   -53.840  1.00 50.31  ? 514  GLY   A N   1 
ATOM   1712  C  CA  . GLY   A  1 213 ? 9.908   7.300   -54.838  1.00 46.47  ? 514  GLY   A CA  1 
ATOM   1713  C  C   . GLY   A  1 213 ? 8.730   8.221   -54.625  1.00 44.78  ? 514  GLY   A C   1 
ATOM   1714  O  O   . GLY   A  1 213 ? 8.537   9.140   -55.428  1.00 47.41  ? 514  GLY   A O   1 
ATOM   1715  N  N   . TRP   A  1 214 ? 7.934   8.008   -53.580  1.00 42.27  ? 515  TRP   A N   1 
ATOM   1716  C  CA  . TRP   A  1 214 ? 6.809   8.898   -53.329  1.00 41.52  ? 515  TRP   A CA  1 
ATOM   1717  C  C   . TRP   A  1 214 ? 7.318   10.287  -52.971  1.00 47.33  ? 515  TRP   A C   1 
ATOM   1718  O  O   . TRP   A  1 214 ? 8.250   10.438  -52.175  1.00 48.32  ? 515  TRP   A O   1 
ATOM   1719  C  CB  . TRP   A  1 214 ? 5.921   8.360   -52.210  1.00 34.21  ? 515  TRP   A CB  1 
ATOM   1720  C  CG  . TRP   A  1 214 ? 4.660   9.167   -52.017  1.00 41.57  ? 515  TRP   A CG  1 
ATOM   1721  C  CD1 . TRP   A  1 214 ? 3.734   9.479   -52.973  1.00 41.97  ? 515  TRP   A CD1 1 
ATOM   1722  C  CD2 . TRP   A  1 214 ? 4.179   9.740   -50.793  1.00 39.77  ? 515  TRP   A CD2 1 
ATOM   1723  N  NE1 . TRP   A  1 214 ? 2.711   10.216  -52.421  1.00 35.21  ? 515  TRP   A NE1 1 
ATOM   1724  C  CE2 . TRP   A  1 214 ? 2.960   10.390  -51.086  1.00 34.54  ? 515  TRP   A CE2 1 
ATOM   1725  C  CE3 . TRP   A  1 214 ? 4.657   9.765   -49.481  1.00 37.85  ? 515  TRP   A CE3 1 
ATOM   1726  C  CZ2 . TRP   A  1 214 ? 2.214   11.050  -50.116  1.00 36.60  ? 515  TRP   A CZ2 1 
ATOM   1727  C  CZ3 . TRP   A  1 214 ? 3.914   10.435  -48.515  1.00 41.23  ? 515  TRP   A CZ3 1 
ATOM   1728  C  CH2 . TRP   A  1 214 ? 2.709   11.068  -48.840  1.00 35.92  ? 515  TRP   A CH2 1 
ATOM   1729  N  N   . LYS   A  1 215 ? 6.705   11.298  -53.578  1.00 40.98  ? 516  LYS   A N   1 
ATOM   1730  C  CA  . LYS   A  1 215 ? 7.008   12.694  -53.317  1.00 41.93  ? 516  LYS   A CA  1 
ATOM   1731  C  C   . LYS   A  1 215 ? 6.016   13.194  -52.283  1.00 49.35  ? 516  LYS   A C   1 
ATOM   1732  O  O   . LYS   A  1 215 ? 4.854   13.468  -52.611  1.00 61.56  ? 516  LYS   A O   1 
ATOM   1733  C  CB  . LYS   A  1 215 ? 6.926   13.526  -54.598  1.00 55.00  ? 516  LYS   A CB  1 
ATOM   1734  C  CG  . LYS   A  1 215 ? 7.862   13.042  -55.698  1.00 62.29  ? 516  LYS   A CG  1 
ATOM   1735  C  CD  . LYS   A  1 215 ? 9.319   13.301  -55.331  1.00 69.27  ? 516  LYS   A CD  1 
ATOM   1736  C  CE  . LYS   A  1 215 ? 10.271  12.934  -56.468  1.00 68.82  ? 516  LYS   A CE  1 
ATOM   1737  N  NZ  . LYS   A  1 215 ? 10.822  11.567  -56.279  1.00 63.35  ? 516  LYS   A NZ  1 
ATOM   1738  N  N   . PRO   A  1 216 ? 6.424   13.296  -51.027  1.00 45.54  ? 517  PRO   A N   1 
ATOM   1739  C  CA  . PRO   A  1 216 ? 5.502   13.687  -49.984  1.00 42.72  ? 517  PRO   A CA  1 
ATOM   1740  C  C   . PRO   A  1 216 ? 5.221   15.173  -50.052  1.00 46.68  ? 517  PRO   A C   1 
ATOM   1741  O  O   . PRO   A  1 216 ? 6.145   15.984  -50.212  1.00 48.68  ? 517  PRO   A O   1 
ATOM   1742  C  CB  . PRO   A  1 216 ? 6.259   13.325  -48.704  1.00 50.80  ? 517  PRO   A CB  1 
ATOM   1743  C  CG  . PRO   A  1 216 ? 7.687   13.483  -49.082  1.00 55.62  ? 517  PRO   A CG  1 
ATOM   1744  C  CD  . PRO   A  1 216 ? 7.784   13.065  -50.514  1.00 45.85  ? 517  PRO   A CD  1 
ATOM   1745  N  N   . PRO   A  1 217 ? 3.953   15.573  -49.971  1.00 47.58  ? 518  PRO   A N   1 
ATOM   1746  C  CA  . PRO   A  1 217 ? 3.656   17.001  -49.767  1.00 44.93  ? 518  PRO   A CA  1 
ATOM   1747  C  C   . PRO   A  1 217 ? 4.036   17.487  -48.376  1.00 48.95  ? 518  PRO   A C   1 
ATOM   1748  O  O   . PRO   A  1 217 ? 4.123   18.705  -48.159  1.00 51.17  ? 518  PRO   A O   1 
ATOM   1749  C  CB  . PRO   A  1 217 ? 2.143   17.093  -50.014  1.00 40.70  ? 518  PRO   A CB  1 
ATOM   1750  C  CG  . PRO   A  1 217 ? 1.631   15.692  -49.982  1.00 41.92  ? 518  PRO   A CG  1 
ATOM   1751  C  CD  . PRO   A  1 217 ? 2.760   14.762  -50.262  1.00 42.08  ? 518  PRO   A CD  1 
ATOM   1752  N  N   . ARG   A  1 218 ? 4.287   16.570  -47.441  1.00 40.35  ? 519  ARG   A N   1 
ATOM   1753  C  CA  . ARG   A  1 218 ? 4.759   16.905  -46.098  1.00 50.83  ? 519  ARG   A CA  1 
ATOM   1754  C  C   . ARG   A  1 218 ? 3.806   17.866  -45.390  1.00 50.35  ? 519  ARG   A C   1 
ATOM   1755  O  O   . ARG   A  1 218 ? 4.224   18.856  -44.783  1.00 52.18  ? 519  ARG   A O   1 
ATOM   1756  C  CB  . ARG   A  1 218 ? 6.185   17.457  -46.140  1.00 57.31  ? 519  ARG   A CB  1 
ATOM   1757  C  CG  . ARG   A  1 218 ? 7.143   16.516  -46.856  1.00 64.03  ? 519  ARG   A CG  1 
ATOM   1758  C  CD  . ARG   A  1 218 ? 8.598   16.855  -46.589  1.00 69.05  ? 519  ARG   A CD  1 
ATOM   1759  N  NE  . ARG   A  1 218 ? 9.096   16.215  -45.375  1.00 72.89  ? 519  ARG   A NE  1 
ATOM   1760  C  CZ  . ARG   A  1 218 ? 9.850   15.117  -45.358  1.00 73.43  ? 519  ARG   A CZ  1 
ATOM   1761  N  NH1 . ARG   A  1 218 ? 10.253  14.615  -44.196  1.00 76.76  ? 519  ARG   A NH1 1 
ATOM   1762  N  NH2 . ARG   A  1 218 ? 10.208  14.527  -46.495  1.00 65.87  ? 519  ARG   A NH2 1 
ATOM   1763  N  N   . GLY   A  1 219 ? 2.507   17.571  -45.486  1.00 46.87  ? 520  GLY   A N   1 
ATOM   1764  C  CA  . GLY   A  1 219 ? 1.499   18.209  -44.672  1.00 45.69  ? 520  GLY   A CA  1 
ATOM   1765  C  C   . GLY   A  1 219 ? 1.027   17.288  -43.554  1.00 46.33  ? 520  GLY   A C   1 
ATOM   1766  O  O   . GLY   A  1 219 ? 1.518   16.178  -43.371  1.00 40.12  ? 520  GLY   A O   1 
ATOM   1767  N  N   . ARG   A  1 220 ? 0.032   17.775  -42.806  1.00 49.40  ? 521  ARG   A N   1 
ATOM   1768  C  CA  . ARG   A  1 220 ? -0.472  17.037  -41.651  1.00 45.07  ? 521  ARG   A CA  1 
ATOM   1769  C  C   . ARG   A  1 220 ? -1.473  15.949  -42.027  1.00 40.46  ? 521  ARG   A C   1 
ATOM   1770  O  O   . ARG   A  1 220 ? -1.720  15.038  -41.221  1.00 32.46  ? 521  ARG   A O   1 
ATOM   1771  C  CB  . ARG   A  1 220 ? -1.109  18.010  -40.653  1.00 45.76  ? 521  ARG   A CB  1 
ATOM   1772  C  CG  . ARG   A  1 220 ? -1.267  17.414  -39.271  1.00 50.30  ? 521  ARG   A CG  1 
ATOM   1773  C  CD  . ARG   A  1 220 ? -1.880  18.382  -38.276  1.00 55.98  ? 521  ARG   A CD  1 
ATOM   1774  N  NE  . ARG   A  1 220 ? -1.742  17.852  -36.926  1.00 57.02  ? 521  ARG   A NE  1 
ATOM   1775  C  CZ  . ARG   A  1 220 ? -2.476  18.223  -35.884  1.00 62.71  ? 521  ARG   A CZ  1 
ATOM   1776  N  NH1 . ARG   A  1 220 ? -3.429  19.134  -36.019  1.00 59.64  ? 521  ARG   A NH1 1 
ATOM   1777  N  NH2 . ARG   A  1 220 ? -2.257  17.663  -34.700  1.00 63.70  ? 521  ARG   A NH2 1 
ATOM   1778  N  N   . PHE   A  1 221 ? -2.054  16.017  -43.225  1.00 33.55  ? 522  PHE   A N   1 
ATOM   1779  C  CA  . PHE   A  1 221 ? -3.070  15.065  -43.665  1.00 33.19  ? 522  PHE   A CA  1 
ATOM   1780  C  C   . PHE   A  1 221 ? -2.829  14.713  -45.134  1.00 38.55  ? 522  PHE   A C   1 
ATOM   1781  O  O   . PHE   A  1 221 ? -3.662  14.933  -46.012  1.00 47.98  ? 522  PHE   A O   1 
ATOM   1782  C  CB  . PHE   A  1 221 ? -4.483  15.616  -43.479  1.00 35.07  ? 522  PHE   A CB  1 
ATOM   1783  C  CG  . PHE   A  1 221 ? -4.821  15.969  -42.050  1.00 40.25  ? 522  PHE   A CG  1 
ATOM   1784  C  CD1 . PHE   A  1 221 ? -4.851  17.297  -41.644  1.00 39.26  ? 522  PHE   A CD1 1 
ATOM   1785  C  CD2 . PHE   A  1 221 ? -5.112  14.979  -41.121  1.00 33.77  ? 522  PHE   A CD2 1 
ATOM   1786  C  CE1 . PHE   A  1 221 ? -5.163  17.634  -40.340  1.00 43.11  ? 522  PHE   A CE1 1 
ATOM   1787  C  CE2 . PHE   A  1 221 ? -5.429  15.315  -39.806  1.00 35.92  ? 522  PHE   A CE2 1 
ATOM   1788  C  CZ  . PHE   A  1 221 ? -5.447  16.646  -39.419  1.00 36.16  ? 522  PHE   A CZ  1 
ATOM   1789  N  N   . ASP   A  1 222 ? -1.662  14.143  -45.412  1.00 39.22  ? 523  ASP   A N   1 
ATOM   1790  C  CA  . ASP   A  1 222 ? -1.313  13.708  -46.760  1.00 39.40  ? 523  ASP   A CA  1 
ATOM   1791  C  C   . ASP   A  1 222 ? -1.810  12.286  -46.945  1.00 38.29  ? 523  ASP   A C   1 
ATOM   1792  O  O   . ASP   A  1 222 ? -1.284  11.361  -46.319  1.00 35.03  ? 523  ASP   A O   1 
ATOM   1793  C  CB  . ASP   A  1 222 ? 0.193   13.783  -46.979  1.00 41.23  ? 523  ASP   A CB  1 
ATOM   1794  C  CG  . ASP   A  1 222 ? 0.723   15.185  -46.856  1.00 42.83  ? 523  ASP   A CG  1 
ATOM   1795  O  OD1 . ASP   A  1 222 ? -0.077  16.133  -47.021  1.00 41.76  ? 523  ASP   A OD1 1 
ATOM   1796  O  OD2 . ASP   A  1 222 ? 1.938   15.337  -46.608  1.00 43.70  ? 523  ASP   A OD2 1 
ATOM   1797  N  N   . VAL   A  1 223 ? -2.832  12.107  -47.786  1.00 30.38  ? 524  VAL   A N   1 
ATOM   1798  C  CA  . VAL   A  1 223 ? -3.309  10.751  -48.050  1.00 29.40  ? 524  VAL   A CA  1 
ATOM   1799  C  C   . VAL   A  1 223 ? -2.157  9.957   -48.637  1.00 28.36  ? 524  VAL   A C   1 
ATOM   1800  O  O   . VAL   A  1 223 ? -1.547  10.366  -49.632  1.00 30.39  ? 524  VAL   A O   1 
ATOM   1801  C  CB  . VAL   A  1 223 ? -4.523  10.750  -48.988  1.00 33.29  ? 524  VAL   A CB  1 
ATOM   1802  C  CG1 . VAL   A  1 223 ? -4.885  9.313   -49.368  1.00 27.76  ? 524  VAL   A CG1 1 
ATOM   1803  C  CG2 . VAL   A  1 223 ? -5.713  11.428  -48.340  1.00 29.60  ? 524  VAL   A CG2 1 
ATOM   1804  N  N   . LEU   A  1 224 ? -1.826  8.846   -47.999  1.00 23.78  ? 525  LEU   A N   1 
ATOM   1805  C  CA  . LEU   A  1 224 ? -0.701  8.050   -48.430  1.00 27.10  ? 525  LEU   A CA  1 
ATOM   1806  C  C   . LEU   A  1 224 ? -1.006  7.365   -49.762  1.00 28.28  ? 525  LEU   A C   1 
ATOM   1807  O  O   . LEU   A  1 224 ? -2.168  7.091   -50.084  1.00 23.82  ? 525  LEU   A O   1 
ATOM   1808  C  CB  . LEU   A  1 224 ? -0.363  6.993   -47.382  1.00 24.44  ? 525  LEU   A CB  1 
ATOM   1809  C  CG  . LEU   A  1 224 ? 0.405   7.521   -46.178  1.00 31.12  ? 525  LEU   A CG  1 
ATOM   1810  C  CD1 . LEU   A  1 224 ? 0.200   6.610   -44.969  1.00 27.33  ? 525  LEU   A CD1 1 
ATOM   1811  C  CD2 . LEU   A  1 224 ? 1.875   7.642   -46.561  1.00 35.20  ? 525  LEU   A CD2 1 
ATOM   1812  N  N   . PRO   A  1 225 ? 0.019   7.059   -50.539  1.00 24.44  ? 526  PRO   A N   1 
ATOM   1813  C  CA  . PRO   A  1 225 ? -0.197  6.256   -51.739  1.00 24.13  ? 526  PRO   A CA  1 
ATOM   1814  C  C   . PRO   A  1 225 ? -0.489  4.830   -51.332  1.00 32.10  ? 526  PRO   A C   1 
ATOM   1815  O  O   . PRO   A  1 225 ? -0.204  4.406   -50.207  1.00 30.94  ? 526  PRO   A O   1 
ATOM   1816  C  CB  . PRO   A  1 225 ? 1.138   6.360   -52.473  1.00 25.35  ? 526  PRO   A CB  1 
ATOM   1817  C  CG  . PRO   A  1 225 ? 2.126   6.485   -51.375  1.00 29.72  ? 526  PRO   A CG  1 
ATOM   1818  C  CD  . PRO   A  1 225 ? 1.450   7.338   -50.323  1.00 28.27  ? 526  PRO   A CD  1 
ATOM   1819  N  N   . LEU   A  1 226 ? -1.088  4.091   -52.257  1.00 24.33  ? 527  LEU   A N   1 
ATOM   1820  C  CA  . LEU   A  1 226 ? -1.187  2.652   -52.090  1.00 27.02  ? 527  LEU   A CA  1 
ATOM   1821  C  C   . LEU   A  1 226 ? 0.142   2.016   -52.461  1.00 26.74  ? 527  LEU   A C   1 
ATOM   1822  O  O   . LEU   A  1 226 ? 0.784   2.421   -53.435  1.00 32.47  ? 527  LEU   A O   1 
ATOM   1823  C  CB  . LEU   A  1 226 ? -2.298  2.082   -52.956  1.00 27.85  ? 527  LEU   A CB  1 
ATOM   1824  C  CG  . LEU   A  1 226 ? -3.704  2.504   -52.558  1.00 31.07  ? 527  LEU   A CG  1 
ATOM   1825  C  CD1 . LEU   A  1 226 ? -4.650  2.118   -53.684  1.00 27.32  ? 527  LEU   A CD1 1 
ATOM   1826  C  CD2 . LEU   A  1 226 ? -4.116  1.869   -51.232  1.00 24.75  ? 527  LEU   A CD2 1 
ATOM   1827  N  N   . LEU   A  1 227 ? 0.574   1.051   -51.651  1.00 26.64  ? 528  LEU   A N   1 
ATOM   1828  C  CA  . LEU   A  1 227 ? 1.790   0.274   -51.897  1.00 25.76  ? 528  LEU   A CA  1 
ATOM   1829  C  C   . LEU   A  1 227 ? 1.310   -1.150  -52.096  1.00 27.53  ? 528  LEU   A C   1 
ATOM   1830  O  O   . LEU   A  1 227 ? 1.014   -1.845  -51.119  1.00 25.95  ? 528  LEU   A O   1 
ATOM   1831  C  CB  . LEU   A  1 227 ? 2.769   0.357   -50.733  1.00 31.28  ? 528  LEU   A CB  1 
ATOM   1832  C  CG  . LEU   A  1 227 ? 4.234   0.737   -50.950  1.00 38.82  ? 528  LEU   A CG  1 
ATOM   1833  C  CD1 . LEU   A  1 227 ? 5.081   0.238   -49.774  1.00 32.27  ? 528  LEU   A CD1 1 
ATOM   1834  C  CD2 . LEU   A  1 227 ? 4.790   0.294   -52.319  1.00 32.99  ? 528  LEU   A CD2 1 
ATOM   1835  N  N   . LEU   A  1 228 ? 1.229   -1.578  -53.353  1.00 33.25  ? 529  LEU   A N   1 
ATOM   1836  C  CA  . LEU   A  1 228 ? 0.527   -2.796  -53.733  1.00 33.34  ? 529  LEU   A CA  1 
ATOM   1837  C  C   . LEU   A  1 228 ? 1.503   -3.846  -54.234  1.00 34.29  ? 529  LEU   A C   1 
ATOM   1838  O  O   . LEU   A  1 228 ? 2.304   -3.569  -55.139  1.00 28.30  ? 529  LEU   A O   1 
ATOM   1839  C  CB  . LEU   A  1 228 ? -0.505  -2.498  -54.815  1.00 25.18  ? 529  LEU   A CB  1 
ATOM   1840  C  CG  . LEU   A  1 228 ? -1.492  -1.406  -54.402  1.00 21.96  ? 529  LEU   A CG  1 
ATOM   1841  C  CD1 . LEU   A  1 228 ? -2.532  -1.245  -55.496  1.00 21.86  ? 529  LEU   A CD1 1 
ATOM   1842  C  CD2 . LEU   A  1 228 ? -2.150  -1.743  -53.061  1.00 21.88  ? 529  LEU   A CD2 1 
ATOM   1843  N  N   . GLN   A  1 229 ? 1.406   -5.051  -53.670  1.00 26.94  ? 530  GLN   A N   1 
ATOM   1844  C  CA  . GLN   A  1 229 ? 2.230   -6.192  -54.056  1.00 29.35  ? 530  GLN   A CA  1 
ATOM   1845  C  C   . GLN   A  1 229 ? 1.357   -7.298  -54.627  1.00 32.12  ? 530  GLN   A C   1 
ATOM   1846  O  O   . GLN   A  1 229 ? 0.442   -7.787  -53.950  1.00 28.11  ? 530  GLN   A O   1 
ATOM   1847  C  CB  . GLN   A  1 229 ? 3.016   -6.737  -52.870  1.00 29.27  ? 530  GLN   A CB  1 
ATOM   1848  C  CG  . GLN   A  1 229 ? 3.633   -8.098  -53.140  1.00 30.29  ? 530  GLN   A CG  1 
ATOM   1849  C  CD  . GLN   A  1 229 ? 4.358   -8.625  -51.924  1.00 35.01  ? 530  GLN   A CD  1 
ATOM   1850  O  OE1 . GLN   A  1 229 ? 4.101   -8.184  -50.812  1.00 33.69  ? 530  GLN   A OE1 1 
ATOM   1851  N  NE2 . GLN   A  1 229 ? 5.285   -9.549  -52.133  1.00 49.00  ? 530  GLN   A NE2 1 
ATOM   1852  N  N   . ALA   A  1 230 ? 1.669   -7.710  -55.850  1.00 29.52  ? 531  ALA   A N   1 
ATOM   1853  C  CA  . ALA   A  1 230 ? 0.982   -8.777  -56.564  1.00 30.68  ? 531  ALA   A CA  1 
ATOM   1854  C  C   . ALA   A  1 230 ? 1.943   -9.925  -56.834  1.00 33.22  ? 531  ALA   A C   1 
ATOM   1855  O  O   . ALA   A  1 230 ? 3.089   -9.706  -57.248  1.00 29.65  ? 531  ALA   A O   1 
ATOM   1856  C  CB  . ALA   A  1 230 ? 0.422   -8.285  -57.896  1.00 37.60  ? 531  ALA   A CB  1 
ATOM   1857  N  N   . ASN   A  1 231 ? 1.467   -11.145 -56.591  1.00 34.42  ? 532  ASN   A N   1 
ATOM   1858  C  CA  . ASN   A  1 231 ? 2.188   -12.361 -56.958  1.00 37.95  ? 532  ASN   A CA  1 
ATOM   1859  C  C   . ASN   A  1 231 ? 3.626   -12.353 -56.442  1.00 38.99  ? 532  ASN   A C   1 
ATOM   1860  O  O   . ASN   A  1 231 ? 4.559   -12.793 -57.119  1.00 40.62  ? 532  ASN   A O   1 
ATOM   1861  C  CB  . ASN   A  1 231 ? 2.157   -12.568 -58.466  1.00 39.57  ? 532  ASN   A CB  1 
ATOM   1862  C  CG  . ASN   A  1 231 ? 2.365   -14.011 -58.844  1.00 55.75  ? 532  ASN   A CG  1 
ATOM   1863  O  OD1 . ASN   A  1 231 ? 2.046   -14.914 -58.064  1.00 55.70  ? 532  ASN   A OD1 1 
ATOM   1864  N  ND2 . ASN   A  1 231 ? 2.912   -14.246 -60.037  1.00 55.93  ? 532  ASN   A ND2 1 
ATOM   1865  N  N   . GLY   A  1 232 ? 3.804   -11.838 -55.229  1.00 35.37  ? 533  GLY   A N   1 
ATOM   1866  C  CA  . GLY   A  1 232 ? 5.085   -11.846 -54.557  1.00 36.46  ? 533  GLY   A CA  1 
ATOM   1867  C  C   . GLY   A  1 232 ? 6.116   -10.874 -55.084  1.00 40.68  ? 533  GLY   A C   1 
ATOM   1868  O  O   . GLY   A  1 232 ? 7.221   -10.820 -54.535  1.00 40.66  ? 533  GLY   A O   1 
ATOM   1869  N  N   . ASN   A  1 233 ? 5.798   -10.095 -56.114  1.00 33.23  ? 534  ASN   A N   1 
ATOM   1870  C  CA  . ASN   A  1 233 ? 6.765   -9.172  -56.683  1.00 35.85  ? 534  ASN   A CA  1 
ATOM   1871  C  C   . ASN   A  1 233 ? 6.941   -7.945  -55.783  1.00 33.26  ? 534  ASN   A C   1 
ATOM   1872  O  O   . ASN   A  1 233 ? 6.182   -7.714  -54.839  1.00 30.68  ? 534  ASN   A O   1 
ATOM   1873  C  CB  . ASN   A  1 233 ? 6.325   -8.763  -58.092  1.00 43.05  ? 534  ASN   A CB  1 
ATOM   1874  C  CG  . ASN   A  1 233 ? 6.194   -9.958  -59.024  1.00 46.42  ? 534  ASN   A CG  1 
ATOM   1875  O  OD1 . ASN   A  1 233 ? 7.125   -10.751 -59.168  1.00 52.85  ? 534  ASN   A OD1 1 
ATOM   1876  N  ND2 . ASN   A  1 233 ? 5.029   -10.109 -59.636  1.00 43.62  ? 534  ASN   A ND2 1 
ATOM   1877  N  N   . ASP   A  1 234 ? 7.967   -7.153  -56.084  1.00 34.14  ? 535  ASP   A N   1 
ATOM   1878  C  CA  . ASP   A  1 234 ? 8.179   -5.902  -55.370  1.00 36.02  ? 535  ASP   A CA  1 
ATOM   1879  C  C   . ASP   A  1 234 ? 6.902   -5.060  -55.395  1.00 30.73  ? 535  ASP   A C   1 
ATOM   1880  O  O   . ASP   A  1 234 ? 6.185   -5.053  -56.404  1.00 31.13  ? 535  ASP   A O   1 
ATOM   1881  C  CB  . ASP   A  1 234 ? 9.334   -5.116  -55.998  1.00 41.27  ? 535  ASP   A CB  1 
ATOM   1882  C  CG  . ASP   A  1 234 ? 10.690  -5.697  -55.656  1.00 44.89  ? 535  ASP   A CG  1 
ATOM   1883  O  OD1 . ASP   A  1 234 ? 11.697  -5.217  -56.217  1.00 46.83  ? 535  ASP   A OD1 1 
ATOM   1884  O  OD2 . ASP   A  1 234 ? 10.750  -6.631  -54.828  1.00 50.30  ? 535  ASP   A OD2 1 
ATOM   1885  N  N   . PRO   A  1 235 ? 6.571   -4.363  -54.314  1.00 30.59  ? 536  PRO   A N   1 
ATOM   1886  C  CA  . PRO   A  1 235 ? 5.341   -3.568  -54.313  1.00 31.71  ? 536  PRO   A CA  1 
ATOM   1887  C  C   . PRO   A  1 235 ? 5.514   -2.307  -55.145  1.00 33.99  ? 536  PRO   A C   1 
ATOM   1888  O  O   . PRO   A  1 235 ? 6.628   -1.865  -55.421  1.00 36.75  ? 536  PRO   A O   1 
ATOM   1889  C  CB  . PRO   A  1 235 ? 5.124   -3.252  -52.829  1.00 28.21  ? 536  PRO   A CB  1 
ATOM   1890  C  CG  . PRO   A  1 235 ? 6.502   -3.265  -52.241  1.00 28.42  ? 536  PRO   A CG  1 
ATOM   1891  C  CD  . PRO   A  1 235 ? 7.259   -4.327  -53.011  1.00 31.27  ? 536  PRO   A CD  1 
ATOM   1892  N  N   . GLU   A  1 236 ? 4.384   -1.742  -55.578  1.00 28.57  ? 537  GLU   A N   1 
ATOM   1893  C  CA  . GLU   A  1 236 ? 4.384   -0.599  -56.477  1.00 26.41  ? 537  GLU   A CA  1 
ATOM   1894  C  C   . GLU   A  1 236 ? 3.483   0.500   -55.927  1.00 30.75  ? 537  GLU   A C   1 
ATOM   1895  O  O   . GLU   A  1 236 ? 2.408   0.218   -55.398  1.00 31.52  ? 537  GLU   A O   1 
ATOM   1896  C  CB  . GLU   A  1 236 ? 3.920   -1.028  -57.892  1.00 26.73  ? 537  GLU   A CB  1 
ATOM   1897  C  CG  . GLU   A  1 236 ? 4.782   -2.148  -58.462  1.00 30.55  ? 537  GLU   A CG  1 
ATOM   1898  C  CD  . GLU   A  1 236 ? 4.257   -2.737  -59.775  1.00 42.29  ? 537  GLU   A CD  1 
ATOM   1899  O  OE1 . GLU   A  1 236 ? 3.522   -2.049  -60.528  1.00 43.55  ? 537  GLU   A OE1 1 
ATOM   1900  O  OE2 . GLU   A  1 236 ? 4.602   -3.907  -60.049  1.00 41.72  ? 537  GLU   A OE2 1 
ATOM   1901  N  N   . LEU   A  1 237 ? 3.916   1.750   -56.074  1.00 35.32  ? 538  LEU   A N   1 
ATOM   1902  C  CA  . LEU   A  1 237 ? 3.166   2.895   -55.573  1.00 28.31  ? 538  LEU   A CA  1 
ATOM   1903  C  C   . LEU   A  1 237 ? 2.084   3.337   -56.551  1.00 29.32  ? 538  LEU   A C   1 
ATOM   1904  O  O   . LEU   A  1 237 ? 2.311   3.415   -57.756  1.00 30.13  ? 538  LEU   A O   1 
ATOM   1905  C  CB  . LEU   A  1 237 ? 4.108   4.075   -55.319  1.00 27.48  ? 538  LEU   A CB  1 
ATOM   1906  C  CG  . LEU   A  1 237 ? 5.070   3.952   -54.146  1.00 35.28  ? 538  LEU   A CG  1 
ATOM   1907  C  CD1 . LEU   A  1 237 ? 6.113   5.054   -54.203  1.00 29.52  ? 538  LEU   A CD1 1 
ATOM   1908  C  CD2 . LEU   A  1 237 ? 4.293   4.005   -52.836  1.00 34.33  ? 538  LEU   A CD2 1 
ATOM   1909  N  N   . PHE   A  1 238 ? 0.914   3.665   -56.017  1.00 27.71  ? 539  PHE   A N   1 
ATOM   1910  C  CA  . PHE   A  1 238 ? -0.164  4.247   -56.802  1.00 27.77  ? 539  PHE   A CA  1 
ATOM   1911  C  C   . PHE   A  1 238 ? -0.846  5.321   -55.981  1.00 32.06  ? 539  PHE   A C   1 
ATOM   1912  O  O   . PHE   A  1 238 ? -1.120  5.122   -54.796  1.00 35.06  ? 539  PHE   A O   1 
ATOM   1913  C  CB  . PHE   A  1 238 ? -1.218  3.211   -57.203  1.00 28.14  ? 539  PHE   A CB  1 
ATOM   1914  C  CG  . PHE   A  1 238 ? -0.671  2.071   -57.988  1.00 25.68  ? 539  PHE   A CG  1 
ATOM   1915  C  CD1 . PHE   A  1 238 ? -0.109  0.977   -57.341  1.00 25.09  ? 539  PHE   A CD1 1 
ATOM   1916  C  CD2 . PHE   A  1 238 ? -0.717  2.088   -59.382  1.00 24.41  ? 539  PHE   A CD2 1 
ATOM   1917  C  CE1 . PHE   A  1 238 ? 0.411   -0.088  -58.071  1.00 25.73  ? 539  PHE   A CE1 1 
ATOM   1918  C  CE2 . PHE   A  1 238 ? -0.207  1.026   -60.109  1.00 29.44  ? 539  PHE   A CE2 1 
ATOM   1919  C  CZ  . PHE   A  1 238 ? 0.355   -0.066  -59.450  1.00 27.37  ? 539  PHE   A CZ  1 
ATOM   1920  N  N   . GLN   A  1 239 ? -1.143  6.445   -56.610  1.00 35.54  ? 540  GLN   A N   1 
ATOM   1921  C  CA  . GLN   A  1 239 ? -1.877  7.507   -55.940  1.00 38.56  ? 540  GLN   A CA  1 
ATOM   1922  C  C   . GLN   A  1 239 ? -3.372  7.284   -56.129  1.00 32.23  ? 540  GLN   A C   1 
ATOM   1923  O  O   . GLN   A  1 239 ? -3.866  7.285   -57.262  1.00 26.73  ? 540  GLN   A O   1 
ATOM   1924  C  CB  . GLN   A  1 239 ? -1.470  8.867   -56.489  1.00 35.95  ? 540  GLN   A CB  1 
ATOM   1925  C  CG  . GLN   A  1 239 ? -2.213  10.005  -55.851  1.00 42.18  ? 540  GLN   A CG  1 
ATOM   1926  C  CD  . GLN   A  1 239 ? -2.055  11.277  -56.644  1.00 53.67  ? 540  GLN   A CD  1 
ATOM   1927  O  OE1 . GLN   A  1 239 ? -2.722  11.474  -57.663  1.00 46.94  ? 540  GLN   A OE1 1 
ATOM   1928  N  NE2 . GLN   A  1 239 ? -1.158  12.144  -56.195  1.00 66.90  ? 540  GLN   A NE2 1 
ATOM   1929  N  N   . ILE   A  1 240 ? -4.088  7.087   -55.032  1.00 28.64  ? 541  ILE   A N   1 
ATOM   1930  C  CA  . ILE   A  1 240 ? -5.548  6.996   -55.146  1.00 33.23  ? 541  ILE   A CA  1 
ATOM   1931  C  C   . ILE   A  1 240 ? -6.064  8.296   -55.742  1.00 34.19  ? 541  ILE   A C   1 
ATOM   1932  O  O   . ILE   A  1 240 ? -5.639  9.379   -55.302  1.00 33.81  ? 541  ILE   A O   1 
ATOM   1933  C  CB  . ILE   A  1 240 ? -6.181  6.737   -53.770  1.00 28.14  ? 541  ILE   A CB  1 
ATOM   1934  C  CG1 . ILE   A  1 240 ? -5.515  5.535   -53.107  1.00 26.30  ? 541  ILE   A CG1 1 
ATOM   1935  C  CG2 . ILE   A  1 240 ? -7.682  6.521   -53.905  1.00 28.63  ? 541  ILE   A CG2 1 
ATOM   1936  C  CD1 . ILE   A  1 240 ? -5.853  5.385   -51.619  1.00 33.24  ? 541  ILE   A CD1 1 
ATOM   1937  N  N   . PRO   A  1 241 ? -6.910  8.264   -56.769  1.00 35.34  ? 542  PRO   A N   1 
ATOM   1938  C  CA  . PRO   A  1 241 ? -7.489  9.508   -57.282  1.00 37.60  ? 542  PRO   A CA  1 
ATOM   1939  C  C   . PRO   A  1 241 ? -8.182  10.265  -56.164  1.00 34.49  ? 542  PRO   A C   1 
ATOM   1940  O  O   . PRO   A  1 241 ? -9.041  9.704   -55.462  1.00 30.02  ? 542  PRO   A O   1 
ATOM   1941  C  CB  . PRO   A  1 241 ? -8.484  9.026   -58.348  1.00 36.85  ? 542  PRO   A CB  1 
ATOM   1942  C  CG  . PRO   A  1 241 ? -7.900  7.745   -58.822  1.00 31.95  ? 542  PRO   A CG  1 
ATOM   1943  C  CD  . PRO   A  1 241 ? -7.276  7.105   -57.601  1.00 33.66  ? 542  PRO   A CD  1 
ATOM   1944  N  N   . PRO   A  1 242 ? -7.794  11.525  -55.938  1.00 29.40  ? 543  PRO   A N   1 
ATOM   1945  C  CA  . PRO   A  1 242 ? -8.304  12.246  -54.760  1.00 32.00  ? 543  PRO   A CA  1 
ATOM   1946  C  C   . PRO   A  1 242 ? -9.809  12.406  -54.771  1.00 35.98  ? 543  PRO   A C   1 
ATOM   1947  O  O   . PRO   A  1 242 ? -10.424 12.471  -53.698  1.00 36.36  ? 543  PRO   A O   1 
ATOM   1948  C  CB  . PRO   A  1 242 ? -7.579  13.598  -54.834  1.00 32.44  ? 543  PRO   A CB  1 
ATOM   1949  C  CG  . PRO   A  1 242 ? -6.341  13.314  -55.643  1.00 39.43  ? 543  PRO   A CG  1 
ATOM   1950  C  CD  . PRO   A  1 242 ? -6.762  12.293  -56.657  1.00 35.09  ? 543  PRO   A CD  1 
ATOM   1951  N  N   . GLU   A  1 243 ? -10.432 12.427  -55.954  1.00 31.05  ? 544  GLU   A N   1 
ATOM   1952  C  CA  . GLU   A  1 243 ? -11.887 12.484  -56.002  1.00 32.10  ? 544  GLU   A CA  1 
ATOM   1953  C  C   . GLU   A  1 243 ? -12.522 11.219  -55.449  1.00 29.39  ? 544  GLU   A C   1 
ATOM   1954  O  O   . GLU   A  1 243 ? -13.707 11.234  -55.107  1.00 31.94  ? 544  GLU   A O   1 
ATOM   1955  C  CB  . GLU   A  1 243 ? -12.375 12.733  -57.436  1.00 36.77  ? 544  GLU   A CB  1 
ATOM   1956  C  CG  . GLU   A  1 243 ? -12.092 11.595  -58.404  1.00 33.52  ? 544  GLU   A CG  1 
ATOM   1957  C  CD  . GLU   A  1 243 ? -10.743 11.735  -59.053  1.00 38.85  ? 544  GLU   A CD  1 
ATOM   1958  O  OE1 . GLU   A  1 243 ? -9.954  12.575  -58.580  1.00 34.51  ? 544  GLU   A OE1 1 
ATOM   1959  O  OE2 . GLU   A  1 243 ? -10.477 11.026  -60.052  1.00 52.41  ? 544  GLU   A OE2 1 
ATOM   1960  N  N   . LEU   A  1 244 ? -11.774 10.125  -55.355  1.00 27.00  ? 545  LEU   A N   1 
ATOM   1961  C  CA  . LEU   A  1 244 ? -12.312 8.947   -54.695  1.00 26.46  ? 545  LEU   A CA  1 
ATOM   1962  C  C   . LEU   A  1 244 ? -12.153 8.983   -53.181  1.00 27.06  ? 545  LEU   A C   1 
ATOM   1963  O  O   . LEU   A  1 244 ? -12.763 8.148   -52.509  1.00 25.09  ? 545  LEU   A O   1 
ATOM   1964  C  CB  . LEU   A  1 244 ? -11.645 7.673   -55.208  1.00 25.37  ? 545  LEU   A CB  1 
ATOM   1965  C  CG  . LEU   A  1 244 ? -11.892 7.289   -56.669  1.00 32.02  ? 545  LEU   A CG  1 
ATOM   1966  C  CD1 . LEU   A  1 244 ? -11.352 5.892   -56.909  1.00 29.63  ? 545  LEU   A CD1 1 
ATOM   1967  C  CD2 . LEU   A  1 244 ? -13.361 7.394   -57.063  1.00 32.97  ? 545  LEU   A CD2 1 
ATOM   1968  N  N   . VAL   A  1 245 ? -11.340 9.890   -52.637  1.00 27.82  ? 546  VAL   A N   1 
ATOM   1969  C  CA  . VAL   A  1 245 ? -11.038 9.911   -51.200  1.00 28.62  ? 546  VAL   A CA  1 
ATOM   1970  C  C   . VAL   A  1 245 ? -11.938 10.955  -50.556  1.00 27.36  ? 546  VAL   A C   1 
ATOM   1971  O  O   . VAL   A  1 245 ? -11.621 12.148  -50.542  1.00 30.24  ? 546  VAL   A O   1 
ATOM   1972  C  CB  . VAL   A  1 245 ? -9.566  10.215  -50.919  1.00 31.88  ? 546  VAL   A CB  1 
ATOM   1973  C  CG1 . VAL   A  1 245 ? -9.297  10.152  -49.418  1.00 27.48  ? 546  VAL   A CG1 1 
ATOM   1974  C  CG2 . VAL   A  1 245 ? -8.667  9.258   -51.657  1.00 30.97  ? 546  VAL   A CG2 1 
ATOM   1975  N  N   . LEU   A  1 246 ? -13.071 10.504  -50.032  1.00 24.76  ? 547  LEU   A N   1 
ATOM   1976  C  CA  . LEU   A  1 246 ? -13.991 11.400  -49.359  1.00 24.98  ? 547  LEU   A CA  1 
ATOM   1977  C  C   . LEU   A  1 246 ? -13.418 11.781  -47.999  1.00 30.48  ? 547  LEU   A C   1 
ATOM   1978  O  O   . LEU   A  1 246 ? -12.978 10.919  -47.237  1.00 34.30  ? 547  LEU   A O   1 
ATOM   1979  C  CB  . LEU   A  1 246 ? -15.353 10.727  -49.199  1.00 30.71  ? 547  LEU   A CB  1 
ATOM   1980  C  CG  . LEU   A  1 246 ? -16.457 11.505  -48.502  1.00 38.19  ? 547  LEU   A CG  1 
ATOM   1981  C  CD1 . LEU   A  1 246 ? -16.609 12.877  -49.104  1.00 39.67  ? 547  LEU   A CD1 1 
ATOM   1982  C  CD2 . LEU   A  1 246 ? -17.750 10.737  -48.639  1.00 38.01  ? 547  LEU   A CD2 1 
ATOM   1983  N  N   . GLU   A  1 247 ? -13.401 13.073  -47.712  1.00 28.28  ? 548  GLU   A N   1 
ATOM   1984  C  CA  . GLU   A  1 247 ? -12.832 13.603  -46.485  1.00 33.81  ? 548  GLU   A CA  1 
ATOM   1985  C  C   . GLU   A  1 247 ? -13.824 14.560  -45.850  1.00 34.15  ? 548  GLU   A C   1 
ATOM   1986  O  O   . GLU   A  1 247 ? -14.619 15.199  -46.543  1.00 33.84  ? 548  GLU   A O   1 
ATOM   1987  C  CB  . GLU   A  1 247 ? -11.495 14.321  -46.749  1.00 32.29  ? 548  GLU   A CB  1 
ATOM   1988  C  CG  . GLU   A  1 247 ? -10.326 13.367  -47.001  1.00 28.98  ? 548  GLU   A CG  1 
ATOM   1989  C  CD  . GLU   A  1 247 ? -9.027  14.093  -47.317  1.00 35.06  ? 548  GLU   A CD  1 
ATOM   1990  O  OE1 . GLU   A  1 247 ? -8.976  14.835  -48.318  1.00 43.01  ? 548  GLU   A OE1 1 
ATOM   1991  O  OE2 . GLU   A  1 247 ? -8.050  13.917  -46.566  1.00 37.19  ? 548  GLU   A OE2 1 
ATOM   1992  N  N   . VAL   A  1 248 ? -13.783 14.643  -44.524  1.00 34.79  ? 549  VAL   A N   1 
ATOM   1993  C  CA  . VAL   A  1 248 ? -14.718 15.483  -43.787  1.00 33.81  ? 549  VAL   A CA  1 
ATOM   1994  C  C   . VAL   A  1 248 ? -13.936 16.536  -43.010  1.00 35.06  ? 549  VAL   A C   1 
ATOM   1995  O  O   . VAL   A  1 248 ? -13.160 16.181  -42.111  1.00 41.80  ? 549  VAL   A O   1 
ATOM   1996  C  CB  . VAL   A  1 248 ? -15.590 14.652  -42.834  1.00 32.04  ? 549  VAL   A CB  1 
ATOM   1997  C  CG1 . VAL   A  1 248 ? -16.622 15.556  -42.140  1.00 31.22  ? 549  VAL   A CG1 1 
ATOM   1998  C  CG2 . VAL   A  1 248 ? -16.257 13.489  -43.581  1.00 31.03  ? 549  VAL   A CG2 1 
ATOM   1999  N  N   . PRO   A  1 249 ? -14.104 17.825  -43.308  1.00 33.37  ? 550  PRO   A N   1 
ATOM   2000  C  CA  . PRO   A  1 249 ? -13.524 18.855  -42.440  1.00 35.54  ? 550  PRO   A CA  1 
ATOM   2001  C  C   . PRO   A  1 249 ? -14.224 18.806  -41.092  1.00 35.27  ? 550  PRO   A C   1 
ATOM   2002  O  O   . PRO   A  1 249 ? -15.450 18.694  -41.032  1.00 35.37  ? 550  PRO   A O   1 
ATOM   2003  C  CB  . PRO   A  1 249 ? -13.823 20.172  -43.176  1.00 33.57  ? 550  PRO   A CB  1 
ATOM   2004  C  CG  . PRO   A  1 249 ? -14.429 19.779  -44.507  1.00 36.54  ? 550  PRO   A CG  1 
ATOM   2005  C  CD  . PRO   A  1 249 ? -15.000 18.403  -44.326  1.00 32.26  ? 550  PRO   A CD  1 
ATOM   2006  N  N   . ILE   A  1 250 ? -13.452 18.867  -40.009  1.00 33.71  ? 551  ILE   A N   1 
ATOM   2007  C  CA  . ILE   A  1 250 ? -14.029 18.716  -38.676  1.00 31.41  ? 551  ILE   A CA  1 
ATOM   2008  C  C   . ILE   A  1 250 ? -14.347 20.098  -38.121  1.00 34.95  ? 551  ILE   A C   1 
ATOM   2009  O  O   . ILE   A  1 250 ? -13.469 20.961  -38.009  1.00 35.23  ? 551  ILE   A O   1 
ATOM   2010  C  CB  . ILE   A  1 250 ? -13.100 17.936  -37.732  1.00 35.87  ? 551  ILE   A CB  1 
ATOM   2011  C  CG1 . ILE   A  1 250 ? -12.665 16.606  -38.368  1.00 34.57  ? 551  ILE   A CG1 1 
ATOM   2012  C  CG2 . ILE   A  1 250 ? -13.804 17.682  -36.395  1.00 31.44  ? 551  ILE   A CG2 1 
ATOM   2013  C  CD1 . ILE   A  1 250 ? -13.780 15.599  -38.566  1.00 24.07  ? 551  ILE   A CD1 1 
ATOM   2014  N  N   . ARG   A  1 251 ? -15.610 20.321  -37.793  1.00 36.11  ? 552  ARG   A N   1 
ATOM   2015  C  CA  . ARG   A  1 251 ? -16.018 21.543  -37.123  1.00 38.07  ? 552  ARG   A CA  1 
ATOM   2016  C  C   . ARG   A  1 251 ? -16.961 21.179  -35.983  1.00 34.14  ? 552  ARG   A C   1 
ATOM   2017  O  O   . ARG   A  1 251 ? -17.439 20.045  -35.883  1.00 31.13  ? 552  ARG   A O   1 
ATOM   2018  C  CB  . ARG   A  1 251 ? -16.661 22.540  -38.098  1.00 43.46  ? 552  ARG   A CB  1 
ATOM   2019  C  CG  . ARG   A  1 251 ? -17.887 22.047  -38.828  1.00 44.06  ? 552  ARG   A CG  1 
ATOM   2020  C  CD  . ARG   A  1 251 ? -17.511 21.194  -40.022  1.00 42.76  ? 552  ARG   A CD  1 
ATOM   2021  N  NE  . ARG   A  1 251 ? -18.657 21.052  -40.902  1.00 45.60  ? 552  ARG   A NE  1 
ATOM   2022  C  CZ  . ARG   A  1 251 ? -18.757 20.171  -41.890  1.00 39.78  ? 552  ARG   A CZ  1 
ATOM   2023  N  NH1 . ARG   A  1 251 ? -19.864 20.154  -42.613  1.00 35.57  ? 552  ARG   A NH1 1 
ATOM   2024  N  NH2 . ARG   A  1 251 ? -17.778 19.300  -42.149  1.00 29.53  ? 552  ARG   A NH2 1 
ATOM   2025  N  N   . HIS   A  1 252 ? -17.206 22.149  -35.100  1.00 35.62  ? 553  HIS   A N   1 
ATOM   2026  C  CA  . HIS   A  1 252 ? -17.988 21.938  -33.891  1.00 34.30  ? 553  HIS   A CA  1 
ATOM   2027  C  C   . HIS   A  1 252 ? -19.294 22.718  -33.963  1.00 37.03  ? 553  HIS   A C   1 
ATOM   2028  O  O   . HIS   A  1 252 ? -19.303 23.858  -34.431  1.00 37.78  ? 553  HIS   A O   1 
ATOM   2029  C  CB  . HIS   A  1 252 ? -17.197 22.383  -32.655  1.00 35.09  ? 553  HIS   A CB  1 
ATOM   2030  C  CG  . HIS   A  1 252 ? -17.757 21.890  -31.359  1.00 37.72  ? 553  HIS   A CG  1 
ATOM   2031  N  ND1 . HIS   A  1 252 ? -18.823 22.495  -30.732  1.00 43.31  ? 553  HIS   A ND1 1 
ATOM   2032  C  CD2 . HIS   A  1 252 ? -17.384 20.860  -30.559  1.00 40.43  ? 553  HIS   A CD2 1 
ATOM   2033  C  CE1 . HIS   A  1 252 ? -19.089 21.857  -29.603  1.00 41.41  ? 553  HIS   A CE1 1 
ATOM   2034  N  NE2 . HIS   A  1 252 ? -18.227 20.863  -29.473  1.00 41.95  ? 553  HIS   A NE2 1 
ATOM   2035  N  N   . PRO   A  1 253 ? -20.413 22.137  -33.525  1.00 33.36  ? 554  PRO   A N   1 
ATOM   2036  C  CA  . PRO   A  1 253 ? -21.696 22.844  -33.640  1.00 39.74  ? 554  PRO   A CA  1 
ATOM   2037  C  C   . PRO   A  1 253 ? -21.792 24.088  -32.777  1.00 47.67  ? 554  PRO   A C   1 
ATOM   2038  O  O   . PRO   A  1 253 ? -22.729 24.873  -32.966  1.00 51.82  ? 554  PRO   A O   1 
ATOM   2039  C  CB  . PRO   A  1 253 ? -22.719 21.784  -33.209  1.00 38.13  ? 554  PRO   A CB  1 
ATOM   2040  C  CG  . PRO   A  1 253 ? -21.947 20.798  -32.431  1.00 39.11  ? 554  PRO   A CG  1 
ATOM   2041  C  CD  . PRO   A  1 253 ? -20.588 20.757  -33.050  1.00 32.21  ? 554  PRO   A CD  1 
ATOM   2042  N  N   . LYS   A  1 254 ? -20.854 24.307  -31.871  1.00 45.60  ? 555  LYS   A N   1 
ATOM   2043  C  CA  . LYS   A  1 254 ? -20.891 25.416  -30.930  1.00 46.58  ? 555  LYS   A CA  1 
ATOM   2044  C  C   . LYS   A  1 254 ? -19.608 26.235  -30.926  1.00 47.26  ? 555  LYS   A C   1 
ATOM   2045  O  O   . LYS   A  1 254 ? -19.664 27.459  -30.798  1.00 57.15  ? 555  LYS   A O   1 
ATOM   2046  C  CB  . LYS   A  1 254 ? -21.157 24.854  -29.532  1.00 53.88  ? 555  LYS   A CB  1 
ATOM   2047  C  CG  . LYS   A  1 254 ? -21.940 25.764  -28.617  1.00 65.21  ? 555  LYS   A CG  1 
ATOM   2048  C  CD  . LYS   A  1 254 ? -21.578 25.486  -27.165  1.00 71.10  ? 555  LYS   A CD  1 
ATOM   2049  C  CE  . LYS   A  1 254 ? -21.535 23.992  -26.874  1.00 74.76  ? 555  LYS   A CE  1 
ATOM   2050  N  NZ  . LYS   A  1 254 ? -20.642 23.649  -25.726  1.00 75.87  ? 555  LYS   A NZ  1 
ATOM   2051  N  N   . PHE   A  1 255 ? -18.453 25.590  -31.056  1.00 44.73  ? 556  PHE   A N   1 
ATOM   2052  C  CA  . PHE   A  1 255 ? -17.163 26.269  -30.969  1.00 44.28  ? 556  PHE   A CA  1 
ATOM   2053  C  C   . PHE   A  1 255 ? -16.737 26.640  -32.383  1.00 43.49  ? 556  PHE   A C   1 
ATOM   2054  O  O   . PHE   A  1 255 ? -16.225 25.802  -33.133  1.00 43.16  ? 556  PHE   A O   1 
ATOM   2055  C  CB  . PHE   A  1 255 ? -16.128 25.377  -30.288  1.00 44.81  ? 556  PHE   A CB  1 
ATOM   2056  C  CG  . PHE   A  1 255 ? -16.489 24.985  -28.867  1.00 45.55  ? 556  PHE   A CG  1 
ATOM   2057  C  CD1 . PHE   A  1 255 ? -16.053 23.778  -28.334  1.00 43.50  ? 556  PHE   A CD1 1 
ATOM   2058  C  CD2 . PHE   A  1 255 ? -17.259 25.820  -28.075  1.00 46.67  ? 556  PHE   A CD2 1 
ATOM   2059  C  CE1 . PHE   A  1 255 ? -16.380 23.409  -27.022  1.00 41.75  ? 556  PHE   A CE1 1 
ATOM   2060  C  CE2 . PHE   A  1 255 ? -17.595 25.458  -26.767  1.00 49.16  ? 556  PHE   A CE2 1 
ATOM   2061  C  CZ  . PHE   A  1 255 ? -17.155 24.250  -26.245  1.00 41.02  ? 556  PHE   A CZ  1 
ATOM   2062  N  N   . GLU   A  1 256 ? -16.956 27.901  -32.756  1.00 45.42  ? 557  GLU   A N   1 
ATOM   2063  C  CA  . GLU   A  1 256 ? -16.612 28.331  -34.105  1.00 53.89  ? 557  GLU   A CA  1 
ATOM   2064  C  C   . GLU   A  1 256 ? -15.111 28.284  -34.346  1.00 49.72  ? 557  GLU   A C   1 
ATOM   2065  O  O   . GLU   A  1 256 ? -14.678 28.195  -35.500  1.00 46.69  ? 557  GLU   A O   1 
ATOM   2066  C  CB  . GLU   A  1 256 ? -17.171 29.731  -34.361  1.00 62.99  ? 557  GLU   A CB  1 
ATOM   2067  C  CG  . GLU   A  1 256 ? -18.688 29.785  -34.248  1.00 74.78  ? 557  GLU   A CG  1 
ATOM   2068  C  CD  . GLU   A  1 256 ? -19.266 31.115  -34.676  1.00 91.36  ? 557  GLU   A CD  1 
ATOM   2069  O  OE1 . GLU   A  1 256 ? -20.504 31.271  -34.615  1.00 97.62  ? 557  GLU   A OE1 1 
ATOM   2070  O  OE2 . GLU   A  1 256 ? -18.486 32.003  -35.076  1.00 98.88  ? 557  GLU   A OE2 1 
ATOM   2071  N  N   . TRP   A  1 257 ? -14.312 28.297  -33.281  1.00 48.82  ? 558  TRP   A N   1 
ATOM   2072  C  CA  . TRP   A  1 257 ? -12.870 28.204  -33.435  1.00 47.06  ? 558  TRP   A CA  1 
ATOM   2073  C  C   . TRP   A  1 257 ? -12.415 26.797  -33.796  1.00 45.18  ? 558  TRP   A C   1 
ATOM   2074  O  O   . TRP   A  1 257 ? -11.271 26.627  -34.226  1.00 44.98  ? 558  TRP   A O   1 
ATOM   2075  C  CB  . TRP   A  1 257 ? -12.176 28.650  -32.148  1.00 45.17  ? 558  TRP   A CB  1 
ATOM   2076  C  CG  . TRP   A  1 257 ? -12.659 27.936  -30.917  1.00 48.62  ? 558  TRP   A CG  1 
ATOM   2077  C  CD1 . TRP   A  1 257 ? -13.534 28.415  -29.983  1.00 51.84  ? 558  TRP   A CD1 1 
ATOM   2078  C  CD2 . TRP   A  1 257 ? -12.291 26.619  -30.481  1.00 44.37  ? 558  TRP   A CD2 1 
ATOM   2079  N  NE1 . TRP   A  1 257 ? -13.733 27.478  -28.991  1.00 48.55  ? 558  TRP   A NE1 1 
ATOM   2080  C  CE2 . TRP   A  1 257 ? -12.979 26.371  -29.271  1.00 42.05  ? 558  TRP   A CE2 1 
ATOM   2081  C  CE3 . TRP   A  1 257 ? -11.435 25.636  -30.984  1.00 36.37  ? 558  TRP   A CE3 1 
ATOM   2082  C  CZ2 . TRP   A  1 257 ? -12.855 25.173  -28.574  1.00 41.10  ? 558  TRP   A CZ2 1 
ATOM   2083  C  CZ3 . TRP   A  1 257 ? -11.317 24.438  -30.288  1.00 43.02  ? 558  TRP   A CZ3 1 
ATOM   2084  C  CH2 . TRP   A  1 257 ? -12.022 24.221  -29.097  1.00 42.62  ? 558  TRP   A CH2 1 
ATOM   2085  N  N   . PHE   A  1 258 ? -13.265 25.786  -33.605  1.00 36.71  ? 559  PHE   A N   1 
ATOM   2086  C  CA  . PHE   A  1 258 ? -12.816 24.412  -33.798  1.00 37.86  ? 559  PHE   A CA  1 
ATOM   2087  C  C   . PHE   A  1 258 ? -12.322 24.183  -35.221  1.00 40.30  ? 559  PHE   A C   1 
ATOM   2088  O  O   . PHE   A  1 258 ? -11.340 23.463  -35.438  1.00 35.57  ? 559  PHE   A O   1 
ATOM   2089  C  CB  . PHE   A  1 258 ? -13.941 23.438  -33.462  1.00 39.29  ? 559  PHE   A CB  1 
ATOM   2090  C  CG  . PHE   A  1 258 ? -13.455 22.049  -33.158  1.00 41.87  ? 559  PHE   A CG  1 
ATOM   2091  C  CD1 . PHE   A  1 258 ? -13.253 21.646  -31.843  1.00 37.12  ? 559  PHE   A CD1 1 
ATOM   2092  C  CD2 . PHE   A  1 258 ? -13.171 21.162  -34.179  1.00 35.21  ? 559  PHE   A CD2 1 
ATOM   2093  C  CE1 . PHE   A  1 258 ? -12.798 20.383  -31.555  1.00 36.59  ? 559  PHE   A CE1 1 
ATOM   2094  C  CE2 . PHE   A  1 258 ? -12.709 19.889  -33.903  1.00 39.21  ? 559  PHE   A CE2 1 
ATOM   2095  C  CZ  . PHE   A  1 258 ? -12.524 19.492  -32.584  1.00 34.12  ? 559  PHE   A CZ  1 
ATOM   2096  N  N   . LYS   A  1 259 ? -12.986 24.794  -36.205  1.00 39.89  ? 560  LYS   A N   1 
ATOM   2097  C  CA  . LYS   A  1 259 ? -12.585 24.589  -37.589  1.00 45.90  ? 560  LYS   A CA  1 
ATOM   2098  C  C   . LYS   A  1 259 ? -11.181 25.112  -37.837  1.00 52.10  ? 560  LYS   A C   1 
ATOM   2099  O  O   . LYS   A  1 259 ? -10.458 24.574  -38.685  1.00 49.28  ? 560  LYS   A O   1 
ATOM   2100  C  CB  . LYS   A  1 259 ? -13.579 25.260  -38.537  1.00 47.94  ? 560  LYS   A CB  1 
ATOM   2101  C  CG  . LYS   A  1 259 ? -13.681 26.774  -38.366  1.00 54.20  ? 560  LYS   A CG  1 
ATOM   2102  C  CD  . LYS   A  1 259 ? -14.582 27.399  -39.435  1.00 47.98  ? 560  LYS   A CD  1 
ATOM   2103  C  CE  . LYS   A  1 259 ? -14.797 28.883  -39.182  1.00 52.87  ? 560  LYS   A CE  1 
ATOM   2104  N  NZ  . LYS   A  1 259 ? -15.360 29.120  -37.810  1.00 55.29  ? 560  LYS   A NZ  1 
ATOM   2105  N  N   . ASP   A  1 260 ? -10.772 26.143  -37.095  1.00 43.65  ? 561  ASP   A N   1 
ATOM   2106  C  CA  . ASP   A  1 260 ? -9.434  26.693  -37.250  1.00 52.52  ? 561  ASP   A CA  1 
ATOM   2107  C  C   . ASP   A  1 260 ? -8.345  25.711  -36.837  1.00 51.49  ? 561  ASP   A C   1 
ATOM   2108  O  O   . ASP   A  1 260 ? -7.175  25.939  -37.166  1.00 53.56  ? 561  ASP   A O   1 
ATOM   2109  C  CB  . ASP   A  1 260 ? -9.300  27.984  -36.443  1.00 65.28  ? 561  ASP   A CB  1 
ATOM   2110  C  CG  . ASP   A  1 260 ? -10.306 29.034  -36.861  1.00 75.76  ? 561  ASP   A CG  1 
ATOM   2111  O  OD1 . ASP   A  1 260 ? -10.676 29.053  -38.056  1.00 79.18  ? 561  ASP   A OD1 1 
ATOM   2112  O  OD2 . ASP   A  1 260 ? -10.726 29.833  -35.994  1.00 79.55  ? 561  ASP   A OD2 1 
ATOM   2113  N  N   . LEU   A  1 261 ? -8.692  24.636  -36.117  1.00 45.21  ? 562  LEU   A N   1 
ATOM   2114  C  CA  . LEU   A  1 261 ? -7.713  23.588  -35.835  1.00 46.22  ? 562  LEU   A CA  1 
ATOM   2115  C  C   . LEU   A  1 261 ? -7.254  22.882  -37.102  1.00 45.82  ? 562  LEU   A C   1 
ATOM   2116  O  O   . LEU   A  1 261 ? -6.260  22.148  -37.059  1.00 42.20  ? 562  LEU   A O   1 
ATOM   2117  C  CB  . LEU   A  1 261 ? -8.289  22.557  -34.856  1.00 46.50  ? 562  LEU   A CB  1 
ATOM   2118  C  CG  . LEU   A  1 261 ? -8.684  23.040  -33.461  1.00 48.28  ? 562  LEU   A CG  1 
ATOM   2119  C  CD1 . LEU   A  1 261 ? -9.663  22.077  -32.810  1.00 42.67  ? 562  LEU   A CD1 1 
ATOM   2120  C  CD2 . LEU   A  1 261 ? -7.448  23.202  -32.595  1.00 53.25  ? 562  LEU   A CD2 1 
ATOM   2121  N  N   . GLY   A  1 262 ? -7.961  23.076  -38.216  1.00 43.05  ? 563  GLY   A N   1 
ATOM   2122  C  CA  . GLY   A  1 262 ? -7.589  22.479  -39.483  1.00 40.28  ? 563  GLY   A CA  1 
ATOM   2123  C  C   . GLY   A  1 262 ? -7.659  20.977  -39.505  1.00 40.26  ? 563  GLY   A C   1 
ATOM   2124  O  O   . GLY   A  1 262 ? -6.926  20.344  -40.265  1.00 42.67  ? 563  GLY   A O   1 
ATOM   2125  N  N   . LEU   A  1 263 ? -8.520  20.384  -38.687  1.00 37.96  ? 564  LEU   A N   1 
ATOM   2126  C  CA  . LEU   A  1 263 ? -8.634  18.939  -38.662  1.00 37.13  ? 564  LEU   A CA  1 
ATOM   2127  C  C   . LEU   A  1 263 ? -9.567  18.449  -39.760  1.00 36.71  ? 564  LEU   A C   1 
ATOM   2128  O  O   . LEU   A  1 263 ? -10.532 19.121  -40.147  1.00 34.49  ? 564  LEU   A O   1 
ATOM   2129  C  CB  . LEU   A  1 263 ? -9.141  18.459  -37.303  1.00 31.79  ? 564  LEU   A CB  1 
ATOM   2130  C  CG  . LEU   A  1 263 ? -8.287  18.913  -36.121  1.00 38.26  ? 564  LEU   A CG  1 
ATOM   2131  C  CD1 . LEU   A  1 263 ? -9.071  18.698  -34.847  1.00 37.84  ? 564  LEU   A CD1 1 
ATOM   2132  C  CD2 . LEU   A  1 263 ? -6.947  18.176  -36.079  1.00 38.31  ? 564  LEU   A CD2 1 
ATOM   2133  N  N   . LYS   A  1 264 ? -9.259  17.262  -40.267  1.00 33.01  ? 565  LYS   A N   1 
ATOM   2134  C  CA  . LYS   A  1 264 ? -10.172 16.543  -41.135  1.00 38.76  ? 565  LYS   A CA  1 
ATOM   2135  C  C   . LYS   A  1 264 ? -9.925  15.065  -40.926  1.00 34.89  ? 565  LYS   A C   1 
ATOM   2136  O  O   . LYS   A  1 264 ? -8.941  14.663  -40.305  1.00 32.55  ? 565  LYS   A O   1 
ATOM   2137  C  CB  . LYS   A  1 264 ? -10.000 16.924  -42.616  1.00 40.04  ? 565  LYS   A CB  1 
ATOM   2138  C  CG  . LYS   A  1 264 ? -8.592  16.770  -43.157  1.00 45.89  ? 565  LYS   A CG  1 
ATOM   2139  C  CD  . LYS   A  1 264 ? -8.543  17.093  -44.666  1.00 47.30  ? 565  LYS   A CD  1 
ATOM   2140  C  CE  . LYS   A  1 264 ? -7.158  17.531  -45.111  1.00 54.29  ? 565  LYS   A CE  1 
ATOM   2141  N  NZ  . LYS   A  1 264 ? -7.096  17.835  -46.579  1.00 57.20  ? 565  LYS   A NZ  1 
ATOM   2142  N  N   . TRP   A  1 265 ? -10.835 14.254  -41.443  1.00 29.28  ? 566  TRP   A N   1 
ATOM   2143  C  CA  . TRP   A  1 265 ? -10.587 12.828  -41.508  1.00 31.77  ? 566  TRP   A CA  1 
ATOM   2144  C  C   . TRP   A  1 265 ? -11.243 12.306  -42.767  1.00 31.80  ? 566  TRP   A C   1 
ATOM   2145  O  O   . TRP   A  1 265 ? -12.050 12.990  -43.399  1.00 33.48  ? 566  TRP   A O   1 
ATOM   2146  C  CB  . TRP   A  1 265 ? -11.113 12.092  -40.271  1.00 21.44  ? 566  TRP   A CB  1 
ATOM   2147  C  CG  . TRP   A  1 265 ? -10.391 10.821  -40.027  1.00 21.61  ? 566  TRP   A CG  1 
ATOM   2148  C  CD1 . TRP   A  1 265 ? -10.878 9.553   -40.175  1.00 20.36  ? 566  TRP   A CD1 1 
ATOM   2149  C  CD2 . TRP   A  1 265 ? -9.036  10.685  -39.587  1.00 23.49  ? 566  TRP   A CD2 1 
ATOM   2150  N  NE1 . TRP   A  1 265 ? -9.904  8.630   -39.844  1.00 21.76  ? 566  TRP   A NE1 1 
ATOM   2151  C  CE2 . TRP   A  1 265 ? -8.766  9.303   -39.479  1.00 24.78  ? 566  TRP   A CE2 1 
ATOM   2152  C  CE3 . TRP   A  1 265 ? -8.026  11.597  -39.262  1.00 25.65  ? 566  TRP   A CE3 1 
ATOM   2153  C  CZ2 . TRP   A  1 265 ? -7.529  8.813   -39.065  1.00 25.73  ? 566  TRP   A CZ2 1 
ATOM   2154  C  CZ3 . TRP   A  1 265 ? -6.801  11.110  -38.864  1.00 21.87  ? 566  TRP   A CZ3 1 
ATOM   2155  C  CH2 . TRP   A  1 265 ? -6.562  9.731   -38.763  1.00 20.96  ? 566  TRP   A CH2 1 
ATOM   2156  N  N   . TYR   A  1 266 ? -10.880 11.087  -43.127  1.00 25.44  ? 567  TYR   A N   1 
ATOM   2157  C  CA  . TYR   A  1 266 ? -11.456 10.446  -44.294  1.00 32.28  ? 567  TYR   A CA  1 
ATOM   2158  C  C   . TYR   A  1 266 ? -12.681 9.649   -43.886  1.00 30.93  ? 567  TYR   A C   1 
ATOM   2159  O  O   . TYR   A  1 266 ? -12.811 9.209   -42.742  1.00 29.52  ? 567  TYR   A O   1 
ATOM   2160  C  CB  . TYR   A  1 266 ? -10.435 9.534   -44.969  1.00 24.30  ? 567  TYR   A CB  1 
ATOM   2161  C  CG  . TYR   A  1 266 ? -9.704  8.630   -44.013  1.00 27.13  ? 567  TYR   A CG  1 
ATOM   2162  C  CD1 . TYR   A  1 266 ? -10.181 7.353   -43.735  1.00 25.85  ? 567  TYR   A CD1 1 
ATOM   2163  C  CD2 . TYR   A  1 266 ? -8.541  9.050   -43.382  1.00 28.20  ? 567  TYR   A CD2 1 
ATOM   2164  C  CE1 . TYR   A  1 266 ? -9.522  6.517   -42.855  1.00 29.20  ? 567  TYR   A CE1 1 
ATOM   2165  C  CE2 . TYR   A  1 266 ? -7.873  8.216   -42.488  1.00 30.21  ? 567  TYR   A CE2 1 
ATOM   2166  C  CZ  . TYR   A  1 266 ? -8.371  6.951   -42.230  1.00 30.17  ? 567  TYR   A CZ  1 
ATOM   2167  O  OH  . TYR   A  1 266 ? -7.719  6.103   -41.357  1.00 33.94  ? 567  TYR   A OH  1 
ATOM   2168  N  N   . GLY   A  1 267 ? -13.586 9.460   -44.848  1.00 28.22  ? 568  GLY   A N   1 
ATOM   2169  C  CA  . GLY   A  1 267 ? -14.849 8.813   -44.549  1.00 23.66  ? 568  GLY   A CA  1 
ATOM   2170  C  C   . GLY   A  1 267 ? -14.788 7.303   -44.487  1.00 23.26  ? 568  GLY   A C   1 
ATOM   2171  O  O   . GLY   A  1 267 ? -15.599 6.687   -43.793  1.00 26.83  ? 568  GLY   A O   1 
ATOM   2172  N  N   . LEU   A  1 268 ? -13.827 6.688   -45.177  1.00 21.89  ? 569  LEU   A N   1 
ATOM   2173  C  CA  . LEU   A  1 268 ? -13.855 5.253   -45.448  1.00 17.77  ? 569  LEU   A CA  1 
ATOM   2174  C  C   . LEU   A  1 268 ? -12.828 4.505   -44.602  1.00 24.82  ? 569  LEU   A C   1 
ATOM   2175  O  O   . LEU   A  1 268 ? -11.622 4.543   -44.910  1.00 22.86  ? 569  LEU   A O   1 
ATOM   2176  C  CB  . LEU   A  1 268 ? -13.600 4.993   -46.941  1.00 17.84  ? 569  LEU   A CB  1 
ATOM   2177  C  CG  . LEU   A  1 268 ? -13.835 3.526   -47.342  1.00 26.48  ? 569  LEU   A CG  1 
ATOM   2178  C  CD1 . LEU   A  1 268 ? -15.316 3.197   -47.237  1.00 26.59  ? 569  LEU   A CD1 1 
ATOM   2179  C  CD2 . LEU   A  1 268 ? -13.305 3.188   -48.736  1.00 24.00  ? 569  LEU   A CD2 1 
ATOM   2180  N  N   . PRO   A  1 269 ? -13.241 3.811   -43.537  1.00 22.99  ? 570  PRO   A N   1 
ATOM   2181  C  CA  . PRO   A  1 269 ? -12.317 2.924   -42.814  1.00 20.06  ? 570  PRO   A CA  1 
ATOM   2182  C  C   . PRO   A  1 269 ? -12.183 1.608   -43.565  1.00 23.87  ? 570  PRO   A C   1 
ATOM   2183  O  O   . PRO   A  1 269 ? -13.147 0.856   -43.704  1.00 23.13  ? 570  PRO   A O   1 
ATOM   2184  C  CB  . PRO   A  1 269 ? -13.005 2.728   -41.457  1.00 15.87  ? 570  PRO   A CB  1 
ATOM   2185  C  CG  . PRO   A  1 269 ? -14.479 2.803   -41.784  1.00 17.91  ? 570  PRO   A CG  1 
ATOM   2186  C  CD  . PRO   A  1 269 ? -14.603 3.780   -42.967  1.00 18.86  ? 570  PRO   A CD  1 
ATOM   2187  N  N   . ALA   A  1 270 ? -10.985 1.311   -44.031  1.00 22.66  ? 571  ALA   A N   1 
ATOM   2188  C  CA  . ALA   A  1 270 ? -10.824 0.207   -44.977  1.00 17.47  ? 571  ALA   A CA  1 
ATOM   2189  C  C   . ALA   A  1 270 ? -9.572  -0.575  -44.597  1.00 23.68  ? 571  ALA   A C   1 
ATOM   2190  O  O   . ALA   A  1 270 ? -8.471  -0.206  -45.002  1.00 26.82  ? 571  ALA   A O   1 
ATOM   2191  C  CB  . ALA   A  1 270 ? -10.756 0.748   -46.401  1.00 19.12  ? 571  ALA   A CB  1 
ATOM   2192  N  N   . VAL   A  1 271 ? -9.741  -1.632  -43.801  1.00 23.42  ? 572  VAL   A N   1 
ATOM   2193  C  CA  . VAL   A  1 271 ? -8.597  -2.381  -43.282  1.00 19.19  ? 572  VAL   A CA  1 
ATOM   2194  C  C   . VAL   A  1 271 ? -8.045  -3.264  -44.386  1.00 19.87  ? 572  VAL   A C   1 
ATOM   2195  O  O   . VAL   A  1 271 ? -8.791  -4.029  -45.010  1.00 22.28  ? 572  VAL   A O   1 
ATOM   2196  C  CB  . VAL   A  1 271 ? -8.998  -3.234  -42.070  1.00 21.34  ? 572  VAL   A CB  1 
ATOM   2197  C  CG1 . VAL   A  1 271 ? -7.890  -4.276  -41.780  1.00 21.52  ? 572  VAL   A CG1 1 
ATOM   2198  C  CG2 . VAL   A  1 271 ? -9.246  -2.371  -40.847  1.00 19.93  ? 572  VAL   A CG2 1 
ATOM   2199  N  N   . SER   A  1 272 ? -6.724  -3.221  -44.587  1.00 20.41  ? 573  SER   A N   1 
ATOM   2200  C  CA  . SER   A  1 272 ? -6.134  -3.899  -45.734  1.00 25.90  ? 573  SER   A CA  1 
ATOM   2201  C  C   . SER   A  1 272 ? -4.907  -4.729  -45.383  1.00 27.58  ? 573  SER   A C   1 
ATOM   2202  O  O   . SER   A  1 272 ? -4.227  -5.212  -46.295  1.00 30.82  ? 573  SER   A O   1 
ATOM   2203  C  CB  . SER   A  1 272 ? -5.786  -2.886  -46.839  1.00 18.79  ? 573  SER   A CB  1 
ATOM   2204  O  OG  . SER   A  1 272 ? -5.027  -1.784  -46.339  1.00 19.98  ? 573  SER   A OG  1 
ATOM   2205  N  N   . ASN   A  1 273 ? -4.609  -4.933  -44.101  1.00 23.40  ? 574  ASN   A N   1 
ATOM   2206  C  CA  . ASN   A  1 273 ? -3.440  -5.721  -43.733  1.00 23.46  ? 574  ASN   A CA  1 
ATOM   2207  C  C   . ASN   A  1 273 ? -3.797  -7.039  -43.075  1.00 23.83  ? 574  ASN   A C   1 
ATOM   2208  O  O   . ASN   A  1 273 ? -2.908  -7.725  -42.572  1.00 28.09  ? 574  ASN   A O   1 
ATOM   2209  C  CB  . ASN   A  1 273 ? -2.508  -4.925  -42.826  1.00 28.07  ? 574  ASN   A CB  1 
ATOM   2210  C  CG  . ASN   A  1 273 ? -3.173  -4.472  -41.536  1.00 25.07  ? 574  ASN   A CG  1 
ATOM   2211  O  OD1 . ASN   A  1 273 ? -4.373  -4.666  -41.313  1.00 26.69  ? 574  ASN   A OD1 1 
ATOM   2212  N  ND2 . ASN   A  1 273 ? -2.387  -3.850  -40.688  1.00 30.56  ? 574  ASN   A ND2 1 
ATOM   2213  N  N   . MET   A  1 274 ? -5.060  -7.429  -43.094  1.00 23.43  ? 575  MET   A N   1 
ATOM   2214  C  CA  . MET   A  1 274 ? -5.465  -8.659  -42.439  1.00 21.91  ? 575  MET   A CA  1 
ATOM   2215  C  C   . MET   A  1 274 ? -5.543  -9.788  -43.442  1.00 26.08  ? 575  MET   A C   1 
ATOM   2216  O  O   . MET   A  1 274 ? -5.506  -9.586  -44.659  1.00 23.29  ? 575  MET   A O   1 
ATOM   2217  C  CB  . MET   A  1 274 ? -6.797  -8.474  -41.721  1.00 21.90  ? 575  MET   A CB  1 
ATOM   2218  C  CG  . MET   A  1 274 ? -6.616  -7.656  -40.441  1.00 22.41  ? 575  MET   A CG  1 
ATOM   2219  S  SD  . MET   A  1 274 ? -8.138  -7.577  -39.509  1.00 27.10  ? 575  MET   A SD  1 
ATOM   2220  C  CE  . MET   A  1 274 ? -7.940  -9.014  -38.426  1.00 21.99  ? 575  MET   A CE  1 
ATOM   2221  N  N   . LEU   A  1 275 ? -5.614  -10.995 -42.905  1.00 21.07  ? 576  LEU   A N   1 
ATOM   2222  C  CA  . LEU   A  1 275 ? -5.642  -12.206 -43.704  1.00 27.71  ? 576  LEU   A CA  1 
ATOM   2223  C  C   . LEU   A  1 275 ? -7.012  -12.834 -43.536  1.00 27.79  ? 576  LEU   A C   1 
ATOM   2224  O  O   . LEU   A  1 275 ? -7.500  -12.974 -42.411  1.00 28.42  ? 576  LEU   A O   1 
ATOM   2225  C  CB  . LEU   A  1 275 ? -4.532  -13.159 -43.257  1.00 33.59  ? 576  LEU   A CB  1 
ATOM   2226  C  CG  . LEU   A  1 275 ? -4.319  -14.474 -44.009  1.00 46.68  ? 576  LEU   A CG  1 
ATOM   2227  C  CD1 . LEU   A  1 275 ? -2.846  -14.849 -43.991  1.00 48.67  ? 576  LEU   A CD1 1 
ATOM   2228  C  CD2 . LEU   A  1 275 ? -5.135  -15.574 -43.354  1.00 44.80  ? 576  LEU   A CD2 1 
ATOM   2229  N  N   . LEU   A  1 276 ? -7.645  -13.176 -44.642  1.00 22.67  ? 577  LEU   A N   1 
ATOM   2230  C  CA  . LEU   A  1 276 ? -8.936  -13.847 -44.617  1.00 26.77  ? 577  LEU   A CA  1 
ATOM   2231  C  C   . LEU   A  1 276 ? -8.690  -15.335 -44.806  1.00 25.03  ? 577  LEU   A C   1 
ATOM   2232  O  O   . LEU   A  1 276 ? -8.088  -15.751 -45.802  1.00 26.18  ? 577  LEU   A O   1 
ATOM   2233  C  CB  . LEU   A  1 276 ? -9.856  -13.295 -45.701  1.00 21.80  ? 577  LEU   A CB  1 
ATOM   2234  C  CG  . LEU   A  1 276 ? -11.087 -14.116 -46.071  1.00 22.12  ? 577  LEU   A CG  1 
ATOM   2235  C  CD1 . LEU   A  1 276 ? -12.011 -14.292 -44.891  1.00 20.16  ? 577  LEU   A CD1 1 
ATOM   2236  C  CD2 . LEU   A  1 276 ? -11.820 -13.440 -47.229  1.00 25.04  ? 577  LEU   A CD2 1 
ATOM   2237  N  N   . GLU   A  1 277 ? -9.143  -16.129 -43.849  1.00 21.60  ? 578  GLU   A N   1 
ATOM   2238  C  CA  . GLU   A  1 277 ? -8.897  -17.562 -43.840  1.00 22.41  ? 578  GLU   A CA  1 
ATOM   2239  C  C   . GLU   A  1 277 ? -10.226 -18.281 -44.045  1.00 28.95  ? 578  GLU   A C   1 
ATOM   2240  O  O   . GLU   A  1 277 ? -11.141 -18.156 -43.224  1.00 26.53  ? 578  GLU   A O   1 
ATOM   2241  C  CB  . GLU   A  1 277 ? -8.220  -17.975 -42.531  1.00 35.78  ? 578  GLU   A CB  1 
ATOM   2242  C  CG  . GLU   A  1 277 ? -7.534  -19.326 -42.582  1.00 51.20  ? 578  GLU   A CG  1 
ATOM   2243  C  CD  . GLU   A  1 277 ? -8.489  -20.471 -42.300  1.00 64.94  ? 578  GLU   A CD  1 
ATOM   2244  O  OE1 . GLU   A  1 277 ? -8.217  -21.589 -42.772  1.00 70.61  ? 578  GLU   A OE1 1 
ATOM   2245  O  OE2 . GLU   A  1 277 ? -9.507  -20.255 -41.606  1.00 66.31  ? 578  GLU   A OE2 1 
ATOM   2246  N  N   . ILE   A  1 278 ? -10.340 -19.004 -45.156  1.00 26.09  ? 579  ILE   A N   1 
ATOM   2247  C  CA  . ILE   A  1 278 ? -11.541 -19.765 -45.490  1.00 29.10  ? 579  ILE   A CA  1 
ATOM   2248  C  C   . ILE   A  1 278 ? -11.105 -21.159 -45.900  1.00 29.97  ? 579  ILE   A C   1 
ATOM   2249  O  O   . ILE   A  1 278 ? -10.364 -21.312 -46.882  1.00 27.86  ? 579  ILE   A O   1 
ATOM   2250  C  CB  . ILE   A  1 278 ? -12.348 -19.127 -46.632  1.00 31.08  ? 579  ILE   A CB  1 
ATOM   2251  C  CG1 . ILE   A  1 278 ? -12.700 -17.675 -46.329  1.00 23.15  ? 579  ILE   A CG1 1 
ATOM   2252  C  CG2 . ILE   A  1 278 ? -13.584 -19.957 -46.897  1.00 31.19  ? 579  ILE   A CG2 1 
ATOM   2253  C  CD1 . ILE   A  1 278 ? -13.292 -16.935 -47.517  1.00 22.93  ? 579  ILE   A CD1 1 
ATOM   2254  N  N   . GLY   A  1 279 ? -11.553 -22.166 -45.151  1.00 28.25  ? 580  GLY   A N   1 
ATOM   2255  C  CA  . GLY   A  1 279 ? -11.299 -23.551 -45.504  1.00 32.17  ? 580  GLY   A CA  1 
ATOM   2256  C  C   . GLY   A  1 279 ? -9.842  -23.901 -45.681  1.00 32.98  ? 580  GLY   A C   1 
ATOM   2257  O  O   . GLY   A  1 279 ? -9.508  -24.756 -46.510  1.00 31.52  ? 580  GLY   A O   1 
ATOM   2258  N  N   . GLY   A  1 280 ? -8.963  -23.277 -44.913  1.00 26.67  ? 581  GLY   A N   1 
ATOM   2259  C  CA  . GLY   A  1 280 ? -7.546  -23.512 -45.065  1.00 37.48  ? 581  GLY   A CA  1 
ATOM   2260  C  C   . GLY   A  1 280 ? -6.884  -22.653 -46.109  1.00 34.31  ? 581  GLY   A C   1 
ATOM   2261  O  O   . GLY   A  1 280 ? -5.648  -22.645 -46.191  1.00 34.78  ? 581  GLY   A O   1 
ATOM   2262  N  N   . LEU   A  1 281 ? -7.659  -21.924 -46.901  1.00 28.28  ? 582  LEU   A N   1 
ATOM   2263  C  CA  . LEU   A  1 281 ? -7.100  -20.985 -47.858  1.00 29.01  ? 582  LEU   A CA  1 
ATOM   2264  C  C   . LEU   A  1 281 ? -6.861  -19.655 -47.173  1.00 28.92  ? 582  LEU   A C   1 
ATOM   2265  O  O   . LEU   A  1 281 ? -7.641  -19.233 -46.318  1.00 31.53  ? 582  LEU   A O   1 
ATOM   2266  C  CB  . LEU   A  1 281 ? -8.039  -20.800 -49.046  1.00 30.24  ? 582  LEU   A CB  1 
ATOM   2267  C  CG  . LEU   A  1 281 ? -8.516  -22.116 -49.636  1.00 26.27  ? 582  LEU   A CG  1 
ATOM   2268  C  CD1 . LEU   A  1 281 ? -9.498  -21.845 -50.749  1.00 27.95  ? 582  LEU   A CD1 1 
ATOM   2269  C  CD2 . LEU   A  1 281 ? -7.306  -22.884 -50.132  1.00 29.91  ? 582  LEU   A CD2 1 
ATOM   2270  N  N   . GLU   A  1 282 ? -5.771  -19.003 -47.545  1.00 28.22  ? 583  GLU   A N   1 
ATOM   2271  C  CA  . GLU   A  1 282 ? -5.338  -17.770 -46.904  1.00 29.30  ? 583  GLU   A CA  1 
ATOM   2272  C  C   . GLU   A  1 282 ? -5.334  -16.667 -47.953  1.00 34.77  ? 583  GLU   A C   1 
ATOM   2273  O  O   . GLU   A  1 282 ? -4.523  -16.689 -48.886  1.00 31.44  ? 583  GLU   A O   1 
ATOM   2274  C  CB  . GLU   A  1 282 ? -3.959  -17.944 -46.280  1.00 34.45  ? 583  GLU   A CB  1 
ATOM   2275  C  CG  . GLU   A  1 282 ? -3.905  -19.040 -45.244  1.00 41.87  ? 583  GLU   A CG  1 
ATOM   2276  C  CD  . GLU   A  1 282 ? -2.581  -19.067 -44.540  1.00 52.20  ? 583  GLU   A CD  1 
ATOM   2277  O  OE1 . GLU   A  1 282 ? -1.540  -19.008 -45.236  1.00 49.70  ? 583  GLU   A OE1 1 
ATOM   2278  O  OE2 . GLU   A  1 282 ? -2.587  -19.128 -43.290  1.00 58.76  ? 583  GLU   A OE2 1 
ATOM   2279  N  N   . PHE   A  1 283 ? -6.241  -15.716 -47.799  1.00 26.85  ? 584  PHE   A N   1 
ATOM   2280  C  CA  . PHE   A  1 283 ? -6.331  -14.568 -48.687  1.00 22.22  ? 584  PHE   A CA  1 
ATOM   2281  C  C   . PHE   A  1 283 ? -5.598  -13.408 -48.017  1.00 29.39  ? 584  PHE   A C   1 
ATOM   2282  O  O   . PHE   A  1 283 ? -6.159  -12.706 -47.168  1.00 28.75  ? 584  PHE   A O   1 
ATOM   2283  C  CB  . PHE   A  1 283 ? -7.793  -14.261 -48.976  1.00 23.93  ? 584  PHE   A CB  1 
ATOM   2284  C  CG  . PHE   A  1 283 ? -8.489  -15.369 -49.720  1.00 26.26  ? 584  PHE   A CG  1 
ATOM   2285  C  CD1 . PHE   A  1 283 ? -9.213  -16.342 -49.033  1.00 22.71  ? 584  PHE   A CD1 1 
ATOM   2286  C  CD2 . PHE   A  1 283 ? -8.398  -15.451 -51.100  1.00 28.35  ? 584  PHE   A CD2 1 
ATOM   2287  C  CE1 . PHE   A  1 283 ? -9.853  -17.359 -49.717  1.00 27.86  ? 584  PHE   A CE1 1 
ATOM   2288  C  CE2 . PHE   A  1 283 ? -9.041  -16.455 -51.800  1.00 30.62  ? 584  PHE   A CE2 1 
ATOM   2289  C  CZ  . PHE   A  1 283 ? -9.764  -17.419 -51.109  1.00 30.54  ? 584  PHE   A CZ  1 
ATOM   2290  N  N   . SER   A  1 284 ? -4.322  -13.234 -48.383  1.00 27.64  ? 585  SER   A N   1 
ATOM   2291  C  CA  . SER   A  1 284 ? -3.430  -12.289 -47.724  1.00 26.18  ? 585  SER   A CA  1 
ATOM   2292  C  C   . SER   A  1 284 ? -3.702  -10.843 -48.097  1.00 30.08  ? 585  SER   A C   1 
ATOM   2293  O  O   . SER   A  1 284 ? -3.172  -9.932  -47.442  1.00 26.96  ? 585  SER   A O   1 
ATOM   2294  C  CB  . SER   A  1 284 ? -1.978  -12.628 -48.064  1.00 30.47  ? 585  SER   A CB  1 
ATOM   2295  O  OG  . SER   A  1 284 ? -1.826  -12.854 -49.457  1.00 32.16  ? 585  SER   A OG  1 
ATOM   2296  N  N   . ALA   A  1 285 ? -4.474  -10.612 -49.149  1.00 32.17  ? 586  ALA   A N   1 
ATOM   2297  C  CA  . ALA   A  1 285 ? -4.895  -9.277  -49.547  1.00 27.91  ? 586  ALA   A CA  1 
ATOM   2298  C  C   . ALA   A  1 285 ? -6.405  -9.331  -49.659  1.00 22.82  ? 586  ALA   A C   1 
ATOM   2299  O  O   . ALA   A  1 285 ? -6.942  -9.962  -50.580  1.00 25.88  ? 586  ALA   A O   1 
ATOM   2300  C  CB  . ALA   A  1 285 ? -4.260  -8.849  -50.873  1.00 30.09  ? 586  ALA   A CB  1 
ATOM   2301  N  N   . CYS   A  1 286 ? -7.077  -8.689  -48.729  1.00 22.74  ? 587  CYS   A N   1 
ATOM   2302  C  CA  . CYS   A  1 286 ? -8.523  -8.767  -48.682  1.00 19.78  ? 587  CYS   A CA  1 
ATOM   2303  C  C   . CYS   A  1 286 ? -9.072  -7.485  -48.075  1.00 23.86  ? 587  CYS   A C   1 
ATOM   2304  O  O   . CYS   A  1 286 ? -9.785  -7.534  -47.063  1.00 24.50  ? 587  CYS   A O   1 
ATOM   2305  C  CB  . CYS   A  1 286 ? -8.949  -9.980  -47.865  1.00 26.09  ? 587  CYS   A CB  1 
ATOM   2306  S  SG  . CYS   A  1 286 ? -8.310  -9.956  -46.168  1.00 25.38  ? 587  CYS   A SG  1 
ATOM   2307  N  N   . PRO   A  1 287 ? -8.768  -6.322  -48.652  1.00 25.88  ? 588  PRO   A N   1 
ATOM   2308  C  CA  . PRO   A  1 287 ? -9.191  -5.074  -48.010  1.00 23.25  ? 588  PRO   A CA  1 
ATOM   2309  C  C   . PRO   A  1 287 ? -10.699 -5.077  -47.827  1.00 21.18  ? 588  PRO   A C   1 
ATOM   2310  O  O   . PRO   A  1 287 ? -11.445 -5.503  -48.715  1.00 25.75  ? 588  PRO   A O   1 
ATOM   2311  C  CB  . PRO   A  1 287 ? -8.726  -3.992  -48.989  1.00 25.36  ? 588  PRO   A CB  1 
ATOM   2312  C  CG  . PRO   A  1 287 ? -8.608  -4.711  -50.322  1.00 28.39  ? 588  PRO   A CG  1 
ATOM   2313  C  CD  . PRO   A  1 287 ? -8.162  -6.090  -49.978  1.00 25.46  ? 588  PRO   A CD  1 
ATOM   2314  N  N   . PHE   A  1 288 ? -11.136 -4.695  -46.623  1.00 25.31  ? 589  PHE   A N   1 
ATOM   2315  C  CA  . PHE   A  1 288 ? -12.549 -4.617  -46.305  1.00 14.98  ? 589  PHE   A CA  1 
ATOM   2316  C  C   . PHE   A  1 288 ? -12.833 -3.281  -45.640  1.00 21.56  ? 589  PHE   A C   1 
ATOM   2317  O  O   . PHE   A  1 288 ? -11.960 -2.676  -45.011  1.00 25.53  ? 589  PHE   A O   1 
ATOM   2318  C  CB  . PHE   A  1 288 ? -13.002 -5.776  -45.420  1.00 19.71  ? 589  PHE   A CB  1 
ATOM   2319  C  CG  . PHE   A  1 288 ? -12.265 -5.886  -44.095  1.00 22.59  ? 589  PHE   A CG  1 
ATOM   2320  C  CD1 . PHE   A  1 288 ? -12.672 -5.152  -42.987  1.00 23.59  ? 589  PHE   A CD1 1 
ATOM   2321  C  CD2 . PHE   A  1 288 ? -11.191 -6.756  -43.954  1.00 18.98  ? 589  PHE   A CD2 1 
ATOM   2322  C  CE1 . PHE   A  1 288 ? -12.017 -5.266  -41.764  1.00 21.89  ? 589  PHE   A CE1 1 
ATOM   2323  C  CE2 . PHE   A  1 288 ? -10.518 -6.879  -42.734  1.00 21.14  ? 589  PHE   A CE2 1 
ATOM   2324  C  CZ  . PHE   A  1 288 ? -10.935 -6.136  -41.633  1.00 18.88  ? 589  PHE   A CZ  1 
ATOM   2325  N  N   . SER   A  1 289 ? -14.058 -2.807  -45.801  1.00 21.22  ? 590  SER   A N   1 
ATOM   2326  C  CA  . SER   A  1 289 ? -14.355 -1.458  -45.365  1.00 16.84  ? 590  SER   A CA  1 
ATOM   2327  C  C   . SER   A  1 289 ? -15.792 -1.425  -44.913  1.00 15.61  ? 590  SER   A C   1 
ATOM   2328  O  O   . SER   A  1 289 ? -16.610 -2.211  -45.376  1.00 19.68  ? 590  SER   A O   1 
ATOM   2329  C  CB  . SER   A  1 289 ? -14.115 -0.428  -46.479  1.00 23.41  ? 590  SER   A CB  1 
ATOM   2330  O  OG  . SER   A  1 289 ? -14.979 -0.632  -47.582  1.00 25.28  ? 590  SER   A OG  1 
ATOM   2331  N  N   . GLY   A  1 290 ? -16.083 -0.526  -43.980  1.00 20.76  ? 591  GLY   A N   1 
ATOM   2332  C  CA  . GLY   A  1 290 ? -17.462 -0.296  -43.604  1.00 22.62  ? 591  GLY   A CA  1 
ATOM   2333  C  C   . GLY   A  1 290 ? -17.689 1.184   -43.424  1.00 25.68  ? 591  GLY   A C   1 
ATOM   2334  O  O   . GLY   A  1 290 ? -17.502 1.975   -44.360  1.00 23.61  ? 591  GLY   A O   1 
ATOM   2335  N  N   . TRP   A  1 291 ? -18.058 1.582   -42.211  1.00 23.96  ? 592  TRP   A N   1 
ATOM   2336  C  CA  . TRP   A  1 291 ? -18.136 2.993   -41.897  1.00 24.89  ? 592  TRP   A CA  1 
ATOM   2337  C  C   . TRP   A  1 291 ? -17.745 3.170   -40.442  1.00 20.68  ? 592  TRP   A C   1 
ATOM   2338  O  O   . TRP   A  1 291 ? -17.781 2.233   -39.655  1.00 20.73  ? 592  TRP   A O   1 
ATOM   2339  C  CB  . TRP   A  1 291 ? -19.526 3.564   -42.163  1.00 19.49  ? 592  TRP   A CB  1 
ATOM   2340  C  CG  . TRP   A  1 291 ? -20.605 2.793   -41.506  1.00 24.48  ? 592  TRP   A CG  1 
ATOM   2341  C  CD1 . TRP   A  1 291 ? -20.967 2.848   -40.185  1.00 30.73  ? 592  TRP   A CD1 1 
ATOM   2342  C  CD2 . TRP   A  1 291 ? -21.480 1.854   -42.125  1.00 22.32  ? 592  TRP   A CD2 1 
ATOM   2343  N  NE1 . TRP   A  1 291 ? -22.021 2.001   -39.956  1.00 26.80  ? 592  TRP   A NE1 1 
ATOM   2344  C  CE2 . TRP   A  1 291 ? -22.354 1.379   -41.130  1.00 24.81  ? 592  TRP   A CE2 1 
ATOM   2345  C  CE3 . TRP   A  1 291 ? -21.619 1.373   -43.434  1.00 26.18  ? 592  TRP   A CE3 1 
ATOM   2346  C  CZ2 . TRP   A  1 291 ? -23.347 0.440   -41.395  1.00 31.14  ? 592  TRP   A CZ2 1 
ATOM   2347  C  CZ3 . TRP   A  1 291 ? -22.603 0.439   -43.699  1.00 30.15  ? 592  TRP   A CZ3 1 
ATOM   2348  C  CH2 . TRP   A  1 291 ? -23.460 -0.012  -42.687  1.00 35.43  ? 592  TRP   A CH2 1 
ATOM   2349  N  N   . TYR   A  1 292 ? -17.357 4.380   -40.110  1.00 22.38  ? 593  TYR   A N   1 
ATOM   2350  C  CA  . TYR   A  1 292 ? -16.725 4.644   -38.832  1.00 22.62  ? 593  TYR   A CA  1 
ATOM   2351  C  C   . TYR   A  1 292 ? -17.730 4.676   -37.701  1.00 26.32  ? 593  TYR   A C   1 
ATOM   2352  O  O   . TYR   A  1 292 ? -18.868 5.125   -37.863  1.00 25.95  ? 593  TYR   A O   1 
ATOM   2353  C  CB  . TYR   A  1 292 ? -16.016 5.993   -38.861  1.00 18.18  ? 593  TYR   A CB  1 
ATOM   2354  C  CG  . TYR   A  1 292 ? -14.563 5.916   -39.198  1.00 18.13  ? 593  TYR   A CG  1 
ATOM   2355  C  CD1 . TYR   A  1 292 ? -14.045 6.567   -40.330  1.00 25.99  ? 593  TYR   A CD1 1 
ATOM   2356  C  CD2 . TYR   A  1 292 ? -13.703 5.202   -38.404  1.00 17.86  ? 593  TYR   A CD2 1 
ATOM   2357  C  CE1 . TYR   A  1 292 ? -12.694 6.514   -40.624  1.00 21.35  ? 593  TYR   A CE1 1 
ATOM   2358  C  CE2 . TYR   A  1 292 ? -12.352 5.138   -38.695  1.00 23.30  ? 593  TYR   A CE2 1 
ATOM   2359  C  CZ  . TYR   A  1 292 ? -11.855 5.794   -39.791  1.00 19.87  ? 593  TYR   A CZ  1 
ATOM   2360  O  OH  . TYR   A  1 292 ? -10.503 5.701   -40.033  1.00 26.15  ? 593  TYR   A OH  1 
ATOM   2361  N  N   . MET   A  1 293 ? -17.286 4.212   -36.543  1.00 24.32  ? 594  MET   A N   1 
ATOM   2362  C  CA  . MET   A  1 293 ? -17.843 4.666   -35.280  1.00 20.04  ? 594  MET   A CA  1 
ATOM   2363  C  C   . MET   A  1 293 ? -17.048 5.897   -34.862  1.00 21.05  ? 594  MET   A C   1 
ATOM   2364  O  O   . MET   A  1 293 ? -15.815 5.913   -34.971  1.00 24.42  ? 594  MET   A O   1 
ATOM   2365  C  CB  . MET   A  1 293 ? -17.772 3.558   -34.227  1.00 20.16  ? 594  MET   A CB  1 
ATOM   2366  C  CG  . MET   A  1 293 ? -18.453 3.907   -32.917  1.00 21.60  ? 594  MET   A CG  1 
ATOM   2367  S  SD  . MET   A  1 293 ? -18.577 2.452   -31.866  1.00 25.67  ? 594  MET   A SD  1 
ATOM   2368  C  CE  . MET   A  1 293 ? -16.858 2.234   -31.396  1.00 22.50  ? 594  MET   A CE  1 
ATOM   2369  N  N   . GLY   A  1 294 ? -17.756 6.939   -34.429  1.00 25.61  ? 595  GLY   A N   1 
ATOM   2370  C  CA  . GLY   A  1 294 ? -17.112 8.232   -34.212  1.00 24.21  ? 595  GLY   A CA  1 
ATOM   2371  C  C   . GLY   A  1 294 ? -15.896 8.178   -33.305  1.00 24.60  ? 595  GLY   A C   1 
ATOM   2372  O  O   . GLY   A  1 294 ? -14.918 8.902   -33.521  1.00 25.33  ? 595  GLY   A O   1 
ATOM   2373  N  N   . THR   A  1 295 ? -15.938 7.325   -32.270  1.00 24.78  ? 596  THR   A N   1 
ATOM   2374  C  CA  . THR   A  1 295 ? -14.843 7.278   -31.304  1.00 25.64  ? 596  THR   A CA  1 
ATOM   2375  C  C   . THR   A  1 295 ? -13.545 6.817   -31.934  1.00 24.56  ? 596  THR   A C   1 
ATOM   2376  O  O   . THR   A  1 295 ? -12.467 7.157   -31.438  1.00 22.01  ? 596  THR   A O   1 
ATOM   2377  C  CB  . THR   A  1 295 ? -15.171 6.341   -30.136  1.00 24.78  ? 596  THR   A CB  1 
ATOM   2378  O  OG1 . THR   A  1 295 ? -15.503 5.039   -30.642  1.00 20.01  ? 596  THR   A OG1 1 
ATOM   2379  C  CG2 . THR   A  1 295 ? -16.317 6.914   -29.283  1.00 25.43  ? 596  THR   A CG2 1 
ATOM   2380  N  N   . GLU   A  1 296 ? -13.620 6.009   -32.995  1.00 23.18  ? 597  GLU   A N   1 
ATOM   2381  C  CA  . GLU   A  1 296 ? -12.400 5.582   -33.669  1.00 29.27  ? 597  GLU   A CA  1 
ATOM   2382  C  C   . GLU   A  1 296 ? -11.570 6.782   -34.100  1.00 28.32  ? 597  GLU   A C   1 
ATOM   2383  O  O   . GLU   A  1 296 ? -10.340 6.785   -33.954  1.00 28.09  ? 597  GLU   A O   1 
ATOM   2384  C  CB  . GLU   A  1 296 ? -12.747 4.733   -34.889  1.00 34.87  ? 597  GLU   A CB  1 
ATOM   2385  C  CG  . GLU   A  1 296 ? -13.544 3.477   -34.599  1.00 28.49  ? 597  GLU   A CG  1 
ATOM   2386  C  CD  . GLU   A  1 296 ? -13.806 2.719   -35.886  1.00 24.52  ? 597  GLU   A CD  1 
ATOM   2387  O  OE1 . GLU   A  1 296 ? -12.848 2.104   -36.398  1.00 17.76  ? 597  GLU   A OE1 1 
ATOM   2388  O  OE2 . GLU   A  1 296 ? -14.949 2.766   -36.387  1.00 20.08  ? 597  GLU   A OE2 1 
ATOM   2389  N  N   . ILE   A  1 297 ? -12.243 7.815   -34.616  1.00 20.08  ? 598  ILE   A N   1 
ATOM   2390  C  CA  . ILE   A  1 297 ? -11.587 9.059   -35.011  1.00 21.93  ? 598  ILE   A CA  1 
ATOM   2391  C  C   . ILE   A  1 297 ? -11.401 9.984   -33.814  1.00 25.11  ? 598  ILE   A C   1 
ATOM   2392  O  O   . ILE   A  1 297 ? -10.288 10.446  -33.523  1.00 24.39  ? 598  ILE   A O   1 
ATOM   2393  C  CB  . ILE   A  1 297 ? -12.401 9.766   -36.108  1.00 20.87  ? 598  ILE   A CB  1 
ATOM   2394  C  CG1 . ILE   A  1 297 ? -12.695 8.804   -37.284  1.00 22.67  ? 598  ILE   A CG1 1 
ATOM   2395  C  CG2 . ILE   A  1 297 ? -11.662 11.013  -36.553  1.00 22.05  ? 598  ILE   A CG2 1 
ATOM   2396  C  CD1 . ILE   A  1 297 ? -13.708 9.369   -38.297  1.00 19.09  ? 598  ILE   A CD1 1 
ATOM   2397  N  N   . GLY   A  1 298 ? -12.506 10.316  -33.139  1.00 22.93  ? 599  GLY   A N   1 
ATOM   2398  C  CA  . GLY   A  1 298 ? -12.462 11.334  -32.098  1.00 27.00  ? 599  GLY   A CA  1 
ATOM   2399  C  C   . GLY   A  1 298 ? -11.674 10.935  -30.859  1.00 23.16  ? 599  GLY   A C   1 
ATOM   2400  O  O   . GLY   A  1 298 ? -11.077 11.789  -30.197  1.00 29.80  ? 599  GLY   A O   1 
ATOM   2401  N  N   . VAL   A  1 299 ? -11.641 9.645   -30.534  1.00 27.72  ? 600  VAL   A N   1 
ATOM   2402  C  CA  . VAL   A  1 299 ? -10.912 9.213   -29.347  1.00 26.54  ? 600  VAL   A CA  1 
ATOM   2403  C  C   . VAL   A  1 299 ? -9.524  8.699   -29.707  1.00 31.01  ? 600  VAL   A C   1 
ATOM   2404  O  O   . VAL   A  1 299 ? -8.516  9.193   -29.190  1.00 30.76  ? 600  VAL   A O   1 
ATOM   2405  C  CB  . VAL   A  1 299 ? -11.688 8.135   -28.576  1.00 28.08  ? 600  VAL   A CB  1 
ATOM   2406  C  CG1 . VAL   A  1 299 ? -10.952 7.803   -27.303  1.00 28.41  ? 600  VAL   A CG1 1 
ATOM   2407  C  CG2 . VAL   A  1 299 ? -13.107 8.613   -28.270  1.00 30.30  ? 600  VAL   A CG2 1 
ATOM   2408  N  N   . ARG   A  1 300 ? -9.454  7.685   -30.572  1.00 29.46  ? 601  ARG   A N   1 
ATOM   2409  C  CA  . ARG   A  1 300 ? -8.167  7.028   -30.815  1.00 24.37  ? 601  ARG   A CA  1 
ATOM   2410  C  C   . ARG   A  1 300 ? -7.310  7.829   -31.788  1.00 26.38  ? 601  ARG   A C   1 
ATOM   2411  O  O   . ARG   A  1 300 ? -6.173  8.194   -31.474  1.00 34.51  ? 601  ARG   A O   1 
ATOM   2412  C  CB  . ARG   A  1 300 ? -8.385  5.605   -31.339  1.00 18.23  ? 601  ARG   A CB  1 
ATOM   2413  C  CG  . ARG   A  1 300 ? -9.269  4.750   -30.454  1.00 22.95  ? 601  ARG   A CG  1 
ATOM   2414  C  CD  . ARG   A  1 300 ? -8.672  4.625   -29.049  1.00 23.04  ? 601  ARG   A CD  1 
ATOM   2415  N  NE  . ARG   A  1 300 ? -7.264  4.270   -29.132  1.00 27.42  ? 601  ARG   A NE  1 
ATOM   2416  C  CZ  . ARG   A  1 300 ? -6.825  3.044   -29.391  1.00 26.55  ? 601  ARG   A CZ  1 
ATOM   2417  N  NH1 . ARG   A  1 300 ? -7.684  2.046   -29.556  1.00 19.25  ? 601  ARG   A NH1 1 
ATOM   2418  N  NH2 . ARG   A  1 300 ? -5.528  2.815   -29.463  1.00 27.86  ? 601  ARG   A NH2 1 
ATOM   2419  N  N   . ASP   A  1 301 ? -7.836  8.092   -32.988  1.00 28.35  ? 602  ASP   A N   1 
ATOM   2420  C  CA  . ASP   A  1 301 ? -7.035  8.748   -34.018  1.00 29.41  ? 602  ASP   A CA  1 
ATOM   2421  C  C   . ASP   A  1 301 ? -6.608  10.131  -33.566  1.00 28.86  ? 602  ASP   A C   1 
ATOM   2422  O  O   . ASP   A  1 301 ? -5.437  10.513  -33.692  1.00 29.06  ? 602  ASP   A O   1 
ATOM   2423  C  CB  . ASP   A  1 301 ? -7.822  8.832   -35.331  1.00 26.96  ? 602  ASP   A CB  1 
ATOM   2424  C  CG  . ASP   A  1 301 ? -8.083  7.463   -35.952  1.00 30.14  ? 602  ASP   A CG  1 
ATOM   2425  O  OD1 . ASP   A  1 301 ? -7.217  6.570   -35.840  1.00 30.53  ? 602  ASP   A OD1 1 
ATOM   2426  O  OD2 . ASP   A  1 301 ? -9.152  7.282   -36.570  1.00 31.70  ? 602  ASP   A OD2 1 
ATOM   2427  N  N   . TYR   A  1 302 ? -7.547  10.888  -33.015  1.00 22.83  ? 603  TYR   A N   1 
ATOM   2428  C  CA  . TYR   A  1 302 ? -7.260  12.259  -32.621  1.00 25.94  ? 603  TYR   A CA  1 
ATOM   2429  C  C   . TYR   A  1 302 ? -6.597  12.365  -31.251  1.00 32.90  ? 603  TYR   A C   1 
ATOM   2430  O  O   . TYR   A  1 302 ? -5.759  13.250  -31.044  1.00 31.08  ? 603  TYR   A O   1 
ATOM   2431  C  CB  . TYR   A  1 302 ? -8.548  13.068  -32.658  1.00 32.40  ? 603  TYR   A CB  1 
ATOM   2432  C  CG  . TYR   A  1 302 ? -8.906  13.531  -34.050  1.00 34.88  ? 603  TYR   A CG  1 
ATOM   2433  C  CD1 . TYR   A  1 302 ? -10.147 14.082  -34.320  1.00 33.72  ? 603  TYR   A CD1 1 
ATOM   2434  C  CD2 . TYR   A  1 302 ? -7.987  13.427  -35.093  1.00 37.66  ? 603  TYR   A CD2 1 
ATOM   2435  C  CE1 . TYR   A  1 302 ? -10.472 14.527  -35.611  1.00 29.51  ? 603  TYR   A CE1 1 
ATOM   2436  C  CE2 . TYR   A  1 302 ? -8.300  13.863  -36.371  1.00 37.70  ? 603  TYR   A CE2 1 
ATOM   2437  C  CZ  . TYR   A  1 302 ? -9.542  14.410  -36.622  1.00 35.26  ? 603  TYR   A CZ  1 
ATOM   2438  O  OH  . TYR   A  1 302 ? -9.855  14.845  -37.890  1.00 32.81  ? 603  TYR   A OH  1 
ATOM   2439  N  N   . CYS   A  1 303 ? -6.924  11.488  -30.301  1.00 28.26  ? 604  CYS   A N   1 
ATOM   2440  C  CA  . CYS   A  1 303 ? -6.504  11.756  -28.933  1.00 32.53  ? 604  CYS   A CA  1 
ATOM   2441  C  C   . CYS   A  1 303 ? -5.522  10.768  -28.320  1.00 33.43  ? 604  CYS   A C   1 
ATOM   2442  O  O   . CYS   A  1 303 ? -5.008  11.062  -27.234  1.00 32.82  ? 604  CYS   A O   1 
ATOM   2443  C  CB  . CYS   A  1 303 ? -7.726  11.876  -28.009  1.00 32.96  ? 604  CYS   A CB  1 
ATOM   2444  S  SG  . CYS   A  1 303 ? -8.742  13.303  -28.430  1.00 34.82  ? 604  CYS   A SG  1 
ATOM   2445  N  N   . ASP   A  1 304 ? -5.233  9.624   -28.949  1.00 25.21  ? 605  ASP   A N   1 
ATOM   2446  C  CA  . ASP   A  1 304 ? -4.101  8.826   -28.472  1.00 28.29  ? 605  ASP   A CA  1 
ATOM   2447  C  C   . ASP   A  1 304 ? -2.854  9.703   -28.434  1.00 37.09  ? 605  ASP   A C   1 
ATOM   2448  O  O   . ASP   A  1 304 ? -2.645  10.551  -29.310  1.00 36.80  ? 605  ASP   A O   1 
ATOM   2449  C  CB  . ASP   A  1 304 ? -3.828  7.607   -29.370  1.00 27.50  ? 605  ASP   A CB  1 
ATOM   2450  C  CG  . ASP   A  1 304 ? -4.772  6.432   -29.113  1.00 34.77  ? 605  ASP   A CG  1 
ATOM   2451  O  OD1 . ASP   A  1 304 ? -5.761  6.574   -28.353  1.00 34.15  ? 605  ASP   A OD1 1 
ATOM   2452  O  OD2 . ASP   A  1 304 ? -4.509  5.351   -29.693  1.00 35.48  ? 605  ASP   A OD2 1 
ATOM   2453  N  N   . ASN   A  1 305 ? -2.023  9.494   -27.409  1.00 30.34  ? 606  ASN   A N   1 
ATOM   2454  C  CA  . ASN   A  1 305 ? -0.769  10.236  -27.297  1.00 30.34  ? 606  ASN   A CA  1 
ATOM   2455  C  C   . ASN   A  1 305 ? 0.157   9.950   -28.474  1.00 33.51  ? 606  ASN   A C   1 
ATOM   2456  O  O   . ASN   A  1 305 ? 0.906   10.825  -28.911  1.00 32.89  ? 606  ASN   A O   1 
ATOM   2457  C  CB  . ASN   A  1 305 ? -0.068  9.888   -25.986  1.00 32.36  ? 606  ASN   A CB  1 
ATOM   2458  C  CG  . ASN   A  1 305 ? -0.860  10.332  -24.779  1.00 42.73  ? 606  ASN   A CG  1 
ATOM   2459  O  OD1 . ASN   A  1 305 ? -1.264  11.493  -24.688  1.00 52.42  ? 606  ASN   A OD1 1 
ATOM   2460  N  ND2 . ASN   A  1 305 ? -1.109  9.409   -23.854  1.00 43.24  ? 606  ASN   A ND2 1 
ATOM   2461  N  N   . SER   A  1 306 ? 0.143   8.727   -28.983  1.00 41.35  ? 607  SER   A N   1 
ATOM   2462  C  CA  . SER   A  1 306 ? 1.011   8.378   -30.094  1.00 39.98  ? 607  SER   A CA  1 
ATOM   2463  C  C   . SER   A  1 306 ? 0.324   8.541   -31.443  1.00 36.28  ? 607  SER   A C   1 
ATOM   2464  O  O   . SER   A  1 306 ? 0.828   8.027   -32.447  1.00 38.66  ? 607  SER   A O   1 
ATOM   2465  C  CB  . SER   A  1 306 ? 1.517   6.946   -29.927  1.00 32.83  ? 607  SER   A CB  1 
ATOM   2466  O  OG  . SER   A  1 306 ? 0.412   6.064   -29.933  1.00 40.67  ? 607  SER   A OG  1 
ATOM   2467  N  N   . ARG   A  1 307 ? -0.822  9.223   -31.490  1.00 30.77  ? 608  ARG   A N   1 
ATOM   2468  C  CA  . ARG   A  1 307 ? -1.456  9.528   -32.768  1.00 31.71  ? 608  ARG   A CA  1 
ATOM   2469  C  C   . ARG   A  1 307 ? -1.487  11.038  -32.973  1.00 31.85  ? 608  ARG   A C   1 
ATOM   2470  O  O   . ARG   A  1 307 ? -0.466  11.706  -32.764  1.00 29.03  ? 608  ARG   A O   1 
ATOM   2471  C  CB  . ARG   A  1 307 ? -2.855  8.905   -32.845  1.00 29.05  ? 608  ARG   A CB  1 
ATOM   2472  C  CG  . ARG   A  1 307 ? -2.856  7.377   -32.712  1.00 32.31  ? 608  ARG   A CG  1 
ATOM   2473  C  CD  . ARG   A  1 307 ? -2.168  6.673   -33.890  1.00 38.87  ? 608  ARG   A CD  1 
ATOM   2474  N  NE  . ARG   A  1 307 ? -2.729  7.080   -35.177  1.00 32.67  ? 608  ARG   A NE  1 
ATOM   2475  C  CZ  . ARG   A  1 307 ? -3.936  6.732   -35.613  1.00 32.33  ? 608  ARG   A CZ  1 
ATOM   2476  N  NH1 . ARG   A  1 307 ? -4.727  5.960   -34.870  1.00 28.52  ? 608  ARG   A NH1 1 
ATOM   2477  N  NH2 . ARG   A  1 307 ? -4.362  7.166   -36.795  1.00 30.42  ? 608  ARG   A NH2 1 
ATOM   2478  N  N   . TYR   A  1 308 ? -2.625  11.607  -33.383  1.00 26.97  ? 609  TYR   A N   1 
ATOM   2479  C  CA  . TYR   A  1 308 ? -2.621  13.049  -33.612  1.00 28.36  ? 609  TYR   A CA  1 
ATOM   2480  C  C   . TYR   A  1 308 ? -2.547  13.850  -32.319  1.00 35.51  ? 609  TYR   A C   1 
ATOM   2481  O  O   . TYR   A  1 308 ? -2.157  15.018  -32.366  1.00 33.37  ? 609  TYR   A O   1 
ATOM   2482  C  CB  . TYR   A  1 308 ? -3.830  13.466  -34.437  1.00 29.26  ? 609  TYR   A CB  1 
ATOM   2483  C  CG  . TYR   A  1 308 ? -3.568  13.258  -35.907  1.00 38.31  ? 609  TYR   A CG  1 
ATOM   2484  C  CD1 . TYR   A  1 308 ? -3.714  12.005  -36.485  1.00 28.27  ? 609  TYR   A CD1 1 
ATOM   2485  C  CD2 . TYR   A  1 308 ? -3.136  14.309  -36.711  1.00 40.50  ? 609  TYR   A CD2 1 
ATOM   2486  C  CE1 . TYR   A  1 308 ? -3.467  11.811  -37.826  1.00 29.75  ? 609  TYR   A CE1 1 
ATOM   2487  C  CE2 . TYR   A  1 308 ? -2.887  14.117  -38.052  1.00 40.91  ? 609  TYR   A CE2 1 
ATOM   2488  C  CZ  . TYR   A  1 308 ? -3.054  12.869  -38.599  1.00 25.09  ? 609  TYR   A CZ  1 
ATOM   2489  O  OH  . TYR   A  1 308 ? -2.799  12.678  -39.935  1.00 33.24  ? 609  TYR   A OH  1 
ATOM   2490  N  N   . ASN   A  1 309 ? -2.897  13.250  -31.176  1.00 33.21  ? 610  ASN   A N   1 
ATOM   2491  C  CA  . ASN   A  1 309 ? -2.586  13.811  -29.859  1.00 30.20  ? 610  ASN   A CA  1 
ATOM   2492  C  C   . ASN   A  1 309 ? -3.096  15.243  -29.701  1.00 30.96  ? 610  ASN   A C   1 
ATOM   2493  O  O   . ASN   A  1 309 ? -2.364  16.146  -29.291  1.00 33.09  ? 610  ASN   A O   1 
ATOM   2494  C  CB  . ASN   A  1 309 ? -1.074  13.735  -29.612  1.00 35.50  ? 610  ASN   A CB  1 
ATOM   2495  C  CG  . ASN   A  1 309 ? -0.671  14.108  -28.185  1.00 39.38  ? 610  ASN   A CG  1 
ATOM   2496  O  OD1 . ASN   A  1 309 ? -1.439  13.947  -27.234  1.00 34.76  ? 610  ASN   A OD1 1 
ATOM   2497  N  ND2 . ASN   A  1 309 ? 0.543   14.614  -28.040  1.00 38.34  ? 610  ASN   A ND2 1 
ATOM   2498  N  N   . ILE   A  1 310 ? -4.377  15.469  -30.015  1.00 28.29  ? 611  ILE   A N   1 
ATOM   2499  C  CA  . ILE   A  1 310 ? -4.837  16.857  -30.109  1.00 32.38  ? 611  ILE   A CA  1 
ATOM   2500  C  C   . ILE   A  1 310 ? -5.479  17.385  -28.827  1.00 37.65  ? 611  ILE   A C   1 
ATOM   2501  O  O   . ILE   A  1 310 ? -5.961  18.529  -28.825  1.00 40.50  ? 611  ILE   A O   1 
ATOM   2502  C  CB  . ILE   A  1 310 ? -5.824  17.058  -31.282  1.00 38.96  ? 611  ILE   A CB  1 
ATOM   2503  C  CG1 . ILE   A  1 310 ? -7.179  16.421  -30.967  1.00 33.83  ? 611  ILE   A CG1 1 
ATOM   2504  C  CG2 . ILE   A  1 310 ? -5.235  16.509  -32.564  1.00 35.67  ? 611  ILE   A CG2 1 
ATOM   2505  C  CD1 . ILE   A  1 310 ? -8.269  16.829  -31.947  1.00 34.45  ? 611  ILE   A CD1 1 
ATOM   2506  N  N   . LEU   A  1 311 ? -5.480  16.614  -27.735  1.00 35.10  ? 612  LEU   A N   1 
ATOM   2507  C  CA  . LEU   A  1 311 ? -6.157  17.071  -26.518  1.00 33.85  ? 612  LEU   A CA  1 
ATOM   2508  C  C   . LEU   A  1 311 ? -5.605  18.406  -26.039  1.00 33.82  ? 612  LEU   A C   1 
ATOM   2509  O  O   . LEU   A  1 311 ? -6.369  19.319  -25.711  1.00 38.47  ? 612  LEU   A O   1 
ATOM   2510  C  CB  . LEU   A  1 311 ? -6.044  16.023  -25.408  1.00 31.43  ? 612  LEU   A CB  1 
ATOM   2511  C  CG  . LEU   A  1 311 ? -6.917  14.778  -25.537  1.00 31.89  ? 612  LEU   A CG  1 
ATOM   2512  C  CD1 . LEU   A  1 311 ? -6.575  13.780  -24.448  1.00 33.01  ? 612  LEU   A CD1 1 
ATOM   2513  C  CD2 . LEU   A  1 311 ? -8.375  15.166  -25.470  1.00 34.68  ? 612  LEU   A CD2 1 
ATOM   2514  N  N   . GLU   A  1 312 ? -4.276  18.534  -25.985  1.00 46.04  ? 613  GLU   A N   1 
ATOM   2515  C  CA  . GLU   A  1 312 ? -3.628  19.785  -25.589  1.00 51.94  ? 613  GLU   A CA  1 
ATOM   2516  C  C   . GLU   A  1 312 ? -4.187  20.982  -26.356  1.00 53.55  ? 613  GLU   A C   1 
ATOM   2517  O  O   . GLU   A  1 312 ? -4.681  21.945  -25.758  1.00 48.69  ? 613  GLU   A O   1 
ATOM   2518  C  CB  . GLU   A  1 312 ? -2.120  19.663  -25.821  1.00 70.17  ? 613  GLU   A CB  1 
ATOM   2519  C  CG  . GLU   A  1 312 ? -1.255  20.584  -24.995  1.00 85.46  ? 613  GLU   A CG  1 
ATOM   2520  C  CD  . GLU   A  1 312 ? -0.684  19.880  -23.785  1.00 97.25  ? 613  GLU   A CD  1 
ATOM   2521  O  OE1 . GLU   A  1 312 ? -1.468  19.527  -22.882  1.00 100.38 ? 613  GLU   A OE1 1 
ATOM   2522  O  OE2 . GLU   A  1 312 ? 0.544   19.656  -23.746  1.00 101.85 ? 613  GLU   A OE2 1 
ATOM   2523  N  N   . GLU   A  1 313 ? -4.096  20.937  -27.695  1.00 44.82  ? 614  GLU   A N   1 
ATOM   2524  C  CA  . GLU   A  1 313 ? -4.578  22.029  -28.541  1.00 51.87  ? 614  GLU   A CA  1 
ATOM   2525  C  C   . GLU   A  1 313 ? -6.033  22.364  -28.243  1.00 48.32  ? 614  GLU   A C   1 
ATOM   2526  O  O   . GLU   A  1 313 ? -6.409  23.534  -28.122  1.00 49.01  ? 614  GLU   A O   1 
ATOM   2527  C  CB  . GLU   A  1 313 ? -4.428  21.652  -30.016  1.00 65.85  ? 614  GLU   A CB  1 
ATOM   2528  C  CG  . GLU   A  1 313 ? -3.140  22.095  -30.682  1.00 86.07  ? 614  GLU   A CG  1 
ATOM   2529  C  CD  . GLU   A  1 313 ? -3.233  23.496  -31.270  1.00 99.93  ? 614  GLU   A CD  1 
ATOM   2530  O  OE1 . GLU   A  1 313 ? -2.609  24.426  -30.709  1.00 103.24 ? 614  GLU   A OE1 1 
ATOM   2531  O  OE2 . GLU   A  1 313 ? -3.941  23.667  -32.288  1.00 101.94 ? 614  GLU   A OE2 1 
ATOM   2532  N  N   . VAL   A  1 314 ? -6.871  21.341  -28.131  1.00 47.86  ? 615  VAL   A N   1 
ATOM   2533  C  CA  . VAL   A  1 314 ? -8.299  21.578  -27.982  1.00 39.76  ? 615  VAL   A CA  1 
ATOM   2534  C  C   . VAL   A  1 314 ? -8.605  22.169  -26.617  1.00 36.77  ? 615  VAL   A C   1 
ATOM   2535  O  O   . VAL   A  1 314 ? -9.374  23.130  -26.499  1.00 34.94  ? 615  VAL   A O   1 
ATOM   2536  C  CB  . VAL   A  1 314 ? -9.062  20.270  -28.222  1.00 35.90  ? 615  VAL   A CB  1 
ATOM   2537  C  CG1 . VAL   A  1 314 ? -10.529 20.450  -27.887  1.00 33.04  ? 615  VAL   A CG1 1 
ATOM   2538  C  CG2 . VAL   A  1 314 ? -8.853  19.815  -29.670  1.00 33.61  ? 615  VAL   A CG2 1 
ATOM   2539  N  N   . ALA   A  1 315 ? -8.014  21.600  -25.567  1.00 37.98  ? 616  ALA   A N   1 
ATOM   2540  C  CA  . ALA   A  1 315 ? -8.271  22.088  -24.215  1.00 40.12  ? 616  ALA   A CA  1 
ATOM   2541  C  C   . ALA   A  1 315 ? -7.853  23.544  -24.059  1.00 39.29  ? 616  ALA   A C   1 
ATOM   2542  O  O   . ALA   A  1 315 ? -8.548  24.324  -23.398  1.00 44.79  ? 616  ALA   A O   1 
ATOM   2543  C  CB  . ALA   A  1 315 ? -7.555  21.209  -23.192  1.00 37.25  ? 616  ALA   A CB  1 
ATOM   2544  N  N   . LYS   A  1 316 ? -6.724  23.930  -24.660  1.00 48.03  ? 617  LYS   A N   1 
ATOM   2545  C  CA  . LYS   A  1 316 ? -6.297  25.327  -24.632  1.00 52.74  ? 617  LYS   A CA  1 
ATOM   2546  C  C   . LYS   A  1 316 ? -7.387  26.243  -25.176  1.00 56.02  ? 617  LYS   A C   1 
ATOM   2547  O  O   . LYS   A  1 316 ? -7.819  27.189  -24.508  1.00 53.64  ? 617  LYS   A O   1 
ATOM   2548  C  CB  . LYS   A  1 316 ? -5.015  25.506  -25.445  1.00 56.56  ? 617  LYS   A CB  1 
ATOM   2549  C  CG  . LYS   A  1 316 ? -3.729  25.050  -24.795  1.00 64.01  ? 617  LYS   A CG  1 
ATOM   2550  C  CD  . LYS   A  1 316 ? -2.575  25.352  -25.740  1.00 77.70  ? 617  LYS   A CD  1 
ATOM   2551  C  CE  . LYS   A  1 316 ? -1.231  25.341  -25.041  1.00 85.04  ? 617  LYS   A CE  1 
ATOM   2552  N  NZ  . LYS   A  1 316 ? -0.883  23.994  -24.517  1.00 81.40  ? 617  LYS   A NZ  1 
ATOM   2553  N  N   . LYS   A  1 317 ? -7.839  25.973  -26.403  1.00 55.13  ? 618  LYS   A N   1 
ATOM   2554  C  CA  . LYS   A  1 317 ? -8.898  26.769  -27.015  1.00 51.17  ? 618  LYS   A CA  1 
ATOM   2555  C  C   . LYS   A  1 317 ? -10.170 26.754  -26.175  1.00 49.66  ? 618  LYS   A C   1 
ATOM   2556  O  O   . LYS   A  1 317 ? -10.964 27.701  -26.225  1.00 46.05  ? 618  LYS   A O   1 
ATOM   2557  C  CB  . LYS   A  1 317 ? -9.186  26.247  -28.423  1.00 51.40  ? 618  LYS   A CB  1 
ATOM   2558  C  CG  . LYS   A  1 317 ? -7.977  26.217  -29.370  1.00 56.10  ? 618  LYS   A CG  1 
ATOM   2559  C  CD  . LYS   A  1 317 ? -7.924  27.448  -30.250  1.00 66.36  ? 618  LYS   A CD  1 
ATOM   2560  C  CE  . LYS   A  1 317 ? -6.486  27.808  -30.612  1.00 76.18  ? 618  LYS   A CE  1 
ATOM   2561  N  NZ  . LYS   A  1 317 ? -6.287  27.881  -32.091  1.00 79.75  ? 618  LYS   A NZ  1 
ATOM   2562  N  N   . MET   A  1 318 ? -10.384 25.693  -25.400  1.00 43.30  ? 619  MET   A N   1 
ATOM   2563  C  CA  . MET   A  1 318 ? -11.540 25.636  -24.518  1.00 44.81  ? 619  MET   A CA  1 
ATOM   2564  C  C   . MET   A  1 318 ? -11.309 26.352  -23.200  1.00 45.77  ? 619  MET   A C   1 
ATOM   2565  O  O   . MET   A  1 318 ? -12.245 26.445  -22.399  1.00 44.60  ? 619  MET   A O   1 
ATOM   2566  C  CB  . MET   A  1 318 ? -11.928 24.189  -24.241  1.00 35.54  ? 619  MET   A CB  1 
ATOM   2567  C  CG  . MET   A  1 318 ? -12.661 23.542  -25.376  1.00 34.31  ? 619  MET   A CG  1 
ATOM   2568  S  SD  . MET   A  1 318 ? -13.002 21.815  -25.027  1.00 39.94  ? 619  MET   A SD  1 
ATOM   2569  C  CE  . MET   A  1 318 ? -14.070 21.948  -23.591  1.00 39.55  ? 619  MET   A CE  1 
ATOM   2570  N  N   . ASN   A  1 319 ? -10.092 26.843  -22.960  1.00 44.52  ? 620  ASN   A N   1 
ATOM   2571  C  CA  . ASN   A  1 319 ? -9.771  27.581  -21.743  1.00 52.54  ? 620  ASN   A CA  1 
ATOM   2572  C  C   . ASN   A  1 319 ? -10.030 26.740  -20.497  1.00 50.23  ? 620  ASN   A C   1 
ATOM   2573  O  O   . ASN   A  1 319 ? -10.541 27.224  -19.486  1.00 44.96  ? 620  ASN   A O   1 
ATOM   2574  C  CB  . ASN   A  1 319 ? -10.538 28.901  -21.697  1.00 64.52  ? 620  ASN   A CB  1 
ATOM   2575  C  CG  . ASN   A  1 319 ? -10.010 29.893  -22.710  1.00 74.31  ? 620  ASN   A CG  1 
ATOM   2576  O  OD1 . ASN   A  1 319 ? -8.803  30.098  -22.794  1.00 80.16  ? 620  ASN   A OD1 1 
ATOM   2577  N  ND2 . ASN   A  1 319 ? -10.901 30.481  -23.512  1.00 79.50  ? 620  ASN   A ND2 1 
ATOM   2578  N  N   . LEU   A  1 320 ? -9.665  25.470  -20.569  1.00 46.00  ? 621  LEU   A N   1 
ATOM   2579  C  CA  . LEU   A  1 320 ? -9.771  24.598  -19.413  1.00 42.15  ? 621  LEU   A CA  1 
ATOM   2580  C  C   . LEU   A  1 320 ? -8.518  24.706  -18.551  1.00 49.49  ? 621  LEU   A C   1 
ATOM   2581  O  O   . LEU   A  1 320 ? -7.444  25.099  -19.018  1.00 48.22  ? 621  LEU   A O   1 
ATOM   2582  C  CB  . LEU   A  1 320 ? -9.980  23.153  -19.849  1.00 39.09  ? 621  LEU   A CB  1 
ATOM   2583  C  CG  . LEU   A  1 320 ? -11.123 22.957  -20.843  1.00 40.53  ? 621  LEU   A CG  1 
ATOM   2584  C  CD1 . LEU   A  1 320 ? -11.001 21.602  -21.499  1.00 38.39  ? 621  LEU   A CD1 1 
ATOM   2585  C  CD2 . LEU   A  1 320 ? -12.492 23.116  -20.172  1.00 42.78  ? 621  LEU   A CD2 1 
ATOM   2586  N  N   . ASP   A  1 321 ? -8.673  24.360  -17.275  1.00 48.97  ? 622  ASP   A N   1 
ATOM   2587  C  CA  . ASP   A  1 321 ? -7.551  24.304  -16.340  1.00 55.26  ? 622  ASP   A CA  1 
ATOM   2588  C  C   . ASP   A  1 321 ? -6.769  23.025  -16.605  1.00 53.57  ? 622  ASP   A C   1 
ATOM   2589  O  O   . ASP   A  1 321 ? -7.192  21.937  -16.212  1.00 54.13  ? 622  ASP   A O   1 
ATOM   2590  C  CB  . ASP   A  1 321 ? -8.044  24.342  -14.898  1.00 57.16  ? 622  ASP   A CB  1 
ATOM   2591  C  CG  . ASP   A  1 321 ? -6.908  24.268  -13.897  1.00 71.13  ? 622  ASP   A CG  1 
ATOM   2592  O  OD1 . ASP   A  1 321 ? -5.760  24.574  -14.293  1.00 68.29  ? 622  ASP   A OD1 1 
ATOM   2593  O  OD2 . ASP   A  1 321 ? -7.158  23.899  -12.724  1.00 78.41  ? 622  ASP   A OD2 1 
ATOM   2594  N  N   . MET   A  1 322 ? -5.609  23.146  -17.253  1.00 50.47  ? 623  MET   A N   1 
ATOM   2595  C  CA  . MET   A  1 322 ? -4.816  21.982  -17.627  1.00 49.42  ? 623  MET   A CA  1 
ATOM   2596  C  C   . MET   A  1 322 ? -3.641  21.741  -16.693  1.00 53.84  ? 623  MET   A C   1 
ATOM   2597  O  O   . MET   A  1 322 ? -2.722  20.993  -17.046  1.00 58.64  ? 623  MET   A O   1 
ATOM   2598  C  CB  . MET   A  1 322 ? -4.317  22.118  -19.058  1.00 42.16  ? 623  MET   A CB  1 
ATOM   2599  C  CG  . MET   A  1 322 ? -5.424  22.356  -20.052  1.00 51.71  ? 623  MET   A CG  1 
ATOM   2600  S  SD  . MET   A  1 322 ? -4.771  22.996  -21.592  1.00 57.27  ? 623  MET   A SD  1 
ATOM   2601  C  CE  . MET   A  1 322 ? -3.710  21.652  -22.122  1.00 43.81  ? 623  MET   A CE  1 
ATOM   2602  N  N   . ARG   A  1 323 ? -3.661  22.337  -15.502  1.00 52.59  ? 624  ARG   A N   1 
ATOM   2603  C  CA  . ARG   A  1 323 ? -2.544  22.188  -14.578  1.00 52.79  ? 624  ARG   A CA  1 
ATOM   2604  C  C   . ARG   A  1 323 ? -2.512  20.808  -13.926  1.00 51.10  ? 624  ARG   A C   1 
ATOM   2605  O  O   . ARG   A  1 323 ? -1.430  20.250  -13.706  1.00 52.59  ? 624  ARG   A O   1 
ATOM   2606  C  CB  . ARG   A  1 323 ? -2.620  23.279  -13.517  1.00 59.02  ? 624  ARG   A CB  1 
ATOM   2607  C  CG  . ARG   A  1 323 ? -1.647  23.120  -12.376  1.00 62.71  ? 624  ARG   A CG  1 
ATOM   2608  C  CD  . ARG   A  1 323 ? -1.730  24.325  -11.462  1.00 61.79  ? 624  ARG   A CD  1 
ATOM   2609  N  NE  . ARG   A  1 323 ? -1.530  23.963  -10.068  1.00 76.87  ? 624  ARG   A NE  1 
ATOM   2610  C  CZ  . ARG   A  1 323 ? -2.509  23.591  -9.251   1.00 89.16  ? 624  ARG   A CZ  1 
ATOM   2611  N  NH1 . ARG   A  1 323 ? -3.759  23.536  -9.696   1.00 90.28  ? 624  ARG   A NH1 1 
ATOM   2612  N  NH2 . ARG   A  1 323 ? -2.240  23.284  -7.986   1.00 92.89  ? 624  ARG   A NH2 1 
ATOM   2613  N  N   . LYS   A  1 324 ? -3.675  20.247  -13.598  1.00 48.13  ? 625  LYS   A N   1 
ATOM   2614  C  CA  . LYS   A  1 324 ? -3.755  18.977  -12.885  1.00 54.92  ? 625  LYS   A CA  1 
ATOM   2615  C  C   . LYS   A  1 324 ? -4.713  18.040  -13.606  1.00 48.54  ? 625  LYS   A C   1 
ATOM   2616  O  O   . LYS   A  1 324 ? -5.669  18.484  -14.245  1.00 48.30  ? 625  LYS   A O   1 
ATOM   2617  C  CB  . LYS   A  1 324 ? -4.211  19.184  -11.429  1.00 61.75  ? 625  LYS   A CB  1 
ATOM   2618  C  CG  . LYS   A  1 324 ? -5.477  20.021  -11.291  1.00 70.35  ? 625  LYS   A CG  1 
ATOM   2619  C  CD  . LYS   A  1 324 ? -5.545  20.727  -9.939   1.00 77.53  ? 625  LYS   A CD  1 
ATOM   2620  C  CE  . LYS   A  1 324 ? -6.687  21.734  -9.908   1.00 80.47  ? 625  LYS   A CE  1 
ATOM   2621  N  NZ  . LYS   A  1 324 ? -8.006  21.061  -10.094  1.00 79.22  ? 625  LYS   A NZ  1 
ATOM   2622  N  N   . THR   A  1 325 ? -4.458  16.733  -13.496  1.00 38.76  ? 626  THR   A N   1 
ATOM   2623  C  CA  . THR   A  1 325 ? -5.327  15.775  -14.177  1.00 46.18  ? 626  THR   A CA  1 
ATOM   2624  C  C   . THR   A  1 325 ? -6.754  15.822  -13.641  1.00 39.48  ? 626  THR   A C   1 
ATOM   2625  O  O   . THR   A  1 325 ? -7.701  15.539  -14.383  1.00 37.04  ? 626  THR   A O   1 
ATOM   2626  C  CB  . THR   A  1 325 ? -4.772  14.356  -14.048  1.00 48.19  ? 626  THR   A CB  1 
ATOM   2627  O  OG1 . THR   A  1 325 ? -4.665  14.012  -12.662  1.00 52.56  ? 626  THR   A OG1 1 
ATOM   2628  C  CG2 . THR   A  1 325 ? -3.404  14.260  -14.688  1.00 51.83  ? 626  THR   A CG2 1 
ATOM   2629  N  N   . SER   A  1 326 ? -6.929  16.186  -12.367  1.00 39.39  ? 627  SER   A N   1 
ATOM   2630  C  CA  . SER   A  1 326 ? -8.234  16.072  -11.734  1.00 34.80  ? 627  SER   A CA  1 
ATOM   2631  C  C   . SER   A  1 326 ? -9.227  17.122  -12.208  1.00 41.02  ? 627  SER   A C   1 
ATOM   2632  O  O   . SER   A  1 326 ? -10.412 17.001  -11.889  1.00 43.91  ? 627  SER   A O   1 
ATOM   2633  C  CB  . SER   A  1 326 ? -8.098  16.138  -10.209  1.00 38.61  ? 627  SER   A CB  1 
ATOM   2634  O  OG  . SER   A  1 326 ? -7.276  17.208  -9.823   1.00 46.78  ? 627  SER   A OG  1 
ATOM   2635  N  N   . SER   A  1 327 ? -8.802  18.141  -12.960  1.00 35.83  ? 628  SER   A N   1 
ATOM   2636  C  CA  . SER   A  1 327 ? -9.811  18.989  -13.581  1.00 36.38  ? 628  SER   A CA  1 
ATOM   2637  C  C   . SER   A  1 327 ? -10.561 18.261  -14.679  1.00 36.83  ? 628  SER   A C   1 
ATOM   2638  O  O   . SER   A  1 327 ? -11.566 18.787  -15.165  1.00 38.31  ? 628  SER   A O   1 
ATOM   2639  C  CB  . SER   A  1 327 ? -9.189  20.257  -14.158  1.00 34.90  ? 628  SER   A CB  1 
ATOM   2640  O  OG  . SER   A  1 327 ? -8.317  19.938  -15.222  1.00 38.12  ? 628  SER   A OG  1 
ATOM   2641  N  N   . LEU   A  1 328 ? -10.095 17.068  -15.061  1.00 31.98  ? 629  LEU   A N   1 
ATOM   2642  C  CA  . LEU   A  1 328 ? -10.671 16.277  -16.138  1.00 34.20  ? 629  LEU   A CA  1 
ATOM   2643  C  C   . LEU   A  1 328 ? -10.728 17.082  -17.433  1.00 35.23  ? 629  LEU   A C   1 
ATOM   2644  O  O   . LEU   A  1 328 ? -11.644 16.938  -18.250  1.00 33.57  ? 629  LEU   A O   1 
ATOM   2645  C  CB  . LEU   A  1 328 ? -12.045 15.726  -15.752  1.00 32.25  ? 629  LEU   A CB  1 
ATOM   2646  C  CG  . LEU   A  1 328 ? -12.091 14.933  -14.437  1.00 35.41  ? 629  LEU   A CG  1 
ATOM   2647  C  CD1 . LEU   A  1 328 ? -13.368 14.136  -14.370  1.00 31.18  ? 629  LEU   A CD1 1 
ATOM   2648  C  CD2 . LEU   A  1 328 ? -10.901 14.002  -14.311  1.00 30.57  ? 629  LEU   A CD2 1 
ATOM   2649  N  N   . TRP   A  1 329 ? -9.715  17.924  -17.632  1.00 32.64  ? 630  TRP   A N   1 
ATOM   2650  C  CA  . TRP   A  1 329 ? -9.644  18.703  -18.860  1.00 34.92  ? 630  TRP   A CA  1 
ATOM   2651  C  C   . TRP   A  1 329 ? -9.496  17.799  -20.081  1.00 35.72  ? 630  TRP   A C   1 
ATOM   2652  O  O   . TRP   A  1 329 ? -10.072 18.082  -21.138  1.00 35.43  ? 630  TRP   A O   1 
ATOM   2653  C  CB  . TRP   A  1 329 ? -8.507  19.718  -18.782  1.00 37.10  ? 630  TRP   A CB  1 
ATOM   2654  C  CG  . TRP   A  1 329 ? -7.143  19.134  -18.705  1.00 39.60  ? 630  TRP   A CG  1 
ATOM   2655  C  CD1 . TRP   A  1 329 ? -6.423  18.870  -17.573  1.00 46.45  ? 630  TRP   A CD1 1 
ATOM   2656  C  CD2 . TRP   A  1 329 ? -6.310  18.772  -19.804  1.00 42.79  ? 630  TRP   A CD2 1 
ATOM   2657  N  NE1 . TRP   A  1 329 ? -5.197  18.355  -17.905  1.00 44.91  ? 630  TRP   A NE1 1 
ATOM   2658  C  CE2 . TRP   A  1 329 ? -5.103  18.284  -19.270  1.00 42.18  ? 630  TRP   A CE2 1 
ATOM   2659  C  CE3 . TRP   A  1 329 ? -6.471  18.804  -21.192  1.00 39.08  ? 630  TRP   A CE3 1 
ATOM   2660  C  CZ2 . TRP   A  1 329 ? -4.061  17.839  -20.077  1.00 40.37  ? 630  TRP   A CZ2 1 
ATOM   2661  C  CZ3 . TRP   A  1 329 ? -5.437  18.369  -21.993  1.00 38.04  ? 630  TRP   A CZ3 1 
ATOM   2662  C  CH2 . TRP   A  1 329 ? -4.246  17.891  -21.435  1.00 39.18  ? 630  TRP   A CH2 1 
ATOM   2663  N  N   . LYS   A  1 330 ? -8.757  16.691  -19.953  1.00 28.97  ? 631  LYS   A N   1 
ATOM   2664  C  CA  . LYS   A  1 330 ? -8.661  15.763  -21.073  1.00 27.74  ? 631  LYS   A CA  1 
ATOM   2665  C  C   . LYS   A  1 330 ? -10.026 15.185  -21.408  1.00 37.07  ? 631  LYS   A C   1 
ATOM   2666  O  O   . LYS   A  1 330 ? -10.418 15.115  -22.579  1.00 28.70  ? 631  LYS   A O   1 
ATOM   2667  C  CB  . LYS   A  1 330 ? -7.667  14.647  -20.768  1.00 28.24  ? 631  LYS   A CB  1 
ATOM   2668  C  CG  . LYS   A  1 330 ? -6.218  15.082  -20.843  1.00 32.54  ? 631  LYS   A CG  1 
ATOM   2669  C  CD  . LYS   A  1 330 ? -5.271  13.907  -20.691  1.00 38.24  ? 631  LYS   A CD  1 
ATOM   2670  C  CE  . LYS   A  1 330 ? -3.836  14.347  -20.885  1.00 42.37  ? 631  LYS   A CE  1 
ATOM   2671  N  NZ  . LYS   A  1 330 ? -2.904  13.210  -20.771  1.00 46.74  ? 631  LYS   A NZ  1 
ATOM   2672  N  N   . ASP   A  1 331 ? -10.772 14.783  -20.380  1.00 29.58  ? 632  ASP   A N   1 
ATOM   2673  C  CA  . ASP   A  1 331 ? -12.076 14.172  -20.599  1.00 27.03  ? 632  ASP   A CA  1 
ATOM   2674  C  C   . ASP   A  1 331 ? -13.038 15.166  -21.222  1.00 30.65  ? 632  ASP   A C   1 
ATOM   2675  O  O   . ASP   A  1 331 ? -13.854 14.807  -22.078  1.00 30.33  ? 632  ASP   A O   1 
ATOM   2676  C  CB  . ASP   A  1 331 ? -12.640 13.666  -19.270  1.00 28.98  ? 632  ASP   A CB  1 
ATOM   2677  C  CG  . ASP   A  1 331 ? -11.620 12.888  -18.472  1.00 30.90  ? 632  ASP   A CG  1 
ATOM   2678  O  OD1 . ASP   A  1 331 ? -10.679 13.519  -17.948  1.00 31.36  ? 632  ASP   A OD1 1 
ATOM   2679  O  OD2 . ASP   A  1 331 ? -11.738 11.648  -18.402  1.00 29.77  ? 632  ASP   A OD2 1 
ATOM   2680  N  N   . GLN   A  1 332 ? -12.974 16.415  -20.769  1.00 30.83  ? 633  GLN   A N   1 
ATOM   2681  C  CA  . GLN   A  1 332 ? -13.865 17.442  -21.276  1.00 33.72  ? 633  GLN   A CA  1 
ATOM   2682  C  C   . GLN   A  1 332 ? -13.580 17.723  -22.742  1.00 32.61  ? 633  GLN   A C   1 
ATOM   2683  O  O   . GLN   A  1 332 ? -14.498 17.746  -23.567  1.00 28.90  ? 633  GLN   A O   1 
ATOM   2684  C  CB  . GLN   A  1 332 ? -13.710 18.704  -20.436  1.00 35.90  ? 633  GLN   A CB  1 
ATOM   2685  C  CG  . GLN   A  1 332 ? -14.984 19.468  -20.241  1.00 51.64  ? 633  GLN   A CG  1 
ATOM   2686  C  CD  . GLN   A  1 332 ? -14.924 20.348  -19.015  1.00 59.91  ? 633  GLN   A CD  1 
ATOM   2687  O  OE1 . GLN   A  1 332 ? -13.846 20.641  -18.494  1.00 50.31  ? 633  GLN   A OE1 1 
ATOM   2688  N  NE2 . GLN   A  1 332 ? -16.083 20.767  -18.537  1.00 72.68  ? 633  GLN   A NE2 1 
ATOM   2689  N  N   . ALA   A  1 333 ? -12.306 17.920  -23.088  1.00 32.42  ? 634  ALA   A N   1 
ATOM   2690  C  CA  . ALA   A  1 333 ? -11.955 18.110  -24.492  1.00 34.14  ? 634  ALA   A CA  1 
ATOM   2691  C  C   . ALA   A  1 333 ? -12.318 16.886  -25.305  1.00 32.69  ? 634  ALA   A C   1 
ATOM   2692  O  O   . ALA   A  1 333 ? -12.791 17.001  -26.444  1.00 28.85  ? 634  ALA   A O   1 
ATOM   2693  C  CB  . ALA   A  1 333 ? -10.465 18.415  -24.632  1.00 33.62  ? 634  ALA   A CB  1 
ATOM   2694  N  N   . LEU   A  1 334 ? -12.112 15.701  -24.728  1.00 34.40  ? 635  LEU   A N   1 
ATOM   2695  C  CA  . LEU   A  1 334 ? -12.390 14.470  -25.451  1.00 32.01  ? 635  LEU   A CA  1 
ATOM   2696  C  C   . LEU   A  1 334 ? -13.831 14.440  -25.936  1.00 34.64  ? 635  LEU   A C   1 
ATOM   2697  O  O   . LEU   A  1 334 ? -14.099 14.095  -27.095  1.00 29.11  ? 635  LEU   A O   1 
ATOM   2698  C  CB  . LEU   A  1 334 ? -12.088 13.264  -24.566  1.00 27.66  ? 635  LEU   A CB  1 
ATOM   2699  C  CG  . LEU   A  1 334 ? -12.378 11.936  -25.265  1.00 29.16  ? 635  LEU   A CG  1 
ATOM   2700  C  CD1 . LEU   A  1 334 ? -11.402 11.720  -26.406  1.00 32.98  ? 635  LEU   A CD1 1 
ATOM   2701  C  CD2 . LEU   A  1 334 ? -12.311 10.792  -24.280  1.00 27.69  ? 635  LEU   A CD2 1 
ATOM   2702  N  N   . VAL   A  1 335 ? -14.773 14.841  -25.078  1.00 31.22  ? 636  VAL   A N   1 
ATOM   2703  C  CA  . VAL   A  1 335 ? -16.172 14.816  -25.483  1.00 31.71  ? 636  VAL   A CA  1 
ATOM   2704  C  C   . VAL   A  1 335 ? -16.425 15.811  -26.614  1.00 33.41  ? 636  VAL   A C   1 
ATOM   2705  O  O   . VAL   A  1 335 ? -17.092 15.487  -27.605  1.00 30.07  ? 636  VAL   A O   1 
ATOM   2706  C  CB  . VAL   A  1 335 ? -17.084 15.079  -24.277  1.00 30.75  ? 636  VAL   A CB  1 
ATOM   2707  C  CG1 . VAL   A  1 335 ? -18.503 15.214  -24.745  1.00 27.06  ? 636  VAL   A CG1 1 
ATOM   2708  C  CG2 . VAL   A  1 335 ? -16.963 13.940  -23.264  1.00 31.12  ? 636  VAL   A CG2 1 
ATOM   2709  N  N   . GLU   A  1 336 ? -15.882 17.022  -26.493  1.00 26.45  ? 637  GLU   A N   1 
ATOM   2710  C  CA  . GLU   A  1 336 ? -16.121 18.046  -27.497  1.00 27.30  ? 637  GLU   A CA  1 
ATOM   2711  C  C   . GLU   A  1 336 ? -15.580 17.613  -28.846  1.00 35.22  ? 637  GLU   A C   1 
ATOM   2712  O  O   . GLU   A  1 336 ? -16.227 17.817  -29.878  1.00 35.34  ? 637  GLU   A O   1 
ATOM   2713  C  CB  . GLU   A  1 336 ? -15.488 19.365  -27.061  1.00 31.50  ? 637  GLU   A CB  1 
ATOM   2714  C  CG  . GLU   A  1 336 ? -16.108 19.955  -25.814  1.00 41.72  ? 637  GLU   A CG  1 
ATOM   2715  C  CD  . GLU   A  1 336 ? -17.607 20.240  -25.942  1.00 53.12  ? 637  GLU   A CD  1 
ATOM   2716  O  OE1 . GLU   A  1 336 ? -18.150 20.331  -27.074  1.00 46.83  ? 637  GLU   A OE1 1 
ATOM   2717  O  OE2 . GLU   A  1 336 ? -18.245 20.379  -24.881  1.00 56.35  ? 637  GLU   A OE2 1 
ATOM   2718  N  N   . ILE   A  1 337 ? -14.408 16.981  -28.845  1.00 31.79  ? 638  ILE   A N   1 
ATOM   2719  C  CA  . ILE   A  1 337 ? -13.822 16.489  -30.081  1.00 33.26  ? 638  ILE   A CA  1 
ATOM   2720  C  C   . ILE   A  1 337 ? -14.745 15.470  -30.723  1.00 33.39  ? 638  ILE   A C   1 
ATOM   2721  O  O   . ILE   A  1 337 ? -15.028 15.527  -31.925  1.00 31.39  ? 638  ILE   A O   1 
ATOM   2722  C  CB  . ILE   A  1 337 ? -12.425 15.911  -29.791  1.00 33.31  ? 638  ILE   A CB  1 
ATOM   2723  C  CG1 . ILE   A  1 337 ? -11.456 17.051  -29.447  1.00 33.55  ? 638  ILE   A CG1 1 
ATOM   2724  C  CG2 . ILE   A  1 337 ? -11.907 15.109  -30.973  1.00 28.21  ? 638  ILE   A CG2 1 
ATOM   2725  C  CD1 . ILE   A  1 337 ? -10.185 16.577  -28.809  1.00 36.26  ? 638  ILE   A CD1 1 
ATOM   2726  N  N   . ASN   A  1 338 ? -15.285 14.564  -29.919  1.00 27.32  ? 639  ASN   A N   1 
ATOM   2727  C  CA  . ASN   A  1 338 ? -16.149 13.539  -30.476  1.00 26.93  ? 639  ASN   A CA  1 
ATOM   2728  C  C   . ASN   A  1 338 ? -17.507 14.088  -30.883  1.00 29.18  ? 639  ASN   A C   1 
ATOM   2729  O  O   . ASN   A  1 338 ? -18.107 13.575  -31.833  1.00 29.96  ? 639  ASN   A O   1 
ATOM   2730  C  CB  . ASN   A  1 338 ? -16.268 12.402  -29.487  1.00 23.92  ? 639  ASN   A CB  1 
ATOM   2731  C  CG  . ASN   A  1 338 ? -15.053 11.521  -29.527  1.00 31.17  ? 639  ASN   A CG  1 
ATOM   2732  O  OD1 . ASN   A  1 338 ? -15.032 10.524  -30.248  1.00 32.52  ? 639  ASN   A OD1 1 
ATOM   2733  N  ND2 . ASN   A  1 338 ? -13.997 11.932  -28.827  1.00 28.05  ? 639  ASN   A ND2 1 
ATOM   2734  N  N   . ILE   A  1 339 ? -17.998 15.124  -30.200  1.00 24.95  ? 640  ILE   A N   1 
ATOM   2735  C  CA  . ILE   A  1 339 ? -19.180 15.829  -30.685  1.00 29.91  ? 640  ILE   A CA  1 
ATOM   2736  C  C   . ILE   A  1 339 ? -18.915 16.400  -32.073  1.00 36.61  ? 640  ILE   A C   1 
ATOM   2737  O  O   . ILE   A  1 339 ? -19.729 16.250  -32.992  1.00 28.78  ? 640  ILE   A O   1 
ATOM   2738  C  CB  . ILE   A  1 339 ? -19.594 16.930  -29.699  1.00 28.36  ? 640  ILE   A CB  1 
ATOM   2739  C  CG1 . ILE   A  1 339 ? -20.140 16.306  -28.398  1.00 28.48  ? 640  ILE   A CG1 1 
ATOM   2740  C  CG2 . ILE   A  1 339 ? -20.573 17.897  -30.359  1.00 28.95  ? 640  ILE   A CG2 1 
ATOM   2741  C  CD1 . ILE   A  1 339 ? -20.577 17.310  -27.384  1.00 27.23  ? 640  ILE   A CD1 1 
ATOM   2742  N  N   . ALA   A  1 340 ? -17.761 17.054  -32.239  1.00 32.55  ? 641  ALA   A N   1 
ATOM   2743  C  CA  . ALA   A  1 340 ? -17.420 17.681  -33.507  1.00 34.48  ? 641  ALA   A CA  1 
ATOM   2744  C  C   . ALA   A  1 340 ? -17.316 16.654  -34.630  1.00 34.69  ? 641  ALA   A C   1 
ATOM   2745  O  O   . ALA   A  1 340 ? -17.823 16.878  -35.733  1.00 30.64  ? 641  ALA   A O   1 
ATOM   2746  C  CB  . ALA   A  1 340 ? -16.111 18.458  -33.360  1.00 30.27  ? 641  ALA   A CB  1 
ATOM   2747  N  N   . VAL   A  1 341 ? -16.661 15.523  -34.370  1.00 27.67  ? 642  VAL   A N   1 
ATOM   2748  C  CA  . VAL   A  1 341 ? -16.478 14.523  -35.415  1.00 28.63  ? 642  VAL   A CA  1 
ATOM   2749  C  C   . VAL   A  1 341 ? -17.827 14.046  -35.927  1.00 32.21  ? 642  VAL   A C   1 
ATOM   2750  O  O   . VAL   A  1 341 ? -18.089 14.040  -37.138  1.00 28.75  ? 642  VAL   A O   1 
ATOM   2751  C  CB  . VAL   A  1 341 ? -15.630 13.354  -34.891  1.00 28.30  ? 642  VAL   A CB  1 
ATOM   2752  C  CG1 . VAL   A  1 341 ? -15.812 12.130  -35.772  1.00 25.93  ? 642  VAL   A CG1 1 
ATOM   2753  C  CG2 . VAL   A  1 341 ? -14.167 13.764  -34.810  1.00 28.68  ? 642  VAL   A CG2 1 
ATOM   2754  N  N   . LEU   A  1 342 ? -18.708 13.653  -35.005  1.00 29.50  ? 643  LEU   A N   1 
ATOM   2755  C  CA  . LEU   A  1 342 ? -20.045 13.208  -35.380  1.00 31.54  ? 643  LEU   A CA  1 
ATOM   2756  C  C   . LEU   A  1 342 ? -20.804 14.304  -36.105  1.00 32.68  ? 643  LEU   A C   1 
ATOM   2757  O  O   . LEU   A  1 342 ? -21.411 14.068  -37.154  1.00 31.58  ? 643  LEU   A O   1 
ATOM   2758  C  CB  . LEU   A  1 342 ? -20.820 12.785  -34.136  1.00 28.77  ? 643  LEU   A CB  1 
ATOM   2759  C  CG  . LEU   A  1 342 ? -20.302 11.510  -33.475  1.00 27.94  ? 643  LEU   A CG  1 
ATOM   2760  C  CD1 . LEU   A  1 342 ? -20.908 11.384  -32.067  1.00 21.57  ? 643  LEU   A CD1 1 
ATOM   2761  C  CD2 . LEU   A  1 342 ? -20.599 10.288  -34.350  1.00 22.89  ? 643  LEU   A CD2 1 
ATOM   2762  N  N   . TYR   A  1 343 ? -20.822 15.500  -35.525  1.00 37.02  ? 644  TYR   A N   1 
ATOM   2763  C  CA  . TYR   A  1 343 ? -21.517 16.613  -36.149  1.00 35.19  ? 644  TYR   A CA  1 
ATOM   2764  C  C   . TYR   A  1 343 ? -21.012 16.861  -37.568  1.00 34.63  ? 644  TYR   A C   1 
ATOM   2765  O  O   . TYR   A  1 343 ? -21.795 17.180  -38.474  1.00 32.72  ? 644  TYR   A O   1 
ATOM   2766  C  CB  . TYR   A  1 343 ? -21.334 17.853  -35.290  1.00 28.68  ? 644  TYR   A CB  1 
ATOM   2767  C  CG  . TYR   A  1 343 ? -21.780 19.119  -35.962  1.00 30.33  ? 644  TYR   A CG  1 
ATOM   2768  C  CD1 . TYR   A  1 343 ? -23.125 19.423  -36.079  1.00 36.06  ? 644  TYR   A CD1 1 
ATOM   2769  C  CD2 . TYR   A  1 343 ? -20.852 20.025  -36.454  1.00 33.79  ? 644  TYR   A CD2 1 
ATOM   2770  C  CE1 . TYR   A  1 343 ? -23.535 20.585  -36.677  1.00 36.65  ? 644  TYR   A CE1 1 
ATOM   2771  C  CE2 . TYR   A  1 343 ? -21.251 21.196  -37.052  1.00 38.48  ? 644  TYR   A CE2 1 
ATOM   2772  C  CZ  . TYR   A  1 343 ? -22.591 21.471  -37.163  1.00 39.91  ? 644  TYR   A CZ  1 
ATOM   2773  O  OH  . TYR   A  1 343 ? -22.995 22.638  -37.760  1.00 42.53  ? 644  TYR   A OH  1 
ATOM   2774  N  N   . SER   A  1 344 ? -19.705 16.714  -37.780  1.00 35.26  ? 645  SER   A N   1 
ATOM   2775  C  CA  . SER   A  1 344 ? -19.124 17.060  -39.071  1.00 36.01  ? 645  SER   A CA  1 
ATOM   2776  C  C   . SER   A  1 344 ? -19.480 16.017  -40.117  1.00 37.75  ? 645  SER   A C   1 
ATOM   2777  O  O   . SER   A  1 344 ? -19.888 16.351  -41.239  1.00 31.42  ? 645  SER   A O   1 
ATOM   2778  C  CB  . SER   A  1 344 ? -17.609 17.208  -38.931  1.00 29.96  ? 645  SER   A CB  1 
ATOM   2779  O  OG  . SER   A  1 344 ? -17.290 18.361  -38.155  1.00 33.12  ? 645  SER   A OG  1 
ATOM   2780  N  N   . PHE   A  1 345 ? -19.328 14.745  -39.763  1.00 31.68  ? 646  PHE   A N   1 
ATOM   2781  C  CA  . PHE   A  1 345 ? -19.717 13.680  -40.671  1.00 29.34  ? 646  PHE   A CA  1 
ATOM   2782  C  C   . PHE   A  1 345 ? -21.194 13.789  -41.013  1.00 31.89  ? 646  PHE   A C   1 
ATOM   2783  O  O   . PHE   A  1 345 ? -21.581 13.733  -42.187  1.00 28.32  ? 646  PHE   A O   1 
ATOM   2784  C  CB  . PHE   A  1 345 ? -19.391 12.328  -40.044  1.00 24.23  ? 646  PHE   A CB  1 
ATOM   2785  C  CG  . PHE   A  1 345 ? -18.021 11.829  -40.373  1.00 26.00  ? 646  PHE   A CG  1 
ATOM   2786  C  CD1 . PHE   A  1 345 ? -16.891 12.483  -39.903  1.00 26.37  ? 646  PHE   A CD1 1 
ATOM   2787  C  CD2 . PHE   A  1 345 ? -17.864 10.699  -41.155  1.00 23.95  ? 646  PHE   A CD2 1 
ATOM   2788  C  CE1 . PHE   A  1 345 ? -15.614 12.005  -40.219  1.00 23.13  ? 646  PHE   A CE1 1 
ATOM   2789  C  CE2 . PHE   A  1 345 ? -16.609 10.211  -41.469  1.00 22.72  ? 646  PHE   A CE2 1 
ATOM   2790  C  CZ  . PHE   A  1 345 ? -15.478 10.855  -41.008  1.00 20.23  ? 646  PHE   A CZ  1 
ATOM   2791  N  N   . GLN   A  1 346 ? -22.029 13.997  -39.999  1.00 32.92  ? 647  GLN   A N   1 
ATOM   2792  C  CA  . GLN   A  1 346 ? -23.465 14.083  -40.231  1.00 32.79  ? 647  GLN   A CA  1 
ATOM   2793  C  C   . GLN   A  1 346 ? -23.818 15.286  -41.082  1.00 33.24  ? 647  GLN   A C   1 
ATOM   2794  O  O   . GLN   A  1 346 ? -24.726 15.219  -41.919  1.00 37.88  ? 647  GLN   A O   1 
ATOM   2795  C  CB  . GLN   A  1 346 ? -24.203 14.138  -38.898  1.00 29.82  ? 647  GLN   A CB  1 
ATOM   2796  C  CG  . GLN   A  1 346 ? -24.189 12.797  -38.171  1.00 35.51  ? 647  GLN   A CG  1 
ATOM   2797  C  CD  . GLN   A  1 346 ? -24.611 12.919  -36.717  1.00 35.08  ? 647  GLN   A CD  1 
ATOM   2798  O  OE1 . GLN   A  1 346 ? -24.765 14.020  -36.198  1.00 43.37  ? 647  GLN   A OE1 1 
ATOM   2799  N  NE2 . GLN   A  1 346 ? -24.795 11.784  -36.059  1.00 35.24  ? 647  GLN   A NE2 1 
ATOM   2800  N  N   . SER   A  1 347 ? -23.126 16.403  -40.871  1.00 30.04  ? 648  SER   A N   1 
ATOM   2801  C  CA  . SER   A  1 347 ? -23.428 17.597  -41.643  1.00 27.90  ? 648  SER   A CA  1 
ATOM   2802  C  C   . SER   A  1 347 ? -23.078 17.387  -43.103  1.00 34.59  ? 648  SER   A C   1 
ATOM   2803  O  O   . SER   A  1 347 ? -23.739 17.944  -43.987  1.00 37.85  ? 648  SER   A O   1 
ATOM   2804  C  CB  . SER   A  1 347 ? -22.679 18.804  -41.077  1.00 37.83  ? 648  SER   A CB  1 
ATOM   2805  O  OG  . SER   A  1 347 ? -23.109 19.101  -39.747  1.00 42.32  ? 648  SER   A OG  1 
ATOM   2806  N  N   . ASP   A  1 348 ? -22.058 16.576  -43.370  1.00 32.95  ? 649  ASP   A N   1 
ATOM   2807  C  CA  . ASP   A  1 348 ? -21.636 16.270  -44.725  1.00 28.90  ? 649  ASP   A CA  1 
ATOM   2808  C  C   . ASP   A  1 348 ? -22.309 15.031  -45.273  1.00 33.06  ? 649  ASP   A C   1 
ATOM   2809  O  O   . ASP   A  1 348 ? -21.954 14.581  -46.369  1.00 34.07  ? 649  ASP   A O   1 
ATOM   2810  C  CB  . ASP   A  1 348 ? -20.120 16.107  -44.774  1.00 34.26  ? 649  ASP   A CB  1 
ATOM   2811  C  CG  . ASP   A  1 348 ? -19.407 17.427  -44.733  1.00 37.15  ? 649  ASP   A CG  1 
ATOM   2812  O  OD1 . ASP   A  1 348 ? -20.102 18.465  -44.649  1.00 35.31  ? 649  ASP   A OD1 1 
ATOM   2813  O  OD2 . ASP   A  1 348 ? -18.162 17.433  -44.796  1.00 38.76  ? 649  ASP   A OD2 1 
ATOM   2814  N  N   . LYS   A  1 349 ? -23.275 14.476  -44.543  1.00 27.38  ? 650  LYS   A N   1 
ATOM   2815  C  CA  . LYS   A  1 349 ? -24.014 13.306  -45.003  1.00 30.97  ? 650  LYS   A CA  1 
ATOM   2816  C  C   . LYS   A  1 349 ? -23.057 12.163  -45.329  1.00 31.38  ? 650  LYS   A C   1 
ATOM   2817  O  O   . LYS   A  1 349 ? -23.167 11.500  -46.361  1.00 32.96  ? 650  LYS   A O   1 
ATOM   2818  C  CB  . LYS   A  1 349 ? -24.891 13.652  -46.208  1.00 36.31  ? 650  LYS   A CB  1 
ATOM   2819  C  CG  . LYS   A  1 349 ? -26.014 14.619  -45.880  1.00 48.13  ? 650  LYS   A CG  1 
ATOM   2820  C  CD  . LYS   A  1 349 ? -27.074 14.615  -46.972  1.00 59.36  ? 650  LYS   A CD  1 
ATOM   2821  C  CE  . LYS   A  1 349 ? -28.387 15.190  -46.471  1.00 70.48  ? 650  LYS   A CE  1 
ATOM   2822  N  NZ  . LYS   A  1 349 ? -28.281 16.647  -46.180  1.00 77.23  ? 650  LYS   A NZ  1 
ATOM   2823  N  N   . VAL   A  1 350 ? -22.093 11.948  -44.442  1.00 28.35  ? 651  VAL   A N   1 
ATOM   2824  C  CA  . VAL   A  1 350 ? -21.177 10.821  -44.530  1.00 27.36  ? 651  VAL   A CA  1 
ATOM   2825  C  C   . VAL   A  1 350 ? -21.535 9.852   -43.411  1.00 33.53  ? 651  VAL   A C   1 
ATOM   2826  O  O   . VAL   A  1 350 ? -21.638 10.250  -42.241  1.00 31.08  ? 651  VAL   A O   1 
ATOM   2827  C  CB  . VAL   A  1 350 ? -19.713 11.278  -44.434  1.00 25.92  ? 651  VAL   A CB  1 
ATOM   2828  C  CG1 . VAL   A  1 350 ? -18.787 10.073  -44.512  1.00 24.97  ? 651  VAL   A CG1 1 
ATOM   2829  C  CG2 . VAL   A  1 350 ? -19.402 12.274  -45.531  1.00 23.60  ? 651  VAL   A CG2 1 
ATOM   2830  N  N   . THR   A  1 351 ? -21.747 8.589   -43.772  1.00 29.82  ? 652  THR   A N   1 
ATOM   2831  C  CA  . THR   A  1 351 ? -22.184 7.608   -42.794  1.00 25.73  ? 652  THR   A CA  1 
ATOM   2832  C  C   . THR   A  1 351 ? -21.204 7.542   -41.639  1.00 27.83  ? 652  THR   A C   1 
ATOM   2833  O  O   . THR   A  1 351 ? -19.989 7.413   -41.834  1.00 26.97  ? 652  THR   A O   1 
ATOM   2834  C  CB  . THR   A  1 351 ? -22.324 6.232   -43.435  1.00 25.63  ? 652  THR   A CB  1 
ATOM   2835  O  OG1 . THR   A  1 351 ? -23.163 6.339   -44.586  1.00 31.03  ? 652  THR   A OG1 1 
ATOM   2836  C  CG2 . THR   A  1 351 ? -22.948 5.247   -42.426  1.00 21.47  ? 652  THR   A CG2 1 
ATOM   2837  N  N   . ILE   A  1 352 ? -21.747 7.664   -40.432  1.00 24.85  ? 653  ILE   A N   1 
ATOM   2838  C  CA  . ILE   A  1 352 ? -20.992 7.481   -39.205  1.00 19.91  ? 653  ILE   A CA  1 
ATOM   2839  C  C   . ILE   A  1 352 ? -21.992 7.041   -38.148  1.00 23.65  ? 653  ILE   A C   1 
ATOM   2840  O  O   . ILE   A  1 352 ? -23.188 7.335   -38.238  1.00 29.03  ? 653  ILE   A O   1 
ATOM   2841  C  CB  . ILE   A  1 352 ? -20.252 8.783   -38.809  1.00 21.70  ? 653  ILE   A CB  1 
ATOM   2842  C  CG1 . ILE   A  1 352 ? -19.151 8.510   -37.789  1.00 29.95  ? 653  ILE   A CG1 1 
ATOM   2843  C  CG2 . ILE   A  1 352 ? -21.217 9.766   -38.231  1.00 22.51  ? 653  ILE   A CG2 1 
ATOM   2844  C  CD1 . ILE   A  1 352 ? -18.166 9.663   -37.654  1.00 25.71  ? 653  ILE   A CD1 1 
ATOM   2845  N  N   . VAL   A  1 353 ? -21.514 6.315   -37.149  1.00 25.14  ? 654  VAL   A N   1 
ATOM   2846  C  CA  . VAL   A  1 353 ? -22.376 5.880   -36.060  1.00 27.46  ? 654  VAL   A CA  1 
ATOM   2847  C  C   . VAL   A  1 353 ? -21.739 6.317   -34.747  1.00 24.48  ? 654  VAL   A C   1 
ATOM   2848  O  O   . VAL   A  1 353 ? -20.517 6.239   -34.582  1.00 25.81  ? 654  VAL   A O   1 
ATOM   2849  C  CB  . VAL   A  1 353 ? -22.631 4.354   -36.102  1.00 23.94  ? 654  VAL   A CB  1 
ATOM   2850  C  CG1 . VAL   A  1 353 ? -21.335 3.577   -35.947  1.00 19.41  ? 654  VAL   A CG1 1 
ATOM   2851  C  CG2 . VAL   A  1 353 ? -23.634 3.934   -35.030  1.00 35.16  ? 654  VAL   A CG2 1 
ATOM   2852  N  N   . ASP   A  1 354 ? -22.552 6.821   -33.832  1.00 24.20  ? 655  ASP   A N   1 
ATOM   2853  C  CA  . ASP   A  1 354 ? -21.963 7.137   -32.539  1.00 26.98  ? 655  ASP   A CA  1 
ATOM   2854  C  C   . ASP   A  1 354 ? -21.865 5.867   -31.694  1.00 26.27  ? 655  ASP   A C   1 
ATOM   2855  O  O   . ASP   A  1 354 ? -22.561 4.879   -31.934  1.00 30.87  ? 655  ASP   A O   1 
ATOM   2856  C  CB  . ASP   A  1 354 ? -22.761 8.221   -31.801  1.00 31.13  ? 655  ASP   A CB  1 
ATOM   2857  C  CG  . ASP   A  1 354 ? -24.166 7.779   -31.426  1.00 39.46  ? 655  ASP   A CG  1 
ATOM   2858  O  OD1 . ASP   A  1 354 ? -25.137 8.338   -31.979  1.00 50.70  ? 655  ASP   A OD1 1 
ATOM   2859  O  OD2 . ASP   A  1 354 ? -24.310 6.870   -30.587  1.00 41.50  ? 655  ASP   A OD2 1 
ATOM   2860  N  N   . HIS   A  1 355 ? -20.994 5.909   -30.684  1.00 26.02  ? 656  HIS   A N   1 
ATOM   2861  C  CA  . HIS   A  1 355 ? -20.768 4.725   -29.853  1.00 26.23  ? 656  HIS   A CA  1 
ATOM   2862  C  C   . HIS   A  1 355 ? -22.014 4.301   -29.078  1.00 28.17  ? 656  HIS   A C   1 
ATOM   2863  O  O   . HIS   A  1 355 ? -22.170 3.111   -28.780  1.00 28.88  ? 656  HIS   A O   1 
ATOM   2864  C  CB  . HIS   A  1 355 ? -19.607 4.959   -28.895  1.00 24.72  ? 656  HIS   A CB  1 
ATOM   2865  C  CG  . HIS   A  1 355 ? -19.705 6.228   -28.111  1.00 26.90  ? 656  HIS   A CG  1 
ATOM   2866  N  ND1 . HIS   A  1 355 ? -19.448 7.465   -28.663  1.00 28.78  ? 656  HIS   A ND1 1 
ATOM   2867  C  CD2 . HIS   A  1 355 ? -19.989 6.448   -26.803  1.00 21.56  ? 656  HIS   A CD2 1 
ATOM   2868  C  CE1 . HIS   A  1 355 ? -19.597 8.396   -27.734  1.00 31.24  ? 656  HIS   A CE1 1 
ATOM   2869  N  NE2 . HIS   A  1 355 ? -19.925 7.805   -26.598  1.00 27.63  ? 656  HIS   A NE2 1 
ATOM   2870  N  N   . HIS   A  1 356 ? -22.924 5.229   -28.759  1.00 21.31  ? 657  HIS   A N   1 
ATOM   2871  C  CA  . HIS   A  1 356 ? -24.166 4.808   -28.116  1.00 24.28  ? 657  HIS   A CA  1 
ATOM   2872  C  C   . HIS   A  1 356 ? -25.015 3.956   -29.059  1.00 27.23  ? 657  HIS   A C   1 
ATOM   2873  O  O   . HIS   A  1 356 ? -25.463 2.861   -28.695  1.00 28.37  ? 657  HIS   A O   1 
ATOM   2874  C  CB  . HIS   A  1 356 ? -24.950 6.024   -27.634  1.00 23.56  ? 657  HIS   A CB  1 
ATOM   2875  C  CG  . HIS   A  1 356 ? -24.159 6.910   -26.736  1.00 30.94  ? 657  HIS   A CG  1 
ATOM   2876  N  ND1 . HIS   A  1 356 ? -23.819 6.547   -25.453  1.00 29.11  ? 657  HIS   A ND1 1 
ATOM   2877  C  CD2 . HIS   A  1 356 ? -23.596 8.121   -26.950  1.00 35.93  ? 657  HIS   A CD2 1 
ATOM   2878  C  CE1 . HIS   A  1 356 ? -23.101 7.510   -24.904  1.00 32.71  ? 657  HIS   A CE1 1 
ATOM   2879  N  NE2 . HIS   A  1 356 ? -22.952 8.476   -25.792  1.00 31.69  ? 657  HIS   A NE2 1 
ATOM   2880  N  N   . SER   A  1 357 ? -25.251 4.449   -30.274  1.00 25.68  ? 658  SER   A N   1 
ATOM   2881  C  CA  A SER   A  1 357 ? -26.042 3.694   -31.240  0.47 28.96  ? 658  SER   A CA  1 
ATOM   2882  C  CA  B SER   A  1 357 ? -26.047 3.686   -31.231  0.53 29.11  ? 658  SER   A CA  1 
ATOM   2883  C  C   . SER   A  1 357 ? -25.360 2.382   -31.615  1.00 26.65  ? 658  SER   A C   1 
ATOM   2884  O  O   . SER   A  1 357 ? -26.009 1.336   -31.709  1.00 24.95  ? 658  SER   A O   1 
ATOM   2885  C  CB  A SER   A  1 357 ? -26.284 4.549   -32.486  0.47 25.47  ? 658  SER   A CB  1 
ATOM   2886  C  CB  B SER   A  1 357 ? -26.327 4.533   -32.473  0.53 25.39  ? 658  SER   A CB  1 
ATOM   2887  O  OG  A SER   A  1 357 ? -27.009 3.834   -33.464  0.47 26.49  ? 658  SER   A OG  1 
ATOM   2888  O  OG  B SER   A  1 357 ? -27.008 5.718   -32.109  0.53 28.08  ? 658  SER   A OG  1 
ATOM   2889  N  N   . ALA   A  1 358 ? -24.051 2.420   -31.851  1.00 22.36  ? 659  ALA   A N   1 
ATOM   2890  C  CA  . ALA   A  1 358 ? -23.351 1.210   -32.268  1.00 21.36  ? 659  ALA   A CA  1 
ATOM   2891  C  C   . ALA   A  1 358 ? -23.412 0.139   -31.181  1.00 27.29  ? 659  ALA   A C   1 
ATOM   2892  O  O   . ALA   A  1 358 ? -23.723 -1.028  -31.454  1.00 22.79  ? 659  ALA   A O   1 
ATOM   2893  C  CB  . ALA   A  1 358 ? -21.900 1.543   -32.616  1.00 19.56  ? 659  ALA   A CB  1 
ATOM   2894  N  N   . THR   A  1 359 ? -23.121 0.515   -29.935  1.00 26.49  ? 660  THR   A N   1 
ATOM   2895  C  CA  . THR   A  1 359 ? -23.115 -0.497  -28.887  1.00 23.19  ? 660  THR   A CA  1 
ATOM   2896  C  C   . THR   A  1 359 ? -24.510 -1.046  -28.671  1.00 23.18  ? 660  THR   A C   1 
ATOM   2897  O  O   . THR   A  1 359 ? -24.675 -2.252  -28.460  1.00 23.67  ? 660  THR   A O   1 
ATOM   2898  C  CB  . THR   A  1 359 ? -22.535 0.057   -27.582  1.00 21.14  ? 660  THR   A CB  1 
ATOM   2899  O  OG1 . THR   A  1 359 ? -23.186 1.281   -27.238  1.00 26.37  ? 660  THR   A OG1 1 
ATOM   2900  C  CG2 . THR   A  1 359 ? -21.043 0.320   -27.755  1.00 18.88  ? 660  THR   A CG2 1 
ATOM   2901  N  N   . GLU   A  1 360 ? -25.530 -0.189  -28.753  1.00 20.02  ? 661  GLU   A N   1 
ATOM   2902  C  CA  . GLU   A  1 360 ? -26.896 -0.685  -28.650  1.00 24.44  ? 661  GLU   A CA  1 
ATOM   2903  C  C   . GLU   A  1 360 ? -27.188 -1.688  -29.765  1.00 29.52  ? 661  GLU   A C   1 
ATOM   2904  O  O   . GLU   A  1 360 ? -27.751 -2.761  -29.521  1.00 31.40  ? 661  GLU   A O   1 
ATOM   2905  C  CB  . GLU   A  1 360 ? -27.882 0.483   -28.694  1.00 35.66  ? 661  GLU   A CB  1 
ATOM   2906  C  CG  . GLU   A  1 360 ? -29.337 0.065   -28.564  1.00 47.15  ? 661  GLU   A CG  1 
ATOM   2907  C  CD  . GLU   A  1 360 ? -30.316 1.210   -28.816  1.00 67.76  ? 661  GLU   A CD  1 
ATOM   2908  O  OE1 . GLU   A  1 360 ? -29.945 2.191   -29.497  1.00 70.24  ? 661  GLU   A OE1 1 
ATOM   2909  O  OE2 . GLU   A  1 360 ? -31.465 1.128   -28.328  1.00 78.25  ? 661  GLU   A OE2 1 
ATOM   2910  N  N   . SER   A  1 361 ? -26.793 -1.359  -30.999  1.00 27.05  ? 662  SER   A N   1 
ATOM   2911  C  CA  . SER   A  1 361 ? -26.982 -2.297  -32.102  1.00 28.73  ? 662  SER   A CA  1 
ATOM   2912  C  C   . SER   A  1 361 ? -26.286 -3.615  -31.819  1.00 25.64  ? 662  SER   A C   1 
ATOM   2913  O  O   . SER   A  1 361 ? -26.819 -4.685  -32.132  1.00 26.96  ? 662  SER   A O   1 
ATOM   2914  C  CB  . SER   A  1 361 ? -26.469 -1.700  -33.418  1.00 31.37  ? 662  SER   A CB  1 
ATOM   2915  O  OG  . SER   A  1 361 ? -27.227 -0.555  -33.751  1.00 46.03  ? 662  SER   A OG  1 
ATOM   2916  N  N   . PHE   A  1 362 ? -25.103 -3.564  -31.206  1.00 27.68  ? 663  PHE   A N   1 
ATOM   2917  C  CA  . PHE   A  1 362 ? -24.371 -4.801  -30.976  1.00 29.69  ? 663  PHE   A CA  1 
ATOM   2918  C  C   . PHE   A  1 362 ? -25.082 -5.692  -29.962  1.00 29.99  ? 663  PHE   A C   1 
ATOM   2919  O  O   . PHE   A  1 362 ? -25.133 -6.913  -30.146  1.00 32.65  ? 663  PHE   A O   1 
ATOM   2920  C  CB  . PHE   A  1 362 ? -22.930 -4.522  -30.536  1.00 19.83  ? 663  PHE   A CB  1 
ATOM   2921  C  CG  . PHE   A  1 362 ? -22.117 -5.769  -30.405  1.00 24.72  ? 663  PHE   A CG  1 
ATOM   2922  C  CD1 . PHE   A  1 362 ? -21.699 -6.455  -31.540  1.00 25.56  ? 663  PHE   A CD1 1 
ATOM   2923  C  CD2 . PHE   A  1 362 ? -21.843 -6.310  -29.161  1.00 24.60  ? 663  PHE   A CD2 1 
ATOM   2924  C  CE1 . PHE   A  1 362 ? -20.982 -7.629  -31.436  1.00 28.91  ? 663  PHE   A CE1 1 
ATOM   2925  C  CE2 . PHE   A  1 362 ? -21.122 -7.484  -29.047  1.00 27.00  ? 663  PHE   A CE2 1 
ATOM   2926  C  CZ  . PHE   A  1 362 ? -20.685 -8.147  -30.184  1.00 30.73  ? 663  PHE   A CZ  1 
ATOM   2927  N  N   . ILE   A  1 363 ? -25.624 -5.111  -28.882  1.00 26.48  ? 664  ILE   A N   1 
ATOM   2928  C  CA  . ILE   A  1 363 ? -26.428 -5.890  -27.939  1.00 26.98  ? 664  ILE   A CA  1 
ATOM   2929  C  C   . ILE   A  1 363 ? -27.581 -6.561  -28.670  1.00 30.39  ? 664  ILE   A C   1 
ATOM   2930  O  O   . ILE   A  1 363 ? -27.895 -7.737  -28.440  1.00 27.51  ? 664  ILE   A O   1 
ATOM   2931  C  CB  . ILE   A  1 363 ? -26.956 -4.997  -26.796  1.00 27.78  ? 664  ILE   A CB  1 
ATOM   2932  C  CG1 . ILE   A  1 363 ? -25.817 -4.461  -25.930  1.00 25.47  ? 664  ILE   A CG1 1 
ATOM   2933  C  CG2 . ILE   A  1 363 ? -27.948 -5.764  -25.940  1.00 25.52  ? 664  ILE   A CG2 1 
ATOM   2934  C  CD1 . ILE   A  1 363 ? -25.039 -5.555  -25.214  1.00 26.43  ? 664  ILE   A CD1 1 
ATOM   2935  N  N   . LYS   A  1 364 ? -28.261 -5.798  -29.528  1.00 21.88  ? 665  LYS   A N   1 
ATOM   2936  C  CA  . LYS   A  1 364 ? -29.321 -6.372  -30.348  1.00 31.18  ? 665  LYS   A CA  1 
ATOM   2937  C  C   . LYS   A  1 364 ? -28.778 -7.499  -31.217  1.00 29.90  ? 665  LYS   A C   1 
ATOM   2938  O  O   . LYS   A  1 364 ? -29.393 -8.570  -31.327  1.00 28.59  ? 665  LYS   A O   1 
ATOM   2939  C  CB  . LYS   A  1 364 ? -29.953 -5.279  -31.211  1.00 28.73  ? 665  LYS   A CB  1 
ATOM   2940  C  CG  . LYS   A  1 364 ? -31.034 -5.777  -32.149  1.00 49.53  ? 665  LYS   A CG  1 
ATOM   2941  C  CD  . LYS   A  1 364 ? -32.422 -5.496  -31.597  1.00 62.64  ? 665  LYS   A CD  1 
ATOM   2942  C  CE  . LYS   A  1 364 ? -33.364 -6.668  -31.842  1.00 68.24  ? 665  LYS   A CE  1 
ATOM   2943  N  NZ  . LYS   A  1 364 ? -34.740 -6.375  -31.351  1.00 74.83  ? 665  LYS   A NZ  1 
ATOM   2944  N  N   . HIS   A  1 365 ? -27.613 -7.276  -31.824  1.00 24.45  ? 666  HIS   A N   1 
ATOM   2945  C  CA  . HIS   A  1 365 ? -26.984 -8.305  -32.641  1.00 24.37  ? 666  HIS   A CA  1 
ATOM   2946  C  C   . HIS   A  1 365 ? -26.646 -9.529  -31.807  1.00 31.16  ? 666  HIS   A C   1 
ATOM   2947  O  O   . HIS   A  1 365 ? -26.893 -10.663 -32.234  1.00 28.92  ? 666  HIS   A O   1 
ATOM   2948  C  CB  . HIS   A  1 365 ? -25.730 -7.747  -33.315  1.00 23.74  ? 666  HIS   A CB  1 
ATOM   2949  C  CG  . HIS   A  1 365 ? -24.950 -8.776  -34.067  1.00 22.20  ? 666  HIS   A CG  1 
ATOM   2950  N  ND1 . HIS   A  1 365 ? -25.475 -9.466  -35.135  1.00 22.47  ? 666  HIS   A ND1 1 
ATOM   2951  C  CD2 . HIS   A  1 365 ? -23.703 -9.265  -33.880  1.00 22.14  ? 666  HIS   A CD2 1 
ATOM   2952  C  CE1 . HIS   A  1 365 ? -24.577 -10.320 -35.591  1.00 29.69  ? 666  HIS   A CE1 1 
ATOM   2953  N  NE2 . HIS   A  1 365 ? -23.492 -10.219 -34.847  1.00 23.18  ? 666  HIS   A NE2 1 
ATOM   2954  N  N   . MET   A  1 366 ? -26.108 -9.323  -30.598  1.00 28.66  ? 667  MET   A N   1 
ATOM   2955  C  CA  . MET   A  1 366 ? -25.804 -10.458 -29.732  1.00 28.35  ? 667  MET   A CA  1 
ATOM   2956  C  C   . MET   A  1 366 ? -27.039 -11.296 -29.493  1.00 19.70  ? 667  MET   A C   1 
ATOM   2957  O  O   . MET   A  1 366 ? -27.007 -12.521 -29.622  1.00 22.96  ? 667  MET   A O   1 
ATOM   2958  C  CB  . MET   A  1 366 ? -25.240 -9.989  -28.393  1.00 27.44  ? 667  MET   A CB  1 
ATOM   2959  C  CG  . MET   A  1 366 ? -23.757 -9.826  -28.399  1.00 30.48  ? 667  MET   A CG  1 
ATOM   2960  S  SD  . MET   A  1 366 ? -23.150 -9.509  -26.742  1.00 34.10  ? 667  MET   A SD  1 
ATOM   2961  C  CE  . MET   A  1 366 ? -23.173 -11.123 -25.971  1.00 32.41  ? 667  MET   A CE  1 
ATOM   2962  N  N   . GLU   A  1 367 ? -28.147 -10.645 -29.142  1.00 21.46  ? 668  GLU   A N   1 
ATOM   2963  C  CA  . GLU   A  1 367 ? -29.361 -11.390 -28.854  1.00 30.68  ? 668  GLU   A CA  1 
ATOM   2964  C  C   . GLU   A  1 367 ? -29.841 -12.151 -30.077  1.00 26.90  ? 668  GLU   A C   1 
ATOM   2965  O  O   . GLU   A  1 367 ? -30.247 -13.316 -29.970  1.00 32.34  ? 668  GLU   A O   1 
ATOM   2966  C  CB  . GLU   A  1 367 ? -30.438 -10.442 -28.344  1.00 38.77  ? 668  GLU   A CB  1 
ATOM   2967  C  CG  . GLU   A  1 367 ? -30.050 -9.767  -27.043  1.00 53.86  ? 668  GLU   A CG  1 
ATOM   2968  C  CD  . GLU   A  1 367 ? -31.074 -8.749  -26.602  1.00 69.16  ? 668  GLU   A CD  1 
ATOM   2969  O  OE1 . GLU   A  1 367 ? -32.073 -8.561  -27.336  1.00 76.08  ? 668  GLU   A OE1 1 
ATOM   2970  O  OE2 . GLU   A  1 367 ? -30.875 -8.143  -25.527  1.00 71.37  ? 668  GLU   A OE2 1 
ATOM   2971  N  N   . ASN   A  1 368 ? -29.815 -11.509 -31.247  1.00 28.30  ? 669  ASN   A N   1 
ATOM   2972  C  CA  . ASN   A  1 368 ? -30.168 -12.201 -32.487  1.00 28.87  ? 669  ASN   A CA  1 
ATOM   2973  C  C   . ASN   A  1 368 ? -29.317 -13.444 -32.675  1.00 28.55  ? 669  ASN   A C   1 
ATOM   2974  O  O   . ASN   A  1 368 ? -29.827 -14.534 -32.966  1.00 28.12  ? 669  ASN   A O   1 
ATOM   2975  C  CB  . ASN   A  1 368 ? -29.978 -11.272 -33.679  1.00 25.62  ? 669  ASN   A CB  1 
ATOM   2976  C  CG  . ASN   A  1 368 ? -30.965 -10.124 -33.704  1.00 34.39  ? 669  ASN   A CG  1 
ATOM   2977  O  OD1 . ASN   A  1 368 ? -32.017 -10.164 -33.063  1.00 37.72  ? 669  ASN   A OD1 1 
ATOM   2978  N  ND2 . ASN   A  1 368 ? -30.632 -9.090  -34.473  1.00 34.58  ? 669  ASN   A ND2 1 
ATOM   2979  N  N   . GLU   A  1 369 ? -28.008 -13.292 -32.505  1.00 26.47  ? 670  GLU   A N   1 
ATOM   2980  C  CA  . GLU   A  1 369 ? -27.093 -14.405 -32.706  1.00 23.46  ? 670  GLU   A CA  1 
ATOM   2981  C  C   . GLU   A  1 369 ? -27.313 -15.509 -31.679  1.00 26.66  ? 670  GLU   A C   1 
ATOM   2982  O  O   . GLU   A  1 369 ? -27.293 -16.693 -32.033  1.00 31.89  ? 670  GLU   A O   1 
ATOM   2983  C  CB  . GLU   A  1 369 ? -25.653 -13.895 -32.667  1.00 22.94  ? 670  GLU   A CB  1 
ATOM   2984  C  CG  . GLU   A  1 369 ? -25.339 -12.973 -33.831  1.00 24.11  ? 670  GLU   A CG  1 
ATOM   2985  C  CD  . GLU   A  1 369 ? -25.216 -13.716 -35.169  1.00 29.61  ? 670  GLU   A CD  1 
ATOM   2986  O  OE1 . GLU   A  1 369 ? -24.072 -13.968 -35.606  1.00 23.97  ? 670  GLU   A OE1 1 
ATOM   2987  O  OE2 . GLU   A  1 369 ? -26.254 -14.057 -35.775  1.00 28.95  ? 670  GLU   A OE2 1 
ATOM   2988  N  N   . TYR   A  1 370 ? -27.531 -15.158 -30.403  1.00 25.19  ? 671  TYR   A N   1 
ATOM   2989  C  CA  . TYR   A  1 370 ? -27.806 -16.216 -29.436  1.00 26.33  ? 671  TYR   A CA  1 
ATOM   2990  C  C   . TYR   A  1 370 ? -29.102 -16.926 -29.788  1.00 31.95  ? 671  TYR   A C   1 
ATOM   2991  O  O   . TYR   A  1 370 ? -29.198 -18.154 -29.676  1.00 30.00  ? 671  TYR   A O   1 
ATOM   2992  C  CB  . TYR   A  1 370 ? -27.841 -15.663 -28.000  1.00 22.16  ? 671  TYR   A CB  1 
ATOM   2993  C  CG  . TYR   A  1 370 ? -26.452 -15.640 -27.407  1.00 29.17  ? 671  TYR   A CG  1 
ATOM   2994  C  CD1 . TYR   A  1 370 ? -25.589 -14.584 -27.663  1.00 25.76  ? 671  TYR   A CD1 1 
ATOM   2995  C  CD2 . TYR   A  1 370 ? -25.985 -16.710 -26.640  1.00 32.06  ? 671  TYR   A CD2 1 
ATOM   2996  C  CE1 . TYR   A  1 370 ? -24.301 -14.570 -27.162  1.00 26.55  ? 671  TYR   A CE1 1 
ATOM   2997  C  CE2 . TYR   A  1 370 ? -24.709 -16.713 -26.135  1.00 30.08  ? 671  TYR   A CE2 1 
ATOM   2998  C  CZ  . TYR   A  1 370 ? -23.868 -15.645 -26.396  1.00 31.03  ? 671  TYR   A CZ  1 
ATOM   2999  O  OH  . TYR   A  1 370 ? -22.591 -15.648 -25.895  1.00 35.34  ? 671  TYR   A OH  1 
ATOM   3000  N  N   . ARG   A  1 371 ? -30.096 -16.177 -30.265  1.00 31.91  ? 672  ARG   A N   1 
ATOM   3001  C  CA  . ARG   A  1 371 ? -31.377 -16.795 -30.592  1.00 35.94  ? 672  ARG   A CA  1 
ATOM   3002  C  C   . ARG   A  1 371 ? -31.269 -17.706 -31.815  1.00 38.16  ? 672  ARG   A C   1 
ATOM   3003  O  O   . ARG   A  1 371 ? -31.729 -18.850 -31.786  1.00 37.13  ? 672  ARG   A O   1 
ATOM   3004  C  CB  . ARG   A  1 371 ? -32.447 -15.728 -30.817  1.00 41.11  ? 672  ARG   A CB  1 
ATOM   3005  C  CG  . ARG   A  1 371 ? -33.781 -16.316 -31.246  1.00 58.71  ? 672  ARG   A CG  1 
ATOM   3006  C  CD  . ARG   A  1 371 ? -34.791 -15.245 -31.615  1.00 74.15  ? 672  ARG   A CD  1 
ATOM   3007  N  NE  . ARG   A  1 371 ? -34.693 -14.074 -30.745  1.00 84.99  ? 672  ARG   A NE  1 
ATOM   3008  C  CZ  . ARG   A  1 371 ? -34.433 -12.842 -31.178  1.00 87.18  ? 672  ARG   A CZ  1 
ATOM   3009  N  NH1 . ARG   A  1 371 ? -34.258 -12.617 -32.478  1.00 84.38  ? 672  ARG   A NH1 1 
ATOM   3010  N  NH2 . ARG   A  1 371 ? -34.359 -11.834 -30.315  1.00 83.89  ? 672  ARG   A NH2 1 
ATOM   3011  N  N   . CYS   A  1 372 ? -30.662 -17.233 -32.903  1.00 32.19  ? 673  CYS   A N   1 
ATOM   3012  C  CA  A CYS   A  1 372 ? -30.632 -18.054 -34.105  0.57 36.51  ? 673  CYS   A CA  1 
ATOM   3013  C  CA  B CYS   A  1 372 ? -30.631 -18.048 -34.109  0.43 36.54  ? 673  CYS   A CA  1 
ATOM   3014  C  C   . CYS   A  1 372 ? -29.411 -18.957 -34.183  1.00 38.97  ? 673  CYS   A C   1 
ATOM   3015  O  O   . CYS   A  1 372 ? -29.503 -20.052 -34.739  1.00 46.49  ? 673  CYS   A O   1 
ATOM   3016  C  CB  A CYS   A  1 372 ? -30.682 -17.179 -35.360  0.57 36.74  ? 673  CYS   A CB  1 
ATOM   3017  C  CB  B CYS   A  1 372 ? -30.701 -17.152 -35.353  0.43 36.89  ? 673  CYS   A CB  1 
ATOM   3018  S  SG  A CYS   A  1 372 ? -29.115 -16.422 -35.758  0.57 32.91  ? 673  CYS   A SG  1 
ATOM   3019  S  SG  B CYS   A  1 372 ? -32.269 -16.227 -35.511  0.43 44.41  ? 673  CYS   A SG  1 
ATOM   3020  N  N   . ARG   A  1 373 ? -28.276 -18.544 -33.627  1.00 31.35  ? 674  ARG   A N   1 
ATOM   3021  C  CA  . ARG   A  1 373 ? -27.027 -19.267 -33.829  1.00 29.90  ? 674  ARG   A CA  1 
ATOM   3022  C  C   . ARG   A  1 373 ? -26.518 -19.966 -32.579  1.00 33.91  ? 674  ARG   A C   1 
ATOM   3023  O  O   . ARG   A  1 373 ? -25.617 -20.805 -32.684  1.00 29.35  ? 674  ARG   A O   1 
ATOM   3024  C  CB  . ARG   A  1 373 ? -25.948 -18.295 -34.344  1.00 32.12  ? 674  ARG   A CB  1 
ATOM   3025  C  CG  . ARG   A  1 373 ? -24.892 -18.900 -35.249  1.00 33.93  ? 674  ARG   A CG  1 
ATOM   3026  C  CD  . ARG   A  1 373 ? -23.755 -17.913 -35.516  1.00 26.65  ? 674  ARG   A CD  1 
ATOM   3027  N  NE  . ARG   A  1 373 ? -22.751 -18.513 -36.385  1.00 27.06  ? 674  ARG   A NE  1 
ATOM   3028  C  CZ  . ARG   A  1 373 ? -21.554 -17.995 -36.623  1.00 35.08  ? 674  ARG   A CZ  1 
ATOM   3029  N  NH1 . ARG   A  1 373 ? -21.204 -16.849 -36.060  1.00 25.54  ? 674  ARG   A NH1 1 
ATOM   3030  N  NH2 . ARG   A  1 373 ? -20.708 -18.624 -37.428  1.00 32.36  ? 674  ARG   A NH2 1 
ATOM   3031  N  N   . GLY   A  1 374 ? -27.054 -19.642 -31.405  1.00 31.43  ? 675  GLY   A N   1 
ATOM   3032  C  CA  . GLY   A  1 374 ? -26.560 -20.234 -30.183  1.00 28.27  ? 675  GLY   A CA  1 
ATOM   3033  C  C   . GLY   A  1 374 ? -25.321 -19.578 -29.620  1.00 33.07  ? 675  GLY   A C   1 
ATOM   3034  O  O   . GLY   A  1 374 ? -24.644 -20.187 -28.781  1.00 30.42  ? 675  GLY   A O   1 
ATOM   3035  N  N   . GLY   A  1 375 ? -24.999 -18.366 -30.049  1.00 26.31  ? 676  GLY   A N   1 
ATOM   3036  C  CA  . GLY   A  1 375 ? -23.833 -17.692 -29.523  1.00 27.76  ? 676  GLY   A CA  1 
ATOM   3037  C  C   . GLY   A  1 375 ? -23.342 -16.606 -30.448  1.00 35.56  ? 676  GLY   A C   1 
ATOM   3038  O  O   . GLY   A  1 375 ? -23.736 -16.492 -31.609  1.00 32.26  ? 676  GLY   A O   1 
ATOM   3039  N  N   . CYS   A  1 376 ? -22.466 -15.798 -29.895  1.00 30.01  ? 677  CYS   A N   1 
ATOM   3040  C  CA  . CYS   A  1 376 ? -21.850 -14.701 -30.633  1.00 29.60  ? 677  CYS   A CA  1 
ATOM   3041  C  C   . CYS   A  1 376 ? -20.519 -14.431 -29.959  1.00 30.09  ? 677  CYS   A C   1 
ATOM   3042  O  O   . CYS   A  1 376 ? -20.481 -13.869 -28.856  1.00 27.74  ? 677  CYS   A O   1 
ATOM   3043  C  CB  . CYS   A  1 376 ? -22.732 -13.459 -30.635  1.00 25.91  ? 677  CYS   A CB  1 
ATOM   3044  S  SG  . CYS   A  1 376 ? -22.000 -12.084 -31.516  1.00 28.87  ? 677  CYS   A SG  1 
ATOM   3045  N  N   . PRO   A  1 377 ? -19.410 -14.878 -30.547  1.00 22.36  ? 678  PRO   A N   1 
ATOM   3046  C  CA  . PRO   A  1 377 ? -18.103 -14.572 -29.955  1.00 24.09  ? 678  PRO   A CA  1 
ATOM   3047  C  C   . PRO   A  1 377 ? -17.903 -13.065 -29.924  1.00 25.60  ? 678  PRO   A C   1 
ATOM   3048  O  O   . PRO   A  1 377 ? -18.198 -12.363 -30.895  1.00 21.50  ? 678  PRO   A O   1 
ATOM   3049  C  CB  . PRO   A  1 377 ? -17.116 -15.266 -30.896  1.00 27.72  ? 678  PRO   A CB  1 
ATOM   3050  C  CG  . PRO   A  1 377 ? -17.845 -15.255 -32.261  1.00 22.51  ? 678  PRO   A CG  1 
ATOM   3051  C  CD  . PRO   A  1 377 ? -19.311 -15.380 -31.932  1.00 20.35  ? 678  PRO   A CD  1 
ATOM   3052  N  N   . ALA   A  1 378 ? -17.456 -12.558 -28.777  1.00 26.29  ? 679  ALA   A N   1 
ATOM   3053  C  CA  . ALA   A  1 378 ? -17.319 -11.118 -28.622  1.00 22.27  ? 679  ALA   A CA  1 
ATOM   3054  C  C   . ALA   A  1 378 ? -16.197 -10.814 -27.647  1.00 19.90  ? 679  ALA   A C   1 
ATOM   3055  O  O   . ALA   A  1 378 ? -16.102 -11.424 -26.578  1.00 20.88  ? 679  ALA   A O   1 
ATOM   3056  C  CB  . ALA   A  1 378 ? -18.630 -10.483 -28.146  1.00 23.65  ? 679  ALA   A CB  1 
ATOM   3057  N  N   . ASP   A  1 379 ? -15.376 -9.849  -28.028  1.00 21.36  ? 680  ASP   A N   1 
ATOM   3058  C  CA  . ASP   A  1 379 ? -14.162 -9.487  -27.317  1.00 22.05  ? 680  ASP   A CA  1 
ATOM   3059  C  C   . ASP   A  1 379 ? -14.459 -8.180  -26.585  1.00 22.36  ? 680  ASP   A C   1 
ATOM   3060  O  O   . ASP   A  1 379 ? -14.321 -7.095  -27.151  1.00 19.35  ? 680  ASP   A O   1 
ATOM   3061  C  CB  . ASP   A  1 379 ? -13.006 -9.364  -28.304  1.00 23.10  ? 680  ASP   A CB  1 
ATOM   3062  C  CG  . ASP   A  1 379 ? -11.695 -9.034  -27.635  1.00 29.21  ? 680  ASP   A CG  1 
ATOM   3063  O  OD1 . ASP   A  1 379 ? -10.635 -9.321  -28.235  1.00 27.41  ? 680  ASP   A OD1 1 
ATOM   3064  O  OD2 . ASP   A  1 379 ? -11.714 -8.504  -26.505  1.00 28.50  ? 680  ASP   A OD2 1 
ATOM   3065  N  N   . TRP   A  1 380 ? -14.852 -8.298  -25.311  1.00 22.78  ? 681  TRP   A N   1 
ATOM   3066  C  CA  . TRP   A  1 380 ? -15.256 -7.139  -24.508  1.00 22.90  ? 681  TRP   A CA  1 
ATOM   3067  C  C   . TRP   A  1 380 ? -14.230 -6.023  -24.582  1.00 19.92  ? 681  TRP   A C   1 
ATOM   3068  O  O   . TRP   A  1 380 ? -14.579 -4.843  -24.707  1.00 18.79  ? 681  TRP   A O   1 
ATOM   3069  C  CB  . TRP   A  1 380 ? -15.437 -7.592  -23.061  1.00 20.82  ? 681  TRP   A CB  1 
ATOM   3070  C  CG  . TRP   A  1 380 ? -16.187 -6.659  -22.150  1.00 22.86  ? 681  TRP   A CG  1 
ATOM   3071  C  CD1 . TRP   A  1 380 ? -17.514 -6.727  -21.813  1.00 23.74  ? 681  TRP   A CD1 1 
ATOM   3072  C  CD2 . TRP   A  1 380 ? -15.643 -5.562  -21.421  1.00 18.84  ? 681  TRP   A CD2 1 
ATOM   3073  N  NE1 . TRP   A  1 380 ? -17.827 -5.729  -20.921  1.00 22.90  ? 681  TRP   A NE1 1 
ATOM   3074  C  CE2 . TRP   A  1 380 ? -16.697 -4.989  -20.679  1.00 23.37  ? 681  TRP   A CE2 1 
ATOM   3075  C  CE3 . TRP   A  1 380 ? -14.373 -4.983  -21.350  1.00 18.36  ? 681  TRP   A CE3 1 
ATOM   3076  C  CZ2 . TRP   A  1 380 ? -16.516 -3.873  -19.868  1.00 22.34  ? 681  TRP   A CZ2 1 
ATOM   3077  C  CZ3 . TRP   A  1 380 ? -14.197 -3.877  -20.525  1.00 22.49  ? 681  TRP   A CZ3 1 
ATOM   3078  C  CH2 . TRP   A  1 380 ? -15.262 -3.336  -19.801  1.00 19.93  ? 681  TRP   A CH2 1 
ATOM   3079  N  N   . VAL   A  1 381 ? -12.951 -6.386  -24.517  1.00 15.89  ? 682  VAL   A N   1 
ATOM   3080  C  CA  . VAL   A  1 381 ? -11.879 -5.401  -24.532  1.00 21.97  ? 682  VAL   A CA  1 
ATOM   3081  C  C   . VAL   A  1 381 ? -11.948 -4.516  -25.767  1.00 27.08  ? 682  VAL   A C   1 
ATOM   3082  O  O   . VAL   A  1 381 ? -11.627 -3.323  -25.701  1.00 23.34  ? 682  VAL   A O   1 
ATOM   3083  C  CB  . VAL   A  1 381 ? -10.532 -6.136  -24.436  1.00 17.95  ? 682  VAL   A CB  1 
ATOM   3084  C  CG1 . VAL   A  1 381 ? -9.395  -5.173  -24.609  1.00 18.35  ? 682  VAL   A CG1 1 
ATOM   3085  C  CG2 . VAL   A  1 381 ? -10.431 -6.861  -23.066  1.00 16.64  ? 682  VAL   A CG2 1 
ATOM   3086  N  N   . TRP   A  1 382 ? -12.369 -5.077  -26.912  1.00 21.43  ? 683  TRP   A N   1 
ATOM   3087  C  CA  . TRP   A  1 382 ? -12.457 -4.322  -28.153  1.00 22.15  ? 683  TRP   A CA  1 
ATOM   3088  C  C   . TRP   A  1 382 ? -13.834 -3.723  -28.383  1.00 21.18  ? 683  TRP   A C   1 
ATOM   3089  O  O   . TRP   A  1 382 ? -13.947 -2.669  -29.019  1.00 21.87  ? 683  TRP   A O   1 
ATOM   3090  C  CB  . TRP   A  1 382 ? -12.089 -5.222  -29.335  1.00 20.66  ? 683  TRP   A CB  1 
ATOM   3091  C  CG  . TRP   A  1 382 ? -10.619 -5.229  -29.586  1.00 18.51  ? 683  TRP   A CG  1 
ATOM   3092  C  CD1 . TRP   A  1 382 ? -9.641  -5.698  -28.751  1.00 23.54  ? 683  TRP   A CD1 1 
ATOM   3093  C  CD2 . TRP   A  1 382 ? -9.952  -4.703  -30.733  1.00 21.92  ? 683  TRP   A CD2 1 
ATOM   3094  N  NE1 . TRP   A  1 382 ? -8.404  -5.506  -29.322  1.00 21.04  ? 683  TRP   A NE1 1 
ATOM   3095  C  CE2 . TRP   A  1 382 ? -8.567  -4.896  -30.539  1.00 24.76  ? 683  TRP   A CE2 1 
ATOM   3096  C  CE3 . TRP   A  1 382 ? -10.391 -4.103  -31.917  1.00 27.35  ? 683  TRP   A CE3 1 
ATOM   3097  C  CZ2 . TRP   A  1 382 ? -7.618  -4.510  -31.486  1.00 23.74  ? 683  TRP   A CZ2 1 
ATOM   3098  C  CZ3 . TRP   A  1 382 ? -9.445  -3.716  -32.856  1.00 24.63  ? 683  TRP   A CZ3 1 
ATOM   3099  C  CH2 . TRP   A  1 382 ? -8.074  -3.923  -32.630  1.00 26.14  ? 683  TRP   A CH2 1 
ATOM   3100  N  N   . ILE   A  1 383 ? -14.881 -4.385  -27.894  1.00 17.51  ? 684  ILE   A N   1 
ATOM   3101  C  CA  . ILE   A  1 383 ? -16.237 -3.943  -28.174  1.00 16.85  ? 684  ILE   A CA  1 
ATOM   3102  C  C   . ILE   A  1 383 ? -16.571 -2.692  -27.370  1.00 23.88  ? 684  ILE   A C   1 
ATOM   3103  O  O   . ILE   A  1 383 ? -17.260 -1.790  -27.865  1.00 23.03  ? 684  ILE   A O   1 
ATOM   3104  C  CB  . ILE   A  1 383 ? -17.224 -5.088  -27.879  1.00 20.03  ? 684  ILE   A CB  1 
ATOM   3105  C  CG1 . ILE   A  1 383 ? -17.021 -6.249  -28.861  1.00 23.57  ? 684  ILE   A CG1 1 
ATOM   3106  C  CG2 . ILE   A  1 383 ? -18.666 -4.580  -27.934  1.00 16.41  ? 684  ILE   A CG2 1 
ATOM   3107  C  CD1 . ILE   A  1 383 ? -17.253 -5.869  -30.300  1.00 24.22  ? 684  ILE   A CD1 1 
ATOM   3108  N  N   . VAL   A  1 384 ? -16.129 -2.637  -26.116  1.00 18.52  ? 685  VAL   A N   1 
ATOM   3109  C  CA  . VAL   A  1 384 ? -16.446 -1.479  -25.276  1.00 18.50  ? 685  VAL   A CA  1 
ATOM   3110  C  C   . VAL   A  1 384 ? -15.746 -0.254  -25.844  1.00 21.32  ? 685  VAL   A C   1 
ATOM   3111  O  O   . VAL   A  1 384 ? -14.521 -0.287  -26.050  1.00 26.06  ? 685  VAL   A O   1 
ATOM   3112  C  CB  . VAL   A  1 384 ? -16.021 -1.729  -23.822  1.00 21.18  ? 685  VAL   A CB  1 
ATOM   3113  C  CG1 . VAL   A  1 384 ? -16.213 -0.459  -22.997  1.00 17.77  ? 685  VAL   A CG1 1 
ATOM   3114  C  CG2 . VAL   A  1 384 ? -16.818 -2.864  -23.237  1.00 19.79  ? 685  VAL   A CG2 1 
ATOM   3115  N  N   . PRO   A  1 385 ? -16.464 0.837   -26.093  1.00 20.55  ? 686  PRO   A N   1 
ATOM   3116  C  CA  . PRO   A  1 385 ? -15.844 1.984   -26.734  1.00 19.17  ? 686  PRO   A CA  1 
ATOM   3117  C  C   . PRO   A  1 385 ? -14.760 2.578   -25.851  1.00 22.57  ? 686  PRO   A C   1 
ATOM   3118  O  O   . PRO   A  1 385 ? -14.800 2.443   -24.613  1.00 22.87  ? 686  PRO   A O   1 
ATOM   3119  C  CB  . PRO   A  1 385 ? -17.013 2.958   -26.919  1.00 26.73  ? 686  PRO   A CB  1 
ATOM   3120  C  CG  . PRO   A  1 385 ? -18.191 2.077   -27.013  1.00 26.16  ? 686  PRO   A CG  1 
ATOM   3121  C  CD  . PRO   A  1 385 ? -17.931 0.955   -26.052  1.00 21.27  ? 686  PRO   A CD  1 
ATOM   3122  N  N   . PRO   A  1 386 ? -13.777 3.246   -26.452  1.00 27.35  ? 687  PRO   A N   1 
ATOM   3123  C  CA  . PRO   A  1 386 ? -12.659 3.789   -25.675  1.00 21.09  ? 687  PRO   A CA  1 
ATOM   3124  C  C   . PRO   A  1 386 ? -12.978 5.069   -24.921  1.00 23.90  ? 687  PRO   A C   1 
ATOM   3125  O  O   . PRO   A  1 386 ? -12.071 5.641   -24.297  1.00 26.65  ? 687  PRO   A O   1 
ATOM   3126  C  CB  . PRO   A  1 386 ? -11.609 4.039   -26.753  1.00 24.79  ? 687  PRO   A CB  1 
ATOM   3127  C  CG  . PRO   A  1 386 ? -12.442 4.449   -27.938  1.00 21.83  ? 687  PRO   A CG  1 
ATOM   3128  C  CD  . PRO   A  1 386 ? -13.639 3.533   -27.893  1.00 21.01  ? 687  PRO   A CD  1 
ATOM   3129  N  N   . MET   A  1 387 ? -14.221 5.547   -24.958  1.00 22.11  ? 688  MET   A N   1 
ATOM   3130  C  CA  . MET   A  1 387 ? -14.662 6.599   -24.046  1.00 24.42  ? 688  MET   A CA  1 
ATOM   3131  C  C   . MET   A  1 387 ? -16.037 6.226   -23.509  1.00 31.53  ? 688  MET   A C   1 
ATOM   3132  O  O   . MET   A  1 387 ? -16.774 5.455   -24.136  1.00 26.08  ? 688  MET   A O   1 
ATOM   3133  C  CB  . MET   A  1 387 ? -14.722 7.983   -24.710  1.00 27.52  ? 688  MET   A CB  1 
ATOM   3134  C  CG  . MET   A  1 387 ? -15.893 8.155   -25.653  1.00 34.65  ? 688  MET   A CG  1 
ATOM   3135  S  SD  . MET   A  1 387 ? -15.968 9.781   -26.464  1.00 37.04  ? 688  MET   A SD  1 
ATOM   3136  C  CE  . MET   A  1 387 ? -16.638 10.773  -25.137  1.00 31.87  ? 688  MET   A CE  1 
ATOM   3137  N  N   . SER   A  1 388 ? -16.354 6.748   -22.318  1.00 28.66  ? 689  SER   A N   1 
ATOM   3138  C  CA  . SER   A  1 388 ? -17.688 6.616   -21.732  1.00 27.17  ? 689  SER   A CA  1 
ATOM   3139  C  C   . SER   A  1 388 ? -18.145 5.163   -21.649  1.00 25.35  ? 689  SER   A C   1 
ATOM   3140  O  O   . SER   A  1 388 ? -19.328 4.862   -21.813  1.00 28.93  ? 689  SER   A O   1 
ATOM   3141  C  CB  . SER   A  1 388 ? -18.693 7.438   -22.526  1.00 35.04  ? 689  SER   A CB  1 
ATOM   3142  O  OG  . SER   A  1 388 ? -18.203 8.748   -22.647  1.00 38.92  ? 689  SER   A OG  1 
ATOM   3143  N  N   . GLY   A  1 389 ? -17.208 4.255   -21.393  1.00 23.99  ? 690  GLY   A N   1 
ATOM   3144  C  CA  . GLY   A  1 389 ? -17.494 2.836   -21.436  1.00 23.03  ? 690  GLY   A CA  1 
ATOM   3145  C  C   . GLY   A  1 389 ? -18.786 2.419   -20.765  1.00 25.78  ? 690  GLY   A C   1 
ATOM   3146  O  O   . GLY   A  1 389 ? -19.687 1.875   -21.413  1.00 24.96  ? 690  GLY   A O   1 
ATOM   3147  N  N   . SER   A  1 390 ? -18.917 2.709   -19.474  1.00 22.27  ? 691  SER   A N   1 
ATOM   3148  C  CA  . SER   A  1 390 ? -20.030 2.130   -18.741  1.00 21.34  ? 691  SER   A CA  1 
ATOM   3149  C  C   . SER   A  1 390 ? -21.355 2.823   -19.014  1.00 21.63  ? 691  SER   A C   1 
ATOM   3150  O  O   . SER   A  1 390 ? -22.389 2.362   -18.524  1.00 25.12  ? 691  SER   A O   1 
ATOM   3151  C  CB  . SER   A  1 390 ? -19.744 2.125   -17.230  1.00 27.13  ? 691  SER   A CB  1 
ATOM   3152  O  OG  . SER   A  1 390 ? -19.800 3.424   -16.718  1.00 27.23  ? 691  SER   A OG  1 
ATOM   3153  N  N   . ILE   A  1 391 ? -21.395 3.904   -19.791  1.00 26.18  ? 692  ILE   A N   1 
ATOM   3154  C  CA  . ILE   A  1 391 ? -22.713 4.411   -20.141  1.00 29.20  ? 692  ILE   A CA  1 
ATOM   3155  C  C   . ILE   A  1 391 ? -23.176 3.826   -21.459  1.00 30.75  ? 692  ILE   A C   1 
ATOM   3156  O  O   . ILE   A  1 391 ? -24.285 4.134   -21.909  1.00 35.44  ? 692  ILE   A O   1 
ATOM   3157  C  CB  . ILE   A  1 391 ? -22.779 5.954   -20.115  1.00 31.59  ? 692  ILE   A CB  1 
ATOM   3158  C  CG1 . ILE   A  1 391 ? -21.794 6.563   -21.091  1.00 35.22  ? 692  ILE   A CG1 1 
ATOM   3159  C  CG2 . ILE   A  1 391 ? -22.554 6.469   -18.655  1.00 33.60  ? 692  ILE   A CG2 1 
ATOM   3160  C  CD1 . ILE   A  1 391 ? -22.101 8.001   -21.416  1.00 41.89  ? 692  ILE   A CD1 1 
ATOM   3161  N  N   . THR   A  1 392 ? -22.370 2.926   -22.063  1.00 29.65  ? 693  THR   A N   1 
ATOM   3162  C  CA  . THR   A  1 392 ? -22.862 2.118   -23.165  1.00 30.97  ? 693  THR   A CA  1 
ATOM   3163  C  C   . THR   A  1 392 ? -23.282 0.744   -22.659  1.00 30.38  ? 693  THR   A C   1 
ATOM   3164  O  O   . THR   A  1 392 ? -22.733 0.242   -21.674  1.00 24.81  ? 693  THR   A O   1 
ATOM   3165  C  CB  . THR   A  1 392 ? -21.799 1.942   -24.245  1.00 29.41  ? 693  THR   A CB  1 
ATOM   3166  O  OG1 . THR   A  1 392 ? -20.731 1.135   -23.733  1.00 30.89  ? 693  THR   A OG1 1 
ATOM   3167  C  CG2 . THR   A  1 392 ? -21.266 3.283   -24.682  1.00 24.72  ? 693  THR   A CG2 1 
ATOM   3168  N  N   . PRO   A  1 393 ? -24.258 0.108   -23.308  1.00 29.57  ? 694  PRO   A N   1 
ATOM   3169  C  CA  . PRO   A  1 393 ? -24.778 -1.149  -22.751  1.00 25.15  ? 694  PRO   A CA  1 
ATOM   3170  C  C   . PRO   A  1 393 ? -23.768 -2.272  -22.782  1.00 21.81  ? 694  PRO   A C   1 
ATOM   3171  O  O   . PRO   A  1 393 ? -23.866 -3.187  -21.960  1.00 28.99  ? 694  PRO   A O   1 
ATOM   3172  C  CB  . PRO   A  1 393 ? -25.999 -1.458  -23.637  1.00 29.60  ? 694  PRO   A CB  1 
ATOM   3173  C  CG  . PRO   A  1 393 ? -25.765 -0.683  -24.925  1.00 25.48  ? 694  PRO   A CG  1 
ATOM   3174  C  CD  . PRO   A  1 393 ? -25.034 0.570   -24.472  1.00 26.08  ? 694  PRO   A CD  1 
ATOM   3175  N  N   . VAL   A  1 394 ? -22.785 -2.227  -23.685  1.00 24.03  ? 695  VAL   A N   1 
ATOM   3176  C  CA  . VAL   A  1 394 ? -21.885 -3.368  -23.813  1.00 24.69  ? 695  VAL   A CA  1 
ATOM   3177  C  C   . VAL   A  1 394 ? -20.977 -3.476  -22.612  1.00 20.98  ? 695  VAL   A C   1 
ATOM   3178  O  O   . VAL   A  1 394 ? -20.462 -4.556  -22.329  1.00 18.44  ? 695  VAL   A O   1 
ATOM   3179  C  CB  . VAL   A  1 394 ? -21.038 -3.315  -25.105  1.00 19.12  ? 695  VAL   A CB  1 
ATOM   3180  C  CG1 . VAL   A  1 394 ? -21.928 -3.532  -26.352  1.00 20.04  ? 695  VAL   A CG1 1 
ATOM   3181  C  CG2 . VAL   A  1 394 ? -20.280 -1.991  -25.210  1.00 19.43  ? 695  VAL   A CG2 1 
ATOM   3182  N  N   . PHE   A  1 395 ? -20.772 -2.379  -21.892  1.00 23.30  ? 696  PHE   A N   1 
ATOM   3183  C  CA  . PHE   A  1 395 ? -19.909 -2.436  -20.723  1.00 29.40  ? 696  PHE   A CA  1 
ATOM   3184  C  C   . PHE   A  1 395 ? -20.455 -3.418  -19.705  1.00 23.81  ? 696  PHE   A C   1 
ATOM   3185  O  O   . PHE   A  1 395 ? -19.695 -4.147  -19.067  1.00 20.08  ? 696  PHE   A O   1 
ATOM   3186  C  CB  . PHE   A  1 395 ? -19.770 -1.043  -20.122  1.00 25.29  ? 696  PHE   A CB  1 
ATOM   3187  C  CG  . PHE   A  1 395 ? -18.965 -0.999  -18.847  1.00 23.16  ? 696  PHE   A CG  1 
ATOM   3188  C  CD1 . PHE   A  1 395 ? -17.629 -0.620  -18.881  1.00 26.00  ? 696  PHE   A CD1 1 
ATOM   3189  C  CD2 . PHE   A  1 395 ? -19.552 -1.297  -17.622  1.00 23.74  ? 696  PHE   A CD2 1 
ATOM   3190  C  CE1 . PHE   A  1 395 ? -16.885 -0.548  -17.715  1.00 24.83  ? 696  PHE   A CE1 1 
ATOM   3191  C  CE2 . PHE   A  1 395 ? -18.819 -1.229  -16.452  1.00 27.10  ? 696  PHE   A CE2 1 
ATOM   3192  C  CZ  . PHE   A  1 395 ? -17.482 -0.854  -16.497  1.00 26.55  ? 696  PHE   A CZ  1 
ATOM   3193  N  N   . HIS   A  1 396 ? -21.772 -3.490  -19.591  1.00 20.12  ? 697  HIS   A N   1 
ATOM   3194  C  CA  . HIS   A  1 396 ? -22.459 -4.305  -18.613  1.00 22.20  ? 697  HIS   A CA  1 
ATOM   3195  C  C   . HIS   A  1 396 ? -22.800 -5.677  -19.145  1.00 23.43  ? 697  HIS   A C   1 
ATOM   3196  O  O   . HIS   A  1 396 ? -23.439 -6.464  -18.438  1.00 27.54  ? 697  HIS   A O   1 
ATOM   3197  C  CB  . HIS   A  1 396 ? -23.730 -3.575  -18.172  1.00 25.82  ? 697  HIS   A CB  1 
ATOM   3198  C  CG  . HIS   A  1 396 ? -23.469 -2.168  -17.741  1.00 31.94  ? 697  HIS   A CG  1 
ATOM   3199  N  ND1 . HIS   A  1 396 ? -23.096 -1.843  -16.454  1.00 32.25  ? 697  HIS   A ND1 1 
ATOM   3200  C  CD2 . HIS   A  1 396 ? -23.479 -1.006  -18.435  1.00 36.75  ? 697  HIS   A CD2 1 
ATOM   3201  C  CE1 . HIS   A  1 396 ? -22.912 -0.538  -16.367  1.00 36.36  ? 697  HIS   A CE1 1 
ATOM   3202  N  NE2 . HIS   A  1 396 ? -23.137 -0.006  -17.555  1.00 33.17  ? 697  HIS   A NE2 1 
ATOM   3203  N  N   . GLN   A  1 397 ? -22.384 -5.969  -20.372  1.00 19.75  ? 698  GLN   A N   1 
ATOM   3204  C  CA  . GLN   A  1 397 ? -22.689 -7.213  -21.053  1.00 22.31  ? 698  GLN   A CA  1 
ATOM   3205  C  C   . GLN   A  1 397 ? -21.512 -8.169  -20.904  1.00 23.32  ? 698  GLN   A C   1 
ATOM   3206  O  O   . GLN   A  1 397 ? -20.416 -7.887  -21.401  1.00 28.77  ? 698  GLN   A O   1 
ATOM   3207  C  CB  . GLN   A  1 397 ? -22.947 -6.939  -22.539  1.00 20.87  ? 698  GLN   A CB  1 
ATOM   3208  C  CG  . GLN   A  1 397 ? -23.221 -8.187  -23.332  1.00 18.24  ? 698  GLN   A CG  1 
ATOM   3209  C  CD  . GLN   A  1 397 ? -24.506 -8.812  -22.893  1.00 23.07  ? 698  GLN   A CD  1 
ATOM   3210  O  OE1 . GLN   A  1 397 ? -25.560 -8.168  -22.923  1.00 20.70  ? 698  GLN   A OE1 1 
ATOM   3211  N  NE2 . GLN   A  1 397 ? -24.432 -10.062 -22.445  1.00 20.73  ? 698  GLN   A NE2 1 
ATOM   3212  N  N   . GLU   A  1 398 ? -21.736 -9.301  -20.249  1.00 19.93  ? 699  GLU   A N   1 
ATOM   3213  C  CA  . GLU   A  1 398 ? -20.718 -10.339 -20.264  1.00 18.63  ? 699  GLU   A CA  1 
ATOM   3214  C  C   . GLU   A  1 398 ? -20.628 -10.923 -21.667  1.00 23.98  ? 699  GLU   A C   1 
ATOM   3215  O  O   . GLU   A  1 398 ? -21.631 -11.052 -22.368  1.00 22.32  ? 699  GLU   A O   1 
ATOM   3216  C  CB  . GLU   A  1 398 ? -21.048 -11.432 -19.264  1.00 22.49  ? 699  GLU   A CB  1 
ATOM   3217  C  CG  . GLU   A  1 398 ? -20.984 -10.953 -17.818  1.00 20.67  ? 699  GLU   A CG  1 
ATOM   3218  C  CD  . GLU   A  1 398 ? -21.255 -12.066 -16.859  1.00 26.12  ? 699  GLU   A CD  1 
ATOM   3219  O  OE1 . GLU   A  1 398 ? -20.912 -11.929 -15.660  1.00 27.70  ? 699  GLU   A OE1 1 
ATOM   3220  O  OE2 . GLU   A  1 398 ? -21.801 -13.090 -17.312  1.00 31.52  ? 699  GLU   A OE2 1 
ATOM   3221  N  N   . MET   A  1 399 ? -19.421 -11.265 -22.075  1.00 22.96  ? 700  MET   A N   1 
ATOM   3222  C  CA  . MET   A  1 399 ? -19.184 -11.784 -23.408  1.00 26.22  ? 700  MET   A CA  1 
ATOM   3223  C  C   . MET   A  1 399 ? -18.302 -13.013 -23.305  1.00 27.20  ? 700  MET   A C   1 
ATOM   3224  O  O   . MET   A  1 399 ? -17.509 -13.157 -22.372  1.00 31.92  ? 700  MET   A O   1 
ATOM   3225  C  CB  . MET   A  1 399 ? -18.531 -10.725 -24.300  1.00 25.19  ? 700  MET   A CB  1 
ATOM   3226  C  CG  . MET   A  1 399 ? -19.439 -9.546  -24.553  1.00 18.17  ? 700  MET   A CG  1 
ATOM   3227  S  SD  . MET   A  1 399 ? -18.592 -8.185  -25.360  1.00 26.18  ? 700  MET   A SD  1 
ATOM   3228  C  CE  . MET   A  1 399 ? -19.851 -6.914  -25.243  1.00 25.09  ? 700  MET   A CE  1 
ATOM   3229  N  N   . LEU   A  1 400 ? -18.498 -13.925 -24.240  1.00 19.21  ? 701  LEU   A N   1 
ATOM   3230  C  CA  . LEU   A  1 400 ? -17.635 -15.080 -24.397  1.00 19.18  ? 701  LEU   A CA  1 
ATOM   3231  C  C   . LEU   A  1 400 ? -16.848 -14.871 -25.667  1.00 26.88  ? 701  LEU   A C   1 
ATOM   3232  O  O   . LEU   A  1 400 ? -17.429 -14.531 -26.702  1.00 28.86  ? 701  LEU   A O   1 
ATOM   3233  C  CB  . LEU   A  1 400 ? -18.435 -16.374 -24.494  1.00 22.20  ? 701  LEU   A CB  1 
ATOM   3234  C  CG  . LEU   A  1 400 ? -19.059 -16.871 -23.210  1.00 28.81  ? 701  LEU   A CG  1 
ATOM   3235  C  CD1 . LEU   A  1 400 ? -19.892 -18.087 -23.535  1.00 29.46  ? 701  LEU   A CD1 1 
ATOM   3236  C  CD2 . LEU   A  1 400 ? -17.954 -17.216 -22.244  1.00 28.15  ? 701  LEU   A CD2 1 
ATOM   3237  N  N   . ASN   A  1 401 ? -15.535 -15.028 -25.585  1.00 27.34  ? 702  ASN   A N   1 
ATOM   3238  C  CA  . ASN   A  1 401 ? -14.683 -14.859 -26.750  1.00 21.71  ? 702  ASN   A CA  1 
ATOM   3239  C  C   . ASN   A  1 401 ? -14.133 -16.211 -27.168  1.00 24.49  ? 702  ASN   A C   1 
ATOM   3240  O  O   . ASN   A  1 401 ? -13.569 -16.943 -26.346  1.00 25.66  ? 702  ASN   A O   1 
ATOM   3241  C  CB  . ASN   A  1 401 ? -13.535 -13.888 -26.484  1.00 26.53  ? 702  ASN   A CB  1 
ATOM   3242  C  CG  . ASN   A  1 401 ? -12.895 -13.425 -27.762  1.00 28.85  ? 702  ASN   A CG  1 
ATOM   3243  O  OD1 . ASN   A  1 401 ? -13.483 -13.576 -28.823  1.00 26.66  ? 702  ASN   A OD1 1 
ATOM   3244  N  ND2 . ASN   A  1 401 ? -11.697 -12.879 -27.680  1.00 26.37  ? 702  ASN   A ND2 1 
ATOM   3245  N  N   . TYR   A  1 402 ? -14.318 -16.546 -28.438  1.00 26.56  ? 703  TYR   A N   1 
ATOM   3246  C  CA  . TYR   A  1 402 ? -13.796 -17.787 -28.988  1.00 18.31  ? 703  TYR   A CA  1 
ATOM   3247  C  C   . TYR   A  1 402 ? -13.634 -17.586 -30.486  1.00 22.65  ? 703  TYR   A C   1 
ATOM   3248  O  O   . TYR   A  1 402 ? -14.177 -16.643 -31.069  1.00 22.95  ? 703  TYR   A O   1 
ATOM   3249  C  CB  . TYR   A  1 402 ? -14.702 -18.984 -28.668  1.00 20.43  ? 703  TYR   A CB  1 
ATOM   3250  C  CG  . TYR   A  1 402 ? -16.191 -18.736 -28.880  1.00 26.75  ? 703  TYR   A CG  1 
ATOM   3251  C  CD1 . TYR   A  1 402 ? -16.814 -19.036 -30.098  1.00 26.49  ? 703  TYR   A CD1 1 
ATOM   3252  C  CD2 . TYR   A  1 402 ? -16.981 -18.231 -27.851  1.00 26.59  ? 703  TYR   A CD2 1 
ATOM   3253  C  CE1 . TYR   A  1 402 ? -18.184 -18.820 -30.277  1.00 20.50  ? 703  TYR   A CE1 1 
ATOM   3254  C  CE2 . TYR   A  1 402 ? -18.342 -18.016 -28.018  1.00 22.15  ? 703  TYR   A CE2 1 
ATOM   3255  C  CZ  . TYR   A  1 402 ? -18.941 -18.314 -29.222  1.00 24.96  ? 703  TYR   A CZ  1 
ATOM   3256  O  OH  . TYR   A  1 402 ? -20.298 -18.092 -29.353  1.00 28.02  ? 703  TYR   A OH  1 
ATOM   3257  N  N   . ARG   A  1 403 ? -12.857 -18.460 -31.093  1.00 25.26  ? 704  ARG   A N   1 
ATOM   3258  C  CA  . ARG   A  1 403 ? -12.380 -18.246 -32.450  1.00 26.00  ? 704  ARG   A CA  1 
ATOM   3259  C  C   . ARG   A  1 403 ? -13.085 -19.227 -33.379  1.00 29.62  ? 704  ARG   A C   1 
ATOM   3260  O  O   . ARG   A  1 403 ? -12.841 -20.436 -33.314  1.00 32.79  ? 704  ARG   A O   1 
ATOM   3261  C  CB  . ARG   A  1 403 ? -10.867 -18.389 -32.505  1.00 25.78  ? 704  ARG   A CB  1 
ATOM   3262  C  CG  . ARG   A  1 403 ? -10.154 -17.382 -31.611  1.00 31.67  ? 704  ARG   A CG  1 
ATOM   3263  C  CD  . ARG   A  1 403 ? -8.653  -17.531 -31.703  1.00 46.05  ? 704  ARG   A CD  1 
ATOM   3264  N  NE  . ARG   A  1 403 ? -8.145  -16.988 -32.959  1.00 55.36  ? 704  ARG   A NE  1 
ATOM   3265  C  CZ  . ARG   A  1 403 ? -6.919  -17.199 -33.425  1.00 59.97  ? 704  ARG   A CZ  1 
ATOM   3266  N  NH1 . ARG   A  1 403 ? -6.064  -17.954 -32.745  1.00 62.08  ? 704  ARG   A NH1 1 
ATOM   3267  N  NH2 . ARG   A  1 403 ? -6.550  -16.657 -34.575  1.00 58.32  ? 704  ARG   A NH2 1 
ATOM   3268  N  N   . LEU   A  1 404 ? -13.983 -18.702 -34.213  1.00 27.51  ? 705  LEU   A N   1 
ATOM   3269  C  CA  . LEU   A  1 404 ? -14.693 -19.484 -35.214  1.00 25.36  ? 705  LEU   A CA  1 
ATOM   3270  C  C   . LEU   A  1 404 ? -14.064 -19.259 -36.576  1.00 22.75  ? 705  LEU   A C   1 
ATOM   3271  O  O   . LEU   A  1 404 ? -13.487 -18.205 -36.844  1.00 25.65  ? 705  LEU   A O   1 
ATOM   3272  C  CB  . LEU   A  1 404 ? -16.175 -19.098 -35.270  1.00 24.94  ? 705  LEU   A CB  1 
ATOM   3273  C  CG  . LEU   A  1 404 ? -16.958 -19.277 -33.964  1.00 27.07  ? 705  LEU   A CG  1 
ATOM   3274  C  CD1 . LEU   A  1 404 ? -18.384 -18.813 -34.178  1.00 25.48  ? 705  LEU   A CD1 1 
ATOM   3275  C  CD2 . LEU   A  1 404 ? -16.925 -20.744 -33.514  1.00 22.81  ? 705  LEU   A CD2 1 
ATOM   3276  N  N   . THR   A  1 405 ? -14.187 -20.252 -37.435  1.00 28.10  ? 706  THR   A N   1 
ATOM   3277  C  CA  . THR   A  1 405 ? -13.726 -20.093 -38.799  1.00 28.49  ? 706  THR   A CA  1 
ATOM   3278  C  C   . THR   A  1 405 ? -14.912 -20.154 -39.759  1.00 30.97  ? 706  THR   A C   1 
ATOM   3279  O  O   . THR   A  1 405 ? -15.906 -20.826 -39.466  1.00 26.16  ? 706  THR   A O   1 
ATOM   3280  C  CB  . THR   A  1 405 ? -12.723 -21.195 -39.154  1.00 35.66  ? 706  THR   A CB  1 
ATOM   3281  O  OG1 . THR   A  1 405 ? -12.148 -20.938 -40.442  1.00 39.14  ? 706  THR   A OG1 1 
ATOM   3282  C  CG2 . THR   A  1 405 ? -13.421 -22.552 -39.176  1.00 33.68  ? 706  THR   A CG2 1 
ATOM   3283  N  N   . PRO   A  1 406 ? -14.863 -19.453 -40.909  1.00 30.72  ? 707  PRO   A N   1 
ATOM   3284  C  CA  . PRO   A  1 406 ? -13.846 -18.538 -41.438  1.00 25.39  ? 707  PRO   A CA  1 
ATOM   3285  C  C   . PRO   A  1 406 ? -13.563 -17.338 -40.557  1.00 25.70  ? 707  PRO   A C   1 
ATOM   3286  O  O   . PRO   A  1 406 ? -14.372 -16.957 -39.702  1.00 28.92  ? 707  PRO   A O   1 
ATOM   3287  C  CB  . PRO   A  1 406 ? -14.453 -18.073 -42.775  1.00 29.99  ? 707  PRO   A CB  1 
ATOM   3288  C  CG  . PRO   A  1 406 ? -15.372 -19.155 -43.157  1.00 34.18  ? 707  PRO   A CG  1 
ATOM   3289  C  CD  . PRO   A  1 406 ? -15.960 -19.642 -41.871  1.00 32.43  ? 707  PRO   A CD  1 
ATOM   3290  N  N   . SER   A  1 407 ? -12.405 -16.723 -40.768  1.00 22.45  ? 708  SER   A N   1 
ATOM   3291  C  CA  . SER   A  1 407 ? -12.031 -15.635 -39.881  1.00 25.66  ? 708  SER   A CA  1 
ATOM   3292  C  C   . SER   A  1 407 ? -11.066 -14.698 -40.584  1.00 25.96  ? 708  SER   A C   1 
ATOM   3293  O  O   . SER   A  1 407 ? -10.452 -15.036 -41.604  1.00 26.73  ? 708  SER   A O   1 
ATOM   3294  C  CB  . SER   A  1 407 ? -11.402 -16.174 -38.597  1.00 32.64  ? 708  SER   A CB  1 
ATOM   3295  O  OG  . SER   A  1 407 ? -10.212 -16.877 -38.906  1.00 39.74  ? 708  SER   A OG  1 
ATOM   3296  N  N   . PHE   A  1 408 ? -10.957 -13.505 -40.011  1.00 24.12  ? 709  PHE   A N   1 
ATOM   3297  C  CA  . PHE   A  1 408 ? -9.905  -12.554 -40.325  1.00 23.48  ? 709  PHE   A CA  1 
ATOM   3298  C  C   . PHE   A  1 408 ? -8.802  -12.722 -39.298  1.00 29.73  ? 709  PHE   A C   1 
ATOM   3299  O  O   . PHE   A  1 408 ? -9.073  -12.784 -38.093  1.00 29.65  ? 709  PHE   A O   1 
ATOM   3300  C  CB  . PHE   A  1 408 ? -10.440 -11.119 -40.315  1.00 23.13  ? 709  PHE   A CB  1 
ATOM   3301  C  CG  . PHE   A  1 408 ? -11.401 -10.832 -41.425  1.00 26.51  ? 709  PHE   A CG  1 
ATOM   3302  C  CD1 . PHE   A  1 408 ? -12.748 -10.651 -41.162  1.00 25.51  ? 709  PHE   A CD1 1 
ATOM   3303  C  CD2 . PHE   A  1 408 ? -10.958 -10.754 -42.740  1.00 27.31  ? 709  PHE   A CD2 1 
ATOM   3304  C  CE1 . PHE   A  1 408 ? -13.639 -10.381 -42.182  1.00 22.58  ? 709  PHE   A CE1 1 
ATOM   3305  C  CE2 . PHE   A  1 408 ? -11.842 -10.484 -43.762  1.00 23.43  ? 709  PHE   A CE2 1 
ATOM   3306  C  CZ  . PHE   A  1 408 ? -13.191 -10.300 -43.485  1.00 21.72  ? 709  PHE   A CZ  1 
ATOM   3307  N  N   . GLU   A  1 409 ? -7.570  -12.817 -39.777  1.00 25.72  ? 710  GLU   A N   1 
ATOM   3308  C  CA  . GLU   A  1 409 ? -6.420  -13.060 -38.930  1.00 29.12  ? 710  GLU   A CA  1 
ATOM   3309  C  C   . GLU   A  1 409 ? -5.393  -11.968 -39.166  1.00 30.66  ? 710  GLU   A C   1 
ATOM   3310  O  O   . GLU   A  1 409 ? -5.349  -11.362 -40.238  1.00 28.56  ? 710  GLU   A O   1 
ATOM   3311  C  CB  . GLU   A  1 409 ? -5.797  -14.424 -39.228  1.00 28.05  ? 710  GLU   A CB  1 
ATOM   3312  C  CG  . GLU   A  1 409 ? -6.773  -15.566 -39.099  1.00 38.23  ? 710  GLU   A CG  1 
ATOM   3313  C  CD  . GLU   A  1 409 ? -7.180  -15.812 -37.653  1.00 47.42  ? 710  GLU   A CD  1 
ATOM   3314  O  OE1 . GLU   A  1 409 ? -6.510  -15.277 -36.744  1.00 47.24  ? 710  GLU   A OE1 1 
ATOM   3315  O  OE2 . GLU   A  1 409 ? -8.164  -16.547 -37.428  1.00 48.62  ? 710  GLU   A OE2 1 
ATOM   3316  N  N   . TYR   A  1 410 ? -4.562  -11.727 -38.162  1.00 23.41  ? 711  TYR   A N   1 
ATOM   3317  C  CA  . TYR   A  1 410 ? -3.409  -10.869 -38.358  1.00 24.36  ? 711  TYR   A CA  1 
ATOM   3318  C  C   . TYR   A  1 410 ? -2.348  -11.592 -39.171  1.00 24.40  ? 711  TYR   A C   1 
ATOM   3319  O  O   . TYR   A  1 410 ? -2.298  -12.823 -39.217  1.00 30.87  ? 711  TYR   A O   1 
ATOM   3320  C  CB  . TYR   A  1 410 ? -2.802  -10.464 -37.017  1.00 33.68  ? 711  TYR   A CB  1 
ATOM   3321  C  CG  . TYR   A  1 410 ? -3.677  -9.574  -36.185  1.00 39.08  ? 711  TYR   A CG  1 
ATOM   3322  C  CD1 . TYR   A  1 410 ? -4.136  -9.979  -34.943  1.00 61.38  ? 711  TYR   A CD1 1 
ATOM   3323  C  CD2 . TYR   A  1 410 ? -4.038  -8.325  -36.642  1.00 47.22  ? 711  TYR   A CD2 1 
ATOM   3324  C  CE1 . TYR   A  1 410 ? -4.928  -9.153  -34.180  1.00 64.35  ? 711  TYR   A CE1 1 
ATOM   3325  C  CE2 . TYR   A  1 410 ? -4.829  -7.499  -35.893  1.00 59.73  ? 711  TYR   A CE2 1 
ATOM   3326  C  CZ  . TYR   A  1 410 ? -5.270  -7.910  -34.665  1.00 57.07  ? 711  TYR   A CZ  1 
ATOM   3327  O  OH  . TYR   A  1 410 ? -6.057  -7.059  -33.932  1.00 56.86  ? 711  TYR   A OH  1 
ATOM   3328  N  N   . GLN   A  1 411 ? -1.463  -10.814 -39.783  1.00 21.63  ? 712  GLN   A N   1 
ATOM   3329  C  CA  . GLN   A  1 411 ? -0.356  -11.379 -40.535  1.00 24.16  ? 712  GLN   A CA  1 
ATOM   3330  C  C   . GLN   A  1 411 ? 0.817   -10.427 -40.408  1.00 32.38  ? 712  GLN   A C   1 
ATOM   3331  O  O   . GLN   A  1 411 ? 0.630   -9.248  -40.082  1.00 29.64  ? 712  GLN   A O   1 
ATOM   3332  C  CB  . GLN   A  1 411 ? -0.728  -11.612 -42.014  1.00 29.14  ? 712  GLN   A CB  1 
ATOM   3333  C  CG  . GLN   A  1 411 ? -1.232  -10.364 -42.730  1.00 24.89  ? 712  GLN   A CG  1 
ATOM   3334  C  CD  . GLN   A  1 411 ? -1.643  -10.628 -44.179  1.00 19.09  ? 712  GLN   A CD  1 
ATOM   3335  O  OE1 . GLN   A  1 411 ? -1.236  -11.617 -44.784  1.00 30.93  ? 712  GLN   A OE1 1 
ATOM   3336  N  NE2 . GLN   A  1 411 ? -2.475  -9.748  -44.725  1.00 26.61  ? 712  GLN   A NE2 1 
ATOM   3337  N  N   . PRO   A  1 412 ? 2.039   -10.906 -40.627  1.00 36.77  ? 713  PRO   A N   1 
ATOM   3338  C  CA  . PRO   A  1 412 ? 3.195   -10.017 -40.490  1.00 40.25  ? 713  PRO   A CA  1 
ATOM   3339  C  C   . PRO   A  1 412 ? 3.113   -8.877  -41.492  1.00 39.83  ? 713  PRO   A C   1 
ATOM   3340  O  O   . PRO   A  1 412 ? 2.574   -9.025  -42.590  1.00 34.95  ? 713  PRO   A O   1 
ATOM   3341  C  CB  . PRO   A  1 412 ? 4.392   -10.933 -40.781  1.00 42.77  ? 713  PRO   A CB  1 
ATOM   3342  C  CG  . PRO   A  1 412 ? 3.865   -12.337 -40.663  1.00 42.12  ? 713  PRO   A CG  1 
ATOM   3343  C  CD  . PRO   A  1 412 ? 2.429   -12.259 -41.068  1.00 37.33  ? 713  PRO   A CD  1 
ATOM   3344  N  N   . ASP   A  1 413 ? 3.623   -7.724  -41.087  1.00 39.80  ? 714  ASP   A N   1 
ATOM   3345  C  CA  . ASP   A  1 413 ? 3.825   -6.634  -42.022  1.00 39.88  ? 714  ASP   A CA  1 
ATOM   3346  C  C   . ASP   A  1 413 ? 4.726   -7.112  -43.155  1.00 42.33  ? 714  ASP   A C   1 
ATOM   3347  O  O   . ASP   A  1 413 ? 5.756   -7.749  -42.895  1.00 44.49  ? 714  ASP   A O   1 
ATOM   3348  C  CB  . ASP   A  1 413 ? 4.449   -5.429  -41.322  1.00 42.26  ? 714  ASP   A CB  1 
ATOM   3349  C  CG  . ASP   A  1 413 ? 3.508   -4.784  -40.331  1.00 54.04  ? 714  ASP   A CG  1 
ATOM   3350  O  OD1 . ASP   A  1 413 ? 2.293   -4.719  -40.628  1.00 52.78  ? 714  ASP   A OD1 1 
ATOM   3351  O  OD2 . ASP   A  1 413 ? 3.982   -4.340  -39.262  1.00 61.54  ? 714  ASP   A OD2 1 
ATOM   3352  N  N   . PRO   A  1 414 ? 4.378   -6.835  -44.413  1.00 38.76  ? 715  PRO   A N   1 
ATOM   3353  C  CA  . PRO   A  1 414 ? 5.140   -7.422  -45.524  1.00 35.19  ? 715  PRO   A CA  1 
ATOM   3354  C  C   . PRO   A  1 414 ? 6.572   -6.931  -45.597  1.00 37.65  ? 715  PRO   A C   1 
ATOM   3355  O  O   . PRO   A  1 414 ? 7.440   -7.678  -46.063  1.00 44.21  ? 715  PRO   A O   1 
ATOM   3356  C  CB  . PRO   A  1 414 ? 4.331   -7.015  -46.763  1.00 33.49  ? 715  PRO   A CB  1 
ATOM   3357  C  CG  . PRO   A  1 414 ? 3.599   -5.795  -46.349  1.00 35.20  ? 715  PRO   A CG  1 
ATOM   3358  C  CD  . PRO   A  1 414 ? 3.309   -5.936  -44.872  1.00 37.93  ? 715  PRO   A CD  1 
ATOM   3359  N  N   . TRP   A  1 415 ? 6.868   -5.718  -45.125  1.00 34.37  ? 716  TRP   A N   1 
ATOM   3360  C  CA  . TRP   A  1 415 ? 8.255   -5.269  -45.184  1.00 39.63  ? 716  TRP   A CA  1 
ATOM   3361  C  C   . TRP   A  1 415 ? 9.152   -6.004  -44.195  1.00 46.44  ? 716  TRP   A C   1 
ATOM   3362  O  O   . TRP   A  1 415 ? 10.378  -5.936  -44.336  1.00 48.00  ? 716  TRP   A O   1 
ATOM   3363  C  CB  . TRP   A  1 415 ? 8.350   -3.765  -44.948  1.00 36.39  ? 716  TRP   A CB  1 
ATOM   3364  C  CG  . TRP   A  1 415 ? 7.713   -3.320  -43.691  1.00 42.07  ? 716  TRP   A CG  1 
ATOM   3365  C  CD1 . TRP   A  1 415 ? 8.278   -3.295  -42.452  1.00 41.13  ? 716  TRP   A CD1 1 
ATOM   3366  C  CD2 . TRP   A  1 415 ? 6.378   -2.826  -43.538  1.00 44.73  ? 716  TRP   A CD2 1 
ATOM   3367  N  NE1 . TRP   A  1 415 ? 7.378   -2.813  -41.535  1.00 40.91  ? 716  TRP   A NE1 1 
ATOM   3368  C  CE2 . TRP   A  1 415 ? 6.204   -2.516  -42.175  1.00 45.23  ? 716  TRP   A CE2 1 
ATOM   3369  C  CE3 . TRP   A  1 415 ? 5.315   -2.613  -44.422  1.00 43.79  ? 716  TRP   A CE3 1 
ATOM   3370  C  CZ2 . TRP   A  1 415 ? 5.011   -2.010  -41.671  1.00 49.58  ? 716  TRP   A CZ2 1 
ATOM   3371  C  CZ3 . TRP   A  1 415 ? 4.130   -2.106  -43.924  1.00 44.99  ? 716  TRP   A CZ3 1 
ATOM   3372  C  CH2 . TRP   A  1 415 ? 3.987   -1.812  -42.556  1.00 51.40  ? 716  TRP   A CH2 1 
ATOM   3373  N  N   . ASN   A  1 416 ? 8.580   -6.703  -43.205  1.00 48.81  ? 717  ASN   A N   1 
ATOM   3374  C  CA  . ASN   A  1 416 ? 9.382   -7.553  -42.326  1.00 54.25  ? 717  ASN   A CA  1 
ATOM   3375  C  C   . ASN   A  1 416 ? 9.758   -8.875  -42.976  1.00 57.82  ? 717  ASN   A C   1 
ATOM   3376  O  O   . ASN   A  1 416 ? 10.713  -9.520  -42.529  1.00 61.44  ? 717  ASN   A O   1 
ATOM   3377  C  CB  . ASN   A  1 416 ? 8.640   -7.855  -41.020  1.00 45.18  ? 717  ASN   A CB  1 
ATOM   3378  C  CG  . ASN   A  1 416 ? 8.407   -6.621  -40.188  1.00 52.54  ? 717  ASN   A CG  1 
ATOM   3379  O  OD1 . ASN   A  1 416 ? 9.191   -5.672  -40.234  1.00 61.09  ? 717  ASN   A OD1 1 
ATOM   3380  N  ND2 . ASN   A  1 416 ? 7.321   -6.619  -39.423  1.00 44.32  ? 717  ASN   A ND2 1 
ATOM   3381  N  N   . THR   A  1 417 ? 9.030   -9.294  -44.011  1.00 54.46  ? 718  THR   A N   1 
ATOM   3382  C  CA  . THR   A  1 417 ? 9.207   -10.613 -44.593  1.00 51.24  ? 718  THR   A CA  1 
ATOM   3383  C  C   . THR   A  1 417 ? 9.593   -10.592 -46.066  1.00 56.51  ? 718  THR   A C   1 
ATOM   3384  O  O   . THR   A  1 417 ? 10.070  -11.615 -46.575  1.00 55.50  ? 718  THR   A O   1 
ATOM   3385  C  CB  . THR   A  1 417 ? 7.924   -11.439 -44.417  1.00 51.02  ? 718  THR   A CB  1 
ATOM   3386  O  OG1 . THR   A  1 417 ? 6.800   -10.686 -44.888  1.00 53.19  ? 718  THR   A OG1 1 
ATOM   3387  C  CG2 . THR   A  1 417 ? 7.702   -11.773 -42.945  1.00 47.88  ? 718  THR   A CG2 1 
ATOM   3388  N  N   . HIS   A  1 418 ? 9.432   -9.466  -46.757  1.00 54.54  ? 719  HIS   A N   1 
ATOM   3389  C  CA  . HIS   A  1 418 ? 9.649   -9.420  -48.201  1.00 57.65  ? 719  HIS   A CA  1 
ATOM   3390  C  C   . HIS   A  1 418 ? 11.139  -9.357  -48.518  1.00 59.96  ? 719  HIS   A C   1 
ATOM   3391  O  O   . HIS   A  1 418 ? 11.841  -8.460  -48.041  1.00 57.10  ? 719  HIS   A O   1 
ATOM   3392  C  CB  . HIS   A  1 418 ? 8.933   -8.215  -48.806  1.00 55.14  ? 719  HIS   A CB  1 
ATOM   3393  C  CG  . HIS   A  1 418 ? 9.053   -8.124  -50.296  1.00 50.68  ? 719  HIS   A CG  1 
ATOM   3394  N  ND1 . HIS   A  1 418 ? 8.376   -8.969  -51.149  1.00 48.41  ? 719  HIS   A ND1 1 
ATOM   3395  C  CD2 . HIS   A  1 418 ? 9.761   -7.280  -51.084  1.00 49.76  ? 719  HIS   A CD2 1 
ATOM   3396  C  CE1 . HIS   A  1 418 ? 8.670   -8.656  -52.399  1.00 49.80  ? 719  HIS   A CE1 1 
ATOM   3397  N  NE2 . HIS   A  1 418 ? 9.509   -7.635  -52.387  1.00 51.16  ? 719  HIS   A NE2 1 
ATOM   3398  N  N   . VAL   A  1 419 ? 11.616  -10.301 -49.322  1.00 65.42  ? 720  VAL   A N   1 
ATOM   3399  C  CA  . VAL   A  1 419 ? 12.947  -10.210 -49.916  1.00 71.66  ? 720  VAL   A CA  1 
ATOM   3400  C  C   . VAL   A  1 419 ? 12.813  -9.438  -51.224  1.00 67.61  ? 720  VAL   A C   1 
ATOM   3401  O  O   . VAL   A  1 419 ? 12.156  -9.897  -52.165  1.00 64.21  ? 720  VAL   A O   1 
ATOM   3402  C  CB  . VAL   A  1 419 ? 13.569  -11.597 -50.141  1.00 76.61  ? 720  VAL   A CB  1 
ATOM   3403  C  CG1 . VAL   A  1 419 ? 14.453  -11.978 -48.960  1.00 75.80  ? 720  VAL   A CG1 1 
ATOM   3404  C  CG2 . VAL   A  1 419 ? 12.492  -12.657 -50.374  1.00 78.03  ? 720  VAL   A CG2 1 
ATOM   3405  N  N   . TRP   A  1 420 ? 13.418  -8.256  -51.273  1.00 65.35  ? 721  TRP   A N   1 
ATOM   3406  C  CA  . TRP   A  1 420 ? 13.279  -7.385  -52.429  1.00 66.26  ? 721  TRP   A CA  1 
ATOM   3407  C  C   . TRP   A  1 420 ? 14.010  -7.955  -53.638  1.00 69.70  ? 721  TRP   A C   1 
ATOM   3408  O  O   . TRP   A  1 420 ? 14.849  -8.854  -53.529  1.00 74.05  ? 721  TRP   A O   1 
ATOM   3409  C  CB  . TRP   A  1 420 ? 13.804  -5.988  -52.103  1.00 62.87  ? 721  TRP   A CB  1 
ATOM   3410  C  CG  . TRP   A  1 420 ? 12.859  -5.219  -51.235  1.00 61.65  ? 721  TRP   A CG  1 
ATOM   3411  C  CD1 . TRP   A  1 420 ? 12.683  -5.357  -49.886  1.00 56.61  ? 721  TRP   A CD1 1 
ATOM   3412  C  CD2 . TRP   A  1 420 ? 11.940  -4.205  -51.659  1.00 53.00  ? 721  TRP   A CD2 1 
ATOM   3413  N  NE1 . TRP   A  1 420 ? 11.718  -4.483  -49.444  1.00 52.18  ? 721  TRP   A NE1 1 
ATOM   3414  C  CE2 . TRP   A  1 420 ? 11.246  -3.765  -50.512  1.00 52.39  ? 721  TRP   A CE2 1 
ATOM   3415  C  CE3 . TRP   A  1 420 ? 11.642  -3.622  -52.896  1.00 52.64  ? 721  TRP   A CE3 1 
ATOM   3416  C  CZ2 . TRP   A  1 420 ? 10.272  -2.771  -50.565  1.00 50.04  ? 721  TRP   A CZ2 1 
ATOM   3417  C  CZ3 . TRP   A  1 420 ? 10.676  -2.632  -52.948  1.00 53.46  ? 721  TRP   A CZ3 1 
ATOM   3418  C  CH2 . TRP   A  1 420 ? 10.002  -2.217  -51.787  1.00 54.93  ? 721  TRP   A CH2 1 
ATOM   3419  N  N   . LYS   A  1 421 ? 13.674  -7.421  -54.806  1.00 72.70  ? 722  LYS   A N   1 
ATOM   3420  C  CA  . LYS   A  1 421 ? 14.335  -7.825  -56.042  1.00 77.67  ? 722  LYS   A CA  1 
ATOM   3421  C  C   . LYS   A  1 421 ? 15.140  -6.665  -56.637  1.00 81.63  ? 722  LYS   A C   1 
ATOM   3422  O  O   . LYS   A  1 421 ? 16.258  -6.861  -57.111  1.00 83.44  ? 722  LYS   A O   1 
ATOM   3423  C  CB  . LYS   A  1 421 ? 13.310  -8.338  -57.059  1.00 76.96  ? 722  LYS   A CB  1 
ATOM   3424  C  CG  . LYS   A  1 421 ? 12.387  -9.449  -56.544  1.00 78.70  ? 722  LYS   A CG  1 
ATOM   3425  C  CD  . LYS   A  1 421 ? 11.501  -9.996  -57.670  1.00 79.18  ? 722  LYS   A CD  1 
ATOM   3426  C  CE  . LYS   A  1 421 ? 10.255  -10.718 -57.144  1.00 77.38  ? 722  LYS   A CE  1 
ATOM   3427  N  NZ  . LYS   A  1 421 ? 10.543  -12.029 -56.492  1.00 76.01  ? 722  LYS   A NZ  1 
ATOM   3428  N  N   . ARG   B  1 3   ? 9.783   -20.806 -18.649  1.00 67.74  ? 304  ARG   B N   1 
ATOM   3429  C  CA  . ARG   B  1 3   ? 8.844   -20.179 -19.569  1.00 67.59  ? 304  ARG   B CA  1 
ATOM   3430  C  C   . ARG   B  1 3   ? 8.531   -18.733 -19.159  1.00 68.96  ? 304  ARG   B C   1 
ATOM   3431  O  O   . ARG   B  1 3   ? 8.510   -18.388 -17.975  1.00 68.04  ? 304  ARG   B O   1 
ATOM   3432  C  CB  . ARG   B  1 3   ? 7.554   -21.001 -19.662  1.00 70.03  ? 304  ARG   B CB  1 
ATOM   3433  C  CG  . ARG   B  1 3   ? 6.469   -20.366 -20.527  1.00 73.52  ? 304  ARG   B CG  1 
ATOM   3434  C  CD  . ARG   B  1 3   ? 5.372   -21.354 -20.869  1.00 77.07  ? 304  ARG   B CD  1 
ATOM   3435  N  NE  . ARG   B  1 3   ? 4.759   -21.962 -19.689  1.00 79.08  ? 304  ARG   B NE  1 
ATOM   3436  C  CZ  . ARG   B  1 3   ? 3.649   -21.511 -19.105  1.00 76.53  ? 304  ARG   B CZ  1 
ATOM   3437  N  NH1 . ARG   B  1 3   ? 3.028   -20.442 -19.590  1.00 67.34  ? 304  ARG   B NH1 1 
ATOM   3438  N  NH2 . ARG   B  1 3   ? 3.157   -22.129 -18.038  1.00 74.40  ? 304  ARG   B NH2 1 
ATOM   3439  N  N   . PHE   B  1 4   ? 8.304   -17.891 -20.161  1.00 60.56  ? 305  PHE   B N   1 
ATOM   3440  C  CA  . PHE   B  1 4   ? 8.080   -16.469 -19.974  1.00 55.03  ? 305  PHE   B CA  1 
ATOM   3441  C  C   . PHE   B  1 4   ? 6.871   -16.072 -20.808  1.00 48.79  ? 305  PHE   B C   1 
ATOM   3442  O  O   . PHE   B  1 4   ? 6.544   -16.729 -21.797  1.00 38.24  ? 305  PHE   B O   1 
ATOM   3443  C  CB  . PHE   B  1 4   ? 9.318   -15.638 -20.402  1.00 66.67  ? 305  PHE   B CB  1 
ATOM   3444  C  CG  . PHE   B  1 4   ? 10.614  -16.031 -19.708  1.00 79.48  ? 305  PHE   B CG  1 
ATOM   3445  C  CD1 . PHE   B  1 4   ? 11.290  -17.195 -20.058  1.00 88.00  ? 305  PHE   B CD1 1 
ATOM   3446  C  CD2 . PHE   B  1 4   ? 11.180  -15.210 -18.738  1.00 80.94  ? 305  PHE   B CD2 1 
ATOM   3447  C  CE1 . PHE   B  1 4   ? 12.484  -17.548 -19.428  1.00 90.12  ? 305  PHE   B CE1 1 
ATOM   3448  C  CE2 . PHE   B  1 4   ? 12.376  -15.555 -18.106  1.00 80.66  ? 305  PHE   B CE2 1 
ATOM   3449  C  CZ  . PHE   B  1 4   ? 13.026  -16.723 -18.451  1.00 86.23  ? 305  PHE   B CZ  1 
ATOM   3450  N  N   . LEU   B  1 5   ? 6.188   -15.007 -20.395  1.00 36.67  ? 306  LEU   B N   1 
ATOM   3451  C  CA  . LEU   B  1 5   ? 5.149   -14.409 -21.222  1.00 31.98  ? 306  LEU   B CA  1 
ATOM   3452  C  C   . LEU   B  1 5   ? 5.426   -12.924 -21.301  1.00 34.06  ? 306  LEU   B C   1 
ATOM   3453  O  O   . LEU   B  1 5   ? 5.756   -12.303 -20.290  1.00 36.62  ? 306  LEU   B O   1 
ATOM   3454  C  CB  . LEU   B  1 5   ? 3.747   -14.658 -20.668  1.00 28.53  ? 306  LEU   B CB  1 
ATOM   3455  C  CG  . LEU   B  1 5   ? 3.286   -16.105 -20.780  1.00 34.43  ? 306  LEU   B CG  1 
ATOM   3456  C  CD1 . LEU   B  1 5   ? 1.955   -16.288 -20.099  1.00 35.37  ? 306  LEU   B CD1 1 
ATOM   3457  C  CD2 . LEU   B  1 5   ? 3.178   -16.470 -22.247  1.00 34.51  ? 306  LEU   B CD2 1 
ATOM   3458  N  N   . LYS   B  1 6   ? 5.325   -12.364 -22.495  1.00 36.18  ? 307  LYS   B N   1 
ATOM   3459  C  CA  . LYS   B  1 6   ? 5.604   -10.953 -22.684  1.00 39.20  ? 307  LYS   B CA  1 
ATOM   3460  C  C   . LYS   B  1 6   ? 4.296   -10.190 -22.762  1.00 32.31  ? 307  LYS   B C   1 
ATOM   3461  O  O   . LYS   B  1 6   ? 3.315   -10.677 -23.323  1.00 31.41  ? 307  LYS   B O   1 
ATOM   3462  C  CB  . LYS   B  1 6   ? 6.443   -10.714 -23.938  1.00 40.90  ? 307  LYS   B CB  1 
ATOM   3463  C  CG  . LYS   B  1 6   ? 7.897   -11.128 -23.773  1.00 46.87  ? 307  LYS   B CG  1 
ATOM   3464  C  CD  . LYS   B  1 6   ? 8.750   -10.568 -24.903  1.00 60.81  ? 307  LYS   B CD  1 
ATOM   3465  C  CE  . LYS   B  1 6   ? 10.139  -11.178 -24.896  1.00 65.28  ? 307  LYS   B CE  1 
ATOM   3466  N  NZ  . LYS   B  1 6   ? 10.618  -11.380 -23.499  1.00 62.41  ? 307  LYS   B NZ  1 
ATOM   3467  N  N   . VAL   B  1 7   ? 4.271   -9.023  -22.138  1.00 30.26  ? 308  VAL   B N   1 
ATOM   3468  C  CA  . VAL   B  1 7   ? 3.179   -8.080  -22.306  1.00 28.98  ? 308  VAL   B CA  1 
ATOM   3469  C  C   . VAL   B  1 7   ? 3.783   -6.782  -22.804  1.00 32.66  ? 308  VAL   B C   1 
ATOM   3470  O  O   . VAL   B  1 7   ? 4.883   -6.388  -22.404  1.00 38.32  ? 308  VAL   B O   1 
ATOM   3471  C  CB  . VAL   B  1 7   ? 2.354   -7.841  -21.021  1.00 31.31  ? 308  VAL   B CB  1 
ATOM   3472  C  CG1 . VAL   B  1 7   ? 1.580   -9.094  -20.647  1.00 30.32  ? 308  VAL   B CG1 1 
ATOM   3473  C  CG2 . VAL   B  1 7   ? 3.239   -7.371  -19.866  1.00 29.04  ? 308  VAL   B CG2 1 
ATOM   3474  N  N   . LYS   B  1 8   ? 3.041   -6.112  -23.672  1.00 27.13  ? 309  LYS   B N   1 
ATOM   3475  C  CA  . LYS   B  1 8   ? 3.495   -4.916  -24.355  1.00 26.13  ? 309  LYS   B CA  1 
ATOM   3476  C  C   . LYS   B  1 8   ? 2.546   -3.777  -24.041  1.00 26.53  ? 309  LYS   B C   1 
ATOM   3477  O  O   . LYS   B  1 8   ? 1.332   -3.978  -23.949  1.00 29.52  ? 309  LYS   B O   1 
ATOM   3478  C  CB  . LYS   B  1 8   ? 3.545   -5.161  -25.878  1.00 30.22  ? 309  LYS   B CB  1 
ATOM   3479  C  CG  . LYS   B  1 8   ? 3.754   -3.937  -26.724  1.00 35.68  ? 309  LYS   B CG  1 
ATOM   3480  C  CD  . LYS   B  1 8   ? 3.866   -4.346  -28.184  1.00 34.95  ? 309  LYS   B CD  1 
ATOM   3481  C  CE  . LYS   B  1 8   ? 4.366   -3.198  -29.030  1.00 45.46  ? 309  LYS   B CE  1 
ATOM   3482  N  NZ  . LYS   B  1 8   ? 4.423   -3.590  -30.458  1.00 47.12  ? 309  LYS   B NZ  1 
ATOM   3483  N  N   . ASN   B  1 9   ? 3.100   -2.587  -23.880  1.00 26.18  ? 310  ASN   B N   1 
ATOM   3484  C  CA  . ASN   B  1 9   ? 2.305   -1.376  -23.864  1.00 32.28  ? 310  ASN   B CA  1 
ATOM   3485  C  C   . ASN   B  1 9   ? 2.323   -0.806  -25.277  1.00 32.83  ? 310  ASN   B C   1 
ATOM   3486  O  O   . ASN   B  1 9   ? 3.392   -0.539  -25.829  1.00 28.37  ? 310  ASN   B O   1 
ATOM   3487  C  CB  . ASN   B  1 9   ? 2.836   -0.369  -22.850  1.00 35.68  ? 310  ASN   B CB  1 
ATOM   3488  C  CG  . ASN   B  1 9   ? 1.933   0.829   -22.722  1.00 34.02  ? 310  ASN   B CG  1 
ATOM   3489  O  OD1 . ASN   B  1 9   ? 1.750   1.588   -23.684  1.00 32.68  ? 310  ASN   B OD1 1 
ATOM   3490  N  ND2 . ASN   B  1 9   ? 1.347   1.006   -21.544  1.00 30.53  ? 310  ASN   B ND2 1 
ATOM   3491  N  N   . TRP   B  1 10  ? 1.148   -0.649  -25.870  1.00 28.72  ? 311  TRP   B N   1 
ATOM   3492  C  CA  . TRP   B  1 10  ? 1.101   -0.243  -27.268  1.00 32.56  ? 311  TRP   B CA  1 
ATOM   3493  C  C   . TRP   B  1 10  ? 1.262   1.254   -27.440  1.00 35.06  ? 311  TRP   B C   1 
ATOM   3494  O  O   . TRP   B  1 10  ? 1.376   1.729   -28.571  1.00 32.91  ? 311  TRP   B O   1 
ATOM   3495  C  CB  . TRP   B  1 10  ? -0.196  -0.730  -27.902  1.00 27.83  ? 311  TRP   B CB  1 
ATOM   3496  C  CG  . TRP   B  1 10  ? -0.148  -2.188  -28.058  1.00 32.82  ? 311  TRP   B CG  1 
ATOM   3497  C  CD1 . TRP   B  1 10  ? -0.519  -3.128  -27.138  1.00 27.00  ? 311  TRP   B CD1 1 
ATOM   3498  C  CD2 . TRP   B  1 10  ? 0.354   -2.903  -29.190  1.00 37.70  ? 311  TRP   B CD2 1 
ATOM   3499  N  NE1 . TRP   B  1 10  ? -0.288  -4.395  -27.639  1.00 28.80  ? 311  TRP   B NE1 1 
ATOM   3500  C  CE2 . TRP   B  1 10  ? 0.241   -4.280  -28.899  1.00 31.88  ? 311  TRP   B CE2 1 
ATOM   3501  C  CE3 . TRP   B  1 10  ? 0.874   -2.512  -30.433  1.00 41.79  ? 311  TRP   B CE3 1 
ATOM   3502  C  CZ2 . TRP   B  1 10  ? 0.635   -5.267  -29.800  1.00 35.70  ? 311  TRP   B CZ2 1 
ATOM   3503  C  CZ3 . TRP   B  1 10  ? 1.260   -3.494  -31.332  1.00 44.21  ? 311  TRP   B CZ3 1 
ATOM   3504  C  CH2 . TRP   B  1 10  ? 1.141   -4.854  -31.010  1.00 42.73  ? 311  TRP   B CH2 1 
ATOM   3505  N  N   . GLU   B  1 11  ? 1.301   1.995   -26.343  1.00 30.34  ? 312  GLU   B N   1 
ATOM   3506  C  CA  . GLU   B  1 11  ? 1.547   3.430   -26.351  1.00 38.02  ? 312  GLU   B CA  1 
ATOM   3507  C  C   . GLU   B  1 11  ? 3.038   3.730   -26.220  1.00 37.76  ? 312  GLU   B C   1 
ATOM   3508  O  O   . GLU   B  1 11  ? 3.588   4.521   -26.988  1.00 31.74  ? 312  GLU   B O   1 
ATOM   3509  C  CB  . GLU   B  1 11  ? 0.756   4.089   -25.212  1.00 36.83  ? 312  GLU   B CB  1 
ATOM   3510  C  CG  . GLU   B  1 11  ? 0.640   5.580   -25.310  1.00 40.78  ? 312  GLU   B CG  1 
ATOM   3511  C  CD  . GLU   B  1 11  ? 0.336   6.241   -23.978  1.00 46.41  ? 312  GLU   B CD  1 
ATOM   3512  O  OE1 . GLU   B  1 11  ? -0.407  5.659   -23.153  1.00 43.63  ? 312  GLU   B OE1 1 
ATOM   3513  O  OE2 . GLU   B  1 11  ? 0.856   7.354   -23.752  1.00 52.85  ? 312  GLU   B OE2 1 
ATOM   3514  N  N   . THR   B  1 12  ? 3.707   3.091   -25.267  1.00 36.07  ? 313  THR   B N   1 
ATOM   3515  C  CA  . THR   B  1 12  ? 5.121   3.318   -25.016  1.00 38.08  ? 313  THR   B CA  1 
ATOM   3516  C  C   . THR   B  1 12  ? 6.020   2.275   -25.661  1.00 40.90  ? 313  THR   B C   1 
ATOM   3517  O  O   . THR   B  1 12  ? 7.235   2.490   -25.737  1.00 44.00  ? 313  THR   B O   1 
ATOM   3518  C  CB  . THR   B  1 12  ? 5.388   3.325   -23.510  1.00 35.78  ? 313  THR   B CB  1 
ATOM   3519  O  OG1 . THR   B  1 12  ? 5.102   2.025   -22.988  1.00 32.03  ? 313  THR   B OG1 1 
ATOM   3520  C  CG2 . THR   B  1 12  ? 4.491   4.344   -22.803  1.00 37.88  ? 313  THR   B CG2 1 
ATOM   3521  N  N   . GLU   B  1 13  ? 5.463   1.151   -26.100  1.00 34.53  ? 314  GLU   B N   1 
ATOM   3522  C  CA  . GLU   B  1 13  ? 6.200   -0.003  -26.614  1.00 37.29  ? 314  GLU   B CA  1 
ATOM   3523  C  C   . GLU   B  1 13  ? 7.100   -0.658  -25.566  1.00 33.83  ? 314  GLU   B C   1 
ATOM   3524  O  O   . GLU   B  1 13  ? 7.918   -1.521  -25.912  1.00 38.50  ? 314  GLU   B O   1 
ATOM   3525  C  CB  . GLU   B  1 13  ? 6.997   0.350   -27.875  1.00 38.60  ? 314  GLU   B CB  1 
ATOM   3526  C  CG  . GLU   B  1 13  ? 6.144   0.230   -29.118  1.00 51.83  ? 314  GLU   B CG  1 
ATOM   3527  C  CD  . GLU   B  1 13  ? 6.745   0.909   -30.317  1.00 68.76  ? 314  GLU   B CD  1 
ATOM   3528  O  OE1 . GLU   B  1 13  ? 6.213   0.703   -31.428  1.00 73.09  ? 314  GLU   B OE1 1 
ATOM   3529  O  OE2 . GLU   B  1 13  ? 7.738   1.649   -30.154  1.00 72.60  ? 314  GLU   B OE2 1 
ATOM   3530  N  N   . VAL   B  1 14  ? 6.941   -0.303  -24.288  1.00 37.98  ? 315  VAL   B N   1 
ATOM   3531  C  CA  . VAL   B  1 14  ? 7.605   -1.042  -23.220  1.00 39.38  ? 315  VAL   B CA  1 
ATOM   3532  C  C   . VAL   B  1 14  ? 7.082   -2.468  -23.204  1.00 38.96  ? 315  VAL   B C   1 
ATOM   3533  O  O   . VAL   B  1 14  ? 5.871   -2.705  -23.310  1.00 36.03  ? 315  VAL   B O   1 
ATOM   3534  C  CB  . VAL   B  1 14  ? 7.382   -0.356  -21.865  1.00 40.49  ? 315  VAL   B CB  1 
ATOM   3535  C  CG1 . VAL   B  1 14  ? 7.788   -1.287  -20.720  1.00 34.66  ? 315  VAL   B CG1 1 
ATOM   3536  C  CG2 . VAL   B  1 14  ? 8.142   0.971   -21.791  1.00 40.74  ? 315  VAL   B CG2 1 
ATOM   3537  N  N   . VAL   B  1 15  ? 7.996   -3.430  -23.098  1.00 37.72  ? 316  VAL   B N   1 
ATOM   3538  C  CA  . VAL   B  1 15  ? 7.653   -4.844  -23.034  1.00 36.70  ? 316  VAL   B CA  1 
ATOM   3539  C  C   . VAL   B  1 15  ? 8.135   -5.389  -21.696  1.00 37.29  ? 316  VAL   B C   1 
ATOM   3540  O  O   . VAL   B  1 15  ? 9.293   -5.192  -21.317  1.00 36.69  ? 316  VAL   B O   1 
ATOM   3541  C  CB  . VAL   B  1 15  ? 8.248   -5.639  -24.212  1.00 38.76  ? 316  VAL   B CB  1 
ATOM   3542  C  CG1 . VAL   B  1 15  ? 7.940   -7.124  -24.062  1.00 36.80  ? 316  VAL   B CG1 1 
ATOM   3543  C  CG2 . VAL   B  1 15  ? 7.707   -5.113  -25.545  1.00 29.07  ? 316  VAL   B CG2 1 
ATOM   3544  N  N   . LEU   B  1 16  ? 7.236   -6.043  -20.975  1.00 38.60  ? 317  LEU   B N   1 
ATOM   3545  C  CA  . LEU   B  1 16  ? 7.518   -6.654  -19.686  1.00 36.15  ? 317  LEU   B CA  1 
ATOM   3546  C  C   . LEU   B  1 16  ? 7.382   -8.163  -19.806  1.00 40.69  ? 317  LEU   B C   1 
ATOM   3547  O  O   . LEU   B  1 16  ? 6.648   -8.675  -20.659  1.00 44.36  ? 317  LEU   B O   1 
ATOM   3548  C  CB  . LEU   B  1 16  ? 6.564   -6.144  -18.621  1.00 29.37  ? 317  LEU   B CB  1 
ATOM   3549  C  CG  . LEU   B  1 16  ? 6.482   -4.626  -18.528  1.00 32.15  ? 317  LEU   B CG  1 
ATOM   3550  C  CD1 . LEU   B  1 16  ? 5.305   -4.231  -17.650  1.00 26.68  ? 317  LEU   B CD1 1 
ATOM   3551  C  CD2 . LEU   B  1 16  ? 7.783   -4.052  -17.990  1.00 31.12  ? 317  LEU   B CD2 1 
ATOM   3552  N  N   . THR   B  1 17  ? 8.101   -8.873  -18.948  1.00 31.44  ? 318  THR   B N   1 
ATOM   3553  C  CA  . THR   B  1 17  ? 8.236   -10.315 -19.057  1.00 32.39  ? 318  THR   B CA  1 
ATOM   3554  C  C   . THR   B  1 17  ? 7.699   -10.951 -17.791  1.00 32.08  ? 318  THR   B C   1 
ATOM   3555  O  O   . THR   B  1 17  ? 8.248   -10.739 -16.705  1.00 28.56  ? 318  THR   B O   1 
ATOM   3556  C  CB  . THR   B  1 17  ? 9.695   -10.709 -19.268  1.00 37.88  ? 318  THR   B CB  1 
ATOM   3557  O  OG1 . THR   B  1 17  ? 10.224  -9.996  -20.390  1.00 47.21  ? 318  THR   B OG1 1 
ATOM   3558  C  CG2 . THR   B  1 17  ? 9.778   -12.185 -19.531  1.00 39.56  ? 318  THR   B CG2 1 
ATOM   3559  N  N   . ASP   B  1 18  ? 6.643   -11.737 -17.925  1.00 30.61  ? 319  ASP   B N   1 
ATOM   3560  C  CA  . ASP   B  1 18  ? 5.953   -12.274 -16.765  1.00 31.77  ? 319  ASP   B CA  1 
ATOM   3561  C  C   . ASP   B  1 18  ? 6.413   -13.702 -16.530  1.00 34.58  ? 319  ASP   B C   1 
ATOM   3562  O  O   . ASP   B  1 18  ? 6.182   -14.578 -17.368  1.00 36.20  ? 319  ASP   B O   1 
ATOM   3563  C  CB  . ASP   B  1 18  ? 4.442   -12.215 -16.959  1.00 26.58  ? 319  ASP   B CB  1 
ATOM   3564  C  CG  . ASP   B  1 18  ? 3.674   -12.635 -15.720  1.00 31.76  ? 319  ASP   B CG  1 
ATOM   3565  O  OD1 . ASP   B  1 18  ? 3.828   -13.795 -15.263  1.00 32.79  ? 319  ASP   B OD1 1 
ATOM   3566  O  OD2 . ASP   B  1 18  ? 2.904   -11.793 -15.213  1.00 32.95  ? 319  ASP   B OD2 1 
ATOM   3567  N  N   . THR   B  1 19  ? 7.070   -13.923 -15.398  1.00 34.15  ? 320  THR   B N   1 
ATOM   3568  C  CA  . THR   B  1 19  ? 7.347   -15.259 -14.901  1.00 41.55  ? 320  THR   B CA  1 
ATOM   3569  C  C   . THR   B  1 19  ? 6.456   -15.638 -13.733  1.00 38.19  ? 320  THR   B C   1 
ATOM   3570  O  O   . THR   B  1 19  ? 6.341   -16.829 -13.422  1.00 32.61  ? 320  THR   B O   1 
ATOM   3571  C  CB  . THR   B  1 19  ? 8.806   -15.371 -14.452  1.00 40.67  ? 320  THR   B CB  1 
ATOM   3572  O  OG1 . THR   B  1 19  ? 9.062   -14.377 -13.451  1.00 37.31  ? 320  THR   B OG1 1 
ATOM   3573  C  CG2 . THR   B  1 19  ? 9.729   -15.151 -15.629  1.00 35.38  ? 320  THR   B CG2 1 
ATOM   3574  N  N   . LEU   B  1 20  ? 5.825   -14.651 -13.090  1.00 31.04  ? 321  LEU   B N   1 
ATOM   3575  C  CA  . LEU   B  1 20  ? 5.070   -14.922 -11.873  1.00 25.96  ? 321  LEU   B CA  1 
ATOM   3576  C  C   . LEU   B  1 20  ? 3.851   -15.793 -12.144  1.00 29.51  ? 321  LEU   B C   1 
ATOM   3577  O  O   . LEU   B  1 20  ? 3.390   -16.508 -11.244  1.00 26.69  ? 321  LEU   B O   1 
ATOM   3578  C  CB  . LEU   B  1 20  ? 4.658   -13.608 -11.227  1.00 27.82  ? 321  LEU   B CB  1 
ATOM   3579  C  CG  . LEU   B  1 20  ? 3.867   -13.658 -9.921   1.00 31.39  ? 321  LEU   B CG  1 
ATOM   3580  C  CD1 . LEU   B  1 20  ? 4.625   -14.407 -8.816   1.00 28.99  ? 321  LEU   B CD1 1 
ATOM   3581  C  CD2 . LEU   B  1 20  ? 3.497   -12.242 -9.495   1.00 31.00  ? 321  LEU   B CD2 1 
ATOM   3582  N  N   . HIS   B  1 21  ? 3.329   -15.770 -13.374  1.00 25.38  ? 322  HIS   B N   1 
ATOM   3583  C  CA  . HIS   B  1 21  ? 2.150   -16.564 -13.688  1.00 24.26  ? 322  HIS   B CA  1 
ATOM   3584  C  C   . HIS   B  1 21  ? 2.381   -18.050 -13.478  1.00 31.41  ? 322  HIS   B C   1 
ATOM   3585  O  O   . HIS   B  1 21  ? 1.410   -18.801 -13.339  1.00 29.69  ? 322  HIS   B O   1 
ATOM   3586  C  CB  . HIS   B  1 21  ? 1.723   -16.320 -15.135  1.00 29.41  ? 322  HIS   B CB  1 
ATOM   3587  C  CG  . HIS   B  1 21  ? 2.677   -16.877 -16.135  1.00 31.81  ? 322  HIS   B CG  1 
ATOM   3588  N  ND1 . HIS   B  1 21  ? 3.798   -16.193 -16.553  1.00 37.55  ? 322  HIS   B ND1 1 
ATOM   3589  C  CD2 . HIS   B  1 21  ? 2.692   -18.061 -16.791  1.00 34.97  ? 322  HIS   B CD2 1 
ATOM   3590  C  CE1 . HIS   B  1 21  ? 4.454   -16.925 -17.437  1.00 35.56  ? 322  HIS   B CE1 1 
ATOM   3591  N  NE2 . HIS   B  1 21  ? 3.805   -18.064 -17.598  1.00 36.72  ? 322  HIS   B NE2 1 
ATOM   3592  N  N   . LEU   B  1 22  ? 3.642   -18.494 -13.471  1.00 32.88  ? 323  LEU   B N   1 
ATOM   3593  C  CA  . LEU   B  1 22  ? 3.946   -19.900 -13.230  1.00 36.56  ? 323  LEU   B CA  1 
ATOM   3594  C  C   . LEU   B  1 22  ? 3.610   -20.314 -11.811  1.00 36.83  ? 323  LEU   B C   1 
ATOM   3595  O  O   . LEU   B  1 22  ? 3.437   -21.508 -11.543  1.00 38.21  ? 323  LEU   B O   1 
ATOM   3596  C  CB  . LEU   B  1 22  ? 5.425   -20.175 -13.511  1.00 35.21  ? 323  LEU   B CB  1 
ATOM   3597  C  CG  . LEU   B  1 22  ? 5.874   -19.755 -14.909  1.00 43.80  ? 323  LEU   B CG  1 
ATOM   3598  C  CD1 . LEU   B  1 22  ? 7.394   -19.772 -15.042  1.00 45.23  ? 323  LEU   B CD1 1 
ATOM   3599  C  CD2 . LEU   B  1 22  ? 5.218   -20.649 -15.955  1.00 45.63  ? 323  LEU   B CD2 1 
ATOM   3600  N  N   . LYS   B  1 23  ? 3.511   -19.357 -10.901  1.00 32.83  ? 324  LYS   B N   1 
ATOM   3601  C  CA  . LYS   B  1 23  ? 3.109   -19.644 -9.535   1.00 37.60  ? 324  LYS   B CA  1 
ATOM   3602  C  C   . LYS   B  1 23  ? 1.607   -19.686 -9.366   1.00 44.50  ? 324  LYS   B C   1 
ATOM   3603  O  O   . LYS   B  1 23  ? 1.133   -19.869 -8.242   1.00 48.77  ? 324  LYS   B O   1 
ATOM   3604  C  CB  . LYS   B  1 23  ? 3.691   -18.601 -8.582   1.00 33.11  ? 324  LYS   B CB  1 
ATOM   3605  C  CG  . LYS   B  1 23  ? 5.043   -18.970 -8.018   1.00 49.14  ? 324  LYS   B CG  1 
ATOM   3606  C  CD  . LYS   B  1 23  ? 6.136   -18.843 -9.046   1.00 59.65  ? 324  LYS   B CD  1 
ATOM   3607  C  CE  . LYS   B  1 23  ? 7.168   -19.937 -8.849   1.00 67.76  ? 324  LYS   B CE  1 
ATOM   3608  N  NZ  . LYS   B  1 23  ? 7.389   -20.214 -7.405   1.00 63.51  ? 324  LYS   B NZ  1 
ATOM   3609  N  N   . SER   B  1 24  ? 0.835   -19.518 -10.437  1.00 35.49  ? 325  SER   B N   1 
ATOM   3610  C  CA  . SER   B  1 24  ? -0.594  -19.420 -10.204  1.00 40.04  ? 325  SER   B CA  1 
ATOM   3611  C  C   . SER   B  1 24  ? -1.179  -20.807 -9.975   1.00 43.58  ? 325  SER   B C   1 
ATOM   3612  O  O   . SER   B  1 24  ? -0.588  -21.835 -10.317  1.00 46.60  ? 325  SER   B O   1 
ATOM   3613  C  CB  . SER   B  1 24  ? -1.304  -18.695 -11.346  1.00 34.85  ? 325  SER   B CB  1 
ATOM   3614  O  OG  . SER   B  1 24  ? -1.105  -19.392 -12.560  1.00 51.85  ? 325  SER   B OG  1 
ATOM   3615  N  N   . THR   B  1 25  ? -2.345  -20.816 -9.341   1.00 56.45  ? 326  THR   B N   1 
ATOM   3616  C  CA  . THR   B  1 25  ? -2.841  -21.999 -8.648   1.00 72.98  ? 326  THR   B CA  1 
ATOM   3617  C  C   . THR   B  1 25  ? -4.239  -22.351 -9.116   1.00 71.58  ? 326  THR   B C   1 
ATOM   3618  O  O   . THR   B  1 25  ? -4.497  -23.443 -9.619   1.00 72.54  ? 326  THR   B O   1 
ATOM   3619  C  CB  . THR   B  1 25  ? -2.865  -21.752 -7.136   1.00 77.50  ? 326  THR   B CB  1 
ATOM   3620  O  OG1 . THR   B  1 25  ? -3.229  -20.384 -6.906   1.00 79.45  ? 326  THR   B OG1 1 
ATOM   3621  C  CG2 . THR   B  1 25  ? -1.516  -22.032 -6.485   1.00 73.92  ? 326  THR   B CG2 1 
ATOM   3622  N  N   . LEU   B  1 26  ? -5.134  -21.395 -8.959   1.00 70.18  ? 327  LEU   B N   1 
ATOM   3623  C  CA  . LEU   B  1 26  ? -6.558  -21.566 -9.135   1.00 70.27  ? 327  LEU   B CA  1 
ATOM   3624  C  C   . LEU   B  1 26  ? -6.950  -21.112 -10.529  1.00 63.98  ? 327  LEU   B C   1 
ATOM   3625  O  O   . LEU   B  1 26  ? -6.162  -20.510 -11.257  1.00 65.32  ? 327  LEU   B O   1 
ATOM   3626  C  CB  . LEU   B  1 26  ? -7.262  -20.760 -8.047   1.00 71.72  ? 327  LEU   B CB  1 
ATOM   3627  C  CG  . LEU   B  1 26  ? -6.537  -20.973 -6.699   1.00 65.85  ? 327  LEU   B CG  1 
ATOM   3628  C  CD1 . LEU   B  1 26  ? -6.778  -19.841 -5.669   1.00 64.97  ? 327  LEU   B CD1 1 
ATOM   3629  C  CD2 . LEU   B  1 26  ? -6.903  -22.340 -6.109   1.00 60.12  ? 327  LEU   B CD2 1 
ATOM   3630  N  N   . GLU   B  1 27  ? -8.199  -21.361 -10.873  1.00 58.41  ? 328  GLU   B N   1 
ATOM   3631  C  CA  . GLU   B  1 27  ? -8.636  -21.211 -12.244  1.00 50.00  ? 328  GLU   B CA  1 
ATOM   3632  C  C   . GLU   B  1 27  ? -9.072  -19.783 -12.530  1.00 45.18  ? 328  GLU   B C   1 
ATOM   3633  O  O   . GLU   B  1 27  ? -9.567  -19.076 -11.649  1.00 45.37  ? 328  GLU   B O   1 
ATOM   3634  C  CB  . GLU   B  1 27  ? -9.770  -22.187 -12.537  1.00 54.85  ? 328  GLU   B CB  1 
ATOM   3635  C  CG  . GLU   B  1 27  ? -9.319  -23.639 -12.490  1.00 71.78  ? 328  GLU   B CG  1 
ATOM   3636  C  CD  . GLU   B  1 27  ? -10.439 -24.610 -12.786  1.00 89.10  ? 328  GLU   B CD  1 
ATOM   3637  O  OE1 . GLU   B  1 27  ? -10.402 -25.249 -13.862  1.00 97.96  ? 328  GLU   B OE1 1 
ATOM   3638  O  OE2 . GLU   B  1 27  ? -11.352 -24.738 -11.938  1.00 93.72  ? 328  GLU   B OE2 1 
ATOM   3639  N  N   . THR   B  1 28  ? -8.867  -19.366 -13.781  1.00 40.45  ? 329  THR   B N   1 
ATOM   3640  C  CA  . THR   B  1 28  ? -9.360  -18.086 -14.264  1.00 35.51  ? 329  THR   B CA  1 
ATOM   3641  C  C   . THR   B  1 28  ? -10.809 -18.155 -14.707  1.00 31.41  ? 329  THR   B C   1 
ATOM   3642  O  O   . THR   B  1 28  ? -11.477 -17.119 -14.760  1.00 40.23  ? 329  THR   B O   1 
ATOM   3643  C  CB  . THR   B  1 28  ? -8.525  -17.592 -15.452  1.00 43.45  ? 329  THR   B CB  1 
ATOM   3644  O  OG1 . THR   B  1 28  ? -8.675  -18.487 -16.586  1.00 32.44  ? 329  THR   B OG1 1 
ATOM   3645  C  CG2 . THR   B  1 28  ? -7.063  -17.464 -15.057  1.00 41.42  ? 329  THR   B CG2 1 
ATOM   3646  N  N   . GLY   B  1 29  ? -11.306 -19.345 -15.030  1.00 28.59  ? 330  GLY   B N   1 
ATOM   3647  C  CA  . GLY   B  1 29  ? -12.550 -19.484 -15.741  1.00 35.99  ? 330  GLY   B CA  1 
ATOM   3648  C  C   . GLY   B  1 29  ? -12.380 -19.661 -17.235  1.00 35.59  ? 330  GLY   B C   1 
ATOM   3649  O  O   . GLY   B  1 29  ? -13.268 -20.221 -17.884  1.00 41.30  ? 330  GLY   B O   1 
ATOM   3650  N  N   . CYS   B  1 30  ? -11.262 -19.217 -17.798  1.00 28.58  ? 331  CYS   B N   1 
ATOM   3651  C  CA  . CYS   B  1 30  ? -11.078 -19.425 -19.224  1.00 26.60  ? 331  CYS   B CA  1 
ATOM   3652  C  C   . CYS   B  1 30  ? -10.664 -20.864 -19.497  1.00 32.54  ? 331  CYS   B C   1 
ATOM   3653  O  O   . CYS   B  1 30  ? -10.192 -21.584 -18.621  1.00 36.86  ? 331  CYS   B O   1 
ATOM   3654  C  CB  . CYS   B  1 30  ? -10.027 -18.467 -19.790  1.00 26.29  ? 331  CYS   B CB  1 
ATOM   3655  S  SG  . CYS   B  1 30  ? -10.343 -16.690 -19.509  1.00 27.34  ? 331  CYS   B SG  1 
ATOM   3656  N  N   . THR   B  1 31  ? -10.872 -21.289 -20.727  1.00 30.87  ? 332  THR   B N   1 
ATOM   3657  C  CA  . THR   B  1 31  ? -10.316 -22.528 -21.227  1.00 35.86  ? 332  THR   B CA  1 
ATOM   3658  C  C   . THR   B  1 31  ? -9.364  -22.181 -22.364  1.00 35.73  ? 332  THR   B C   1 
ATOM   3659  O  O   . THR   B  1 31  ? -9.201  -21.014 -22.737  1.00 33.23  ? 332  THR   B O   1 
ATOM   3660  C  CB  . THR   B  1 31  ? -11.410 -23.497 -21.694  1.00 39.27  ? 332  THR   B CB  1 
ATOM   3661  O  OG1 . THR   B  1 31  ? -11.808 -23.162 -23.026  1.00 43.44  ? 332  THR   B OG1 1 
ATOM   3662  C  CG2 . THR   B  1 31  ? -12.637 -23.427 -20.804  1.00 38.82  ? 332  THR   B CG2 1 
ATOM   3663  N  N   . GLU   B  1 32  ? -8.734  -23.210 -22.921  1.00 33.61  ? 333  GLU   B N   1 
ATOM   3664  C  CA  . GLU   B  1 32  ? -7.822  -22.988 -24.031  1.00 41.17  ? 333  GLU   B CA  1 
ATOM   3665  C  C   . GLU   B  1 32  ? -8.546  -22.477 -25.268  1.00 41.69  ? 333  GLU   B C   1 
ATOM   3666  O  O   . GLU   B  1 32  ? -7.914  -21.860 -26.133  1.00 38.35  ? 333  GLU   B O   1 
ATOM   3667  C  CB  . GLU   B  1 32  ? -7.069  -24.281 -24.340  1.00 51.38  ? 333  GLU   B CB  1 
ATOM   3668  C  CG  . GLU   B  1 32  ? -6.144  -24.724 -23.219  1.00 69.81  ? 333  GLU   B CG  1 
ATOM   3669  C  CD  . GLU   B  1 32  ? -5.898  -26.218 -23.222  1.00 86.59  ? 333  GLU   B CD  1 
ATOM   3670  O  OE1 . GLU   B  1 32  ? -6.882  -26.982 -23.123  1.00 91.61  ? 333  GLU   B OE1 1 
ATOM   3671  O  OE2 . GLU   B  1 32  ? -4.724  -26.628 -23.329  1.00 93.28  ? 333  GLU   B OE2 1 
ATOM   3672  N  N   . TYR   B  1 33  ? -9.857  -22.697 -25.364  1.00 28.47  ? 334  TYR   B N   1 
ATOM   3673  C  CA  . TYR   B  1 33  ? -10.605 -22.303 -26.542  1.00 27.37  ? 334  TYR   B CA  1 
ATOM   3674  C  C   . TYR   B  1 33  ? -11.673 -21.264 -26.252  1.00 31.67  ? 334  TYR   B C   1 
ATOM   3675  O  O   . TYR   B  1 33  ? -12.309 -20.778 -27.191  1.00 32.20  ? 334  TYR   B O   1 
ATOM   3676  C  CB  . TYR   B  1 33  ? -11.223 -23.540 -27.203  1.00 34.95  ? 334  TYR   B CB  1 
ATOM   3677  C  CG  . TYR   B  1 33  ? -10.160 -24.450 -27.782  1.00 43.23  ? 334  TYR   B CG  1 
ATOM   3678  C  CD1 . TYR   B  1 33  ? -9.564  -24.160 -29.008  1.00 49.31  ? 334  TYR   B CD1 1 
ATOM   3679  C  CD2 . TYR   B  1 33  ? -9.731  -25.579 -27.098  1.00 46.94  ? 334  TYR   B CD2 1 
ATOM   3680  C  CE1 . TYR   B  1 33  ? -8.577  -24.976 -29.538  1.00 58.02  ? 334  TYR   B CE1 1 
ATOM   3681  C  CE2 . TYR   B  1 33  ? -8.748  -26.402 -27.621  1.00 48.49  ? 334  TYR   B CE2 1 
ATOM   3682  C  CZ  . TYR   B  1 33  ? -8.173  -26.095 -28.842  1.00 59.31  ? 334  TYR   B CZ  1 
ATOM   3683  O  OH  . TYR   B  1 33  ? -7.191  -26.909 -29.369  1.00 68.06  ? 334  TYR   B OH  1 
ATOM   3684  N  N   . ILE   B  1 34  ? -11.890 -20.890 -24.994  1.00 26.01  ? 335  ILE   B N   1 
ATOM   3685  C  CA  . ILE   B  1 34  ? -12.888 -19.875 -24.673  1.00 25.30  ? 335  ILE   B CA  1 
ATOM   3686  C  C   . ILE   B  1 34  ? -12.280 -18.902 -23.677  1.00 32.37  ? 335  ILE   B C   1 
ATOM   3687  O  O   . ILE   B  1 34  ? -11.656 -19.325 -22.699  1.00 33.53  ? 335  ILE   B O   1 
ATOM   3688  C  CB  . ILE   B  1 34  ? -14.183 -20.497 -24.114  1.00 33.93  ? 335  ILE   B CB  1 
ATOM   3689  C  CG1 . ILE   B  1 34  ? -14.722 -21.570 -25.053  1.00 38.39  ? 335  ILE   B CG1 1 
ATOM   3690  C  CG2 . ILE   B  1 34  ? -15.263 -19.449 -23.999  1.00 36.17  ? 335  ILE   B CG2 1 
ATOM   3691  C  CD1 . ILE   B  1 34  ? -14.882 -22.931 -24.424  1.00 51.89  ? 335  ILE   B CD1 1 
ATOM   3692  N  N   . CYS   B  1 35  ? -12.437 -17.602 -23.926  1.00 26.91  ? 336  CYS   B N   1 
ATOM   3693  C  CA  . CYS   B  1 35  ? -12.034 -16.591 -22.963  1.00 22.44  ? 336  CYS   B CA  1 
ATOM   3694  C  C   . CYS   B  1 35  ? -13.266 -16.066 -22.250  1.00 28.06  ? 336  CYS   B C   1 
ATOM   3695  O  O   . CYS   B  1 35  ? -14.242 -15.678 -22.898  1.00 29.40  ? 336  CYS   B O   1 
ATOM   3696  C  CB  . CYS   B  1 35  ? -11.287 -15.430 -23.615  1.00 23.32  ? 336  CYS   B CB  1 
ATOM   3697  S  SG  . CYS   B  1 35  ? -10.759 -14.185 -22.405  1.00 28.48  ? 336  CYS   B SG  1 
ATOM   3698  N  N   . MET   B  1 36  ? -13.209 -16.050 -20.918  1.00 27.14  ? 337  MET   B N   1 
ATOM   3699  C  CA  . MET   B  1 36  ? -14.295 -15.573 -20.071  1.00 27.72  ? 337  MET   B CA  1 
ATOM   3700  C  C   . MET   B  1 36  ? -13.857 -14.348 -19.283  1.00 28.19  ? 337  MET   B C   1 
ATOM   3701  O  O   . MET   B  1 36  ? -14.373 -14.065 -18.189  1.00 24.49  ? 337  MET   B O   1 
ATOM   3702  C  CB  . MET   B  1 36  ? -14.777 -16.688 -19.146  1.00 35.54  ? 337  MET   B CB  1 
ATOM   3703  C  CG  . MET   B  1 36  ? -15.210 -17.917 -19.912  1.00 41.82  ? 337  MET   B CG  1 
ATOM   3704  S  SD  . MET   B  1 36  ? -16.417 -18.948 -19.075  1.00 51.05  ? 337  MET   B SD  1 
ATOM   3705  C  CE  . MET   B  1 36  ? -15.956 -18.669 -17.374  1.00 49.50  ? 337  MET   B CE  1 
ATOM   3706  N  N   . GLY   B  1 37  ? -12.902 -13.607 -19.851  1.00 24.06  ? 338  GLY   B N   1 
ATOM   3707  C  CA  . GLY   B  1 37  ? -12.315 -12.465 -19.177  1.00 24.12  ? 338  GLY   B CA  1 
ATOM   3708  C  C   . GLY   B  1 37  ? -13.296 -11.375 -18.806  1.00 27.91  ? 338  GLY   B C   1 
ATOM   3709  O  O   . GLY   B  1 37  ? -12.993 -10.572 -17.919  1.00 33.22  ? 338  GLY   B O   1 
ATOM   3710  N  N   . SER   B  1 38  ? -14.463 -11.315 -19.457  1.00 23.67  ? 339  SER   B N   1 
ATOM   3711  C  CA  . SER   B  1 38  ? -15.460 -10.311 -19.095  1.00 28.34  ? 339  SER   B CA  1 
ATOM   3712  C  C   . SER   B  1 38  ? -16.587 -10.881 -18.255  1.00 33.18  ? 339  SER   B C   1 
ATOM   3713  O  O   . SER   B  1 38  ? -17.541 -10.159 -17.957  1.00 30.21  ? 339  SER   B O   1 
ATOM   3714  C  CB  . SER   B  1 38  ? -16.053 -9.637  -20.342  1.00 22.14  ? 339  SER   B CB  1 
ATOM   3715  O  OG  . SER   B  1 38  ? -16.906 -10.508 -21.062  1.00 27.94  ? 339  SER   B OG  1 
ATOM   3716  N  N   . ILE   B  1 39  ? -16.510 -12.158 -17.886  1.00 28.99  ? 340  ILE   B N   1 
ATOM   3717  C  CA  . ILE   B  1 39  ? -17.478 -12.738 -16.965  1.00 29.76  ? 340  ILE   B CA  1 
ATOM   3718  C  C   . ILE   B  1 39  ? -17.196 -12.223 -15.564  1.00 22.36  ? 340  ILE   B C   1 
ATOM   3719  O  O   . ILE   B  1 39  ? -16.053 -12.277 -15.095  1.00 26.13  ? 340  ILE   B O   1 
ATOM   3720  C  CB  . ILE   B  1 39  ? -17.402 -14.267 -17.004  1.00 34.94  ? 340  ILE   B CB  1 
ATOM   3721  C  CG1 . ILE   B  1 39  ? -17.615 -14.756 -18.436  1.00 35.88  ? 340  ILE   B CG1 1 
ATOM   3722  C  CG2 . ILE   B  1 39  ? -18.393 -14.871 -16.003  1.00 31.61  ? 340  ILE   B CG2 1 
ATOM   3723  C  CD1 . ILE   B  1 39  ? -18.940 -14.379 -18.996  1.00 37.24  ? 340  ILE   B CD1 1 
ATOM   3724  N  N   . MET   B  1 40  ? -18.238 -11.744 -14.882  1.00 24.40  ? 341  MET   B N   1 
ATOM   3725  C  CA  . MET   B  1 40  ? -18.048 -11.132 -13.562  1.00 28.79  ? 341  MET   B CA  1 
ATOM   3726  C  C   . MET   B  1 40  ? -17.640 -12.163 -12.509  1.00 28.15  ? 341  MET   B C   1 
ATOM   3727  O  O   . MET   B  1 40  ? -16.667 -11.958 -11.774  1.00 29.83  ? 341  MET   B O   1 
ATOM   3728  C  CB  . MET   B  1 40  ? -19.321 -10.407 -13.128  1.00 32.19  ? 341  MET   B CB  1 
ATOM   3729  C  CG  . MET   B  1 40  ? -19.191 -9.664  -11.802  1.00 50.98  ? 341  MET   B CG  1 
ATOM   3730  S  SD  . MET   B  1 40  ? -19.047 -7.887  -12.057  1.00 60.68  ? 341  MET   B SD  1 
ATOM   3731  C  CE  . MET   B  1 40  ? -20.515 -7.554  -13.022  1.00 39.44  ? 341  MET   B CE  1 
ATOM   3732  N  N   . HIS   B  1 41  ? -18.382 -13.267 -12.406  1.00 32.55  ? 342  HIS   B N   1 
ATOM   3733  C  CA  . HIS   B  1 41  ? -18.081 -14.363 -11.482  1.00 41.20  ? 342  HIS   B CA  1 
ATOM   3734  C  C   . HIS   B  1 41  ? -17.943 -15.638 -12.307  1.00 44.99  ? 342  HIS   B C   1 
ATOM   3735  O  O   . HIS   B  1 41  ? -18.913 -16.397 -12.448  1.00 42.72  ? 342  HIS   B O   1 
ATOM   3736  C  CB  . HIS   B  1 41  ? -19.167 -14.565 -10.419  1.00 48.25  ? 342  HIS   B CB  1 
ATOM   3737  C  CG  . HIS   B  1 41  ? -19.693 -13.302 -9.806   1.00 70.52  ? 342  HIS   B CG  1 
ATOM   3738  N  ND1 . HIS   B  1 41  ? -18.977 -12.561 -8.888   1.00 77.36  ? 342  HIS   B ND1 1 
ATOM   3739  C  CD2 . HIS   B  1 41  ? -20.884 -12.670 -9.948   1.00 75.54  ? 342  HIS   B CD2 1 
ATOM   3740  C  CE1 . HIS   B  1 41  ? -19.693 -11.516 -8.512   1.00 75.57  ? 342  HIS   B CE1 1 
ATOM   3741  N  NE2 . HIS   B  1 41  ? -20.856 -11.559 -9.138   1.00 72.97  ? 342  HIS   B NE2 1 
ATOM   3742  N  N   . PRO   B  1 42  ? -16.772 -15.906 -12.873  1.00 48.39  ? 343  PRO   B N   1 
ATOM   3743  C  CA  . PRO   B  1 42  ? -16.583 -17.132 -13.656  1.00 53.50  ? 343  PRO   B CA  1 
ATOM   3744  C  C   . PRO   B  1 42  ? -16.387 -18.329 -12.728  1.00 67.17  ? 343  PRO   B C   1 
ATOM   3745  O  O   . PRO   B  1 42  ? -16.396 -18.191 -11.503  1.00 70.83  ? 343  PRO   B O   1 
ATOM   3746  C  CB  . PRO   B  1 42  ? -15.338 -16.833 -14.494  1.00 46.33  ? 343  PRO   B CB  1 
ATOM   3747  C  CG  . PRO   B  1 42  ? -14.585 -15.821 -13.716  1.00 47.64  ? 343  PRO   B CG  1 
ATOM   3748  C  CD  . PRO   B  1 42  ? -15.585 -15.032 -12.906  1.00 50.40  ? 343  PRO   B CD  1 
ATOM   3749  N  N   . SER   B  1 43  ? -16.198 -19.499 -13.351  1.00 75.10  ? 344  SER   B N   1 
ATOM   3750  C  CA  . SER   B  1 43  ? -16.193 -20.849 -12.744  1.00 82.91  ? 344  SER   B CA  1 
ATOM   3751  C  C   . SER   B  1 43  ? -17.613 -21.409 -12.719  1.00 86.05  ? 344  SER   B C   1 
ATOM   3752  O  O   . SER   B  1 43  ? -17.850 -22.503 -12.206  1.00 89.74  ? 344  SER   B O   1 
ATOM   3753  C  CB  . SER   B  1 43  ? -15.597 -20.877 -11.326  1.00 84.37  ? 344  SER   B CB  1 
ATOM   3754  O  OG  . SER   B  1 43  ? -16.506 -20.349 -10.369  1.00 83.83  ? 344  SER   B OG  1 
ATOM   3755  N  N   . ASP   B  1 51  ? -17.928 -28.630 1.881    1.00 77.73  ? 352  ASP   B N   1 
ATOM   3756  C  CA  . ASP   B  1 51  ? -18.274 -27.279 2.310    1.00 81.40  ? 352  ASP   B CA  1 
ATOM   3757  C  C   . ASP   B  1 51  ? -17.030 -26.523 2.800    1.00 80.32  ? 352  ASP   B C   1 
ATOM   3758  O  O   . ASP   B  1 51  ? -16.847 -25.342 2.484    1.00 78.77  ? 352  ASP   B O   1 
ATOM   3759  C  CB  . ASP   B  1 51  ? -19.353 -27.332 3.401    1.00 86.03  ? 352  ASP   B CB  1 
ATOM   3760  C  CG  . ASP   B  1 51  ? -19.983 -25.969 3.681    1.00 91.12  ? 352  ASP   B CG  1 
ATOM   3761  O  OD1 . ASP   B  1 51  ? -20.120 -25.612 4.873    1.00 83.98  ? 352  ASP   B OD1 1 
ATOM   3762  O  OD2 . ASP   B  1 51  ? -20.337 -25.255 2.713    1.00 95.45  ? 352  ASP   B OD2 1 
ATOM   3763  N  N   . VAL   B  1 52  ? -16.183 -27.211 3.573    1.00 72.02  ? 353  VAL   B N   1 
ATOM   3764  C  CA  . VAL   B  1 52  ? -14.921 -26.666 4.060    1.00 64.72  ? 353  VAL   B CA  1 
ATOM   3765  C  C   . VAL   B  1 52  ? -13.822 -27.688 3.805    1.00 59.32  ? 353  VAL   B C   1 
ATOM   3766  O  O   . VAL   B  1 52  ? -14.069 -28.895 3.729    1.00 62.26  ? 353  VAL   B O   1 
ATOM   3767  C  CB  . VAL   B  1 52  ? -14.958 -26.288 5.563    1.00 66.42  ? 353  VAL   B CB  1 
ATOM   3768  C  CG1 . VAL   B  1 52  ? -16.050 -25.268 5.842    1.00 67.57  ? 353  VAL   B CG1 1 
ATOM   3769  C  CG2 . VAL   B  1 52  ? -15.129 -27.533 6.443    1.00 58.04  ? 353  VAL   B CG2 1 
ATOM   3770  N  N   . ALA   B  1 53  ? -12.593 -27.185 3.710    1.00 54.14  ? 354  ALA   B N   1 
ATOM   3771  C  CA  . ALA   B  1 53  ? -11.466 -27.999 3.268    1.00 54.80  ? 354  ALA   B CA  1 
ATOM   3772  C  C   . ALA   B  1 53  ? -11.203 -29.167 4.212    1.00 54.92  ? 354  ALA   B C   1 
ATOM   3773  O  O   . ALA   B  1 53  ? -11.221 -29.020 5.437    1.00 53.08  ? 354  ALA   B O   1 
ATOM   3774  C  CB  . ALA   B  1 53  ? -10.212 -27.134 3.147    1.00 52.38  ? 354  ALA   B CB  1 
ATOM   3775  N  N   . THR   B  1 54  ? -10.958 -30.337 3.633    1.00 60.25  ? 355  THR   B N   1 
ATOM   3776  C  CA  . THR   B  1 54  ? -10.575 -31.493 4.426    1.00 66.95  ? 355  THR   B CA  1 
ATOM   3777  C  C   . THR   B  1 54  ? -9.149  -31.324 4.946    1.00 64.67  ? 355  THR   B C   1 
ATOM   3778  O  O   . THR   B  1 54  ? -8.419  -30.401 4.565    1.00 58.77  ? 355  THR   B O   1 
ATOM   3779  C  CB  . THR   B  1 54  ? -10.680 -32.770 3.597    1.00 68.24  ? 355  THR   B CB  1 
ATOM   3780  O  OG1 . THR   B  1 54  ? -9.720  -32.722 2.534    1.00 68.22  ? 355  THR   B OG1 1 
ATOM   3781  C  CG2 . THR   B  1 54  ? -12.075 -32.902 3.006    1.00 73.30  ? 355  THR   B CG2 1 
ATOM   3782  N  N   . LYS   B  1 55  ? -8.754  -32.239 5.833    1.00 62.96  ? 356  LYS   B N   1 
ATOM   3783  C  CA  . LYS   B  1 55  ? -7.383  -32.241 6.330    1.00 57.03  ? 356  LYS   B CA  1 
ATOM   3784  C  C   . LYS   B  1 55  ? -6.388  -32.358 5.185    1.00 58.24  ? 356  LYS   B C   1 
ATOM   3785  O  O   . LYS   B  1 55  ? -5.388  -31.632 5.140    1.00 56.96  ? 356  LYS   B O   1 
ATOM   3786  C  CB  . LYS   B  1 55  ? -7.177  -33.388 7.315    1.00 52.75  ? 356  LYS   B CB  1 
ATOM   3787  C  CG  . LYS   B  1 55  ? -7.386  -33.035 8.756    1.00 45.63  ? 356  LYS   B CG  1 
ATOM   3788  C  CD  . LYS   B  1 55  ? -7.076  -34.251 9.617    1.00 46.15  ? 356  LYS   B CD  1 
ATOM   3789  C  CE  . LYS   B  1 55  ? -7.627  -34.078 11.016   1.00 55.41  ? 356  LYS   B CE  1 
ATOM   3790  N  NZ  . LYS   B  1 55  ? -7.336  -35.263 11.866   1.00 62.90  ? 356  LYS   B NZ  1 
ATOM   3791  N  N   . ASP   B  1 56  ? -6.650  -33.276 4.249    1.00 57.00  ? 357  ASP   B N   1 
ATOM   3792  C  CA  . ASP   B  1 56  ? -5.702  -33.544 3.170    1.00 61.33  ? 357  ASP   B CA  1 
ATOM   3793  C  C   . ASP   B  1 56  ? -5.571  -32.354 2.233    1.00 56.43  ? 357  ASP   B C   1 
ATOM   3794  O  O   . ASP   B  1 56  ? -4.478  -32.072 1.731    1.00 56.35  ? 357  ASP   B O   1 
ATOM   3795  C  CB  . ASP   B  1 56  ? -6.126  -34.789 2.391    1.00 65.63  ? 357  ASP   B CB  1 
ATOM   3796  C  CG  . ASP   B  1 56  ? -5.694  -36.069 3.070    1.00 72.50  ? 357  ASP   B CG  1 
ATOM   3797  O  OD1 . ASP   B  1 56  ? -5.234  -36.000 4.233    1.00 71.88  ? 357  ASP   B OD1 1 
ATOM   3798  O  OD2 . ASP   B  1 56  ? -5.801  -37.140 2.437    1.00 79.00  ? 357  ASP   B OD2 1 
ATOM   3799  N  N   . GLN   B  1 57  ? -6.672  -31.652 1.975    1.00 47.24  ? 358  GLN   B N   1 
ATOM   3800  C  CA  . GLN   B  1 57  ? -6.599  -30.457 1.147    1.00 45.28  ? 358  GLN   B CA  1 
ATOM   3801  C  C   . GLN   B  1 57  ? -5.850  -29.331 1.845    1.00 43.58  ? 358  GLN   B C   1 
ATOM   3802  O  O   . GLN   B  1 57  ? -5.213  -28.506 1.176    1.00 35.64  ? 358  GLN   B O   1 
ATOM   3803  C  CB  . GLN   B  1 57  ? -8.004  -29.994 0.774    1.00 50.64  ? 358  GLN   B CB  1 
ATOM   3804  C  CG  . GLN   B  1 57  ? -8.805  -31.008 -0.030   1.00 56.90  ? 358  GLN   B CG  1 
ATOM   3805  C  CD  . GLN   B  1 57  ? -10.248 -30.585 -0.208   1.00 60.43  ? 358  GLN   B CD  1 
ATOM   3806  O  OE1 . GLN   B  1 57  ? -10.886 -30.102 0.729    1.00 61.06  ? 358  GLN   B OE1 1 
ATOM   3807  N  NE2 . GLN   B  1 57  ? -10.768 -30.750 -1.417   1.00 63.63  ? 358  GLN   B NE2 1 
ATOM   3808  N  N   . LEU   B  1 58  ? -5.907  -29.276 3.181    1.00 34.96  ? 359  LEU   B N   1 
ATOM   3809  C  CA  . LEU   B  1 58  ? -5.394  -28.100 3.874    1.00 37.89  ? 359  LEU   B CA  1 
ATOM   3810  C  C   . LEU   B  1 58  ? -3.871  -28.110 3.966    1.00 35.17  ? 359  LEU   B C   1 
ATOM   3811  O  O   . LEU   B  1 58  ? -3.243  -27.052 3.853    1.00 39.41  ? 359  LEU   B O   1 
ATOM   3812  C  CB  . LEU   B  1 58  ? -6.020  -27.987 5.272    1.00 38.07  ? 359  LEU   B CB  1 
ATOM   3813  C  CG  . LEU   B  1 58  ? -5.785  -26.668 6.006    1.00 35.38  ? 359  LEU   B CG  1 
ATOM   3814  C  CD1 . LEU   B  1 58  ? -6.157  -25.469 5.123    1.00 45.27  ? 359  LEU   B CD1 1 
ATOM   3815  C  CD2 . LEU   B  1 58  ? -6.556  -26.630 7.317    1.00 40.30  ? 359  LEU   B CD2 1 
ATOM   3816  N  N   . PHE   B  1 59  ? -3.261  -29.287 4.160    1.00 37.28  ? 360  PHE   B N   1 
ATOM   3817  C  CA  . PHE   B  1 59  ? -1.811  -29.401 4.310    1.00 47.19  ? 360  PHE   B CA  1 
ATOM   3818  C  C   . PHE   B  1 59  ? -1.064  -28.680 3.189    1.00 43.76  ? 360  PHE   B C   1 
ATOM   3819  O  O   . PHE   B  1 59  ? -0.288  -27.759 3.476    1.00 45.85  ? 360  PHE   B O   1 
ATOM   3820  C  CB  . PHE   B  1 59  ? -1.351  -30.862 4.341    1.00 55.05  ? 360  PHE   B CB  1 
ATOM   3821  C  CG  . PHE   B  1 59  ? -1.745  -31.621 5.572    1.00 66.49  ? 360  PHE   B CG  1 
ATOM   3822  C  CD1 . PHE   B  1 59  ? -1.265  -31.260 6.820    1.00 66.92  ? 360  PHE   B CD1 1 
ATOM   3823  C  CD2 . PHE   B  1 59  ? -2.545  -32.751 5.468    1.00 69.09  ? 360  PHE   B CD2 1 
ATOM   3824  C  CE1 . PHE   B  1 59  ? -1.611  -31.992 7.950    1.00 63.37  ? 360  PHE   B CE1 1 
ATOM   3825  C  CE2 . PHE   B  1 59  ? -2.895  -33.479 6.587    1.00 68.47  ? 360  PHE   B CE2 1 
ATOM   3826  C  CZ  . PHE   B  1 59  ? -2.430  -33.096 7.828    1.00 63.81  ? 360  PHE   B CZ  1 
ATOM   3827  N  N   . PRO   B  1 60  ? -1.251  -29.053 1.915    1.00 44.45  ? 361  PRO   B N   1 
ATOM   3828  C  CA  . PRO   B  1 60  ? -0.453  -28.402 0.864    1.00 36.57  ? 361  PRO   B CA  1 
ATOM   3829  C  C   . PRO   B  1 60  ? -0.739  -26.928 0.720    1.00 34.39  ? 361  PRO   B C   1 
ATOM   3830  O  O   . PRO   B  1 60  ? 0.176   -26.169 0.383    1.00 33.27  ? 361  PRO   B O   1 
ATOM   3831  C  CB  . PRO   B  1 60  ? -0.846  -29.168 -0.403   1.00 42.25  ? 361  PRO   B CB  1 
ATOM   3832  C  CG  . PRO   B  1 60  ? -2.203  -29.631 -0.138   1.00 44.59  ? 361  PRO   B CG  1 
ATOM   3833  C  CD  . PRO   B  1 60  ? -2.223  -29.992 1.322    1.00 44.14  ? 361  PRO   B CD  1 
ATOM   3834  N  N   . LEU   B  1 61  ? -1.983  -26.495 0.938    1.00 31.85  ? 362  LEU   B N   1 
ATOM   3835  C  CA  . LEU   B  1 61  ? -2.274  -25.067 0.872    1.00 30.97  ? 362  LEU   B CA  1 
ATOM   3836  C  C   . LEU   B  1 61  ? -1.517  -24.329 1.959    1.00 33.35  ? 362  LEU   B C   1 
ATOM   3837  O  O   . LEU   B  1 61  ? -0.899  -23.286 1.713    1.00 31.90  ? 362  LEU   B O   1 
ATOM   3838  C  CB  . LEU   B  1 61  ? -3.775  -24.830 1.006    1.00 34.19  ? 362  LEU   B CB  1 
ATOM   3839  C  CG  . LEU   B  1 61  ? -4.621  -25.446 -0.111   1.00 39.79  ? 362  LEU   B CG  1 
ATOM   3840  C  CD1 . LEU   B  1 61  ? -6.099  -25.298 0.215    1.00 38.73  ? 362  LEU   B CD1 1 
ATOM   3841  C  CD2 . LEU   B  1 61  ? -4.291  -24.771 -1.421   1.00 34.32  ? 362  LEU   B CD2 1 
ATOM   3842  N  N   . ALA   B  1 62  ? -1.560  -24.869 3.177    1.00 31.11  ? 363  ALA   B N   1 
ATOM   3843  C  CA  . ALA   B  1 62  ? -0.812  -24.291 4.281    1.00 30.15  ? 363  ALA   B CA  1 
ATOM   3844  C  C   . ALA   B  1 62  ? 0.674   -24.280 3.967    1.00 35.01  ? 363  ALA   B C   1 
ATOM   3845  O  O   . ALA   B  1 62  ? 1.346   -23.256 4.127    1.00 28.45  ? 363  ALA   B O   1 
ATOM   3846  C  CB  . ALA   B  1 62  ? -1.099  -25.073 5.562    1.00 26.35  ? 363  ALA   B CB  1 
ATOM   3847  N  N   . LYS   B  1 63  ? 1.200   -25.408 3.488    1.00 38.69  ? 364  LYS   B N   1 
ATOM   3848  C  CA  . LYS   B  1 63  ? 2.626   -25.475 3.200    1.00 39.02  ? 364  LYS   B CA  1 
ATOM   3849  C  C   . LYS   B  1 63  ? 3.032   -24.408 2.194    1.00 35.70  ? 364  LYS   B C   1 
ATOM   3850  O  O   . LYS   B  1 63  ? 4.016   -23.691 2.402    1.00 37.87  ? 364  LYS   B O   1 
ATOM   3851  C  CB  . LYS   B  1 63  ? 3.008   -26.859 2.689    1.00 38.31  ? 364  LYS   B CB  1 
ATOM   3852  C  CG  . LYS   B  1 63  ? 4.500   -26.973 2.408    1.00 37.60  ? 364  LYS   B CG  1 
ATOM   3853  C  CD  . LYS   B  1 63  ? 4.862   -28.312 1.828    1.00 46.35  ? 364  LYS   B CD  1 
ATOM   3854  C  CE  . LYS   B  1 63  ? 6.349   -28.578 1.994    1.00 57.33  ? 364  LYS   B CE  1 
ATOM   3855  N  NZ  . LYS   B  1 63  ? 7.184   -27.564 1.285    1.00 60.05  ? 364  LYS   B NZ  1 
ATOM   3856  N  N   . GLU   B  1 64  ? 2.276   -24.274 1.101    1.00 29.69  ? 365  GLU   B N   1 
ATOM   3857  C  CA  . GLU   B  1 64  ? 2.668   -23.311 0.078    1.00 31.06  ? 365  GLU   B CA  1 
ATOM   3858  C  C   . GLU   B  1 64  ? 2.667   -21.903 0.643    1.00 30.37  ? 365  GLU   B C   1 
ATOM   3859  O  O   . GLU   B  1 64  ? 3.588   -21.122 0.383    1.00 27.37  ? 365  GLU   B O   1 
ATOM   3860  C  CB  . GLU   B  1 64  ? 1.757   -23.399 -1.150   1.00 39.17  ? 365  GLU   B CB  1 
ATOM   3861  C  CG  . GLU   B  1 64  ? 2.514   -23.678 -2.460   1.00 64.86  ? 365  GLU   B CG  1 
ATOM   3862  C  CD  . GLU   B  1 64  ? 3.359   -22.497 -2.962   1.00 84.07  ? 365  GLU   B CD  1 
ATOM   3863  O  OE1 . GLU   B  1 64  ? 4.216   -21.977 -2.211   1.00 89.22  ? 365  GLU   B OE1 1 
ATOM   3864  O  OE2 . GLU   B  1 64  ? 3.168   -22.090 -4.129   1.00 90.98  ? 365  GLU   B OE2 1 
ATOM   3865  N  N   . PHE   B  1 65  ? 1.664   -21.572 1.457    1.00 28.46  ? 366  PHE   B N   1 
ATOM   3866  C  CA  . PHE   B  1 65  ? 1.646   -20.242 2.050    1.00 29.34  ? 366  PHE   B CA  1 
ATOM   3867  C  C   . PHE   B  1 65  ? 2.818   -20.042 3.000    1.00 27.74  ? 366  PHE   B C   1 
ATOM   3868  O  O   . PHE   B  1 65  ? 3.512   -19.019 2.936    1.00 26.57  ? 366  PHE   B O   1 
ATOM   3869  C  CB  . PHE   B  1 65  ? 0.334   -19.990 2.773    1.00 27.54  ? 366  PHE   B CB  1 
ATOM   3870  C  CG  . PHE   B  1 65  ? 0.358   -18.755 3.590    1.00 29.34  ? 366  PHE   B CG  1 
ATOM   3871  C  CD1 . PHE   B  1 65  ? 0.294   -17.513 2.977    1.00 31.35  ? 366  PHE   B CD1 1 
ATOM   3872  C  CD2 . PHE   B  1 65  ? 0.486   -18.826 4.966    1.00 25.51  ? 366  PHE   B CD2 1 
ATOM   3873  C  CE1 . PHE   B  1 65  ? 0.339   -16.358 3.728    1.00 29.58  ? 366  PHE   B CE1 1 
ATOM   3874  C  CE2 . PHE   B  1 65  ? 0.526   -17.673 5.729    1.00 32.36  ? 366  PHE   B CE2 1 
ATOM   3875  C  CZ  . PHE   B  1 65  ? 0.455   -16.441 5.113    1.00 31.12  ? 366  PHE   B CZ  1 
ATOM   3876  N  N   . ILE   B  1 66  ? 3.051   -21.001 3.900    1.00 28.04  ? 367  ILE   B N   1 
ATOM   3877  C  CA  . ILE   B  1 66  ? 4.140   -20.835 4.859    1.00 30.78  ? 367  ILE   B CA  1 
ATOM   3878  C  C   . ILE   B  1 66  ? 5.474   -20.786 4.125    1.00 33.71  ? 367  ILE   B C   1 
ATOM   3879  O  O   . ILE   B  1 66  ? 6.371   -20.011 4.482    1.00 32.15  ? 367  ILE   B O   1 
ATOM   3880  C  CB  . ILE   B  1 66  ? 4.100   -21.952 5.918    1.00 31.58  ? 367  ILE   B CB  1 
ATOM   3881  C  CG1 . ILE   B  1 66  ? 2.807   -21.859 6.719    1.00 31.92  ? 367  ILE   B CG1 1 
ATOM   3882  C  CG2 . ILE   B  1 66  ? 5.307   -21.865 6.854    1.00 30.16  ? 367  ILE   B CG2 1 
ATOM   3883  C  CD1 . ILE   B  1 66  ? 2.730   -20.611 7.589    1.00 35.10  ? 367  ILE   B CD1 1 
ATOM   3884  N  N   . ASP   B  1 67  ? 5.613   -21.586 3.065    1.00 29.46  ? 368  ASP   B N   1 
ATOM   3885  C  CA  . ASP   B  1 67  ? 6.816   -21.507 2.240    1.00 32.06  ? 368  ASP   B CA  1 
ATOM   3886  C  C   . ASP   B  1 67  ? 6.970   -20.121 1.638    1.00 28.50  ? 368  ASP   B C   1 
ATOM   3887  O  O   . ASP   B  1 67  ? 8.075   -19.572 1.590    1.00 29.71  ? 368  ASP   B O   1 
ATOM   3888  C  CB  . ASP   B  1 67  ? 6.777   -22.549 1.117    1.00 31.99  ? 368  ASP   B CB  1 
ATOM   3889  C  CG  . ASP   B  1 67  ? 7.049   -23.952 1.605    1.00 34.92  ? 368  ASP   B CG  1 
ATOM   3890  O  OD1 . ASP   B  1 67  ? 7.420   -24.143 2.789    1.00 36.67  ? 368  ASP   B OD1 1 
ATOM   3891  O  OD2 . ASP   B  1 67  ? 6.895   -24.873 0.783    1.00 33.71  ? 368  ASP   B OD2 1 
ATOM   3892  N  N   . GLN   B  1 68  ? 5.881   -19.535 1.158    1.00 25.20  ? 369  GLN   B N   1 
ATOM   3893  C  CA  . GLN   B  1 68  ? 6.079   -18.248 0.514    1.00 32.28  ? 369  GLN   B CA  1 
ATOM   3894  C  C   . GLN   B  1 68  ? 6.255   -17.144 1.545    1.00 33.46  ? 369  GLN   B C   1 
ATOM   3895  O  O   . GLN   B  1 68  ? 7.011   -16.196 1.309    1.00 34.97  ? 369  GLN   B O   1 
ATOM   3896  C  CB  . GLN   B  1 68  ? 4.940   -17.954 -0.464   1.00 40.20  ? 369  GLN   B CB  1 
ATOM   3897  C  CG  . GLN   B  1 68  ? 3.662   -17.476 0.140    1.00 51.86  ? 369  GLN   B CG  1 
ATOM   3898  C  CD  . GLN   B  1 68  ? 2.727   -16.919 -0.914   1.00 54.36  ? 369  GLN   B CD  1 
ATOM   3899  O  OE1 . GLN   B  1 68  ? 2.425   -15.721 -0.926   1.00 44.73  ? 369  GLN   B OE1 1 
ATOM   3900  N  NE2 . GLN   B  1 68  ? 2.271   -17.788 -1.816   1.00 59.07  ? 369  GLN   B NE2 1 
ATOM   3901  N  N   . TYR   B  1 69  ? 5.636   -17.278 2.718    1.00 29.03  ? 370  TYR   B N   1 
ATOM   3902  C  CA  . TYR   B  1 69  ? 5.919   -16.324 3.784    1.00 32.04  ? 370  TYR   B CA  1 
ATOM   3903  C  C   . TYR   B  1 69  ? 7.391   -16.362 4.174    1.00 31.91  ? 370  TYR   B C   1 
ATOM   3904  O  O   . TYR   B  1 69  ? 8.028   -15.318 4.352    1.00 35.17  ? 370  TYR   B O   1 
ATOM   3905  C  CB  . TYR   B  1 69  ? 5.048   -16.596 5.005    1.00 28.40  ? 370  TYR   B CB  1 
ATOM   3906  C  CG  . TYR   B  1 69  ? 5.502   -15.761 6.171    1.00 34.83  ? 370  TYR   B CG  1 
ATOM   3907  C  CD1 . TYR   B  1 69  ? 5.188   -14.410 6.234    1.00 42.25  ? 370  TYR   B CD1 1 
ATOM   3908  C  CD2 . TYR   B  1 69  ? 6.286   -16.305 7.185    1.00 26.38  ? 370  TYR   B CD2 1 
ATOM   3909  C  CE1 . TYR   B  1 69  ? 5.614   -13.627 7.289    1.00 35.87  ? 370  TYR   B CE1 1 
ATOM   3910  C  CE2 . TYR   B  1 69  ? 6.721   -15.523 8.244    1.00 33.24  ? 370  TYR   B CE2 1 
ATOM   3911  C  CZ  . TYR   B  1 69  ? 6.379   -14.183 8.287    1.00 35.74  ? 370  TYR   B CZ  1 
ATOM   3912  O  OH  . TYR   B  1 69  ? 6.795   -13.387 9.332    1.00 43.64  ? 370  TYR   B OH  1 
ATOM   3913  N  N   . TYR   B  1 70  ? 7.952   -17.559 4.319    1.00 27.94  ? 371  TYR   B N   1 
ATOM   3914  C  CA  . TYR   B  1 70  ? 9.336   -17.634 4.763    1.00 29.04  ? 371  TYR   B CA  1 
ATOM   3915  C  C   . TYR   B  1 70  ? 10.310  -17.269 3.660    1.00 30.76  ? 371  TYR   B C   1 
ATOM   3916  O  O   . TYR   B  1 70  ? 11.390  -16.735 3.941    1.00 37.26  ? 371  TYR   B O   1 
ATOM   3917  C  CB  . TYR   B  1 70  ? 9.622   -19.017 5.324    1.00 29.04  ? 371  TYR   B CB  1 
ATOM   3918  C  CG  . TYR   B  1 70  ? 9.243   -19.030 6.774    1.00 27.99  ? 371  TYR   B CG  1 
ATOM   3919  C  CD1 . TYR   B  1 70  ? 7.969   -19.405 7.171    1.00 28.11  ? 371  TYR   B CD1 1 
ATOM   3920  C  CD2 . TYR   B  1 70  ? 10.130  -18.580 7.733    1.00 28.64  ? 371  TYR   B CD2 1 
ATOM   3921  C  CE1 . TYR   B  1 70  ? 7.609   -19.388 8.492    1.00 38.08  ? 371  TYR   B CE1 1 
ATOM   3922  C  CE2 . TYR   B  1 70  ? 9.782   -18.558 9.067    1.00 33.83  ? 371  TYR   B CE2 1 
ATOM   3923  C  CZ  . TYR   B  1 70  ? 8.521   -18.961 9.442    1.00 39.33  ? 371  TYR   B CZ  1 
ATOM   3924  O  OH  . TYR   B  1 70  ? 8.155   -18.947 10.765   1.00 37.07  ? 371  TYR   B OH  1 
ATOM   3925  N  N   . SER   B  1 71  ? 9.943   -17.535 2.412    1.00 27.08  ? 372  SER   B N   1 
ATOM   3926  C  CA  . SER   B  1 71  ? 10.728  -17.046 1.288    1.00 42.20  ? 372  SER   B CA  1 
ATOM   3927  C  C   . SER   B  1 71  ? 10.728  -15.522 1.237    1.00 45.19  ? 372  SER   B C   1 
ATOM   3928  O  O   . SER   B  1 71  ? 11.773  -14.906 1.005    1.00 48.75  ? 372  SER   B O   1 
ATOM   3929  C  CB  . SER   B  1 71  ? 10.188  -17.637 -0.011   1.00 34.39  ? 372  SER   B CB  1 
ATOM   3930  O  OG  . SER   B  1 71  ? 11.183  -17.604 -1.018   1.00 54.14  ? 372  SER   B OG  1 
ATOM   3931  N  N   . SER   B  1 72  ? 9.569   -14.896 1.477    1.00 41.44  ? 373  SER   B N   1 
ATOM   3932  C  CA  . SER   B  1 72  ? 9.476   -13.436 1.429    1.00 41.76  ? 373  SER   B CA  1 
ATOM   3933  C  C   . SER   B  1 72  ? 10.396  -12.765 2.440    1.00 46.21  ? 373  SER   B C   1 
ATOM   3934  O  O   . SER   B  1 72  ? 10.893  -11.662 2.189    1.00 48.59  ? 373  SER   B O   1 
ATOM   3935  C  CB  . SER   B  1 72  ? 8.049   -12.991 1.702    1.00 38.75  ? 373  SER   B CB  1 
ATOM   3936  O  OG  . SER   B  1 72  ? 7.816   -13.003 3.105    1.00 39.08  ? 373  SER   B OG  1 
ATOM   3937  N  N   . ILE   B  1 73  ? 10.613  -13.394 3.588    1.00 46.26  ? 374  ILE   B N   1 
ATOM   3938  C  CA  . ILE   B  1 73  ? 11.444  -12.832 4.632    1.00 44.63  ? 374  ILE   B CA  1 
ATOM   3939  C  C   . ILE   B  1 73  ? 12.849  -13.440 4.627    1.00 45.16  ? 374  ILE   B C   1 
ATOM   3940  O  O   . ILE   B  1 73  ? 13.564  -13.348 5.624    1.00 48.65  ? 374  ILE   B O   1 
ATOM   3941  C  CB  . ILE   B  1 73  ? 10.781  -12.972 6.008    1.00 44.45  ? 374  ILE   B CB  1 
ATOM   3942  C  CG1 . ILE   B  1 73  ? 10.691  -14.441 6.432    1.00 40.59  ? 374  ILE   B CG1 1 
ATOM   3943  C  CG2 . ILE   B  1 73  ? 9.399   -12.318 5.991    1.00 39.36  ? 374  ILE   B CG2 1 
ATOM   3944  C  CD1 . ILE   B  1 73  ? 10.411  -14.632 7.942    1.00 39.19  ? 374  ILE   B CD1 1 
ATOM   3945  N  N   . LYS   B  1 74  ? 13.253  -14.054 3.513    1.00 50.32  ? 375  LYS   B N   1 
ATOM   3946  C  CA  . LYS   B  1 74  ? 14.597  -14.621 3.346    1.00 50.94  ? 375  LYS   B CA  1 
ATOM   3947  C  C   . LYS   B  1 74  ? 14.940  -15.586 4.475    1.00 45.70  ? 375  LYS   B C   1 
ATOM   3948  O  O   . LYS   B  1 74  ? 16.045  -15.574 5.018    1.00 47.34  ? 375  LYS   B O   1 
ATOM   3949  C  CB  . LYS   B  1 74  ? 15.654  -13.521 3.237    1.00 57.02  ? 375  LYS   B CB  1 
ATOM   3950  C  CG  . LYS   B  1 74  ? 15.325  -12.425 2.239    1.00 59.34  ? 375  LYS   B CG  1 
ATOM   3951  C  CD  . LYS   B  1 74  ? 14.978  -12.990 0.869    1.00 67.69  ? 375  LYS   B CD  1 
ATOM   3952  C  CE  . LYS   B  1 74  ? 14.661  -11.876 -0.130   1.00 68.48  ? 375  LYS   B CE  1 
ATOM   3953  N  NZ  . LYS   B  1 74  ? 13.659  -12.303 -1.149   1.00 69.45  ? 375  LYS   B NZ  1 
ATOM   3954  N  N   . ARG   B  1 75  ? 13.967  -16.414 4.850    1.00 43.99  ? 376  ARG   B N   1 
ATOM   3955  C  CA  . ARG   B  1 75  ? 14.162  -17.443 5.865    1.00 42.48  ? 376  ARG   B CA  1 
ATOM   3956  C  C   . ARG   B  1 75  ? 13.729  -18.809 5.350    1.00 37.63  ? 376  ARG   B C   1 
ATOM   3957  O  O   . ARG   B  1 75  ? 13.411  -19.702 6.148    1.00 37.86  ? 376  ARG   B O   1 
ATOM   3958  C  CB  . ARG   B  1 75  ? 13.404  -17.103 7.154    1.00 44.69  ? 376  ARG   B CB  1 
ATOM   3959  C  CG  . ARG   B  1 75  ? 13.900  -15.865 7.866    1.00 45.65  ? 376  ARG   B CG  1 
ATOM   3960  C  CD  . ARG   B  1 75  ? 15.329  -16.036 8.349    1.00 55.14  ? 376  ARG   B CD  1 
ATOM   3961  N  NE  . ARG   B  1 75  ? 15.692  -14.983 9.296    1.00 56.58  ? 376  ARG   B NE  1 
ATOM   3962  C  CZ  . ARG   B  1 75  ? 16.188  -13.802 8.936    1.00 53.04  ? 376  ARG   B CZ  1 
ATOM   3963  N  NH1 . ARG   B  1 75  ? 16.479  -12.898 9.863    1.00 44.75  ? 376  ARG   B NH1 1 
ATOM   3964  N  NH2 . ARG   B  1 75  ? 16.398  -13.530 7.647    1.00 45.83  ? 376  ARG   B NH2 1 
ATOM   3965  N  N   . PHE   B  1 76  ? 13.685  -18.982 4.034    1.00 35.75  ? 377  PHE   B N   1 
ATOM   3966  C  CA  . PHE   B  1 76  ? 13.276  -20.261 3.482    1.00 38.09  ? 377  PHE   B CA  1 
ATOM   3967  C  C   . PHE   B  1 76  ? 14.263  -21.334 3.916    1.00 41.16  ? 377  PHE   B C   1 
ATOM   3968  O  O   . PHE   B  1 76  ? 15.479  -21.135 3.874    1.00 46.27  ? 377  PHE   B O   1 
ATOM   3969  C  CB  . PHE   B  1 76  ? 13.194  -20.188 1.956    1.00 37.22  ? 377  PHE   B CB  1 
ATOM   3970  C  CG  . PHE   B  1 76  ? 12.515  -21.369 1.339    1.00 34.18  ? 377  PHE   B CG  1 
ATOM   3971  C  CD1 . PHE   B  1 76  ? 11.144  -21.386 1.177    1.00 38.90  ? 377  PHE   B CD1 1 
ATOM   3972  C  CD2 . PHE   B  1 76  ? 13.248  -22.470 0.936    1.00 40.74  ? 377  PHE   B CD2 1 
ATOM   3973  C  CE1 . PHE   B  1 76  ? 10.517  -22.476 0.619    1.00 40.12  ? 377  PHE   B CE1 1 
ATOM   3974  C  CE2 . PHE   B  1 76  ? 12.626  -23.560 0.372    1.00 42.64  ? 377  PHE   B CE2 1 
ATOM   3975  C  CZ  . PHE   B  1 76  ? 11.259  -23.564 0.215    1.00 39.55  ? 377  PHE   B CZ  1 
ATOM   3976  N  N   . GLY   B  1 77  ? 13.734  -22.469 4.360    1.00 37.20  ? 378  GLY   B N   1 
ATOM   3977  C  CA  . GLY   B  1 77  ? 14.581  -23.539 4.851    1.00 40.06  ? 378  GLY   B CA  1 
ATOM   3978  C  C   . GLY   B  1 77  ? 15.171  -23.306 6.223    1.00 43.15  ? 378  GLY   B C   1 
ATOM   3979  O  O   . GLY   B  1 77  ? 15.854  -24.194 6.743    1.00 49.46  ? 378  GLY   B O   1 
ATOM   3980  N  N   . SER   B  1 78  ? 14.937  -22.143 6.826    1.00 43.87  ? 379  SER   B N   1 
ATOM   3981  C  CA  . SER   B  1 78  ? 15.462  -21.877 8.153    1.00 47.34  ? 379  SER   B CA  1 
ATOM   3982  C  C   . SER   B  1 78  ? 14.866  -22.849 9.164    1.00 50.08  ? 379  SER   B C   1 
ATOM   3983  O  O   . SER   B  1 78  ? 13.879  -23.547 8.903    1.00 41.14  ? 379  SER   B O   1 
ATOM   3984  C  CB  . SER   B  1 78  ? 15.165  -20.441 8.575    1.00 42.37  ? 379  SER   B CB  1 
ATOM   3985  O  OG  . SER   B  1 78  ? 13.770  -20.216 8.640    1.00 39.46  ? 379  SER   B OG  1 
ATOM   3986  N  N   . LYS   B  1 79  ? 15.498  -22.900 10.336   1.00 49.37  ? 380  LYS   B N   1 
ATOM   3987  C  CA  . LYS   B  1 79  ? 14.948  -23.705 11.416   1.00 44.06  ? 380  LYS   B CA  1 
ATOM   3988  C  C   . LYS   B  1 79  ? 13.552  -23.220 11.787   1.00 39.82  ? 380  LYS   B C   1 
ATOM   3989  O  O   . LYS   B  1 79  ? 12.635  -24.029 11.963   1.00 41.36  ? 380  LYS   B O   1 
ATOM   3990  C  CB  . LYS   B  1 79  ? 15.879  -23.668 12.629   1.00 53.92  ? 380  LYS   B CB  1 
ATOM   3991  C  CG  . LYS   B  1 79  ? 15.912  -24.969 13.427   1.00 66.42  ? 380  LYS   B CG  1 
ATOM   3992  C  CD  . LYS   B  1 79  ? 15.829  -24.729 14.938   1.00 75.45  ? 380  LYS   B CD  1 
ATOM   3993  C  CE  . LYS   B  1 79  ? 17.009  -23.923 15.478   1.00 78.43  ? 380  LYS   B CE  1 
ATOM   3994  N  NZ  . LYS   B  1 79  ? 18.076  -24.801 16.034   1.00 81.67  ? 380  LYS   B NZ  1 
ATOM   3995  N  N   . ALA   B  1 80  ? 13.365  -21.898 11.870   1.00 36.62  ? 381  ALA   B N   1 
ATOM   3996  C  CA  . ALA   B  1 80  ? 12.044  -21.349 12.165   1.00 42.23  ? 381  ALA   B CA  1 
ATOM   3997  C  C   . ALA   B  1 80  ? 11.035  -21.711 11.080   1.00 42.72  ? 381  ALA   B C   1 
ATOM   3998  O  O   . ALA   B  1 80  ? 9.866   -21.984 11.374   1.00 45.44  ? 381  ALA   B O   1 
ATOM   3999  C  CB  . ALA   B  1 80  ? 12.128  -19.831 12.326   1.00 39.91  ? 381  ALA   B CB  1 
ATOM   4000  N  N   . HIS   B  1 81  ? 11.463  -21.702 9.819    1.00 36.94  ? 382  HIS   B N   1 
ATOM   4001  C  CA  . HIS   B  1 81  ? 10.580  -22.138 8.743    1.00 32.26  ? 382  HIS   B CA  1 
ATOM   4002  C  C   . HIS   B  1 81  ? 10.140  -23.582 8.957    1.00 32.48  ? 382  HIS   B C   1 
ATOM   4003  O  O   . HIS   B  1 81  ? 8.946   -23.898 8.890    1.00 35.04  ? 382  HIS   B O   1 
ATOM   4004  C  CB  . HIS   B  1 81  ? 11.289  -21.975 7.394    1.00 33.76  ? 382  HIS   B CB  1 
ATOM   4005  C  CG  . HIS   B  1 81  ? 10.475  -22.409 6.215    1.00 31.68  ? 382  HIS   B CG  1 
ATOM   4006  N  ND1 . HIS   B  1 81  ? 11.018  -22.563 4.956    1.00 34.42  ? 382  HIS   B ND1 1 
ATOM   4007  C  CD2 . HIS   B  1 81  ? 9.161   -22.718 6.098    1.00 30.35  ? 382  HIS   B CD2 1 
ATOM   4008  C  CE1 . HIS   B  1 81  ? 10.075  -22.949 4.116    1.00 31.12  ? 382  HIS   B CE1 1 
ATOM   4009  N  NE2 . HIS   B  1 81  ? 8.938   -23.047 4.781    1.00 35.10  ? 382  HIS   B NE2 1 
ATOM   4010  N  N   . MET   B  1 82  ? 11.096  -24.470 9.237    1.00 35.50  ? 383  MET   B N   1 
ATOM   4011  C  CA  . MET   B  1 82  ? 10.775  -25.884 9.382    1.00 40.89  ? 383  MET   B CA  1 
ATOM   4012  C  C   . MET   B  1 82  ? 9.935   -26.141 10.630   1.00 37.19  ? 383  MET   B C   1 
ATOM   4013  O  O   . MET   B  1 82  ? 9.008   -26.960 10.605   1.00 40.54  ? 383  MET   B O   1 
ATOM   4014  C  CB  . MET   B  1 82  ? 12.065  -26.709 9.398    1.00 39.44  ? 383  MET   B CB  1 
ATOM   4015  C  CG  . MET   B  1 82  ? 12.808  -26.675 8.068    1.00 50.82  ? 383  MET   B CG  1 
ATOM   4016  S  SD  . MET   B  1 82  ? 11.868  -27.434 6.706    1.00 59.74  ? 383  MET   B SD  1 
ATOM   4017  C  CE  . MET   B  1 82  ? 11.977  -26.168 5.456    1.00 58.61  ? 383  MET   B CE  1 
ATOM   4018  N  N   . GLU   B  1 83  ? 10.223  -25.443 11.727   1.00 37.92  ? 384  GLU   B N   1 
ATOM   4019  C  CA  . GLU   B  1 83  ? 9.417   -25.638 12.929   1.00 38.27  ? 384  GLU   B CA  1 
ATOM   4020  C  C   . GLU   B  1 83  ? 8.001   -25.123 12.727   1.00 33.91  ? 384  GLU   B C   1 
ATOM   4021  O  O   . GLU   B  1 83  ? 7.042   -25.708 13.246   1.00 37.30  ? 384  GLU   B O   1 
ATOM   4022  C  CB  . GLU   B  1 83  ? 10.074  -24.957 14.125   1.00 45.32  ? 384  GLU   B CB  1 
ATOM   4023  C  CG  . GLU   B  1 83  ? 10.937  -25.897 14.931   1.00 57.70  ? 384  GLU   B CG  1 
ATOM   4024  C  CD  . GLU   B  1 83  ? 12.018  -25.178 15.689   1.00 66.80  ? 384  GLU   B CD  1 
ATOM   4025  O  OE1 . GLU   B  1 83  ? 11.872  -23.957 15.920   1.00 71.74  ? 384  GLU   B OE1 1 
ATOM   4026  O  OE2 . GLU   B  1 83  ? 13.018  -25.837 16.043   1.00 71.27  ? 384  GLU   B OE2 1 
ATOM   4027  N  N   . ARG   B  1 84  ? 7.849   -24.032 11.977   1.00 32.92  ? 385  ARG   B N   1 
ATOM   4028  C  CA  . ARG   B  1 84  ? 6.513   -23.529 11.682   1.00 35.03  ? 385  ARG   B CA  1 
ATOM   4029  C  C   . ARG   B  1 84  ? 5.719   -24.539 10.859   1.00 35.04  ? 385  ARG   B C   1 
ATOM   4030  O  O   . ARG   B  1 84  ? 4.538   -24.785 11.136   1.00 35.11  ? 385  ARG   B O   1 
ATOM   4031  C  CB  . ARG   B  1 84  ? 6.614   -22.185 10.962   1.00 29.71  ? 385  ARG   B CB  1 
ATOM   4032  C  CG  . ARG   B  1 84  ? 5.274   -21.515 10.675   1.00 30.36  ? 385  ARG   B CG  1 
ATOM   4033  C  CD  . ARG   B  1 84  ? 4.467   -21.314 11.949   1.00 30.91  ? 385  ARG   B CD  1 
ATOM   4034  N  NE  . ARG   B  1 84  ? 3.159   -20.745 11.653   1.00 31.42  ? 385  ARG   B NE  1 
ATOM   4035  C  CZ  . ARG   B  1 84  ? 2.065   -20.958 12.372   1.00 34.10  ? 385  ARG   B CZ  1 
ATOM   4036  N  NH1 . ARG   B  1 84  ? 2.114   -21.730 13.461   1.00 33.70  ? 385  ARG   B NH1 1 
ATOM   4037  N  NH2 . ARG   B  1 84  ? 0.919   -20.397 12.000   1.00 25.44  ? 385  ARG   B NH2 1 
ATOM   4038  N  N   . LEU   B  1 85  ? 6.355   -25.151 9.855    1.00 35.33  ? 386  LEU   B N   1 
ATOM   4039  C  CA  . LEU   B  1 85  ? 5.676   -26.188 9.079    1.00 38.57  ? 386  LEU   B CA  1 
ATOM   4040  C  C   . LEU   B  1 85  ? 5.278   -27.357 9.969    1.00 43.98  ? 386  LEU   B C   1 
ATOM   4041  O  O   . LEU   B  1 85  ? 4.140   -27.838 9.915    1.00 41.63  ? 386  LEU   B O   1 
ATOM   4042  C  CB  . LEU   B  1 85  ? 6.570   -26.670 7.948    1.00 41.25  ? 386  LEU   B CB  1 
ATOM   4043  C  CG  . LEU   B  1 85  ? 6.597   -25.812 6.690    1.00 41.17  ? 386  LEU   B CG  1 
ATOM   4044  C  CD1 . LEU   B  1 85  ? 7.606   -26.404 5.729    1.00 39.91  ? 386  LEU   B CD1 1 
ATOM   4045  C  CD2 . LEU   B  1 85  ? 5.212   -25.743 6.064    1.00 38.24  ? 386  LEU   B CD2 1 
ATOM   4046  N  N   . GLU   B  1 86  ? 6.222   -27.831 10.786   1.00 42.89  ? 387  GLU   B N   1 
ATOM   4047  C  CA  . GLU   B  1 86  ? 5.935   -28.861 11.775   1.00 49.57  ? 387  GLU   B CA  1 
ATOM   4048  C  C   . GLU   B  1 86  ? 4.730   -28.473 12.614   1.00 43.95  ? 387  GLU   B C   1 
ATOM   4049  O  O   . GLU   B  1 86  ? 3.764   -29.234 12.738   1.00 39.29  ? 387  GLU   B O   1 
ATOM   4050  C  CB  . GLU   B  1 86  ? 7.166   -29.050 12.659   1.00 58.72  ? 387  GLU   B CB  1 
ATOM   4051  C  CG  . GLU   B  1 86  ? 7.363   -30.411 13.245   1.00 75.08  ? 387  GLU   B CG  1 
ATOM   4052  C  CD  . GLU   B  1 86  ? 8.726   -30.532 13.901   1.00 89.97  ? 387  GLU   B CD  1 
ATOM   4053  O  OE1 . GLU   B  1 86  ? 8.946   -29.887 14.950   1.00 94.82  ? 387  GLU   B OE1 1 
ATOM   4054  O  OE2 . GLU   B  1 86  ? 9.587   -31.251 13.353   1.00 97.11  ? 387  GLU   B OE2 1 
ATOM   4055  N  N   . GLU   B  1 87  ? 4.764   -27.258 13.163   1.00 41.84  ? 388  GLU   B N   1 
ATOM   4056  C  CA  . GLU   B  1 87  ? 3.701   -26.787 14.040   1.00 40.08  ? 388  GLU   B CA  1 
ATOM   4057  C  C   . GLU   B  1 87  ? 2.362   -26.707 13.313   1.00 42.51  ? 388  GLU   B C   1 
ATOM   4058  O  O   . GLU   B  1 87  ? 1.331   -27.137 13.849   1.00 35.60  ? 388  GLU   B O   1 
ATOM   4059  C  CB  . GLU   B  1 87  ? 4.087   -25.425 14.614   1.00 41.87  ? 388  GLU   B CB  1 
ATOM   4060  C  CG  . GLU   B  1 87  ? 3.047   -24.821 15.519   1.00 43.45  ? 388  GLU   B CG  1 
ATOM   4061  C  CD  . GLU   B  1 87  ? 3.446   -23.451 16.018   1.00 54.47  ? 388  GLU   B CD  1 
ATOM   4062  O  OE1 . GLU   B  1 87  ? 3.905   -22.626 15.197   1.00 52.87  ? 388  GLU   B OE1 1 
ATOM   4063  O  OE2 . GLU   B  1 87  ? 3.305   -23.204 17.236   1.00 61.70  ? 388  GLU   B OE2 1 
ATOM   4064  N  N   . VAL   B  1 88  ? 2.355   -26.135 12.095   1.00 31.46  ? 389  VAL   B N   1 
ATOM   4065  C  CA  . VAL   B  1 88  ? 1.118   -26.028 11.321   1.00 34.71  ? 389  VAL   B CA  1 
ATOM   4066  C  C   . VAL   B  1 88  ? 0.535   -27.409 11.075   1.00 42.16  ? 389  VAL   B C   1 
ATOM   4067  O  O   . VAL   B  1 88  ? -0.668  -27.640 11.256   1.00 42.04  ? 389  VAL   B O   1 
ATOM   4068  C  CB  . VAL   B  1 88  ? 1.363   -25.290 9.988    1.00 34.58  ? 389  VAL   B CB  1 
ATOM   4069  C  CG1 . VAL   B  1 88  ? 0.230   -25.573 9.018    1.00 27.85  ? 389  VAL   B CG1 1 
ATOM   4070  C  CG2 . VAL   B  1 88  ? 1.502   -23.792 10.209   1.00 32.47  ? 389  VAL   B CG2 1 
ATOM   4071  N  N   . ASN   B  1 89  ? 1.385   -28.347 10.660   1.00 43.14  ? 390  ASN   B N   1 
ATOM   4072  C  CA  . ASN   B  1 89  ? 0.943   -29.711 10.407   1.00 39.68  ? 390  ASN   B CA  1 
ATOM   4073  C  C   . ASN   B  1 89  ? 0.328   -30.351 11.646   1.00 38.75  ? 390  ASN   B C   1 
ATOM   4074  O  O   . ASN   B  1 89  ? -0.686  -31.050 11.542   1.00 40.38  ? 390  ASN   B O   1 
ATOM   4075  C  CB  . ASN   B  1 89  ? 2.120   -30.531 9.902    1.00 49.73  ? 390  ASN   B CB  1 
ATOM   4076  C  CG  . ASN   B  1 89  ? 2.079   -30.726 8.416    1.00 64.65  ? 390  ASN   B CG  1 
ATOM   4077  O  OD1 . ASN   B  1 89  ? 2.103   -31.859 7.938    1.00 72.98  ? 390  ASN   B OD1 1 
ATOM   4078  N  ND2 . ASN   B  1 89  ? 1.977   -29.621 7.666    1.00 63.32  ? 390  ASN   B ND2 1 
ATOM   4079  N  N   . LYS   B  1 90  ? 0.922   -30.121 12.822   1.00 37.44  ? 391  LYS   B N   1 
ATOM   4080  C  CA  . LYS   B  1 90  ? 0.352   -30.636 14.067   1.00 49.78  ? 391  LYS   B CA  1 
ATOM   4081  C  C   . LYS   B  1 90  ? -1.080  -30.160 14.254   1.00 45.18  ? 391  LYS   B C   1 
ATOM   4082  O  O   . LYS   B  1 90  ? -1.970  -30.950 14.593   1.00 44.86  ? 391  LYS   B O   1 
ATOM   4083  C  CB  . LYS   B  1 90  ? 1.172   -30.193 15.285   1.00 59.14  ? 391  LYS   B CB  1 
ATOM   4084  C  CG  . LYS   B  1 90  ? 2.603   -30.663 15.379   1.00 69.85  ? 391  LYS   B CG  1 
ATOM   4085  C  CD  . LYS   B  1 90  ? 3.245   -30.089 16.647   1.00 76.79  ? 391  LYS   B CD  1 
ATOM   4086  C  CE  . LYS   B  1 90  ? 4.763   -30.057 16.548   1.00 79.90  ? 391  LYS   B CE  1 
ATOM   4087  N  NZ  . LYS   B  1 90  ? 5.299   -31.371 16.101   1.00 80.72  ? 391  LYS   B NZ  1 
ATOM   4088  N  N   . GLU   B  1 91  ? -1.307  -28.852 14.096   1.00 36.63  ? 392  GLU   B N   1 
ATOM   4089  C  CA  . GLU   B  1 91  ? -2.645  -28.307 14.311   1.00 38.09  ? 392  GLU   B CA  1 
ATOM   4090  C  C   . GLU   B  1 91  ? -3.636  -28.847 13.290   1.00 38.45  ? 392  GLU   B C   1 
ATOM   4091  O  O   . GLU   B  1 91  ? -4.788  -29.133 13.631   1.00 43.36  ? 392  GLU   B O   1 
ATOM   4092  C  CB  . GLU   B  1 91  ? -2.629  -26.780 14.250   1.00 35.78  ? 392  GLU   B CB  1 
ATOM   4093  C  CG  . GLU   B  1 91  ? -1.633  -26.108 15.135   1.00 38.25  ? 392  GLU   B CG  1 
ATOM   4094  C  CD  . GLU   B  1 91  ? -1.904  -24.624 15.266   1.00 47.37  ? 392  GLU   B CD  1 
ATOM   4095  O  OE1 . GLU   B  1 91  ? -3.060  -24.206 15.048   1.00 49.42  ? 392  GLU   B OE1 1 
ATOM   4096  O  OE2 . GLU   B  1 91  ? -0.961  -23.877 15.591   1.00 56.50  ? 392  GLU   B OE2 1 
ATOM   4097  N  N   . ILE   B  1 92  ? -3.228  -28.960 12.026   1.00 38.23  ? 393  ILE   B N   1 
ATOM   4098  C  CA  . ILE   B  1 92  ? -4.122  -29.535 11.027   1.00 39.37  ? 393  ILE   B CA  1 
ATOM   4099  C  C   . ILE   B  1 92  ? -4.449  -30.975 11.390   1.00 44.40  ? 393  ILE   B C   1 
ATOM   4100  O  O   . ILE   B  1 92  ? -5.608  -31.399 11.337   1.00 56.16  ? 393  ILE   B O   1 
ATOM   4101  C  CB  . ILE   B  1 92  ? -3.506  -29.432 9.622    1.00 36.26  ? 393  ILE   B CB  1 
ATOM   4102  C  CG1 . ILE   B  1 92  ? -3.279  -27.960 9.254    1.00 37.78  ? 393  ILE   B CG1 1 
ATOM   4103  C  CG2 . ILE   B  1 92  ? -4.401  -30.149 8.592    1.00 36.49  ? 393  ILE   B CG2 1 
ATOM   4104  C  CD1 . ILE   B  1 92  ? -2.597  -27.750 7.929    1.00 36.42  ? 393  ILE   B CD1 1 
ATOM   4105  N  N   . ASP   B  1 93  ? -3.429  -31.748 11.771   1.00 44.70  ? 394  ASP   B N   1 
ATOM   4106  C  CA  . ASP   B  1 93  ? -3.644  -33.138 12.169   1.00 50.03  ? 394  ASP   B CA  1 
ATOM   4107  C  C   . ASP   B  1 93  ? -4.606  -33.243 13.344   1.00 44.30  ? 394  ASP   B C   1 
ATOM   4108  O  O   . ASP   B  1 93  ? -5.537  -34.054 13.327   1.00 50.89  ? 394  ASP   B O   1 
ATOM   4109  C  CB  . ASP   B  1 93  ? -2.312  -33.796 12.525   1.00 60.71  ? 394  ASP   B CB  1 
ATOM   4110  C  CG  . ASP   B  1 93  ? -1.865  -34.794 11.489   1.00 77.01  ? 394  ASP   B CG  1 
ATOM   4111  O  OD1 . ASP   B  1 93  ? -1.653  -34.382 10.333   1.00 83.78  ? 394  ASP   B OD1 1 
ATOM   4112  O  OD2 . ASP   B  1 93  ? -1.725  -35.988 11.824   1.00 82.50  ? 394  ASP   B OD2 1 
ATOM   4113  N  N   . THR   B  1 94  ? -4.397  -32.431 14.375   1.00 44.80  ? 395  THR   B N   1 
ATOM   4114  C  CA  . THR   B  1 94  ? -5.146  -32.571 15.616   1.00 50.87  ? 395  THR   B CA  1 
ATOM   4115  C  C   . THR   B  1 94  ? -6.441  -31.769 15.649   1.00 52.78  ? 395  THR   B C   1 
ATOM   4116  O  O   . THR   B  1 94  ? -7.363  -32.138 16.385   1.00 62.42  ? 395  THR   B O   1 
ATOM   4117  C  CB  . THR   B  1 94  ? -4.274  -32.151 16.801   1.00 59.99  ? 395  THR   B CB  1 
ATOM   4118  O  OG1 . THR   B  1 94  ? -3.838  -30.800 16.609   1.00 60.82  ? 395  THR   B OG1 1 
ATOM   4119  C  CG2 . THR   B  1 94  ? -3.059  -33.061 16.919   1.00 64.26  ? 395  THR   B CG2 1 
ATOM   4120  N  N   . THR   B  1 95  ? -6.540  -30.673 14.894   1.00 48.43  ? 396  THR   B N   1 
ATOM   4121  C  CA  . THR   B  1 95  ? -7.694  -29.783 14.986   1.00 45.11  ? 396  THR   B CA  1 
ATOM   4122  C  C   . THR   B  1 95  ? -8.430  -29.606 13.668   1.00 46.76  ? 396  THR   B C   1 
ATOM   4123  O  O   . THR   B  1 95  ? -9.473  -28.945 13.647   1.00 54.22  ? 396  THR   B O   1 
ATOM   4124  C  CB  . THR   B  1 95  ? -7.275  -28.397 15.506   1.00 45.70  ? 396  THR   B CB  1 
ATOM   4125  O  OG1 . THR   B  1 95  ? -6.639  -27.662 14.450   1.00 45.11  ? 396  THR   B OG1 1 
ATOM   4126  C  CG2 . THR   B  1 95  ? -6.309  -28.516 16.700   1.00 41.68  ? 396  THR   B CG2 1 
ATOM   4127  N  N   . SER   B  1 96  ? -7.920  -30.170 12.576   1.00 44.34  ? 397  SER   B N   1 
ATOM   4128  C  CA  . SER   B  1 96  ? -8.441  -30.033 11.219   1.00 46.93  ? 397  SER   B CA  1 
ATOM   4129  C  C   . SER   B  1 96  ? -8.329  -28.617 10.687   1.00 45.04  ? 397  SER   B C   1 
ATOM   4130  O  O   . SER   B  1 96  ? -8.932  -28.303 9.661    1.00 39.81  ? 397  SER   B O   1 
ATOM   4131  C  CB  . SER   B  1 96  ? -9.892  -30.506 11.104   1.00 57.22  ? 397  SER   B CB  1 
ATOM   4132  O  OG  . SER   B  1 96  ? -9.947  -31.921 11.119   1.00 62.72  ? 397  SER   B OG  1 
ATOM   4133  N  N   . THR   B  1 97  ? -7.571  -27.756 11.352   1.00 44.89  ? 398  THR   B N   1 
ATOM   4134  C  CA  . THR   B  1 97  ? -7.314  -26.404 10.874   1.00 36.81  ? 398  THR   B CA  1 
ATOM   4135  C  C   . THR   B  1 97  ? -6.058  -25.909 11.575   1.00 35.39  ? 398  THR   B C   1 
ATOM   4136  O  O   . THR   B  1 97  ? -5.377  -26.673 12.264   1.00 39.95  ? 398  THR   B O   1 
ATOM   4137  C  CB  . THR   B  1 97  ? -8.515  -25.488 11.129   1.00 35.00  ? 398  THR   B CB  1 
ATOM   4138  O  OG1 . THR   B  1 97  ? -8.281  -24.212 10.516   1.00 39.01  ? 398  THR   B OG1 1 
ATOM   4139  C  CG2 . THR   B  1 97  ? -8.753  -25.319 12.634   1.00 28.34  ? 398  THR   B CG2 1 
ATOM   4140  N  N   . TYR   B  1 98  ? -5.733  -24.634 11.391   1.00 31.40  ? 399  TYR   B N   1 
ATOM   4141  C  CA  . TYR   B  1 98  ? -4.595  -24.064 12.093   1.00 34.98  ? 399  TYR   B CA  1 
ATOM   4142  C  C   . TYR   B  1 98  ? -4.813  -22.572 12.234   1.00 33.28  ? 399  TYR   B C   1 
ATOM   4143  O  O   . TYR   B  1 98  ? -5.719  -21.996 11.625   1.00 32.77  ? 399  TYR   B O   1 
ATOM   4144  C  CB  . TYR   B  1 98  ? -3.272  -24.371 11.376   1.00 36.38  ? 399  TYR   B CB  1 
ATOM   4145  C  CG  . TYR   B  1 98  ? -3.059  -23.683 10.037   1.00 36.60  ? 399  TYR   B CG  1 
ATOM   4146  C  CD1 . TYR   B  1 98  ? -2.165  -22.620 9.917    1.00 31.49  ? 399  TYR   B CD1 1 
ATOM   4147  C  CD2 . TYR   B  1 98  ? -3.717  -24.117 8.894    1.00 25.05  ? 399  TYR   B CD2 1 
ATOM   4148  C  CE1 . TYR   B  1 98  ? -1.940  -22.011 8.703    1.00 32.19  ? 399  TYR   B CE1 1 
ATOM   4149  C  CE2 . TYR   B  1 98  ? -3.508  -23.503 7.675    1.00 25.91  ? 399  TYR   B CE2 1 
ATOM   4150  C  CZ  . TYR   B  1 98  ? -2.612  -22.449 7.586    1.00 29.43  ? 399  TYR   B CZ  1 
ATOM   4151  O  OH  . TYR   B  1 98  ? -2.379  -21.821 6.382    1.00 32.36  ? 399  TYR   B OH  1 
ATOM   4152  N  N   . GLN   B  1 99  ? -3.980  -21.949 13.059   1.00 26.02  ? 400  GLN   B N   1 
ATOM   4153  C  CA  . GLN   B  1 99  ? -4.060  -20.517 13.303   1.00 25.28  ? 400  GLN   B CA  1 
ATOM   4154  C  C   . GLN   B  1 99  ? -2.824  -19.839 12.743   1.00 31.57  ? 400  GLN   B C   1 
ATOM   4155  O  O   . GLN   B  1 99  ? -1.706  -20.317 12.962   1.00 30.72  ? 400  GLN   B O   1 
ATOM   4156  C  CB  . GLN   B  1 99  ? -4.190  -20.223 14.797   1.00 31.14  ? 400  GLN   B CB  1 
ATOM   4157  C  CG  . GLN   B  1 99  ? -5.403  -20.852 15.401   1.00 36.45  ? 400  GLN   B CG  1 
ATOM   4158  C  CD  . GLN   B  1 99  ? -6.661  -20.280 14.798   1.00 36.77  ? 400  GLN   B CD  1 
ATOM   4159  O  OE1 . GLN   B  1 99  ? -6.758  -19.075 14.580   1.00 41.79  ? 400  GLN   B OE1 1 
ATOM   4160  N  NE2 . GLN   B  1 99  ? -7.626  -21.142 14.506   1.00 34.29  ? 400  GLN   B NE2 1 
ATOM   4161  N  N   . LEU   B  1 100 ? -3.030  -18.733 12.023   1.00 26.75  ? 401  LEU   B N   1 
ATOM   4162  C  CA  . LEU   B  1 100 ? -1.917  -17.935 11.524   1.00 26.07  ? 401  LEU   B CA  1 
ATOM   4163  C  C   . LEU   B  1 100 ? -1.265  -17.153 12.657   1.00 30.64  ? 401  LEU   B C   1 
ATOM   4164  O  O   . LEU   B  1 100 ? -1.947  -16.627 13.538   1.00 26.18  ? 401  LEU   B O   1 
ATOM   4165  C  CB  . LEU   B  1 100 ? -2.403  -16.957 10.453   1.00 22.85  ? 401  LEU   B CB  1 
ATOM   4166  C  CG  . LEU   B  1 100 ? -2.945  -17.594 9.169    1.00 22.73  ? 401  LEU   B CG  1 
ATOM   4167  C  CD1 . LEU   B  1 100 ? -3.581  -16.555 8.259    1.00 21.33  ? 401  LEU   B CD1 1 
ATOM   4168  C  CD2 . LEU   B  1 100 ? -1.833  -18.320 8.458    1.00 22.58  ? 401  LEU   B CD2 1 
ATOM   4169  N  N   . LYS   B  1 101 ? 0.062   -17.074 12.631   1.00 29.43  ? 402  LYS   B N   1 
ATOM   4170  C  CA  . LYS   B  1 101 ? 0.741   -16.053 13.412   1.00 27.02  ? 402  LYS   B CA  1 
ATOM   4171  C  C   . LYS   B  1 101 ? 0.327   -14.677 12.913   1.00 29.41  ? 402  LYS   B C   1 
ATOM   4172  O  O   . LYS   B  1 101 ? -0.133  -14.514 11.779   1.00 26.60  ? 402  LYS   B O   1 
ATOM   4173  C  CB  . LYS   B  1 101 ? 2.258   -16.197 13.299   1.00 26.66  ? 402  LYS   B CB  1 
ATOM   4174  C  CG  . LYS   B  1 101 ? 2.787   -17.556 13.702   1.00 34.92  ? 402  LYS   B CG  1 
ATOM   4175  C  CD  . LYS   B  1 101 ? 2.468   -17.863 15.162   1.00 37.95  ? 402  LYS   B CD  1 
ATOM   4176  C  CE  . LYS   B  1 101 ? 3.572   -18.709 15.791   1.00 48.72  ? 402  LYS   B CE  1 
ATOM   4177  N  NZ  . LYS   B  1 101 ? 3.026   -19.949 16.407   1.00 55.93  ? 402  LYS   B NZ  1 
ATOM   4178  N  N   . ASP   B  1 102 ? 0.512   -13.674 13.774   1.00 27.68  ? 403  ASP   B N   1 
ATOM   4179  C  CA  . ASP   B  1 102 ? 0.138   -12.306 13.428   1.00 28.72  ? 403  ASP   B CA  1 
ATOM   4180  C  C   . ASP   B  1 102 ? 0.928   -11.805 12.233   1.00 27.09  ? 403  ASP   B C   1 
ATOM   4181  O  O   . ASP   B  1 102 ? 0.384   -11.120 11.357   1.00 28.72  ? 403  ASP   B O   1 
ATOM   4182  C  CB  . ASP   B  1 102 ? 0.373   -11.379 14.624   1.00 32.74  ? 403  ASP   B CB  1 
ATOM   4183  C  CG  . ASP   B  1 102 ? -0.497  -11.733 15.821   1.00 50.85  ? 403  ASP   B CG  1 
ATOM   4184  O  OD1 . ASP   B  1 102 ? -1.324  -12.668 15.703   1.00 52.98  ? 403  ASP   B OD1 1 
ATOM   4185  O  OD2 . ASP   B  1 102 ? -0.350  -11.073 16.875   1.00 52.51  ? 403  ASP   B OD2 1 
ATOM   4186  N  N   . THR   B  1 103 ? 2.230   -12.080 12.217   1.00 25.61  ? 404  THR   B N   1 
ATOM   4187  C  CA  . THR   B  1 103 ? 3.052   -11.727 11.067   1.00 28.35  ? 404  THR   B CA  1 
ATOM   4188  C  C   . THR   B  1 103 ? 2.487   -12.333 9.788    1.00 32.37  ? 404  THR   B C   1 
ATOM   4189  O  O   . THR   B  1 103 ? 2.414   -11.664 8.752    1.00 28.22  ? 404  THR   B O   1 
ATOM   4190  C  CB  . THR   B  1 103 ? 4.481   -12.214 11.301   1.00 29.73  ? 404  THR   B CB  1 
ATOM   4191  O  OG1 . THR   B  1 103 ? 4.431   -13.576 11.737   1.00 35.15  ? 404  THR   B OG1 1 
ATOM   4192  C  CG2 . THR   B  1 103 ? 5.161   -11.382 12.380   1.00 31.00  ? 404  THR   B CG2 1 
ATOM   4193  N  N   . GLU   B  1 104 ? 2.074   -13.601 9.853    1.00 31.16  ? 405  GLU   B N   1 
ATOM   4194  C  CA  . GLU   B  1 104 ? 1.572   -14.289 8.670    1.00 34.93  ? 405  GLU   B CA  1 
ATOM   4195  C  C   . GLU   B  1 104 ? 0.228   -13.717 8.246    1.00 28.99  ? 405  GLU   B C   1 
ATOM   4196  O  O   . GLU   B  1 104 ? -0.059  -13.599 7.046    1.00 28.17  ? 405  GLU   B O   1 
ATOM   4197  C  CB  . GLU   B  1 104 ? 1.457   -15.788 8.947    1.00 28.91  ? 405  GLU   B CB  1 
ATOM   4198  C  CG  . GLU   B  1 104 ? 2.747   -16.466 9.385    1.00 32.77  ? 405  GLU   B CG  1 
ATOM   4199  C  CD  . GLU   B  1 104 ? 2.497   -17.831 10.007   1.00 32.95  ? 405  GLU   B CD  1 
ATOM   4200  O  OE1 . GLU   B  1 104 ? 3.462   -18.609 10.164   1.00 30.09  ? 405  GLU   B OE1 1 
ATOM   4201  O  OE2 . GLU   B  1 104 ? 1.329   -18.128 10.326   1.00 30.84  ? 405  GLU   B OE2 1 
ATOM   4202  N  N   . LEU   B  1 105 ? -0.602  -13.349 9.220    1.00 28.11  ? 406  LEU   B N   1 
ATOM   4203  C  CA  . LEU   B  1 105 ? -1.874  -12.709 8.908    1.00 27.30  ? 406  LEU   B CA  1 
ATOM   4204  C  C   . LEU   B  1 105 ? -1.650  -11.390 8.188    1.00 25.59  ? 406  LEU   B C   1 
ATOM   4205  O  O   . LEU   B  1 105 ? -2.323  -11.089 7.203    1.00 25.52  ? 406  LEU   B O   1 
ATOM   4206  C  CB  . LEU   B  1 105 ? -2.670  -12.482 10.189   1.00 24.23  ? 406  LEU   B CB  1 
ATOM   4207  C  CG  . LEU   B  1 105 ? -4.079  -11.925 9.999    1.00 28.62  ? 406  LEU   B CG  1 
ATOM   4208  C  CD1 . LEU   B  1 105 ? -4.936  -12.995 9.385    1.00 25.42  ? 406  LEU   B CD1 1 
ATOM   4209  C  CD2 . LEU   B  1 105 ? -4.655  -11.466 11.351   1.00 30.85  ? 406  LEU   B CD2 1 
ATOM   4210  N  N   . ILE   B  1 106 ? -0.723  -10.572 8.693    1.00 24.74  ? 407  ILE   B N   1 
ATOM   4211  C  CA  . ILE   B  1 106 ? -0.456  -9.278  8.073    1.00 22.24  ? 407  ILE   B CA  1 
ATOM   4212  C  C   . ILE   B  1 106 ? 0.077   -9.468  6.662    1.00 20.41  ? 407  ILE   B C   1 
ATOM   4213  O  O   . ILE   B  1 106 ? -0.353  -8.801  5.715    1.00 20.64  ? 407  ILE   B O   1 
ATOM   4214  C  CB  . ILE   B  1 106 ? 0.537   -8.480  8.927    1.00 23.20  ? 407  ILE   B CB  1 
ATOM   4215  C  CG1 . ILE   B  1 106 ? -0.102  -8.103  10.263   1.00 31.57  ? 407  ILE   B CG1 1 
ATOM   4216  C  CG2 . ILE   B  1 106 ? 1.018   -7.280  8.166    1.00 20.88  ? 407  ILE   B CG2 1 
ATOM   4217  C  CD1 . ILE   B  1 106 ? 0.902   -7.690  11.310   1.00 28.60  ? 407  ILE   B CD1 1 
ATOM   4218  N  N   . TYR   B  1 107 ? 1.064   -10.348 6.520    1.00 28.64  ? 408  TYR   B N   1 
ATOM   4219  C  CA  . TYR   B  1 107 ? 1.609   -10.674 5.213    1.00 23.50  ? 408  TYR   B CA  1 
ATOM   4220  C  C   . TYR   B  1 107 ? 0.519   -11.178 4.289    1.00 28.89  ? 408  TYR   B C   1 
ATOM   4221  O  O   . TYR   B  1 107 ? 0.456   -10.803 3.111    1.00 26.74  ? 408  TYR   B O   1 
ATOM   4222  C  CB  . TYR   B  1 107 ? 2.700   -11.726 5.379    1.00 22.64  ? 408  TYR   B CB  1 
ATOM   4223  C  CG  . TYR   B  1 107 ? 3.155   -12.333 4.078    1.00 27.37  ? 408  TYR   B CG  1 
ATOM   4224  C  CD1 . TYR   B  1 107 ? 4.224   -11.793 3.385    1.00 28.06  ? 408  TYR   B CD1 1 
ATOM   4225  C  CD2 . TYR   B  1 107 ? 2.529   -13.463 3.548    1.00 29.69  ? 408  TYR   B CD2 1 
ATOM   4226  C  CE1 . TYR   B  1 107 ? 4.649   -12.342 2.189    1.00 26.89  ? 408  TYR   B CE1 1 
ATOM   4227  C  CE2 . TYR   B  1 107 ? 2.945   -14.015 2.344    1.00 25.56  ? 408  TYR   B CE2 1 
ATOM   4228  C  CZ  . TYR   B  1 107 ? 4.011   -13.448 1.669    1.00 33.42  ? 408  TYR   B CZ  1 
ATOM   4229  O  OH  . TYR   B  1 107 ? 4.459   -13.980 0.468    1.00 34.05  ? 408  TYR   B OH  1 
ATOM   4230  N  N   . GLY   B  1 108 ? -0.326  -12.072 4.804    1.00 25.38  ? 409  GLY   B N   1 
ATOM   4231  C  CA  . GLY   B  1 108 ? -1.350  -12.668 3.967    1.00 22.58  ? 409  GLY   B CA  1 
ATOM   4232  C  C   . GLY   B  1 108 ? -2.352  -11.641 3.491    1.00 29.02  ? 409  GLY   B C   1 
ATOM   4233  O  O   . GLY   B  1 108 ? -2.724  -11.618 2.318    1.00 24.86  ? 409  GLY   B O   1 
ATOM   4234  N  N   . ALA   B  1 109 ? -2.791  -10.763 4.396    1.00 20.82  ? 410  ALA   B N   1 
ATOM   4235  C  CA  . ALA   B  1 109 ? -3.763  -9.748  4.009    1.00 20.75  ? 410  ALA   B CA  1 
ATOM   4236  C  C   . ALA   B  1 109 ? -3.178  -8.814  2.960    1.00 21.85  ? 410  ALA   B C   1 
ATOM   4237  O  O   . ALA   B  1 109 ? -3.843  -8.484  1.968    1.00 22.28  ? 410  ALA   B O   1 
ATOM   4238  C  CB  . ALA   B  1 109 ? -4.226  -8.956  5.238    1.00 21.16  ? 410  ALA   B CB  1 
ATOM   4239  N  N   . LYS   B  1 110 ? -1.931  -8.381  3.166    1.00 22.43  ? 411  LYS   B N   1 
ATOM   4240  C  CA  . LYS   B  1 110 ? -1.284  -7.483  2.222    1.00 22.18  ? 411  LYS   B CA  1 
ATOM   4241  C  C   . LYS   B  1 110 ? -1.144  -8.135  0.858    1.00 28.33  ? 411  LYS   B C   1 
ATOM   4242  O  O   . LYS   B  1 110 ? -1.376  -7.495  -0.174   1.00 23.47  ? 411  LYS   B O   1 
ATOM   4243  C  CB  . LYS   B  1 110 ? 0.088   -7.061  2.757    1.00 23.00  ? 411  LYS   B CB  1 
ATOM   4244  C  CG  . LYS   B  1 110 ? -0.002  -6.050  3.909    1.00 22.88  ? 411  LYS   B CG  1 
ATOM   4245  C  CD  . LYS   B  1 110 ? 1.387   -5.621  4.403    1.00 24.71  ? 411  LYS   B CD  1 
ATOM   4246  C  CE  . LYS   B  1 110 ? 1.259   -4.640  5.570    1.00 28.94  ? 411  LYS   B CE  1 
ATOM   4247  N  NZ  . LYS   B  1 110 ? 2.560   -4.045  6.003    1.00 28.20  ? 411  LYS   B NZ  1 
ATOM   4248  N  N   . HIS   B  1 111 ? -0.792  -9.414  0.830    1.00 26.98  ? 412  HIS   B N   1 
ATOM   4249  C  CA  . HIS   B  1 111 ? -0.584  -10.054 -0.455   1.00 27.78  ? 412  HIS   B CA  1 
ATOM   4250  C  C   . HIS   B  1 111 ? -1.895  -10.374 -1.151   1.00 22.56  ? 412  HIS   B C   1 
ATOM   4251  O  O   . HIS   B  1 111 ? -1.964  -10.320 -2.381   1.00 24.38  ? 412  HIS   B O   1 
ATOM   4252  C  CB  . HIS   B  1 111 ? 0.310   -11.280 -0.275   1.00 22.10  ? 412  HIS   B CB  1 
ATOM   4253  C  CG  . HIS   B  1 111 ? 1.759   -10.916 -0.260   1.00 25.72  ? 412  HIS   B CG  1 
ATOM   4254  N  ND1 . HIS   B  1 111 ? 2.338   -10.234 0.793    1.00 28.96  ? 412  HIS   B ND1 1 
ATOM   4255  C  CD2 . HIS   B  1 111 ? 2.723   -11.043 -1.203   1.00 25.01  ? 412  HIS   B CD2 1 
ATOM   4256  C  CE1 . HIS   B  1 111 ? 3.605   -9.985  0.508    1.00 26.10  ? 412  HIS   B CE1 1 
ATOM   4257  N  NE2 . HIS   B  1 111 ? 3.866   -10.474 -0.695   1.00 26.92  ? 412  HIS   B NE2 1 
ATOM   4258  N  N   . ALA   B  1 112 ? -2.958  -10.647 -0.405   1.00 26.32  ? 413  ALA   B N   1 
ATOM   4259  C  CA  . ALA   B  1 112 ? -4.248  -10.754 -1.068   1.00 28.21  ? 413  ALA   B CA  1 
ATOM   4260  C  C   . ALA   B  1 112 ? -4.573  -9.462  -1.796   1.00 27.43  ? 413  ALA   B C   1 
ATOM   4261  O  O   . ALA   B  1 112 ? -5.083  -9.480  -2.923   1.00 25.07  ? 413  ALA   B O   1 
ATOM   4262  C  CB  . ALA   B  1 112 ? -5.336  -11.102 -0.065   1.00 18.18  ? 413  ALA   B CB  1 
ATOM   4263  N  N   . TRP   B  1 113 ? -4.240  -8.326  -1.190   1.00 24.60  ? 414  TRP   B N   1 
ATOM   4264  C  CA  . TRP   B  1 113 ? -4.423  -7.064  -1.897   1.00 26.10  ? 414  TRP   B CA  1 
ATOM   4265  C  C   . TRP   B  1 113 ? -3.480  -6.975  -3.085   1.00 21.40  ? 414  TRP   B C   1 
ATOM   4266  O  O   . TRP   B  1 113 ? -3.899  -6.649  -4.193   1.00 27.26  ? 414  TRP   B O   1 
ATOM   4267  C  CB  . TRP   B  1 113 ? -4.204  -5.888  -0.948   1.00 20.28  ? 414  TRP   B CB  1 
ATOM   4268  C  CG  . TRP   B  1 113 ? -4.478  -4.539  -1.544   1.00 20.75  ? 414  TRP   B CG  1 
ATOM   4269  C  CD1 . TRP   B  1 113 ? -5.065  -4.254  -2.760   1.00 25.45  ? 414  TRP   B CD1 1 
ATOM   4270  C  CD2 . TRP   B  1 113 ? -4.173  -3.282  -0.945   1.00 28.36  ? 414  TRP   B CD2 1 
ATOM   4271  N  NE1 . TRP   B  1 113 ? -5.132  -2.892  -2.940   1.00 28.89  ? 414  TRP   B NE1 1 
ATOM   4272  C  CE2 . TRP   B  1 113 ? -4.589  -2.274  -1.840   1.00 32.34  ? 414  TRP   B CE2 1 
ATOM   4273  C  CE3 . TRP   B  1 113 ? -3.599  -2.910  0.270    1.00 22.37  ? 414  TRP   B CE3 1 
ATOM   4274  C  CZ2 . TRP   B  1 113 ? -4.432  -0.923  -1.555   1.00 29.95  ? 414  TRP   B CZ2 1 
ATOM   4275  C  CZ3 . TRP   B  1 113 ? -3.445  -1.577  0.546    1.00 26.55  ? 414  TRP   B CZ3 1 
ATOM   4276  C  CH2 . TRP   B  1 113 ? -3.860  -0.597  -0.358   1.00 26.79  ? 414  TRP   B CH2 1 
ATOM   4277  N  N   . ARG   B  1 114 ? -2.197  -7.247  -2.855   1.00 23.14  ? 415  ARG   B N   1 
ATOM   4278  C  CA  . ARG   B  1 114 ? -1.207  -7.231  -3.916   1.00 23.26  ? 415  ARG   B CA  1 
ATOM   4279  C  C   . ARG   B  1 114 ? -1.613  -8.148  -5.055   1.00 25.72  ? 415  ARG   B C   1 
ATOM   4280  O  O   . ARG   B  1 114 ? -1.299  -7.879  -6.224   1.00 22.39  ? 415  ARG   B O   1 
ATOM   4281  C  CB  . ARG   B  1 114 ? 0.140   -7.652  -3.338   1.00 24.88  ? 415  ARG   B CB  1 
ATOM   4282  C  CG  . ARG   B  1 114 ? 1.311   -7.507  -4.272   1.00 22.61  ? 415  ARG   B CG  1 
ATOM   4283  C  CD  . ARG   B  1 114 ? 2.554   -8.161  -3.677   1.00 23.16  ? 415  ARG   B CD  1 
ATOM   4284  N  NE  . ARG   B  1 114 ? 3.748   -7.699  -4.361   1.00 22.32  ? 415  ARG   B NE  1 
ATOM   4285  C  CZ  . ARG   B  1 114 ? 4.978   -8.061  -4.039   1.00 25.97  ? 415  ARG   B CZ  1 
ATOM   4286  N  NH1 . ARG   B  1 114 ? 6.005   -7.585  -4.729   1.00 21.90  ? 415  ARG   B NH1 1 
ATOM   4287  N  NH2 . ARG   B  1 114 ? 5.175   -8.892  -3.024   1.00 25.37  ? 415  ARG   B NH2 1 
ATOM   4288  N  N   . ASN   B  1 115 ? -2.327  -9.220  -4.746   1.00 23.50  ? 416  ASN   B N   1 
ATOM   4289  C  CA  . ASN   B  1 115 ? -2.731  -10.174 -5.760   1.00 25.13  ? 416  ASN   B CA  1 
ATOM   4290  C  C   . ASN   B  1 115 ? -4.085  -9.860  -6.378   1.00 26.49  ? 416  ASN   B C   1 
ATOM   4291  O  O   . ASN   B  1 115 ? -4.536  -10.623 -7.239   1.00 24.55  ? 416  ASN   B O   1 
ATOM   4292  C  CB  . ASN   B  1 115 ? -2.758  -11.583 -5.170   1.00 24.15  ? 416  ASN   B CB  1 
ATOM   4293  C  CG  . ASN   B  1 115 ? -1.387  -12.064 -4.742   1.00 25.77  ? 416  ASN   B CG  1 
ATOM   4294  O  OD1 . ASN   B  1 115 ? -0.375  -11.549 -5.198   1.00 22.19  ? 416  ASN   B OD1 1 
ATOM   4295  N  ND2 . ASN   B  1 115 ? -1.351  -13.065 -3.856   1.00 21.07  ? 416  ASN   B ND2 1 
ATOM   4296  N  N   . ALA   B  1 116 ? -4.747  -8.779  -5.962   1.00 20.29  ? 417  ALA   B N   1 
ATOM   4297  C  CA  . ALA   B  1 116 ? -6.092  -8.477  -6.455   1.00 21.21  ? 417  ALA   B CA  1 
ATOM   4298  C  C   . ALA   B  1 116 ? -5.984  -7.953  -7.884   1.00 24.51  ? 417  ALA   B C   1 
ATOM   4299  O  O   . ALA   B  1 116 ? -5.740  -6.770  -8.108   1.00 23.85  ? 417  ALA   B O   1 
ATOM   4300  C  CB  . ALA   B  1 116 ? -6.792  -7.462  -5.560   1.00 17.29  ? 417  ALA   B CB  1 
ATOM   4301  N  N   . SER   B  1 117 ? -6.171  -8.834  -8.863   1.00 20.58  ? 418  SER   B N   1 
ATOM   4302  C  CA  A SER   B  1 117 ? -5.957  -8.423  -10.244  0.63 20.01  ? 418  SER   B CA  1 
ATOM   4303  C  CA  B SER   B  1 117 ? -5.990  -8.452  -10.260  0.37 20.74  ? 418  SER   B CA  1 
ATOM   4304  C  C   . SER   B  1 117 ? -6.914  -7.319  -10.677  1.00 24.52  ? 418  SER   B C   1 
ATOM   4305  O  O   . SER   B  1 117 ? -6.595  -6.578  -11.610  1.00 26.70  ? 418  SER   B O   1 
ATOM   4306  C  CB  A SER   B  1 117 ? -6.085  -9.627  -11.165  0.63 23.23  ? 418  SER   B CB  1 
ATOM   4307  C  CB  B SER   B  1 117 ? -6.233  -9.652  -11.165  0.37 22.62  ? 418  SER   B CB  1 
ATOM   4308  O  OG  A SER   B  1 117 ? -7.371  -10.209 -11.063  0.63 20.56  ? 418  SER   B OG  1 
ATOM   4309  O  OG  B SER   B  1 117 ? -5.405  -10.744 -10.814  0.37 23.64  ? 418  SER   B OG  1 
ATOM   4310  N  N   . ARG   B  1 118 ? -8.051  -7.167  -10.008  1.00 18.26  ? 419  ARG   B N   1 
ATOM   4311  C  CA  . ARG   B  1 118 ? -9.017  -6.160  -10.398  1.00 18.62  ? 419  ARG   B CA  1 
ATOM   4312  C  C   . ARG   B  1 118 ? -8.787  -4.817  -9.737   1.00 23.15  ? 419  ARG   B C   1 
ATOM   4313  O  O   . ARG   B  1 118 ? -9.531  -3.873  -10.028  1.00 25.49  ? 419  ARG   B O   1 
ATOM   4314  C  CB  . ARG   B  1 118 ? -10.431 -6.654  -10.097  1.00 21.77  ? 419  ARG   B CB  1 
ATOM   4315  C  CG  . ARG   B  1 118 ? -10.870 -7.774  -11.050  1.00 23.59  ? 419  ARG   B CG  1 
ATOM   4316  C  CD  . ARG   B  1 118 ? -12.203 -8.346  -10.660  1.00 20.65  ? 419  ARG   B CD  1 
ATOM   4317  N  NE  . ARG   B  1 118 ? -12.740 -9.183  -11.720  1.00 26.96  ? 419  ARG   B NE  1 
ATOM   4318  C  CZ  . ARG   B  1 118 ? -13.902 -9.810  -11.638  1.00 27.72  ? 419  ARG   B CZ  1 
ATOM   4319  N  NH1 . ARG   B  1 118 ? -14.624 -9.677  -10.545  1.00 29.70  ? 419  ARG   B NH1 1 
ATOM   4320  N  NH2 . ARG   B  1 118 ? -14.332 -10.564 -12.641  1.00 25.19  ? 419  ARG   B NH2 1 
ATOM   4321  N  N   . CYS   B  1 119 ? -7.782  -4.685  -8.878   1.00 19.09  ? 420  CYS   B N   1 
ATOM   4322  C  CA  . CYS   B  1 119 ? -7.622  -3.465  -8.096   1.00 17.20  ? 420  CYS   B CA  1 
ATOM   4323  C  C   . CYS   B  1 119 ? -6.571  -2.577  -8.743   1.00 17.46  ? 420  CYS   B C   1 
ATOM   4324  O  O   . CYS   B  1 119 ? -5.400  -2.954  -8.847   1.00 17.66  ? 420  CYS   B O   1 
ATOM   4325  C  CB  . CYS   B  1 119 ? -7.256  -3.770  -6.638   1.00 17.15  ? 420  CYS   B CB  1 
ATOM   4326  S  SG  . CYS   B  1 119 ? -6.902  -2.283  -5.661   1.00 22.82  ? 420  CYS   B SG  1 
ATOM   4327  N  N   . VAL   B  1 120 ? -6.999  -1.393  -9.180   1.00 17.52  ? 421  VAL   B N   1 
ATOM   4328  C  CA  . VAL   B  1 120 ? -6.075  -0.413  -9.744   1.00 22.21  ? 421  VAL   B CA  1 
ATOM   4329  C  C   . VAL   B  1 120 ? -5.257  0.306   -8.684   1.00 24.82  ? 421  VAL   B C   1 
ATOM   4330  O  O   . VAL   B  1 120 ? -4.288  1.000   -9.024   1.00 24.40  ? 421  VAL   B O   1 
ATOM   4331  C  CB  . VAL   B  1 120 ? -6.885  0.601   -10.574  1.00 26.31  ? 421  VAL   B CB  1 
ATOM   4332  C  CG1 . VAL   B  1 120 ? -7.686  1.522   -9.663   1.00 24.78  ? 421  VAL   B CG1 1 
ATOM   4333  C  CG2 . VAL   B  1 120 ? -5.981  1.382   -11.565  1.00 26.01  ? 421  VAL   B CG2 1 
ATOM   4334  N  N   . GLY   B  1 121 ? -5.604  0.157   -7.408   1.00 25.31  ? 422  GLY   B N   1 
ATOM   4335  C  CA  . GLY   B  1 121 ? -4.946  0.943   -6.384   1.00 21.10  ? 422  GLY   B CA  1 
ATOM   4336  C  C   . GLY   B  1 121 ? -3.804  0.251   -5.670   1.00 23.81  ? 422  GLY   B C   1 
ATOM   4337  O  O   . GLY   B  1 121 ? -3.388  0.675   -4.588   1.00 28.52  ? 422  GLY   B O   1 
ATOM   4338  N  N   . ARG   B  1 122 ? -3.248  -0.783  -6.288   1.00 21.03  ? 423  ARG   B N   1 
ATOM   4339  C  CA  . ARG   B  1 122 ? -2.323  -1.668  -5.600   1.00 19.44  ? 423  ARG   B CA  1 
ATOM   4340  C  C   . ARG   B  1 122 ? -0.933  -1.094  -5.388   1.00 25.60  ? 423  ARG   B C   1 
ATOM   4341  O  O   . ARG   B  1 122 ? -0.157  -1.707  -4.644   1.00 26.98  ? 423  ARG   B O   1 
ATOM   4342  C  CB  . ARG   B  1 122 ? -2.210  -2.982  -6.358   1.00 18.30  ? 423  ARG   B CB  1 
ATOM   4343  C  CG  . ARG   B  1 122 ? -3.340  -3.916  -6.060   1.00 23.23  ? 423  ARG   B CG  1 
ATOM   4344  C  CD  . ARG   B  1 122 ? -3.134  -5.166  -6.852   1.00 18.01  ? 423  ARG   B CD  1 
ATOM   4345  N  NE  . ARG   B  1 122 ? -3.520  -4.991  -8.258   1.00 20.19  ? 423  ARG   B NE  1 
ATOM   4346  C  CZ  . ARG   B  1 122 ? -3.266  -5.893  -9.202   1.00 24.84  ? 423  ARG   B CZ  1 
ATOM   4347  N  NH1 . ARG   B  1 122 ? -2.600  -7.006  -8.889   1.00 18.37  ? 423  ARG   B NH1 1 
ATOM   4348  N  NH2 . ARG   B  1 122 ? -3.669  -5.686  -10.449  1.00 21.07  ? 423  ARG   B NH2 1 
ATOM   4349  N  N   . ILE   B  1 123 ? -0.591  0.051   -5.985   1.00 21.46  ? 424  ILE   B N   1 
ATOM   4350  C  CA  . ILE   B  1 123 ? 0.699   0.646   -5.660   1.00 20.89  ? 424  ILE   B CA  1 
ATOM   4351  C  C   . ILE   B  1 123 ? 0.828   0.837   -4.147   1.00 23.70  ? 424  ILE   B C   1 
ATOM   4352  O  O   . ILE   B  1 123 ? 1.936   0.876   -3.618   1.00 23.14  ? 424  ILE   B O   1 
ATOM   4353  C  CB  . ILE   B  1 123 ? 0.902   1.972   -6.420   1.00 25.00  ? 424  ILE   B CB  1 
ATOM   4354  C  CG1 . ILE   B  1 123 ? 2.357   2.423   -6.324   1.00 25.17  ? 424  ILE   B CG1 1 
ATOM   4355  C  CG2 . ILE   B  1 123 ? -0.024  3.077   -5.891   1.00 20.41  ? 424  ILE   B CG2 1 
ATOM   4356  C  CD1 . ILE   B  1 123 ? 2.697   3.564   -7.260   1.00 29.94  ? 424  ILE   B CD1 1 
ATOM   4357  N  N   . GLN   B  1 124 ? -0.298  0.908   -3.445   1.00 20.92  ? 425  GLN   B N   1 
ATOM   4358  C  CA  . GLN   B  1 124 ? -0.387  1.122   -2.001   1.00 27.57  ? 425  GLN   B CA  1 
ATOM   4359  C  C   . GLN   B  1 124 ? -0.395  -0.169  -1.183   1.00 29.81  ? 425  GLN   B C   1 
ATOM   4360  O  O   . GLN   B  1 124 ? -0.514  -0.097  0.051    1.00 29.19  ? 425  GLN   B O   1 
ATOM   4361  C  CB  . GLN   B  1 124 ? -1.669  1.916   -1.690   1.00 28.11  ? 425  GLN   B CB  1 
ATOM   4362  C  CG  . GLN   B  1 124 ? -1.669  3.348   -2.221   1.00 34.01  ? 425  GLN   B CG  1 
ATOM   4363  C  CD  . GLN   B  1 124 ? -0.875  4.261   -1.313   1.00 39.80  ? 425  GLN   B CD  1 
ATOM   4364  O  OE1 . GLN   B  1 124 ? -0.683  3.953   -0.140   1.00 40.93  ? 425  GLN   B OE1 1 
ATOM   4365  N  NE2 . GLN   B  1 124 ? -0.409  5.377   -1.842   1.00 44.52  ? 425  GLN   B NE2 1 
ATOM   4366  N  N   . TRP   B  1 125 ? -0.253  -1.338  -1.829   1.00 24.66  ? 426  TRP   B N   1 
ATOM   4367  C  CA  . TRP   B  1 125 ? -0.558  -2.608  -1.165   1.00 24.85  ? 426  TRP   B CA  1 
ATOM   4368  C  C   . TRP   B  1 125 ? 0.228   -2.791  0.131    1.00 29.76  ? 426  TRP   B C   1 
ATOM   4369  O  O   . TRP   B  1 125 ? -0.299  -3.312  1.116    1.00 28.97  ? 426  TRP   B O   1 
ATOM   4370  C  CB  . TRP   B  1 125 ? -0.307  -3.783  -2.120   1.00 22.96  ? 426  TRP   B CB  1 
ATOM   4371  C  CG  . TRP   B  1 125 ? 1.147   -4.105  -2.356   1.00 22.67  ? 426  TRP   B CG  1 
ATOM   4372  C  CD1 . TRP   B  1 125 ? 1.950   -3.621  -3.358   1.00 28.10  ? 426  TRP   B CD1 1 
ATOM   4373  C  CD2 . TRP   B  1 125 ? 1.958   -5.003  -1.594   1.00 19.85  ? 426  TRP   B CD2 1 
ATOM   4374  N  NE1 . TRP   B  1 125 ? 3.223   -4.144  -3.243   1.00 23.76  ? 426  TRP   B NE1 1 
ATOM   4375  C  CE2 . TRP   B  1 125 ? 3.250   -4.998  -2.171   1.00 24.54  ? 426  TRP   B CE2 1 
ATOM   4376  C  CE3 . TRP   B  1 125 ? 1.720   -5.812  -0.475   1.00 19.83  ? 426  TRP   B CE3 1 
ATOM   4377  C  CZ2 . TRP   B  1 125 ? 4.292   -5.767  -1.668   1.00 22.54  ? 426  TRP   B CZ2 1 
ATOM   4378  C  CZ3 . TRP   B  1 125 ? 2.759   -6.565  0.022    1.00 26.73  ? 426  TRP   B CZ3 1 
ATOM   4379  C  CH2 . TRP   B  1 125 ? 4.031   -6.538  -0.574   1.00 28.87  ? 426  TRP   B CH2 1 
ATOM   4380  N  N   . SER   B  1 126 ? 1.483   -2.374  0.162    1.00 26.19  ? 427  SER   B N   1 
ATOM   4381  C  CA  . SER   B  1 126 ? 2.276   -2.711  1.328    1.00 25.96  ? 427  SER   B CA  1 
ATOM   4382  C  C   . SER   B  1 126 ? 1.972   -1.812  2.519    1.00 31.61  ? 427  SER   B C   1 
ATOM   4383  O  O   . SER   B  1 126 ? 2.432   -2.091  3.626    1.00 29.70  ? 427  SER   B O   1 
ATOM   4384  C  CB  . SER   B  1 126 ? 3.756   -2.619  0.991    1.00 23.52  ? 427  SER   B CB  1 
ATOM   4385  O  OG  . SER   B  1 126 ? 4.097   -1.259  0.787    1.00 36.38  ? 427  SER   B OG  1 
ATOM   4386  N  N   . LYS   B  1 127 ? 1.233   -0.733  2.315    1.00 31.36  ? 428  LYS   B N   1 
ATOM   4387  C  CA  . LYS   B  1 127 ? 0.858   0.158   3.402    1.00 39.46  ? 428  LYS   B CA  1 
ATOM   4388  C  C   . LYS   B  1 127 ? -0.607  -0.099  3.732    1.00 49.12  ? 428  LYS   B C   1 
ATOM   4389  O  O   . LYS   B  1 127 ? -1.516  0.633   3.345    1.00 66.79  ? 428  LYS   B O   1 
ATOM   4390  C  CB  . LYS   B  1 127 ? 1.135   1.606   3.017    1.00 40.39  ? 428  LYS   B CB  1 
ATOM   4391  C  CG  . LYS   B  1 127 ? 2.613   1.843   2.690    1.00 53.13  ? 428  LYS   B CG  1 
ATOM   4392  C  CD  . LYS   B  1 127 ? 2.891   3.273   2.277    1.00 64.76  ? 428  LYS   B CD  1 
ATOM   4393  C  CE  . LYS   B  1 127 ? 4.281   3.408   1.677    1.00 69.98  ? 428  LYS   B CE  1 
ATOM   4394  N  NZ  . LYS   B  1 127 ? 4.265   4.274   0.462    1.00 68.15  ? 428  LYS   B NZ  1 
ATOM   4395  N  N   . LEU   B  1 128 ? -0.817  -1.219  4.401    1.00 37.74  ? 429  LEU   B N   1 
ATOM   4396  C  CA  . LEU   B  1 128 ? -2.137  -1.693  4.775    1.00 26.06  ? 429  LEU   B CA  1 
ATOM   4397  C  C   . LEU   B  1 128 ? -2.138  -1.886  6.278    1.00 25.92  ? 429  LEU   B C   1 
ATOM   4398  O  O   . LEU   B  1 128 ? -1.234  -2.519  6.825    1.00 28.45  ? 429  LEU   B O   1 
ATOM   4399  C  CB  . LEU   B  1 128 ? -2.483  -3.004  4.074    1.00 19.31  ? 429  LEU   B CB  1 
ATOM   4400  C  CG  . LEU   B  1 128 ? -3.846  -3.601  4.457    1.00 22.89  ? 429  LEU   B CG  1 
ATOM   4401  C  CD1 . LEU   B  1 128 ? -5.007  -2.707  3.986    1.00 19.96  ? 429  LEU   B CD1 1 
ATOM   4402  C  CD2 . LEU   B  1 128 ? -3.988  -5.027  3.920    1.00 18.94  ? 429  LEU   B CD2 1 
ATOM   4403  N  N   . GLN   B  1 129 ? -3.113  -1.302  6.941    1.00 22.48  ? 430  GLN   B N   1 
ATOM   4404  C  CA  . GLN   B  1 129 ? -3.231  -1.447  8.376    1.00 24.37  ? 430  GLN   B CA  1 
ATOM   4405  C  C   . GLN   B  1 129 ? -4.124  -2.653  8.621    1.00 25.69  ? 430  GLN   B C   1 
ATOM   4406  O  O   . GLN   B  1 129 ? -5.262  -2.693  8.147    1.00 29.88  ? 430  GLN   B O   1 
ATOM   4407  C  CB  . GLN   B  1 129 ? -3.804  -0.185  9.012    1.00 28.81  ? 430  GLN   B CB  1 
ATOM   4408  C  CG  . GLN   B  1 129 ? -3.890  -0.273  10.533   1.00 29.52  ? 430  GLN   B CG  1 
ATOM   4409  C  CD  . GLN   B  1 129 ? -2.533  -0.504  11.165   1.00 41.34  ? 430  GLN   B CD  1 
ATOM   4410  O  OE1 . GLN   B  1 129 ? -1.541  0.137   10.797   1.00 41.59  ? 430  GLN   B OE1 1 
ATOM   4411  N  NE2 . GLN   B  1 129 ? -2.477  -1.433  12.110   1.00 45.05  ? 430  GLN   B NE2 1 
ATOM   4412  N  N   . VAL   B  1 130 ? -3.591  -3.652  9.307    1.00 26.85  ? 431  VAL   B N   1 
ATOM   4413  C  CA  . VAL   B  1 130 ? -4.279  -4.916  9.508    1.00 24.09  ? 431  VAL   B CA  1 
ATOM   4414  C  C   . VAL   B  1 130 ? -4.749  -4.948  10.958   1.00 27.34  ? 431  VAL   B C   1 
ATOM   4415  O  O   . VAL   B  1 130 ? -3.938  -4.925  11.885   1.00 29.70  ? 431  VAL   B O   1 
ATOM   4416  C  CB  . VAL   B  1 130 ? -3.362  -6.098  9.175    1.00 22.70  ? 431  VAL   B CB  1 
ATOM   4417  C  CG1 . VAL   B  1 130 ? -4.059  -7.429  9.429    1.00 23.98  ? 431  VAL   B CG1 1 
ATOM   4418  C  CG2 . VAL   B  1 130 ? -2.898  -5.984  7.709    1.00 32.10  ? 431  VAL   B CG2 1 
ATOM   4419  N  N   . PHE   B  1 131 ? -6.059  -4.973  11.159   1.00 23.60  ? 432  PHE   B N   1 
ATOM   4420  C  CA  . PHE   B  1 131 ? -6.644  -5.132  12.480   1.00 21.52  ? 432  PHE   B CA  1 
ATOM   4421  C  C   . PHE   B  1 131 ? -7.021  -6.592  12.651   1.00 26.20  ? 432  PHE   B C   1 
ATOM   4422  O  O   . PHE   B  1 131 ? -7.875  -7.120  11.928   1.00 28.15  ? 432  PHE   B O   1 
ATOM   4423  C  CB  . PHE   B  1 131 ? -7.836  -4.206  12.657   1.00 19.26  ? 432  PHE   B CB  1 
ATOM   4424  C  CG  . PHE   B  1 131 ? -7.456  -2.771  12.606   1.00 24.36  ? 432  PHE   B CG  1 
ATOM   4425  C  CD1 . PHE   B  1 131 ? -6.609  -2.238  13.573   1.00 29.31  ? 432  PHE   B CD1 1 
ATOM   4426  C  CD2 . PHE   B  1 131 ? -7.889  -1.961  11.564   1.00 26.76  ? 432  PHE   B CD2 1 
ATOM   4427  C  CE1 . PHE   B  1 131 ? -6.234  -0.909  13.530   1.00 27.04  ? 432  PHE   B CE1 1 
ATOM   4428  C  CE2 . PHE   B  1 131 ? -7.521  -0.629  11.517   1.00 27.43  ? 432  PHE   B CE2 1 
ATOM   4429  C  CZ  . PHE   B  1 131 ? -6.694  -0.103  12.501   1.00 32.43  ? 432  PHE   B CZ  1 
ATOM   4430  N  N   . ASP   B  1 132 ? -6.336  -7.252  13.570   1.00 26.41  ? 433  ASP   B N   1 
ATOM   4431  C  CA  . ASP   B  1 132 ? -6.579  -8.650  13.875   1.00 21.60  ? 433  ASP   B CA  1 
ATOM   4432  C  C   . ASP   B  1 132 ? -7.796  -8.712  14.782   1.00 25.33  ? 433  ASP   B C   1 
ATOM   4433  O  O   . ASP   B  1 132 ? -7.720  -8.342  15.952   1.00 26.56  ? 433  ASP   B O   1 
ATOM   4434  C  CB  . ASP   B  1 132 ? -5.346  -9.249  14.544   1.00 28.35  ? 433  ASP   B CB  1 
ATOM   4435  C  CG  . ASP   B  1 132 ? -5.482  -10.730 14.799   1.00 32.01  ? 433  ASP   B CG  1 
ATOM   4436  O  OD1 . ASP   B  1 132 ? -4.453  -11.352 15.120   1.00 30.93  ? 433  ASP   B OD1 1 
ATOM   4437  O  OD2 . ASP   B  1 132 ? -6.600  -11.277 14.659   1.00 32.29  ? 433  ASP   B OD2 1 
ATOM   4438  N  N   . ALA   B  1 133 ? -8.923  -9.164  14.254   1.00 29.15  ? 434  ALA   B N   1 
ATOM   4439  C  CA  . ALA   B  1 133 ? -10.126 -9.333  15.053   1.00 25.09  ? 434  ALA   B CA  1 
ATOM   4440  C  C   . ALA   B  1 133 ? -10.458 -10.806 15.259   1.00 24.97  ? 434  ALA   B C   1 
ATOM   4441  O  O   . ALA   B  1 133 ? -11.623 -11.168 15.435   1.00 24.26  ? 434  ALA   B O   1 
ATOM   4442  C  CB  . ALA   B  1 133 ? -11.308 -8.602  14.415   1.00 25.31  ? 434  ALA   B CB  1 
ATOM   4443  N  N   . ARG   B  1 134 ? -9.446  -11.673 15.247   1.00 20.72  ? 435  ARG   B N   1 
ATOM   4444  C  CA  . ARG   B  1 134 ? -9.740  -13.095 15.372   1.00 28.57  ? 435  ARG   B CA  1 
ATOM   4445  C  C   . ARG   B  1 134 ? -10.146 -13.511 16.783   1.00 24.01  ? 435  ARG   B C   1 
ATOM   4446  O  O   . ARG   B  1 134 ? -10.590 -14.646 16.958   1.00 27.43  ? 435  ARG   B O   1 
ATOM   4447  C  CB  . ARG   B  1 134 ? -8.550  -13.918 14.903   1.00 23.17  ? 435  ARG   B CB  1 
ATOM   4448  C  CG  . ARG   B  1 134 ? -8.314  -13.835 13.393   1.00 25.63  ? 435  ARG   B CG  1 
ATOM   4449  C  CD  . ARG   B  1 134 ? -7.029  -14.548 13.054   1.00 23.50  ? 435  ARG   B CD  1 
ATOM   4450  N  NE  . ARG   B  1 134 ? -5.902  -13.899 13.714   1.00 24.39  ? 435  ARG   B NE  1 
ATOM   4451  C  CZ  . ARG   B  1 134 ? -4.680  -14.411 13.761   1.00 29.88  ? 435  ARG   B CZ  1 
ATOM   4452  N  NH1 . ARG   B  1 134 ? -4.436  -15.589 13.201   1.00 31.32  ? 435  ARG   B NH1 1 
ATOM   4453  N  NH2 . ARG   B  1 134 ? -3.712  -13.749 14.369   1.00 23.11  ? 435  ARG   B NH2 1 
ATOM   4454  N  N   . ASP   B  1 135 ? -10.053 -12.630 17.776   1.00 21.78  ? 436  ASP   B N   1 
ATOM   4455  C  CA  . ASP   B  1 135 ? -10.563 -12.954 19.108   1.00 29.11  ? 436  ASP   B CA  1 
ATOM   4456  C  C   . ASP   B  1 135 ? -12.038 -12.610 19.267   1.00 28.99  ? 436  ASP   B C   1 
ATOM   4457  O  O   . ASP   B  1 135 ? -12.607 -12.849 20.333   1.00 26.60  ? 436  ASP   B O   1 
ATOM   4458  C  CB  . ASP   B  1 135 ? -9.755  -12.225 20.183   1.00 27.66  ? 436  ASP   B CB  1 
ATOM   4459  C  CG  . ASP   B  1 135 ? -9.912  -10.723 20.104   1.00 30.11  ? 436  ASP   B CG  1 
ATOM   4460  O  OD1 . ASP   B  1 135 ? -9.518  -10.032 21.071   1.00 33.10  ? 436  ASP   B OD1 1 
ATOM   4461  O  OD2 . ASP   B  1 135 ? -10.427 -10.230 19.072   1.00 36.56  ? 436  ASP   B OD2 1 
ATOM   4462  N  N   . CYS   B  1 136 ? -12.653 -12.038 18.241   1.00 28.09  ? 437  CYS   B N   1 
ATOM   4463  C  CA  . CYS   B  1 136 ? -14.046 -11.620 18.318   1.00 25.20  ? 437  CYS   B CA  1 
ATOM   4464  C  C   . CYS   B  1 136 ? -14.977 -12.825 18.414   1.00 25.47  ? 437  CYS   B C   1 
ATOM   4465  O  O   . CYS   B  1 136 ? -14.742 -13.857 17.782   1.00 27.99  ? 437  CYS   B O   1 
ATOM   4466  C  CB  . CYS   B  1 136 ? -14.382 -10.790 17.083   1.00 32.85  ? 437  CYS   B CB  1 
ATOM   4467  S  SG  . CYS   B  1 136 ? -15.900 -9.890  17.157   1.00 28.91  ? 437  CYS   B SG  1 
ATOM   4468  N  N   . THR   B  1 137 ? -16.057 -12.695 19.197   1.00 23.70  ? 438  THR   B N   1 
ATOM   4469  C  CA  . THR   B  1 137 ? -16.994 -13.802 19.376   1.00 23.06  ? 438  THR   B CA  1 
ATOM   4470  C  C   . THR   B  1 137 ? -18.453 -13.436 19.162   1.00 26.71  ? 438  THR   B C   1 
ATOM   4471  O  O   . THR   B  1 137 ? -19.288 -14.344 19.107   1.00 28.94  ? 438  THR   B O   1 
ATOM   4472  C  CB  . THR   B  1 137 ? -16.889 -14.399 20.788   1.00 25.56  ? 438  THR   B CB  1 
ATOM   4473  O  OG1 . THR   B  1 137 ? -17.379 -13.440 21.736   1.00 28.69  ? 438  THR   B OG1 1 
ATOM   4474  C  CG2 . THR   B  1 137 ? -15.450 -14.792 21.126   1.00 33.40  ? 438  THR   B CG2 1 
ATOM   4475  N  N   . THR   B  1 138 ? -18.795 -12.155 19.088   1.00 22.59  ? 439  THR   B N   1 
ATOM   4476  C  CA  . THR   B  1 138 ? -20.187 -11.735 19.035   1.00 27.16  ? 439  THR   B CA  1 
ATOM   4477  C  C   . THR   B  1 138 ? -20.332 -10.580 18.057   1.00 25.49  ? 439  THR   B C   1 
ATOM   4478  O  O   . THR   B  1 138 ? -19.366 -9.881  17.734   1.00 23.55  ? 439  THR   B O   1 
ATOM   4479  C  CB  . THR   B  1 138 ? -20.711 -11.288 20.411   1.00 26.09  ? 439  THR   B CB  1 
ATOM   4480  O  OG1 . THR   B  1 138 ? -19.996 -10.110 20.805   1.00 23.82  ? 439  THR   B OG1 1 
ATOM   4481  C  CG2 . THR   B  1 138 ? -20.534 -12.393 21.470   1.00 23.98  ? 439  THR   B CG2 1 
ATOM   4482  N  N   . ALA   B  1 139 ? -21.571 -10.368 17.608   1.00 29.22  ? 440  ALA   B N   1 
ATOM   4483  C  CA  . ALA   B  1 139 ? -21.832 -9.263  16.693   1.00 27.14  ? 440  ALA   B CA  1 
ATOM   4484  C  C   . ALA   B  1 139 ? -21.509 -7.926  17.339   1.00 24.46  ? 440  ALA   B C   1 
ATOM   4485  O  O   . ALA   B  1 139 ? -21.055 -6.998  16.655   1.00 22.17  ? 440  ALA   B O   1 
ATOM   4486  C  CB  . ALA   B  1 139 ? -23.284 -9.287  16.227   1.00 22.12  ? 440  ALA   B CB  1 
ATOM   4487  N  N   . HIS   B  1 140 ? -21.719 -7.808  18.654   1.00 26.52  ? 441  HIS   B N   1 
ATOM   4488  C  CA  . HIS   B  1 140 ? -21.335 -6.572  19.331   1.00 23.05  ? 441  HIS   B CA  1 
ATOM   4489  C  C   . HIS   B  1 140 ? -19.846 -6.329  19.213   1.00 22.98  ? 441  HIS   B C   1 
ATOM   4490  O  O   . HIS   B  1 140 ? -19.413 -5.197  18.977   1.00 23.15  ? 441  HIS   B O   1 
ATOM   4491  C  CB  . HIS   B  1 140 ? -21.722 -6.624  20.806   1.00 22.92  ? 441  HIS   B CB  1 
ATOM   4492  C  CG  . HIS   B  1 140 ? -23.143 -6.256  21.058   1.00 26.33  ? 441  HIS   B CG  1 
ATOM   4493  N  ND1 . HIS   B  1 140 ? -24.178 -7.151  20.903   1.00 30.87  ? 441  HIS   B ND1 1 
ATOM   4494  C  CD2 . HIS   B  1 140 ? -23.706 -5.086  21.432   1.00 30.08  ? 441  HIS   B CD2 1 
ATOM   4495  C  CE1 . HIS   B  1 140 ? -25.320 -6.553  21.186   1.00 33.11  ? 441  HIS   B CE1 1 
ATOM   4496  N  NE2 . HIS   B  1 140 ? -25.062 -5.298  21.507   1.00 34.94  ? 441  HIS   B NE2 1 
ATOM   4497  N  N   . GLY   B  1 141 ? -19.044 -7.379  19.413   1.00 25.22  ? 442  GLY   B N   1 
ATOM   4498  C  CA  . GLY   B  1 141 ? -17.615 -7.244  19.218   1.00 23.16  ? 442  GLY   B CA  1 
ATOM   4499  C  C   . GLY   B  1 141 ? -17.272 -6.838  17.799   1.00 27.01  ? 442  GLY   B C   1 
ATOM   4500  O  O   . GLY   B  1 141 ? -16.396 -5.999  17.580   1.00 21.93  ? 442  GLY   B O   1 
ATOM   4501  N  N   . MET   B  1 142 ? -17.962 -7.425  16.814   1.00 23.10  ? 443  MET   B N   1 
ATOM   4502  C  CA  . MET   B  1 142 ? -17.712 -7.045  15.425   1.00 24.89  ? 443  MET   B CA  1 
ATOM   4503  C  C   . MET   B  1 142 ? -18.015 -5.574  15.208   1.00 20.04  ? 443  MET   B C   1 
ATOM   4504  O  O   . MET   B  1 142 ? -17.251 -4.869  14.537   1.00 20.43  ? 443  MET   B O   1 
ATOM   4505  C  CB  . MET   B  1 142 ? -18.552 -7.890  14.459   1.00 27.76  ? 443  MET   B CB  1 
ATOM   4506  C  CG  . MET   B  1 142 ? -18.301 -9.374  14.546   1.00 25.10  ? 443  MET   B CG  1 
ATOM   4507  S  SD  . MET   B  1 142 ? -19.389 -10.306 13.445   1.00 26.26  ? 443  MET   B SD  1 
ATOM   4508  C  CE  . MET   B  1 142 ? -18.851 -9.736  11.809   1.00 19.76  ? 443  MET   B CE  1 
ATOM   4509  N  N   . PHE   B  1 143 ? -19.133 -5.099  15.769   1.00 24.54  ? 444  PHE   B N   1 
ATOM   4510  C  CA  . PHE   B  1 143 ? -19.497 -3.695  15.634   1.00 23.71  ? 444  PHE   B CA  1 
ATOM   4511  C  C   . PHE   B  1 143 ? -18.396 -2.799  16.171   1.00 26.86  ? 444  PHE   B C   1 
ATOM   4512  O  O   . PHE   B  1 143 ? -17.999 -1.816  15.525   1.00 27.16  ? 444  PHE   B O   1 
ATOM   4513  C  CB  . PHE   B  1 143 ? -20.807 -3.421  16.372   1.00 24.35  ? 444  PHE   B CB  1 
ATOM   4514  C  CG  . PHE   B  1 143 ? -21.165 -1.974  16.427   1.00 27.46  ? 444  PHE   B CG  1 
ATOM   4515  C  CD1 . PHE   B  1 143 ? -21.146 -1.283  17.626   1.00 30.97  ? 444  PHE   B CD1 1 
ATOM   4516  C  CD2 . PHE   B  1 143 ? -21.494 -1.291  15.262   1.00 28.21  ? 444  PHE   B CD2 1 
ATOM   4517  C  CE1 . PHE   B  1 143 ? -21.481 0.070   17.667   1.00 33.76  ? 444  PHE   B CE1 1 
ATOM   4518  C  CE2 . PHE   B  1 143 ? -21.835 0.042   15.294   1.00 29.06  ? 444  PHE   B CE2 1 
ATOM   4519  C  CZ  . PHE   B  1 143 ? -21.827 0.728   16.500   1.00 35.48  ? 444  PHE   B CZ  1 
ATOM   4520  N  N   . ASN   B  1 144 ? -17.895 -3.129  17.365   1.00 24.96  ? 445  ASN   B N   1 
ATOM   4521  C  CA  . ASN   B  1 144 ? -16.819 -2.359  17.968   1.00 23.42  ? 445  ASN   B CA  1 
ATOM   4522  C  C   . ASN   B  1 144 ? -15.581 -2.373  17.074   1.00 21.61  ? 445  ASN   B C   1 
ATOM   4523  O  O   . ASN   B  1 144 ? -14.999 -1.323  16.781   1.00 21.56  ? 445  ASN   B O   1 
ATOM   4524  C  CB  . ASN   B  1 144 ? -16.533 -2.926  19.372   1.00 25.58  ? 445  ASN   B CB  1 
ATOM   4525  C  CG  . ASN   B  1 144 ? -15.470 -2.156  20.122   1.00 31.01  ? 445  ASN   B CG  1 
ATOM   4526  O  OD1 . ASN   B  1 144 ? -14.455 -2.719  20.525   1.00 39.65  ? 445  ASN   B OD1 1 
ATOM   4527  N  ND2 . ASN   B  1 144 ? -15.699 -0.865  20.323   1.00 31.08  ? 445  ASN   B ND2 1 
ATOM   4528  N  N   . TYR   B  1 145 ? -15.181 -3.560  16.606   1.00 24.01  ? 446  TYR   B N   1 
ATOM   4529  C  CA  . TYR   B  1 145 ? -14.047 -3.651  15.691   1.00 23.53  ? 446  TYR   B CA  1 
ATOM   4530  C  C   . TYR   B  1 145 ? -14.275 -2.835  14.417   1.00 26.49  ? 446  TYR   B C   1 
ATOM   4531  O  O   . TYR   B  1 145 ? -13.340 -2.228  13.882   1.00 21.44  ? 446  TYR   B O   1 
ATOM   4532  C  CB  . TYR   B  1 145 ? -13.785 -5.110  15.323   1.00 20.97  ? 446  TYR   B CB  1 
ATOM   4533  C  CG  . TYR   B  1 145 ? -12.767 -5.804  16.200   1.00 25.28  ? 446  TYR   B CG  1 
ATOM   4534  C  CD1 . TYR   B  1 145 ? -13.134 -6.854  17.029   1.00 21.21  ? 446  TYR   B CD1 1 
ATOM   4535  C  CD2 . TYR   B  1 145 ? -11.433 -5.405  16.190   1.00 25.62  ? 446  TYR   B CD2 1 
ATOM   4536  C  CE1 . TYR   B  1 145 ? -12.193 -7.495  17.832   1.00 22.12  ? 446  TYR   B CE1 1 
ATOM   4537  C  CE2 . TYR   B  1 145 ? -10.498 -6.034  16.966   1.00 22.75  ? 446  TYR   B CE2 1 
ATOM   4538  C  CZ  . TYR   B  1 145 ? -10.874 -7.073  17.788   1.00 25.59  ? 446  TYR   B CZ  1 
ATOM   4539  O  OH  . TYR   B  1 145 ? -9.905  -7.678  18.559   1.00 29.35  ? 446  TYR   B OH  1 
ATOM   4540  N  N   . ILE   B  1 146 ? -15.500 -2.824  13.901   1.00 21.37  ? 447  ILE   B N   1 
ATOM   4541  C  CA  . ILE   B  1 146 ? -15.736 -2.126  12.635   1.00 21.58  ? 447  ILE   B CA  1 
ATOM   4542  C  C   . ILE   B  1 146 ? -15.735 -0.617  12.845   1.00 26.12  ? 447  ILE   B C   1 
ATOM   4543  O  O   . ILE   B  1 146 ? -15.194 0.134   12.024   1.00 23.33  ? 447  ILE   B O   1 
ATOM   4544  C  CB  . ILE   B  1 146 ? -17.043 -2.615  11.990   1.00 20.84  ? 447  ILE   B CB  1 
ATOM   4545  C  CG1 . ILE   B  1 146 ? -16.848 -4.030  11.450   1.00 25.10  ? 447  ILE   B CG1 1 
ATOM   4546  C  CG2 . ILE   B  1 146 ? -17.495 -1.648  10.864   1.00 22.77  ? 447  ILE   B CG2 1 
ATOM   4547  C  CD1 . ILE   B  1 146 ? -18.142 -4.773  11.205   1.00 25.29  ? 447  ILE   B CD1 1 
ATOM   4548  N  N   . CYS   B  1 147 ? -16.311 -0.147  13.958   1.00 23.19  ? 448  CYS   B N   1 
ATOM   4549  C  CA  . CYS   B  1 147 ? -16.238 1.278   14.272   1.00 19.83  ? 448  CYS   B CA  1 
ATOM   4550  C  C   . CYS   B  1 147 ? -14.797 1.735   14.374   1.00 24.87  ? 448  CYS   B C   1 
ATOM   4551  O  O   . CYS   B  1 147 ? -14.429 2.791   13.839   1.00 26.14  ? 448  CYS   B O   1 
ATOM   4552  C  CB  . CYS   B  1 147 ? -16.967 1.580   15.585   1.00 22.42  ? 448  CYS   B CB  1 
ATOM   4553  S  SG  . CYS   B  1 147 ? -18.711 1.362   15.475   1.00 32.02  ? 448  CYS   B SG  1 
ATOM   4554  N  N   . ASN   B  1 148 ? -13.969 0.961   15.087   1.00 19.90  ? 449  ASN   B N   1 
ATOM   4555  C  CA  . ASN   B  1 148 ? -12.556 1.311   15.199   1.00 26.88  ? 449  ASN   B CA  1 
ATOM   4556  C  C   . ASN   B  1 148 ? -11.903 1.350   13.822   1.00 19.61  ? 449  ASN   B C   1 
ATOM   4557  O  O   . ASN   B  1 148 ? -11.106 2.251   13.521   1.00 23.32  ? 449  ASN   B O   1 
ATOM   4558  C  CB  . ASN   B  1 148 ? -11.839 0.316   16.111   1.00 20.18  ? 449  ASN   B CB  1 
ATOM   4559  C  CG  . ASN   B  1 148 ? -12.309 0.413   17.574   1.00 30.60  ? 449  ASN   B CG  1 
ATOM   4560  O  OD1 . ASN   B  1 148 ? -13.030 1.347   17.948   1.00 24.35  ? 449  ASN   B OD1 1 
ATOM   4561  N  ND2 . ASN   B  1 148 ? -11.873 -0.542  18.406   1.00 20.90  ? 449  ASN   B ND2 1 
ATOM   4562  N  N   . HIS   B  1 149 ? -12.226 0.371   12.982   1.00 20.90  ? 450  HIS   B N   1 
ATOM   4563  C  CA  . HIS   B  1 149 ? -11.759 0.378   11.600   1.00 21.90  ? 450  HIS   B CA  1 
ATOM   4564  C  C   . HIS   B  1 149 ? -12.201 1.649   10.882   1.00 18.85  ? 450  HIS   B C   1 
ATOM   4565  O  O   . HIS   B  1 149 ? -11.384 2.362   10.286   1.00 20.32  ? 450  HIS   B O   1 
ATOM   4566  C  CB  . HIS   B  1 149 ? -12.292 -0.870  10.882   1.00 18.53  ? 450  HIS   B CB  1 
ATOM   4567  C  CG  . HIS   B  1 149 ? -11.883 -0.973  9.439    1.00 25.41  ? 450  HIS   B CG  1 
ATOM   4568  N  ND1 . HIS   B  1 149 ? -11.426 -2.147  8.886    1.00 23.37  ? 450  HIS   B ND1 1 
ATOM   4569  C  CD2 . HIS   B  1 149 ? -11.882 -0.061  8.434    1.00 22.78  ? 450  HIS   B CD2 1 
ATOM   4570  C  CE1 . HIS   B  1 149 ? -11.161 -1.957  7.605    1.00 23.08  ? 450  HIS   B CE1 1 
ATOM   4571  N  NE2 . HIS   B  1 149 ? -11.414 -0.694  7.312    1.00 20.88  ? 450  HIS   B NE2 1 
ATOM   4572  N  N   . VAL   B  1 150 ? -13.498 1.939   10.913   1.00 18.90  ? 451  VAL   B N   1 
ATOM   4573  C  CA  . VAL   B  1 150 ? -14.000 3.114   10.211   1.00 18.97  ? 451  VAL   B CA  1 
ATOM   4574  C  C   . VAL   B  1 150 ? -13.291 4.363   10.696   1.00 22.17  ? 451  VAL   B C   1 
ATOM   4575  O  O   . VAL   B  1 150 ? -12.833 5.194   9.905    1.00 21.01  ? 451  VAL   B O   1 
ATOM   4576  C  CB  . VAL   B  1 150 ? -15.519 3.239   10.385   1.00 24.27  ? 451  VAL   B CB  1 
ATOM   4577  C  CG1 . VAL   B  1 150 ? -15.955 4.627   9.961    1.00 19.37  ? 451  VAL   B CG1 1 
ATOM   4578  C  CG2 . VAL   B  1 150 ? -16.214 2.162   9.554    1.00 23.18  ? 451  VAL   B CG2 1 
ATOM   4579  N  N   . LYS   B  1 151 ? -13.180 4.511   12.015   1.00 24.86  ? 452  LYS   B N   1 
ATOM   4580  C  CA  . LYS   B  1 151 ? -12.590 5.723   12.555   1.00 20.61  ? 452  LYS   B CA  1 
ATOM   4581  C  C   . LYS   B  1 151 ? -11.124 5.831   12.169   1.00 20.72  ? 452  LYS   B C   1 
ATOM   4582  O  O   . LYS   B  1 151 ? -10.644 6.910   11.818   1.00 23.01  ? 452  LYS   B O   1 
ATOM   4583  C  CB  . LYS   B  1 151 ? -12.749 5.732   14.089   1.00 20.63  ? 452  LYS   B CB  1 
ATOM   4584  C  CG  . LYS   B  1 151 ? -12.279 7.024   14.734   1.00 21.24  ? 452  LYS   B CG  1 
ATOM   4585  C  CD  . LYS   B  1 151 ? -12.677 6.993   16.214   1.00 24.67  ? 452  LYS   B CD  1 
ATOM   4586  C  CE  . LYS   B  1 151 ? -12.581 8.361   16.856   1.00 31.92  ? 452  LYS   B CE  1 
ATOM   4587  N  NZ  . LYS   B  1 151 ? -13.137 8.317   18.248   1.00 34.72  ? 452  LYS   B NZ  1 
ATOM   4588  N  N   . TYR   B  1 152 ? -10.388 4.723   12.257   1.00 20.71  ? 453  TYR   B N   1 
ATOM   4589  C  CA  . TYR   B  1 152 ? -8.980  4.764   11.895   1.00 22.74  ? 453  TYR   B CA  1 
ATOM   4590  C  C   . TYR   B  1 152 ? -8.816  5.026   10.405   1.00 21.40  ? 453  TYR   B C   1 
ATOM   4591  O  O   . TYR   B  1 152 ? -7.966  5.822   9.992    1.00 22.96  ? 453  TYR   B O   1 
ATOM   4592  C  CB  . TYR   B  1 152 ? -8.299  3.449   12.250   1.00 21.76  ? 453  TYR   B CB  1 
ATOM   4593  C  CG  . TYR   B  1 152 ? -6.904  3.366   11.681   1.00 23.44  ? 453  TYR   B CG  1 
ATOM   4594  C  CD1 . TYR   B  1 152 ? -5.817  3.795   12.430   1.00 31.24  ? 453  TYR   B CD1 1 
ATOM   4595  C  CD2 . TYR   B  1 152 ? -6.672  2.880   10.393   1.00 25.32  ? 453  TYR   B CD2 1 
ATOM   4596  C  CE1 . TYR   B  1 152 ? -4.542  3.738   11.925   1.00 32.72  ? 453  TYR   B CE1 1 
ATOM   4597  C  CE2 . TYR   B  1 152 ? -5.396  2.824   9.880    1.00 28.58  ? 453  TYR   B CE2 1 
ATOM   4598  C  CZ  . TYR   B  1 152 ? -4.335  3.255   10.658   1.00 32.49  ? 453  TYR   B CZ  1 
ATOM   4599  O  OH  . TYR   B  1 152 ? -3.053  3.208   10.172   1.00 40.44  ? 453  TYR   B OH  1 
ATOM   4600  N  N   . ALA   B  1 153 ? -9.603  4.339   9.592    1.00 21.54  ? 454  ALA   B N   1 
ATOM   4601  C  CA  . ALA   B  1 153 ? -9.448  4.461   8.148    1.00 20.56  ? 454  ALA   B CA  1 
ATOM   4602  C  C   . ALA   B  1 153 ? -9.825  5.861   7.688    1.00 26.97  ? 454  ALA   B C   1 
ATOM   4603  O  O   . ALA   B  1 153 ? -9.132  6.454   6.856    1.00 29.38  ? 454  ALA   B O   1 
ATOM   4604  C  CB  . ALA   B  1 153 ? -10.305 3.393   7.454    1.00 18.58  ? 454  ALA   B CB  1 
ATOM   4605  N  N   . THR   B  1 154 ? -10.901 6.414   8.256    1.00 30.49  ? 455  THR   B N   1 
ATOM   4606  C  CA  . THR   B  1 154 ? -11.400 7.710   7.820    1.00 25.07  ? 455  THR   B CA  1 
ATOM   4607  C  C   . THR   B  1 154 ? -10.448 8.834   8.210    1.00 28.29  ? 455  THR   B C   1 
ATOM   4608  O  O   . THR   B  1 154 ? -10.179 9.732   7.400    1.00 33.31  ? 455  THR   B O   1 
ATOM   4609  C  CB  . THR   B  1 154 ? -12.794 7.943   8.390    1.00 30.07  ? 455  THR   B CB  1 
ATOM   4610  O  OG1 . THR   B  1 154 ? -13.680 6.928   7.886    1.00 26.85  ? 455  THR   B OG1 1 
ATOM   4611  C  CG2 . THR   B  1 154 ? -13.306 9.302   7.971    1.00 26.55  ? 455  THR   B CG2 1 
ATOM   4612  N  N   . ASN   B  1 155 ? -9.931  8.806   9.442    1.00 26.14  ? 456  ASN   B N   1 
ATOM   4613  C  CA  . ASN   B  1 155 ? -8.831  9.687   9.839    1.00 24.92  ? 456  ASN   B CA  1 
ATOM   4614  C  C   . ASN   B  1 155 ? -9.126  11.145  9.473    1.00 28.65  ? 456  ASN   B C   1 
ATOM   4615  O  O   . ASN   B  1 155 ? -8.268  11.864  8.952    1.00 26.54  ? 456  ASN   B O   1 
ATOM   4616  C  CB  . ASN   B  1 155 ? -7.525  9.191   9.199    1.00 21.13  ? 456  ASN   B CB  1 
ATOM   4617  C  CG  . ASN   B  1 155 ? -6.289  9.878   9.753    1.00 29.28  ? 456  ASN   B CG  1 
ATOM   4618  O  OD1 . ASN   B  1 155 ? -6.243  10.270  10.907   1.00 28.92  ? 456  ASN   B OD1 1 
ATOM   4619  N  ND2 . ASN   B  1 155 ? -5.277  10.015  8.918    1.00 25.09  ? 456  ASN   B ND2 1 
ATOM   4620  N  N   . LYS   B  1 156 ? -10.375 11.573  9.705    1.00 24.66  ? 457  LYS   B N   1 
ATOM   4621  C  CA  . LYS   B  1 156 ? -10.809 12.955  9.450    1.00 22.44  ? 457  LYS   B CA  1 
ATOM   4622  C  C   . LYS   B  1 156 ? -10.604 13.384  7.996    1.00 23.67  ? 457  LYS   B C   1 
ATOM   4623  O  O   . LYS   B  1 156 ? -10.361 14.562  7.721    1.00 31.03  ? 457  LYS   B O   1 
ATOM   4624  C  CB  . LYS   B  1 156 ? -10.099 13.949  10.374   1.00 29.05  ? 457  LYS   B CB  1 
ATOM   4625  C  CG  . LYS   B  1 156 ? -10.455 13.784  11.840   1.00 32.93  ? 457  LYS   B CG  1 
ATOM   4626  C  CD  . LYS   B  1 156 ? -9.748  14.827  12.680   1.00 42.11  ? 457  LYS   B CD  1 
ATOM   4627  C  CE  . LYS   B  1 156 ? -10.064 14.632  14.164   1.00 50.77  ? 457  LYS   B CE  1 
ATOM   4628  N  NZ  . LYS   B  1 156 ? -8.901  14.995  15.038   1.00 51.30  ? 457  LYS   B NZ  1 
ATOM   4629  N  N   . GLY   B  1 157 ? -10.684 12.444  7.062    1.00 24.67  ? 458  GLY   B N   1 
ATOM   4630  C  CA  . GLY   B  1 157 ? -10.550 12.725  5.648    1.00 27.61  ? 458  GLY   B CA  1 
ATOM   4631  C  C   . GLY   B  1 157 ? -9.222  12.328  5.051    1.00 29.48  ? 458  GLY   B C   1 
ATOM   4632  O  O   . GLY   B  1 157 ? -9.114  12.213  3.823    1.00 24.36  ? 458  GLY   B O   1 
ATOM   4633  N  N   . ASN   B  1 158 ? -8.207  12.119  5.880    1.00 24.50  ? 459  ASN   B N   1 
ATOM   4634  C  CA  . ASN   B  1 158 ? -6.898  11.700  5.388    1.00 28.24  ? 459  ASN   B CA  1 
ATOM   4635  C  C   . ASN   B  1 158 ? -6.879  10.180  5.431    1.00 29.42  ? 459  ASN   B C   1 
ATOM   4636  O  O   . ASN   B  1 158 ? -6.292  9.561   6.321    1.00 27.23  ? 459  ASN   B O   1 
ATOM   4637  C  CB  . ASN   B  1 158 ? -5.788  12.305  6.234    1.00 32.93  ? 459  ASN   B CB  1 
ATOM   4638  C  CG  . ASN   B  1 158 ? -4.412  12.002  5.690    1.00 38.85  ? 459  ASN   B CG  1 
ATOM   4639  O  OD1 . ASN   B  1 158 ? -4.254  11.638  4.520    1.00 38.69  ? 459  ASN   B OD1 1 
ATOM   4640  N  ND2 . ASN   B  1 158 ? -3.401  12.154  6.536    1.00 35.78  ? 459  ASN   B ND2 1 
ATOM   4641  N  N   . LEU   B  1 159 ? -7.542  9.575   4.444    1.00 25.95  ? 460  LEU   B N   1 
ATOM   4642  C  CA  . LEU   B  1 159 ? -7.887  8.160   4.541    1.00 23.91  ? 460  LEU   B CA  1 
ATOM   4643  C  C   . LEU   B  1 159 ? -6.657  7.264   4.534    1.00 25.95  ? 460  LEU   B C   1 
ATOM   4644  O  O   . LEU   B  1 159 ? -5.660  7.530   3.859    1.00 26.13  ? 460  LEU   B O   1 
ATOM   4645  C  CB  . LEU   B  1 159 ? -8.810  7.729   3.400    1.00 23.16  ? 460  LEU   B CB  1 
ATOM   4646  C  CG  . LEU   B  1 159 ? -10.093 8.524   3.156    1.00 39.80  ? 460  LEU   B CG  1 
ATOM   4647  C  CD1 . LEU   B  1 159 ? -11.056 7.725   2.265    1.00 38.26  ? 460  LEU   B CD1 1 
ATOM   4648  C  CD2 . LEU   B  1 159 ? -10.754 8.893   4.445    1.00 34.10  ? 460  LEU   B CD2 1 
ATOM   4649  N  N   . ARG   B  1 160 ? -6.754  6.170   5.274    1.00 23.21  ? 461  ARG   B N   1 
ATOM   4650  C  CA  . ARG   B  1 160 ? -5.681  5.199   5.398    1.00 21.16  ? 461  ARG   B CA  1 
ATOM   4651  C  C   . ARG   B  1 160 ? -6.270  3.834   5.104    1.00 26.53  ? 461  ARG   B C   1 
ATOM   4652  O  O   . ARG   B  1 160 ? -7.349  3.501   5.607    1.00 22.43  ? 461  ARG   B O   1 
ATOM   4653  C  CB  . ARG   B  1 160 ? -5.072  5.214   6.806    1.00 28.98  ? 461  ARG   B CB  1 
ATOM   4654  C  CG  . ARG   B  1 160 ? -4.577  6.571   7.256    1.00 23.82  ? 461  ARG   B CG  1 
ATOM   4655  C  CD  . ARG   B  1 160 ? -3.996  6.487   8.644    1.00 26.58  ? 461  ARG   B CD  1 
ATOM   4656  N  NE  . ARG   B  1 160 ? -5.029  6.524   9.677    1.00 29.98  ? 461  ARG   B NE  1 
ATOM   4657  C  CZ  . ARG   B  1 160 ? -4.798  6.938   10.920   1.00 29.69  ? 461  ARG   B CZ  1 
ATOM   4658  N  NH1 . ARG   B  1 160 ? -3.579  7.322   11.257   1.00 27.06  ? 461  ARG   B NH1 1 
ATOM   4659  N  NH2 . ARG   B  1 160 ? -5.771  6.963   11.820   1.00 25.49  ? 461  ARG   B NH2 1 
ATOM   4660  N  N   . SER   B  1 161 ? -5.563  3.053   4.298    1.00 23.76  ? 462  SER   B N   1 
ATOM   4661  C  CA  . SER   B  1 161 ? -6.022  1.714   3.972    1.00 27.06  ? 462  SER   B CA  1 
ATOM   4662  C  C   . SER   B  1 161 ? -6.015  0.835   5.210    1.00 25.14  ? 462  SER   B C   1 
ATOM   4663  O  O   . SER   B  1 161 ? -5.094  0.889   6.026    1.00 20.07  ? 462  SER   B O   1 
ATOM   4664  C  CB  . SER   B  1 161 ? -5.125  1.102   2.908    1.00 22.59  ? 462  SER   B CB  1 
ATOM   4665  O  OG  . SER   B  1 161 ? -5.061  1.982   1.801    1.00 43.13  ? 462  SER   B OG  1 
ATOM   4666  N  N   . ALA   B  1 162 ? -7.024  -0.015  5.325    1.00 20.39  ? 463  ALA   B N   1 
ATOM   4667  C  CA  . ALA   B  1 162 ? -7.076  -0.875  6.491    1.00 20.02  ? 463  ALA   B CA  1 
ATOM   4668  C  C   . ALA   B  1 162 ? -7.968  -2.058  6.171    1.00 25.19  ? 463  ALA   B C   1 
ATOM   4669  O  O   . ALA   B  1 162 ? -8.825  -1.986  5.289    1.00 22.20  ? 463  ALA   B O   1 
ATOM   4670  C  CB  . ALA   B  1 162 ? -7.592  -0.118  7.728    1.00 18.80  ? 463  ALA   B CB  1 
ATOM   4671  N  N   . ILE   B  1 163 ? -7.731  -3.151  6.886    1.00 27.04  ? 464  ILE   B N   1 
ATOM   4672  C  CA  . ILE   B  1 163 ? -8.569  -4.341  6.833    1.00 23.63  ? 464  ILE   B CA  1 
ATOM   4673  C  C   . ILE   B  1 163 ? -8.752  -4.829  8.263    1.00 24.61  ? 464  ILE   B C   1 
ATOM   4674  O  O   . ILE   B  1 163 ? -7.839  -4.725  9.089    1.00 23.04  ? 464  ILE   B O   1 
ATOM   4675  C  CB  . ILE   B  1 163 ? -7.945  -5.439  5.943    1.00 18.15  ? 464  ILE   B CB  1 
ATOM   4676  C  CG1 . ILE   B  1 163 ? -8.830  -6.681  5.905    1.00 17.71  ? 464  ILE   B CG1 1 
ATOM   4677  C  CG2 . ILE   B  1 163 ? -6.578  -5.816  6.454    1.00 18.09  ? 464  ILE   B CG2 1 
ATOM   4678  C  CD1 . ILE   B  1 163 ? -8.519  -7.598  4.703    1.00 19.44  ? 464  ILE   B CD1 1 
ATOM   4679  N  N   . THR   B  1 164 ? -9.928  -5.357  8.559    1.00 24.77  ? 465  THR   B N   1 
ATOM   4680  C  CA  . THR   B  1 164 ? -10.183 -5.991  9.841    1.00 25.93  ? 465  THR   B CA  1 
ATOM   4681  C  C   . THR   B  1 164 ? -10.558 -7.438  9.582    1.00 26.72  ? 465  THR   B C   1 
ATOM   4682  O  O   . THR   B  1 164 ? -11.480 -7.713  8.810    1.00 22.46  ? 465  THR   B O   1 
ATOM   4683  C  CB  . THR   B  1 164 ? -11.286 -5.264  10.603   1.00 25.20  ? 465  THR   B CB  1 
ATOM   4684  O  OG1 . THR   B  1 164 ? -10.825 -3.948  10.923   1.00 24.82  ? 465  THR   B OG1 1 
ATOM   4685  C  CG2 . THR   B  1 164 ? -11.623 -6.014  11.896   1.00 25.68  ? 465  THR   B CG2 1 
ATOM   4686  N  N   . ILE   B  1 165 ? -9.837  -8.358  10.205   1.00 22.17  ? 466  ILE   B N   1 
ATOM   4687  C  CA  . ILE   B  1 165 ? -9.975  -9.773  9.899    1.00 22.42  ? 466  ILE   B CA  1 
ATOM   4688  C  C   . ILE   B  1 165 ? -10.603 -10.480 11.098   1.00 22.28  ? 466  ILE   B C   1 
ATOM   4689  O  O   . ILE   B  1 165 ? -10.000 -10.580 12.174   1.00 25.90  ? 466  ILE   B O   1 
ATOM   4690  C  CB  . ILE   B  1 165 ? -8.628  -10.390 9.501    1.00 28.21  ? 466  ILE   B CB  1 
ATOM   4691  C  CG1 . ILE   B  1 165 ? -8.086  -9.696  8.230    1.00 26.93  ? 466  ILE   B CG1 1 
ATOM   4692  C  CG2 . ILE   B  1 165 ? -8.816  -11.855 9.217    1.00 19.15  ? 466  ILE   B CG2 1 
ATOM   4693  C  CD1 . ILE   B  1 165 ? -6.633  -10.039 7.921    1.00 19.90  ? 466  ILE   B CD1 1 
ATOM   4694  N  N   . PHE   B  1 166 ? -11.816 -10.974 10.896   1.00 25.52  ? 467  PHE   B N   1 
ATOM   4695  C  CA  . PHE   B  1 166 ? -12.584 -11.708 11.887   1.00 24.77  ? 467  PHE   B CA  1 
ATOM   4696  C  C   . PHE   B  1 166 ? -12.247 -13.188 11.827   1.00 28.47  ? 467  PHE   B C   1 
ATOM   4697  O  O   . PHE   B  1 166 ? -11.520 -13.622 10.941   1.00 24.33  ? 467  PHE   B O   1 
ATOM   4698  C  CB  . PHE   B  1 166 ? -14.057 -11.439 11.649   1.00 19.48  ? 467  PHE   B CB  1 
ATOM   4699  C  CG  . PHE   B  1 166 ? -14.450 -10.037 12.013   1.00 24.16  ? 467  PHE   B CG  1 
ATOM   4700  C  CD1 . PHE   B  1 166 ? -14.511 -9.652  13.351   1.00 22.12  ? 467  PHE   B CD1 1 
ATOM   4701  C  CD2 . PHE   B  1 166 ? -14.716 -9.098  11.025   1.00 25.22  ? 467  PHE   B CD2 1 
ATOM   4702  C  CE1 . PHE   B  1 166 ? -14.861 -8.369  13.702   1.00 23.26  ? 467  PHE   B CE1 1 
ATOM   4703  C  CE2 . PHE   B  1 166 ? -15.076 -7.812  11.359   1.00 30.60  ? 467  PHE   B CE2 1 
ATOM   4704  C  CZ  . PHE   B  1 166 ? -15.139 -7.430  12.714   1.00 22.40  ? 467  PHE   B CZ  1 
ATOM   4705  N  N   . PRO   B  1 167 ? -12.725 -13.994 12.783   1.00 26.46  ? 468  PRO   B N   1 
ATOM   4706  C  CA  . PRO   B  1 167 ? -12.278 -15.391 12.846   1.00 31.75  ? 468  PRO   B CA  1 
ATOM   4707  C  C   . PRO   B  1 167 ? -12.559 -16.159 11.562   1.00 29.85  ? 468  PRO   B C   1 
ATOM   4708  O  O   . PRO   B  1 167 ? -13.569 -15.945 10.884   1.00 24.71  ? 468  PRO   B O   1 
ATOM   4709  C  CB  . PRO   B  1 167 ? -13.071 -15.965 14.031   1.00 24.97  ? 468  PRO   B CB  1 
ATOM   4710  C  CG  . PRO   B  1 167 ? -13.274 -14.795 14.914   1.00 21.33  ? 468  PRO   B CG  1 
ATOM   4711  C  CD  . PRO   B  1 167 ? -13.495 -13.628 13.993   1.00 27.26  ? 468  PRO   B CD  1 
ATOM   4712  N  N   . GLN   B  1 168 ? -11.636 -17.057 11.236   1.00 26.36  ? 469  GLN   B N   1 
ATOM   4713  C  CA  . GLN   B  1 168 ? -11.731 -17.852 10.029   1.00 26.46  ? 469  GLN   B CA  1 
ATOM   4714  C  C   . GLN   B  1 168 ? -12.872 -18.855 10.124   1.00 28.59  ? 469  GLN   B C   1 
ATOM   4715  O  O   . GLN   B  1 168 ? -13.357 -19.205 11.202   1.00 30.56  ? 469  GLN   B O   1 
ATOM   4716  C  CB  . GLN   B  1 168 ? -10.432 -18.600 9.782    1.00 22.96  ? 469  GLN   B CB  1 
ATOM   4717  C  CG  . GLN   B  1 168 ? -10.139 -19.630 10.866   1.00 25.68  ? 469  GLN   B CG  1 
ATOM   4718  C  CD  . GLN   B  1 168 ? -8.664  -19.876 11.018   1.00 29.25  ? 469  GLN   B CD  1 
ATOM   4719  O  OE1 . GLN   B  1 168 ? -7.875  -18.937 11.094   1.00 32.91  ? 469  GLN   B OE1 1 
ATOM   4720  N  NE2 . GLN   B  1 168 ? -8.274  -21.142 11.055   1.00 30.36  ? 469  GLN   B NE2 1 
ATOM   4721  N  N   . ARG   B  1 169 ? -13.288 -19.325 8.960    1.00 26.93  ? 470  ARG   B N   1 
ATOM   4722  C  CA  . ARG   B  1 169 ? -14.304 -20.357 8.884    1.00 25.88  ? 470  ARG   B CA  1 
ATOM   4723  C  C   . ARG   B  1 169 ? -13.810 -21.615 9.579    1.00 26.55  ? 470  ARG   B C   1 
ATOM   4724  O  O   . ARG   B  1 169 ? -12.618 -21.938 9.536    1.00 26.80  ? 470  ARG   B O   1 
ATOM   4725  C  CB  . ARG   B  1 169 ? -14.621 -20.628 7.412    1.00 32.62  ? 470  ARG   B CB  1 
ATOM   4726  C  CG  . ARG   B  1 169 ? -15.584 -21.758 7.147    1.00 42.51  ? 470  ARG   B CG  1 
ATOM   4727  C  CD  . ARG   B  1 169 ? -16.073 -21.697 5.705    1.00 39.77  ? 470  ARG   B CD  1 
ATOM   4728  N  NE  . ARG   B  1 169 ? -16.850 -20.489 5.469    1.00 35.50  ? 470  ARG   B NE  1 
ATOM   4729  C  CZ  . ARG   B  1 169 ? -17.200 -20.046 4.270    1.00 53.21  ? 470  ARG   B CZ  1 
ATOM   4730  N  NH1 . ARG   B  1 169 ? -16.831 -20.717 3.185    1.00 58.07  ? 470  ARG   B NH1 1 
ATOM   4731  N  NH2 . ARG   B  1 169 ? -17.914 -18.930 4.153    1.00 49.98  ? 470  ARG   B NH2 1 
ATOM   4732  N  N   . THR   B  1 170 ? -14.727 -22.317 10.249   1.00 25.70  ? 471  THR   B N   1 
ATOM   4733  C  CA  . THR   B  1 170 ? -14.380 -23.558 10.920   1.00 26.03  ? 471  THR   B CA  1 
ATOM   4734  C  C   . THR   B  1 170 ? -15.103 -24.672 10.187   1.00 31.87  ? 471  THR   B C   1 
ATOM   4735  O  O   . THR   B  1 170 ? -14.539 -25.261 9.248    1.00 35.43  ? 471  THR   B O   1 
ATOM   4736  C  CB  . THR   B  1 170 ? -14.698 -23.499 12.428   1.00 31.00  ? 471  THR   B CB  1 
ATOM   4737  O  OG1 . THR   B  1 170 ? -16.078 -23.168 12.639   1.00 37.04  ? 471  THR   B OG1 1 
ATOM   4738  C  CG2 . THR   B  1 170 ? -13.830 -22.452 13.117   1.00 29.01  ? 471  THR   B CG2 1 
ATOM   4739  N  N   . ASP   B  1 171 ? -16.335 -25.001 10.547   1.00 38.97  ? 472  ASP   B N   1 
ATOM   4740  C  CA  . ASP   B  1 171 ? -17.083 -26.048 9.867    1.00 41.88  ? 472  ASP   B CA  1 
ATOM   4741  C  C   . ASP   B  1 171 ? -18.013 -25.492 8.800    1.00 44.89  ? 472  ASP   B C   1 
ATOM   4742  O  O   . ASP   B  1 171 ? -18.806 -26.247 8.231    1.00 52.65  ? 472  ASP   B O   1 
ATOM   4743  C  CB  . ASP   B  1 171 ? -17.881 -26.857 10.887   1.00 49.06  ? 472  ASP   B CB  1 
ATOM   4744  C  CG  . ASP   B  1 171 ? -18.720 -25.977 11.787   1.00 56.73  ? 472  ASP   B CG  1 
ATOM   4745  O  OD1 . ASP   B  1 171 ? -18.805 -24.763 11.510   1.00 56.94  ? 472  ASP   B OD1 1 
ATOM   4746  O  OD2 . ASP   B  1 171 ? -19.284 -26.493 12.772   1.00 57.69  ? 472  ASP   B OD2 1 
ATOM   4747  N  N   . GLY   B  1 172 ? -17.934 -24.190 8.517    1.00 39.36  ? 473  GLY   B N   1 
ATOM   4748  C  CA  . GLY   B  1 172 ? -18.863 -23.548 7.612    1.00 37.23  ? 473  GLY   B CA  1 
ATOM   4749  C  C   . GLY   B  1 172 ? -20.218 -23.256 8.209    1.00 41.51  ? 473  GLY   B C   1 
ATOM   4750  O  O   . GLY   B  1 172 ? -21.051 -22.630 7.538    1.00 40.83  ? 473  GLY   B O   1 
ATOM   4751  N  N   . LYS   B  1 173 ? -20.464 -23.692 9.448    1.00 44.36  ? 474  LYS   B N   1 
ATOM   4752  C  CA  . LYS   B  1 173 ? -21.704 -23.449 10.170   1.00 42.51  ? 474  LYS   B CA  1 
ATOM   4753  C  C   . LYS   B  1 173 ? -21.569 -22.340 11.199   1.00 36.35  ? 474  LYS   B C   1 
ATOM   4754  O  O   . LYS   B  1 173 ? -22.551 -22.001 11.864   1.00 42.01  ? 474  LYS   B O   1 
ATOM   4755  C  CB  . LYS   B  1 173 ? -22.167 -24.733 10.874   1.00 44.75  ? 474  LYS   B CB  1 
ATOM   4756  C  CG  . LYS   B  1 173 ? -22.314 -25.954 9.979    1.00 58.39  ? 474  LYS   B CG  1 
ATOM   4757  C  CD  . LYS   B  1 173 ? -23.187 -25.650 8.771    1.00 67.06  ? 474  LYS   B CD  1 
ATOM   4758  C  CE  . LYS   B  1 173 ? -24.020 -26.854 8.350    1.00 76.04  ? 474  LYS   B CE  1 
ATOM   4759  N  NZ  . LYS   B  1 173 ? -23.207 -28.081 8.101    1.00 81.41  ? 474  LYS   B NZ  1 
ATOM   4760  N  N   . HIS   B  1 174 ? -20.380 -21.781 11.362   1.00 34.76  ? 475  HIS   B N   1 
ATOM   4761  C  CA  . HIS   B  1 174 ? -20.137 -20.765 12.374   1.00 29.68  ? 475  HIS   B CA  1 
ATOM   4762  C  C   . HIS   B  1 174 ? -19.471 -19.559 11.757   1.00 30.13  ? 475  HIS   B C   1 
ATOM   4763  O  O   . HIS   B  1 174 ? -18.604 -18.930 12.365   1.00 28.08  ? 475  HIS   B O   1 
ATOM   4764  C  CB  . HIS   B  1 174 ? -19.300 -21.331 13.513   1.00 36.62  ? 475  HIS   B CB  1 
ATOM   4765  C  CG  . HIS   B  1 174 ? -19.990 -22.425 14.261   1.00 37.58  ? 475  HIS   B CG  1 
ATOM   4766  N  ND1 . HIS   B  1 174 ? -20.048 -23.723 13.796   1.00 41.52  ? 475  HIS   B ND1 1 
ATOM   4767  C  CD2 . HIS   B  1 174 ? -20.691 -22.407 15.418   1.00 39.70  ? 475  HIS   B CD2 1 
ATOM   4768  C  CE1 . HIS   B  1 174 ? -20.735 -24.463 14.649   1.00 42.77  ? 475  HIS   B CE1 1 
ATOM   4769  N  NE2 . HIS   B  1 174 ? -21.135 -23.689 15.643   1.00 42.37  ? 475  HIS   B NE2 1 
ATOM   4770  N  N   . ASP   B  1 175 ? -19.863 -19.223 10.529   1.00 32.23  ? 476  ASP   B N   1 
ATOM   4771  C  CA  . ASP   B  1 175 ? -19.202 -18.152 9.802    1.00 26.80  ? 476  ASP   B CA  1 
ATOM   4772  C  C   . ASP   B  1 175 ? -19.440 -16.810 10.466   1.00 21.65  ? 476  ASP   B C   1 
ATOM   4773  O  O   . ASP   B  1 175 ? -20.538 -16.512 10.941   1.00 28.19  ? 476  ASP   B O   1 
ATOM   4774  C  CB  . ASP   B  1 175 ? -19.702 -18.069 8.353    1.00 34.24  ? 476  ASP   B CB  1 
ATOM   4775  C  CG  . ASP   B  1 175 ? -19.183 -19.191 7.482    1.00 34.76  ? 476  ASP   B CG  1 
ATOM   4776  O  OD1 . ASP   B  1 175 ? -18.445 -20.070 7.987    1.00 34.50  ? 476  ASP   B OD1 1 
ATOM   4777  O  OD2 . ASP   B  1 175 ? -19.526 -19.177 6.280    1.00 34.54  ? 476  ASP   B OD2 1 
ATOM   4778  N  N   . PHE   B  1 176 ? -18.395 -16.000 10.488   1.00 21.76  ? 477  PHE   B N   1 
ATOM   4779  C  CA  . PHE   B  1 176 ? -18.535 -14.571 10.690   1.00 27.00  ? 477  PHE   B CA  1 
ATOM   4780  C  C   . PHE   B  1 176 ? -18.781 -13.941 9.328    1.00 29.46  ? 477  PHE   B C   1 
ATOM   4781  O  O   . PHE   B  1 176 ? -18.105 -14.281 8.355    1.00 27.53  ? 477  PHE   B O   1 
ATOM   4782  C  CB  . PHE   B  1 176 ? -17.284 -13.985 11.331   1.00 20.42  ? 477  PHE   B CB  1 
ATOM   4783  C  CG  . PHE   B  1 176 ? -17.158 -14.293 12.802   1.00 24.07  ? 477  PHE   B CG  1 
ATOM   4784  C  CD1 . PHE   B  1 176 ? -16.814 -15.571 13.226   1.00 26.08  ? 477  PHE   B CD1 1 
ATOM   4785  C  CD2 . PHE   B  1 176 ? -17.368 -13.305 13.749   1.00 20.88  ? 477  PHE   B CD2 1 
ATOM   4786  C  CE1 . PHE   B  1 176 ? -16.678 -15.863 14.577   1.00 30.44  ? 477  PHE   B CE1 1 
ATOM   4787  C  CE2 . PHE   B  1 176 ? -17.235 -13.596 15.117   1.00 29.93  ? 477  PHE   B CE2 1 
ATOM   4788  C  CZ  . PHE   B  1 176 ? -16.900 -14.878 15.518   1.00 28.18  ? 477  PHE   B CZ  1 
ATOM   4789  N  N   . ARG   B  1 177 ? -19.762 -13.049 9.259    1.00 26.18  ? 478  ARG   B N   1 
ATOM   4790  C  CA  . ARG   B  1 177 ? -20.088 -12.365 8.021    1.00 26.45  ? 478  ARG   B CA  1 
ATOM   4791  C  C   . ARG   B  1 177 ? -20.532 -10.958 8.357    1.00 28.35  ? 478  ARG   B C   1 
ATOM   4792  O  O   . ARG   B  1 177 ? -21.311 -10.755 9.291    1.00 23.78  ? 478  ARG   B O   1 
ATOM   4793  C  CB  . ARG   B  1 177 ? -21.220 -13.051 7.243    1.00 26.30  ? 478  ARG   B CB  1 
ATOM   4794  C  CG  . ARG   B  1 177 ? -20.920 -14.423 6.688    1.00 27.26  ? 478  ARG   B CG  1 
ATOM   4795  C  CD  . ARG   B  1 177 ? -19.831 -14.372 5.635    1.00 23.61  ? 478  ARG   B CD  1 
ATOM   4796  N  NE  . ARG   B  1 177 ? -20.161 -13.551 4.476    1.00 30.71  ? 478  ARG   B NE  1 
ATOM   4797  C  CZ  . ARG   B  1 177 ? -20.770 -14.015 3.382    1.00 33.83  ? 478  ARG   B CZ  1 
ATOM   4798  N  NH1 . ARG   B  1 177 ? -21.156 -15.281 3.322    1.00 26.08  ? 478  ARG   B NH1 1 
ATOM   4799  N  NH2 . ARG   B  1 177 ? -21.006 -13.211 2.353    1.00 35.33  ? 478  ARG   B NH2 1 
ATOM   4800  N  N   . VAL   B  1 178 ? -20.040 -9.992  7.595    1.00 25.91  ? 479  VAL   B N   1 
ATOM   4801  C  CA  . VAL   B  1 178 ? -20.704 -8.703  7.493    1.00 29.12  ? 479  VAL   B CA  1 
ATOM   4802  C  C   . VAL   B  1 178 ? -21.721 -8.842  6.372    1.00 27.44  ? 479  VAL   B C   1 
ATOM   4803  O  O   . VAL   B  1 178 ? -21.355 -9.146  5.232    1.00 27.15  ? 479  VAL   B O   1 
ATOM   4804  C  CB  . VAL   B  1 178 ? -19.703 -7.578  7.208    1.00 32.12  ? 479  VAL   B CB  1 
ATOM   4805  C  CG1 . VAL   B  1 178 ? -20.430 -6.243  7.139    1.00 30.25  ? 479  VAL   B CG1 1 
ATOM   4806  C  CG2 . VAL   B  1 178 ? -18.583 -7.566  8.255    1.00 25.19  ? 479  VAL   B CG2 1 
ATOM   4807  N  N   . TRP   B  1 179 ? -23.005 -8.665  6.691    1.00 25.03  ? 480  TRP   B N   1 
ATOM   4808  C  CA  . TRP   B  1 179 ? -24.006 -8.866  5.650    1.00 27.95  ? 480  TRP   B CA  1 
ATOM   4809  C  C   . TRP   B  1 179 ? -24.014 -7.707  4.658    1.00 26.29  ? 480  TRP   B C   1 
ATOM   4810  O  O   . TRP   B  1 179 ? -24.384 -7.891  3.495    1.00 28.60  ? 480  TRP   B O   1 
ATOM   4811  C  CB  . TRP   B  1 179 ? -25.384 -9.094  6.276    1.00 24.85  ? 480  TRP   B CB  1 
ATOM   4812  C  CG  . TRP   B  1 179 ? -25.555 -10.508 6.788    1.00 21.99  ? 480  TRP   B CG  1 
ATOM   4813  C  CD1 . TRP   B  1 179 ? -24.596 -11.289 7.365    1.00 20.89  ? 480  TRP   B CD1 1 
ATOM   4814  C  CD2 . TRP   B  1 179 ? -26.742 -11.311 6.730    1.00 21.72  ? 480  TRP   B CD2 1 
ATOM   4815  N  NE1 . TRP   B  1 179 ? -25.117 -12.518 7.689    1.00 24.64  ? 480  TRP   B NE1 1 
ATOM   4816  C  CE2 . TRP   B  1 179 ? -26.431 -12.558 7.303    1.00 21.99  ? 480  TRP   B CE2 1 
ATOM   4817  C  CE3 . TRP   B  1 179 ? -28.034 -11.095 6.249    1.00 22.23  ? 480  TRP   B CE3 1 
ATOM   4818  C  CZ2 . TRP   B  1 179 ? -27.365 -13.585 7.408    1.00 28.16  ? 480  TRP   B CZ2 1 
ATOM   4819  C  CZ3 . TRP   B  1 179 ? -28.963 -12.111 6.359    1.00 27.11  ? 480  TRP   B CZ3 1 
ATOM   4820  C  CH2 . TRP   B  1 179 ? -28.623 -13.342 6.931    1.00 28.40  ? 480  TRP   B CH2 1 
ATOM   4821  N  N   . ASN   B  1 180 ? -23.603 -6.522  5.093    1.00 25.71  ? 481  ASN   B N   1 
ATOM   4822  C  CA  . ASN   B  1 180 ? -23.435 -5.399  4.183    1.00 24.69  ? 481  ASN   B CA  1 
ATOM   4823  C  C   . ASN   B  1 180 ? -22.418 -5.735  3.111    1.00 25.86  ? 481  ASN   B C   1 
ATOM   4824  O  O   . ASN   B  1 180 ? -21.425 -6.419  3.368    1.00 21.37  ? 481  ASN   B O   1 
ATOM   4825  C  CB  . ASN   B  1 180 ? -22.948 -4.171  4.943    1.00 21.09  ? 481  ASN   B CB  1 
ATOM   4826  C  CG  . ASN   B  1 180 ? -23.768 -3.903  6.171    1.00 26.25  ? 481  ASN   B CG  1 
ATOM   4827  O  OD1 . ASN   B  1 180 ? -23.775 -4.702  7.107    1.00 25.32  ? 481  ASN   B OD1 1 
ATOM   4828  N  ND2 . ASN   B  1 180 ? -24.475 -2.778  6.176    1.00 24.03  ? 481  ASN   B ND2 1 
ATOM   4829  N  N   . SER   B  1 181 ? -22.654 -5.220  1.906    1.00 23.11  ? 482  SER   B N   1 
ATOM   4830  C  CA  . SER   B  1 181 ? -21.672 -5.409  0.847    1.00 23.67  ? 482  SER   B CA  1 
ATOM   4831  C  C   . SER   B  1 181 ? -20.514 -4.441  1.035    1.00 22.02  ? 482  SER   B C   1 
ATOM   4832  O  O   . SER   B  1 181 ? -19.352 -4.800  0.810    1.00 24.45  ? 482  SER   B O   1 
ATOM   4833  C  CB  . SER   B  1 181 ? -22.339 -5.245  -0.523   1.00 27.12  ? 482  SER   B CB  1 
ATOM   4834  O  OG  . SER   B  1 181 ? -23.034 -4.009  -0.623   1.00 25.35  ? 482  SER   B OG  1 
ATOM   4835  N  N   . GLN   B  1 182 ? -20.814 -3.223  1.473    1.00 18.04  ? 483  GLN   B N   1 
ATOM   4836  C  CA  . GLN   B  1 182 ? -19.810 -2.305  1.969    1.00 24.65  ? 483  GLN   B CA  1 
ATOM   4837  C  C   . GLN   B  1 182 ? -20.222 -1.815  3.345    1.00 24.62  ? 483  GLN   B C   1 
ATOM   4838  O  O   . GLN   B  1 182 ? -21.410 -1.772  3.678    1.00 25.14  ? 483  GLN   B O   1 
ATOM   4839  C  CB  . GLN   B  1 182 ? -19.625 -1.087  1.075    1.00 29.63  ? 483  GLN   B CB  1 
ATOM   4840  C  CG  . GLN   B  1 182 ? -19.013 -1.321  -0.256   1.00 35.57  ? 483  GLN   B CG  1 
ATOM   4841  C  CD  . GLN   B  1 182 ? -19.382 -0.185  -1.174   1.00 38.83  ? 483  GLN   B CD  1 
ATOM   4842  O  OE1 . GLN   B  1 182 ? -18.957 0.973   -0.987   1.00 33.52  ? 483  GLN   B OE1 1 
ATOM   4843  N  NE2 . GLN   B  1 182 ? -20.224 -0.488  -2.135   1.00 26.29  ? 483  GLN   B NE2 1 
ATOM   4844  N  N   . LEU   B  1 183 ? -19.229 -1.383  4.124    1.00 21.42  ? 484  LEU   B N   1 
ATOM   4845  C  CA  . LEU   B  1 183 ? -19.523 -0.924  5.482    1.00 30.04  ? 484  LEU   B CA  1 
ATOM   4846  C  C   . LEU   B  1 183 ? -20.456 0.276   5.465    1.00 31.60  ? 484  LEU   B C   1 
ATOM   4847  O  O   . LEU   B  1 183 ? -21.380 0.380   6.282    1.00 23.17  ? 484  LEU   B O   1 
ATOM   4848  C  CB  . LEU   B  1 183 ? -18.231 -0.561  6.204    1.00 24.22  ? 484  LEU   B CB  1 
ATOM   4849  C  CG  . LEU   B  1 183 ? -17.281 -1.721  6.444    1.00 18.40  ? 484  LEU   B CG  1 
ATOM   4850  C  CD1 . LEU   B  1 183 ? -16.056 -1.234  7.247    1.00 17.90  ? 484  LEU   B CD1 1 
ATOM   4851  C  CD2 . LEU   B  1 183 ? -18.025 -2.847  7.167    1.00 18.08  ? 484  LEU   B CD2 1 
ATOM   4852  N  N   . ILE   B  1 184 ? -20.222 1.195   4.545    1.00 18.49  ? 485  ILE   B N   1 
ATOM   4853  C  CA  . ILE   B  1 184 ? -21.018 2.401   4.408    1.00 18.87  ? 485  ILE   B CA  1 
ATOM   4854  C  C   . ILE   B  1 184 ? -21.619 2.362   3.015    1.00 23.94  ? 485  ILE   B C   1 
ATOM   4855  O  O   . ILE   B  1 184 ? -20.883 2.306   2.028    1.00 23.08  ? 485  ILE   B O   1 
ATOM   4856  C  CB  . ILE   B  1 184 ? -20.169 3.663   4.626    1.00 26.07  ? 485  ILE   B CB  1 
ATOM   4857  C  CG1 . ILE   B  1 184 ? -19.581 3.640   6.041    1.00 34.07  ? 485  ILE   B CG1 1 
ATOM   4858  C  CG2 . ILE   B  1 184 ? -21.000 4.917   4.415    1.00 19.41  ? 485  ILE   B CG2 1 
ATOM   4859  C  CD1 . ILE   B  1 184 ? -18.704 4.808   6.330    1.00 42.91  ? 485  ILE   B CD1 1 
ATOM   4860  N  N   . ARG   B  1 185 ? -22.948 2.299   2.949    1.00 24.00  ? 486  ARG   B N   1 
ATOM   4861  C  CA  . ARG   B  1 185 ? -23.715 2.437   1.721    1.00 25.33  ? 486  ARG   B CA  1 
ATOM   4862  C  C   . ARG   B  1 185 ? -25.022 3.104   2.097    1.00 33.17  ? 486  ARG   B C   1 
ATOM   4863  O  O   . ARG   B  1 185 ? -25.393 3.172   3.273    1.00 31.26  ? 486  ARG   B O   1 
ATOM   4864  C  CB  . ARG   B  1 185 ? -24.031 1.099   1.033    1.00 25.12  ? 486  ARG   B CB  1 
ATOM   4865  C  CG  . ARG   B  1 185 ? -22.847 0.259   0.638    1.00 26.02  ? 486  ARG   B CG  1 
ATOM   4866  C  CD  . ARG   B  1 185 ? -23.292 -0.774  -0.360   1.00 27.99  ? 486  ARG   B CD  1 
ATOM   4867  N  NE  . ARG   B  1 185 ? -23.590 -0.153  -1.637   1.00 35.09  ? 486  ARG   B NE  1 
ATOM   4868  C  CZ  . ARG   B  1 185 ? -23.781 -0.832  -2.764   1.00 36.27  ? 486  ARG   B CZ  1 
ATOM   4869  N  NH1 . ARG   B  1 185 ? -23.717 -2.152  -2.758   1.00 29.14  ? 486  ARG   B NH1 1 
ATOM   4870  N  NH2 . ARG   B  1 185 ? -24.036 -0.189  -3.892   1.00 30.32  ? 486  ARG   B NH2 1 
ATOM   4871  N  N   . TYR   B  1 186 ? -25.735 3.566   1.090    1.00 20.45  ? 487  TYR   B N   1 
ATOM   4872  C  CA  . TYR   B  1 186 ? -27.006 4.214   1.319    1.00 23.27  ? 487  TYR   B CA  1 
ATOM   4873  C  C   . TYR   B  1 186 ? -28.151 3.257   1.044    1.00 23.14  ? 487  TYR   B C   1 
ATOM   4874  O  O   . TYR   B  1 186 ? -28.058 2.380   0.184    1.00 27.63  ? 487  TYR   B O   1 
ATOM   4875  C  CB  . TYR   B  1 186 ? -27.145 5.443   0.441    1.00 21.48  ? 487  TYR   B CB  1 
ATOM   4876  C  CG  . TYR   B  1 186 ? -26.137 6.511   0.751    1.00 30.54  ? 487  TYR   B CG  1 
ATOM   4877  C  CD1 . TYR   B  1 186 ? -25.253 6.951   -0.224   1.00 29.99  ? 487  TYR   B CD1 1 
ATOM   4878  C  CD2 . TYR   B  1 186 ? -26.076 7.097   2.026    1.00 23.56  ? 487  TYR   B CD2 1 
ATOM   4879  C  CE1 . TYR   B  1 186 ? -24.336 7.944   0.045    1.00 34.61  ? 487  TYR   B CE1 1 
ATOM   4880  C  CE2 . TYR   B  1 186 ? -25.162 8.104   2.304    1.00 24.65  ? 487  TYR   B CE2 1 
ATOM   4881  C  CZ  . TYR   B  1 186 ? -24.290 8.523   1.301    1.00 29.48  ? 487  TYR   B CZ  1 
ATOM   4882  O  OH  . TYR   B  1 186 ? -23.370 9.525   1.551    1.00 24.13  ? 487  TYR   B OH  1 
ATOM   4883  N  N   . ALA   B  1 187 ? -29.241 3.450   1.773    1.00 22.46  ? 488  ALA   B N   1 
ATOM   4884  C  CA  . ALA   B  1 187 ? -30.409 2.606   1.609    1.00 30.03  ? 488  ALA   B CA  1 
ATOM   4885  C  C   . ALA   B  1 187 ? -31.095 2.888   0.279    1.00 30.91  ? 488  ALA   B C   1 
ATOM   4886  O  O   . ALA   B  1 187 ? -30.911 3.935   -0.346   1.00 27.26  ? 488  ALA   B O   1 
ATOM   4887  C  CB  . ALA   B  1 187 ? -31.399 2.821   2.756    1.00 31.63  ? 488  ALA   B CB  1 
ATOM   4888  N  N   . GLY   B  1 188 ? -31.882 1.921   -0.146   1.00 31.90  ? 489  GLY   B N   1 
ATOM   4889  C  CA  . GLY   B  1 188 ? -32.731 2.080   -1.312   1.00 31.05  ? 489  GLY   B CA  1 
ATOM   4890  C  C   . GLY   B  1 188 ? -34.116 1.585   -0.964   1.00 34.64  ? 489  GLY   B C   1 
ATOM   4891  O  O   . GLY   B  1 188 ? -34.271 0.566   -0.291   1.00 25.82  ? 489  GLY   B O   1 
ATOM   4892  N  N   . TYR   B  1 189 ? -35.121 2.324   -1.420   1.00 33.10  ? 490  TYR   B N   1 
ATOM   4893  C  CA  . TYR   B  1 189 ? -36.511 2.020   -1.116   1.00 36.72  ? 490  TYR   B CA  1 
ATOM   4894  C  C   . TYR   B  1 189 ? -37.308 1.996   -2.407   1.00 41.10  ? 490  TYR   B C   1 
ATOM   4895  O  O   . TYR   B  1 189 ? -37.419 3.024   -3.084   1.00 39.86  ? 490  TYR   B O   1 
ATOM   4896  C  CB  . TYR   B  1 189 ? -37.106 3.055   -0.174   1.00 31.47  ? 490  TYR   B CB  1 
ATOM   4897  C  CG  . TYR   B  1 189 ? -36.264 3.375   1.024    1.00 31.96  ? 490  TYR   B CG  1 
ATOM   4898  C  CD1 . TYR   B  1 189 ? -35.419 4.481   1.030    1.00 30.80  ? 490  TYR   B CD1 1 
ATOM   4899  C  CD2 . TYR   B  1 189 ? -36.330 2.589   2.165    1.00 32.47  ? 490  TYR   B CD2 1 
ATOM   4900  C  CE1 . TYR   B  1 189 ? -34.656 4.787   2.143    1.00 31.28  ? 490  TYR   B CE1 1 
ATOM   4901  C  CE2 . TYR   B  1 189 ? -35.574 2.884   3.281    1.00 31.95  ? 490  TYR   B CE2 1 
ATOM   4902  C  CZ  . TYR   B  1 189 ? -34.745 3.988   3.270    1.00 35.29  ? 490  TYR   B CZ  1 
ATOM   4903  O  OH  . TYR   B  1 189 ? -33.997 4.274   4.393    1.00 34.76  ? 490  TYR   B OH  1 
ATOM   4904  N  N   . LYS   B  1 190 ? -37.866 0.834   -2.739   1.00 38.82  ? 491  LYS   B N   1 
ATOM   4905  C  CA  . LYS   B  1 190 ? -38.791 0.752   -3.856   1.00 41.91  ? 491  LYS   B CA  1 
ATOM   4906  C  C   . LYS   B  1 190 ? -40.095 1.432   -3.471   1.00 40.84  ? 491  LYS   B C   1 
ATOM   4907  O  O   . LYS   B  1 190 ? -40.681 1.124   -2.430   1.00 43.04  ? 491  LYS   B O   1 
ATOM   4908  C  CB  . LYS   B  1 190 ? -39.045 -0.705  -4.248   1.00 45.37  ? 491  LYS   B CB  1 
ATOM   4909  C  CG  . LYS   B  1 190 ? -39.358 -0.900  -5.738   1.00 53.78  ? 491  LYS   B CG  1 
ATOM   4910  C  CD  . LYS   B  1 190 ? -38.079 -0.848  -6.578   1.00 61.67  ? 491  LYS   B CD  1 
ATOM   4911  C  CE  . LYS   B  1 190 ? -38.361 -0.575  -8.057   1.00 67.61  ? 491  LYS   B CE  1 
ATOM   4912  N  NZ  . LYS   B  1 190 ? -39.240 -1.595  -8.704   1.00 71.11  ? 491  LYS   B NZ  1 
ATOM   4913  N  N   . GLN   B  1 191 ? -40.540 2.369   -4.303   1.00 34.36  ? 492  GLN   B N   1 
ATOM   4914  C  CA  . GLN   B  1 191 ? -41.805 3.038   -4.060   1.00 42.74  ? 492  GLN   B CA  1 
ATOM   4915  C  C   . GLN   B  1 191 ? -42.948 2.242   -4.671   1.00 44.12  ? 492  GLN   B C   1 
ATOM   4916  O  O   . GLN   B  1 191 ? -42.743 1.413   -5.568   1.00 40.49  ? 492  GLN   B O   1 
ATOM   4917  C  CB  . GLN   B  1 191 ? -41.778 4.454   -4.638   1.00 45.31  ? 492  GLN   B CB  1 
ATOM   4918  C  CG  . GLN   B  1 191 ? -40.592 5.288   -4.193   1.00 49.64  ? 492  GLN   B CG  1 
ATOM   4919  C  CD  . GLN   B  1 191 ? -40.722 5.815   -2.786   1.00 57.54  ? 492  GLN   B CD  1 
ATOM   4920  O  OE1 . GLN   B  1 191 ? -41.562 5.362   -2.008   1.00 57.17  ? 492  GLN   B OE1 1 
ATOM   4921  N  NE2 . GLN   B  1 191 ? -39.889 6.789   -2.449   1.00 65.67  ? 492  GLN   B NE2 1 
ATOM   4922  N  N   . PRO   B  1 192 ? -44.168 2.454   -4.185   1.00 48.94  ? 493  PRO   B N   1 
ATOM   4923  C  CA  . PRO   B  1 192 ? -45.314 1.771   -4.803   1.00 48.10  ? 493  PRO   B CA  1 
ATOM   4924  C  C   . PRO   B  1 192 ? -45.423 2.028   -6.301   1.00 48.32  ? 493  PRO   B C   1 
ATOM   4925  O  O   . PRO   B  1 192 ? -45.895 1.150   -7.041   1.00 42.05  ? 493  PRO   B O   1 
ATOM   4926  C  CB  . PRO   B  1 192 ? -46.514 2.341   -4.030   1.00 44.44  ? 493  PRO   B CB  1 
ATOM   4927  C  CG  . PRO   B  1 192 ? -45.935 2.785   -2.701   1.00 46.38  ? 493  PRO   B CG  1 
ATOM   4928  C  CD  . PRO   B  1 192 ? -44.544 3.244   -2.996   1.00 43.70  ? 493  PRO   B CD  1 
ATOM   4929  N  N   . ASP   B  1 193 ? -44.969 3.189   -6.779   1.00 36.71  ? 494  ASP   B N   1 
ATOM   4930  C  CA  . ASP   B  1 193 ? -45.113 3.529   -8.191   1.00 42.13  ? 494  ASP   B CA  1 
ATOM   4931  C  C   . ASP   B  1 193 ? -43.973 2.991   -9.050   1.00 40.40  ? 494  ASP   B C   1 
ATOM   4932  O  O   . ASP   B  1 193 ? -43.861 3.367   -10.223  1.00 43.38  ? 494  ASP   B O   1 
ATOM   4933  C  CB  . ASP   B  1 193 ? -45.255 5.047   -8.359   1.00 41.61  ? 494  ASP   B CB  1 
ATOM   4934  C  CG  . ASP   B  1 193 ? -43.988 5.811   -8.031   1.00 46.00  ? 494  ASP   B CG  1 
ATOM   4935  O  OD1 . ASP   B  1 193 ? -42.995 5.213   -7.554   1.00 48.17  ? 494  ASP   B OD1 1 
ATOM   4936  O  OD2 . ASP   B  1 193 ? -43.990 7.035   -8.266   1.00 50.05  ? 494  ASP   B OD2 1 
ATOM   4937  N  N   . GLY   B  1 194 ? -43.139 2.110   -8.499   1.00 40.65  ? 495  GLY   B N   1 
ATOM   4938  C  CA  . GLY   B  1 194 ? -42.023 1.553   -9.216   1.00 42.14  ? 495  GLY   B CA  1 
ATOM   4939  C  C   . GLY   B  1 194 ? -40.768 2.394   -9.184   1.00 45.97  ? 495  GLY   B C   1 
ATOM   4940  O  O   . GLY   B  1 194 ? -39.692 1.888   -9.521   1.00 45.37  ? 495  GLY   B O   1 
ATOM   4941  N  N   . SER   B  1 195 ? -40.867 3.664   -8.808   1.00 41.61  ? 496  SER   B N   1 
ATOM   4942  C  CA  . SER   B  1 195 ? -39.652 4.442   -8.651   1.00 40.95  ? 496  SER   B CA  1 
ATOM   4943  C  C   . SER   B  1 195 ? -38.882 3.944   -7.432   1.00 46.79  ? 496  SER   B C   1 
ATOM   4944  O  O   . SER   B  1 195 ? -39.411 3.231   -6.578   1.00 49.17  ? 496  SER   B O   1 
ATOM   4945  C  CB  . SER   B  1 195 ? -39.973 5.929   -8.507   1.00 38.42  ? 496  SER   B CB  1 
ATOM   4946  O  OG  . SER   B  1 195 ? -40.492 6.204   -7.228   1.00 37.30  ? 496  SER   B OG  1 
ATOM   4947  N  N   . THR   B  1 196 ? -37.611 4.310   -7.368   1.00 42.88  ? 497  THR   B N   1 
ATOM   4948  C  CA  . THR   B  1 196 ? -36.768 3.972   -6.237   1.00 41.58  ? 497  THR   B CA  1 
ATOM   4949  C  C   . THR   B  1 196 ? -36.260 5.251   -5.593   1.00 38.82  ? 497  THR   B C   1 
ATOM   4950  O  O   . THR   B  1 196 ? -35.909 6.209   -6.286   1.00 44.26  ? 497  THR   B O   1 
ATOM   4951  C  CB  . THR   B  1 196 ? -35.597 3.085   -6.671   1.00 45.07  ? 497  THR   B CB  1 
ATOM   4952  O  OG1 . THR   B  1 196 ? -36.105 1.939   -7.365   1.00 47.30  ? 497  THR   B OG1 1 
ATOM   4953  C  CG2 . THR   B  1 196 ? -34.792 2.626   -5.460   1.00 41.91  ? 497  THR   B CG2 1 
ATOM   4954  N  N   . LEU   B  1 197 ? -36.258 5.279   -4.267   1.00 33.34  ? 498  LEU   B N   1 
ATOM   4955  C  CA  . LEU   B  1 197 ? -35.620 6.349   -3.518   1.00 30.04  ? 498  LEU   B CA  1 
ATOM   4956  C  C   . LEU   B  1 197 ? -34.300 5.821   -2.986   1.00 33.09  ? 498  LEU   B C   1 
ATOM   4957  O  O   . LEU   B  1 197 ? -34.219 4.673   -2.544   1.00 37.25  ? 498  LEU   B O   1 
ATOM   4958  C  CB  . LEU   B  1 197 ? -36.518 6.825   -2.377   1.00 37.07  ? 498  LEU   B CB  1 
ATOM   4959  C  CG  . LEU   B  1 197 ? -35.976 7.840   -1.369   1.00 39.17  ? 498  LEU   B CG  1 
ATOM   4960  C  CD1 . LEU   B  1 197 ? -35.585 9.134   -2.065   1.00 36.09  ? 498  LEU   B CD1 1 
ATOM   4961  C  CD2 . LEU   B  1 197 ? -37.013 8.098   -0.272   1.00 40.26  ? 498  LEU   B CD2 1 
ATOM   4962  N  N   . GLY   B  1 198 ? -33.261 6.645   -3.058   1.00 34.63  ? 499  GLY   B N   1 
ATOM   4963  C  CA  . GLY   B  1 198 ? -31.952 6.199   -2.616   1.00 26.81  ? 499  GLY   B CA  1 
ATOM   4964  C  C   . GLY   B  1 198 ? -31.275 5.331   -3.663   1.00 32.17  ? 499  GLY   B C   1 
ATOM   4965  O  O   . GLY   B  1 198 ? -31.485 5.488   -4.861   1.00 36.45  ? 499  GLY   B O   1 
ATOM   4966  N  N   . ASP   B  1 199 ? -30.475 4.382   -3.189   1.00 31.21  ? 500  ASP   B N   1 
ATOM   4967  C  CA  . ASP   B  1 199 ? -29.624 3.585   -4.059   1.00 30.97  ? 500  ASP   B CA  1 
ATOM   4968  C  C   . ASP   B  1 199 ? -30.354 2.312   -4.477   1.00 30.02  ? 500  ASP   B C   1 
ATOM   4969  O  O   . ASP   B  1 199 ? -30.526 1.408   -3.642   1.00 30.62  ? 500  ASP   B O   1 
ATOM   4970  C  CB  . ASP   B  1 199 ? -28.318 3.249   -3.345   1.00 34.57  ? 500  ASP   B CB  1 
ATOM   4971  C  CG  . ASP   B  1 199 ? -27.308 2.575   -4.248   1.00 34.00  ? 500  ASP   B CG  1 
ATOM   4972  O  OD1 . ASP   B  1 199 ? -27.722 1.885   -5.200   1.00 32.87  ? 500  ASP   B OD1 1 
ATOM   4973  O  OD2 . ASP   B  1 199 ? -26.094 2.735   -4.000   1.00 32.40  ? 500  ASP   B OD2 1 
ATOM   4974  N  N   . PRO   B  1 200 ? -30.745 2.171   -5.748   1.00 29.92  ? 501  PRO   B N   1 
ATOM   4975  C  CA  . PRO   B  1 200 ? -31.478 0.966   -6.173   1.00 25.57  ? 501  PRO   B CA  1 
ATOM   4976  C  C   . PRO   B  1 200 ? -30.719 -0.325  -5.950   1.00 27.43  ? 501  PRO   B C   1 
ATOM   4977  O  O   . PRO   B  1 200 ? -31.341 -1.376  -5.742   1.00 28.66  ? 501  PRO   B O   1 
ATOM   4978  C  CB  . PRO   B  1 200 ? -31.711 1.214   -7.673   1.00 30.89  ? 501  PRO   B CB  1 
ATOM   4979  C  CG  . PRO   B  1 200 ? -31.634 2.695   -7.826   1.00 27.46  ? 501  PRO   B CG  1 
ATOM   4980  C  CD  . PRO   B  1 200 ? -30.606 3.151   -6.841   1.00 26.18  ? 501  PRO   B CD  1 
ATOM   4981  N  N   . ALA   B  1 201 ? -29.387 -0.277  -5.988   1.00 31.35  ? 502  ALA   B N   1 
ATOM   4982  C  CA  . ALA   B  1 201 ? -28.582 -1.471  -5.756   1.00 35.20  ? 502  ALA   B CA  1 
ATOM   4983  C  C   . ALA   B  1 201 ? -28.826 -2.088  -4.385   1.00 29.99  ? 502  ALA   B C   1 
ATOM   4984  O  O   . ALA   B  1 201 ? -28.543 -3.273  -4.188   1.00 28.32  ? 502  ALA   B O   1 
ATOM   4985  C  CB  . ALA   B  1 201 ? -27.093 -1.136  -5.896   1.00 30.18  ? 502  ALA   B CB  1 
ATOM   4986  N  N   . ASN   B  1 202 ? -29.336 -1.316  -3.431   1.00 26.53  ? 503  ASN   B N   1 
ATOM   4987  C  CA  . ASN   B  1 202 ? -29.379 -1.746  -2.039   1.00 30.16  ? 503  ASN   B CA  1 
ATOM   4988  C  C   . ASN   B  1 202 ? -30.800 -1.994  -1.561   1.00 29.98  ? 503  ASN   B C   1 
ATOM   4989  O  O   . ASN   B  1 202 ? -31.038 -2.114  -0.354   1.00 28.55  ? 503  ASN   B O   1 
ATOM   4990  C  CB  . ASN   B  1 202 ? -28.681 -0.710  -1.166   1.00 24.13  ? 503  ASN   B CB  1 
ATOM   4991  C  CG  . ASN   B  1 202 ? -27.197 -0.677  -1.402   1.00 28.51  ? 503  ASN   B CG  1 
ATOM   4992  O  OD1 . ASN   B  1 202 ? -26.594 -1.707  -1.696   1.00 32.51  ? 503  ASN   B OD1 1 
ATOM   4993  N  ND2 . ASN   B  1 202 ? -26.593 0.501   -1.280   1.00 25.85  ? 503  ASN   B ND2 1 
ATOM   4994  N  N   . VAL   B  1 203 ? -31.743 -2.077  -2.496   1.00 29.50  ? 504  VAL   B N   1 
ATOM   4995  C  CA  . VAL   B  1 203 ? -33.146 -2.262  -2.146   1.00 32.84  ? 504  VAL   B CA  1 
ATOM   4996  C  C   . VAL   B  1 203 ? -33.340 -3.559  -1.369   1.00 39.75  ? 504  VAL   B C   1 
ATOM   4997  O  O   . VAL   B  1 203 ? -33.974 -3.576  -0.305   1.00 31.41  ? 504  VAL   B O   1 
ATOM   4998  C  CB  . VAL   B  1 203 ? -34.013 -2.222  -3.415   1.00 36.23  ? 504  VAL   B CB  1 
ATOM   4999  C  CG1 . VAL   B  1 203 ? -35.345 -2.896  -3.163   1.00 36.45  ? 504  VAL   B CG1 1 
ATOM   5000  C  CG2 . VAL   B  1 203 ? -34.201 -0.777  -3.872   1.00 34.99  ? 504  VAL   B CG2 1 
ATOM   5001  N  N   . GLN   B  1 204 ? -32.798 -4.666  -1.886   1.00 37.68  ? 505  GLN   B N   1 
ATOM   5002  C  CA  . GLN   B  1 204 ? -32.971 -5.950  -1.213   1.00 33.26  ? 505  GLN   B CA  1 
ATOM   5003  C  C   . GLN   B  1 204 ? -32.354 -5.922  0.178    1.00 31.29  ? 505  GLN   B C   1 
ATOM   5004  O  O   . GLN   B  1 204 ? -32.979 -6.349  1.153    1.00 29.03  ? 505  GLN   B O   1 
ATOM   5005  C  CB  . GLN   B  1 204 ? -32.353 -7.081  -2.032   1.00 36.07  ? 505  GLN   B CB  1 
ATOM   5006  C  CG  . GLN   B  1 204 ? -32.973 -8.438  -1.715   1.00 55.00  ? 505  GLN   B CG  1 
ATOM   5007  C  CD  . GLN   B  1 204 ? -32.060 -9.621  -2.015   1.00 60.52  ? 505  GLN   B CD  1 
ATOM   5008  O  OE1 . GLN   B  1 204 ? -31.007 -9.477  -2.644   1.00 54.21  ? 505  GLN   B OE1 1 
ATOM   5009  N  NE2 . GLN   B  1 204 ? -32.465 -10.803 -1.555   1.00 60.60  ? 505  GLN   B NE2 1 
ATOM   5010  N  N   . PHE   B  1 205 ? -31.116 -5.437  0.287    1.00 27.49  ? 506  PHE   B N   1 
ATOM   5011  C  CA  . PHE   B  1 205 ? -30.476 -5.398  1.594    1.00 31.23  ? 506  PHE   B CA  1 
ATOM   5012  C  C   . PHE   B  1 205 ? -31.210 -4.457  2.538    1.00 32.64  ? 506  PHE   B C   1 
ATOM   5013  O  O   . PHE   B  1 205 ? -31.308 -4.725  3.744    1.00 24.45  ? 506  PHE   B O   1 
ATOM   5014  C  CB  . PHE   B  1 205 ? -29.019 -4.981  1.460    1.00 31.55  ? 506  PHE   B CB  1 
ATOM   5015  C  CG  . PHE   B  1 205 ? -28.308 -4.939  2.761    1.00 33.74  ? 506  PHE   B CG  1 
ATOM   5016  C  CD1 . PHE   B  1 205 ? -27.803 -6.099  3.319    1.00 37.48  ? 506  PHE   B CD1 1 
ATOM   5017  C  CD2 . PHE   B  1 205 ? -28.171 -3.748  3.455    1.00 32.19  ? 506  PHE   B CD2 1 
ATOM   5018  C  CE1 . PHE   B  1 205 ? -27.154 -6.068  4.540    1.00 35.32  ? 506  PHE   B CE1 1 
ATOM   5019  C  CE2 . PHE   B  1 205 ? -27.521 -3.715  4.669    1.00 34.27  ? 506  PHE   B CE2 1 
ATOM   5020  C  CZ  . PHE   B  1 205 ? -27.014 -4.878  5.214    1.00 26.76  ? 506  PHE   B CZ  1 
ATOM   5021  N  N   . THR   B  1 206 ? -31.732 -3.349  2.011    1.00 30.77  ? 507  THR   B N   1 
ATOM   5022  C  CA  . THR   B  1 206 ? -32.539 -2.457  2.834    1.00 28.77  ? 507  THR   B CA  1 
ATOM   5023  C  C   . THR   B  1 206 ? -33.778 -3.178  3.362    1.00 34.70  ? 507  THR   B C   1 
ATOM   5024  O  O   . THR   B  1 206 ? -34.134 -3.037  4.540    1.00 34.52  ? 507  THR   B O   1 
ATOM   5025  C  CB  . THR   B  1 206 ? -32.894 -1.210  2.021    1.00 24.99  ? 507  THR   B CB  1 
ATOM   5026  O  OG1 . THR   B  1 206 ? -31.677 -0.536  1.668    1.00 26.61  ? 507  THR   B OG1 1 
ATOM   5027  C  CG2 . THR   B  1 206 ? -33.753 -0.246  2.810    1.00 26.28  ? 507  THR   B CG2 1 
ATOM   5028  N  N   . GLU   B  1 207 ? -34.430 -3.984  2.511    1.00 32.15  ? 508  GLU   B N   1 
ATOM   5029  C  CA  . GLU   B  1 207 ? -35.583 -4.768  2.957    1.00 37.70  ? 508  GLU   B CA  1 
ATOM   5030  C  C   . GLU   B  1 207 ? -35.210 -5.707  4.095    1.00 34.00  ? 508  GLU   B C   1 
ATOM   5031  O  O   . GLU   B  1 207 ? -35.971 -5.860  5.058    1.00 34.82  ? 508  GLU   B O   1 
ATOM   5032  C  CB  . GLU   B  1 207 ? -36.161 -5.590  1.801    1.00 43.67  ? 508  GLU   B CB  1 
ATOM   5033  C  CG  . GLU   B  1 207 ? -36.741 -4.822  0.638    1.00 55.99  ? 508  GLU   B CG  1 
ATOM   5034  C  CD  . GLU   B  1 207 ? -37.052 -5.739  -0.546   1.00 67.30  ? 508  GLU   B CD  1 
ATOM   5035  O  OE1 . GLU   B  1 207 ? -36.272 -6.687  -0.796   1.00 69.53  ? 508  GLU   B OE1 1 
ATOM   5036  O  OE2 . GLU   B  1 207 ? -38.082 -5.519  -1.220   1.00 71.61  ? 508  GLU   B OE2 1 
ATOM   5037  N  N   . ILE   B  1 208 ? -34.055 -6.369  3.985    1.00 31.00  ? 509  ILE   B N   1 
ATOM   5038  C  CA  . ILE   B  1 208 ? -33.614 -7.264  5.049    1.00 26.93  ? 509  ILE   B CA  1 
ATOM   5039  C  C   . ILE   B  1 208 ? -33.424 -6.482  6.338    1.00 30.08  ? 509  ILE   B C   1 
ATOM   5040  O  O   . ILE   B  1 208 ? -33.882 -6.895  7.404    1.00 34.84  ? 509  ILE   B O   1 
ATOM   5041  C  CB  . ILE   B  1 208 ? -32.323 -7.994  4.644    1.00 35.19  ? 509  ILE   B CB  1 
ATOM   5042  C  CG1 . ILE   B  1 208 ? -32.591 -8.944  3.475    1.00 40.40  ? 509  ILE   B CG1 1 
ATOM   5043  C  CG2 . ILE   B  1 208 ? -31.751 -8.743  5.840    1.00 32.40  ? 509  ILE   B CG2 1 
ATOM   5044  C  CD1 . ILE   B  1 208 ? -31.328 -9.552  2.876    1.00 38.90  ? 509  ILE   B CD1 1 
ATOM   5045  N  N   . CYS   B  1 209 ? -32.753 -5.333  6.255    1.00 28.84  ? 510  CYS   B N   1 
ATOM   5046  C  CA  . CYS   B  1 209 ? -32.576 -4.497  7.437    1.00 28.50  ? 510  CYS   B CA  1 
ATOM   5047  C  C   . CYS   B  1 209 ? -33.914 -4.120  8.052    1.00 34.66  ? 510  CYS   B C   1 
ATOM   5048  O  O   . CYS   B  1 209 ? -34.114 -4.257  9.265    1.00 34.50  ? 510  CYS   B O   1 
ATOM   5049  C  CB  . CYS   B  1 209 ? -31.788 -3.242  7.086    1.00 27.32  ? 510  CYS   B CB  1 
ATOM   5050  S  SG  . CYS   B  1 209 ? -30.075 -3.589  6.747    1.00 31.10  ? 510  CYS   B SG  1 
ATOM   5051  N  N   . ILE   B  1 210 ? -34.838 -3.620  7.234    1.00 35.37  ? 511  ILE   B N   1 
ATOM   5052  C  CA  . ILE   B  1 210 ? -36.129 -3.214  7.769    1.00 35.42  ? 511  ILE   B CA  1 
ATOM   5053  C  C   . ILE   B  1 210 ? -36.815 -4.398  8.432    1.00 34.90  ? 511  ILE   B C   1 
ATOM   5054  O  O   . ILE   B  1 210 ? -37.374 -4.280  9.527    1.00 35.83  ? 511  ILE   B O   1 
ATOM   5055  C  CB  . ILE   B  1 210 ? -36.992 -2.595  6.655    1.00 39.20  ? 511  ILE   B CB  1 
ATOM   5056  C  CG1 . ILE   B  1 210 ? -36.376 -1.267  6.204    1.00 36.31  ? 511  ILE   B CG1 1 
ATOM   5057  C  CG2 . ILE   B  1 210 ? -38.431 -2.412  7.135    1.00 36.66  ? 511  ILE   B CG2 1 
ATOM   5058  C  CD1 . ILE   B  1 210 ? -36.892 -0.758  4.866    1.00 30.38  ? 511  ILE   B CD1 1 
ATOM   5059  N  N   . GLN   B  1 211 ? -36.741 -5.569  7.802    1.00 38.75  ? 512  GLN   B N   1 
ATOM   5060  C  CA  . GLN   B  1 211 ? -37.377 -6.749  8.372    1.00 39.68  ? 512  GLN   B CA  1 
ATOM   5061  C  C   . GLN   B  1 211 ? -36.766 -7.123  9.714    1.00 41.36  ? 512  GLN   B C   1 
ATOM   5062  O  O   . GLN   B  1 211 ? -37.462 -7.650  10.584   1.00 38.60  ? 512  GLN   B O   1 
ATOM   5063  C  CB  . GLN   B  1 211 ? -37.270 -7.909  7.395    1.00 40.84  ? 512  GLN   B CB  1 
ATOM   5064  C  CG  . GLN   B  1 211 ? -37.972 -9.151  7.850    1.00 55.96  ? 512  GLN   B CG  1 
ATOM   5065  C  CD  . GLN   B  1 211 ? -37.764 -10.278 6.879    1.00 72.76  ? 512  GLN   B CD  1 
ATOM   5066  O  OE1 . GLN   B  1 211 ? -37.168 -10.092 5.814    1.00 78.78  ? 512  GLN   B OE1 1 
ATOM   5067  N  NE2 . GLN   B  1 211 ? -38.246 -11.460 7.233    1.00 74.39  ? 512  GLN   B NE2 1 
ATOM   5068  N  N   . GLN   B  1 212 ? -35.476 -6.850  9.902    1.00 40.26  ? 513  GLN   B N   1 
ATOM   5069  C  CA  . GLN   B  1 212 ? -34.791 -7.143  11.153   1.00 41.02  ? 513  GLN   B CA  1 
ATOM   5070  C  C   . GLN   B  1 212 ? -35.036 -6.090  12.224   1.00 45.36  ? 513  GLN   B C   1 
ATOM   5071  O  O   . GLN   B  1 212 ? -34.516 -6.233  13.336   1.00 46.16  ? 513  GLN   B O   1 
ATOM   5072  C  CB  . GLN   B  1 212 ? -33.280 -7.282  10.916   1.00 42.73  ? 513  GLN   B CB  1 
ATOM   5073  C  CG  . GLN   B  1 212 ? -32.880 -8.419  9.991    1.00 44.99  ? 513  GLN   B CG  1 
ATOM   5074  C  CD  . GLN   B  1 212 ? -33.479 -9.744  10.407   1.00 51.21  ? 513  GLN   B CD  1 
ATOM   5075  O  OE1 . GLN   B  1 212 ? -34.017 -10.480 9.577    1.00 55.40  ? 513  GLN   B OE1 1 
ATOM   5076  N  NE2 . GLN   B  1 212 ? -33.394 -10.057 11.698   1.00 43.67  ? 513  GLN   B NE2 1 
ATOM   5077  N  N   . GLY   B  1 213 ? -35.791 -5.038  11.924   1.00 39.02  ? 514  GLY   B N   1 
ATOM   5078  C  CA  . GLY   B  1 213 ? -36.163 -4.049  12.919   1.00 40.56  ? 514  GLY   B CA  1 
ATOM   5079  C  C   . GLY   B  1 213 ? -35.686 -2.645  12.630   1.00 41.66  ? 514  GLY   B C   1 
ATOM   5080  O  O   . GLY   B  1 213 ? -36.052 -1.720  13.368   1.00 39.18  ? 514  GLY   B O   1 
ATOM   5081  N  N   . TRP   B  1 214 ? -34.894 -2.435  11.583   1.00 41.10  ? 515  TRP   B N   1 
ATOM   5082  C  CA  . TRP   B  1 214 ? -34.401 -1.101  11.280   1.00 33.34  ? 515  TRP   B CA  1 
ATOM   5083  C  C   . TRP   B  1 214 ? -35.543 -0.158  10.938   1.00 32.31  ? 515  TRP   B C   1 
ATOM   5084  O  O   . TRP   B  1 214 ? -36.394 -0.469  10.101   1.00 39.06  ? 515  TRP   B O   1 
ATOM   5085  C  CB  . TRP   B  1 214 ? -33.419 -1.158  10.117   1.00 33.52  ? 515  TRP   B CB  1 
ATOM   5086  C  CG  . TRP   B  1 214 ? -32.741 0.141   9.888    1.00 34.75  ? 515  TRP   B CG  1 
ATOM   5087  C  CD1 . TRP   B  1 214 ? -32.091 0.902   10.818   1.00 35.05  ? 515  TRP   B CD1 1 
ATOM   5088  C  CD2 . TRP   B  1 214 ? -32.628 0.838   8.646    1.00 33.76  ? 515  TRP   B CD2 1 
ATOM   5089  N  NE1 . TRP   B  1 214 ? -31.583 2.036   10.230   1.00 30.30  ? 515  TRP   B NE1 1 
ATOM   5090  C  CE2 . TRP   B  1 214 ? -31.897 2.019   8.896    1.00 36.36  ? 515  TRP   B CE2 1 
ATOM   5091  C  CE3 . TRP   B  1 214 ? -33.068 0.577   7.345    1.00 29.27  ? 515  TRP   B CE3 1 
ATOM   5092  C  CZ2 . TRP   B  1 214 ? -31.599 2.936   7.894    1.00 23.94  ? 515  TRP   B CZ2 1 
ATOM   5093  C  CZ3 . TRP   B  1 214 ? -32.779 1.493   6.354    1.00 32.56  ? 515  TRP   B CZ3 1 
ATOM   5094  C  CH2 . TRP   B  1 214 ? -32.048 2.656   6.630    1.00 30.99  ? 515  TRP   B CH2 1 
ATOM   5095  N  N   . LYS   B  1 215 ? -35.546 1.003   11.578   1.00 30.16  ? 516  LYS   B N   1 
ATOM   5096  C  CA  . LYS   B  1 215 ? -36.521 2.053   11.329   1.00 35.35  ? 516  LYS   B CA  1 
ATOM   5097  C  C   . LYS   B  1 215 ? -35.906 3.014   10.331   1.00 38.21  ? 516  LYS   B C   1 
ATOM   5098  O  O   . LYS   B  1 215 ? -35.079 3.853   10.703   1.00 45.47  ? 516  LYS   B O   1 
ATOM   5099  C  CB  . LYS   B  1 215 ? -36.891 2.782   12.619   1.00 49.71  ? 516  LYS   B CB  1 
ATOM   5100  C  CG  . LYS   B  1 215 ? -37.307 1.865   13.756   1.00 63.91  ? 516  LYS   B CG  1 
ATOM   5101  C  CD  . LYS   B  1 215 ? -38.819 1.796   13.894   1.00 71.74  ? 516  LYS   B CD  1 
ATOM   5102  C  CE  . LYS   B  1 215 ? -39.258 0.422   14.370   1.00 73.10  ? 516  LYS   B CE  1 
ATOM   5103  N  NZ  . LYS   B  1 215 ? -38.956 -0.630  13.347   1.00 69.81  ? 516  LYS   B NZ  1 
ATOM   5104  N  N   . PRO   B  1 216 ? -36.280 2.920   9.064    1.00 39.49  ? 517  PRO   B N   1 
ATOM   5105  C  CA  . PRO   B  1 216 ? -35.590 3.676   8.022    1.00 39.15  ? 517  PRO   B CA  1 
ATOM   5106  C  C   . PRO   B  1 216 ? -36.058 5.118   7.991    1.00 43.60  ? 517  PRO   B C   1 
ATOM   5107  O  O   . PRO   B  1 216 ? -37.253 5.398   8.162    1.00 44.56  ? 517  PRO   B O   1 
ATOM   5108  C  CB  . PRO   B  1 216 ? -35.997 2.936   6.746    1.00 36.16  ? 517  PRO   B CB  1 
ATOM   5109  C  CG  . PRO   B  1 216 ? -37.396 2.468   7.053    1.00 37.84  ? 517  PRO   B CG  1 
ATOM   5110  C  CD  . PRO   B  1 216 ? -37.427 2.158   8.535    1.00 40.64  ? 517  PRO   B CD  1 
ATOM   5111  N  N   . PRO   B  1 217 ? -35.147 6.068   7.776    1.00 43.35  ? 518  PRO   B N   1 
ATOM   5112  C  CA  . PRO   B  1 217 ? -35.582 7.456   7.543    1.00 39.43  ? 518  PRO   B CA  1 
ATOM   5113  C  C   . PRO   B  1 217 ? -36.334 7.637   6.234    1.00 38.03  ? 518  PRO   B C   1 
ATOM   5114  O  O   . PRO   B  1 217 ? -37.100 8.598   6.103    1.00 40.61  ? 518  PRO   B O   1 
ATOM   5115  C  CB  . PRO   B  1 217 ? -34.264 8.244   7.540    1.00 36.49  ? 518  PRO   B CB  1 
ATOM   5116  C  CG  . PRO   B  1 217 ? -33.263 7.339   8.182    1.00 41.10  ? 518  PRO   B CG  1 
ATOM   5117  C  CD  . PRO   B  1 217 ? -33.685 5.948   7.838    1.00 40.80  ? 518  PRO   B CD  1 
ATOM   5118  N  N   . ARG   B  1 218 ? -36.151 6.740   5.265    1.00 41.96  ? 519  ARG   B N   1 
ATOM   5119  C  CA  . ARG   B  1 218 ? -36.767 6.861   3.942    1.00 42.00  ? 519  ARG   B CA  1 
ATOM   5120  C  C   . ARG   B  1 218 ? -36.371 8.180   3.279    1.00 45.06  ? 519  ARG   B C   1 
ATOM   5121  O  O   . ARG   B  1 218 ? -37.208 8.947   2.800    1.00 50.52  ? 519  ARG   B O   1 
ATOM   5122  C  CB  . ARG   B  1 218 ? -38.286 6.697   4.016    1.00 46.57  ? 519  ARG   B CB  1 
ATOM   5123  C  CG  . ARG   B  1 218 ? -38.694 5.400   4.686    1.00 49.37  ? 519  ARG   B CG  1 
ATOM   5124  C  CD  . ARG   B  1 218 ? -40.104 4.951   4.326    1.00 53.81  ? 519  ARG   B CD  1 
ATOM   5125  N  NE  . ARG   B  1 218 ? -40.141 3.494   4.187    1.00 67.68  ? 519  ARG   B NE  1 
ATOM   5126  C  CZ  . ARG   B  1 218 ? -40.118 2.858   3.018    1.00 72.17  ? 519  ARG   B CZ  1 
ATOM   5127  N  NH1 . ARG   B  1 218 ? -40.137 1.530   2.975    1.00 74.20  ? 519  ARG   B NH1 1 
ATOM   5128  N  NH2 . ARG   B  1 218 ? -40.090 3.552   1.885    1.00 68.64  ? 519  ARG   B NH2 1 
ATOM   5129  N  N   . GLY   B  1 219 ? -35.066 8.447   3.278    1.00 44.53  ? 520  GLY   B N   1 
ATOM   5130  C  CA  . GLY   B  1 219 ? -34.479 9.525   2.521    1.00 39.32  ? 520  GLY   B CA  1 
ATOM   5131  C  C   . GLY   B  1 219 ? -33.626 8.980   1.386    1.00 38.04  ? 520  GLY   B C   1 
ATOM   5132  O  O   . GLY   B  1 219 ? -33.532 7.777   1.155    1.00 36.30  ? 520  GLY   B O   1 
ATOM   5133  N  N   . ARG   B  1 220 ? -32.982 9.906   0.678    1.00 35.32  ? 521  ARG   B N   1 
ATOM   5134  C  CA  . ARG   B  1 220 ? -32.209 9.533   -0.501   1.00 28.35  ? 521  ARG   B CA  1 
ATOM   5135  C  C   . ARG   B  1 220 ? -30.807 9.045   -0.165   1.00 33.51  ? 521  ARG   B C   1 
ATOM   5136  O  O   . ARG   B  1 220 ? -30.184 8.356   -0.988   1.00 32.14  ? 521  ARG   B O   1 
ATOM   5137  C  CB  . ARG   B  1 220 ? -32.126 10.717  -1.460   1.00 25.92  ? 521  ARG   B CB  1 
ATOM   5138  C  CG  . ARG   B  1 220 ? -31.667 10.346  -2.854   1.00 28.33  ? 521  ARG   B CG  1 
ATOM   5139  C  CD  . ARG   B  1 220 ? -31.819 11.551  -3.736   1.00 30.66  ? 521  ARG   B CD  1 
ATOM   5140  N  NE  . ARG   B  1 220 ? -31.402 11.329  -5.109   1.00 40.04  ? 521  ARG   B NE  1 
ATOM   5141  C  CZ  . ARG   B  1 220 ? -30.888 12.285  -5.878   1.00 45.46  ? 521  ARG   B CZ  1 
ATOM   5142  N  NH1 . ARG   B  1 220 ? -30.702 13.511  -5.386   1.00 44.20  ? 521  ARG   B NH1 1 
ATOM   5143  N  NH2 . ARG   B  1 220 ? -30.545 12.014  -7.126   1.00 46.19  ? 521  ARG   B NH2 1 
ATOM   5144  N  N   . PHE   B  1 221 ? -30.294 9.378   1.019    1.00 37.45  ? 522  PHE   B N   1 
ATOM   5145  C  CA  . PHE   B  1 221 ? -28.937 9.024   1.399    1.00 33.72  ? 522  PHE   B CA  1 
ATOM   5146  C  C   . PHE   B  1 221 ? -28.923 8.598   2.865    1.00 32.86  ? 522  PHE   B C   1 
ATOM   5147  O  O   . PHE   B  1 221 ? -28.227 9.169   3.699    1.00 33.78  ? 522  PHE   B O   1 
ATOM   5148  C  CB  . PHE   B  1 221 ? -27.967 10.180  1.158    1.00 30.36  ? 522  PHE   B CB  1 
ATOM   5149  C  CG  . PHE   B  1 221 ? -27.872 10.602  -0.279   1.00 31.87  ? 522  PHE   B CG  1 
ATOM   5150  C  CD1 . PHE   B  1 221 ? -28.495 11.755  -0.713   1.00 29.40  ? 522  PHE   B CD1 1 
ATOM   5151  C  CD2 . PHE   B  1 221 ? -27.160 9.842   -1.195   1.00 29.64  ? 522  PHE   B CD2 1 
ATOM   5152  C  CE1 . PHE   B  1 221 ? -28.406 12.145  -2.039   1.00 37.55  ? 522  PHE   B CE1 1 
ATOM   5153  C  CE2 . PHE   B  1 221 ? -27.064 10.228  -2.510   1.00 39.26  ? 522  PHE   B CE2 1 
ATOM   5154  C  CZ  . PHE   B  1 221 ? -27.691 11.379  -2.934   1.00 35.85  ? 522  PHE   B CZ  1 
ATOM   5155  N  N   . ASP   B  1 222 ? -29.714 7.574   3.185    1.00 26.38  ? 523  ASP   B N   1 
ATOM   5156  C  CA  . ASP   B  1 222 ? -29.703 6.993   4.523    1.00 26.87  ? 523  ASP   B CA  1 
ATOM   5157  C  C   . ASP   B  1 222 ? -28.544 6.020   4.641    1.00 27.06  ? 523  ASP   B C   1 
ATOM   5158  O  O   . ASP   B  1 222 ? -28.523 5.005   3.946    1.00 31.02  ? 523  ASP   B O   1 
ATOM   5159  C  CB  . ASP   B  1 222 ? -31.006 6.253   4.799    1.00 25.51  ? 523  ASP   B CB  1 
ATOM   5160  C  CG  . ASP   B  1 222 ? -32.200 7.137   4.664    1.00 29.57  ? 523  ASP   B CG  1 
ATOM   5161  O  OD1 . ASP   B  1 222 ? -32.021 8.365   4.766    1.00 33.25  ? 523  ASP   B OD1 1 
ATOM   5162  O  OD2 . ASP   B  1 222 ? -33.311 6.608   4.461    1.00 33.65  ? 523  ASP   B OD2 1 
ATOM   5163  N  N   . VAL   B  1 223 ? -27.584 6.303   5.520    1.00 27.94  ? 524  VAL   B N   1 
ATOM   5164  C  CA  . VAL   B  1 223 ? -26.534 5.320   5.751    1.00 27.25  ? 524  VAL   B CA  1 
ATOM   5165  C  C   . VAL   B  1 223 ? -27.165 4.069   6.333    1.00 25.66  ? 524  VAL   B C   1 
ATOM   5166  O  O   . VAL   B  1 223 ? -27.901 4.136   7.320    1.00 25.60  ? 524  VAL   B O   1 
ATOM   5167  C  CB  . VAL   B  1 223 ? -25.458 5.880   6.685    1.00 31.77  ? 524  VAL   B CB  1 
ATOM   5168  C  CG1 . VAL   B  1 223 ? -24.419 4.804   6.951    1.00 28.45  ? 524  VAL   B CG1 1 
ATOM   5169  C  CG2 . VAL   B  1 223 ? -24.821 7.121   6.072    1.00 28.09  ? 524  VAL   B CG2 1 
ATOM   5170  N  N   . LEU   B  1 224 ? -26.894 2.921   5.719    1.00 24.94  ? 525  LEU   B N   1 
ATOM   5171  C  CA  . LEU   B  1 224 ? -27.526 1.698   6.182    1.00 26.54  ? 525  LEU   B CA  1 
ATOM   5172  C  C   . LEU   B  1 224 ? -26.934 1.257   7.523    1.00 23.82  ? 525  LEU   B C   1 
ATOM   5173  O  O   . LEU   B  1 224 ? -25.779 1.554   7.828    1.00 21.46  ? 525  LEU   B O   1 
ATOM   5174  C  CB  . LEU   B  1 224 ? -27.352 0.591   5.151    1.00 21.38  ? 525  LEU   B CB  1 
ATOM   5175  C  CG  . LEU   B  1 224 ? -28.297 0.685   3.954    1.00 24.59  ? 525  LEU   B CG  1 
ATOM   5176  C  CD1 . LEU   B  1 224 ? -27.629 0.073   2.737    1.00 21.47  ? 525  LEU   B CD1 1 
ATOM   5177  C  CD2 . LEU   B  1 224 ? -29.603 -0.037  4.296    1.00 23.28  ? 525  LEU   B CD2 1 
ATOM   5178  N  N   . PRO   B  1 225 ? -27.697 0.535   8.332    1.00 21.60  ? 526  PRO   B N   1 
ATOM   5179  C  CA  . PRO   B  1 225 ? -27.123 -0.051  9.543    1.00 22.68  ? 526  PRO   B CA  1 
ATOM   5180  C  C   . PRO   B  1 225 ? -26.205 -1.200  9.179    1.00 25.66  ? 526  PRO   B C   1 
ATOM   5181  O  O   . PRO   B  1 225 ? -26.337 -1.820  8.124    1.00 24.37  ? 526  PRO   B O   1 
ATOM   5182  C  CB  . PRO   B  1 225 ? -28.351 -0.555  10.304   1.00 22.96  ? 526  PRO   B CB  1 
ATOM   5183  C  CG  . PRO   B  1 225 ? -29.287 -0.929  9.233    1.00 28.40  ? 526  PRO   B CG  1 
ATOM   5184  C  CD  . PRO   B  1 225 ? -29.098 0.112   8.139    1.00 24.96  ? 526  PRO   B CD  1 
ATOM   5185  N  N   . LEU   B  1 226 ? -25.266 -1.491  10.066   1.00 24.41  ? 527  LEU   B N   1 
ATOM   5186  C  CA  . LEU   B  1 226 ? -24.488 -2.709  9.917    1.00 25.57  ? 527  LEU   B CA  1 
ATOM   5187  C  C   . LEU   B  1 226 ? -25.333 -3.906  10.312   1.00 28.13  ? 527  LEU   B C   1 
ATOM   5188  O  O   . LEU   B  1 226 ? -26.094 -3.851  11.282   1.00 30.88  ? 527  LEU   B O   1 
ATOM   5189  C  CB  . LEU   B  1 226 ? -23.229 -2.660  10.761   1.00 21.17  ? 527  LEU   B CB  1 
ATOM   5190  C  CG  . LEU   B  1 226 ? -22.187 -1.660  10.295   1.00 26.06  ? 527  LEU   B CG  1 
ATOM   5191  C  CD1 . LEU   B  1 226 ? -21.098 -1.540  11.334   1.00 23.79  ? 527  LEU   B CD1 1 
ATOM   5192  C  CD2 . LEU   B  1 226 ? -21.607 -2.051  8.932    1.00 23.01  ? 527  LEU   B CD2 1 
ATOM   5193  N  N   . LEU   B  1 227 ? -25.213 -4.983  9.536    1.00 25.94  ? 528  LEU   B N   1 
ATOM   5194  C  CA  . LEU   B  1 227 ? -25.899 -6.249  9.791    1.00 26.43  ? 528  LEU   B CA  1 
ATOM   5195  C  C   . LEU   B  1 227 ? -24.795 -7.278  9.958    1.00 27.80  ? 528  LEU   B C   1 
ATOM   5196  O  O   . LEU   B  1 227 ? -24.190 -7.714  8.971    1.00 25.06  ? 528  LEU   B O   1 
ATOM   5197  C  CB  . LEU   B  1 227 ? -26.830 -6.641  8.653    1.00 32.34  ? 528  LEU   B CB  1 
ATOM   5198  C  CG  . LEU   B  1 227 ? -28.252 -7.110  8.959    1.00 35.43  ? 528  LEU   B CG  1 
ATOM   5199  C  CD1 . LEU   B  1 227 ? -28.699 -8.126  7.923    1.00 31.47  ? 528  LEU   B CD1 1 
ATOM   5200  C  CD2 . LEU   B  1 227 ? -28.429 -7.641  10.381   1.00 28.96  ? 528  LEU   B CD2 1 
ATOM   5201  N  N   . LEU   B  1 228 ? -24.542 -7.676  11.199   1.00 24.44  ? 529  LEU   B N   1 
ATOM   5202  C  CA  . LEU   B  1 228 ? -23.309 -8.360  11.542   1.00 22.68  ? 529  LEU   B CA  1 
ATOM   5203  C  C   . LEU   B  1 228 ? -23.622 -9.734  12.102   1.00 26.94  ? 529  LEU   B C   1 
ATOM   5204  O  O   . LEU   B  1 228 ? -24.452 -9.872  13.010   1.00 26.20  ? 529  LEU   B O   1 
ATOM   5205  C  CB  . LEU   B  1 228 ? -22.501 -7.547  12.558   1.00 22.43  ? 529  LEU   B CB  1 
ATOM   5206  C  CG  . LEU   B  1 228 ? -22.168 -6.140  12.083   1.00 22.99  ? 529  LEU   B CG  1 
ATOM   5207  C  CD1 . LEU   B  1 228 ? -21.427 -5.369  13.153   1.00 26.93  ? 529  LEU   B CD1 1 
ATOM   5208  C  CD2 . LEU   B  1 228 ? -21.351 -6.214  10.804   1.00 24.26  ? 529  LEU   B CD2 1 
ATOM   5209  N  N   . GLN   B  1 229 ? -22.922 -10.735 11.587   1.00 23.81  ? 530  GLN   B N   1 
ATOM   5210  C  CA  . GLN   B  1 229 ? -23.151 -12.122 11.947   1.00 23.58  ? 530  GLN   B CA  1 
ATOM   5211  C  C   . GLN   B  1 229 ? -21.866 -12.679 12.528   1.00 23.44  ? 530  GLN   B C   1 
ATOM   5212  O  O   . GLN   B  1 229 ? -20.817 -12.644 11.875   1.00 24.59  ? 530  GLN   B O   1 
ATOM   5213  C  CB  . GLN   B  1 229 ? -23.588 -12.940 10.730   1.00 23.89  ? 530  GLN   B CB  1 
ATOM   5214  C  CG  . GLN   B  1 229 ? -23.448 -14.416 10.962   1.00 28.97  ? 530  GLN   B CG  1 
ATOM   5215  C  CD  . GLN   B  1 229 ? -23.930 -15.233 9.793    1.00 28.20  ? 530  GLN   B CD  1 
ATOM   5216  O  OE1 . GLN   B  1 229 ? -23.790 -14.832 8.648    1.00 31.61  ? 530  GLN   B OE1 1 
ATOM   5217  N  NE2 . GLN   B  1 229 ? -24.522 -16.383 10.084   1.00 33.93  ? 530  GLN   B NE2 1 
ATOM   5218  N  N   . ALA   B  1 230 ? -21.950 -13.175 13.752   1.00 25.69  ? 531  ALA   B N   1 
ATOM   5219  C  CA  . ALA   B  1 230 ? -20.812 -13.740 14.457   1.00 28.92  ? 531  ALA   B CA  1 
ATOM   5220  C  C   . ALA   B  1 230 ? -21.088 -15.207 14.714   1.00 30.56  ? 531  ALA   B C   1 
ATOM   5221  O  O   . ALA   B  1 230 ? -22.172 -15.559 15.193   1.00 30.27  ? 531  ALA   B O   1 
ATOM   5222  C  CB  . ALA   B  1 230 ? -20.573 -13.018 15.789   1.00 22.07  ? 531  ALA   B CB  1 
ATOM   5223  N  N   . ASN   B  1 231 ? -20.118 -16.054 14.379   1.00 30.38  ? 532  ASN   B N   1 
ATOM   5224  C  CA  . ASN   B  1 231 ? -20.133 -17.446 14.815   1.00 27.36  ? 532  ASN   B CA  1 
ATOM   5225  C  C   . ASN   B  1 231 ? -21.355 -18.196 14.287   1.00 26.57  ? 532  ASN   B C   1 
ATOM   5226  O  O   . ASN   B  1 231 ? -21.855 -19.121 14.931   1.00 28.00  ? 532  ASN   B O   1 
ATOM   5227  C  CB  . ASN   B  1 231 ? -20.068 -17.531 16.344   1.00 30.41  ? 532  ASN   B CB  1 
ATOM   5228  C  CG  . ASN   B  1 231 ? -19.505 -18.851 16.830   1.00 40.98  ? 532  ASN   B CG  1 
ATOM   5229  O  OD1 . ASN   B  1 231 ? -18.524 -19.358 16.283   1.00 41.58  ? 532  ASN   B OD1 1 
ATOM   5230  N  ND2 . ASN   B  1 231 ? -20.138 -19.427 17.852   1.00 41.71  ? 532  ASN   B ND2 1 
ATOM   5231  N  N   . GLY   B  1 232 ? -21.828 -17.834 13.093   1.00 28.86  ? 533  GLY   B N   1 
ATOM   5232  C  CA  . GLY   B  1 232 ? -22.968 -18.507 12.505   1.00 31.86  ? 533  GLY   B CA  1 
ATOM   5233  C  C   . GLY   B  1 232 ? -24.306 -18.182 13.127   1.00 32.95  ? 533  GLY   B C   1 
ATOM   5234  O  O   . GLY   B  1 232 ? -25.318 -18.762 12.715   1.00 32.78  ? 533  GLY   B O   1 
ATOM   5235  N  N   . ASN   B  1 233 ? -24.349 -17.286 14.111   1.00 30.99  ? 534  ASN   B N   1 
ATOM   5236  C  CA  . ASN   B  1 233 ? -25.608 -16.863 14.704   1.00 32.36  ? 534  ASN   B CA  1 
ATOM   5237  C  C   . ASN   B  1 233 ? -26.354 -15.930 13.756   1.00 33.05  ? 534  ASN   B C   1 
ATOM   5238  O  O   . ASN   B  1 233 ? -25.814 -15.446 12.761   1.00 29.55  ? 534  ASN   B O   1 
ATOM   5239  C  CB  . ASN   B  1 233 ? -25.358 -16.167 16.039   1.00 35.29  ? 534  ASN   B CB  1 
ATOM   5240  C  CG  . ASN   B  1 233 ? -24.793 -17.107 17.073   1.00 34.36  ? 534  ASN   B CG  1 
ATOM   5241  O  OD1 . ASN   B  1 233 ? -25.249 -18.235 17.196   1.00 35.08  ? 534  ASN   B OD1 1 
ATOM   5242  N  ND2 . ASN   B  1 233 ? -23.786 -16.659 17.800   1.00 36.17  ? 534  ASN   B ND2 1 
ATOM   5243  N  N   . ASP   B  1 234 ? -27.617 -15.678 14.072   1.00 31.51  ? 535  ASP   B N   1 
ATOM   5244  C  CA  . ASP   B  1 234 ? -28.375 -14.744 13.260   1.00 32.76  ? 535  ASP   B CA  1 
ATOM   5245  C  C   . ASP   B  1 234 ? -27.702 -13.373 13.293   1.00 29.38  ? 535  ASP   B C   1 
ATOM   5246  O  O   . ASP   B  1 234 ? -27.140 -12.978 14.318   1.00 28.47  ? 535  ASP   B O   1 
ATOM   5247  C  CB  . ASP   B  1 234 ? -29.818 -14.631 13.750   1.00 32.66  ? 535  ASP   B CB  1 
ATOM   5248  C  CG  . ASP   B  1 234 ? -30.616 -15.899 13.522   1.00 34.21  ? 535  ASP   B CG  1 
ATOM   5249  O  OD1 . ASP   B  1 234 ? -31.694 -16.032 14.134   1.00 36.47  ? 535  ASP   B OD1 1 
ATOM   5250  O  OD2 . ASP   B  1 234 ? -30.168 -16.765 12.742   1.00 32.24  ? 535  ASP   B OD2 1 
ATOM   5251  N  N   . PRO   B  1 235 ? -27.718 -12.634 12.194   1.00 32.29  ? 536  PRO   B N   1 
ATOM   5252  C  CA  . PRO   B  1 235 ? -27.063 -11.326 12.185   1.00 28.57  ? 536  PRO   B CA  1 
ATOM   5253  C  C   . PRO   B  1 235 ? -27.856 -10.329 13.014   1.00 26.41  ? 536  PRO   B C   1 
ATOM   5254  O  O   . PRO   B  1 235 ? -29.055 -10.489 13.243   1.00 29.37  ? 536  PRO   B O   1 
ATOM   5255  C  CB  . PRO   B  1 235 ? -27.051 -10.947 10.705   1.00 24.55  ? 536  PRO   B CB  1 
ATOM   5256  C  CG  . PRO   B  1 235 ? -28.268 -11.640 10.158   1.00 27.16  ? 536  PRO   B CG  1 
ATOM   5257  C  CD  . PRO   B  1 235 ? -28.372 -12.939 10.910   1.00 28.82  ? 536  PRO   B CD  1 
ATOM   5258  N  N   . GLU   B  1 236 ? -27.157 -9.291  13.468   1.00 24.35  ? 537  GLU   B N   1 
ATOM   5259  C  CA  . GLU   B  1 236 ? -27.718 -8.285  14.362   1.00 25.33  ? 537  GLU   B CA  1 
ATOM   5260  C  C   . GLU   B  1 236 ? -27.478 -6.884  13.807   1.00 24.29  ? 537  GLU   B C   1 
ATOM   5261  O  O   . GLU   B  1 236 ? -26.418 -6.610  13.232   1.00 24.92  ? 537  GLU   B O   1 
ATOM   5262  C  CB  . GLU   B  1 236 ? -27.097 -8.426  15.761   1.00 29.57  ? 537  GLU   B CB  1 
ATOM   5263  C  CG  . GLU   B  1 236 ? -27.353 -9.801  16.398   1.00 35.41  ? 537  GLU   B CG  1 
ATOM   5264  C  CD  . GLU   B  1 236 ? -26.523 -10.046 17.655   1.00 41.65  ? 537  GLU   B CD  1 
ATOM   5265  O  OE1 . GLU   B  1 236 ? -26.299 -9.084  18.424   1.00 38.19  ? 537  GLU   B OE1 1 
ATOM   5266  O  OE2 . GLU   B  1 236 ? -26.093 -11.206 17.869   1.00 43.11  ? 537  GLU   B OE2 1 
ATOM   5267  N  N   . LEU   B  1 237 ? -28.458 -5.997  13.997   1.00 24.30  ? 538  LEU   B N   1 
ATOM   5268  C  CA  . LEU   B  1 237 ? -28.386 -4.628  13.493   1.00 23.62  ? 538  LEU   B CA  1 
ATOM   5269  C  C   . LEU   B  1 237 ? -27.628 -3.701  14.434   1.00 29.30  ? 538  LEU   B C   1 
ATOM   5270  O  O   . LEU   B  1 237 ? -27.811 -3.745  15.654   1.00 31.87  ? 538  LEU   B O   1 
ATOM   5271  C  CB  . LEU   B  1 237 ? -29.793 -4.060  13.291   1.00 24.03  ? 538  LEU   B CB  1 
ATOM   5272  C  CG  . LEU   B  1 237 ? -30.639 -4.647  12.177   1.00 30.84  ? 538  LEU   B CG  1 
ATOM   5273  C  CD1 . LEU   B  1 237 ? -32.010 -4.040  12.301   1.00 31.28  ? 538  LEU   B CD1 1 
ATOM   5274  C  CD2 . LEU   B  1 237 ? -30.011 -4.334  10.822   1.00 32.43  ? 538  LEU   B CD2 1 
ATOM   5275  N  N   . PHE   B  1 238 ? -26.807 -2.825  13.854   1.00 29.84  ? 539  PHE   B N   1 
ATOM   5276  C  CA  . PHE   B  1 238 ? -26.079 -1.800  14.599   1.00 23.55  ? 539  PHE   B CA  1 
ATOM   5277  C  C   . PHE   B  1 238 ? -26.001 -0.546  13.749   1.00 28.11  ? 539  PHE   B C   1 
ATOM   5278  O  O   . PHE   B  1 238 ? -25.646 -0.621  12.567   1.00 30.23  ? 539  PHE   B O   1 
ATOM   5279  C  CB  . PHE   B  1 238 ? -24.657 -2.241  14.943   1.00 23.15  ? 539  PHE   B CB  1 
ATOM   5280  C  CG  . PHE   B  1 238 ? -24.589 -3.464  15.773   1.00 27.84  ? 539  PHE   B CG  1 
ATOM   5281  C  CD1 . PHE   B  1 238 ? -24.474 -4.702  15.182   1.00 26.96  ? 539  PHE   B CD1 1 
ATOM   5282  C  CD2 . PHE   B  1 238 ? -24.631 -3.379  17.154   1.00 24.61  ? 539  PHE   B CD2 1 
ATOM   5283  C  CE1 . PHE   B  1 238 ? -24.408 -5.841  15.945   1.00 33.59  ? 539  PHE   B CE1 1 
ATOM   5284  C  CE2 . PHE   B  1 238 ? -24.565 -4.521  17.930   1.00 32.91  ? 539  PHE   B CE2 1 
ATOM   5285  C  CZ  . PHE   B  1 238 ? -24.452 -5.752  17.327   1.00 38.80  ? 539  PHE   B CZ  1 
ATOM   5286  N  N   . GLN   B  1 239 ? -26.290 0.599   14.354   1.00 25.41  ? 540  GLN   B N   1 
ATOM   5287  C  CA  . GLN   B  1 239 ? -26.171 1.886   13.679   1.00 30.67  ? 540  GLN   B CA  1 
ATOM   5288  C  C   . GLN   B  1 239 ? -24.746 2.399   13.840   1.00 27.95  ? 540  GLN   B C   1 
ATOM   5289  O  O   . GLN   B  1 239 ? -24.285 2.620   14.966   1.00 30.23  ? 540  GLN   B O   1 
ATOM   5290  C  CB  . GLN   B  1 239 ? -27.165 2.903   14.245   1.00 32.60  ? 540  GLN   B CB  1 
ATOM   5291  C  CG  . GLN   B  1 239 ? -27.001 4.330   13.678   1.00 39.02  ? 540  GLN   B CG  1 
ATOM   5292  C  CD  . GLN   B  1 239 ? -27.501 5.437   14.627   1.00 50.59  ? 540  GLN   B CD  1 
ATOM   5293  O  OE1 . GLN   B  1 239 ? -27.193 5.448   15.824   1.00 48.98  ? 540  GLN   B OE1 1 
ATOM   5294  N  NE2 . GLN   B  1 239 ? -28.265 6.377   14.082   1.00 58.32  ? 540  GLN   B NE2 1 
ATOM   5295  N  N   . ILE   B  1 240 ? -24.055 2.597   12.723   1.00 24.12  ? 541  ILE   B N   1 
ATOM   5296  C  CA  . ILE   B  1 240 ? -22.737 3.238   12.811   1.00 27.24  ? 541  ILE   B CA  1 
ATOM   5297  C  C   . ILE   B  1 240 ? -22.920 4.632   13.382   1.00 34.87  ? 541  ILE   B C   1 
ATOM   5298  O  O   . ILE   B  1 240 ? -23.779 5.389   12.883   1.00 33.40  ? 541  ILE   B O   1 
ATOM   5299  C  CB  . ILE   B  1 240 ? -22.073 3.313   11.430   1.00 28.12  ? 541  ILE   B CB  1 
ATOM   5300  C  CG1 . ILE   B  1 240 ? -21.905 1.916   10.837   1.00 32.21  ? 541  ILE   B CG1 1 
ATOM   5301  C  CG2 . ILE   B  1 240 ? -20.738 4.004   11.538   1.00 26.48  ? 541  ILE   B CG2 1 
ATOM   5302  C  CD1 . ILE   B  1 240 ? -21.279 1.933   9.444    1.00 29.56  ? 541  ILE   B CD1 1 
ATOM   5303  N  N   . PRO   B  1 241 ? -22.187 5.021   14.424   1.00 30.15  ? 542  PRO   B N   1 
ATOM   5304  C  CA  . PRO   B  1 241 ? -22.339 6.373   14.963   1.00 31.89  ? 542  PRO   B CA  1 
ATOM   5305  C  C   . PRO   B  1 241 ? -22.135 7.392   13.859   1.00 29.64  ? 542  PRO   B C   1 
ATOM   5306  O  O   . PRO   B  1 241 ? -21.139 7.320   13.115   1.00 23.52  ? 542  PRO   B O   1 
ATOM   5307  C  CB  . PRO   B  1 241 ? -21.237 6.462   16.028   1.00 29.61  ? 542  PRO   B CB  1 
ATOM   5308  C  CG  . PRO   B  1 241 ? -20.944 5.031   16.379   1.00 29.09  ? 542  PRO   B CG  1 
ATOM   5309  C  CD  . PRO   B  1 241 ? -21.093 4.291   15.081   1.00 30.09  ? 542  PRO   B CD  1 
ATOM   5310  N  N   . PRO   B  1 242 ? -23.082 8.318   13.689   1.00 25.86  ? 543  PRO   B N   1 
ATOM   5311  C  CA  . PRO   B  1 242 ? -23.033 9.207   12.516   1.00 31.68  ? 543  PRO   B CA  1 
ATOM   5312  C  C   . PRO   B  1 242 ? -21.763 10.024  12.429   1.00 35.43  ? 543  PRO   B C   1 
ATOM   5313  O  O   . PRO   B  1 242 ? -21.286 10.282  11.315   1.00 34.91  ? 543  PRO   B O   1 
ATOM   5314  C  CB  . PRO   B  1 242 ? -24.276 10.088  12.697   1.00 32.73  ? 543  PRO   B CB  1 
ATOM   5315  C  CG  . PRO   B  1 242 ? -25.215 9.219   13.501   1.00 36.82  ? 543  PRO   B CG  1 
ATOM   5316  C  CD  . PRO   B  1 242 ? -24.309 8.515   14.480   1.00 32.02  ? 543  PRO   B CD  1 
ATOM   5317  N  N   . GLU   B  1 243 ? -21.172 10.402  13.568   1.00 30.98  ? 544  GLU   B N   1 
ATOM   5318  C  CA  . GLU   B  1 243 ? -19.930 11.166  13.553   1.00 31.36  ? 544  GLU   B CA  1 
ATOM   5319  C  C   . GLU   B  1 243 ? -18.759 10.387  12.960   1.00 26.15  ? 544  GLU   B C   1 
ATOM   5320  O  O   . GLU   B  1 243 ? -17.726 10.991  12.661   1.00 30.59  ? 544  GLU   B O   1 
ATOM   5321  C  CB  . GLU   B  1 243 ? -19.576 11.633  14.970   1.00 34.49  ? 544  GLU   B CB  1 
ATOM   5322  C  CG  . GLU   B  1 243 ? -19.224 10.512  15.949   1.00 30.55  ? 544  GLU   B CG  1 
ATOM   5323  C  CD  . GLU   B  1 243 ? -20.430 9.965   16.695   1.00 35.08  ? 544  GLU   B CD  1 
ATOM   5324  O  OE1 . GLU   B  1 243 ? -21.575 10.233  16.271   1.00 36.11  ? 544  GLU   B OE1 1 
ATOM   5325  O  OE2 . GLU   B  1 243 ? -20.232 9.280   17.724   1.00 41.33  ? 544  GLU   B OE2 1 
ATOM   5326  N  N   . LEU   B  1 244 ? -18.880 9.078   12.777   1.00 22.60  ? 545  LEU   B N   1 
ATOM   5327  C  CA  . LEU   B  1 244 ? -17.817 8.322   12.134   1.00 24.29  ? 545  LEU   B CA  1 
ATOM   5328  C  C   . LEU   B  1 244 ? -17.995 8.192   10.622   1.00 24.14  ? 545  LEU   B C   1 
ATOM   5329  O  O   . LEU   B  1 244 ? -17.078 7.708   9.955    1.00 27.00  ? 545  LEU   B O   1 
ATOM   5330  C  CB  . LEU   B  1 244 ? -17.713 6.918   12.729   1.00 20.87  ? 545  LEU   B CB  1 
ATOM   5331  C  CG  . LEU   B  1 244 ? -17.413 6.804   14.222   1.00 32.59  ? 545  LEU   B CG  1 
ATOM   5332  C  CD1 . LEU   B  1 244 ? -17.375 5.336   14.572   1.00 33.84  ? 545  LEU   B CD1 1 
ATOM   5333  C  CD2 . LEU   B  1 244 ? -16.101 7.451   14.542   1.00 33.79  ? 545  LEU   B CD2 1 
ATOM   5334  N  N   . VAL   B  1 245 ? -19.133 8.603   10.074   1.00 25.27  ? 546  VAL   B N   1 
ATOM   5335  C  CA  . VAL   B  1 245 ? -19.430 8.442   8.652    1.00 24.91  ? 546  VAL   B CA  1 
ATOM   5336  C  C   . VAL   B  1 245 ? -19.125 9.771   7.974    1.00 27.90  ? 546  VAL   B C   1 
ATOM   5337  O  O   . VAL   B  1 245 ? -19.945 10.692  7.970    1.00 24.58  ? 546  VAL   B O   1 
ATOM   5338  C  CB  . VAL   B  1 245 ? -20.879 8.009   8.421    1.00 29.90  ? 546  VAL   B CB  1 
ATOM   5339  C  CG1 . VAL   B  1 245 ? -21.214 8.042   6.926    1.00 31.71  ? 546  VAL   B CG1 1 
ATOM   5340  C  CG2 . VAL   B  1 245 ? -21.116 6.620   8.998    1.00 25.22  ? 546  VAL   B CG2 1 
ATOM   5341  N  N   . LEU   B  1 246 ? -17.937 9.884   7.397    1.00 26.87  ? 547  LEU   B N   1 
ATOM   5342  C  CA  . LEU   B  1 246 ? -17.568 11.107  6.705    1.00 24.80  ? 547  LEU   B CA  1 
ATOM   5343  C  C   . LEU   B  1 246 ? -18.268 11.152  5.349    1.00 27.80  ? 547  LEU   B C   1 
ATOM   5344  O  O   . LEU   B  1 246 ? -18.162 10.211  4.555    1.00 24.44  ? 547  LEU   B O   1 
ATOM   5345  C  CB  . LEU   B  1 246 ? -16.054 11.179  6.548    1.00 31.15  ? 547  LEU   B CB  1 
ATOM   5346  C  CG  . LEU   B  1 246 ? -15.537 12.407  5.800    1.00 38.30  ? 547  LEU   B CG  1 
ATOM   5347  C  CD1 . LEU   B  1 246 ? -16.085 13.675  6.434    1.00 39.60  ? 547  LEU   B CD1 1 
ATOM   5348  C  CD2 . LEU   B  1 246 ? -14.026 12.416  5.833    1.00 41.13  ? 547  LEU   B CD2 1 
ATOM   5349  N  N   . GLU   B  1 247 ? -18.994 12.235  5.084    1.00 29.00  ? 548  GLU   B N   1 
ATOM   5350  C  CA  . GLU   B  1 247 ? -19.662 12.402  3.802    1.00 28.82  ? 548  GLU   B CA  1 
ATOM   5351  C  C   . GLU   B  1 247 ? -19.226 13.698  3.142    1.00 31.15  ? 548  GLU   B C   1 
ATOM   5352  O  O   . GLU   B  1 247 ? -18.753 14.631  3.798    1.00 31.02  ? 548  GLU   B O   1 
ATOM   5353  C  CB  . GLU   B  1 247 ? -21.187 12.390  3.948    1.00 28.08  ? 548  GLU   B CB  1 
ATOM   5354  C  CG  . GLU   B  1 247 ? -21.731 11.051  4.410    1.00 34.11  ? 548  GLU   B CG  1 
ATOM   5355  C  CD  . GLU   B  1 247 ? -23.225 11.081  4.639    1.00 37.73  ? 548  GLU   B CD  1 
ATOM   5356  O  OE1 . GLU   B  1 247 ? -23.688 11.864  5.486    1.00 41.62  ? 548  GLU   B OE1 1 
ATOM   5357  O  OE2 . GLU   B  1 247 ? -23.941 10.328  3.962    1.00 36.64  ? 548  GLU   B OE2 1 
ATOM   5358  N  N   . VAL   B  1 248 ? -19.402 13.745  1.824    1.00 22.41  ? 549  VAL   B N   1 
ATOM   5359  C  CA  . VAL   B  1 248 ? -18.982 14.888  1.022    1.00 25.27  ? 549  VAL   B CA  1 
ATOM   5360  C  C   . VAL   B  1 248 ? -20.179 15.372  0.215    1.00 27.76  ? 549  VAL   B C   1 
ATOM   5361  O  O   . VAL   B  1 248 ? -20.668 14.643  -0.657   1.00 29.01  ? 549  VAL   B O   1 
ATOM   5362  C  CB  . VAL   B  1 248 ? -17.820 14.517  0.086    1.00 28.20  ? 549  VAL   B CB  1 
ATOM   5363  C  CG1 . VAL   B  1 248 ? -17.425 15.719  -0.783   1.00 27.54  ? 549  VAL   B CG1 1 
ATOM   5364  C  CG2 . VAL   B  1 248 ? -16.634 13.962  0.870    1.00 25.29  ? 549  VAL   B CG2 1 
ATOM   5365  N  N   . PRO   B  1 249 ? -20.683 16.574  0.463    1.00 27.13  ? 550  PRO   B N   1 
ATOM   5366  C  CA  . PRO   B  1 249 ? -21.736 17.115  -0.404   1.00 28.82  ? 550  PRO   B CA  1 
ATOM   5367  C  C   . PRO   B  1 249 ? -21.140 17.474  -1.756   1.00 30.68  ? 550  PRO   B C   1 
ATOM   5368  O  O   . PRO   B  1 249 ? -20.073 18.085  -1.831   1.00 26.00  ? 550  PRO   B O   1 
ATOM   5369  C  CB  . PRO   B  1 249 ? -22.213 18.356  0.351    1.00 25.66  ? 550  PRO   B CB  1 
ATOM   5370  C  CG  . PRO   B  1 249 ? -20.995 18.796  1.122    1.00 36.19  ? 550  PRO   B CG  1 
ATOM   5371  C  CD  . PRO   B  1 249 ? -20.220 17.547  1.469    1.00 26.20  ? 550  PRO   B CD  1 
ATOM   5372  N  N   . ILE   B  1 250 ? -21.814 17.077  -2.827   1.00 28.16  ? 551  ILE   B N   1 
ATOM   5373  C  CA  . ILE   B  1 250 ? -21.233 17.218  -4.158   1.00 24.62  ? 551  ILE   B CA  1 
ATOM   5374  C  C   . ILE   B  1 250 ? -21.654 18.553  -4.748   1.00 29.31  ? 551  ILE   B C   1 
ATOM   5375  O  O   . ILE   B  1 250 ? -22.848 18.840  -4.887   1.00 30.75  ? 551  ILE   B O   1 
ATOM   5376  C  CB  . ILE   B  1 250 ? -21.630 16.059  -5.078   1.00 24.37  ? 551  ILE   B CB  1 
ATOM   5377  C  CG1 . ILE   B  1 250 ? -21.251 14.721  -4.451   1.00 23.48  ? 551  ILE   B CG1 1 
ATOM   5378  C  CG2 . ILE   B  1 250 ? -20.959 16.240  -6.448   1.00 31.92  ? 551  ILE   B CG2 1 
ATOM   5379  C  CD1 . ILE   B  1 250 ? -19.793 14.606  -4.051   1.00 23.93  ? 551  ILE   B CD1 1 
ATOM   5380  N  N   . ARG   B  1 251 ? -20.671 19.376  -5.077   1.00 25.96  ? 552  ARG   B N   1 
ATOM   5381  C  CA  . ARG   B  1 251 ? -20.906 20.623  -5.779   1.00 28.62  ? 552  ARG   B CA  1 
ATOM   5382  C  C   . ARG   B  1 251 ? -19.934 20.700  -6.950   1.00 26.89  ? 552  ARG   B C   1 
ATOM   5383  O  O   . ARG   B  1 251 ? -19.015 19.885  -7.080   1.00 31.23  ? 552  ARG   B O   1 
ATOM   5384  C  CB  . ARG   B  1 251 ? -20.777 21.843  -4.846   1.00 32.86  ? 552  ARG   B CB  1 
ATOM   5385  C  CG  . ARG   B  1 251 ? -19.429 22.024  -4.161   1.00 35.71  ? 552  ARG   B CG  1 
ATOM   5386  C  CD  . ARG   B  1 251 ? -19.239 21.102  -2.939   1.00 30.42  ? 552  ARG   B CD  1 
ATOM   5387  N  NE  . ARG   B  1 251 ? -18.151 21.584  -2.095   1.00 33.89  ? 552  ARG   B NE  1 
ATOM   5388  C  CZ  . ARG   B  1 251 ? -17.606 20.911  -1.086   1.00 37.65  ? 552  ARG   B CZ  1 
ATOM   5389  N  NH1 . ARG   B  1 251 ? -16.627 21.463  -0.383   1.00 37.10  ? 552  ARG   B NH1 1 
ATOM   5390  N  NH2 . ARG   B  1 251 ? -18.027 19.690  -0.777   1.00 32.42  ? 552  ARG   B NH2 1 
ATOM   5391  N  N   . HIS   B  1 252 ? -20.148 21.690  -7.811   1.00 27.77  ? 553  HIS   B N   1 
ATOM   5392  C  CA  . HIS   B  1 252 ? -19.374 21.820  -9.029   1.00 32.97  ? 553  HIS   B CA  1 
ATOM   5393  C  C   . HIS   B  1 252 ? -18.639 23.156  -9.031   1.00 37.28  ? 553  HIS   B C   1 
ATOM   5394  O  O   . HIS   B  1 252 ? -19.200 24.172  -8.610   1.00 35.60  ? 553  HIS   B O   1 
ATOM   5395  C  CB  . HIS   B  1 252 ? -20.301 21.709  -10.252  1.00 30.29  ? 553  HIS   B CB  1 
ATOM   5396  C  CG  . HIS   B  1 252 ? -19.587 21.603  -11.564  1.00 29.08  ? 553  HIS   B CG  1 
ATOM   5397  N  ND1 . HIS   B  1 252 ? -19.030 22.693  -12.198  1.00 32.54  ? 553  HIS   B ND1 1 
ATOM   5398  C  CD2 . HIS   B  1 252 ? -19.390 20.546  -12.391  1.00 30.73  ? 553  HIS   B CD2 1 
ATOM   5399  C  CE1 . HIS   B  1 252 ? -18.500 22.309  -13.349  1.00 31.43  ? 553  HIS   B CE1 1 
ATOM   5400  N  NE2 . HIS   B  1 252 ? -18.704 21.011  -13.490  1.00 27.88  ? 553  HIS   B NE2 1 
ATOM   5401  N  N   . PRO   B  1 253 ? -17.377 23.183  -9.464   1.00 34.89  ? 554  PRO   B N   1 
ATOM   5402  C  CA  . PRO   B  1 253 ? -16.612 24.436  -9.403   1.00 39.09  ? 554  PRO   B CA  1 
ATOM   5403  C  C   . PRO   B  1 253 ? -17.137 25.518  -10.337  1.00 38.85  ? 554  PRO   B C   1 
ATOM   5404  O  O   . PRO   B  1 253 ? -16.889 26.700  -10.083  1.00 40.68  ? 554  PRO   B O   1 
ATOM   5405  C  CB  . PRO   B  1 253 ? -15.195 23.996  -9.794   1.00 36.97  ? 554  PRO   B CB  1 
ATOM   5406  C  CG  . PRO   B  1 253 ? -15.410 22.774  -10.647  1.00 37.74  ? 554  PRO   B CG  1 
ATOM   5407  C  CD  . PRO   B  1 253 ? -16.598 22.077  -10.048  1.00 34.60  ? 554  PRO   B CD  1 
ATOM   5408  N  N   . LYS   B  1 254 ? -17.863 25.166  -11.394  1.00 39.30  ? 555  LYS   B N   1 
ATOM   5409  C  CA  . LYS   B  1 254 ? -18.381 26.158  -12.327  1.00 46.13  ? 555  LYS   B CA  1 
ATOM   5410  C  C   . LYS   B  1 254 ? -19.896 26.281  -12.306  1.00 45.89  ? 555  LYS   B C   1 
ATOM   5411  O  O   . LYS   B  1 254 ? -20.422 27.385  -12.468  1.00 46.65  ? 555  LYS   B O   1 
ATOM   5412  C  CB  . LYS   B  1 254 ? -17.915 25.833  -13.755  1.00 60.09  ? 555  LYS   B CB  1 
ATOM   5413  C  CG  . LYS   B  1 254 ? -16.393 25.770  -13.929  1.00 67.63  ? 555  LYS   B CG  1 
ATOM   5414  C  CD  . LYS   B  1 254 ? -15.738 27.138  -13.774  1.00 77.34  ? 555  LYS   B CD  1 
ATOM   5415  C  CE  . LYS   B  1 254 ? -14.246 27.064  -14.076  1.00 81.15  ? 555  LYS   B CE  1 
ATOM   5416  N  NZ  . LYS   B  1 254 ? -13.936 25.957  -15.034  1.00 78.09  ? 555  LYS   B NZ  1 
ATOM   5417  N  N   . PHE   B  1 255 ? -20.617 25.184  -12.100  1.00 39.67  ? 556  PHE   B N   1 
ATOM   5418  C  CA  . PHE   B  1 255 ? -22.078 25.187  -12.160  1.00 39.53  ? 556  PHE   B CA  1 
ATOM   5419  C  C   . PHE   B  1 255 ? -22.621 25.356  -10.748  1.00 40.37  ? 556  PHE   B C   1 
ATOM   5420  O  O   . PHE   B  1 255 ? -22.608 24.416  -9.947   1.00 33.51  ? 556  PHE   B O   1 
ATOM   5421  C  CB  . PHE   B  1 255 ? -22.589 23.902  -12.802  1.00 41.77  ? 556  PHE   B CB  1 
ATOM   5422  C  CG  . PHE   B  1 255 ? -22.154 23.732  -14.220  1.00 43.77  ? 556  PHE   B CG  1 
ATOM   5423  C  CD1 . PHE   B  1 255 ? -21.981 22.471  -14.761  1.00 44.49  ? 556  PHE   B CD1 1 
ATOM   5424  C  CD2 . PHE   B  1 255 ? -21.909 24.841  -15.016  1.00 45.32  ? 556  PHE   B CD2 1 
ATOM   5425  C  CE1 . PHE   B  1 255 ? -21.576 22.320  -16.085  1.00 38.83  ? 556  PHE   B CE1 1 
ATOM   5426  C  CE2 . PHE   B  1 255 ? -21.498 24.692  -16.333  1.00 45.37  ? 556  PHE   B CE2 1 
ATOM   5427  C  CZ  . PHE   B  1 255 ? -21.333 23.432  -16.862  1.00 42.10  ? 556  PHE   B CZ  1 
ATOM   5428  N  N   . GLU   B  1 256 ? -23.107 26.562  -10.443  1.00 41.18  ? 557  GLU   B N   1 
ATOM   5429  C  CA  . GLU   B  1 256 ? -23.600 26.833  -9.097   1.00 41.32  ? 557  GLU   B CA  1 
ATOM   5430  C  C   . GLU   B  1 256 ? -24.816 25.982  -8.780   1.00 41.35  ? 557  GLU   B C   1 
ATOM   5431  O  O   . GLU   B  1 256 ? -25.073 25.674  -7.613   1.00 41.24  ? 557  GLU   B O   1 
ATOM   5432  C  CB  . GLU   B  1 256 ? -23.932 28.317  -8.940   1.00 44.63  ? 557  GLU   B CB  1 
ATOM   5433  C  CG  . GLU   B  1 256 ? -25.214 28.779  -9.650   1.00 61.02  ? 557  GLU   B CG  1 
ATOM   5434  C  CD  . GLU   B  1 256 ? -25.134 28.797  -11.191  1.00 71.52  ? 557  GLU   B CD  1 
ATOM   5435  O  OE1 . GLU   B  1 256 ? -24.028 28.656  -11.765  1.00 71.12  ? 557  GLU   B OE1 1 
ATOM   5436  O  OE2 . GLU   B  1 256 ? -26.199 28.964  -11.832  1.00 72.06  ? 557  GLU   B OE2 1 
ATOM   5437  N  N   . TRP   B  1 257 ? -25.556 25.566  -9.802   1.00 39.19  ? 558  TRP   B N   1 
ATOM   5438  C  CA  . TRP   B  1 257 ? -26.769 24.800  -9.568   1.00 41.46  ? 558  TRP   B CA  1 
ATOM   5439  C  C   . TRP   B  1 257 ? -26.499 23.351  -9.199   1.00 36.80  ? 558  TRP   B C   1 
ATOM   5440  O  O   . TRP   B  1 257 ? -27.433 22.654  -8.788   1.00 38.31  ? 558  TRP   B O   1 
ATOM   5441  C  CB  . TRP   B  1 257 ? -27.663 24.848  -10.804  1.00 40.79  ? 558  TRP   B CB  1 
ATOM   5442  C  CG  . TRP   B  1 257 ? -26.936 24.516  -12.068  1.00 38.65  ? 558  TRP   B CG  1 
ATOM   5443  C  CD1 . TRP   B  1 257 ? -26.463 25.401  -12.995  1.00 41.34  ? 558  TRP   B CD1 1 
ATOM   5444  C  CD2 . TRP   B  1 257 ? -26.603 23.215  -12.551  1.00 41.98  ? 558  TRP   B CD2 1 
ATOM   5445  N  NE1 . TRP   B  1 257 ? -25.855 24.730  -14.026  1.00 42.06  ? 558  TRP   B NE1 1 
ATOM   5446  C  CE2 . TRP   B  1 257 ? -25.931 23.385  -13.782  1.00 42.36  ? 558  TRP   B CE2 1 
ATOM   5447  C  CE3 . TRP   B  1 257 ? -26.813 21.918  -12.071  1.00 45.53  ? 558  TRP   B CE3 1 
ATOM   5448  C  CZ2 . TRP   B  1 257 ? -25.463 22.310  -14.532  1.00 42.73  ? 558  TRP   B CZ2 1 
ATOM   5449  C  CZ3 . TRP   B  1 257 ? -26.347 20.849  -12.821  1.00 49.80  ? 558  TRP   B CZ3 1 
ATOM   5450  C  CH2 . TRP   B  1 257 ? -25.683 21.054  -14.041  1.00 42.39  ? 558  TRP   B CH2 1 
ATOM   5451  N  N   . PHE   B  1 258 ? -25.262 22.873  -9.344   1.00 34.88  ? 559  PHE   B N   1 
ATOM   5452  C  CA  . PHE   B  1 258 ? -25.006 21.453  -9.115   1.00 33.41  ? 559  PHE   B CA  1 
ATOM   5453  C  C   . PHE   B  1 258 ? -25.335 21.066  -7.686   1.00 37.00  ? 559  PHE   B C   1 
ATOM   5454  O  O   . PHE   B  1 258 ? -25.892 19.989  -7.434   1.00 33.24  ? 559  PHE   B O   1 
ATOM   5455  C  CB  . PHE   B  1 258 ? -23.556 21.120  -9.438   1.00 29.87  ? 559  PHE   B CB  1 
ATOM   5456  C  CG  . PHE   B  1 258 ? -23.325 19.675  -9.749   1.00 33.57  ? 559  PHE   B CG  1 
ATOM   5457  C  CD1 . PHE   B  1 258 ? -23.264 19.238  -11.070  1.00 28.23  ? 559  PHE   B CD1 1 
ATOM   5458  C  CD2 . PHE   B  1 258 ? -23.169 18.749  -8.726   1.00 30.98  ? 559  PHE   B CD2 1 
ATOM   5459  C  CE1 . PHE   B  1 258 ? -23.041 17.901  -11.362  1.00 31.73  ? 559  PHE   B CE1 1 
ATOM   5460  C  CE2 . PHE   B  1 258 ? -22.959 17.413  -9.004   1.00 33.89  ? 559  PHE   B CE2 1 
ATOM   5461  C  CZ  . PHE   B  1 258 ? -22.896 16.981  -10.320  1.00 36.73  ? 559  PHE   B CZ  1 
ATOM   5462  N  N   . LYS   B  1 259 ? -25.021 21.947  -6.735   1.00 35.09  ? 560  LYS   B N   1 
ATOM   5463  C  CA  . LYS   B  1 259 ? -25.332 21.662  -5.343   1.00 39.01  ? 560  LYS   B CA  1 
ATOM   5464  C  C   . LYS   B  1 259 ? -26.831 21.498  -5.127   1.00 39.29  ? 560  LYS   B C   1 
ATOM   5465  O  O   . LYS   B  1 259 ? -27.245 20.789  -4.200   1.00 38.78  ? 560  LYS   B O   1 
ATOM   5466  C  CB  . LYS   B  1 259 ? -24.764 22.759  -4.437   1.00 40.17  ? 560  LYS   B CB  1 
ATOM   5467  C  CG  . LYS   B  1 259 ? -25.278 24.168  -4.696   1.00 43.88  ? 560  LYS   B CG  1 
ATOM   5468  C  CD  . LYS   B  1 259 ? -24.854 25.114  -3.546   1.00 45.82  ? 560  LYS   B CD  1 
ATOM   5469  C  CE  . LYS   B  1 259 ? -25.345 26.531  -3.780   1.00 47.59  ? 560  LYS   B CE  1 
ATOM   5470  N  NZ  . LYS   B  1 259 ? -24.884 27.053  -5.103   1.00 50.18  ? 560  LYS   B NZ  1 
ATOM   5471  N  N   . ASP   B  1 260 ? -27.652 22.117  -5.978   1.00 38.02  ? 561  ASP   B N   1 
ATOM   5472  C  CA  . ASP   B  1 260 ? -29.101 21.965  -5.874   1.00 48.09  ? 561  ASP   B CA  1 
ATOM   5473  C  C   . ASP   B  1 260 ? -29.565 20.550  -6.200   1.00 45.41  ? 561  ASP   B C   1 
ATOM   5474  O  O   . ASP   B  1 260 ? -30.692 20.189  -5.848   1.00 49.47  ? 561  ASP   B O   1 
ATOM   5475  C  CB  . ASP   B  1 260 ? -29.817 22.951  -6.803   1.00 61.23  ? 561  ASP   B CB  1 
ATOM   5476  C  CG  . ASP   B  1 260 ? -29.464 24.399  -6.514   1.00 69.46  ? 561  ASP   B CG  1 
ATOM   5477  O  OD1 . ASP   B  1 260 ? -28.828 24.675  -5.471   1.00 67.89  ? 561  ASP   B OD1 1 
ATOM   5478  O  OD2 . ASP   B  1 260 ? -29.825 25.264  -7.341   1.00 72.14  ? 561  ASP   B OD2 1 
ATOM   5479  N  N   . LEU   B  1 261 ? -28.742 19.750  -6.882   1.00 36.66  ? 562  LEU   B N   1 
ATOM   5480  C  CA  . LEU   B  1 261 ? -29.094 18.350  -7.084   1.00 39.23  ? 562  LEU   B CA  1 
ATOM   5481  C  C   . LEU   B  1 261 ? -29.183 17.588  -5.768   1.00 37.98  ? 562  LEU   B C   1 
ATOM   5482  O  O   . LEU   B  1 261 ? -29.766 16.498  -5.737   1.00 38.98  ? 562  LEU   B O   1 
ATOM   5483  C  CB  . LEU   B  1 261 ? -28.078 17.672  -8.006   1.00 33.26  ? 562  LEU   B CB  1 
ATOM   5484  C  CG  . LEU   B  1 261 ? -27.958 18.298  -9.397   1.00 35.86  ? 562  LEU   B CG  1 
ATOM   5485  C  CD1 . LEU   B  1 261 ? -26.772 17.736  -10.141  1.00 29.15  ? 562  LEU   B CD1 1 
ATOM   5486  C  CD2 . LEU   B  1 261 ? -29.228 18.075  -10.185  1.00 40.14  ? 562  LEU   B CD2 1 
ATOM   5487  N  N   . GLY   B  1 262 ? -28.617 18.131  -4.691   1.00 33.72  ? 563  GLY   B N   1 
ATOM   5488  C  CA  . GLY   B  1 262 ? -28.683 17.491  -3.391   1.00 34.69  ? 563  GLY   B CA  1 
ATOM   5489  C  C   . GLY   B  1 262 ? -27.862 16.228  -3.276   1.00 39.78  ? 563  GLY   B C   1 
ATOM   5490  O  O   . GLY   B  1 262 ? -28.205 15.338  -2.493   1.00 38.72  ? 563  GLY   B O   1 
ATOM   5491  N  N   . LEU   B  1 263 ? -26.786 16.118  -4.035   1.00 25.89  ? 564  LEU   B N   1 
ATOM   5492  C  CA  . LEU   B  1 263 ? -26.023 14.892  -4.033   1.00 28.04  ? 564  LEU   B CA  1 
ATOM   5493  C  C   . LEU   B  1 263 ? -24.961 14.927  -2.951   1.00 27.78  ? 564  LEU   B C   1 
ATOM   5494  O  O   . LEU   B  1 263 ? -24.356 15.964  -2.666   1.00 27.72  ? 564  LEU   B O   1 
ATOM   5495  C  CB  . LEU   B  1 263 ? -25.367 14.656  -5.391   1.00 31.76  ? 564  LEU   B CB  1 
ATOM   5496  C  CG  . LEU   B  1 263 ? -26.368 14.578  -6.539   1.00 40.82  ? 564  LEU   B CG  1 
ATOM   5497  C  CD1 . LEU   B  1 263 ? -25.627 14.598  -7.849   1.00 33.77  ? 564  LEU   B CD1 1 
ATOM   5498  C  CD2 . LEU   B  1 263 ? -27.236 13.329  -6.417   1.00 38.00  ? 564  LEU   B CD2 1 
ATOM   5499  N  N   . LYS   B  1 264 ? -24.717 13.767  -2.371   1.00 30.20  ? 565  LYS   B N   1 
ATOM   5500  C  CA  . LYS   B  1 264 ? -23.565 13.585  -1.514   1.00 35.03  ? 565  LYS   B CA  1 
ATOM   5501  C  C   . LYS   B  1 264 ? -23.075 12.163  -1.721   1.00 32.25  ? 565  LYS   B C   1 
ATOM   5502  O  O   . LYS   B  1 264 ? -23.738 11.345  -2.365   1.00 32.58  ? 565  LYS   B O   1 
ATOM   5503  C  CB  . LYS   B  1 264 ? -23.913 13.876  -0.047   1.00 31.34  ? 565  LYS   B CB  1 
ATOM   5504  C  CG  . LYS   B  1 264 ? -25.028 13.008  0.513    1.00 29.53  ? 565  LYS   B CG  1 
ATOM   5505  C  CD  . LYS   B  1 264 ? -25.098 13.142  2.043    1.00 33.91  ? 565  LYS   B CD  1 
ATOM   5506  C  CE  . LYS   B  1 264 ? -26.525 13.236  2.524    1.00 45.71  ? 565  LYS   B CE  1 
ATOM   5507  N  NZ  . LYS   B  1 264 ? -26.595 13.149  4.015    1.00 51.16  ? 565  LYS   B NZ  1 
ATOM   5508  N  N   . TRP   B  1 265 ? -21.890 11.881  -1.193   1.00 23.73  ? 566  TRP   B N   1 
ATOM   5509  C  CA  . TRP   B  1 265 ? -21.393 10.516  -1.113   1.00 27.86  ? 566  TRP   B CA  1 
ATOM   5510  C  C   . TRP   B  1 265 ? -20.580 10.384  0.165    1.00 32.09  ? 566  TRP   B C   1 
ATOM   5511  O  O   . TRP   B  1 265 ? -20.240 11.377  0.811    1.00 32.71  ? 566  TRP   B O   1 
ATOM   5512  C  CB  . TRP   B  1 265 ? -20.552 10.124  -2.340   1.00 20.70  ? 566  TRP   B CB  1 
ATOM   5513  C  CG  . TRP   B  1 265 ? -20.566 8.659   -2.575   1.00 21.42  ? 566  TRP   B CG  1 
ATOM   5514  C  CD1 . TRP   B  1 265 ? -19.535 7.767   -2.390   1.00 22.62  ? 566  TRP   B CD1 1 
ATOM   5515  C  CD2 . TRP   B  1 265 ? -21.691 7.888   -3.000   1.00 20.17  ? 566  TRP   B CD2 1 
ATOM   5516  N  NE1 . TRP   B  1 265 ? -19.953 6.490   -2.704   1.00 19.40  ? 566  TRP   B NE1 1 
ATOM   5517  C  CE2 . TRP   B  1 265 ? -21.274 6.540   -3.077   1.00 19.62  ? 566  TRP   B CE2 1 
ATOM   5518  C  CE3 . TRP   B  1 265 ? -23.011 8.209   -3.327   1.00 22.13  ? 566  TRP   B CE3 1 
ATOM   5519  C  CZ2 . TRP   B  1 265 ? -22.132 5.519   -3.462   1.00 20.86  ? 566  TRP   B CZ2 1 
ATOM   5520  C  CZ3 . TRP   B  1 265 ? -23.854 7.200   -3.723   1.00 25.18  ? 566  TRP   B CZ3 1 
ATOM   5521  C  CH2 . TRP   B  1 265 ? -23.414 5.867   -3.784   1.00 23.56  ? 566  TRP   B CH2 1 
ATOM   5522  N  N   . TYR   B  1 266 ? -20.290 9.148   0.542    1.00 27.98  ? 567  TYR   B N   1 
ATOM   5523  C  CA  . TYR   B  1 266 ? -19.441 8.913   1.695    1.00 26.57  ? 567  TYR   B CA  1 
ATOM   5524  C  C   . TYR   B  1 266 ? -17.987 8.831   1.258    1.00 30.02  ? 567  TYR   B C   1 
ATOM   5525  O  O   . TYR   B  1 266 ? -17.675 8.508   0.110    1.00 27.02  ? 567  TYR   B O   1 
ATOM   5526  C  CB  . TYR   B  1 266 ? -19.845 7.634   2.409    1.00 21.65  ? 567  TYR   B CB  1 
ATOM   5527  C  CG  . TYR   B  1 266 ? -20.075 6.468   1.483    1.00 25.42  ? 567  TYR   B CG  1 
ATOM   5528  C  CD1 . TYR   B  1 266 ? -19.036 5.618   1.131    1.00 25.10  ? 567  TYR   B CD1 1 
ATOM   5529  C  CD2 . TYR   B  1 266 ? -21.337 6.207   0.966    1.00 24.03  ? 567  TYR   B CD2 1 
ATOM   5530  C  CE1 . TYR   B  1 266 ? -19.245 4.545   0.288    1.00 20.18  ? 567  TYR   B CE1 1 
ATOM   5531  C  CE2 . TYR   B  1 266 ? -21.557 5.133   0.112    1.00 23.39  ? 567  TYR   B CE2 1 
ATOM   5532  C  CZ  . TYR   B  1 266 ? -20.509 4.304   -0.211   1.00 25.09  ? 567  TYR   B CZ  1 
ATOM   5533  O  OH  . TYR   B  1 266 ? -20.725 3.235   -1.046   1.00 24.83  ? 567  TYR   B OH  1 
ATOM   5534  N  N   . GLY   B  1 267 ? -17.088 9.132   2.190    1.00 22.65  ? 568  GLY   B N   1 
ATOM   5535  C  CA  . GLY   B  1 267 ? -15.684 9.162   1.836    1.00 23.83  ? 568  GLY   B CA  1 
ATOM   5536  C  C   . GLY   B  1 267 ? -15.020 7.807   1.841    1.00 21.53  ? 568  GLY   B C   1 
ATOM   5537  O  O   . GLY   B  1 267 ? -14.011 7.612   1.155    1.00 28.39  ? 568  GLY   B O   1 
ATOM   5538  N  N   . LEU   B  1 268 ? -15.568 6.850   2.584    1.00 22.35  ? 569  LEU   B N   1 
ATOM   5539  C  CA  . LEU   B  1 268 ? -14.840 5.621   2.886    1.00 26.16  ? 569  LEU   B CA  1 
ATOM   5540  C  C   . LEU   B  1 268 ? -15.372 4.447   2.074    1.00 24.12  ? 569  LEU   B C   1 
ATOM   5541  O  O   . LEU   B  1 268 ? -16.447 3.912   2.398    1.00 27.42  ? 569  LEU   B O   1 
ATOM   5542  C  CB  . LEU   B  1 268 ? -14.931 5.312   4.383    1.00 29.24  ? 569  LEU   B CB  1 
ATOM   5543  C  CG  . LEU   B  1 268 ? -14.050 4.150   4.824    1.00 22.15  ? 569  LEU   B CG  1 
ATOM   5544  C  CD1 . LEU   B  1 268 ? -12.564 4.497   4.656    1.00 26.58  ? 569  LEU   B CD1 1 
ATOM   5545  C  CD2 . LEU   B  1 268 ? -14.365 3.737   6.271    1.00 22.00  ? 569  LEU   B CD2 1 
ATOM   5546  N  N   . PRO   B  1 269 ? -14.673 4.000   1.026    1.00 23.27  ? 570  PRO   B N   1 
ATOM   5547  C  CA  . PRO   B  1 269 ? -15.084 2.766   0.336    1.00 19.17  ? 570  PRO   B CA  1 
ATOM   5548  C  C   . PRO   B  1 269 ? -14.527 1.560   1.080    1.00 21.93  ? 570  PRO   B C   1 
ATOM   5549  O  O   . PRO   B  1 269 ? -13.311 1.381   1.185    1.00 26.12  ? 570  PRO   B O   1 
ATOM   5550  C  CB  . PRO   B  1 269 ? -14.455 2.913   -1.058   1.00 17.53  ? 570  PRO   B CB  1 
ATOM   5551  C  CG  . PRO   B  1 269 ? -13.169 3.697   -0.785   1.00 17.66  ? 570  PRO   B CG  1 
ATOM   5552  C  CD  . PRO   B  1 269 ? -13.491 4.632   0.398    1.00 21.98  ? 570  PRO   B CD  1 
ATOM   5553  N  N   . ALA   B  1 270 ? -15.422 0.730   1.602    1.00 22.15  ? 571  ALA   B N   1 
ATOM   5554  C  CA  . ALA   B  1 270 ? -15.050 -0.317  2.552    1.00 20.71  ? 571  ALA   B CA  1 
ATOM   5555  C  C   . ALA   B  1 270 ? -15.816 -1.581  2.184    1.00 29.99  ? 571  ALA   B C   1 
ATOM   5556  O  O   . ALA   B  1 270 ? -16.973 -1.724  2.573    1.00 25.09  ? 571  ALA   B O   1 
ATOM   5557  C  CB  . ALA   B  1 270 ? -15.354 0.125   3.980    1.00 20.21  ? 571  ALA   B CB  1 
ATOM   5558  N  N   . VAL   B  1 271 ? -15.174 -2.478  1.437    1.00 24.92  ? 572  VAL   B N   1 
ATOM   5559  C  CA  . VAL   B  1 271 ? -15.823 -3.688  0.944    1.00 20.67  ? 572  VAL   B CA  1 
ATOM   5560  C  C   . VAL   B  1 271 ? -15.837 -4.728  2.049    1.00 17.13  ? 572  VAL   B C   1 
ATOM   5561  O  O   . VAL   B  1 271 ? -14.800 -5.049  2.631    1.00 20.92  ? 572  VAL   B O   1 
ATOM   5562  C  CB  . VAL   B  1 271 ? -15.099 -4.234  -0.297   1.00 22.11  ? 572  VAL   B CB  1 
ATOM   5563  C  CG1 . VAL   B  1 271 ? -15.534 -5.680  -0.569   1.00 22.50  ? 572  VAL   B CG1 1 
ATOM   5564  C  CG2 . VAL   B  1 271 ? -15.329 -3.321  -1.542   1.00 18.85  ? 572  VAL   B CG2 1 
ATOM   5565  N  N   . SER   B  1 272 ? -16.997 -5.313  2.293    1.00 19.99  ? 573  SER   B N   1 
ATOM   5566  C  CA  . SER   B  1 272 ? -17.158 -6.178  3.445    1.00 25.52  ? 573  SER   B CA  1 
ATOM   5567  C  C   . SER   B  1 272 ? -17.788 -7.525  3.111    1.00 23.90  ? 573  SER   B C   1 
ATOM   5568  O  O   . SER   B  1 272 ? -18.024 -8.316  4.028    1.00 24.31  ? 573  SER   B O   1 
ATOM   5569  C  CB  . SER   B  1 272 ? -17.979 -5.449  4.524    1.00 23.61  ? 573  SER   B CB  1 
ATOM   5570  O  OG  . SER   B  1 272 ? -19.205 -4.945  3.991    1.00 21.42  ? 573  SER   B OG  1 
ATOM   5571  N  N   . ASN   B  1 273 ? -18.021 -7.849  1.835    1.00 22.41  ? 574  ASN   B N   1 
ATOM   5572  C  CA  . ASN   B  1 273 ? -18.687 -9.109  1.515    1.00 17.98  ? 574  ASN   B CA  1 
ATOM   5573  C  C   . ASN   B  1 273 ? -17.771 -10.099 0.825    1.00 22.80  ? 574  ASN   B C   1 
ATOM   5574  O  O   . ASN   B  1 273 ? -18.249 -11.101 0.300    1.00 26.12  ? 574  ASN   B O   1 
ATOM   5575  C  CB  . ASN   B  1 273 ? -19.934 -8.877  0.660    1.00 22.57  ? 574  ASN   B CB  1 
ATOM   5576  C  CG  . ASN   B  1 273 ? -19.624 -8.230  -0.674   1.00 28.45  ? 574  ASN   B CG  1 
ATOM   5577  O  OD1 . ASN   B  1 273 ? -18.488 -7.828  -0.953   1.00 24.42  ? 574  ASN   B OD1 1 
ATOM   5578  N  ND2 . ASN   B  1 273 ? -20.650 -8.088  -1.493   1.00 25.59  ? 574  ASN   B ND2 1 
ATOM   5579  N  N   . MET   B  1 274 ? -16.475 -9.852  0.821    1.00 20.04  ? 575  MET   B N   1 
ATOM   5580  C  CA  . MET   B  1 274 ? -15.545 -10.749 0.168    1.00 19.03  ? 575  MET   B CA  1 
ATOM   5581  C  C   . MET   B  1 274 ? -14.949 -11.713 1.168    1.00 28.22  ? 575  MET   B C   1 
ATOM   5582  O  O   . MET   B  1 274 ? -15.124 -11.587 2.382    1.00 28.98  ? 575  MET   B O   1 
ATOM   5583  C  CB  . MET   B  1 274 ? -14.451 -9.958  -0.547   1.00 17.38  ? 575  MET   B CB  1 
ATOM   5584  C  CG  . MET   B  1 274 ? -15.001 -9.323  -1.837   1.00 21.93  ? 575  MET   B CG  1 
ATOM   5585  S  SD  . MET   B  1 274 ? -13.722 -8.519  -2.791   1.00 26.67  ? 575  MET   B SD  1 
ATOM   5586  C  CE  . MET   B  1 274 ? -13.171 -9.874  -3.816   1.00 21.64  ? 575  MET   B CE  1 
ATOM   5587  N  N   . LEU   B  1 275 ? -14.253 -12.707 0.636    1.00 25.41  ? 576  LEU   B N   1 
ATOM   5588  C  CA  . LEU   B  1 275 ? -13.628 -13.730 1.448    1.00 19.80  ? 576  LEU   B CA  1 
ATOM   5589  C  C   . LEU   B  1 275 ? -12.133 -13.650 1.231    1.00 26.39  ? 576  LEU   B C   1 
ATOM   5590  O  O   . LEU   B  1 275 ? -11.663 -13.602 0.089    1.00 25.66  ? 576  LEU   B O   1 
ATOM   5591  C  CB  . LEU   B  1 275 ? -14.154 -15.119 1.099    1.00 25.47  ? 576  LEU   B CB  1 
ATOM   5592  C  CG  . LEU   B  1 275 ? -13.652 -16.259 1.989    1.00 30.72  ? 576  LEU   B CG  1 
ATOM   5593  C  CD1 . LEU   B  1 275 ? -14.786 -17.233 2.287    1.00 30.22  ? 576  LEU   B CD1 1 
ATOM   5594  C  CD2 . LEU   B  1 275 ? -12.533 -16.978 1.293    1.00 27.93  ? 576  LEU   B CD2 1 
ATOM   5595  N  N   . LEU   B  1 276 ? -11.405 -13.619 2.330    1.00 19.09  ? 577  LEU   B N   1 
ATOM   5596  C  CA  . LEU   B  1 276 ? -9.955  -13.550 2.345    1.00 20.67  ? 577  LEU   B CA  1 
ATOM   5597  C  C   . LEU   B  1 276 ? -9.432  -14.963 2.563    1.00 25.91  ? 577  LEU   B C   1 
ATOM   5598  O  O   . LEU   B  1 276 ? -9.696  -15.573 3.605    1.00 22.57  ? 577  LEU   B O   1 
ATOM   5599  C  CB  . LEU   B  1 276 ? -9.489  -12.618 3.470    1.00 23.29  ? 577  LEU   B CB  1 
ATOM   5600  C  CG  . LEU   B  1 276 ? -8.012  -12.675 3.820    1.00 24.16  ? 577  LEU   B CG  1 
ATOM   5601  C  CD1 . LEU   B  1 276 ? -7.164  -12.374 2.578    1.00 21.59  ? 577  LEU   B CD1 1 
ATOM   5602  C  CD2 . LEU   B  1 276 ? -7.720  -11.697 4.937    1.00 22.11  ? 577  LEU   B CD2 1 
ATOM   5603  N  N   . GLU   B  1 277 ? -8.699  -15.481 1.593    1.00 26.62  ? 578  GLU   B N   1 
ATOM   5604  C  CA  . GLU   B  1 277 ? -8.148  -16.821 1.681    1.00 25.15  ? 578  GLU   B CA  1 
ATOM   5605  C  C   . GLU   B  1 277 ? -6.651  -16.696 1.889    1.00 25.43  ? 578  GLU   B C   1 
ATOM   5606  O  O   . GLU   B  1 277 ? -5.966  -16.067 1.078    1.00 27.37  ? 578  GLU   B O   1 
ATOM   5607  C  CB  . GLU   B  1 277 ? -8.460  -17.634 0.425    1.00 31.65  ? 578  GLU   B CB  1 
ATOM   5608  C  CG  . GLU   B  1 277 ? -8.138  -19.095 0.589    1.00 51.52  ? 578  GLU   B CG  1 
ATOM   5609  C  CD  . GLU   B  1 277 ? -7.019  -19.541 -0.317   1.00 71.25  ? 578  GLU   B CD  1 
ATOM   5610  O  OE1 . GLU   B  1 277 ? -7.282  -19.767 -1.520   1.00 81.11  ? 578  GLU   B OE1 1 
ATOM   5611  O  OE2 . GLU   B  1 277 ? -5.875  -19.658 0.171    1.00 73.29  ? 578  GLU   B OE2 1 
ATOM   5612  N  N   . ILE   B  1 278 ? -6.152  -17.283 2.978    1.00 23.29  ? 579  ILE   B N   1 
ATOM   5613  C  CA  . ILE   B  1 278 ? -4.727  -17.294 3.298    1.00 26.19  ? 579  ILE   B CA  1 
ATOM   5614  C  C   . ILE   B  1 278 ? -4.344  -18.709 3.704    1.00 32.53  ? 579  ILE   B C   1 
ATOM   5615  O  O   . ILE   B  1 278 ? -4.827  -19.216 4.729    1.00 30.90  ? 579  ILE   B O   1 
ATOM   5616  C  CB  . ILE   B  1 278 ? -4.371  -16.322 4.435    1.00 26.48  ? 579  ILE   B CB  1 
ATOM   5617  C  CG1 . ILE   B  1 278 ? -4.817  -14.894 4.122    1.00 22.10  ? 579  ILE   B CG1 1 
ATOM   5618  C  CG2 . ILE   B  1 278 ? -2.882  -16.381 4.722    1.00 21.43  ? 579  ILE   B CG2 1 
ATOM   5619  C  CD1 . ILE   B  1 278 ? -4.668  -13.945 5.336    1.00 22.66  ? 579  ILE   B CD1 1 
ATOM   5620  N  N   . GLY   B  1 279 ? -3.459  -19.327 2.928    1.00 24.63  ? 580  GLY   B N   1 
ATOM   5621  C  CA  . GLY   B  1 279 ? -2.962  -20.654 3.255    1.00 25.65  ? 580  GLY   B CA  1 
ATOM   5622  C  C   . GLY   B  1 279 ? -4.059  -21.675 3.441    1.00 35.17  ? 580  GLY   B C   1 
ATOM   5623  O  O   . GLY   B  1 279 ? -3.957  -22.543 4.319    1.00 36.50  ? 580  GLY   B O   1 
ATOM   5624  N  N   . GLY   B  1 280 ? -5.119  -21.582 2.640    1.00 27.12  ? 581  GLY   B N   1 
ATOM   5625  C  CA  . GLY   B  1 280 ? -6.257  -22.458 2.769    1.00 26.80  ? 581  GLY   B CA  1 
ATOM   5626  C  C   . GLY   B  1 280 ? -7.237  -22.060 3.845    1.00 27.05  ? 581  GLY   B C   1 
ATOM   5627  O  O   . GLY   B  1 280 ? -8.312  -22.661 3.931    1.00 29.65  ? 581  GLY   B O   1 
ATOM   5628  N  N   . LEU   B  1 281 ? -6.909  -21.076 4.674    1.00 23.91  ? 582  LEU   B N   1 
ATOM   5629  C  CA  . LEU   B  1 281 ? -7.852  -20.591 5.661    1.00 27.71  ? 582  LEU   B CA  1 
ATOM   5630  C  C   . LEU   B  1 281 ? -8.775  -19.577 5.017    1.00 27.93  ? 582  LEU   B C   1 
ATOM   5631  O  O   . LEU   B  1 281 ? -8.353  -18.775 4.180    1.00 27.45  ? 582  LEU   B O   1 
ATOM   5632  C  CB  . LEU   B  1 281 ? -7.125  -19.962 6.851    1.00 25.34  ? 582  LEU   B CB  1 
ATOM   5633  C  CG  . LEU   B  1 281 ? -6.180  -20.882 7.610    1.00 26.81  ? 582  LEU   B CG  1 
ATOM   5634  C  CD1 . LEU   B  1 281 ? -5.527  -20.138 8.787    1.00 32.56  ? 582  LEU   B CD1 1 
ATOM   5635  C  CD2 . LEU   B  1 281 ? -6.913  -22.143 8.075    1.00 24.84  ? 582  LEU   B CD2 1 
ATOM   5636  N  N   . GLU   B  1 282 ? -10.039 -19.609 5.406    1.00 27.23  ? 583  GLU   B N   1 
ATOM   5637  C  CA  . GLU   B  1 282 ? -11.056 -18.756 4.802    1.00 24.69  ? 583  GLU   B CA  1 
ATOM   5638  C  C   . GLU   B  1 282 ? -11.555 -17.758 5.841    1.00 27.48  ? 583  GLU   B C   1 
ATOM   5639  O  O   . GLU   B  1 282 ? -12.195 -18.146 6.824    1.00 25.48  ? 583  GLU   B O   1 
ATOM   5640  C  CB  . GLU   B  1 282 ? -12.199 -19.597 4.247    1.00 29.91  ? 583  GLU   B CB  1 
ATOM   5641  C  CG  . GLU   B  1 282 ? -11.752 -20.602 3.181    1.00 35.90  ? 583  GLU   B CG  1 
ATOM   5642  C  CD  . GLU   B  1 282 ? -12.925 -21.345 2.580    1.00 42.38  ? 583  GLU   B CD  1 
ATOM   5643  O  OE1 . GLU   B  1 282 ? -13.029 -21.369 1.336    1.00 51.38  ? 583  GLU   B OE1 1 
ATOM   5644  O  OE2 . GLU   B  1 282 ? -13.748 -21.892 3.353    1.00 41.77  ? 583  GLU   B OE2 1 
ATOM   5645  N  N   . PHE   B  1 283 ? -11.272 -16.478 5.612    1.00 28.47  ? 584  PHE   B N   1 
ATOM   5646  C  CA  . PHE   B  1 283 ? -11.750 -15.389 6.461    1.00 22.49  ? 584  PHE   B CA  1 
ATOM   5647  C  C   . PHE   B  1 283 ? -12.967 -14.767 5.787    1.00 24.44  ? 584  PHE   B C   1 
ATOM   5648  O  O   . PHE   B  1 283 ? -12.862 -13.847 4.970    1.00 22.76  ? 584  PHE   B O   1 
ATOM   5649  C  CB  . PHE   B  1 283 ? -10.635 -14.386 6.704    1.00 22.36  ? 584  PHE   B CB  1 
ATOM   5650  C  CG  . PHE   B  1 283 ? -9.464  -14.988 7.414    1.00 29.20  ? 584  PHE   B CG  1 
ATOM   5651  C  CD1 . PHE   B  1 283 ? -8.405  -15.514 6.699    1.00 24.77  ? 584  PHE   B CD1 1 
ATOM   5652  C  CD2 . PHE   B  1 283 ? -9.460  -15.099 8.802    1.00 27.07  ? 584  PHE   B CD2 1 
ATOM   5653  C  CE1 . PHE   B  1 283 ? -7.340  -16.091 7.348    1.00 24.38  ? 584  PHE   B CE1 1 
ATOM   5654  C  CE2 . PHE   B  1 283 ? -8.397  -15.669 9.456    1.00 23.74  ? 584  PHE   B CE2 1 
ATOM   5655  C  CZ  . PHE   B  1 283 ? -7.334  -16.163 8.732    1.00 23.47  ? 584  PHE   B CZ  1 
ATOM   5656  N  N   . SER   B  1 284 ? -14.136 -15.288 6.143    1.00 23.62  ? 585  SER   B N   1 
ATOM   5657  C  CA  . SER   B  1 284 ? -15.375 -14.889 5.486    1.00 24.93  ? 585  SER   B CA  1 
ATOM   5658  C  C   . SER   B  1 284 ? -15.818 -13.480 5.872    1.00 24.37  ? 585  SER   B C   1 
ATOM   5659  O  O   . SER   B  1 284 ? -16.698 -12.919 5.218    1.00 22.37  ? 585  SER   B O   1 
ATOM   5660  C  CB  . SER   B  1 284 ? -16.472 -15.897 5.831    1.00 24.72  ? 585  SER   B CB  1 
ATOM   5661  O  OG  . SER   B  1 284 ? -16.492 -16.158 7.235    1.00 30.92  ? 585  SER   B OG  1 
ATOM   5662  N  N   . ALA   B  1 285 ? -15.262 -12.908 6.933    1.00 25.02  ? 586  ALA   B N   1 
ATOM   5663  C  CA  . ALA   B  1 285 ? -15.574 -11.536 7.313    1.00 24.78  ? 586  ALA   B CA  1 
ATOM   5664  C  C   . ALA   B  1 285 ? -14.255 -10.799 7.448    1.00 25.69  ? 586  ALA   B C   1 
ATOM   5665  O  O   . ALA   B  1 285 ? -13.489 -11.049 8.390    1.00 24.88  ? 586  ALA   B O   1 
ATOM   5666  C  CB  . ALA   B  1 285 ? -16.386 -11.477 8.599    1.00 23.73  ? 586  ALA   B CB  1 
ATOM   5667  N  N   . CYS   B  1 286 ? -13.987 -9.912  6.495    1.00 18.80  ? 587  CYS   B N   1 
ATOM   5668  C  CA  . CYS   B  1 286 ? -12.691 -9.262  6.403    1.00 20.43  ? 587  CYS   B CA  1 
ATOM   5669  C  C   . CYS   B  1 286 ? -12.819 -7.880  5.777    1.00 29.99  ? 587  CYS   B C   1 
ATOM   5670  O  O   . CYS   B  1 286 ? -12.106 -7.583  4.805    1.00 32.53  ? 587  CYS   B O   1 
ATOM   5671  C  CB  . CYS   B  1 286 ? -11.738 -10.116 5.574    1.00 21.41  ? 587  CYS   B CB  1 
ATOM   5672  S  SG  . CYS   B  1 286 ? -12.332 -10.403 3.825    1.00 25.53  ? 587  CYS   B SG  1 
ATOM   5673  N  N   . PRO   B  1 287 ? -13.682 -7.008  6.302    1.00 28.08  ? 588  PRO   B N   1 
ATOM   5674  C  CA  . PRO   B  1 287 ? -13.908 -5.718  5.641    1.00 21.76  ? 588  PRO   B CA  1 
ATOM   5675  C  C   . PRO   B  1 287 ? -12.602 -4.957  5.451    1.00 20.23  ? 588  PRO   B C   1 
ATOM   5676  O  O   . PRO   B  1 287 ? -11.748 -4.920  6.338    1.00 24.85  ? 588  PRO   B O   1 
ATOM   5677  C  CB  . PRO   B  1 287 ? -14.851 -4.989  6.604    1.00 23.79  ? 588  PRO   B CB  1 
ATOM   5678  C  CG  . PRO   B  1 287 ? -14.577 -5.620  7.934    1.00 28.26  ? 588  PRO   B CG  1 
ATOM   5679  C  CD  . PRO   B  1 287 ? -14.339 -7.064  7.623    1.00 26.40  ? 588  PRO   B CD  1 
ATOM   5680  N  N   . PHE   B  1 288 ? -12.431 -4.386  4.260    1.00 18.26  ? 589  PHE   B N   1 
ATOM   5681  C  CA  . PHE   B  1 288 ? -11.204 -3.674  3.929    1.00 18.57  ? 589  PHE   B CA  1 
ATOM   5682  C  C   . PHE   B  1 288 ? -11.570 -2.371  3.247    1.00 23.53  ? 589  PHE   B C   1 
ATOM   5683  O  O   . PHE   B  1 288 ? -12.623 -2.258  2.623    1.00 18.13  ? 589  PHE   B O   1 
ATOM   5684  C  CB  . PHE   B  1 288 ? -10.274 -4.511  3.040    1.00 19.79  ? 589  PHE   B CB  1 
ATOM   5685  C  CG  . PHE   B  1 288 ? -10.897 -4.982  1.724    1.00 26.31  ? 589  PHE   B CG  1 
ATOM   5686  C  CD1 . PHE   B  1 288 ? -10.925 -4.151  0.608    1.00 22.58  ? 589  PHE   B CD1 1 
ATOM   5687  C  CD2 . PHE   B  1 288 ? -11.410 -6.277  1.599    1.00 25.46  ? 589  PHE   B CD2 1 
ATOM   5688  C  CE1 . PHE   B  1 288 ? -11.474 -4.593  -0.612   1.00 22.83  ? 589  PHE   B CE1 1 
ATOM   5689  C  CE2 . PHE   B  1 288 ? -11.949 -6.728  0.379    1.00 28.98  ? 589  PHE   B CE2 1 
ATOM   5690  C  CZ  . PHE   B  1 288 ? -11.983 -5.886  -0.716   1.00 23.24  ? 589  PHE   B CZ  1 
ATOM   5691  N  N   . SER   B  1 289 ? -10.708 -1.375  3.387    1.00 23.07  ? 590  SER   B N   1 
ATOM   5692  C  CA  . SER   B  1 289 ? -11.086 -0.065  2.916    1.00 18.26  ? 590  SER   B CA  1 
ATOM   5693  C  C   . SER   B  1 289 ? -9.858  0.640   2.394    1.00 20.19  ? 590  SER   B C   1 
ATOM   5694  O  O   . SER   B  1 289 ? -8.743  0.369   2.832    1.00 21.38  ? 590  SER   B O   1 
ATOM   5695  C  CB  . SER   B  1 289 ? -11.746 0.755   4.027    1.00 18.90  ? 590  SER   B CB  1 
ATOM   5696  O  OG  . SER   B  1 289 ? -10.833 0.933   5.104    1.00 22.24  ? 590  SER   B OG  1 
ATOM   5697  N  N   . GLY   B  1 290 ? -10.072 1.521   1.422    1.00 23.38  ? 591  GLY   B N   1 
ATOM   5698  C  CA  . GLY   B  1 290 ? -9.000  2.372   0.952    1.00 20.06  ? 591  GLY   B CA  1 
ATOM   5699  C  C   . GLY   B  1 290 ? -9.503  3.790   0.811    1.00 26.64  ? 591  GLY   B C   1 
ATOM   5700  O  O   . GLY   B  1 290 ? -10.004 4.392   1.769    1.00 26.09  ? 591  GLY   B O   1 
ATOM   5701  N  N   . TRP   B  1 291 ? -9.383  4.335   -0.392   1.00 25.76  ? 592  TRP   B N   1 
ATOM   5702  C  CA  . TRP   B  1 291 ? -10.030 5.587   -0.728   1.00 21.72  ? 592  TRP   B CA  1 
ATOM   5703  C  C   . TRP   B  1 291 ? -10.524 5.496   -2.169   1.00 22.16  ? 592  TRP   B C   1 
ATOM   5704  O  O   . TRP   B  1 291 ? -10.135 4.610   -2.940   1.00 19.43  ? 592  TRP   B O   1 
ATOM   5705  C  CB  . TRP   B  1 291 ? -9.091  6.784   -0.525   1.00 20.02  ? 592  TRP   B CB  1 
ATOM   5706  C  CG  . TRP   B  1 291 ? -7.812  6.643   -1.229   1.00 28.23  ? 592  TRP   B CG  1 
ATOM   5707  C  CD1 . TRP   B  1 291 ? -7.591  6.843   -2.570   1.00 30.59  ? 592  TRP   B CD1 1 
ATOM   5708  C  CD2 . TRP   B  1 291 ? -6.554  6.265   -0.667   1.00 30.71  ? 592  TRP   B CD2 1 
ATOM   5709  N  NE1 . TRP   B  1 291 ? -6.276  6.619   -2.861   1.00 29.57  ? 592  TRP   B NE1 1 
ATOM   5710  C  CE2 . TRP   B  1 291 ? -5.614  6.265   -1.717   1.00 30.95  ? 592  TRP   B CE2 1 
ATOM   5711  C  CE3 . TRP   B  1 291 ? -6.123  5.941   0.625    1.00 36.47  ? 592  TRP   B CE3 1 
ATOM   5712  C  CZ2 . TRP   B  1 291 ? -4.269  5.946   -1.517   1.00 35.15  ? 592  TRP   B CZ2 1 
ATOM   5713  C  CZ3 . TRP   B  1 291 ? -4.789  5.623   0.825    1.00 33.74  ? 592  TRP   B CZ3 1 
ATOM   5714  C  CH2 . TRP   B  1 291 ? -3.878  5.628   -0.239   1.00 41.03  ? 592  TRP   B CH2 1 
ATOM   5715  N  N   . TYR   B  1 292 ? -11.401 6.423   -2.523   1.00 29.16  ? 593  TYR   B N   1 
ATOM   5716  C  CA  . TYR   B  1 292 ? -12.110 6.332   -3.787   1.00 27.45  ? 593  TYR   B CA  1 
ATOM   5717  C  C   . TYR   B  1 292 ? -11.268 6.810   -4.962   1.00 22.48  ? 593  TYR   B C   1 
ATOM   5718  O  O   . TYR   B  1 292 ? -10.492 7.762   -4.857   1.00 20.10  ? 593  TYR   B O   1 
ATOM   5719  C  CB  . TYR   B  1 292 ? -13.385 7.157   -3.728   1.00 20.13  ? 593  TYR   B CB  1 
ATOM   5720  C  CG  . TYR   B  1 292 ? -14.617 6.370   -3.372   1.00 23.76  ? 593  TYR   B CG  1 
ATOM   5721  C  CD1 . TYR   B  1 292 ? -15.366 6.679   -2.228   1.00 19.15  ? 593  TYR   B CD1 1 
ATOM   5722  C  CD2 . TYR   B  1 292 ? -15.043 5.332   -4.179   1.00 21.47  ? 593  TYR   B CD2 1 
ATOM   5723  C  CE1 . TYR   B  1 292 ? -16.511 5.971   -1.926   1.00 22.80  ? 593  TYR   B CE1 1 
ATOM   5724  C  CE2 . TYR   B  1 292 ? -16.178 4.625   -3.886   1.00 25.43  ? 593  TYR   B CE2 1 
ATOM   5725  C  CZ  . TYR   B  1 292 ? -16.910 4.946   -2.757   1.00 22.38  ? 593  TYR   B CZ  1 
ATOM   5726  O  OH  . TYR   B  1 292 ? -18.047 4.231   -2.479   1.00 24.05  ? 593  TYR   B OH  1 
ATOM   5727  N  N   . MET   B  1 293 ? -11.435 6.129   -6.086   1.00 20.16  ? 594  MET   B N   1 
ATOM   5728  C  CA  . MET   B  1 293 ? -11.190 6.725   -7.386   1.00 21.54  ? 594  MET   B CA  1 
ATOM   5729  C  C   . MET   B  1 293 ? -12.491 7.385   -7.823   1.00 22.57  ? 594  MET   B C   1 
ATOM   5730  O  O   . MET   B  1 293 ? -13.564 6.797   -7.680   1.00 23.48  ? 594  MET   B O   1 
ATOM   5731  C  CB  . MET   B  1 293 ? -10.734 5.667   -8.385   1.00 18.46  ? 594  MET   B CB  1 
ATOM   5732  C  CG  . MET   B  1 293 ? -10.328 6.254   -9.727   1.00 25.10  ? 594  MET   B CG  1 
ATOM   5733  S  SD  . MET   B  1 293 ? -9.485  5.031   -10.754  1.00 25.40  ? 594  MET   B SD  1 
ATOM   5734  C  CE  . MET   B  1 293 ? -10.858 4.027   -11.295  1.00 22.02  ? 594  MET   B CE  1 
ATOM   5735  N  N   . GLY   B  1 294 ? -12.407 8.624   -8.304   1.00 25.10  ? 595  GLY   B N   1 
ATOM   5736  C  CA  . GLY   B  1 294 ? -13.619 9.417   -8.503   1.00 26.35  ? 595  GLY   B CA  1 
ATOM   5737  C  C   . GLY   B  1 294 ? -14.646 8.795   -9.436   1.00 30.75  ? 595  GLY   B C   1 
ATOM   5738  O  O   . GLY   B  1 294 ? -15.858 8.980   -9.245   1.00 22.74  ? 595  GLY   B O   1 
ATOM   5739  N  N   . THR   B  1 295 ? -14.192 8.069   -10.465  1.00 27.27  ? 596  THR   B N   1 
ATOM   5740  C  CA  . THR   B  1 295 ? -15.142 7.483   -11.405  1.00 27.48  ? 596  THR   B CA  1 
ATOM   5741  C  C   . THR   B  1 295 ? -16.019 6.441   -10.735  1.00 22.04  ? 596  THR   B C   1 
ATOM   5742  O  O   . THR   B  1 295 ? -17.126 6.176   -11.216  1.00 23.16  ? 596  THR   B O   1 
ATOM   5743  C  CB  . THR   B  1 295 ? -14.428 6.832   -12.602  1.00 21.20  ? 596  THR   B CB  1 
ATOM   5744  O  OG1 . THR   B  1 295 ? -13.409 5.944   -12.125  1.00 21.48  ? 596  THR   B OG1 1 
ATOM   5745  C  CG2 . THR   B  1 295 ? -13.824 7.871   -13.533  1.00 23.39  ? 596  THR   B CG2 1 
ATOM   5746  N  N   . GLU   B  1 296 ? -15.553 5.832   -9.645   1.00 21.82  ? 597  GLU   B N   1 
ATOM   5747  C  CA  . GLU   B  1 296 ? -16.424 4.896   -8.951   1.00 21.75  ? 597  GLU   B CA  1 
ATOM   5748  C  C   . GLU   B  1 296 ? -17.723 5.580   -8.559   1.00 22.01  ? 597  GLU   B C   1 
ATOM   5749  O  O   . GLU   B  1 296 ? -18.811 5.030   -8.761   1.00 21.83  ? 597  GLU   B O   1 
ATOM   5750  C  CB  . GLU   B  1 296 ? -15.727 4.323   -7.722   1.00 26.75  ? 597  GLU   B CB  1 
ATOM   5751  C  CG  . GLU   B  1 296 ? -14.463 3.547   -7.997   1.00 24.03  ? 597  GLU   B CG  1 
ATOM   5752  C  CD  . GLU   B  1 296 ? -13.848 3.044   -6.709   1.00 25.00  ? 597  GLU   B CD  1 
ATOM   5753  O  OE1 . GLU   B  1 296 ? -14.344 2.022   -6.202   1.00 21.95  ? 597  GLU   B OE1 1 
ATOM   5754  O  OE2 . GLU   B  1 296 ? -12.898 3.683   -6.192   1.00 25.35  ? 597  GLU   B OE2 1 
ATOM   5755  N  N   . ILE   B  1 297 ? -17.621 6.798   -8.033   1.00 20.95  ? 598  ILE   B N   1 
ATOM   5756  C  CA  . ILE   B  1 297 ? -18.796 7.565   -7.635   1.00 28.73  ? 598  ILE   B CA  1 
ATOM   5757  C  C   . ILE   B  1 297 ? -19.402 8.260   -8.843   1.00 25.55  ? 598  ILE   B C   1 
ATOM   5758  O  O   . ILE   B  1 297 ? -20.584 8.090   -9.153   1.00 25.93  ? 598  ILE   B O   1 
ATOM   5759  C  CB  . ILE   B  1 297 ? -18.420 8.592   -6.547   1.00 24.89  ? 598  ILE   B CB  1 
ATOM   5760  C  CG1 . ILE   B  1 297 ? -17.777 7.918   -5.320   1.00 22.93  ? 598  ILE   B CG1 1 
ATOM   5761  C  CG2 . ILE   B  1 297 ? -19.634 9.443   -6.165   1.00 20.38  ? 598  ILE   B CG2 1 
ATOM   5762  C  CD1 . ILE   B  1 297 ? -17.049 8.912   -4.417   1.00 21.12  ? 598  ILE   B CD1 1 
ATOM   5763  N  N   . GLY   B  1 298 ? -18.590 9.055   -9.543   1.00 20.37  ? 599  GLY   B N   1 
ATOM   5764  C  CA  . GLY   B  1 298 ? -19.124 9.918   -10.586  1.00 23.44  ? 599  GLY   B CA  1 
ATOM   5765  C  C   . GLY   B  1 298 ? -19.639 9.160   -11.799  1.00 28.98  ? 599  GLY   B C   1 
ATOM   5766  O  O   . GLY   B  1 298 ? -20.608 9.584   -12.435  1.00 31.70  ? 599  GLY   B O   1 
ATOM   5767  N  N   . VAL   B  1 299 ? -19.017 8.034   -12.134  1.00 25.92  ? 600  VAL   B N   1 
ATOM   5768  C  CA  . VAL   B  1 299 ? -19.474 7.265   -13.296  1.00 28.17  ? 600  VAL   B CA  1 
ATOM   5769  C  C   . VAL   B  1 299 ? -20.457 6.174   -12.896  1.00 30.69  ? 600  VAL   B C   1 
ATOM   5770  O  O   . VAL   B  1 299 ? -21.569 6.111   -13.425  1.00 25.06  ? 600  VAL   B O   1 
ATOM   5771  C  CB  . VAL   B  1 299 ? -18.280 6.676   -14.070  1.00 26.84  ? 600  VAL   B CB  1 
ATOM   5772  C  CG1 . VAL   B  1 299 ? -18.781 5.933   -15.299  1.00 26.88  ? 600  VAL   B CG1 1 
ATOM   5773  C  CG2 . VAL   B  1 299 ? -17.328 7.784   -14.473  1.00 23.15  ? 600  VAL   B CG2 1 
ATOM   5774  N  N   . ARG   B  1 300 ? -20.089 5.309   -11.945  1.00 26.77  ? 601  ARG   B N   1 
ATOM   5775  C  CA  . ARG   B  1 300 ? -20.917 4.134   -11.683  1.00 25.91  ? 601  ARG   B CA  1 
ATOM   5776  C  C   . ARG   B  1 300 ? -22.032 4.439   -10.689  1.00 29.51  ? 601  ARG   B C   1 
ATOM   5777  O  O   . ARG   B  1 300 ? -23.210 4.240   -10.999  1.00 30.11  ? 601  ARG   B O   1 
ATOM   5778  C  CB  . ARG   B  1 300 ? -20.040 2.965   -11.210  1.00 20.46  ? 601  ARG   B CB  1 
ATOM   5779  C  CG  . ARG   B  1 300 ? -18.827 2.697   -12.119  1.00 23.81  ? 601  ARG   B CG  1 
ATOM   5780  C  CD  . ARG   B  1 300 ? -19.227 2.249   -13.532  1.00 22.33  ? 601  ARG   B CD  1 
ATOM   5781  N  NE  . ARG   B  1 300 ? -20.279 1.232   -13.487  1.00 20.35  ? 601  ARG   B NE  1 
ATOM   5782  C  CZ  . ARG   B  1 300 ? -20.060 -0.046  -13.188  1.00 19.78  ? 601  ARG   B CZ  1 
ATOM   5783  N  NH1 . ARG   B  1 300 ? -18.824 -0.484  -12.976  1.00 20.21  ? 601  ARG   B NH1 1 
ATOM   5784  N  NH2 . ARG   B  1 300 ? -21.074 -0.891  -13.121  1.00 21.55  ? 601  ARG   B NH2 1 
ATOM   5785  N  N   . ASP   B  1 301 ? -21.677 4.925   -9.490   1.00 29.04  ? 602  ASP   B N   1 
ATOM   5786  C  CA  . ASP   B  1 301 ? -22.694 5.167   -8.470   1.00 30.80  ? 602  ASP   B CA  1 
ATOM   5787  C  C   . ASP   B  1 301 ? -23.720 6.180   -8.954   1.00 31.67  ? 602  ASP   B C   1 
ATOM   5788  O  O   . ASP   B  1 301 ? -24.930 5.990   -8.776   1.00 27.31  ? 602  ASP   B O   1 
ATOM   5789  C  CB  . ASP   B  1 301 ? -22.038 5.634   -7.165   1.00 25.00  ? 602  ASP   B CB  1 
ATOM   5790  C  CG  . ASP   B  1 301 ? -21.172 4.553   -6.531   1.00 27.95  ? 602  ASP   B CG  1 
ATOM   5791  O  OD1 . ASP   B  1 301 ? -21.513 3.364   -6.676   1.00 27.87  ? 602  ASP   B OD1 1 
ATOM   5792  O  OD2 . ASP   B  1 301 ? -20.147 4.890   -5.900   1.00 31.00  ? 602  ASP   B OD2 1 
ATOM   5793  N  N   . TYR   B  1 302 ? -23.268 7.232   -9.620   1.00 29.59  ? 603  TYR   B N   1 
ATOM   5794  C  CA  . TYR   B  1 302 ? -24.199 8.279   -10.009  1.00 25.20  ? 603  TYR   B CA  1 
ATOM   5795  C  C   . TYR   B  1 302 ? -24.847 8.052   -11.371  1.00 30.32  ? 603  TYR   B C   1 
ATOM   5796  O  O   . TYR   B  1 302 ? -25.973 8.516   -11.587  1.00 29.74  ? 603  TYR   B O   1 
ATOM   5797  C  CB  . TYR   B  1 302 ? -23.481 9.629   -10.009  1.00 22.44  ? 603  TYR   B CB  1 
ATOM   5798  C  CG  . TYR   B  1 302 ? -23.318 10.231  -8.641   1.00 23.61  ? 603  TYR   B CG  1 
ATOM   5799  C  CD1 . TYR   B  1 302 ? -22.596 11.403  -8.465   1.00 24.14  ? 603  TYR   B CD1 1 
ATOM   5800  C  CD2 . TYR   B  1 302 ? -23.881 9.628   -7.521   1.00 24.59  ? 603  TYR   B CD2 1 
ATOM   5801  C  CE1 . TYR   B  1 302 ? -22.443 11.966  -7.207   1.00 28.91  ? 603  TYR   B CE1 1 
ATOM   5802  C  CE2 . TYR   B  1 302 ? -23.733 10.190  -6.259   1.00 27.96  ? 603  TYR   B CE2 1 
ATOM   5803  C  CZ  . TYR   B  1 302 ? -23.009 11.350  -6.115   1.00 27.89  ? 603  TYR   B CZ  1 
ATOM   5804  O  OH  . TYR   B  1 302 ? -22.867 11.910  -4.870   1.00 30.04  ? 603  TYR   B OH  1 
ATOM   5805  N  N   . CYS   B  1 303 ? -24.185 7.361   -12.305  1.00 28.47  ? 604  CYS   B N   1 
ATOM   5806  C  CA  . CYS   B  1 303 ? -24.674 7.372   -13.680  1.00 32.65  ? 604  CYS   B CA  1 
ATOM   5807  C  C   . CYS   B  1 303 ? -25.039 6.017   -14.257  1.00 32.40  ? 604  CYS   B C   1 
ATOM   5808  O  O   . CYS   B  1 303 ? -25.601 5.982   -15.355  1.00 27.11  ? 604  CYS   B O   1 
ATOM   5809  C  CB  . CYS   B  1 303 ? -23.654 8.038   -14.609  1.00 26.46  ? 604  CYS   B CB  1 
ATOM   5810  S  SG  . CYS   B  1 303 ? -23.367 9.748   -14.186  1.00 30.20  ? 604  CYS   B SG  1 
ATOM   5811  N  N   . ASP   B  1 304 ? -24.724 4.910   -13.590  1.00 28.03  ? 605  ASP   B N   1 
ATOM   5812  C  CA  . ASP   B  1 304 ? -25.313 3.643   -13.996  1.00 27.88  ? 605  ASP   B CA  1 
ATOM   5813  C  C   . ASP   B  1 304 ? -26.826 3.801   -14.035  1.00 30.21  ? 605  ASP   B C   1 
ATOM   5814  O  O   . ASP   B  1 304 ? -27.420 4.415   -13.145  1.00 34.40  ? 605  ASP   B O   1 
ATOM   5815  C  CB  . ASP   B  1 304 ? -24.948 2.520   -13.022  1.00 22.86  ? 605  ASP   B CB  1 
ATOM   5816  C  CG  . ASP   B  1 304 ? -23.595 1.866   -13.303  1.00 30.99  ? 605  ASP   B CG  1 
ATOM   5817  O  OD1 . ASP   B  1 304 ? -22.812 2.326   -14.169  1.00 32.28  ? 605  ASP   B OD1 1 
ATOM   5818  O  OD2 . ASP   B  1 304 ? -23.318 0.848   -12.629  1.00 33.02  ? 605  ASP   B OD2 1 
ATOM   5819  N  N   . ASN   B  1 305 ? -27.449 3.257   -15.081  1.00 27.61  ? 606  ASN   B N   1 
ATOM   5820  C  CA  . ASN   B  1 305 ? -28.903 3.308   -15.177  1.00 27.05  ? 606  ASN   B CA  1 
ATOM   5821  C  C   . ASN   B  1 305 ? -29.572 2.626   -13.991  1.00 29.24  ? 606  ASN   B C   1 
ATOM   5822  O  O   . ASN   B  1 305 ? -30.680 3.009   -13.610  1.00 31.80  ? 606  ASN   B O   1 
ATOM   5823  C  CB  . ASN   B  1 305 ? -29.364 2.662   -16.478  1.00 30.37  ? 606  ASN   B CB  1 
ATOM   5824  C  CG  . ASN   B  1 305 ? -29.031 3.509   -17.688  1.00 46.75  ? 606  ASN   B CG  1 
ATOM   5825  O  OD1 . ASN   B  1 305 ? -29.300 4.716   -17.706  1.00 46.08  ? 606  ASN   B OD1 1 
ATOM   5826  N  ND2 . ASN   B  1 305 ? -28.430 2.888   -18.705  1.00 48.51  ? 606  ASN   B ND2 1 
ATOM   5827  N  N   . SER   B  1 306 ? -28.910 1.633   -13.394  1.00 33.32  ? 607  SER   B N   1 
ATOM   5828  C  CA  . SER   B  1 306 ? -29.426 0.880   -12.263  1.00 35.81  ? 607  SER   B CA  1 
ATOM   5829  C  C   . SER   B  1 306 ? -29.106 1.513   -10.912  1.00 36.43  ? 607  SER   B C   1 
ATOM   5830  O  O   . SER   B  1 306 ? -29.521 0.978   -9.885   1.00 32.15  ? 607  SER   B O   1 
ATOM   5831  C  CB  . SER   B  1 306 ? -28.861 -0.545  -12.273  1.00 39.16  ? 607  SER   B CB  1 
ATOM   5832  O  OG  . SER   B  1 306 ? -28.965 -1.134  -13.555  1.00 61.70  ? 607  SER   B OG  1 
ATOM   5833  N  N   . ARG   B  1 307 ? -28.359 2.604   -10.884  1.00 36.74  ? 608  ARG   B N   1 
ATOM   5834  C  CA  . ARG   B  1 307 ? -27.902 3.225   -9.642   1.00 23.93  ? 608  ARG   B CA  1 
ATOM   5835  C  C   . ARG   B  1 307 ? -28.620 4.570   -9.475   1.00 25.96  ? 608  ARG   B C   1 
ATOM   5836  O  O   . ARG   B  1 307 ? -29.834 4.611   -9.680   1.00 31.62  ? 608  ARG   B O   1 
ATOM   5837  C  CB  . ARG   B  1 307 ? -26.386 3.296   -9.654   1.00 27.48  ? 608  ARG   B CB  1 
ATOM   5838  C  CG  . ARG   B  1 307 ? -25.697 1.912   -9.739   1.00 29.33  ? 608  ARG   B CG  1 
ATOM   5839  C  CD  . ARG   B  1 307 ? -25.940 1.041   -8.491   1.00 33.02  ? 608  ARG   B CD  1 
ATOM   5840  N  NE  . ARG   B  1 307 ? -25.546 1.696   -7.243   1.00 28.50  ? 608  ARG   B NE  1 
ATOM   5841  C  CZ  . ARG   B  1 307 ? -24.295 1.980   -6.892   1.00 32.07  ? 608  ARG   B CZ  1 
ATOM   5842  N  NH1 . ARG   B  1 307 ? -23.284 1.686   -7.701   1.00 25.30  ? 608  ARG   B NH1 1 
ATOM   5843  N  NH2 . ARG   B  1 307 ? -24.053 2.579   -5.726   1.00 31.66  ? 608  ARG   B NH2 1 
ATOM   5844  N  N   . TYR   B  1 308 ? -27.942 5.653   -9.100   1.00 25.76  ? 609  TYR   B N   1 
ATOM   5845  C  CA  . TYR   B  1 308 ? -28.679 6.889   -8.877   1.00 32.33  ? 609  TYR   B CA  1 
ATOM   5846  C  C   . TYR   B  1 308 ? -29.140 7.523   -10.181  1.00 31.29  ? 609  TYR   B C   1 
ATOM   5847  O  O   . TYR   B  1 308 ? -30.091 8.312   -10.158  1.00 34.72  ? 609  TYR   B O   1 
ATOM   5848  C  CB  . TYR   B  1 308 ? -27.839 7.867   -8.051   1.00 27.85  ? 609  TYR   B CB  1 
ATOM   5849  C  CG  . TYR   B  1 308 ? -27.947 7.593   -6.569   1.00 29.31  ? 609  TYR   B CG  1 
ATOM   5850  C  CD1 . TYR   B  1 308 ? -27.167 6.610   -5.959   1.00 27.84  ? 609  TYR   B CD1 1 
ATOM   5851  C  CD2 . TYR   B  1 308 ? -28.846 8.294   -5.781   1.00 32.35  ? 609  TYR   B CD2 1 
ATOM   5852  C  CE1 . TYR   B  1 308 ? -27.275 6.348   -4.586   1.00 28.76  ? 609  TYR   B CE1 1 
ATOM   5853  C  CE2 . TYR   B  1 308 ? -28.962 8.038   -4.421   1.00 28.97  ? 609  TYR   B CE2 1 
ATOM   5854  C  CZ  . TYR   B  1 308 ? -28.175 7.067   -3.831   1.00 31.97  ? 609  TYR   B CZ  1 
ATOM   5855  O  OH  . TYR   B  1 308 ? -28.287 6.818   -2.477   1.00 27.42  ? 609  TYR   B OH  1 
ATOM   5856  N  N   . ASN   B  1 309 ? -28.483 7.201   -11.303  1.00 27.73  ? 610  ASN   B N   1 
ATOM   5857  C  CA  . ASN   B  1 309 ? -29.001 7.472   -12.648  1.00 32.69  ? 610  ASN   B CA  1 
ATOM   5858  C  C   . ASN   B  1 309 ? -29.353 8.955   -12.837  1.00 31.66  ? 610  ASN   B C   1 
ATOM   5859  O  O   . ASN   B  1 309 ? -30.484 9.325   -13.166  1.00 28.90  ? 610  ASN   B O   1 
ATOM   5860  C  CB  . ASN   B  1 309 ? -30.207 6.561   -12.923  1.00 37.27  ? 610  ASN   B CB  1 
ATOM   5861  C  CG  . ASN   B  1 309 ? -30.756 6.698   -14.327  1.00 36.88  ? 610  ASN   B CG  1 
ATOM   5862  O  OD1 . ASN   B  1 309 ? -30.022 6.997   -15.281  1.00 32.82  ? 610  ASN   B OD1 1 
ATOM   5863  N  ND2 . ASN   B  1 309 ? -32.060 6.482   -14.463  1.00 31.12  ? 610  ASN   B ND2 1 
ATOM   5864  N  N   . ILE   B  1 310 ? -28.353 9.819   -12.635  1.00 30.88  ? 611  ILE   B N   1 
ATOM   5865  C  CA  . ILE   B  1 310 ? -28.603 11.263  -12.624  1.00 25.63  ? 611  ILE   B CA  1 
ATOM   5866  C  C   . ILE   B  1 310 ? -28.278 11.929  -13.948  1.00 33.39  ? 611  ILE   B C   1 
ATOM   5867  O  O   . ILE   B  1 310 ? -28.414 13.155  -14.058  1.00 34.99  ? 611  ILE   B O   1 
ATOM   5868  C  CB  . ILE   B  1 310 ? -27.805 11.969  -11.518  1.00 27.81  ? 611  ILE   B CB  1 
ATOM   5869  C  CG1 . ILE   B  1 310 ? -26.323 11.981  -11.903  1.00 27.57  ? 611  ILE   B CG1 1 
ATOM   5870  C  CG2 . ILE   B  1 310 ? -28.022 11.285  -10.166  1.00 35.11  ? 611  ILE   B CG2 1 
ATOM   5871  C  CD1 . ILE   B  1 310 ? -25.476 12.863  -11.014  1.00 28.24  ? 611  ILE   B CD1 1 
ATOM   5872  N  N   . LEU   B  1 311 ? -27.818 11.170  -14.946  1.00 28.52  ? 612  LEU   B N   1 
ATOM   5873  C  CA  . LEU   B  1 311 ? -27.439 11.777  -16.220  1.00 31.72  ? 612  LEU   B CA  1 
ATOM   5874  C  C   . LEU   B  1 311 ? -28.539 12.683  -16.774  1.00 27.09  ? 612  LEU   B C   1 
ATOM   5875  O  O   . LEU   B  1 311 ? -28.283 13.844  -17.104  1.00 27.63  ? 612  LEU   B O   1 
ATOM   5876  C  CB  . LEU   B  1 311 ? -27.073 10.693  -17.231  1.00 27.83  ? 612  LEU   B CB  1 
ATOM   5877  C  CG  . LEU   B  1 311 ? -25.679 10.100  -17.064  1.00 30.02  ? 612  LEU   B CG  1 
ATOM   5878  C  CD1 . LEU   B  1 311 ? -25.476 9.025   -18.116  1.00 32.96  ? 612  LEU   B CD1 1 
ATOM   5879  C  CD2 . LEU   B  1 311 ? -24.659 11.191  -17.235  1.00 24.72  ? 612  LEU   B CD2 1 
ATOM   5880  N  N   . GLU   B  1 312 ? -29.773 12.178  -16.873  1.00 33.27  ? 613  GLU   B N   1 
ATOM   5881  C  CA  . GLU   B  1 312 ? -30.856 12.997  -17.424  1.00 33.74  ? 613  GLU   B CA  1 
ATOM   5882  C  C   . GLU   B  1 312 ? -30.984 14.328  -16.684  1.00 34.56  ? 613  GLU   B C   1 
ATOM   5883  O  O   . GLU   B  1 312 ? -31.070 15.395  -17.304  1.00 36.77  ? 613  GLU   B O   1 
ATOM   5884  C  CB  . GLU   B  1 312 ? -32.189 12.246  -17.361  1.00 43.65  ? 613  GLU   B CB  1 
ATOM   5885  C  CG  . GLU   B  1 312 ? -32.611 11.549  -18.635  1.00 59.17  ? 613  GLU   B CG  1 
ATOM   5886  C  CD  . GLU   B  1 312 ? -34.108 11.279  -18.668  1.00 69.85  ? 613  GLU   B CD  1 
ATOM   5887  O  OE1 . GLU   B  1 312 ? -34.892 12.250  -18.791  1.00 65.86  ? 613  GLU   B OE1 1 
ATOM   5888  O  OE2 . GLU   B  1 312 ? -34.498 10.095  -18.555  1.00 74.53  ? 613  GLU   B OE2 1 
ATOM   5889  N  N   . GLU   B  1 313 ? -31.011 14.278  -15.351  1.00 34.00  ? 614  GLU   B N   1 
ATOM   5890  C  CA  . GLU   B  1 313 ? -31.229 15.501  -14.586  1.00 35.99  ? 614  GLU   B CA  1 
ATOM   5891  C  C   . GLU   B  1 313 ? -30.083 16.478  -14.774  1.00 31.85  ? 614  GLU   B C   1 
ATOM   5892  O  O   . GLU   B  1 313 ? -30.306 17.681  -14.932  1.00 40.05  ? 614  GLU   B O   1 
ATOM   5893  C  CB  . GLU   B  1 313 ? -31.407 15.188  -13.103  1.00 36.20  ? 614  GLU   B CB  1 
ATOM   5894  C  CG  . GLU   B  1 313 ? -32.050 16.342  -12.369  1.00 48.00  ? 614  GLU   B CG  1 
ATOM   5895  C  CD  . GLU   B  1 313 ? -32.060 16.148  -10.878  1.00 65.44  ? 614  GLU   B CD  1 
ATOM   5896  O  OE1 . GLU   B  1 313 ? -32.360 17.130  -10.160  1.00 71.89  ? 614  GLU   B OE1 1 
ATOM   5897  O  OE2 . GLU   B  1 313 ? -31.763 15.018  -10.427  1.00 65.35  ? 614  GLU   B OE2 1 
ATOM   5898  N  N   . VAL   B  1 314 ? -28.851 15.976  -14.773  1.00 31.06  ? 615  VAL   B N   1 
ATOM   5899  C  CA  . VAL   B  1 314 ? -27.704 16.855  -14.940  1.00 28.45  ? 615  VAL   B CA  1 
ATOM   5900  C  C   . VAL   B  1 314 ? -27.693 17.446  -16.335  1.00 35.49  ? 615  VAL   B C   1 
ATOM   5901  O  O   . VAL   B  1 314 ? -27.428 18.640  -16.518  1.00 37.54  ? 615  VAL   B O   1 
ATOM   5902  C  CB  . VAL   B  1 314 ? -26.408 16.088  -14.634  1.00 31.02  ? 615  VAL   B CB  1 
ATOM   5903  C  CG1 . VAL   B  1 314 ? -25.184 16.897  -15.053  1.00 27.37  ? 615  VAL   B CG1 1 
ATOM   5904  C  CG2 . VAL   B  1 314 ? -26.351 15.744  -13.150  1.00 31.21  ? 615  VAL   B CG2 1 
ATOM   5905  N  N   . ALA   B  1 315 ? -27.976 16.622  -17.345  1.00 30.86  ? 616  ALA   B N   1 
ATOM   5906  C  CA  . ALA   B  1 315 ? -27.984 17.130  -18.705  1.00 29.84  ? 616  ALA   B CA  1 
ATOM   5907  C  C   . ALA   B  1 315 ? -29.085 18.166  -18.886  1.00 40.24  ? 616  ALA   B C   1 
ATOM   5908  O  O   . ALA   B  1 315 ? -28.896 19.165  -19.589  1.00 35.81  ? 616  ALA   B O   1 
ATOM   5909  C  CB  . ALA   B  1 315 ? -28.148 15.973  -19.684  1.00 29.55  ? 616  ALA   B CB  1 
ATOM   5910  N  N   . LYS   B  1 316 ? -30.239 17.953  -18.246  1.00 40.50  ? 617  LYS   B N   1 
ATOM   5911  C  CA  . LYS   B  1 316 ? -31.300 18.955  -18.294  1.00 49.75  ? 617  LYS   B CA  1 
ATOM   5912  C  C   . LYS   B  1 316 ? -30.804 20.285  -17.745  1.00 45.59  ? 617  LYS   B C   1 
ATOM   5913  O  O   . LYS   B  1 316 ? -30.896 21.320  -18.410  1.00 42.35  ? 617  LYS   B O   1 
ATOM   5914  C  CB  . LYS   B  1 316 ? -32.522 18.483  -17.503  1.00 56.39  ? 617  LYS   B CB  1 
ATOM   5915  C  CG  . LYS   B  1 316 ? -33.505 17.615  -18.260  1.00 64.07  ? 617  LYS   B CG  1 
ATOM   5916  C  CD  . LYS   B  1 316 ? -34.724 17.341  -17.381  1.00 70.12  ? 617  LYS   B CD  1 
ATOM   5917  C  CE  . LYS   B  1 316 ? -35.803 16.571  -18.125  1.00 72.81  ? 617  LYS   B CE  1 
ATOM   5918  N  NZ  . LYS   B  1 316 ? -35.382 15.175  -18.426  1.00 71.22  ? 617  LYS   B NZ  1 
ATOM   5919  N  N   . LYS   B  1 317 ? -30.250 20.269  -16.531  1.00 45.83  ? 618  LYS   B N   1 
ATOM   5920  C  CA  . LYS   B  1 317 ? -29.733 21.504  -15.956  1.00 43.25  ? 618  LYS   B CA  1 
ATOM   5921  C  C   . LYS   B  1 317 ? -28.597 22.084  -16.785  1.00 43.33  ? 618  LYS   B C   1 
ATOM   5922  O  O   . LYS   B  1 317 ? -28.368 23.294  -16.726  1.00 39.37  ? 618  LYS   B O   1 
ATOM   5923  C  CB  . LYS   B  1 317 ? -29.289 21.276  -14.510  1.00 39.04  ? 618  LYS   B CB  1 
ATOM   5924  C  CG  . LYS   B  1 317 ? -30.422 20.787  -13.609  1.00 50.71  ? 618  LYS   B CG  1 
ATOM   5925  C  CD  . LYS   B  1 317 ? -30.249 21.213  -12.166  1.00 55.55  ? 618  LYS   B CD  1 
ATOM   5926  C  CE  . LYS   B  1 317 ? -30.833 22.592  -11.897  1.00 69.95  ? 618  LYS   B CE  1 
ATOM   5927  N  NZ  . LYS   B  1 317 ? -32.316 22.563  -11.721  1.00 77.04  ? 618  LYS   B NZ  1 
ATOM   5928  N  N   . MET   B  1 318 ? -27.909 21.267  -17.587  1.00 39.44  ? 619  MET   B N   1 
ATOM   5929  C  CA  . MET   B  1 318 ? -26.900 21.787  -18.503  1.00 40.06  ? 619  MET   B CA  1 
ATOM   5930  C  C   . MET   B  1 318 ? -27.482 22.307  -19.811  1.00 41.98  ? 619  MET   B C   1 
ATOM   5931  O  O   . MET   B  1 318 ? -26.723 22.811  -20.646  1.00 41.41  ? 619  MET   B O   1 
ATOM   5932  C  CB  . MET   B  1 318 ? -25.852 20.716  -18.807  1.00 35.35  ? 619  MET   B CB  1 
ATOM   5933  C  CG  . MET   B  1 318 ? -24.877 20.500  -17.671  1.00 31.04  ? 619  MET   B CG  1 
ATOM   5934  S  SD  . MET   B  1 318 ? -23.769 19.118  -17.947  1.00 35.23  ? 619  MET   B SD  1 
ATOM   5935  C  CE  . MET   B  1 318 ? -22.834 19.718  -19.367  1.00 29.60  ? 619  MET   B CE  1 
ATOM   5936  N  N   . ASN   B  1 319 ? -28.798 22.189  -20.009  1.00 42.16  ? 620  ASN   B N   1 
ATOM   5937  C  CA  . ASN   B  1 319 ? -29.465 22.628  -21.235  1.00 50.74  ? 620  ASN   B CA  1 
ATOM   5938  C  C   . ASN   B  1 319 ? -28.944 21.891  -22.470  1.00 53.28  ? 620  ASN   B C   1 
ATOM   5939  O  O   . ASN   B  1 319 ? -28.921 22.440  -23.573  1.00 48.49  ? 620  ASN   B O   1 
ATOM   5940  C  CB  . ASN   B  1 319 ? -29.339 24.140  -21.424  1.00 57.06  ? 620  ASN   B CB  1 
ATOM   5941  C  CG  . ASN   B  1 319 ? -29.958 24.913  -20.287  1.00 67.13  ? 620  ASN   B CG  1 
ATOM   5942  O  OD1 . ASN   B  1 319 ? -31.083 24.631  -19.872  1.00 73.53  ? 620  ASN   B OD1 1 
ATOM   5943  N  ND2 . ASN   B  1 319 ? -29.222 25.884  -19.758  1.00 69.27  ? 620  ASN   B ND2 1 
ATOM   5944  N  N   . LEU   B  1 320 ? -28.529 20.641  -22.300  1.00 47.27  ? 621  LEU   B N   1 
ATOM   5945  C  CA  . LEU   B  1 320 ? -27.993 19.894  -23.423  1.00 48.36  ? 621  LEU   B CA  1 
ATOM   5946  C  C   . LEU   B  1 320 ? -29.114 19.441  -24.348  1.00 52.41  ? 621  LEU   B C   1 
ATOM   5947  O  O   . LEU   B  1 320 ? -30.257 19.240  -23.927  1.00 51.77  ? 621  LEU   B O   1 
ATOM   5948  C  CB  . LEU   B  1 320 ? -27.205 18.691  -22.924  1.00 43.66  ? 621  LEU   B CB  1 
ATOM   5949  C  CG  . LEU   B  1 320 ? -26.013 19.044  -22.040  1.00 37.98  ? 621  LEU   B CG  1 
ATOM   5950  C  CD1 . LEU   B  1 320 ? -25.225 17.785  -21.719  1.00 32.63  ? 621  LEU   B CD1 1 
ATOM   5951  C  CD2 . LEU   B  1 320 ? -25.139 20.059  -22.752  1.00 35.87  ? 621  LEU   B CD2 1 
ATOM   5952  N  N   . ASP   B  1 321 ? -28.779 19.290  -25.627  1.00 59.04  ? 622  ASP   B N   1 
ATOM   5953  C  CA  . ASP   B  1 321 ? -29.698 18.676  -26.580  1.00 57.39  ? 622  ASP   B CA  1 
ATOM   5954  C  C   . ASP   B  1 321 ? -29.744 17.182  -26.309  1.00 43.52  ? 622  ASP   B C   1 
ATOM   5955  O  O   . ASP   B  1 321 ? -28.776 16.467  -26.584  1.00 40.14  ? 622  ASP   B O   1 
ATOM   5956  C  CB  . ASP   B  1 321 ? -29.262 18.964  -28.014  1.00 63.15  ? 622  ASP   B CB  1 
ATOM   5957  C  CG  . ASP   B  1 321 ? -30.078 18.191  -29.043  1.00 68.55  ? 622  ASP   B CG  1 
ATOM   5958  O  OD1 . ASP   B  1 321 ? -29.513 17.831  -30.101  1.00 72.74  ? 622  ASP   B OD1 1 
ATOM   5959  O  OD2 . ASP   B  1 321 ? -31.276 17.930  -28.786  1.00 62.30  ? 622  ASP   B OD2 1 
ATOM   5960  N  N   . MET   B  1 322 ? -30.859 16.709  -25.756  1.00 38.75  ? 623  MET   B N   1 
ATOM   5961  C  CA  . MET   B  1 322 ? -31.023 15.305  -25.409  1.00 41.62  ? 623  MET   B CA  1 
ATOM   5962  C  C   . MET   B  1 322 ? -31.927 14.554  -26.378  1.00 42.64  ? 623  MET   B C   1 
ATOM   5963  O  O   . MET   B  1 322 ? -32.339 13.431  -26.076  1.00 53.96  ? 623  MET   B O   1 
ATOM   5964  C  CB  . MET   B  1 322 ? -31.566 15.174  -23.983  1.00 42.80  ? 623  MET   B CB  1 
ATOM   5965  C  CG  . MET   B  1 322 ? -30.747 15.896  -22.931  1.00 50.06  ? 623  MET   B CG  1 
ATOM   5966  S  SD  . MET   B  1 322 ? -31.600 15.981  -21.345  1.00 51.18  ? 623  MET   B SD  1 
ATOM   5967  C  CE  . MET   B  1 322 ? -31.860 14.245  -20.999  1.00 42.92  ? 623  MET   B CE  1 
ATOM   5968  N  N   . ARG   B  1 323 ? -32.241 15.135  -27.536  1.00 43.13  ? 624  ARG   B N   1 
ATOM   5969  C  CA  . ARG   B  1 323 ? -33.106 14.450  -28.492  1.00 54.44  ? 624  ARG   B CA  1 
ATOM   5970  C  C   . ARG   B  1 323 ? -32.377 13.396  -29.317  1.00 48.74  ? 624  ARG   B C   1 
ATOM   5971  O  O   . ARG   B  1 323 ? -33.038 12.577  -29.965  1.00 53.24  ? 624  ARG   B O   1 
ATOM   5972  C  CB  . ARG   B  1 323 ? -33.762 15.456  -29.437  1.00 62.11  ? 624  ARG   B CB  1 
ATOM   5973  C  CG  . ARG   B  1 323 ? -35.102 15.993  -28.962  1.00 68.82  ? 624  ARG   B CG  1 
ATOM   5974  C  CD  . ARG   B  1 323 ? -35.632 17.048  -29.927  1.00 81.48  ? 624  ARG   B CD  1 
ATOM   5975  N  NE  . ARG   B  1 323 ? -34.791 18.241  -29.934  1.00 88.92  ? 624  ARG   B NE  1 
ATOM   5976  C  CZ  . ARG   B  1 323 ? -33.859 18.507  -30.845  1.00 95.04  ? 624  ARG   B CZ  1 
ATOM   5977  N  NH1 . ARG   B  1 323 ? -33.638 17.666  -31.849  1.00 99.04  ? 624  ARG   B NH1 1 
ATOM   5978  N  NH2 . ARG   B  1 323 ? -33.144 19.618  -30.749  1.00 95.88  ? 624  ARG   B NH2 1 
ATOM   5979  N  N   . LYS   B  1 324 ? -31.047 13.388  -29.316  1.00 42.21  ? 625  LYS   B N   1 
ATOM   5980  C  CA  . LYS   B  1 324 ? -30.297 12.435  -30.120  1.00 47.08  ? 625  LYS   B CA  1 
ATOM   5981  C  C   . LYS   B  1 324 ? -29.044 12.012  -29.370  1.00 45.02  ? 625  LYS   B C   1 
ATOM   5982  O  O   . LYS   B  1 324 ? -28.444 12.816  -28.654  1.00 47.06  ? 625  LYS   B O   1 
ATOM   5983  C  CB  . LYS   B  1 324 ? -29.926 13.041  -31.476  1.00 57.41  ? 625  LYS   B CB  1 
ATOM   5984  C  CG  . LYS   B  1 324 ? -29.301 14.423  -31.353  1.00 68.25  ? 625  LYS   B CG  1 
ATOM   5985  C  CD  . LYS   B  1 324 ? -29.058 15.054  -32.711  1.00 71.95  ? 625  LYS   B CD  1 
ATOM   5986  C  CE  . LYS   B  1 324 ? -27.982 16.119  -32.625  1.00 73.36  ? 625  LYS   B CE  1 
ATOM   5987  N  NZ  . LYS   B  1 324 ? -27.053 16.028  -33.782  1.00 75.87  ? 625  LYS   B NZ  1 
ATOM   5988  N  N   . THR   B  1 325 ? -28.651 10.746  -29.534  1.00 35.86  ? 626  THR   B N   1 
ATOM   5989  C  CA  . THR   B  1 325 ? -27.486 10.256  -28.809  1.00 39.63  ? 626  THR   B CA  1 
ATOM   5990  C  C   . THR   B  1 325 ? -26.202 10.891  -29.325  1.00 33.58  ? 626  THR   B C   1 
ATOM   5991  O  O   . THR   B  1 325 ? -25.267 11.114  -28.545  1.00 34.99  ? 626  THR   B O   1 
ATOM   5992  C  CB  . THR   B  1 325 ? -27.387 8.726   -28.895  1.00 46.92  ? 626  THR   B CB  1 
ATOM   5993  O  OG1 . THR   B  1 325 ? -27.217 8.329   -30.262  1.00 50.48  ? 626  THR   B OG1 1 
ATOM   5994  C  CG2 . THR   B  1 325 ? -28.640 8.060   -28.327  1.00 42.25  ? 626  THR   B CG2 1 
ATOM   5995  N  N   . SER   B  1 326 ? -26.144 11.199  -30.627  1.00 34.96  ? 627  SER   B N   1 
ATOM   5996  C  CA  . SER   B  1 326 ? -24.916 11.701  -31.225  1.00 36.92  ? 627  SER   B CA  1 
ATOM   5997  C  C   . SER   B  1 326 ? -24.596 13.122  -30.783  1.00 38.74  ? 627  SER   B C   1 
ATOM   5998  O  O   . SER   B  1 326 ? -23.525 13.638  -31.122  1.00 33.27  ? 627  SER   B O   1 
ATOM   5999  C  CB  . SER   B  1 326 ? -25.000 11.619  -32.758  1.00 36.31  ? 627  SER   B CB  1 
ATOM   6000  O  OG  . SER   B  1 326 ? -25.830 12.636  -33.273  1.00 44.35  ? 627  SER   B OG  1 
ATOM   6001  N  N   . SER   B  1 327 ? -25.485 13.767  -30.031  1.00 38.65  ? 628  SER   B N   1 
ATOM   6002  C  CA  . SER   B  1 327 ? -25.076 14.993  -29.367  1.00 42.63  ? 628  SER   B CA  1 
ATOM   6003  C  C   . SER   B  1 327 ? -24.096 14.718  -28.238  1.00 37.50  ? 628  SER   B C   1 
ATOM   6004  O  O   . SER   B  1 327 ? -23.466 15.660  -27.748  1.00 32.73  ? 628  SER   B O   1 
ATOM   6005  C  CB  . SER   B  1 327 ? -26.295 15.736  -28.834  1.00 37.89  ? 628  SER   B CB  1 
ATOM   6006  O  OG  . SER   B  1 327 ? -26.790 15.097  -27.676  1.00 38.12  ? 628  SER   B OG  1 
ATOM   6007  N  N   . LEU   B  1 328 ? -23.943 13.449  -27.844  1.00 29.53  ? 629  LEU   B N   1 
ATOM   6008  C  CA  . LEU   B  1 328 ? -23.078 13.041  -26.739  1.00 32.18  ? 629  LEU   B CA  1 
ATOM   6009  C  C   . LEU   B  1 328 ? -23.412 13.813  -25.467  1.00 30.22  ? 629  LEU   B C   1 
ATOM   6010  O  O   . LEU   B  1 328 ? -22.538 14.145  -24.662  1.00 28.31  ? 629  LEU   B O   1 
ATOM   6011  C  CB  . LEU   B  1 328 ? -21.604 13.184  -27.103  1.00 31.24  ? 629  LEU   B CB  1 
ATOM   6012  C  CG  . LEU   B  1 328 ? -21.227 12.490  -28.423  1.00 37.82  ? 629  LEU   B CG  1 
ATOM   6013  C  CD1 . LEU   B  1 328 ? -19.726 12.473  -28.601  1.00 30.02  ? 629  LEU   B CD1 1 
ATOM   6014  C  CD2 . LEU   B  1 328 ? -21.779 11.074  -28.476  1.00 33.40  ? 629  LEU   B CD2 1 
ATOM   6015  N  N   . TRP   B  1 329 ? -24.701 14.097  -25.283  1.00 32.70  ? 630  TRP   B N   1 
ATOM   6016  C  CA  . TRP   B  1 329 ? -25.133 14.772  -24.068  1.00 31.23  ? 630  TRP   B CA  1 
ATOM   6017  C  C   . TRP   B  1 329 ? -24.838 13.933  -22.829  1.00 30.22  ? 630  TRP   B C   1 
ATOM   6018  O  O   . TRP   B  1 329 ? -24.469 14.481  -21.788  1.00 30.26  ? 630  TRP   B O   1 
ATOM   6019  C  CB  . TRP   B  1 329 ? -26.617 15.120  -24.155  1.00 29.98  ? 630  TRP   B CB  1 
ATOM   6020  C  CG  . TRP   B  1 329 ? -27.561 13.947  -24.233  1.00 38.01  ? 630  TRP   B CG  1 
ATOM   6021  C  CD1 . TRP   B  1 329 ? -28.064 13.366  -25.366  1.00 40.58  ? 630  TRP   B CD1 1 
ATOM   6022  C  CD2 . TRP   B  1 329 ? -28.146 13.249  -23.133  1.00 29.33  ? 630  TRP   B CD2 1 
ATOM   6023  N  NE1 . TRP   B  1 329 ? -28.920 12.346  -25.033  1.00 38.19  ? 630  TRP   B NE1 1 
ATOM   6024  C  CE2 . TRP   B  1 329 ? -28.984 12.253  -23.666  1.00 32.33  ? 630  TRP   B CE2 1 
ATOM   6025  C  CE3 . TRP   B  1 329 ? -28.047 13.374  -21.747  1.00 39.05  ? 630  TRP   B CE3 1 
ATOM   6026  C  CZ2 . TRP   B  1 329 ? -29.715 11.385  -22.860  1.00 32.32  ? 630  TRP   B CZ2 1 
ATOM   6027  C  CZ3 . TRP   B  1 329 ? -28.771 12.510  -20.945  1.00 41.73  ? 630  TRP   B CZ3 1 
ATOM   6028  C  CH2 . TRP   B  1 329 ? -29.593 11.525  -21.504  1.00 35.36  ? 630  TRP   B CH2 1 
ATOM   6029  N  N   . LYS   B  1 330 ? -24.979 12.604  -22.916  1.00 27.42  ? 631  LYS   B N   1 
ATOM   6030  C  CA  . LYS   B  1 330 ? -24.621 11.780  -21.767  1.00 27.16  ? 631  LYS   B CA  1 
ATOM   6031  C  C   . LYS   B  1 330 ? -23.138 11.904  -21.448  1.00 33.42  ? 631  LYS   B C   1 
ATOM   6032  O  O   . LYS   B  1 330 ? -22.753 12.043  -20.275  1.00 28.86  ? 631  LYS   B O   1 
ATOM   6033  C  CB  . LYS   B  1 330 ? -24.983 10.318  -22.000  1.00 28.86  ? 631  LYS   B CB  1 
ATOM   6034  C  CG  . LYS   B  1 330 ? -26.465 10.049  -22.034  1.00 33.58  ? 631  LYS   B CG  1 
ATOM   6035  C  CD  . LYS   B  1 330 ? -26.715 8.554   -22.086  1.00 36.51  ? 631  LYS   B CD  1 
ATOM   6036  C  CE  . LYS   B  1 330 ? -28.185 8.241   -21.904  1.00 39.15  ? 631  LYS   B CE  1 
ATOM   6037  N  NZ  . LYS   B  1 330 ? -28.427 6.779   -21.961  1.00 34.51  ? 631  LYS   B NZ  1 
ATOM   6038  N  N   . ASP   B  1 331 ? -22.292 11.862  -22.480  1.00 28.85  ? 632  ASP   B N   1 
ATOM   6039  C  CA  . ASP   B  1 331 ? -20.850 11.969  -22.270  1.00 26.71  ? 632  ASP   B CA  1 
ATOM   6040  C  C   . ASP   B  1 331 ? -20.491 13.309  -21.646  1.00 27.34  ? 632  ASP   B C   1 
ATOM   6041  O  O   . ASP   B  1 331 ? -19.661 13.374  -20.729  1.00 29.09  ? 632  ASP   B O   1 
ATOM   6042  C  CB  . ASP   B  1 331 ? -20.111 11.788  -23.599  1.00 33.46  ? 632  ASP   B CB  1 
ATOM   6043  C  CG  . ASP   B  1 331 ? -20.658 10.627  -24.418  1.00 33.02  ? 632  ASP   B CG  1 
ATOM   6044  O  OD1 . ASP   B  1 331 ? -21.806 10.729  -24.896  1.00 30.42  ? 632  ASP   B OD1 1 
ATOM   6045  O  OD2 . ASP   B  1 331 ? -19.950 9.612   -24.566  1.00 31.42  ? 632  ASP   B OD2 1 
ATOM   6046  N  N   . GLN   B  1 332 ? -21.126 14.389  -22.123  1.00 27.47  ? 633  GLN   B N   1 
ATOM   6047  C  CA  . GLN   B  1 332 ? -20.841 15.720  -21.599  1.00 28.47  ? 633  GLN   B CA  1 
ATOM   6048  C  C   . GLN   B  1 332 ? -21.231 15.835  -20.133  1.00 27.39  ? 633  GLN   B C   1 
ATOM   6049  O  O   . GLN   B  1 332 ? -20.471 16.362  -19.315  1.00 30.59  ? 633  GLN   B O   1 
ATOM   6050  C  CB  . GLN   B  1 332 ? -21.583 16.778  -22.414  1.00 31.36  ? 633  GLN   B CB  1 
ATOM   6051  C  CG  . GLN   B  1 332 ? -20.695 17.509  -23.385  1.00 49.48  ? 633  GLN   B CG  1 
ATOM   6052  C  CD  . GLN   B  1 332 ? -21.406 18.653  -24.066  1.00 53.53  ? 633  GLN   B CD  1 
ATOM   6053  O  OE1 . GLN   B  1 332 ? -22.530 18.506  -24.545  1.00 49.65  ? 633  GLN   B OE1 1 
ATOM   6054  N  NE2 . GLN   B  1 332 ? -20.759 19.807  -24.097  1.00 66.61  ? 633  GLN   B NE2 1 
ATOM   6055  N  N   . ALA   B  1 333 ? -22.443 15.391  -19.799  1.00 26.83  ? 634  ALA   B N   1 
ATOM   6056  C  CA  . ALA   B  1 333 ? -22.897 15.430  -18.417  1.00 28.96  ? 634  ALA   B CA  1 
ATOM   6057  C  C   . ALA   B  1 333 ? -22.024 14.553  -17.528  1.00 30.61  ? 634  ALA   B C   1 
ATOM   6058  O  O   . ALA   B  1 333 ? -21.704 14.929  -16.397  1.00 30.34  ? 634  ALA   B O   1 
ATOM   6059  C  CB  . ALA   B  1 333 ? -24.357 14.991  -18.339  1.00 28.57  ? 634  ALA   B CB  1 
ATOM   6060  N  N   . LEU   B  1 334 ? -21.622 13.384  -18.031  1.00 32.89  ? 635  LEU   B N   1 
ATOM   6061  C  CA  . LEU   B  1 334 ? -20.791 12.472  -17.252  1.00 23.99  ? 635  LEU   B CA  1 
ATOM   6062  C  C   . LEU   B  1 334 ? -19.483 13.130  -16.828  1.00 28.52  ? 635  LEU   B C   1 
ATOM   6063  O  O   . LEU   B  1 334 ? -19.061 13.000  -15.670  1.00 31.86  ? 635  LEU   B O   1 
ATOM   6064  C  CB  . LEU   B  1 334 ? -20.514 11.212  -18.069  1.00 25.35  ? 635  LEU   B CB  1 
ATOM   6065  C  CG  . LEU   B  1 334 ? -19.667 10.131  -17.404  1.00 28.49  ? 635  LEU   B CG  1 
ATOM   6066  C  CD1 . LEU   B  1 334 ? -20.407 9.515   -16.230  1.00 28.32  ? 635  LEU   B CD1 1 
ATOM   6067  C  CD2 . LEU   B  1 334 ? -19.294 9.065   -18.433  1.00 27.34  ? 635  LEU   B CD2 1 
ATOM   6068  N  N   . VAL   B  1 335 ? -18.828 13.854  -17.741  1.00 24.35  ? 636  VAL   B N   1 
ATOM   6069  C  CA  . VAL   B  1 335 ? -17.564 14.496  -17.387  1.00 31.08  ? 636  VAL   B CA  1 
ATOM   6070  C  C   . VAL   B  1 335 ? -17.784 15.517  -16.276  1.00 34.63  ? 636  VAL   B C   1 
ATOM   6071  O  O   . VAL   B  1 335 ? -17.054 15.539  -15.275  1.00 24.33  ? 636  VAL   B O   1 
ATOM   6072  C  CB  . VAL   B  1 335 ? -16.907 15.136  -18.622  1.00 34.86  ? 636  VAL   B CB  1 
ATOM   6073  C  CG1 . VAL   B  1 335 ? -15.702 15.950  -18.202  1.00 32.45  ? 636  VAL   B CG1 1 
ATOM   6074  C  CG2 . VAL   B  1 335 ? -16.506 14.054  -19.643  1.00 28.71  ? 636  VAL   B CG2 1 
ATOM   6075  N  N   . GLU   B  1 336 ? -18.810 16.363  -16.424  1.00 29.24  ? 637  GLU   B N   1 
ATOM   6076  C  CA  . GLU   B  1 336 ? -19.071 17.394  -15.422  1.00 34.05  ? 637  GLU   B CA  1 
ATOM   6077  C  C   . GLU   B  1 336 ? -19.358 16.788  -14.055  1.00 33.54  ? 637  GLU   B C   1 
ATOM   6078  O  O   . GLU   B  1 336 ? -18.901 17.310  -13.034  1.00 29.04  ? 637  GLU   B O   1 
ATOM   6079  C  CB  . GLU   B  1 336 ? -20.242 18.278  -15.847  1.00 28.99  ? 637  GLU   B CB  1 
ATOM   6080  C  CG  . GLU   B  1 336 ? -20.058 18.967  -17.183  1.00 36.49  ? 637  GLU   B CG  1 
ATOM   6081  C  CD  . GLU   B  1 336 ? -18.920 19.973  -17.185  1.00 41.66  ? 637  GLU   B CD  1 
ATOM   6082  O  OE1 . GLU   B  1 336 ? -18.395 20.321  -16.104  1.00 43.00  ? 637  GLU   B OE1 1 
ATOM   6083  O  OE2 . GLU   B  1 336 ? -18.548 20.420  -18.284  1.00 46.47  ? 637  GLU   B OE2 1 
ATOM   6084  N  N   . ILE   B  1 337 ? -20.136 15.703  -14.021  1.00 33.16  ? 638  ILE   B N   1 
ATOM   6085  C  CA  . ILE   B  1 337 ? -20.431 15.025  -12.767  1.00 29.31  ? 638  ILE   B CA  1 
ATOM   6086  C  C   . ILE   B  1 337 ? -19.148 14.556  -12.117  1.00 30.42  ? 638  ILE   B C   1 
ATOM   6087  O  O   . ILE   B  1 337 ? -18.968 14.660  -10.895  1.00 24.58  ? 638  ILE   B O   1 
ATOM   6088  C  CB  . ILE   B  1 337 ? -21.394 13.850  -13.010  1.00 25.16  ? 638  ILE   B CB  1 
ATOM   6089  C  CG1 . ILE   B  1 337 ? -22.773 14.369  -13.405  1.00 30.69  ? 638  ILE   B CG1 1 
ATOM   6090  C  CG2 . ILE   B  1 337 ? -21.477 12.931  -11.780  1.00 25.50  ? 638  ILE   B CG2 1 
ATOM   6091  C  CD1 . ILE   B  1 337 ? -23.607 13.326  -14.103  1.00 33.52  ? 638  ILE   B CD1 1 
ATOM   6092  N  N   . ASN   B  1 338 ? -18.231 14.037  -12.918  1.00 28.05  ? 639  ASN   B N   1 
ATOM   6093  C  CA  . ASN   B  1 338 ? -17.007 13.529  -12.335  1.00 26.00  ? 639  ASN   B CA  1 
ATOM   6094  C  C   . ASN   B  1 338 ? -16.077 14.652  -11.916  1.00 27.50  ? 639  ASN   B C   1 
ATOM   6095  O  O   . ASN   B  1 338 ? -15.345 14.500  -10.933  1.00 29.80  ? 639  ASN   B O   1 
ATOM   6096  C  CB  . ASN   B  1 338 ? -16.352 12.569  -13.316  1.00 23.80  ? 639  ASN   B CB  1 
ATOM   6097  C  CG  . ASN   B  1 338 ? -16.958 11.208  -13.213  1.00 26.59  ? 639  ASN   B CG  1 
ATOM   6098  O  OD1 . ASN   B  1 338 ? -16.544 10.396  -12.376  1.00 27.19  ? 639  ASN   B OD1 1 
ATOM   6099  N  ND2 . ASN   B  1 338 ? -17.998 10.967  -14.001  1.00 28.70  ? 639  ASN   B ND2 1 
ATOM   6100  N  N   . ILE   B  1 339 ? -16.114 15.782  -12.625  1.00 25.12  ? 640  ILE   B N   1 
ATOM   6101  C  CA  . ILE   B  1 339 ? -15.430 16.984  -12.162  1.00 24.37  ? 640  ILE   B CA  1 
ATOM   6102  C  C   . ILE   B  1 339 ? -15.954 17.378  -10.789  1.00 31.68  ? 640  ILE   B C   1 
ATOM   6103  O  O   . ILE   B  1 339 ? -15.183 17.688  -9.876   1.00 27.68  ? 640  ILE   B O   1 
ATOM   6104  C  CB  . ILE   B  1 339 ? -15.603 18.127  -13.182  1.00 25.32  ? 640  ILE   B CB  1 
ATOM   6105  C  CG1 . ILE   B  1 339 ? -14.856 17.816  -14.495  1.00 26.35  ? 640  ILE   B CG1 1 
ATOM   6106  C  CG2 . ILE   B  1 339 ? -15.155 19.474  -12.594  1.00 26.10  ? 640  ILE   B CG2 1 
ATOM   6107  C  CD1 . ILE   B  1 339 ? -15.007 18.888  -15.562  1.00 29.10  ? 640  ILE   B CD1 1 
ATOM   6108  N  N   . ALA   B  1 340 ? -17.278 17.353  -10.624  1.00 28.19  ? 641  ALA   B N   1 
ATOM   6109  C  CA  . ALA   B  1 340 ? -17.876 17.761  -9.363   1.00 33.90  ? 641  ALA   B CA  1 
ATOM   6110  C  C   . ALA   B  1 340 ? -17.447 16.841  -8.231   1.00 36.24  ? 641  ALA   B C   1 
ATOM   6111  O  O   . ALA   B  1 340 ? -17.098 17.306  -7.141   1.00 29.12  ? 641  ALA   B O   1 
ATOM   6112  C  CB  . ALA   B  1 340 ? -19.399 17.787  -9.489   1.00 33.25  ? 641  ALA   B CB  1 
ATOM   6113  N  N   . VAL   B  1 341 ? -17.466 15.531  -8.477   1.00 26.89  ? 642  VAL   B N   1 
ATOM   6114  C  CA  . VAL   B  1 341 ? -17.056 14.575  -7.460   1.00 31.39  ? 642  VAL   B CA  1 
ATOM   6115  C  C   . VAL   B  1 341 ? -15.636 14.875  -6.992   1.00 27.70  ? 642  VAL   B C   1 
ATOM   6116  O  O   . VAL   B  1 341 ? -15.374 14.974  -5.790   1.00 27.87  ? 642  VAL   B O   1 
ATOM   6117  C  CB  . VAL   B  1 341 ? -17.207 13.140  -7.995   1.00 25.26  ? 642  VAL   B CB  1 
ATOM   6118  C  CG1 . VAL   B  1 341 ? -16.528 12.147  -7.078   1.00 24.94  ? 642  VAL   B CG1 1 
ATOM   6119  C  CG2 . VAL   B  1 341 ? -18.695 12.806  -8.119   1.00 22.08  ? 642  VAL   B CG2 1 
ATOM   6120  N  N   . LEU   B  1 342 ? -14.708 15.065  -7.931   1.00 25.63  ? 643  LEU   B N   1 
ATOM   6121  C  CA  . LEU   B  1 342 ? -13.316 15.288  -7.542   1.00 27.24  ? 643  LEU   B CA  1 
ATOM   6122  C  C   . LEU   B  1 342 ? -13.150 16.622  -6.833   1.00 27.85  ? 643  LEU   B C   1 
ATOM   6123  O  O   . LEU   B  1 342 ? -12.492 16.707  -5.792   1.00 30.52  ? 643  LEU   B O   1 
ATOM   6124  C  CB  . LEU   B  1 342 ? -12.404 15.223  -8.765   1.00 22.68  ? 643  LEU   B CB  1 
ATOM   6125  C  CG  . LEU   B  1 342 ? -12.274 13.809  -9.335   1.00 23.07  ? 643  LEU   B CG  1 
ATOM   6126  C  CD1 . LEU   B  1 342 ? -11.760 13.853  -10.775  1.00 27.32  ? 643  LEU   B CD1 1 
ATOM   6127  C  CD2 . LEU   B  1 342 ? -11.392 12.957  -8.461   1.00 22.61  ? 643  LEU   B CD2 1 
ATOM   6128  N  N   . TYR   B  1 343 ? -13.727 17.676  -7.401   1.00 24.76  ? 644  TYR   B N   1 
ATOM   6129  C  CA  . TYR   B  1 343 ? -13.665 18.990  -6.780   1.00 28.23  ? 644  TYR   B CA  1 
ATOM   6130  C  C   . TYR   B  1 343 ? -14.206 18.961  -5.359   1.00 35.88  ? 644  TYR   B C   1 
ATOM   6131  O  O   . TYR   B  1 343 ? -13.650 19.598  -4.456   1.00 27.50  ? 644  TYR   B O   1 
ATOM   6132  C  CB  . TYR   B  1 343 ? -14.464 19.975  -7.617   1.00 26.30  ? 644  TYR   B CB  1 
ATOM   6133  C  CG  . TYR   B  1 343 ? -14.661 21.325  -6.984   1.00 30.67  ? 644  TYR   B CG  1 
ATOM   6134  C  CD1 . TYR   B  1 343 ? -13.618 22.232  -6.920   1.00 31.67  ? 644  TYR   B CD1 1 
ATOM   6135  C  CD2 . TYR   B  1 343 ? -15.905 21.720  -6.510   1.00 27.59  ? 644  TYR   B CD2 1 
ATOM   6136  C  CE1 . TYR   B  1 343 ? -13.794 23.487  -6.387   1.00 34.58  ? 644  TYR   B CE1 1 
ATOM   6137  C  CE2 . TYR   B  1 343 ? -16.093 22.981  -5.966   1.00 35.55  ? 644  TYR   B CE2 1 
ATOM   6138  C  CZ  . TYR   B  1 343 ? -15.029 23.858  -5.907   1.00 34.96  ? 644  TYR   B CZ  1 
ATOM   6139  O  OH  . TYR   B  1 343 ? -15.179 25.117  -5.384   1.00 38.39  ? 644  TYR   B OH  1 
ATOM   6140  N  N   . SER   B  1 344 ? -15.316 18.256  -5.156   1.00 29.59  ? 645  SER   B N   1 
ATOM   6141  C  CA  . SER   B  1 344 ? -15.970 18.275  -3.862   1.00 28.90  ? 645  SER   B CA  1 
ATOM   6142  C  C   . SER   B  1 344 ? -15.104 17.598  -2.810   1.00 26.01  ? 645  SER   B C   1 
ATOM   6143  O  O   . SER   B  1 344 ? -14.874 18.161  -1.736   1.00 29.63  ? 645  SER   B O   1 
ATOM   6144  C  CB  . SER   B  1 344 ? -17.340 17.615  -3.984   1.00 25.76  ? 645  SER   B CB  1 
ATOM   6145  O  OG  . SER   B  1 344 ? -18.174 18.415  -4.816   1.00 31.34  ? 645  SER   B OG  1 
ATOM   6146  N  N   . PHE   B  1 345 ? -14.589 16.403  -3.124   1.00 23.06  ? 646  PHE   B N   1 
ATOM   6147  C  CA  . PHE   B  1 345 ? -13.722 15.681  -2.197   1.00 30.02  ? 646  PHE   B CA  1 
ATOM   6148  C  C   . PHE   B  1 345 ? -12.458 16.477  -1.905   1.00 36.36  ? 646  PHE   B C   1 
ATOM   6149  O  O   . PHE   B  1 345 ? -12.050 16.620  -0.741   1.00 29.09  ? 646  PHE   B O   1 
ATOM   6150  C  CB  . PHE   B  1 345 ? -13.367 14.307  -2.769   1.00 21.80  ? 646  PHE   B CB  1 
ATOM   6151  C  CG  . PHE   B  1 345 ? -14.358 13.218  -2.434   1.00 21.24  ? 646  PHE   B CG  1 
ATOM   6152  C  CD1 . PHE   B  1 345 ? -15.674 13.293  -2.860   1.00 25.96  ? 646  PHE   B CD1 1 
ATOM   6153  C  CD2 . PHE   B  1 345 ? -13.947 12.086  -1.726   1.00 23.81  ? 646  PHE   B CD2 1 
ATOM   6154  C  CE1 . PHE   B  1 345 ? -16.581 12.276  -2.566   1.00 24.69  ? 646  PHE   B CE1 1 
ATOM   6155  C  CE2 . PHE   B  1 345 ? -14.846 11.063  -1.410   1.00 20.84  ? 646  PHE   B CE2 1 
ATOM   6156  C  CZ  . PHE   B  1 345 ? -16.170 11.160  -1.830   1.00 25.95  ? 646  PHE   B CZ  1 
ATOM   6157  N  N   . GLN   B  1 346 ? -11.826 17.009  -2.954   1.00 31.16  ? 647  GLN   B N   1 
ATOM   6158  C  CA  . GLN   B  1 346 ? -10.608 17.786  -2.756   1.00 32.08  ? 647  GLN   B CA  1 
ATOM   6159  C  C   . GLN   B  1 346 ? -10.882 19.026  -1.919   1.00 33.68  ? 647  GLN   B C   1 
ATOM   6160  O  O   . GLN   B  1 346 ? -10.097 19.364  -1.027   1.00 35.71  ? 647  GLN   B O   1 
ATOM   6161  C  CB  . GLN   B  1 346 ? -9.998  18.152  -4.106   1.00 28.17  ? 647  GLN   B CB  1 
ATOM   6162  C  CG  . GLN   B  1 346 ? -9.318  16.963  -4.758   1.00 32.33  ? 647  GLN   B CG  1 
ATOM   6163  C  CD  . GLN   B  1 346 ? -9.019  17.184  -6.230   1.00 39.71  ? 647  GLN   B CD  1 
ATOM   6164  O  OE1 . GLN   B  1 346 ? -9.342  18.229  -6.796   1.00 42.91  ? 647  GLN   B OE1 1 
ATOM   6165  N  NE2 . GLN   B  1 346 ? -8.410  16.191  -6.855   1.00 36.08  ? 647  GLN   B NE2 1 
ATOM   6166  N  N   . SER   B  1 347 ? -12.008 19.696  -2.172   1.00 30.14  ? 648  SER   B N   1 
ATOM   6167  C  CA  . SER   B  1 347 ? -12.375 20.861  -1.380   1.00 31.43  ? 648  SER   B CA  1 
ATOM   6168  C  C   . SER   B  1 347 ? -12.565 20.496  0.089    1.00 40.48  ? 648  SER   B C   1 
ATOM   6169  O  O   . SER   B  1 347 ? -12.167 21.253  0.985    1.00 34.89  ? 648  SER   B O   1 
ATOM   6170  C  CB  . SER   B  1 347 ? -13.642 21.488  -1.947   1.00 31.01  ? 648  SER   B CB  1 
ATOM   6171  O  OG  . SER   B  1 347 ? -13.365 22.105  -3.193   1.00 33.14  ? 648  SER   B OG  1 
ATOM   6172  N  N   . ASP   B  1 348 ? -13.163 19.344  0.360    1.00 31.62  ? 649  ASP   B N   1 
ATOM   6173  C  CA  . ASP   B  1 348 ? -13.347 18.936  1.742    1.00 31.47  ? 649  ASP   B CA  1 
ATOM   6174  C  C   . ASP   B  1 348 ? -12.127 18.220  2.307    1.00 32.55  ? 649  ASP   B C   1 
ATOM   6175  O  O   . ASP   B  1 348 ? -12.162 17.778  3.461    1.00 27.62  ? 649  ASP   B O   1 
ATOM   6176  C  CB  . ASP   B  1 348 ? -14.610 18.074  1.860    1.00 30.78  ? 649  ASP   B CB  1 
ATOM   6177  C  CG  . ASP   B  1 348 ? -15.886 18.902  1.683    1.00 34.10  ? 649  ASP   B CG  1 
ATOM   6178  O  OD1 . ASP   B  1 348 ? -15.761 20.140  1.608    1.00 31.44  ? 649  ASP   B OD1 1 
ATOM   6179  O  OD2 . ASP   B  1 348 ? -17.002 18.337  1.608    1.00 33.70  ? 649  ASP   B OD2 1 
ATOM   6180  N  N   . LYS   B  1 349 ? -11.040 18.126  1.536    1.00 29.04  ? 650  LYS   B N   1 
ATOM   6181  C  CA  . LYS   B  1 349 ? -9.810  17.485  1.999    1.00 30.62  ? 650  LYS   B CA  1 
ATOM   6182  C  C   . LYS   B  1 349 ? -10.080 16.041  2.405    1.00 31.06  ? 650  LYS   B C   1 
ATOM   6183  O  O   . LYS   B  1 349 ? -9.609  15.558  3.435    1.00 31.80  ? 650  LYS   B O   1 
ATOM   6184  C  CB  . LYS   B  1 349 ? -9.172  18.279  3.142    1.00 38.54  ? 650  LYS   B CB  1 
ATOM   6185  C  CG  . LYS   B  1 349 ? -8.799  19.697  2.739    1.00 50.09  ? 650  LYS   B CG  1 
ATOM   6186  C  CD  . LYS   B  1 349 ? -8.034  20.419  3.839    1.00 64.85  ? 650  LYS   B CD  1 
ATOM   6187  C  CE  . LYS   B  1 349 ? -6.698  20.941  3.325    1.00 76.78  ? 650  LYS   B CE  1 
ATOM   6188  N  NZ  . LYS   B  1 349 ? -5.926  21.638  4.395    1.00 85.27  ? 650  LYS   B NZ  1 
ATOM   6189  N  N   . VAL   B  1 350 ? -10.880 15.359  1.598    1.00 28.09  ? 651  VAL   B N   1 
ATOM   6190  C  CA  . VAL   B  1 350 ? -11.127 13.935  1.730    1.00 23.67  ? 651  VAL   B CA  1 
ATOM   6191  C  C   . VAL   B  1 350 ? -10.355 13.256  0.608    1.00 29.12  ? 651  VAL   B C   1 
ATOM   6192  O  O   . VAL   B  1 350 ? -10.518 13.615  -0.566   1.00 22.24  ? 651  VAL   B O   1 
ATOM   6193  C  CB  . VAL   B  1 350 ? -12.629 13.625  1.642    1.00 28.27  ? 651  VAL   B CB  1 
ATOM   6194  C  CG1 . VAL   B  1 350 ? -12.884 12.122  1.652    1.00 26.16  ? 651  VAL   B CG1 1 
ATOM   6195  C  CG2 . VAL   B  1 350 ? -13.386 14.332  2.744    1.00 22.04  ? 651  VAL   B CG2 1 
ATOM   6196  N  N   . THR   B  1 351 ? -9.502  12.300  0.969    1.00 24.37  ? 652  THR   B N   1 
ATOM   6197  C  CA  . THR   B  1 351 ? -8.690  11.607  -0.015   1.00 25.43  ? 652  THR   B CA  1 
ATOM   6198  C  C   . THR   B  1 351 ? -9.555  11.050  -1.134   1.00 27.17  ? 652  THR   B C   1 
ATOM   6199  O  O   . THR   B  1 351 ? -10.587 10.416  -0.894   1.00 26.30  ? 652  THR   B O   1 
ATOM   6200  C  CB  . THR   B  1 351 ? -7.900  10.470  0.630    1.00 27.06  ? 652  THR   B CB  1 
ATOM   6201  O  OG1 . THR   B  1 351 ? -7.212  10.962  1.789    1.00 32.57  ? 652  THR   B OG1 1 
ATOM   6202  C  CG2 . THR   B  1 351 ? -6.883  9.928   -0.361   1.00 23.63  ? 652  THR   B CG2 1 
ATOM   6203  N  N   . ILE   B  1 352 ? -9.127  11.327  -2.363   1.00 22.21  ? 653  ILE   B N   1 
ATOM   6204  C  CA  . ILE   B  1 352 ? -9.720  10.772  -3.565   1.00 22.06  ? 653  ILE   B CA  1 
ATOM   6205  C  C   . ILE   B  1 352 ? -8.640  10.817  -4.632   1.00 25.46  ? 653  ILE   B C   1 
ATOM   6206  O  O   . ILE   B  1 352 ? -7.716  11.632  -4.571   1.00 27.95  ? 653  ILE   B O   1 
ATOM   6207  C  CB  . ILE   B  1 352 ? -10.974 11.560  -4.008   1.00 22.73  ? 653  ILE   B CB  1 
ATOM   6208  C  CG1 . ILE   B  1 352 ? -11.800 10.745  -5.018   1.00 22.53  ? 653  ILE   B CG1 1 
ATOM   6209  C  CG2 . ILE   B  1 352 ? -10.554 12.944  -4.545   1.00 21.19  ? 653  ILE   B CG2 1 
ATOM   6210  C  CD1 . ILE   B  1 352 ? -13.235 11.223  -5.156   1.00 22.60  ? 653  ILE   B CD1 1 
ATOM   6211  N  N   . VAL   B  1 353 ? -8.742  9.924   -5.607   1.00 25.74  ? 654  VAL   B N   1 
ATOM   6212  C  CA  . VAL   B  1 353 ? -7.792  9.887   -6.710   1.00 22.71  ? 654  VAL   B CA  1 
ATOM   6213  C  C   . VAL   B  1 353 ? -8.580  9.894   -8.018   1.00 21.27  ? 654  VAL   B C   1 
ATOM   6214  O  O   . VAL   B  1 353 ? -9.584  9.186   -8.146   1.00 22.97  ? 654  VAL   B O   1 
ATOM   6215  C  CB  . VAL   B  1 353 ? -6.855  8.663   -6.614   1.00 27.05  ? 654  VAL   B CB  1 
ATOM   6216  C  CG1 . VAL   B  1 353 ? -7.619  7.346   -6.771   1.00 19.74  ? 654  VAL   B CG1 1 
ATOM   6217  C  CG2 . VAL   B  1 353 ? -5.732  8.758   -7.638   1.00 23.92  ? 654  VAL   B CG2 1 
ATOM   6218  N  N   . ASP   B  1 354 ? -8.161  10.725  -8.968   1.00 21.16  ? 655  ASP   B N   1 
ATOM   6219  C  CA  . ASP   B  1 354 ? -8.851  10.719  -10.246  1.00 25.94  ? 655  ASP   B CA  1 
ATOM   6220  C  C   . ASP   B  1 354 ? -8.320  9.575   -11.106  1.00 28.46  ? 655  ASP   B C   1 
ATOM   6221  O  O   . ASP   B  1 354 ? -7.228  9.046   -10.879  1.00 26.21  ? 655  ASP   B O   1 
ATOM   6222  C  CB  . ASP   B  1 354 ? -8.701  12.062  -10.973  1.00 25.23  ? 655  ASP   B CB  1 
ATOM   6223  C  CG  . ASP   B  1 354 ? -7.280  12.336  -11.430  1.00 31.92  ? 655  ASP   B CG  1 
ATOM   6224  O  OD1 . ASP   B  1 354 ? -6.571  13.111  -10.757  1.00 41.95  ? 655  ASP   B OD1 1 
ATOM   6225  O  OD2 . ASP   B  1 354 ? -6.859  11.781  -12.459  1.00 33.59  ? 655  ASP   B OD2 1 
ATOM   6226  N  N   . HIS   B  1 355 ? -9.112  9.180   -12.101  1.00 29.57  ? 656  HIS   B N   1 
ATOM   6227  C  CA  . HIS   B  1 355 ? -8.726  8.008   -12.880  1.00 25.62  ? 656  HIS   B CA  1 
ATOM   6228  C  C   . HIS   B  1 355 ? -7.409  8.219   -13.621  1.00 26.30  ? 656  HIS   B C   1 
ATOM   6229  O  O   . HIS   B  1 355 ? -6.667  7.257   -13.837  1.00 29.26  ? 656  HIS   B O   1 
ATOM   6230  C  CB  . HIS   B  1 355 ? -9.845  7.614   -13.842  1.00 23.56  ? 656  HIS   B CB  1 
ATOM   6231  C  CG  . HIS   B  1 355 ? -10.360 8.737   -14.682  1.00 25.40  ? 656  HIS   B CG  1 
ATOM   6232  N  ND1 . HIS   B  1 355 ? -11.118 9.770   -14.168  1.00 29.29  ? 656  HIS   B ND1 1 
ATOM   6233  C  CD2 . HIS   B  1 355 ? -10.271 8.961   -16.017  1.00 21.24  ? 656  HIS   B CD2 1 
ATOM   6234  C  CE1 . HIS   B  1 355 ? -11.449 10.597  -15.146  1.00 30.15  ? 656  HIS   B CE1 1 
ATOM   6235  N  NE2 . HIS   B  1 355 ? -10.944 10.132  -16.277  1.00 27.21  ? 656  HIS   B NE2 1 
ATOM   6236  N  N   . HIS   B  1 356 ? -7.061  9.454   -13.979  1.00 21.02  ? 657  HIS   B N   1 
ATOM   6237  C  CA  . HIS   B  1 356 ? -5.793  9.624   -14.681  1.00 26.76  ? 657  HIS   B CA  1 
ATOM   6238  C  C   . HIS   B  1 356 ? -4.624  9.340   -13.752  1.00 26.10  ? 657  HIS   B C   1 
ATOM   6239  O  O   . HIS   B  1 356 ? -3.753  8.519   -14.059  1.00 28.52  ? 657  HIS   B O   1 
ATOM   6240  C  CB  . HIS   B  1 356 ? -5.698  11.019  -15.283  1.00 28.39  ? 657  HIS   B CB  1 
ATOM   6241  C  CG  . HIS   B  1 356 ? -6.816  11.333  -16.217  1.00 30.70  ? 657  HIS   B CG  1 
ATOM   6242  N  ND1 . HIS   B  1 356 ? -6.941  10.734  -17.451  1.00 30.75  ? 657  HIS   B ND1 1 
ATOM   6243  C  CD2 . HIS   B  1 356 ? -7.883  12.156  -16.085  1.00 34.46  ? 657  HIS   B CD2 1 
ATOM   6244  C  CE1 . HIS   B  1 356 ? -8.031  11.183  -18.047  1.00 33.83  ? 657  HIS   B CE1 1 
ATOM   6245  N  NE2 . HIS   B  1 356 ? -8.621  12.048  -17.239  1.00 35.32  ? 657  HIS   B NE2 1 
ATOM   6246  N  N   . SER   B  1 357 ? -4.616  9.977   -12.587  1.00 26.67  ? 658  SER   B N   1 
ATOM   6247  C  CA  . SER   B  1 357 ? -3.560  9.719   -11.621  1.00 25.66  ? 658  SER   B CA  1 
ATOM   6248  C  C   . SER   B  1 357 ? -3.527  8.249   -11.205  1.00 20.84  ? 658  SER   B C   1 
ATOM   6249  O  O   . SER   B  1 357 ? -2.450  7.651   -11.080  1.00 22.54  ? 658  SER   B O   1 
ATOM   6250  C  CB  . SER   B  1 357 ? -3.751  10.638  -10.410  1.00 24.84  ? 658  SER   B CB  1 
ATOM   6251  O  OG  . SER   B  1 357 ? -2.805  10.325  -9.411   1.00 40.99  ? 658  SER   B OG  1 
ATOM   6252  N  N   . ALA   B  1 358 ? -4.700  7.640   -11.002  1.00 21.94  ? 659  ALA   B N   1 
ATOM   6253  C  CA  . ALA   B  1 358 ? -4.736  6.275   -10.482  1.00 23.20  ? 659  ALA   B CA  1 
ATOM   6254  C  C   . ALA   B  1 358 ? -4.172  5.285   -11.486  1.00 27.28  ? 659  ALA   B C   1 
ATOM   6255  O  O   . ALA   B  1 358 ? -3.400  4.387   -11.122  1.00 21.82  ? 659  ALA   B O   1 
ATOM   6256  C  CB  . ALA   B  1 358 ? -6.167  5.891   -10.114  1.00 23.27  ? 659  ALA   B CB  1 
ATOM   6257  N  N   . THR   B  1 359 ? -4.564  5.416   -12.755  1.00 23.86  ? 660  THR   B N   1 
ATOM   6258  C  CA  . THR   B  1 359 ? -4.055  4.488   -13.760  1.00 19.85  ? 660  THR   B CA  1 
ATOM   6259  C  C   . THR   B  1 359 ? -2.579  4.727   -14.020  1.00 20.36  ? 660  THR   B C   1 
ATOM   6260  O  O   . THR   B  1 359 ? -1.821  3.776   -14.232  1.00 22.20  ? 660  THR   B O   1 
ATOM   6261  C  CB  . THR   B  1 359 ? -4.865  4.613   -15.046  1.00 22.81  ? 660  THR   B CB  1 
ATOM   6262  O  OG1 . THR   B  1 359 ? -4.875  5.980   -15.481  1.00 24.80  ? 660  THR   B OG1 1 
ATOM   6263  C  CG2 . THR   B  1 359 ? -6.294  4.136   -14.810  1.00 19.48  ? 660  THR   B CG2 1 
ATOM   6264  N  N   . GLU   B  1 360 ? -2.151  5.988   -13.980  1.00 20.87  ? 661  GLU   B N   1 
ATOM   6265  C  CA  . GLU   B  1 360 ? -0.733  6.288   -14.117  1.00 29.37  ? 661  GLU   B CA  1 
ATOM   6266  C  C   . GLU   B  1 360 ? 0.067   5.606   -13.014  1.00 28.73  ? 661  GLU   B C   1 
ATOM   6267  O  O   . GLU   B  1 360 ? 1.095   4.969   -13.272  1.00 26.36  ? 661  GLU   B O   1 
ATOM   6268  C  CB  . GLU   B  1 360 ? -0.523  7.806   -14.094  1.00 30.90  ? 661  GLU   B CB  1 
ATOM   6269  C  CG  . GLU   B  1 360 ? 0.934   8.236   -14.106  1.00 46.30  ? 661  GLU   B CG  1 
ATOM   6270  C  CD  . GLU   B  1 360 ? 1.706   7.650   -15.277  1.00 74.95  ? 661  GLU   B CD  1 
ATOM   6271  O  OE1 . GLU   B  1 360 ? 1.135   7.559   -16.391  1.00 90.47  ? 661  GLU   B OE1 1 
ATOM   6272  O  OE2 . GLU   B  1 360 ? 2.882   7.273   -15.083  1.00 77.36  ? 661  GLU   B OE2 1 
ATOM   6273  N  N   . SER   B  1 361 ? -0.394  5.729   -11.769  1.00 29.27  ? 662  SER   B N   1 
ATOM   6274  C  CA  A SER   B  1 361 ? 0.301   5.063   -10.678  0.61 29.41  ? 662  SER   B CA  1 
ATOM   6275  C  CA  B SER   B  1 361 ? 0.296   5.061   -10.673  0.39 29.52  ? 662  SER   B CA  1 
ATOM   6276  C  C   . SER   B  1 361 ? 0.241   3.551   -10.844  1.00 30.04  ? 662  SER   B C   1 
ATOM   6277  O  O   . SER   B  1 361 ? 1.208   2.845   -10.536  1.00 26.03  ? 662  SER   B O   1 
ATOM   6278  C  CB  A SER   B  1 361 ? -0.289  5.500   -9.336   0.61 29.63  ? 662  SER   B CB  1 
ATOM   6279  C  CB  B SER   B  1 361 ? -0.309  5.474   -9.330   0.39 29.42  ? 662  SER   B CB  1 
ATOM   6280  O  OG  A SER   B  1 361 ? -0.049  6.881   -9.118   0.61 26.58  ? 662  SER   B OG  1 
ATOM   6281  O  OG  B SER   B  1 361 ? -1.519  4.783   -9.082   0.39 30.72  ? 662  SER   B OG  1 
ATOM   6282  N  N   . PHE   B  1 362 ? -0.877  3.032   -11.356  1.00 24.04  ? 663  PHE   B N   1 
ATOM   6283  C  CA  . PHE   B  1 362 ? -0.951  1.588   -11.521  1.00 23.98  ? 663  PHE   B CA  1 
ATOM   6284  C  C   . PHE   B  1 362 ? 0.084   1.079   -12.522  1.00 28.35  ? 663  PHE   B C   1 
ATOM   6285  O  O   . PHE   B  1 362 ? 0.671   0.007   -12.322  1.00 28.72  ? 663  PHE   B O   1 
ATOM   6286  C  CB  . PHE   B  1 362 ? -2.342  1.148   -11.940  1.00 25.84  ? 663  PHE   B CB  1 
ATOM   6287  C  CG  . PHE   B  1 362 ? -2.439  -0.335  -12.104  1.00 31.29  ? 663  PHE   B CG  1 
ATOM   6288  C  CD1 . PHE   B  1 362 ? -2.527  -1.155  -10.984  1.00 21.85  ? 663  PHE   B CD1 1 
ATOM   6289  C  CD2 . PHE   B  1 362 ? -2.370  -0.915  -13.368  1.00 24.18  ? 663  PHE   B CD2 1 
ATOM   6290  C  CE1 . PHE   B  1 362 ? -2.585  -2.517  -11.124  1.00 22.84  ? 663  PHE   B CE1 1 
ATOM   6291  C  CE2 . PHE   B  1 362 ? -2.430  -2.277  -13.515  1.00 31.20  ? 663  PHE   B CE2 1 
ATOM   6292  C  CZ  . PHE   B  1 362 ? -2.537  -3.085  -12.398  1.00 30.24  ? 663  PHE   B CZ  1 
ATOM   6293  N  N   . ILE   B  1 363 ? 0.320   1.823   -13.608  1.00 28.10  ? 664  ILE   B N   1 
ATOM   6294  C  CA  . ILE   B  1 363 ? 1.351   1.428   -14.568  1.00 29.58  ? 664  ILE   B CA  1 
ATOM   6295  C  C   . ILE   B  1 363 ? 2.726   1.411   -13.902  1.00 26.01  ? 664  ILE   B C   1 
ATOM   6296  O  O   . ILE   B  1 363 ? 3.512   0.474   -14.089  1.00 28.88  ? 664  ILE   B O   1 
ATOM   6297  C  CB  . ILE   B  1 363 ? 1.339   2.353   -15.799  1.00 24.19  ? 664  ILE   B CB  1 
ATOM   6298  C  CG1 . ILE   B  1 363 ? 0.070   2.123   -16.626  1.00 26.76  ? 664  ILE   B CG1 1 
ATOM   6299  C  CG2 . ILE   B  1 363 ? 2.570   2.102   -16.674  1.00 24.55  ? 664  ILE   B CG2 1 
ATOM   6300  C  CD1 . ILE   B  1 363 ? -0.046  0.709   -17.175  1.00 27.57  ? 664  ILE   B CD1 1 
ATOM   6301  N  N   . LYS   B  1 364 ? 3.042   2.451   -13.126  1.00 25.05  ? 665  LYS   B N   1 
ATOM   6302  C  CA  . LYS   B  1 364 ? 4.308   2.447   -12.397  1.00 30.71  ? 665  LYS   B CA  1 
ATOM   6303  C  C   . LYS   B  1 364 ? 4.375   1.238   -11.476  1.00 30.51  ? 665  LYS   B C   1 
ATOM   6304  O  O   . LYS   B  1 364 ? 5.382   0.518   -11.445  1.00 30.23  ? 665  LYS   B O   1 
ATOM   6305  C  CB  . LYS   B  1 364 ? 4.488   3.739   -11.595  1.00 30.21  ? 665  LYS   B CB  1 
ATOM   6306  C  CG  . LYS   B  1 364 ? 4.354   5.033   -12.386  1.00 37.98  ? 665  LYS   B CG  1 
ATOM   6307  C  CD  . LYS   B  1 364 ? 5.666   5.463   -13.023  1.00 56.06  ? 665  LYS   B CD  1 
ATOM   6308  C  CE  . LYS   B  1 364 ? 6.244   6.699   -12.331  1.00 70.68  ? 665  LYS   B CE  1 
ATOM   6309  N  NZ  . LYS   B  1 364 ? 5.276   7.839   -12.278  1.00 74.79  ? 665  LYS   B NZ  1 
ATOM   6310  N  N   . HIS   B  1 365 ? 3.289   0.984   -10.740  1.00 24.72  ? 666  HIS   B N   1 
ATOM   6311  C  CA  . HIS   B  1 365 ? 3.230   -0.190  -9.875   1.00 27.95  ? 666  HIS   B CA  1 
ATOM   6312  C  C   . HIS   B  1 365 ? 3.427   -1.474  -10.677  1.00 27.68  ? 666  HIS   B C   1 
ATOM   6313  O  O   . HIS   B  1 365 ? 4.233   -2.342  -10.310  1.00 23.16  ? 666  HIS   B O   1 
ATOM   6314  C  CB  . HIS   B  1 365 ? 1.894   -0.225  -9.140   1.00 23.38  ? 666  HIS   B CB  1 
ATOM   6315  C  CG  . HIS   B  1 365 ? 1.630   -1.522  -8.444   1.00 26.99  ? 666  HIS   B CG  1 
ATOM   6316  N  ND1 . HIS   B  1 365 ? 2.364   -1.945  -7.356   1.00 23.45  ? 666  HIS   B ND1 1 
ATOM   6317  C  CD2 . HIS   B  1 365 ? 0.719   -2.496  -8.687   1.00 26.15  ? 666  HIS   B CD2 1 
ATOM   6318  C  CE1 . HIS   B  1 365 ? 1.908   -3.117  -6.951   1.00 26.98  ? 666  HIS   B CE1 1 
ATOM   6319  N  NE2 . HIS   B  1 365 ? 0.917   -3.479  -7.748   1.00 24.43  ? 666  HIS   B NE2 1 
ATOM   6320  N  N   . MET   B  1 366 ? 2.694   -1.611  -11.780  1.00 26.35  ? 667  MET   B N   1 
ATOM   6321  C  CA  . MET   B  1 366 ? 2.812   -2.812  -12.600  1.00 27.73  ? 667  MET   B CA  1 
ATOM   6322  C  C   . MET   B  1 366 ? 4.253   -3.048  -13.026  1.00 28.95  ? 667  MET   B C   1 
ATOM   6323  O  O   . MET   B  1 366 ? 4.796   -4.148  -12.846  1.00 26.95  ? 667  MET   B O   1 
ATOM   6324  C  CB  . MET   B  1 366 ? 1.909   -2.691  -13.821  1.00 28.56  ? 667  MET   B CB  1 
ATOM   6325  C  CG  . MET   B  1 366 ? 1.756   -3.966  -14.595  1.00 35.49  ? 667  MET   B CG  1 
ATOM   6326  S  SD  . MET   B  1 366 ? 0.508   -3.730  -15.866  1.00 38.12  ? 667  MET   B SD  1 
ATOM   6327  C  CE  . MET   B  1 366 ? 0.810   -5.156  -16.920  1.00 37.61  ? 667  MET   B CE  1 
ATOM   6328  N  N   . GLU   B  1 367 ? 4.901   -2.012  -13.570  1.00 24.93  ? 668  GLU   B N   1 
ATOM   6329  C  CA  . GLU   B  1 367 ? 6.278   -2.167  -14.026  1.00 32.87  ? 668  GLU   B CA  1 
ATOM   6330  C  C   . GLU   B  1 367 ? 7.199   -2.521  -12.868  1.00 28.15  ? 668  GLU   B C   1 
ATOM   6331  O  O   . GLU   B  1 367 ? 8.108   -3.342  -13.015  1.00 34.42  ? 668  GLU   B O   1 
ATOM   6332  C  CB  . GLU   B  1 367 ? 6.740   -0.892  -14.725  1.00 32.13  ? 668  GLU   B CB  1 
ATOM   6333  C  CG  . GLU   B  1 367 ? 5.897   -0.571  -15.947  1.00 38.63  ? 668  GLU   B CG  1 
ATOM   6334  C  CD  . GLU   B  1 367 ? 6.338   0.695   -16.668  1.00 43.66  ? 668  GLU   B CD  1 
ATOM   6335  O  OE1 . GLU   B  1 367 ? 6.186   0.740   -17.906  1.00 43.00  ? 668  GLU   B OE1 1 
ATOM   6336  O  OE2 . GLU   B  1 367 ? 6.823   1.640   -16.003  1.00 42.73  ? 668  GLU   B OE2 1 
ATOM   6337  N  N   . ASN   B  1 368 ? 6.972   -1.915  -11.705  1.00 29.47  ? 669  ASN   B N   1 
ATOM   6338  C  CA  . ASN   B  1 368 ? 7.785   -2.237  -10.539  1.00 33.23  ? 669  ASN   B CA  1 
ATOM   6339  C  C   . ASN   B  1 368 ? 7.605   -3.691  -10.128  1.00 28.40  ? 669  ASN   B C   1 
ATOM   6340  O  O   . ASN   B  1 368 ? 8.582   -4.398  -9.837   1.00 28.42  ? 669  ASN   B O   1 
ATOM   6341  C  CB  . ASN   B  1 368 ? 7.424   -1.328  -9.374   1.00 31.00  ? 669  ASN   B CB  1 
ATOM   6342  C  CG  . ASN   B  1 368 ? 8.253   -1.624  -8.184   1.00 35.59  ? 669  ASN   B CG  1 
ATOM   6343  O  OD1 . ASN   B  1 368 ? 9.475   -1.710  -8.297   1.00 34.14  ? 669  ASN   B OD1 1 
ATOM   6344  N  ND2 . ASN   B  1 368 ? 7.611   -1.851  -7.044   1.00 38.61  ? 669  ASN   B ND2 1 
ATOM   6345  N  N   . GLU   B  1 369 ? 6.349   -4.142  -10.080  1.00 25.16  ? 670  GLU   B N   1 
ATOM   6346  C  CA  . GLU   B  1 369 ? 6.049   -5.540  -9.779   1.00 26.84  ? 670  GLU   B CA  1 
ATOM   6347  C  C   . GLU   B  1 369 ? 6.708   -6.496  -10.768  1.00 25.87  ? 670  GLU   B C   1 
ATOM   6348  O  O   . GLU   B  1 369 ? 7.254   -7.527  -10.367  1.00 31.14  ? 670  GLU   B O   1 
ATOM   6349  C  CB  . GLU   B  1 369 ? 4.535   -5.747  -9.767   1.00 23.77  ? 670  GLU   B CB  1 
ATOM   6350  C  CG  . GLU   B  1 369 ? 3.878   -5.043  -8.622   1.00 20.86  ? 670  GLU   B CG  1 
ATOM   6351  C  CD  . GLU   B  1 369 ? 4.135   -5.764  -7.317   1.00 29.76  ? 670  GLU   B CD  1 
ATOM   6352  O  OE1 . GLU   B  1 369 ? 3.246   -6.523  -6.877   1.00 29.90  ? 670  GLU   B OE1 1 
ATOM   6353  O  OE2 . GLU   B  1 369 ? 5.233   -5.594  -6.750   1.00 31.98  ? 670  GLU   B OE2 1 
ATOM   6354  N  N   . TYR   B  1 370 ? 6.648   -6.195  -12.068  1.00 25.95  ? 671  TYR   B N   1 
ATOM   6355  C  CA  . TYR   B  1 370 ? 7.365   -7.037  -13.016  1.00 26.36  ? 671  TYR   B CA  1 
ATOM   6356  C  C   . TYR   B  1 370 ? 8.853   -7.082  -12.689  1.00 34.31  ? 671  TYR   B C   1 
ATOM   6357  O  O   . TYR   B  1 370 ? 9.472   -8.154  -12.714  1.00 34.62  ? 671  TYR   B O   1 
ATOM   6358  C  CB  . TYR   B  1 370 ? 7.131   -6.547  -14.450  1.00 30.21  ? 671  TYR   B CB  1 
ATOM   6359  C  CG  . TYR   B  1 370 ? 5.887   -7.145  -15.064  1.00 31.19  ? 671  TYR   B CG  1 
ATOM   6360  C  CD1 . TYR   B  1 370 ? 4.640   -6.616  -14.790  1.00 31.58  ? 671  TYR   B CD1 1 
ATOM   6361  C  CD2 . TYR   B  1 370 ? 5.960   -8.260  -15.899  1.00 34.90  ? 671  TYR   B CD2 1 
ATOM   6362  C  CE1 . TYR   B  1 370 ? 3.499   -7.166  -15.326  1.00 28.96  ? 671  TYR   B CE1 1 
ATOM   6363  C  CE2 . TYR   B  1 370 ? 4.815   -8.813  -16.454  1.00 30.63  ? 671  TYR   B CE2 1 
ATOM   6364  C  CZ  . TYR   B  1 370 ? 3.594   -8.259  -16.162  1.00 35.83  ? 671  TYR   B CZ  1 
ATOM   6365  O  OH  . TYR   B  1 370 ? 2.449   -8.788  -16.692  1.00 35.59  ? 671  TYR   B OH  1 
ATOM   6366  N  N   . ARG   B  1 371 ? 9.431   -5.932  -12.339  1.00 32.82  ? 672  ARG   B N   1 
ATOM   6367  C  CA  . ARG   B  1 371 ? 10.851  -5.875  -12.009  1.00 38.13  ? 672  ARG   B CA  1 
ATOM   6368  C  C   . ARG   B  1 371 ? 11.172  -6.699  -10.762  1.00 39.94  ? 672  ARG   B C   1 
ATOM   6369  O  O   . ARG   B  1 371 ? 12.093  -7.520  -10.771  1.00 42.88  ? 672  ARG   B O   1 
ATOM   6370  C  CB  . ARG   B  1 371 ? 11.274  -4.417  -11.820  1.00 51.69  ? 672  ARG   B CB  1 
ATOM   6371  C  CG  . ARG   B  1 371 ? 12.717  -4.129  -12.200  1.00 76.41  ? 672  ARG   B CG  1 
ATOM   6372  C  CD  . ARG   B  1 371 ? 13.015  -2.626  -12.303  1.00 90.06  ? 672  ARG   B CD  1 
ATOM   6373  N  NE  . ARG   B  1 371 ? 11.970  -1.870  -12.998  1.00 94.85  ? 672  ARG   B NE  1 
ATOM   6374  C  CZ  . ARG   B  1 371 ? 11.402  -0.763  -12.517  1.00 92.09  ? 672  ARG   B CZ  1 
ATOM   6375  N  NH1 . ARG   B  1 371 ? 11.787  -0.275  -11.344  1.00 91.50  ? 672  ARG   B NH1 1 
ATOM   6376  N  NH2 . ARG   B  1 371 ? 10.456  -0.138  -13.210  1.00 83.99  ? 672  ARG   B NH2 1 
ATOM   6377  N  N   . CYS   B  1 372 ? 10.436  -6.492  -9.672   1.00 34.03  ? 673  CYS   B N   1 
ATOM   6378  C  CA  . CYS   B  1 372 ? 10.837  -7.120  -8.416   1.00 45.19  ? 673  CYS   B CA  1 
ATOM   6379  C  C   . CYS   B  1 372 ? 10.165  -8.466  -8.170   1.00 42.98  ? 673  CYS   B C   1 
ATOM   6380  O  O   . CYS   B  1 372 ? 10.703  -9.285  -7.417   1.00 46.33  ? 673  CYS   B O   1 
ATOM   6381  C  CB  . CYS   B  1 372 ? 10.566  -6.181  -7.228   1.00 46.84  ? 673  CYS   B CB  1 
ATOM   6382  S  SG  . CYS   B  1 372 ? 8.824   -5.934  -6.751   1.00 50.97  ? 673  CYS   B SG  1 
ATOM   6383  N  N   . ARG   B  1 373 ? 9.029   -8.730  -8.803   1.00 32.73  ? 674  ARG   B N   1 
ATOM   6384  C  CA  . ARG   B  1 373 ? 8.247   -9.918  -8.517   1.00 26.46  ? 674  ARG   B CA  1 
ATOM   6385  C  C   . ARG   B  1 373 ? 8.078   -10.834 -9.721   1.00 34.03  ? 674  ARG   B C   1 
ATOM   6386  O  O   . ARG   B  1 373 ? 7.662   -11.987 -9.550   1.00 35.47  ? 674  ARG   B O   1 
ATOM   6387  C  CB  . ARG   B  1 373 ? 6.868   -9.506  -7.980   1.00 25.77  ? 674  ARG   B CB  1 
ATOM   6388  C  CG  . ARG   B  1 373 ? 6.156   -10.533 -7.140   1.00 26.47  ? 674  ARG   B CG  1 
ATOM   6389  C  CD  . ARG   B  1 373 ? 4.718   -10.089 -6.849   1.00 24.32  ? 674  ARG   B CD  1 
ATOM   6390  N  NE  . ARG   B  1 373 ? 4.045   -11.045 -5.980   1.00 29.99  ? 674  ARG   B NE  1 
ATOM   6391  C  CZ  . ARG   B  1 373 ? 2.733   -11.131 -5.816   1.00 29.63  ? 674  ARG   B CZ  1 
ATOM   6392  N  NH1 . ARG   B  1 373 ? 1.915   -10.311 -6.471   1.00 24.88  ? 674  ARG   B NH1 1 
ATOM   6393  N  NH2 . ARG   B  1 373 ? 2.240   -12.041 -4.985   1.00 28.47  ? 674  ARG   B NH2 1 
ATOM   6394  N  N   . GLY   B  1 374 ? 8.400   -10.375 -10.923  1.00 34.78  ? 675  GLY   B N   1 
ATOM   6395  C  CA  . GLY   B  1 374 ? 8.235   -11.205 -12.096  1.00 33.47  ? 675  GLY   B CA  1 
ATOM   6396  C  C   . GLY   B  1 374 ? 6.876   -11.111 -12.740  1.00 32.22  ? 675  GLY   B C   1 
ATOM   6397  O  O   . GLY   B  1 374 ? 6.598   -11.858 -13.686  1.00 27.05  ? 675  GLY   B O   1 
ATOM   6398  N  N   . GLY   B  1 375 ? 6.020   -10.232 -12.255  1.00 30.29  ? 676  GLY   B N   1 
ATOM   6399  C  CA  . GLY   B  1 375 ? 4.743   -10.023 -12.897  1.00 27.05  ? 676  GLY   B CA  1 
ATOM   6400  C  C   . GLY   B  1 375 ? 3.781   -9.342  -11.953  1.00 31.83  ? 676  GLY   B C   1 
ATOM   6401  O  O   . GLY   B  1 375 ? 4.106   -9.011  -10.810  1.00 34.07  ? 676  GLY   B O   1 
ATOM   6402  N  N   . CYS   B  1 376 ? 2.593   -9.141  -12.463  1.00 30.00  ? 677  CYS   B N   1 
ATOM   6403  C  CA  . CYS   B  1 376 ? 1.548   -8.469  -11.724  1.00 29.80  ? 677  CYS   B CA  1 
ATOM   6404  C  C   . CYS   B  1 376 ? 0.227   -8.841  -12.376  1.00 31.12  ? 677  CYS   B C   1 
ATOM   6405  O  O   . CYS   B  1 376 ? -0.102  -8.329  -13.449  1.00 36.68  ? 677  CYS   B O   1 
ATOM   6406  C  CB  . CYS   B  1 376 ? 1.768   -6.961  -11.730  1.00 25.00  ? 677  CYS   B CB  1 
ATOM   6407  S  SG  . CYS   B  1 376 ? 0.406   -6.020  -10.992  1.00 30.12  ? 677  CYS   B SG  1 
ATOM   6408  N  N   . PRO   B  1 377 ? -0.531  -9.752  -11.784  1.00 26.16  ? 678  PRO   B N   1 
ATOM   6409  C  CA  . PRO   B  1 377 ? -1.813  -10.133 -12.379  1.00 19.35  ? 678  PRO   B CA  1 
ATOM   6410  C  C   . PRO   B  1 377 ? -2.739  -8.928  -12.416  1.00 23.67  ? 678  PRO   B C   1 
ATOM   6411  O  O   . PRO   B  1 377 ? -2.862  -8.185  -11.440  1.00 22.26  ? 678  PRO   B O   1 
ATOM   6412  C  CB  . PRO   B  1 377 ? -2.332  -11.220 -11.434  1.00 25.69  ? 678  PRO   B CB  1 
ATOM   6413  C  CG  . PRO   B  1 377 ? -1.692  -10.870 -10.102  1.00 31.26  ? 678  PRO   B CG  1 
ATOM   6414  C  CD  . PRO   B  1 377 ? -0.318  -10.365 -10.463  1.00 25.80  ? 678  PRO   B CD  1 
ATOM   6415  N  N   . ALA   B  1 378 ? -3.381  -8.719  -13.556  1.00 26.41  ? 679  ALA   B N   1 
ATOM   6416  C  CA  . ALA   B  1 378 ? -4.178  -7.511  -13.720  1.00 27.28  ? 679  ALA   B CA  1 
ATOM   6417  C  C   . ALA   B  1 378 ? -5.333  -7.818  -14.646  1.00 24.96  ? 679  ALA   B C   1 
ATOM   6418  O  O   . ALA   B  1 378 ? -5.151  -8.458  -15.689  1.00 19.49  ? 679  ALA   B O   1 
ATOM   6419  C  CB  . ALA   B  1 378 ? -3.344  -6.346  -14.267  1.00 27.14  ? 679  ALA   B CB  1 
ATOM   6420  N  N   . ASP   B  1 379 ? -6.514  -7.374  -14.251  1.00 23.31  ? 680  ASP   B N   1 
ATOM   6421  C  CA  . ASP   B  1 379 ? -7.740  -7.651  -14.983  1.00 23.98  ? 680  ASP   B CA  1 
ATOM   6422  C  C   . ASP   B  1 379 ? -8.075  -6.392  -15.768  1.00 23.44  ? 680  ASP   B C   1 
ATOM   6423  O  O   . ASP   B  1 379 ? -8.703  -5.469  -15.243  1.00 22.86  ? 680  ASP   B O   1 
ATOM   6424  C  CB  . ASP   B  1 379 ? -8.860  -8.045  -14.026  1.00 22.34  ? 680  ASP   B CB  1 
ATOM   6425  C  CG  . ASP   B  1 379 ? -10.126 -8.482  -14.753  1.00 28.65  ? 680  ASP   B CG  1 
ATOM   6426  O  OD1 . ASP   B  1 379 ? -10.912 -9.254  -14.166  1.00 25.93  ? 680  ASP   B OD1 1 
ATOM   6427  O  OD2 . ASP   B  1 379 ? -10.324 -8.062  -15.918  1.00 31.76  ? 680  ASP   B OD2 1 
ATOM   6428  N  N   . TRP   B  1 380 ? -7.662  -6.369  -17.039  1.00 21.12  ? 681  TRP   B N   1 
ATOM   6429  C  CA  . TRP   B  1 380 ? -7.857  -5.188  -17.875  1.00 18.81  ? 681  TRP   B CA  1 
ATOM   6430  C  C   . TRP   B  1 380 ? -9.297  -4.711  -17.843  1.00 18.69  ? 681  TRP   B C   1 
ATOM   6431  O  O   . TRP   B  1 380 ? -9.556  -3.512  -17.758  1.00 19.39  ? 681  TRP   B O   1 
ATOM   6432  C  CB  . TRP   B  1 380 ? -7.456  -5.528  -19.312  1.00 19.71  ? 681  TRP   B CB  1 
ATOM   6433  C  CG  . TRP   B  1 380 ? -7.302  -4.359  -20.259  1.00 20.36  ? 681  TRP   B CG  1 
ATOM   6434  C  CD1 . TRP   B  1 380 ? -6.123  -3.788  -20.653  1.00 19.88  ? 681  TRP   B CD1 1 
ATOM   6435  C  CD2 . TRP   B  1 380 ? -8.336  -3.686  -20.990  1.00 22.12  ? 681  TRP   B CD2 1 
ATOM   6436  N  NE1 . TRP   B  1 380 ? -6.352  -2.803  -21.574  1.00 20.11  ? 681  TRP   B NE1 1 
ATOM   6437  C  CE2 . TRP   B  1 380 ? -7.703  -2.708  -21.797  1.00 25.15  ? 681  TRP   B CE2 1 
ATOM   6438  C  CE3 . TRP   B  1 380 ? -9.730  -3.796  -21.030  1.00 19.59  ? 681  TRP   B CE3 1 
ATOM   6439  C  CZ2 . TRP   B  1 380 ? -8.418  -1.840  -22.631  1.00 20.29  ? 681  TRP   B CZ2 1 
ATOM   6440  C  CZ3 . TRP   B  1 380 ? -10.443 -2.931  -21.877  1.00 21.01  ? 681  TRP   B CZ3 1 
ATOM   6441  C  CH2 . TRP   B  1 380 ? -9.781  -1.964  -22.657  1.00 20.22  ? 681  TRP   B CH2 1 
ATOM   6442  N  N   . VAL   B  1 381 ? -10.245 -5.644  -17.927  1.00 18.69  ? 682  VAL   B N   1 
ATOM   6443  C  CA  . VAL   B  1 381 ? -11.664 -5.304  -17.939  1.00 18.68  ? 682  VAL   B CA  1 
ATOM   6444  C  C   . VAL   B  1 381 ? -12.051 -4.488  -16.712  1.00 24.53  ? 682  VAL   B C   1 
ATOM   6445  O  O   . VAL   B  1 381 ? -12.930 -3.619  -16.784  1.00 19.76  ? 682  VAL   B O   1 
ATOM   6446  C  CB  . VAL   B  1 381 ? -12.492 -6.604  -18.058  1.00 20.62  ? 682  VAL   B CB  1 
ATOM   6447  C  CG1 . VAL   B  1 381 ? -13.979 -6.338  -17.812  1.00 21.92  ? 682  VAL   B CG1 1 
ATOM   6448  C  CG2 . VAL   B  1 381 ? -12.301 -7.251  -19.432  1.00 22.89  ? 682  VAL   B CG2 1 
ATOM   6449  N  N   . TRP   B  1 382 ? -11.396 -4.726  -15.577  1.00 21.73  ? 683  TRP   B N   1 
ATOM   6450  C  CA  . TRP   B  1 382 ? -11.657 -3.939  -14.381  1.00 20.43  ? 683  TRP   B CA  1 
ATOM   6451  C  C   . TRP   B  1 382 ? -10.691 -2.781  -14.200  1.00 23.53  ? 683  TRP   B C   1 
ATOM   6452  O  O   . TRP   B  1 382 ? -11.081 -1.758  -13.639  1.00 22.38  ? 683  TRP   B O   1 
ATOM   6453  C  CB  . TRP   B  1 382 ? -11.609 -4.827  -13.121  1.00 18.38  ? 683  TRP   B CB  1 
ATOM   6454  C  CG  . TRP   B  1 382 ? -12.905 -5.516  -12.851  1.00 18.87  ? 683  TRP   B CG  1 
ATOM   6455  C  CD1 . TRP   B  1 382 ? -13.533 -6.411  -13.655  1.00 21.01  ? 683  TRP   B CD1 1 
ATOM   6456  C  CD2 . TRP   B  1 382 ? -13.735 -5.367  -11.686  1.00 17.47  ? 683  TRP   B CD2 1 
ATOM   6457  N  NE1 . TRP   B  1 382 ? -14.714 -6.828  -13.074  1.00 23.77  ? 683  TRP   B NE1 1 
ATOM   6458  C  CE2 . TRP   B  1 382 ? -14.855 -6.203  -11.863  1.00 31.43  ? 683  TRP   B CE2 1 
ATOM   6459  C  CE3 . TRP   B  1 382 ? -13.638 -4.612  -10.517  1.00 23.05  ? 683  TRP   B CE3 1 
ATOM   6460  C  CZ2 . TRP   B  1 382 ? -15.871 -6.299  -10.916  1.00 26.00  ? 683  TRP   B CZ2 1 
ATOM   6461  C  CZ3 . TRP   B  1 382 ? -14.643 -4.713  -9.578   1.00 27.52  ? 683  TRP   B CZ3 1 
ATOM   6462  C  CH2 . TRP   B  1 382 ? -15.743 -5.553  -9.782   1.00 23.54  ? 683  TRP   B CH2 1 
ATOM   6463  N  N   . ILE   B  1 383 ? -9.442  -2.921  -14.645  1.00 22.38  ? 684  ILE   B N   1 
ATOM   6464  C  CA  . ILE   B  1 383 ? -8.453  -1.879  -14.389  1.00 19.80  ? 684  ILE   B CA  1 
ATOM   6465  C  C   . ILE   B  1 383 ? -8.769  -0.633  -15.207  1.00 24.29  ? 684  ILE   B C   1 
ATOM   6466  O  O   . ILE   B  1 383 ? -8.566  0.493   -14.744  1.00 22.86  ? 684  ILE   B O   1 
ATOM   6467  C  CB  . ILE   B  1 383 ? -7.034  -2.406  -14.688  1.00 24.17  ? 684  ILE   B CB  1 
ATOM   6468  C  CG1 . ILE   B  1 383 ? -6.643  -3.524  -13.720  1.00 23.94  ? 684  ILE   B CG1 1 
ATOM   6469  C  CG2 . ILE   B  1 383 ? -6.020  -1.271  -14.648  1.00 18.50  ? 684  ILE   B CG2 1 
ATOM   6470  C  CD1 . ILE   B  1 383 ? -6.565  -3.095  -12.240  1.00 21.35  ? 684  ILE   B CD1 1 
ATOM   6471  N  N   . VAL   B  1 384 ? -9.265  -0.805  -16.433  1.00 18.55  ? 685  VAL   B N   1 
ATOM   6472  C  CA  . VAL   B  1 384 ? -9.566  0.370   -17.266  1.00 19.57  ? 685  VAL   B CA  1 
ATOM   6473  C  C   . VAL   B  1 384 ? -10.781 1.097   -16.705  1.00 18.81  ? 685  VAL   B C   1 
ATOM   6474  O  O   . VAL   B  1 384 ? -11.820 0.466   -16.454  1.00 22.54  ? 685  VAL   B O   1 
ATOM   6475  C  CB  . VAL   B  1 384 ? -9.786  -0.046  -18.731  1.00 22.99  ? 685  VAL   B CB  1 
ATOM   6476  C  CG1 . VAL   B  1 384 ? -10.199 1.158   -19.592  1.00 19.61  ? 685  VAL   B CG1 1 
ATOM   6477  C  CG2 . VAL   B  1 384 ? -8.506  -0.652  -19.277  1.00 19.97  ? 685  VAL   B CG2 1 
ATOM   6478  N  N   . PRO   B  1 385 ? -10.696 2.402   -16.477  1.00 21.82  ? 686  PRO   B N   1 
ATOM   6479  C  CA  . PRO   B  1 385 ? -11.798 3.134   -15.856  1.00 21.54  ? 686  PRO   B CA  1 
ATOM   6480  C  C   . PRO   B  1 385 ? -13.035 3.139   -16.730  1.00 27.27  ? 686  PRO   B C   1 
ATOM   6481  O  O   . PRO   B  1 385 ? -12.945 3.064   -17.963  1.00 26.39  ? 686  PRO   B O   1 
ATOM   6482  C  CB  . PRO   B  1 385 ? -11.231 4.553   -15.705  1.00 25.88  ? 686  PRO   B CB  1 
ATOM   6483  C  CG  . PRO   B  1 385 ? -9.765  4.333   -15.603  1.00 32.57  ? 686  PRO   B CG  1 
ATOM   6484  C  CD  . PRO   B  1 385 ? -9.468  3.206   -16.543  1.00 26.72  ? 686  PRO   B CD  1 
ATOM   6485  N  N   . PRO   B  1 386 ? -14.214 3.272   -16.126  1.00 27.87  ? 687  PRO   B N   1 
ATOM   6486  C  CA  . PRO   B  1 386 ? -15.463 3.223   -16.894  1.00 24.35  ? 687  PRO   B CA  1 
ATOM   6487  C  C   . PRO   B  1 386 ? -15.744 4.457   -17.740  1.00 24.29  ? 687  PRO   B C   1 
ATOM   6488  O  O   . PRO   B  1 386 ? -16.826 4.551   -18.324  1.00 23.63  ? 687  PRO   B O   1 
ATOM   6489  C  CB  . PRO   B  1 386 ? -16.518 3.080   -15.785  1.00 26.78  ? 687  PRO   B CB  1 
ATOM   6490  C  CG  . PRO   B  1 386 ? -15.921 3.857   -14.640  1.00 19.19  ? 687  PRO   B CG  1 
ATOM   6491  C  CD  . PRO   B  1 386 ? -14.448 3.510   -14.685  1.00 23.07  ? 687  PRO   B CD  1 
ATOM   6492  N  N   . MET   B  1 387 ? -14.854 5.440   -17.794  1.00 22.84  ? 688  MET   B N   1 
ATOM   6493  C  CA  . MET   B  1 387 ? -14.987 6.528   -18.753  1.00 22.71  ? 688  MET   B CA  1 
ATOM   6494  C  C   . MET   B  1 387 ? -13.597 6.830   -19.264  1.00 29.36  ? 688  MET   B C   1 
ATOM   6495  O  O   . MET   B  1 387 ? -12.602 6.523   -18.596  1.00 28.59  ? 688  MET   B O   1 
ATOM   6496  C  CB  . MET   B  1 387 ? -15.589 7.814   -18.159  1.00 23.14  ? 688  MET   B CB  1 
ATOM   6497  C  CG  . MET   B  1 387 ? -14.675 8.502   -17.148  1.00 28.49  ? 688  MET   B CG  1 
ATOM   6498  S  SD  . MET   B  1 387 ? -15.342 10.011  -16.380  1.00 35.09  ? 688  MET   B SD  1 
ATOM   6499  C  CE  . MET   B  1 387 ? -15.233 11.172  -17.734  1.00 38.13  ? 688  MET   B CE  1 
ATOM   6500  N  N   . SER   B  1 388 ? -13.539 7.434   -20.457  1.00 27.57  ? 689  SER   B N   1 
ATOM   6501  C  CA  . SER   B  1 388 ? -12.283 7.945   -21.004  1.00 28.02  ? 689  SER   B CA  1 
ATOM   6502  C  C   . SER   B  1 388 ? -11.197 6.880   -21.039  1.00 25.24  ? 689  SER   B C   1 
ATOM   6503  O  O   . SER   B  1 388 ? -10.014 7.178   -20.844  1.00 27.92  ? 689  SER   B O   1 
ATOM   6504  C  CB  . SER   B  1 388 ? -11.794 9.145   -20.196  1.00 28.71  ? 689  SER   B CB  1 
ATOM   6505  O  OG  . SER   B  1 388 ? -12.748 10.185  -20.253  1.00 36.72  ? 689  SER   B OG  1 
ATOM   6506  N  N   . GLY   B  1 389 ? -11.596 5.629   -21.255  1.00 26.53  ? 690  GLY   B N   1 
ATOM   6507  C  CA  . GLY   B  1 389 ? -10.677 4.513   -21.191  1.00 23.13  ? 690  GLY   B CA  1 
ATOM   6508  C  C   . GLY   B  1 389 ? -9.348  4.719   -21.891  1.00 24.46  ? 690  GLY   B C   1 
ATOM   6509  O  O   . GLY   B  1 389 ? -8.294  4.626   -21.253  1.00 27.57  ? 690  GLY   B O   1 
ATOM   6510  N  N   . SER   B  1 390 ? -9.376  5.027   -23.193  1.00 21.71  ? 691  SER   B N   1 
ATOM   6511  C  CA  . SER   B  1 390 ? -8.137  5.036   -23.951  1.00 25.24  ? 691  SER   B CA  1 
ATOM   6512  C  C   . SER   B  1 390 ? -7.283  6.263   -23.696  1.00 22.47  ? 691  SER   B C   1 
ATOM   6513  O  O   . SER   B  1 390 ? -6.137  6.297   -24.152  1.00 33.14  ? 691  SER   B O   1 
ATOM   6514  C  CB  . SER   B  1 390 ? -8.407  4.936   -25.458  1.00 26.49  ? 691  SER   B CB  1 
ATOM   6515  O  OG  . SER   B  1 390 ? -8.900  6.162   -25.914  1.00 26.09  ? 691  SER   B OG  1 
ATOM   6516  N  N   . ILE   B  1 391 ? -7.785  7.281   -22.995  1.00 25.11  ? 692  ILE   B N   1 
ATOM   6517  C  CA  . ILE   B  1 391 ? -6.892  8.369   -22.636  1.00 25.40  ? 692  ILE   B CA  1 
ATOM   6518  C  C   . ILE   B  1 391 ? -6.210  8.086   -21.307  1.00 22.47  ? 692  ILE   B C   1 
ATOM   6519  O  O   . ILE   B  1 391 ? -5.373  8.885   -20.864  1.00 27.85  ? 692  ILE   B O   1 
ATOM   6520  C  CB  . ILE   B  1 391 ? -7.617  9.734   -22.677  1.00 31.66  ? 692  ILE   B CB  1 
ATOM   6521  C  CG1 . ILE   B  1 391 ? -8.621  9.882   -21.560  1.00 43.04  ? 692  ILE   B CG1 1 
ATOM   6522  C  CG2 . ILE   B  1 391 ? -8.289  9.971   -24.070  1.00 27.11  ? 692  ILE   B CG2 1 
ATOM   6523  C  CD1 . ILE   B  1 391 ? -9.248  11.248  -21.550  1.00 39.96  ? 692  ILE   B CD1 1 
ATOM   6524  N  N   . THR   B  1 392 ? -6.496  6.968   -20.699  1.00 24.24  ? 693  THR   B N   1 
ATOM   6525  C  CA  . THR   B  1 392 ? -5.697  6.527   -19.563  1.00 29.47  ? 693  THR   B CA  1 
ATOM   6526  C  C   . THR   B  1 392 ? -4.675  5.514   -20.044  1.00 29.66  ? 693  THR   B C   1 
ATOM   6527  O  O   . THR   B  1 392 ? -4.919  4.801   -21.024  1.00 25.86  ? 693  THR   B O   1 
ATOM   6528  C  CB  . THR   B  1 392 ? -6.553  5.895   -18.453  1.00 25.45  ? 693  THR   B CB  1 
ATOM   6529  O  OG1 . THR   B  1 392 ? -7.030  4.615   -18.876  1.00 28.10  ? 693  THR   B OG1 1 
ATOM   6530  C  CG2 . THR   B  1 392 ? -7.737  6.774   -18.104  1.00 25.42  ? 693  THR   B CG2 1 
ATOM   6531  N  N   . PRO   B  1 393 ? -3.510  5.436   -19.400  1.00 28.28  ? 694  PRO   B N   1 
ATOM   6532  C  CA  . PRO   B  1 393 ? -2.453  4.573   -19.947  1.00 29.42  ? 694  PRO   B CA  1 
ATOM   6533  C  C   . PRO   B  1 393 ? -2.758  3.095   -19.823  1.00 28.57  ? 694  PRO   B C   1 
ATOM   6534  O  O   . PRO   B  1 393 ? -2.246  2.315   -20.633  1.00 26.77  ? 694  PRO   B O   1 
ATOM   6535  C  CB  . PRO   B  1 393 ? -1.216  4.967   -19.132  1.00 27.64  ? 694  PRO   B CB  1 
ATOM   6536  C  CG  . PRO   B  1 393 ? -1.790  5.511   -17.829  1.00 27.75  ? 694  PRO   B CG  1 
ATOM   6537  C  CD  . PRO   B  1 393 ? -3.036  6.240   -18.261  1.00 29.33  ? 694  PRO   B CD  1 
ATOM   6538  N  N   . VAL   B  1 394 ? -3.580  2.682   -18.849  1.00 24.40  ? 695  VAL   B N   1 
ATOM   6539  C  CA  . VAL   B  1 394 ? -3.849  1.256   -18.688  1.00 20.24  ? 695  VAL   B CA  1 
ATOM   6540  C  C   . VAL   B  1 394 ? -4.536  0.685   -19.921  1.00 23.67  ? 695  VAL   B C   1 
ATOM   6541  O  O   . VAL   B  1 394 ? -4.392  -0.502  -20.219  1.00 20.27  ? 695  VAL   B O   1 
ATOM   6542  C  CB  . VAL   B  1 394 ? -4.686  0.992   -17.431  1.00 21.88  ? 695  VAL   B CB  1 
ATOM   6543  C  CG1 . VAL   B  1 394 ? -3.842  1.220   -16.171  1.00 22.02  ? 695  VAL   B CG1 1 
ATOM   6544  C  CG2 . VAL   B  1 394 ? -5.935  1.851   -17.450  1.00 22.94  ? 695  VAL   B CG2 1 
ATOM   6545  N  N   . PHE   B  1 395 ? -5.305  1.505   -20.638  1.00 21.69  ? 696  PHE   B N   1 
ATOM   6546  C  CA  . PHE   B  1 395 ? -6.012  1.013   -21.818  1.00 23.64  ? 696  PHE   B CA  1 
ATOM   6547  C  C   . PHE   B  1 395 ? -5.042  0.404   -22.817  1.00 25.86  ? 696  PHE   B C   1 
ATOM   6548  O  O   . PHE   B  1 395 ? -5.338  -0.622  -23.440  1.00 24.37  ? 696  PHE   B O   1 
ATOM   6549  C  CB  . PHE   B  1 395 ? -6.804  2.151   -22.454  1.00 22.90  ? 696  PHE   B CB  1 
ATOM   6550  C  CG  . PHE   B  1 395 ? -7.516  1.771   -23.712  1.00 21.85  ? 696  PHE   B CG  1 
ATOM   6551  C  CD1 . PHE   B  1 395 ? -8.849  1.404   -23.681  1.00 21.33  ? 696  PHE   B CD1 1 
ATOM   6552  C  CD2 . PHE   B  1 395 ? -6.855  1.802   -24.938  1.00 22.77  ? 696  PHE   B CD2 1 
ATOM   6553  C  CE1 . PHE   B  1 395 ? -9.510  1.058   -24.858  1.00 21.41  ? 696  PHE   B CE1 1 
ATOM   6554  C  CE2 . PHE   B  1 395 ? -7.511  1.446   -26.112  1.00 24.56  ? 696  PHE   B CE2 1 
ATOM   6555  C  CZ  . PHE   B  1 395 ? -8.835  1.074   -26.067  1.00 21.92  ? 696  PHE   B CZ  1 
ATOM   6556  N  N   . HIS   B  1 396 ? -3.870  1.010   -22.957  1.00 25.35  ? 697  HIS   B N   1 
ATOM   6557  C  CA  . HIS   B  1 396 ? -2.865  0.619   -23.927  1.00 27.89  ? 697  HIS   B CA  1 
ATOM   6558  C  C   . HIS   B  1 396 ? -1.916  -0.435  -23.397  1.00 27.17  ? 697  HIS   B C   1 
ATOM   6559  O  O   . HIS   B  1 396 ? -1.007  -0.861  -24.125  1.00 25.14  ? 697  HIS   B O   1 
ATOM   6560  C  CB  . HIS   B  1 396 ? -2.103  1.863   -24.357  1.00 25.59  ? 697  HIS   B CB  1 
ATOM   6561  C  CG  . HIS   B  1 396 ? -3.009  2.939   -24.847  1.00 29.02  ? 697  HIS   B CG  1 
ATOM   6562  N  ND1 . HIS   B  1 396 ? -3.471  2.973   -26.144  1.00 27.75  ? 697  HIS   B ND1 1 
ATOM   6563  C  CD2 . HIS   B  1 396 ? -3.611  3.966   -24.202  1.00 26.17  ? 697  HIS   B CD2 1 
ATOM   6564  C  CE1 . HIS   B  1 396 ? -4.285  4.002   -26.290  1.00 29.91  ? 697  HIS   B CE1 1 
ATOM   6565  N  NE2 . HIS   B  1 396 ? -4.387  4.623   -25.128  1.00 28.04  ? 697  HIS   B NE2 1 
ATOM   6566  N  N   . GLN   B  1 397 ? -2.130  -0.872  -22.164  1.00 27.86  ? 698  GLN   B N   1 
ATOM   6567  C  CA  . GLN   B  1 397 ? -1.243  -1.789  -21.474  1.00 22.79  ? 698  GLN   B CA  1 
ATOM   6568  C  C   . GLN   B  1 397 ? -1.800  -3.197  -21.588  1.00 24.91  ? 698  GLN   B C   1 
ATOM   6569  O  O   . GLN   B  1 397 ? -2.882  -3.477  -21.056  1.00 28.03  ? 698  GLN   B O   1 
ATOM   6570  C  CB  . GLN   B  1 397 ? -1.129  -1.403  -19.996  1.00 22.53  ? 698  GLN   B CB  1 
ATOM   6571  C  CG  . GLN   B  1 397 ? -0.277  -2.372  -19.214  1.00 25.41  ? 698  GLN   B CG  1 
ATOM   6572  C  CD  . GLN   B  1 397 ? 1.150   -2.365  -19.708  1.00 29.79  ? 698  GLN   B CD  1 
ATOM   6573  O  OE1 . GLN   B  1 397 ? 1.786   -1.315  -19.737  1.00 27.88  ? 698  GLN   B OE1 1 
ATOM   6574  N  NE2 . GLN   B  1 397 ? 1.657   -3.531  -20.122  1.00 25.18  ? 698  GLN   B NE2 1 
ATOM   6575  N  N   . GLU   B  1 398 ? -1.068  -4.087  -22.254  1.00 22.11  ? 699  GLU   B N   1 
ATOM   6576  C  CA  . GLU   B  1 398 ? -1.420  -5.497  -22.171  1.00 21.33  ? 699  GLU   B CA  1 
ATOM   6577  C  C   . GLU   B  1 398 ? -1.203  -5.981  -20.744  1.00 23.15  ? 699  GLU   B C   1 
ATOM   6578  O  O   . GLU   B  1 398 ? -0.263  -5.561  -20.074  1.00 23.15  ? 699  GLU   B O   1 
ATOM   6579  C  CB  . GLU   B  1 398 ? -0.589  -6.335  -23.133  1.00 21.92  ? 699  GLU   B CB  1 
ATOM   6580  C  CG  . GLU   B  1 398 ? -0.995  -6.176  -24.579  1.00 22.28  ? 699  GLU   B CG  1 
ATOM   6581  C  CD  . GLU   B  1 398 ? -0.118  -6.988  -25.491  1.00 28.43  ? 699  GLU   B CD  1 
ATOM   6582  O  OE1 . GLU   B  1 398 ? -0.445  -7.090  -26.693  1.00 28.80  ? 699  GLU   B OE1 1 
ATOM   6583  O  OE2 . GLU   B  1 398 ? 0.904   -7.526  -24.996  1.00 31.41  ? 699  GLU   B OE2 1 
ATOM   6584  N  N   . MET   B  1 399 ? -2.092  -6.856  -20.280  1.00 26.95  ? 700  MET   B N   1 
ATOM   6585  C  CA  . MET   B  1 399 ? -2.059  -7.374  -18.919  1.00 25.92  ? 700  MET   B CA  1 
ATOM   6586  C  C   . MET   B  1 399 ? -2.299  -8.871  -18.964  1.00 27.46  ? 700  MET   B C   1 
ATOM   6587  O  O   . MET   B  1 399 ? -2.991  -9.373  -19.852  1.00 30.84  ? 700  MET   B O   1 
ATOM   6588  C  CB  . MET   B  1 399 ? -3.129  -6.720  -18.048  1.00 22.65  ? 700  MET   B CB  1 
ATOM   6589  C  CG  . MET   B  1 399 ? -2.993  -5.229  -17.921  1.00 26.77  ? 700  MET   B CG  1 
ATOM   6590  S  SD  . MET   B  1 399 ? -4.457  -4.522  -17.155  1.00 26.93  ? 700  MET   B SD  1 
ATOM   6591  C  CE  . MET   B  1 399 ? -4.125  -2.765  -17.396  1.00 25.05  ? 700  MET   B CE  1 
ATOM   6592  N  N   . LEU   B  1 400 ? -1.719  -9.582  -18.014  1.00 25.64  ? 701  LEU   B N   1 
ATOM   6593  C  CA  . LEU   B  1 400 ? -1.995  -10.998 -17.832  1.00 22.36  ? 701  LEU   B CA  1 
ATOM   6594  C  C   . LEU   B  1 400 ? -2.786  -11.160 -16.550  1.00 26.90  ? 701  LEU   B C   1 
ATOM   6595  O  O   . LEU   B  1 400 ? -2.424  -10.578 -15.517  1.00 26.55  ? 701  LEU   B O   1 
ATOM   6596  C  CB  . LEU   B  1 400 ? -0.711  -11.825 -17.760  1.00 25.63  ? 701  LEU   B CB  1 
ATOM   6597  C  CG  . LEU   B  1 400 ? 0.130   -11.884 -19.022  1.00 27.34  ? 701  LEU   B CG  1 
ATOM   6598  C  CD1 . LEU   B  1 400 ? 1.483   -12.498 -18.708  1.00 27.78  ? 701  LEU   B CD1 1 
ATOM   6599  C  CD2 . LEU   B  1 400 ? -0.616  -12.654 -20.111  1.00 21.82  ? 701  LEU   B CD2 1 
ATOM   6600  N  N   . ASN   B  1 401 ? -3.869  -11.921 -16.623  1.00 26.40  ? 702  ASN   B N   1 
ATOM   6601  C  CA  . ASN   B  1 401 ? -4.707  -12.161 -15.460  1.00 31.08  ? 702  ASN   B CA  1 
ATOM   6602  C  C   . ASN   B  1 401 ? -4.520  -13.602 -15.015  1.00 27.86  ? 702  ASN   B C   1 
ATOM   6603  O  O   . ASN   B  1 401 ? -4.594  -14.525 -15.831  1.00 23.01  ? 702  ASN   B O   1 
ATOM   6604  C  CB  . ASN   B  1 401 ? -6.186  -11.867 -15.734  1.00 26.22  ? 702  ASN   B CB  1 
ATOM   6605  C  CG  . ASN   B  1 401 ? -6.963  -11.742 -14.460  1.00 28.68  ? 702  ASN   B CG  1 
ATOM   6606  O  OD1 . ASN   B  1 401 ? -6.358  -11.560 -13.426  1.00 30.70  ? 702  ASN   B OD1 1 
ATOM   6607  N  ND2 . ASN   B  1 401 ? -8.286  -11.869 -14.511  1.00 26.32  ? 702  ASN   B ND2 1 
ATOM   6608  N  N   . TYR   B  1 402 ? -4.220  -13.781 -13.733  1.00 24.41  ? 703  TYR   B N   1 
ATOM   6609  C  CA  . TYR   B  1 402 ? -4.109  -15.107 -13.151  1.00 25.00  ? 703  TYR   B CA  1 
ATOM   6610  C  C   . TYR   B  1 402 ? -4.335  -14.952 -11.663  1.00 29.10  ? 703  TYR   B C   1 
ATOM   6611  O  O   . TYR   B  1 402 ? -4.308  -13.841 -11.135  1.00 23.26  ? 703  TYR   B O   1 
ATOM   6612  C  CB  . TYR   B  1 402 ? -2.758  -15.777 -13.447  1.00 21.16  ? 703  TYR   B CB  1 
ATOM   6613  C  CG  . TYR   B  1 402 ? -1.551  -14.883 -13.299  1.00 22.50  ? 703  TYR   B CG  1 
ATOM   6614  C  CD1 . TYR   B  1 402 ? -0.864  -14.788 -12.094  1.00 24.33  ? 703  TYR   B CD1 1 
ATOM   6615  C  CD2 . TYR   B  1 402 ? -1.091  -14.139 -14.366  1.00 30.73  ? 703  TYR   B CD2 1 
ATOM   6616  C  CE1 . TYR   B  1 402 ? 0.256   -13.964 -11.966  1.00 23.48  ? 703  TYR   B CE1 1 
ATOM   6617  C  CE2 . TYR   B  1 402 ? 0.007   -13.319 -14.247  1.00 29.74  ? 703  TYR   B CE2 1 
ATOM   6618  C  CZ  . TYR   B  1 402 ? 0.683   -13.238 -13.055  1.00 25.24  ? 703  TYR   B CZ  1 
ATOM   6619  O  OH  . TYR   B  1 402 ? 1.783   -12.411 -12.979  1.00 30.09  ? 703  TYR   B OH  1 
ATOM   6620  N  N   . ARG   B  1 403 ? -4.606  -16.067 -10.999  1.00 30.52  ? 704  ARG   B N   1 
ATOM   6621  C  CA  . ARG   B  1 403 ? -5.046  -16.050 -9.612   1.00 29.19  ? 704  ARG   B CA  1 
ATOM   6622  C  C   . ARG   B  1 403 ? -3.891  -16.521 -8.740   1.00 31.11  ? 704  ARG   B C   1 
ATOM   6623  O  O   . ARG   B  1 403 ? -3.484  -17.684 -8.808   1.00 27.31  ? 704  ARG   B O   1 
ATOM   6624  C  CB  . ARG   B  1 403 ? -6.284  -16.921 -9.419   1.00 38.72  ? 704  ARG   B CB  1 
ATOM   6625  C  CG  . ARG   B  1 403 ? -6.742  -16.986 -7.974   1.00 53.67  ? 704  ARG   B CG  1 
ATOM   6626  C  CD  . ARG   B  1 403 ? -8.194  -17.438 -7.854   1.00 70.49  ? 704  ARG   B CD  1 
ATOM   6627  N  NE  . ARG   B  1 403 ? -9.107  -16.639 -8.673   1.00 81.92  ? 704  ARG   B NE  1 
ATOM   6628  C  CZ  . ARG   B  1 403 ? -9.554  -15.425 -8.351   1.00 86.60  ? 704  ARG   B CZ  1 
ATOM   6629  N  NH1 . ARG   B  1 403 ? -9.173  -14.842 -7.221   1.00 89.33  ? 704  ARG   B NH1 1 
ATOM   6630  N  NH2 . ARG   B  1 403 ? -10.382 -14.785 -9.166   1.00 87.22  ? 704  ARG   B NH2 1 
ATOM   6631  N  N   . LEU   B  1 404 ? -3.346  -15.603 -7.958   1.00 25.29  ? 705  LEU   B N   1 
ATOM   6632  C  CA  . LEU   B  1 404 ? -2.358  -15.914 -6.947   1.00 25.04  ? 705  LEU   B CA  1 
ATOM   6633  C  C   . LEU   B  1 404 ? -3.047  -15.959 -5.591   1.00 22.31  ? 705  LEU   B C   1 
ATOM   6634  O  O   . LEU   B  1 404 ? -4.072  -15.308 -5.367   1.00 22.56  ? 705  LEU   B O   1 
ATOM   6635  C  CB  . LEU   B  1 404 ? -1.245  -14.868 -6.916   1.00 23.80  ? 705  LEU   B CB  1 
ATOM   6636  C  CG  . LEU   B  1 404 ? -0.409  -14.689 -8.175   1.00 28.40  ? 705  LEU   B CG  1 
ATOM   6637  C  CD1 . LEU   B  1 404 ? 0.468   -13.467 -7.996   1.00 30.50  ? 705  LEU   B CD1 1 
ATOM   6638  C  CD2 . LEU   B  1 404 ? 0.437   -15.938 -8.417   1.00 26.41  ? 705  LEU   B CD2 1 
ATOM   6639  N  N   . THR   B  1 405 ? -2.480  -16.734 -4.697   1.00 23.77  ? 706  THR   B N   1 
ATOM   6640  C  CA  . THR   B  1 405 ? -2.969  -16.737 -3.330   1.00 26.07  ? 706  THR   B CA  1 
ATOM   6641  C  C   . THR   B  1 405 ? -1.858  -16.254 -2.398   1.00 23.17  ? 706  THR   B C   1 
ATOM   6642  O  O   . THR   B  1 405 ? -0.676  -16.426 -2.710   1.00 27.62  ? 706  THR   B O   1 
ATOM   6643  C  CB  . THR   B  1 405 ? -3.446  -18.147 -2.958   1.00 24.69  ? 706  THR   B CB  1 
ATOM   6644  O  OG1 . THR   B  1 405 ? -4.063  -18.133 -1.667   1.00 42.08  ? 706  THR   B OG1 1 
ATOM   6645  C  CG2 . THR   B  1 405 ? -2.294  -19.123 -2.967   1.00 24.18  ? 706  THR   B CG2 1 
ATOM   6646  N  N   . PRO   B  1 406 ? -2.188  -15.606 -1.265   1.00 25.91  ? 707  PRO   B N   1 
ATOM   6647  C  CA  . PRO   B  1 406 ? -3.502  -15.271 -0.708   1.00 29.82  ? 707  PRO   B CA  1 
ATOM   6648  C  C   . PRO   B  1 406 ? -4.315  -14.417 -1.647   1.00 25.71  ? 707  PRO   B C   1 
ATOM   6649  O  O   . PRO   B  1 406 ? -3.754  -13.735 -2.498   1.00 20.80  ? 707  PRO   B O   1 
ATOM   6650  C  CB  . PRO   B  1 406 ? -3.165  -14.481 0.562    1.00 28.32  ? 707  PRO   B CB  1 
ATOM   6651  C  CG  . PRO   B  1 406 ? -1.781  -14.892 0.903    1.00 28.93  ? 707  PRO   B CG  1 
ATOM   6652  C  CD  . PRO   B  1 406 ? -1.101  -15.111 -0.407   1.00 29.31  ? 707  PRO   B CD  1 
ATOM   6653  N  N   . SER   B  1 407 ? -5.631  -14.450 -1.499   1.00 26.30  ? 708  SER   B N   1 
ATOM   6654  C  CA  . SER   B  1 407 ? -6.460  -13.748 -2.453   1.00 27.24  ? 708  SER   B CA  1 
ATOM   6655  C  C   . SER   B  1 407 ? -7.756  -13.345 -1.782   1.00 22.28  ? 708  SER   B C   1 
ATOM   6656  O  O   . SER   B  1 407 ? -8.164  -13.923 -0.772   1.00 27.89  ? 708  SER   B O   1 
ATOM   6657  C  CB  . SER   B  1 407 ? -6.748  -14.612 -3.679   1.00 40.95  ? 708  SER   B CB  1 
ATOM   6658  O  OG  . SER   B  1 407 ? -7.546  -15.713 -3.314   1.00 52.11  ? 708  SER   B OG  1 
ATOM   6659  N  N   . PHE   B  1 408 ? -8.384  -12.323 -2.348   1.00 18.98  ? 709  PHE   B N   1 
ATOM   6660  C  CA  . PHE   B  1 408 ? -9.757  -11.994 -2.022   1.00 19.08  ? 709  PHE   B CA  1 
ATOM   6661  C  C   . PHE   B  1 408 ? -10.652 -12.679 -3.031   1.00 23.73  ? 709  PHE   B C   1 
ATOM   6662  O  O   . PHE   B  1 408 ? -10.371 -12.656 -4.234   1.00 26.07  ? 709  PHE   B O   1 
ATOM   6663  C  CB  . PHE   B  1 408 ? -9.995  -10.493 -2.055   1.00 18.98  ? 709  PHE   B CB  1 
ATOM   6664  C  CG  . PHE   B  1 408 ? -9.338  -9.779  -0.953   1.00 21.21  ? 709  PHE   B CG  1 
ATOM   6665  C  CD1 . PHE   B  1 408 ? -8.218  -8.994  -1.194   1.00 17.92  ? 709  PHE   B CD1 1 
ATOM   6666  C  CD2 . PHE   B  1 408 ? -9.827  -9.900  0.347    1.00 18.87  ? 709  PHE   B CD2 1 
ATOM   6667  C  CE1 . PHE   B  1 408 ? -7.599  -8.324  -0.145   1.00 26.46  ? 709  PHE   B CE1 1 
ATOM   6668  C  CE2 . PHE   B  1 408 ? -9.216  -9.234  1.389    1.00 23.90  ? 709  PHE   B CE2 1 
ATOM   6669  C  CZ  . PHE   B  1 408 ? -8.098  -8.447  1.147    1.00 18.57  ? 709  PHE   B CZ  1 
ATOM   6670  N  N   . GLU   B  1 409 ? -11.720 -13.285 -2.540   1.00 24.91  ? 710  GLU   B N   1 
ATOM   6671  C  CA  . GLU   B  1 409 ? -12.608 -14.078 -3.365   1.00 27.14  ? 710  GLU   B CA  1 
ATOM   6672  C  C   . GLU   B  1 409 ? -14.036 -13.626 -3.119   1.00 32.97  ? 710  GLU   B C   1 
ATOM   6673  O  O   . GLU   B  1 409 ? -14.374 -13.110 -2.042   1.00 22.76  ? 710  GLU   B O   1 
ATOM   6674  C  CB  . GLU   B  1 409 ? -12.488 -15.587 -3.048   1.00 32.31  ? 710  GLU   B CB  1 
ATOM   6675  C  CG  . GLU   B  1 409 ? -11.072 -16.171 -3.111   1.00 30.96  ? 710  GLU   B CG  1 
ATOM   6676  C  CD  . GLU   B  1 409 ? -10.577 -16.366 -4.546   1.00 46.39  ? 710  GLU   B CD  1 
ATOM   6677  O  OE1 . GLU   B  1 409 ? -11.356 -16.114 -5.487   1.00 49.82  ? 710  GLU   B OE1 1 
ATOM   6678  O  OE2 . GLU   B  1 409 ? -9.411  -16.770 -4.737   1.00 55.06  ? 710  GLU   B OE2 1 
ATOM   6679  N  N   . TYR   B  1 410 ? -14.879 -13.858 -4.116   1.00 25.87  ? 711  TYR   B N   1 
ATOM   6680  C  CA  . TYR   B  1 410 ? -16.308 -13.742 -3.895   1.00 25.02  ? 711  TYR   B CA  1 
ATOM   6681  C  C   . TYR   B  1 410 ? -16.812 -14.916 -3.068   1.00 26.41  ? 711  TYR   B C   1 
ATOM   6682  O  O   . TYR   B  1 410 ? -16.226 -16.002 -3.040   1.00 26.28  ? 711  TYR   B O   1 
ATOM   6683  C  CB  . TYR   B  1 410 ? -17.067 -13.709 -5.220   1.00 26.12  ? 711  TYR   B CB  1 
ATOM   6684  C  CG  . TYR   B  1 410 ? -16.796 -12.492 -6.052   1.00 44.40  ? 711  TYR   B CG  1 
ATOM   6685  C  CD1 . TYR   B  1 410 ? -16.222 -12.603 -7.310   1.00 54.33  ? 711  TYR   B CD1 1 
ATOM   6686  C  CD2 . TYR   B  1 410 ? -17.118 -11.228 -5.588   1.00 42.61  ? 711  TYR   B CD2 1 
ATOM   6687  C  CE1 . TYR   B  1 410 ? -15.986 -11.486 -8.087   1.00 51.45  ? 711  TYR   B CE1 1 
ATOM   6688  C  CE2 . TYR   B  1 410 ? -16.882 -10.109 -6.358   1.00 49.65  ? 711  TYR   B CE2 1 
ATOM   6689  C  CZ  . TYR   B  1 410 ? -16.321 -10.243 -7.607   1.00 44.97  ? 711  TYR   B CZ  1 
ATOM   6690  O  OH  . TYR   B  1 410 ? -16.093 -9.122  -8.366   1.00 39.56  ? 711  TYR   B OH  1 
ATOM   6691  N  N   . GLN   B  1 411 ? -17.927 -14.692 -2.403   1.00 27.02  ? 712  GLN   B N   1 
ATOM   6692  C  CA  . GLN   B  1 411 ? -18.604 -15.726 -1.643   1.00 27.51  ? 712  GLN   B CA  1 
ATOM   6693  C  C   . GLN   B  1 411 ? -20.086 -15.455 -1.779   1.00 26.95  ? 712  GLN   B C   1 
ATOM   6694  O  O   . GLN   B  1 411 ? -20.480 -14.334 -2.115   1.00 27.03  ? 712  GLN   B O   1 
ATOM   6695  C  CB  . GLN   B  1 411 ? -18.172 -15.720 -0.162   1.00 28.48  ? 712  GLN   B CB  1 
ATOM   6696  C  CG  . GLN   B  1 411 ? -18.344 -14.387 0.519    1.00 25.51  ? 712  GLN   B CG  1 
ATOM   6697  C  CD  . GLN   B  1 411 ? -17.899 -14.425 1.970    1.00 29.67  ? 712  GLN   B CD  1 
ATOM   6698  O  OE1 . GLN   B  1 411 ? -17.862 -15.484 2.588    1.00 30.38  ? 712  GLN   B OE1 1 
ATOM   6699  N  NE2 . GLN   B  1 411 ? -17.549 -13.274 2.509    1.00 23.20  ? 712  GLN   B NE2 1 
ATOM   6700  N  N   . PRO   B  1 412 ? -20.930 -16.452 -1.560   1.00 31.01  ? 713  PRO   B N   1 
ATOM   6701  C  CA  . PRO   B  1 412 ? -22.357 -16.208 -1.742   1.00 32.84  ? 713  PRO   B CA  1 
ATOM   6702  C  C   . PRO   B  1 412 ? -22.852 -15.205 -0.709   1.00 35.00  ? 713  PRO   B C   1 
ATOM   6703  O  O   . PRO   B  1 412 ? -22.260 -15.033 0.361    1.00 28.62  ? 713  PRO   B O   1 
ATOM   6704  C  CB  . PRO   B  1 412 ? -22.995 -17.597 -1.577   1.00 39.23  ? 713  PRO   B CB  1 
ATOM   6705  C  CG  . PRO   B  1 412 ? -21.955 -18.479 -0.976   1.00 36.32  ? 713  PRO   B CG  1 
ATOM   6706  C  CD  . PRO   B  1 412 ? -20.617 -17.857 -1.231   1.00 35.18  ? 713  PRO   B CD  1 
ATOM   6707  N  N   . ASP   B  1 413 ? -23.899 -14.478 -1.082   1.00 33.71  ? 714  ASP   B N   1 
ATOM   6708  C  CA  . ASP   B  1 413 ? -24.522 -13.557 -0.151   1.00 39.53  ? 714  ASP   B CA  1 
ATOM   6709  C  C   . ASP   B  1 413 ? -25.058 -14.335 1.046    1.00 39.80  ? 714  ASP   B C   1 
ATOM   6710  O  O   . ASP   B  1 413 ? -25.600 -15.435 0.880    1.00 34.34  ? 714  ASP   B O   1 
ATOM   6711  C  CB  . ASP   B  1 413 ? -25.655 -12.789 -0.827   1.00 43.99  ? 714  ASP   B CB  1 
ATOM   6712  C  CG  . ASP   B  1 413 ? -25.149 -11.768 -1.818   1.00 50.88  ? 714  ASP   B CG  1 
ATOM   6713  O  OD1 . ASP   B  1 413 ? -24.136 -11.101 -1.522   1.00 48.38  ? 714  ASP   B OD1 1 
ATOM   6714  O  OD2 . ASP   B  1 413 ? -25.764 -11.638 -2.897   1.00 56.33  ? 714  ASP   B OD2 1 
ATOM   6715  N  N   . PRO   B  1 414 ? -24.928 -13.794 2.259    1.00 30.20  ? 715  PRO   B N   1 
ATOM   6716  C  CA  . PRO   B  1 414 ? -25.288 -14.583 3.444    1.00 30.82  ? 715  PRO   B CA  1 
ATOM   6717  C  C   . PRO   B  1 414 ? -26.751 -14.945 3.501    1.00 30.79  ? 715  PRO   B C   1 
ATOM   6718  O  O   . PRO   B  1 414 ? -27.090 -16.023 4.004    1.00 35.03  ? 715  PRO   B O   1 
ATOM   6719  C  CB  . PRO   B  1 414 ? -24.901 -13.671 4.621    1.00 31.48  ? 715  PRO   B CB  1 
ATOM   6720  C  CG  . PRO   B  1 414 ? -24.251 -12.466 4.038    1.00 26.94  ? 715  PRO   B CG  1 
ATOM   6721  C  CD  . PRO   B  1 414 ? -24.532 -12.415 2.580    1.00 30.78  ? 715  PRO   B CD  1 
ATOM   6722  N  N   . TRP   B  1 415 ? -27.634 -14.067 3.024    1.00 35.27  ? 716  TRP   B N   1 
ATOM   6723  C  CA  . TRP   B  1 415 ? -29.058 -14.356 3.103    1.00 37.59  ? 716  TRP   B CA  1 
ATOM   6724  C  C   . TRP   B  1 415 ? -29.479 -15.496 2.186    1.00 42.64  ? 716  TRP   B C   1 
ATOM   6725  O  O   . TRP   B  1 415 ? -30.595 -16.005 2.328    1.00 44.51  ? 716  TRP   B O   1 
ATOM   6726  C  CB  . TRP   B  1 415 ? -29.870 -13.101 2.791    1.00 36.13  ? 716  TRP   B CB  1 
ATOM   6727  C  CG  . TRP   B  1 415 ? -29.461 -12.390 1.547    1.00 36.51  ? 716  TRP   B CG  1 
ATOM   6728  C  CD1 . TRP   B  1 415 ? -29.935 -12.605 0.283    1.00 35.20  ? 716  TRP   B CD1 1 
ATOM   6729  C  CD2 . TRP   B  1 415 ? -28.506 -11.326 1.444    1.00 34.52  ? 716  TRP   B CD2 1 
ATOM   6730  N  NE1 . TRP   B  1 415 ? -29.327 -11.742 -0.601   1.00 34.87  ? 716  TRP   B NE1 1 
ATOM   6731  C  CE2 . TRP   B  1 415 ? -28.445 -10.949 0.085    1.00 34.21  ? 716  TRP   B CE2 1 
ATOM   6732  C  CE3 . TRP   B  1 415 ? -27.694 -10.659 2.366    1.00 31.98  ? 716  TRP   B CE3 1 
ATOM   6733  C  CZ2 . TRP   B  1 415 ? -27.604 -9.933  -0.373   1.00 32.94  ? 716  TRP   B CZ2 1 
ATOM   6734  C  CZ3 . TRP   B  1 415 ? -26.860 -9.651  1.908    1.00 38.82  ? 716  TRP   B CZ3 1 
ATOM   6735  C  CH2 . TRP   B  1 415 ? -26.822 -9.300  0.545    1.00 35.60  ? 716  TRP   B CH2 1 
ATOM   6736  N  N   . ASN   B  1 416 ? -28.620 -15.924 1.267    1.00 40.21  ? 717  ASN   B N   1 
ATOM   6737  C  CA  . ASN   B  1 416 ? -28.935 -17.090 0.450    1.00 45.85  ? 717  ASN   B CA  1 
ATOM   6738  C  C   . ASN   B  1 416 ? -28.502 -18.402 1.085    1.00 42.13  ? 717  ASN   B C   1 
ATOM   6739  O  O   . ASN   B  1 416 ? -29.035 -19.450 0.726    1.00 49.31  ? 717  ASN   B O   1 
ATOM   6740  C  CB  . ASN   B  1 416 ? -28.287 -16.964 -0.928   1.00 40.22  ? 717  ASN   B CB  1 
ATOM   6741  C  CG  . ASN   B  1 416 ? -28.738 -15.729 -1.660   1.00 39.86  ? 717  ASN   B CG  1 
ATOM   6742  O  OD1 . ASN   B  1 416 ? -29.878 -15.284 -1.514   1.00 44.07  ? 717  ASN   B OD1 1 
ATOM   6743  N  ND2 . ASN   B  1 416 ? -27.846 -15.158 -2.446   1.00 37.99  ? 717  ASN   B ND2 1 
ATOM   6744  N  N   . THR   B  1 417 ? -27.557 -18.378 2.019    1.00 41.76  ? 718  THR   B N   1 
ATOM   6745  C  CA  . THR   B  1 417 ? -27.088 -19.603 2.642    1.00 45.02  ? 718  THR   B CA  1 
ATOM   6746  C  C   . THR   B  1 417 ? -27.429 -19.709 4.120    1.00 42.87  ? 718  THR   B C   1 
ATOM   6747  O  O   . THR   B  1 417 ? -27.510 -20.827 4.636    1.00 44.57  ? 718  THR   B O   1 
ATOM   6748  C  CB  . THR   B  1 417 ? -25.572 -19.727 2.475    1.00 42.12  ? 718  THR   B CB  1 
ATOM   6749  O  OG1 . THR   B  1 417 ? -24.957 -18.534 2.974    1.00 37.93  ? 718  THR   B OG1 1 
ATOM   6750  C  CG2 . THR   B  1 417 ? -25.226 -19.883 0.993    1.00 38.67  ? 718  THR   B CG2 1 
ATOM   6751  N  N   . HIS   B  1 418 ? -27.649 -18.590 4.802    1.00 35.61  ? 719  HIS   B N   1 
ATOM   6752  C  CA  . HIS   B  1 418 ? -27.846 -18.632 6.242    1.00 33.87  ? 719  HIS   B CA  1 
ATOM   6753  C  C   . HIS   B  1 418 ? -29.162 -19.300 6.598    1.00 39.94  ? 719  HIS   B C   1 
ATOM   6754  O  O   . HIS   B  1 418 ? -30.205 -19.014 6.007    1.00 42.00  ? 719  HIS   B O   1 
ATOM   6755  C  CB  . HIS   B  1 418 ? -27.825 -17.229 6.828    1.00 32.47  ? 719  HIS   B CB  1 
ATOM   6756  C  CG  . HIS   B  1 418 ? -28.067 -17.205 8.301    1.00 38.00  ? 719  HIS   B CG  1 
ATOM   6757  N  ND1 . HIS   B  1 418 ? -27.135 -17.655 9.210    1.00 31.29  ? 719  HIS   B ND1 1 
ATOM   6758  C  CD2 . HIS   B  1 418 ? -29.142 -16.811 9.022    1.00 35.04  ? 719  HIS   B CD2 1 
ATOM   6759  C  CE1 . HIS   B  1 418 ? -27.621 -17.522 10.432   1.00 39.49  ? 719  HIS   B CE1 1 
ATOM   6760  N  NE2 . HIS   B  1 418 ? -28.836 -17.010 10.345   1.00 37.21  ? 719  HIS   B NE2 1 
ATOM   6761  N  N   . VAL   B  1 419 ? -29.119 -20.185 7.580    1.00 43.32  ? 720  VAL   B N   1 
ATOM   6762  C  CA  . VAL   B  1 419 ? -30.325 -20.821 8.083    1.00 51.17  ? 720  VAL   B CA  1 
ATOM   6763  C  C   . VAL   B  1 419 ? -30.627 -20.216 9.449    1.00 41.20  ? 720  VAL   B C   1 
ATOM   6764  O  O   . VAL   B  1 419 ? -29.824 -20.319 10.385   1.00 39.44  ? 720  VAL   B O   1 
ATOM   6765  C  CB  . VAL   B  1 419 ? -30.189 -22.349 8.123    1.00 62.90  ? 720  VAL   B CB  1 
ATOM   6766  C  CG1 . VAL   B  1 419 ? -30.370 -22.908 6.701    1.00 54.74  ? 720  VAL   B CG1 1 
ATOM   6767  C  CG2 . VAL   B  1 419 ? -28.837 -22.755 8.689    1.00 67.50  ? 720  VAL   B CG2 1 
ATOM   6768  N  N   . TRP   B  1 420 ? -31.775 -19.555 9.536    1.00 41.45  ? 721  TRP   B N   1 
ATOM   6769  C  CA  . TRP   B  1 420 ? -32.182 -18.751 10.675   1.00 48.63  ? 721  TRP   B CA  1 
ATOM   6770  C  C   . TRP   B  1 420 ? -32.546 -19.607 11.883   1.00 62.14  ? 721  TRP   B C   1 
ATOM   6771  O  O   . TRP   B  1 420 ? -32.979 -20.758 11.763   1.00 63.42  ? 721  TRP   B O   1 
ATOM   6772  C  CB  . TRP   B  1 420 ? -33.362 -17.875 10.279   1.00 40.80  ? 721  TRP   B CB  1 
ATOM   6773  C  CG  . TRP   B  1 420 ? -32.955 -16.814 9.340    1.00 37.67  ? 721  TRP   B CG  1 
ATOM   6774  C  CD1 . TRP   B  1 420 ? -32.830 -16.911 7.971    1.00 36.34  ? 721  TRP   B CD1 1 
ATOM   6775  C  CD2 . TRP   B  1 420 ? -32.582 -15.483 9.685    1.00 31.27  ? 721  TRP   B CD2 1 
ATOM   6776  N  NE1 . TRP   B  1 420 ? -32.414 -15.707 7.453    1.00 30.06  ? 721  TRP   B NE1 1 
ATOM   6777  C  CE2 . TRP   B  1 420 ? -32.252 -14.814 8.482    1.00 33.49  ? 721  TRP   B CE2 1 
ATOM   6778  C  CE3 . TRP   B  1 420 ? -32.505 -14.782 10.894   1.00 33.43  ? 721  TRP   B CE3 1 
ATOM   6779  C  CZ2 . TRP   B  1 420 ? -31.853 -13.481 8.459    1.00 42.96  ? 721  TRP   B CZ2 1 
ATOM   6780  C  CZ3 . TRP   B  1 420 ? -32.105 -13.464 10.869   1.00 40.93  ? 721  TRP   B CZ3 1 
ATOM   6781  C  CH2 . TRP   B  1 420 ? -31.782 -12.824 9.659    1.00 44.07  ? 721  TRP   B CH2 1 
ATOM   6782  N  N   . LYS   B  1 421 ? -32.398 -19.001 13.067   1.00 70.23  ? 722  LYS   B N   1 
ATOM   6783  C  CA  . LYS   B  1 421 ? -32.555 -19.682 14.344   1.00 70.78  ? 722  LYS   B CA  1 
ATOM   6784  C  C   . LYS   B  1 421 ? -33.627 -19.089 15.252   1.00 83.84  ? 722  LYS   B C   1 
ATOM   6785  O  O   . LYS   B  1 421 ? -34.202 -19.832 16.052   1.00 88.87  ? 722  LYS   B O   1 
ATOM   6786  C  CB  . LYS   B  1 421 ? -31.215 -19.688 15.095   1.00 68.68  ? 722  LYS   B CB  1 
ATOM   6787  C  CG  . LYS   B  1 421 ? -30.012 -19.821 14.172   1.00 69.94  ? 722  LYS   B CG  1 
ATOM   6788  C  CD  . LYS   B  1 421 ? -28.809 -20.436 14.871   1.00 72.24  ? 722  LYS   B CD  1 
ATOM   6789  C  CE  . LYS   B  1 421 ? -27.720 -20.779 13.862   1.00 72.49  ? 722  LYS   B CE  1 
ATOM   6790  N  NZ  . LYS   B  1 421 ? -26.785 -21.831 14.355   1.00 74.34  ? 722  LYS   B NZ  1 
ATOM   6791  N  N   . LEU   B  1 422 ? -33.917 -17.789 15.153   1.00 64.75  ? 723  LEU   B N   1 
ATOM   6792  C  CA  . LEU   B  1 422 ? -34.853 -17.143 16.070   1.00 79.65  ? 723  LEU   B CA  1 
ATOM   6793  C  C   . LEU   B  1 422 ? -36.300 -17.533 15.744   1.00 89.61  ? 723  LEU   B C   1 
ATOM   6794  O  O   . LEU   B  1 422 ? -36.621 -17.969 14.632   1.00 88.13  ? 723  LEU   B O   1 
ATOM   6795  C  CB  . LEU   B  1 422 ? -34.673 -15.617 16.031   1.00 82.79  ? 723  LEU   B CB  1 
ATOM   6796  C  CG  . LEU   B  1 422 ? -35.548 -14.642 16.844   1.00 82.17  ? 723  LEU   B CG  1 
ATOM   6797  C  CD1 . LEU   B  1 422 ? -35.651 -15.042 18.314   1.00 83.44  ? 723  LEU   B CD1 1 
ATOM   6798  C  CD2 . LEU   B  1 422 ? -35.037 -13.203 16.723   1.00 76.82  ? 723  LEU   B CD2 1 
ATOM   6799  N  N   . VAL   B  1 423 ? -37.181 -17.329 16.734   1.00 93.14  ? 724  VAL   B N   1 
ATOM   6800  C  CA  . VAL   B  1 423 ? -38.555 -17.866 16.803   1.00 83.13  ? 724  VAL   B CA  1 
ATOM   6801  C  C   . VAL   B  1 423 ? -38.641 -19.278 16.219   1.00 80.86  ? 724  VAL   B C   1 
ATOM   6802  O  O   . VAL   B  1 423 ? -39.665 -19.659 15.655   1.00 84.57  ? 724  VAL   B O   1 
ATOM   6803  C  CB  . VAL   B  1 423 ? -39.630 -16.918 16.131   1.00 75.12  ? 724  VAL   B CB  1 
ATOM   6804  C  CG1 . VAL   B  1 423 ? -40.371 -16.094 17.196   1.00 71.81  ? 724  VAL   B CG1 1 
ATOM   6805  C  CG2 . VAL   B  1 423 ? -39.041 -16.002 15.055   1.00 68.09  ? 724  VAL   B CG2 1 
ATOM   6806  O  OXT . VAL   B  1 423 ? -37.711 -20.087 16.306   1.00 77.37  ? 724  VAL   B OXT 1 
ATOM   6807  N  N   . ARG   C  1 3   ? 33.323  -36.596 -61.368  1.00 69.38  ? 304  ARG   C N   1 
ATOM   6808  C  CA  . ARG   C  1 3   ? 34.154  -37.031 -62.485  1.00 73.11  ? 304  ARG   C CA  1 
ATOM   6809  C  C   . ARG   C  1 3   ? 34.120  -38.558 -62.668  1.00 71.51  ? 304  ARG   C C   1 
ATOM   6810  O  O   . ARG   C  1 3   ? 34.241  -39.067 -63.786  1.00 78.54  ? 304  ARG   C O   1 
ATOM   6811  C  CB  . ARG   C  1 3   ? 35.595  -36.554 -62.291  1.00 78.66  ? 304  ARG   C CB  1 
ATOM   6812  C  CG  . ARG   C  1 3   ? 36.500  -36.902 -63.457  1.00 86.23  ? 304  ARG   C CG  1 
ATOM   6813  C  CD  . ARG   C  1 3   ? 37.604  -35.888 -63.655  1.00 93.19  ? 304  ARG   C CD  1 
ATOM   6814  N  NE  . ARG   C  1 3   ? 38.039  -35.863 -65.048  1.00 99.91  ? 304  ARG   C NE  1 
ATOM   6815  C  CZ  . ARG   C  1 3   ? 37.325  -35.342 -66.043  1.00 105.77 ? 304  ARG   C CZ  1 
ATOM   6816  N  NH1 . ARG   C  1 3   ? 36.135  -34.805 -65.801  1.00 106.44 ? 304  ARG   C NH1 1 
ATOM   6817  N  NH2 . ARG   C  1 3   ? 37.797  -35.362 -67.284  1.00 107.38 ? 304  ARG   C NH2 1 
ATOM   6818  N  N   . PHE   C  1 4   ? 33.954  -39.283 -61.565  1.00 51.26  ? 305  PHE   C N   1 
ATOM   6819  C  CA  . PHE   C  1 4   ? 33.926  -40.739 -61.572  1.00 49.85  ? 305  PHE   C CA  1 
ATOM   6820  C  C   . PHE   C  1 4   ? 32.767  -41.193 -60.696  1.00 46.76  ? 305  PHE   C C   1 
ATOM   6821  O  O   . PHE   C  1 4   ? 32.537  -40.624 -59.628  1.00 45.02  ? 305  PHE   C O   1 
ATOM   6822  C  CB  . PHE   C  1 4   ? 35.254  -41.349 -61.037  1.00 65.96  ? 305  PHE   C CB  1 
ATOM   6823  C  CG  . PHE   C  1 4   ? 36.465  -41.132 -61.936  1.00 81.67  ? 305  PHE   C CG  1 
ATOM   6824  C  CD1 . PHE   C  1 4   ? 37.102  -39.900 -62.000  1.00 89.84  ? 305  PHE   C CD1 1 
ATOM   6825  C  CD2 . PHE   C  1 4   ? 36.996  -42.180 -62.678  1.00 82.49  ? 305  PHE   C CD2 1 
ATOM   6826  C  CE1 . PHE   C  1 4   ? 38.222  -39.716 -62.817  1.00 89.74  ? 305  PHE   C CE1 1 
ATOM   6827  C  CE2 . PHE   C  1 4   ? 38.113  -42.002 -63.490  1.00 81.04  ? 305  PHE   C CE2 1 
ATOM   6828  C  CZ  . PHE   C  1 4   ? 38.723  -40.770 -63.561  1.00 84.28  ? 305  PHE   C CZ  1 
ATOM   6829  N  N   . LEU   C  1 5   ? 32.030  -42.205 -61.144  1.00 37.36  ? 306  LEU   C N   1 
ATOM   6830  C  CA  . LEU   C  1 5   ? 30.997  -42.821 -60.320  1.00 35.42  ? 306  LEU   C CA  1 
ATOM   6831  C  C   . LEU   C  1 5   ? 31.268  -44.312 -60.235  1.00 34.84  ? 306  LEU   C C   1 
ATOM   6832  O  O   . LEU   C  1 5   ? 31.624  -44.938 -61.233  1.00 35.61  ? 306  LEU   C O   1 
ATOM   6833  C  CB  . LEU   C  1 5   ? 29.595  -42.582 -60.881  1.00 31.65  ? 306  LEU   C CB  1 
ATOM   6834  C  CG  . LEU   C  1 5   ? 29.055  -41.155 -60.811  1.00 34.55  ? 306  LEU   C CG  1 
ATOM   6835  C  CD1 . LEU   C  1 5   ? 27.797  -41.035 -61.655  1.00 35.59  ? 306  LEU   C CD1 1 
ATOM   6836  C  CD2 . LEU   C  1 5   ? 28.764  -40.773 -59.366  1.00 33.67  ? 306  LEU   C CD2 1 
ATOM   6837  N  N   . LYS   C  1 6   ? 31.118  -44.884 -59.047  1.00 36.51  ? 307  LYS   C N   1 
ATOM   6838  C  CA  . LYS   C  1 6   ? 31.386  -46.303 -58.867  1.00 39.37  ? 307  LYS   C CA  1 
ATOM   6839  C  C   . LYS   C  1 6   ? 30.082  -47.077 -58.763  1.00 32.15  ? 307  LYS   C C   1 
ATOM   6840  O  O   . LYS   C  1 6   ? 29.104  -46.593 -58.193  1.00 36.85  ? 307  LYS   C O   1 
ATOM   6841  C  CB  . LYS   C  1 6   ? 32.254  -46.555 -57.633  1.00 42.09  ? 307  LYS   C CB  1 
ATOM   6842  C  CG  . LYS   C  1 6   ? 33.694  -46.094 -57.804  1.00 45.71  ? 307  LYS   C CG  1 
ATOM   6843  C  CD  . LYS   C  1 6   ? 34.582  -46.632 -56.688  1.00 56.99  ? 307  LYS   C CD  1 
ATOM   6844  C  CE  . LYS   C  1 6   ? 35.982  -46.051 -56.771  1.00 57.99  ? 307  LYS   C CE  1 
ATOM   6845  N  NZ  . LYS   C  1 6   ? 36.443  -45.976 -58.186  1.00 59.72  ? 307  LYS   C NZ  1 
ATOM   6846  N  N   . VAL   C  1 7   ? 30.064  -48.268 -59.350  1.00 28.47  ? 308  VAL   C N   1 
ATOM   6847  C  CA  . VAL   C  1 7   ? 28.954  -49.195 -59.194  1.00 25.25  ? 308  VAL   C CA  1 
ATOM   6848  C  C   . VAL   C  1 7   ? 29.528  -50.504 -58.695  1.00 29.04  ? 308  VAL   C C   1 
ATOM   6849  O  O   . VAL   C  1 7   ? 30.611  -50.923 -59.118  1.00 34.74  ? 308  VAL   C O   1 
ATOM   6850  C  CB  . VAL   C  1 7   ? 28.142  -49.419 -60.489  1.00 30.26  ? 308  VAL   C CB  1 
ATOM   6851  C  CG1 . VAL   C  1 7   ? 27.523  -48.119 -60.960  1.00 36.18  ? 308  VAL   C CG1 1 
ATOM   6852  C  CG2 . VAL   C  1 7   ? 28.995  -50.055 -61.580  1.00 28.40  ? 308  VAL   C CG2 1 
ATOM   6853  N  N   . LYS   C  1 8   ? 28.792  -51.149 -57.807  1.00 29.01  ? 309  LYS   C N   1 
ATOM   6854  C  CA  . LYS   C  1 8   ? 29.247  -52.340 -57.111  1.00 30.44  ? 309  LYS   C CA  1 
ATOM   6855  C  C   . LYS   C  1 8   ? 28.313  -53.493 -57.424  1.00 30.33  ? 309  LYS   C C   1 
ATOM   6856  O  O   . LYS   C  1 8   ? 27.089  -53.327 -57.451  1.00 28.20  ? 309  LYS   C O   1 
ATOM   6857  C  CB  . LYS   C  1 8   ? 29.286  -52.089 -55.589  1.00 29.21  ? 309  LYS   C CB  1 
ATOM   6858  C  CG  . LYS   C  1 8   ? 29.584  -53.294 -54.726  1.00 26.51  ? 309  LYS   C CG  1 
ATOM   6859  C  CD  . LYS   C  1 8   ? 29.888  -52.823 -53.289  1.00 26.98  ? 309  LYS   C CD  1 
ATOM   6860  C  CE  . LYS   C  1 8   ? 30.100  -53.995 -52.356  1.00 35.47  ? 309  LYS   C CE  1 
ATOM   6861  N  NZ  . LYS   C  1 8   ? 30.189  -53.546 -50.940  1.00 44.31  ? 309  LYS   C NZ  1 
ATOM   6862  N  N   . ASN   C  1 9   ? 28.894  -54.659 -57.656  1.00 23.84  ? 310  ASN   C N   1 
ATOM   6863  C  CA  . ASN   C  1 9   ? 28.134  -55.891 -57.662  1.00 28.03  ? 310  ASN   C CA  1 
ATOM   6864  C  C   . ASN   C  1 9   ? 28.195  -56.469 -56.254  1.00 30.69  ? 310  ASN   C C   1 
ATOM   6865  O  O   . ASN   C  1 9   ? 29.282  -56.729 -55.730  1.00 30.45  ? 310  ASN   C O   1 
ATOM   6866  C  CB  . ASN   C  1 9   ? 28.676  -56.876 -58.693  1.00 26.97  ? 310  ASN   C CB  1 
ATOM   6867  C  CG  . ASN   C  1 9   ? 27.803  -58.088 -58.820  1.00 29.15  ? 310  ASN   C CG  1 
ATOM   6868  O  OD1 . ASN   C  1 9   ? 27.631  -58.854 -57.855  1.00 33.14  ? 310  ASN   C OD1 1 
ATOM   6869  N  ND2 . ASN   C  1 9   ? 27.227  -58.277 -59.999  1.00 29.13  ? 310  ASN   C ND2 1 
ATOM   6870  N  N   . TRP   C  1 10  ? 27.034  -56.632 -55.632  1.00 26.04  ? 311  TRP   C N   1 
ATOM   6871  C  CA  . TRP   C  1 10  ? 26.995  -57.060 -54.240  1.00 32.48  ? 311  TRP   C CA  1 
ATOM   6872  C  C   . TRP   C  1 10  ? 27.145  -58.563 -54.090  1.00 33.09  ? 311  TRP   C C   1 
ATOM   6873  O  O   . TRP   C  1 10  ? 27.379  -59.047 -52.980  1.00 33.75  ? 311  TRP   C O   1 
ATOM   6874  C  CB  . TRP   C  1 10  ? 25.699  -56.573 -53.596  1.00 25.53  ? 311  TRP   C CB  1 
ATOM   6875  C  CG  . TRP   C  1 10  ? 25.720  -55.106 -53.440  1.00 31.19  ? 311  TRP   C CG  1 
ATOM   6876  C  CD1 . TRP   C  1 10  ? 25.321  -54.165 -54.357  1.00 24.44  ? 311  TRP   C CD1 1 
ATOM   6877  C  CD2 . TRP   C  1 10  ? 26.214  -54.385 -52.311  1.00 33.07  ? 311  TRP   C CD2 1 
ATOM   6878  N  NE1 . TRP   C  1 10  ? 25.526  -52.896 -53.848  1.00 26.59  ? 311  TRP   C NE1 1 
ATOM   6879  C  CE2 . TRP   C  1 10  ? 26.070  -53.008 -52.593  1.00 28.63  ? 311  TRP   C CE2 1 
ATOM   6880  C  CE3 . TRP   C  1 10  ? 26.750  -54.771 -51.075  1.00 37.75  ? 311  TRP   C CE3 1 
ATOM   6881  C  CZ2 . TRP   C  1 10  ? 26.457  -52.022 -51.692  1.00 32.31  ? 311  TRP   C CZ2 1 
ATOM   6882  C  CZ3 . TRP   C  1 10  ? 27.121  -53.791 -50.178  1.00 43.18  ? 311  TRP   C CZ3 1 
ATOM   6883  C  CH2 . TRP   C  1 10  ? 26.974  -52.432 -50.489  1.00 43.80  ? 311  TRP   C CH2 1 
ATOM   6884  N  N   . GLU   C  1 11  ? 27.025  -59.305 -55.181  1.00 26.07  ? 312  GLU   C N   1 
ATOM   6885  C  CA  . GLU   C  1 11  ? 27.275  -60.740 -55.159  1.00 34.10  ? 312  GLU   C CA  1 
ATOM   6886  C  C   . GLU   C  1 11  ? 28.767  -61.039 -55.257  1.00 35.67  ? 312  GLU   C C   1 
ATOM   6887  O  O   . GLU   C  1 11  ? 29.293  -61.862 -54.499  1.00 35.34  ? 312  GLU   C O   1 
ATOM   6888  C  CB  . GLU   C  1 11  ? 26.512  -61.400 -56.308  1.00 34.57  ? 312  GLU   C CB  1 
ATOM   6889  C  CG  . GLU   C  1 11  ? 26.482  -62.900 -56.260  1.00 43.17  ? 312  GLU   C CG  1 
ATOM   6890  C  CD  . GLU   C  1 11  ? 26.109  -63.535 -57.593  1.00 48.01  ? 312  GLU   C CD  1 
ATOM   6891  O  OE1 . GLU   C  1 11  ? 25.413  -62.891 -58.408  1.00 42.98  ? 312  GLU   C OE1 1 
ATOM   6892  O  OE2 . GLU   C  1 11  ? 26.525  -64.691 -57.826  1.00 54.01  ? 312  GLU   C OE2 1 
ATOM   6893  N  N   . THR   C  1 12  ? 29.467  -60.351 -56.154  1.00 33.82  ? 313  THR   C N   1 
ATOM   6894  C  CA  . THR   C  1 12  ? 30.862  -60.625 -56.468  1.00 34.58  ? 313  THR   C CA  1 
ATOM   6895  C  C   . THR   C  1 12  ? 31.832  -59.637 -55.838  1.00 37.19  ? 313  THR   C C   1 
ATOM   6896  O  O   . THR   C  1 12  ? 33.039  -59.898 -55.841  1.00 41.05  ? 313  THR   C O   1 
ATOM   6897  C  CB  . THR   C  1 12  ? 31.075  -60.597 -57.985  1.00 35.45  ? 313  THR   C CB  1 
ATOM   6898  O  OG1 . THR   C  1 12  ? 30.831  -59.268 -58.458  1.00 32.89  ? 313  THR   C OG1 1 
ATOM   6899  C  CG2 . THR   C  1 12  ? 30.119  -61.563 -58.708  1.00 36.37  ? 313  THR   C CG2 1 
ATOM   6900  N  N   . GLU   C  1 13  ? 31.346  -58.504 -55.330  1.00 35.38  ? 314  GLU   C N   1 
ATOM   6901  C  CA  . GLU   C  1 13  ? 32.138  -57.394 -54.788  1.00 43.80  ? 314  GLU   C CA  1 
ATOM   6902  C  C   . GLU   C  1 13  ? 32.872  -56.608 -55.868  1.00 36.58  ? 314  GLU   C C   1 
ATOM   6903  O  O   . GLU   C  1 13  ? 33.591  -55.656 -55.535  1.00 37.13  ? 314  GLU   C O   1 
ATOM   6904  C  CB  . GLU   C  1 13  ? 33.173  -57.838 -53.742  1.00 50.39  ? 314  GLU   C CB  1 
ATOM   6905  C  CG  . GLU   C  1 13  ? 32.665  -58.795 -52.705  1.00 55.93  ? 314  GLU   C CG  1 
ATOM   6906  C  CD  . GLU   C  1 13  ? 32.122  -58.083 -51.510  1.00 70.80  ? 314  GLU   C CD  1 
ATOM   6907  O  OE1 . GLU   C  1 13  ? 31.406  -57.077 -51.697  1.00 79.22  ? 314  GLU   C OE1 1 
ATOM   6908  O  OE2 . GLU   C  1 13  ? 32.428  -58.517 -50.382  1.00 70.06  ? 314  GLU   C OE2 1 
ATOM   6909  N  N   . VAL   C  1 14  ? 32.732  -56.979 -57.144  1.00 38.27  ? 315  VAL   C N   1 
ATOM   6910  C  CA  . VAL   C  1 14  ? 33.363  -56.228 -58.219  1.00 39.23  ? 315  VAL   C CA  1 
ATOM   6911  C  C   . VAL   C  1 14  ? 32.855  -54.798 -58.204  1.00 38.81  ? 315  VAL   C C   1 
ATOM   6912  O  O   . VAL   C  1 14  ? 31.649  -54.550 -58.071  1.00 35.26  ? 315  VAL   C O   1 
ATOM   6913  C  CB  . VAL   C  1 14  ? 33.082  -56.895 -59.574  1.00 39.77  ? 315  VAL   C CB  1 
ATOM   6914  C  CG1 . VAL   C  1 14  ? 33.503  -55.979 -60.723  1.00 36.63  ? 315  VAL   C CG1 1 
ATOM   6915  C  CG2 . VAL   C  1 14  ? 33.775  -58.255 -59.670  1.00 41.19  ? 315  VAL   C CG2 1 
ATOM   6916  N  N   . VAL   C  1 15  ? 33.776  -53.845 -58.332  1.00 33.91  ? 316  VAL   C N   1 
ATOM   6917  C  CA  . VAL   C  1 15  ? 33.436  -52.432 -58.448  1.00 35.35  ? 316  VAL   C CA  1 
ATOM   6918  C  C   . VAL   C  1 15  ? 33.911  -51.930 -59.806  1.00 36.92  ? 316  VAL   C C   1 
ATOM   6919  O  O   . VAL   C  1 15  ? 35.060  -52.162 -60.199  1.00 31.07  ? 316  VAL   C O   1 
ATOM   6920  C  CB  . VAL   C  1 15  ? 34.045  -51.601 -57.308  1.00 39.51  ? 316  VAL   C CB  1 
ATOM   6921  C  CG1 . VAL   C  1 15  ? 33.676  -50.125 -57.472  1.00 37.20  ? 316  VAL   C CG1 1 
ATOM   6922  C  CG2 . VAL   C  1 15  ? 33.572  -52.139 -55.958  1.00 37.23  ? 316  VAL   C CG2 1 
ATOM   6923  N  N   . LEU   C  1 16  ? 33.018  -51.266 -60.524  1.00 38.94  ? 317  LEU   C N   1 
ATOM   6924  C  CA  . LEU   C  1 16  ? 33.316  -50.656 -61.808  1.00 38.61  ? 317  LEU   C CA  1 
ATOM   6925  C  C   . LEU   C  1 16  ? 33.190  -49.148 -61.672  1.00 37.74  ? 317  LEU   C C   1 
ATOM   6926  O  O   . LEU   C  1 16  ? 32.469  -48.645 -60.803  1.00 36.31  ? 317  LEU   C O   1 
ATOM   6927  C  CB  . LEU   C  1 16  ? 32.372  -51.161 -62.890  1.00 33.33  ? 317  LEU   C CB  1 
ATOM   6928  C  CG  . LEU   C  1 16  ? 32.275  -52.680 -63.022  1.00 32.84  ? 317  LEU   C CG  1 
ATOM   6929  C  CD1 . LEU   C  1 16  ? 31.083  -53.029 -63.865  1.00 29.56  ? 317  LEU   C CD1 1 
ATOM   6930  C  CD2 . LEU   C  1 16  ? 33.541  -53.247 -63.634  1.00 38.60  ? 317  LEU   C CD2 1 
ATOM   6931  N  N   . THR   C  1 17  ? 33.901  -48.428 -62.530  1.00 28.23  ? 318  THR   C N   1 
ATOM   6932  C  CA  . THR   C  1 17  ? 33.996  -46.981 -62.426  1.00 34.45  ? 318  THR   C CA  1 
ATOM   6933  C  C   . THR   C  1 17  ? 33.484  -46.361 -63.710  1.00 35.03  ? 318  THR   C C   1 
ATOM   6934  O  O   . THR   C  1 17  ? 34.036  -46.602 -64.789  1.00 31.91  ? 318  THR   C O   1 
ATOM   6935  C  CB  . THR   C  1 17  ? 35.426  -46.524 -62.155  1.00 37.86  ? 318  THR   C CB  1 
ATOM   6936  O  OG1 . THR   C  1 17  ? 35.871  -47.063 -60.906  1.00 47.22  ? 318  THR   C OG1 1 
ATOM   6937  C  CG2 . THR   C  1 17  ? 35.458  -45.020 -62.079  1.00 32.01  ? 318  THR   C CG2 1 
ATOM   6938  N  N   . ASP   C  1 18  ? 32.439  -45.558 -63.589  1.00 30.49  ? 319  ASP   C N   1 
ATOM   6939  C  CA  . ASP   C  1 18  ? 31.756  -45.012 -64.746  1.00 31.79  ? 319  ASP   C CA  1 
ATOM   6940  C  C   . ASP   C  1 18  ? 32.241  -43.595 -64.981  1.00 33.79  ? 319  ASP   C C   1 
ATOM   6941  O  O   . ASP   C  1 18  ? 32.050  -42.723 -64.131  1.00 34.87  ? 319  ASP   C O   1 
ATOM   6942  C  CB  . ASP   C  1 18  ? 30.249  -45.034 -64.539  1.00 27.06  ? 319  ASP   C CB  1 
ATOM   6943  C  CG  . ASP   C  1 18  ? 29.494  -44.642 -65.779  1.00 30.87  ? 319  ASP   C CG  1 
ATOM   6944  O  OD1 . ASP   C  1 18  ? 29.641  -43.480 -66.226  1.00 33.02  ? 319  ASP   C OD1 1 
ATOM   6945  O  OD2 . ASP   C  1 18  ? 28.766  -45.506 -66.310  1.00 37.17  ? 319  ASP   C OD2 1 
ATOM   6946  N  N   . THR   C  1 19  ? 32.886  -43.374 -66.124  1.00 31.06  ? 320  THR   C N   1 
ATOM   6947  C  CA  . THR   C  1 19  ? 33.173  -42.035 -66.607  1.00 35.56  ? 320  THR   C CA  1 
ATOM   6948  C  C   . THR   C  1 19  ? 32.302  -41.650 -67.785  1.00 37.28  ? 320  THR   C C   1 
ATOM   6949  O  O   . THR   C  1 19  ? 32.193  -40.458 -68.093  1.00 35.59  ? 320  THR   C O   1 
ATOM   6950  C  CB  . THR   C  1 19  ? 34.643  -41.917 -67.030  1.00 37.42  ? 320  THR   C CB  1 
ATOM   6951  O  OG1 . THR   C  1 19  ? 34.917  -42.896 -68.039  1.00 37.19  ? 320  THR   C OG1 1 
ATOM   6952  C  CG2 . THR   C  1 19  ? 35.540  -42.170 -65.850  1.00 33.12  ? 320  THR   C CG2 1 
ATOM   6953  N  N   . LEU   C  1 20  ? 31.681  -42.637 -68.439  1.00 32.39  ? 321  LEU   C N   1 
ATOM   6954  C  CA  . LEU   C  1 20  ? 30.902  -42.388 -69.642  1.00 29.87  ? 321  LEU   C CA  1 
ATOM   6955  C  C   . LEU   C  1 20  ? 29.669  -41.545 -69.361  1.00 30.94  ? 321  LEU   C C   1 
ATOM   6956  O  O   . LEU   C  1 20  ? 29.163  -40.880 -70.273  1.00 28.28  ? 321  LEU   C O   1 
ATOM   6957  C  CB  . LEU   C  1 20  ? 30.505  -43.724 -70.269  1.00 30.25  ? 321  LEU   C CB  1 
ATOM   6958  C  CG  . LEU   C  1 20  ? 29.705  -43.705 -71.572  1.00 33.30  ? 321  LEU   C CG  1 
ATOM   6959  C  CD1 . LEU   C  1 20  ? 30.481  -42.992 -72.687  1.00 32.03  ? 321  LEU   C CD1 1 
ATOM   6960  C  CD2 . LEU   C  1 20  ? 29.306  -45.130 -71.980  1.00 28.86  ? 321  LEU   C CD2 1 
ATOM   6961  N  N   . HIS   C  1 21  ? 29.177  -41.549 -68.121  1.00 27.35  ? 322  HIS   C N   1 
ATOM   6962  C  CA  . HIS   C  1 21  ? 27.983  -40.779 -67.798  1.00 23.19  ? 322  HIS   C CA  1 
ATOM   6963  C  C   . HIS   C  1 21  ? 28.195  -39.288 -67.986  1.00 24.97  ? 322  HIS   C C   1 
ATOM   6964  O  O   . HIS   C  1 21  ? 27.216  -38.547 -68.101  1.00 32.52  ? 322  HIS   C O   1 
ATOM   6965  C  CB  . HIS   C  1 21  ? 27.555  -41.043 -66.358  1.00 32.59  ? 322  HIS   C CB  1 
ATOM   6966  C  CG  . HIS   C  1 21  ? 28.482  -40.446 -65.355  1.00 32.39  ? 322  HIS   C CG  1 
ATOM   6967  N  ND1 . HIS   C  1 21  ? 29.670  -41.046 -64.996  1.00 35.76  ? 322  HIS   C ND1 1 
ATOM   6968  C  CD2 . HIS   C  1 21  ? 28.420  -39.285 -64.662  1.00 35.89  ? 322  HIS   C CD2 1 
ATOM   6969  C  CE1 . HIS   C  1 21  ? 30.287  -40.290 -64.105  1.00 40.33  ? 322  HIS   C CE1 1 
ATOM   6970  N  NE2 . HIS   C  1 21  ? 29.549  -39.219 -63.882  1.00 35.36  ? 322  HIS   C NE2 1 
ATOM   6971  N  N   . LEU   C  1 22  ? 29.447  -38.830 -68.024  1.00 29.97  ? 323  LEU   C N   1 
ATOM   6972  C  CA  . LEU   C  1 22  ? 29.725  -37.410 -68.230  1.00 36.38  ? 323  LEU   C CA  1 
ATOM   6973  C  C   . LEU   C  1 22  ? 29.388  -36.950 -69.640  1.00 39.47  ? 323  LEU   C C   1 
ATOM   6974  O  O   . LEU   C  1 22  ? 29.230  -35.746 -69.872  1.00 42.03  ? 323  LEU   C O   1 
ATOM   6975  C  CB  . LEU   C  1 22  ? 31.194  -37.121 -67.930  1.00 33.19  ? 323  LEU   C CB  1 
ATOM   6976  C  CG  . LEU   C  1 22  ? 31.622  -37.491 -66.506  1.00 44.04  ? 323  LEU   C CG  1 
ATOM   6977  C  CD1 . LEU   C  1 22  ? 33.138  -37.386 -66.362  1.00 39.13  ? 323  LEU   C CD1 1 
ATOM   6978  C  CD2 . LEU   C  1 22  ? 30.891  -36.636 -65.455  1.00 42.60  ? 323  LEU   C CD2 1 
ATOM   6979  N  N   . LYS   C  1 23  ? 29.276  -37.874 -70.585  1.00 32.10  ? 324  LYS   C N   1 
ATOM   6980  C  CA  . LYS   C  1 23  ? 28.874  -37.538 -71.938  1.00 36.27  ? 324  LYS   C CA  1 
ATOM   6981  C  C   . LYS   C  1 23  ? 27.378  -37.701 -72.152  1.00 40.16  ? 324  LYS   C C   1 
ATOM   6982  O  O   . LYS   C  1 23  ? 26.928  -37.753 -73.302  1.00 47.53  ? 324  LYS   C O   1 
ATOM   6983  C  CB  . LYS   C  1 23  ? 29.659  -38.388 -72.941  1.00 35.86  ? 324  LYS   C CB  1 
ATOM   6984  C  CG  . LYS   C  1 23  ? 31.168  -38.358 -72.698  1.00 51.59  ? 324  LYS   C CG  1 
ATOM   6985  C  CD  . LYS   C  1 23  ? 31.973  -38.678 -73.950  1.00 67.52  ? 324  LYS   C CD  1 
ATOM   6986  C  CE  . LYS   C  1 23  ? 31.998  -37.506 -74.934  1.00 74.22  ? 324  LYS   C CE  1 
ATOM   6987  N  NZ  . LYS   C  1 23  ? 32.925  -36.418 -74.508  1.00 76.02  ? 324  LYS   C NZ  1 
ATOM   6988  N  N   . SER   C  1 24  ? 26.593  -37.787 -71.080  1.00 31.81  ? 325  SER   C N   1 
ATOM   6989  C  CA  . SER   C  1 24  ? 25.164  -37.973 -71.267  1.00 37.86  ? 325  SER   C CA  1 
ATOM   6990  C  C   . SER   C  1 24  ? 24.497  -36.624 -71.528  1.00 40.99  ? 325  SER   C C   1 
ATOM   6991  O  O   . SER   C  1 24  ? 25.062  -35.565 -71.248  1.00 37.94  ? 325  SER   C O   1 
ATOM   6992  C  CB  . SER   C  1 24  ? 24.549  -38.682 -70.065  1.00 33.62  ? 325  SER   C CB  1 
ATOM   6993  O  OG  . SER   C  1 24  ? 24.830  -37.986 -68.868  1.00 49.75  ? 325  SER   C OG  1 
ATOM   6994  N  N   . THR   C  1 25  ? 23.289  -36.662 -72.096  1.00 58.29  ? 326  THR   C N   1 
ATOM   6995  C  CA  . THR   C  1 25  ? 22.788  -35.427 -72.692  1.00 75.77  ? 326  THR   C CA  1 
ATOM   6996  C  C   . THR   C  1 25  ? 21.333  -35.076 -72.365  1.00 71.21  ? 326  THR   C C   1 
ATOM   6997  O  O   . THR   C  1 25  ? 21.085  -33.994 -71.831  1.00 71.10  ? 326  THR   C O   1 
ATOM   6998  C  CB  . THR   C  1 25  ? 23.022  -35.468 -74.213  1.00 88.98  ? 326  THR   C CB  1 
ATOM   6999  O  OG1 . THR   C  1 25  ? 22.545  -34.259 -74.816  1.00 99.11  ? 326  THR   C OG1 1 
ATOM   7000  C  CG2 . THR   C  1 25  ? 22.369  -36.687 -74.868  1.00 85.69  ? 326  THR   C CG2 1 
ATOM   7001  N  N   . LEU   C  1 26  ? 20.361  -35.928 -72.686  1.00 71.42  ? 327  LEU   C N   1 
ATOM   7002  C  CA  . LEU   C  1 26  ? 18.983  -35.582 -72.368  1.00 74.14  ? 327  LEU   C CA  1 
ATOM   7003  C  C   . LEU   C  1 26  ? 18.664  -36.033 -70.946  1.00 65.82  ? 327  LEU   C C   1 
ATOM   7004  O  O   . LEU   C  1 26  ? 19.479  -36.659 -70.265  1.00 64.12  ? 327  LEU   C O   1 
ATOM   7005  C  CB  . LEU   C  1 26  ? 18.001  -36.188 -73.380  1.00 82.94  ? 327  LEU   C CB  1 
ATOM   7006  C  CG  . LEU   C  1 26  ? 16.491  -35.851 -73.320  1.00 86.87  ? 327  LEU   C CG  1 
ATOM   7007  C  CD1 . LEU   C  1 26  ? 16.216  -34.392 -73.705  1.00 91.00  ? 327  LEU   C CD1 1 
ATOM   7008  C  CD2 . LEU   C  1 26  ? 15.602  -36.815 -74.120  1.00 81.21  ? 327  LEU   C CD2 1 
ATOM   7009  N  N   . GLU   C  1 27  ? 17.453  -35.709 -70.503  1.00 61.82  ? 328  GLU   C N   1 
ATOM   7010  C  CA  . GLU   C  1 27  ? 17.001  -36.011 -69.159  1.00 52.50  ? 328  GLU   C CA  1 
ATOM   7011  C  C   . GLU   C  1 27  ? 16.781  -37.507 -68.957  1.00 42.03  ? 328  GLU   C C   1 
ATOM   7012  O  O   . GLU   C  1 27  ? 16.455  -38.246 -69.888  1.00 41.82  ? 328  GLU   C O   1 
ATOM   7013  C  CB  . GLU   C  1 27  ? 15.703  -35.263 -68.861  1.00 59.50  ? 328  GLU   C CB  1 
ATOM   7014  C  CG  . GLU   C  1 27  ? 15.868  -33.765 -68.710  1.00 72.77  ? 328  GLU   C CG  1 
ATOM   7015  C  CD  . GLU   C  1 27  ? 14.796  -33.158 -67.826  1.00 88.85  ? 328  GLU   C CD  1 
ATOM   7016  O  OE1 . GLU   C  1 27  ? 13.704  -33.761 -67.719  1.00 88.58  ? 328  GLU   C OE1 1 
ATOM   7017  O  OE2 . GLU   C  1 27  ? 15.049  -32.088 -67.226  1.00 98.20  ? 328  GLU   C OE2 1 
ATOM   7018  N  N   . THR   C  1 28  ? 16.987  -37.948 -67.711  1.00 40.19  ? 329  THR   C N   1 
ATOM   7019  C  CA  . THR   C  1 28  ? 16.525  -39.249 -67.243  1.00 37.80  ? 329  THR   C CA  1 
ATOM   7020  C  C   . THR   C  1 28  ? 15.079  -39.205 -66.784  1.00 34.54  ? 329  THR   C C   1 
ATOM   7021  O  O   . THR   C  1 28  ? 14.431  -40.253 -66.702  1.00 43.34  ? 329  THR   C O   1 
ATOM   7022  C  CB  . THR   C  1 28  ? 17.372  -39.744 -66.063  1.00 46.38  ? 329  THR   C CB  1 
ATOM   7023  O  OG1 . THR   C  1 28  ? 17.229  -38.851 -64.930  1.00 34.14  ? 329  THR   C OG1 1 
ATOM   7024  C  CG2 . THR   C  1 28  ? 18.831  -39.861 -66.465  1.00 51.55  ? 329  THR   C CG2 1 
ATOM   7025  N  N   . GLY   C  1 29  ? 14.566  -38.017 -66.486  1.00 29.99  ? 330  GLY   C N   1 
ATOM   7026  C  CA  . GLY   C  1 29  ? 13.318  -37.861 -65.785  1.00 32.49  ? 330  GLY   C CA  1 
ATOM   7027  C  C   . GLY   C  1 29  ? 13.476  -37.648 -64.295  1.00 32.85  ? 330  GLY   C C   1 
ATOM   7028  O  O   . GLY   C  1 29  ? 12.580  -37.073 -63.667  1.00 36.64  ? 330  GLY   C O   1 
ATOM   7029  N  N   . CYS   C  1 30  ? 14.592  -38.069 -63.713  1.00 26.92  ? 331  CYS   C N   1 
ATOM   7030  C  CA  . CYS   C  1 30  ? 14.728  -37.852 -62.280  1.00 26.58  ? 331  CYS   C CA  1 
ATOM   7031  C  C   . CYS   C  1 30  ? 15.172  -36.421 -62.008  1.00 35.27  ? 331  CYS   C C   1 
ATOM   7032  O  O   . CYS   C  1 30  ? 15.642  -35.704 -62.893  1.00 31.23  ? 331  CYS   C O   1 
ATOM   7033  C  CB  . CYS   C  1 30  ? 15.731  -38.823 -61.658  1.00 26.78  ? 331  CYS   C CB  1 
ATOM   7034  S  SG  . CYS   C  1 30  ? 15.494  -40.590 -62.024  1.00 27.20  ? 331  CYS   C SG  1 
ATOM   7035  N  N   . THR   C  1 31  ? 14.995  -36.001 -60.768  1.00 25.46  ? 332  THR   C N   1 
ATOM   7036  C  CA  . THR   C  1 31  ? 15.561  -34.762 -60.276  1.00 32.00  ? 332  THR   C CA  1 
ATOM   7037  C  C   . THR   C  1 31  ? 16.481  -35.099 -59.111  1.00 32.03  ? 332  THR   C C   1 
ATOM   7038  O  O   . THR   C  1 31  ? 16.645  -36.266 -58.740  1.00 35.97  ? 332  THR   C O   1 
ATOM   7039  C  CB  . THR   C  1 31  ? 14.477  -33.759 -59.857  1.00 41.33  ? 332  THR   C CB  1 
ATOM   7040  O  OG1 . THR   C  1 31  ? 13.852  -34.194 -58.641  1.00 45.88  ? 332  THR   C OG1 1 
ATOM   7041  C  CG2 . THR   C  1 31  ? 13.414  -33.601 -60.940  1.00 39.16  ? 332  THR   C CG2 1 
ATOM   7042  N  N   . GLU   C  1 32  ? 17.089  -34.063 -58.535  1.00 33.57  ? 333  GLU   C N   1 
ATOM   7043  C  CA  . GLU   C  1 32  ? 17.977  -34.286 -57.403  1.00 40.69  ? 333  GLU   C CA  1 
ATOM   7044  C  C   . GLU   C  1 32  ? 17.222  -34.852 -56.211  1.00 38.89  ? 333  GLU   C C   1 
ATOM   7045  O  O   . GLU   C  1 32  ? 17.814  -35.544 -55.376  1.00 40.49  ? 333  GLU   C O   1 
ATOM   7046  C  CB  . GLU   C  1 32  ? 18.688  -32.989 -57.019  1.00 50.40  ? 333  GLU   C CB  1 
ATOM   7047  C  CG  . GLU   C  1 32  ? 20.055  -32.819 -57.663  1.00 69.56  ? 333  GLU   C CG  1 
ATOM   7048  C  CD  . GLU   C  1 32  ? 20.121  -31.632 -58.609  1.00 85.51  ? 333  GLU   C CD  1 
ATOM   7049  O  OE1 . GLU   C  1 32  ? 19.174  -30.815 -58.610  1.00 87.50  ? 333  GLU   C OE1 1 
ATOM   7050  O  OE2 . GLU   C  1 32  ? 21.122  -31.519 -59.353  1.00 93.03  ? 333  GLU   C OE2 1 
ATOM   7051  N  N   . TYR   C  1 33  ? 15.920  -34.586 -56.120  1.00 28.57  ? 334  TYR   C N   1 
ATOM   7052  C  CA  . TYR   C  1 33  ? 15.145  -34.984 -54.960  1.00 29.18  ? 334  TYR   C CA  1 
ATOM   7053  C  C   . TYR   C  1 33  ? 14.073  -36.013 -55.275  1.00 28.17  ? 334  TYR   C C   1 
ATOM   7054  O  O   . TYR   C  1 33  ? 13.399  -36.476 -54.357  1.00 35.16  ? 334  TYR   C O   1 
ATOM   7055  C  CB  . TYR   C  1 33  ? 14.526  -33.747 -54.302  1.00 37.89  ? 334  TYR   C CB  1 
ATOM   7056  C  CG  . TYR   C  1 33  ? 15.587  -32.860 -53.680  1.00 46.20  ? 334  TYR   C CG  1 
ATOM   7057  C  CD1 . TYR   C  1 33  ? 16.104  -33.143 -52.422  1.00 45.13  ? 334  TYR   C CD1 1 
ATOM   7058  C  CD2 . TYR   C  1 33  ? 16.099  -31.767 -54.366  1.00 48.05  ? 334  TYR   C CD2 1 
ATOM   7059  C  CE1 . TYR   C  1 33  ? 17.091  -32.352 -51.857  1.00 57.45  ? 334  TYR   C CE1 1 
ATOM   7060  C  CE2 . TYR   C  1 33  ? 17.084  -30.969 -53.807  1.00 51.14  ? 334  TYR   C CE2 1 
ATOM   7061  C  CZ  . TYR   C  1 33  ? 17.577  -31.265 -52.551  1.00 61.24  ? 334  TYR   C CZ  1 
ATOM   7062  O  OH  . TYR   C  1 33  ? 18.558  -30.479 -51.976  1.00 70.04  ? 334  TYR   C OH  1 
ATOM   7063  N  N   . ILE   C  1 34  ? 13.895  -36.403 -56.532  1.00 26.62  ? 335  ILE   C N   1 
ATOM   7064  C  CA  . ILE   C  1 34  ? 12.899  -37.416 -56.869  1.00 26.72  ? 335  ILE   C CA  1 
ATOM   7065  C  C   . ILE   C  1 34  ? 13.515  -38.392 -57.857  1.00 35.22  ? 335  ILE   C C   1 
ATOM   7066  O  O   . ILE   C  1 34  ? 14.101  -37.976 -58.860  1.00 35.34  ? 335  ILE   C O   1 
ATOM   7067  C  CB  . ILE   C  1 34  ? 11.615  -36.796 -57.449  1.00 38.32  ? 335  ILE   C CB  1 
ATOM   7068  C  CG1 . ILE   C  1 34  ? 11.100  -35.690 -56.535  1.00 39.92  ? 335  ILE   C CG1 1 
ATOM   7069  C  CG2 . ILE   C  1 34  ? 10.527  -37.842 -57.557  1.00 38.62  ? 335  ILE   C CG2 1 
ATOM   7070  C  CD1 . ILE   C  1 34  ? 10.341  -34.619 -57.254  1.00 50.59  ? 335  ILE   C CD1 1 
ATOM   7071  N  N   . CYS   C  1 35  ? 13.398  -39.686 -57.574  1.00 26.78  ? 336  CYS   C N   1 
ATOM   7072  C  CA  . CYS   C  1 35  ? 13.781  -40.705 -58.532  1.00 28.03  ? 336  CYS   C CA  1 
ATOM   7073  C  C   . CYS   C  1 35  ? 12.535  -41.206 -59.235  1.00 29.28  ? 336  CYS   C C   1 
ATOM   7074  O  O   . CYS   C  1 35  ? 11.553  -41.574 -58.584  1.00 30.60  ? 336  CYS   C O   1 
ATOM   7075  C  CB  . CYS   C  1 35  ? 14.509  -41.876 -57.882  1.00 29.04  ? 336  CYS   C CB  1 
ATOM   7076  S  SG  . CYS   C  1 35  ? 14.986  -43.115 -59.092  1.00 28.13  ? 336  CYS   C SG  1 
ATOM   7077  N  N   . MET   C  1 36  ? 12.584  -41.217 -60.562  1.00 27.72  ? 337  MET   C N   1 
ATOM   7078  C  CA  . MET   C  1 36  ? 11.495  -41.714 -61.388  1.00 28.24  ? 337  MET   C CA  1 
ATOM   7079  C  C   . MET   C  1 36  ? 11.948  -42.929 -62.181  1.00 28.67  ? 337  MET   C C   1 
ATOM   7080  O  O   . MET   C  1 36  ? 11.439  -43.200 -63.272  1.00 27.28  ? 337  MET   C O   1 
ATOM   7081  C  CB  . MET   C  1 36  ? 10.981  -40.608 -62.306  1.00 32.14  ? 337  MET   C CB  1 
ATOM   7082  C  CG  . MET   C  1 36  ? 10.677  -39.331 -61.554  1.00 39.99  ? 337  MET   C CG  1 
ATOM   7083  S  SD  . MET   C  1 36  ? 9.434   -38.314 -62.351  1.00 51.05  ? 337  MET   C SD  1 
ATOM   7084  C  CE  . MET   C  1 36  ? 9.861   -38.594 -64.063  1.00 49.94  ? 337  MET   C CE  1 
ATOM   7085  N  N   . GLY   C  1 37  ? 12.905  -43.672 -61.623  1.00 23.75  ? 338  GLY   C N   1 
ATOM   7086  C  CA  . GLY   C  1 37  ? 13.472  -44.829 -62.291  1.00 26.94  ? 338  GLY   C CA  1 
ATOM   7087  C  C   . GLY   C  1 37  ? 12.470  -45.893 -62.689  1.00 28.56  ? 338  GLY   C C   1 
ATOM   7088  O  O   . GLY   C  1 37  ? 12.755  -46.683 -63.596  1.00 33.85  ? 338  GLY   C O   1 
ATOM   7089  N  N   . SER   C  1 38  ? 11.298  -45.941 -62.050  1.00 20.21  ? 339  SER   C N   1 
ATOM   7090  C  CA  . SER   C  1 38  ? 10.312  -46.948 -62.430  1.00 28.50  ? 339  SER   C CA  1 
ATOM   7091  C  C   . SER   C  1 38  ? 9.179   -46.382 -63.278  1.00 31.38  ? 339  SER   C C   1 
ATOM   7092  O  O   . SER   C  1 38  ? 8.204   -47.093 -63.539  1.00 27.56  ? 339  SER   C O   1 
ATOM   7093  C  CB  . SER   C  1 38  ? 9.743   -47.651 -61.194  1.00 22.86  ? 339  SER   C CB  1 
ATOM   7094  O  OG  . SER   C  1 38  ? 8.933   -46.798 -60.404  1.00 25.14  ? 339  SER   C OG  1 
ATOM   7095  N  N   . ILE   C  1 39  ? 9.271   -45.123 -63.701  1.00 28.56  ? 340  ILE   C N   1 
ATOM   7096  C  CA  . ILE   C  1 39  ? 8.286   -44.558 -64.619  1.00 25.99  ? 340  ILE   C CA  1 
ATOM   7097  C  C   . ILE   C  1 39  ? 8.592   -45.054 -66.027  1.00 24.09  ? 340  ILE   C C   1 
ATOM   7098  O  O   . ILE   C  1 39  ? 9.738   -44.971 -66.487  1.00 26.43  ? 340  ILE   C O   1 
ATOM   7099  C  CB  . ILE   C  1 39  ? 8.304   -43.024 -64.566  1.00 34.51  ? 340  ILE   C CB  1 
ATOM   7100  C  CG1 . ILE   C  1 39  ? 8.193   -42.537 -63.119  1.00 36.00  ? 340  ILE   C CG1 1 
ATOM   7101  C  CG2 . ILE   C  1 39  ? 7.193   -42.459 -65.449  1.00 35.90  ? 340  ILE   C CG2 1 
ATOM   7102  C  CD1 . ILE   C  1 39  ? 6.906   -42.868 -62.472  1.00 32.32  ? 340  ILE   C CD1 1 
ATOM   7103  N  N   . MET   C  1 40  ? 7.575   -45.575 -66.713  1.00 23.53  ? 341  MET   C N   1 
ATOM   7104  C  CA  . MET   C  1 40  ? 7.801   -46.162 -68.034  1.00 32.32  ? 341  MET   C CA  1 
ATOM   7105  C  C   . MET   C  1 40  ? 8.220   -45.101 -69.053  1.00 28.23  ? 341  MET   C C   1 
ATOM   7106  O  O   . MET   C  1 40  ? 9.233   -45.259 -69.744  1.00 29.51  ? 341  MET   C O   1 
ATOM   7107  C  CB  . MET   C  1 40  ? 6.549   -46.904 -68.505  1.00 35.56  ? 341  MET   C CB  1 
ATOM   7108  C  CG  . MET   C  1 40  ? 6.769   -47.755 -69.769  1.00 53.27  ? 341  MET   C CG  1 
ATOM   7109  S  SD  . MET   C  1 40  ? 6.708   -49.529 -69.420  1.00 61.14  ? 341  MET   C SD  1 
ATOM   7110  C  CE  . MET   C  1 40  ? 5.383   -49.592 -68.226  1.00 36.76  ? 341  MET   C CE  1 
ATOM   7111  N  N   . HIS   C  1 41  ? 7.454   -44.016 -69.164  1.00 36.08  ? 342  HIS   C N   1 
ATOM   7112  C  CA  A HIS   C  1 41  ? 7.760   -42.896 -70.055  0.52 40.53  ? 342  HIS   C CA  1 
ATOM   7113  C  CA  B HIS   C  1 41  ? 7.789   -42.902 -70.050  0.48 40.46  ? 342  HIS   C CA  1 
ATOM   7114  C  C   . HIS   C  1 41  ? 7.875   -41.627 -69.221  1.00 41.60  ? 342  HIS   C C   1 
ATOM   7115  O  O   . HIS   C  1 41  ? 6.862   -40.951 -68.986  1.00 38.89  ? 342  HIS   C O   1 
ATOM   7116  C  CB  A HIS   C  1 41  ? 6.676   -42.691 -71.118  0.52 41.30  ? 342  HIS   C CB  1 
ATOM   7117  C  CB  B HIS   C  1 41  ? 6.774   -42.751 -71.180  0.48 41.68  ? 342  HIS   C CB  1 
ATOM   7118  C  CG  A HIS   C  1 41  ? 6.099   -43.951 -71.685  0.52 41.79  ? 342  HIS   C CG  1 
ATOM   7119  C  CG  B HIS   C  1 41  ? 7.125   -41.672 -72.158  0.48 48.63  ? 342  HIS   C CG  1 
ATOM   7120  N  ND1 A HIS   C  1 41  ? 6.616   -44.568 -72.803  0.52 42.57  ? 342  HIS   C ND1 1 
ATOM   7121  N  ND1 B HIS   C  1 41  ? 8.396   -41.146 -72.260  0.48 48.76  ? 342  HIS   C ND1 1 
ATOM   7122  C  CD2 A HIS   C  1 41  ? 5.009   -44.672 -71.329  0.52 42.08  ? 342  HIS   C CD2 1 
ATOM   7123  C  CD2 B HIS   C  1 41  ? 6.371   -41.012 -73.070  0.48 51.22  ? 342  HIS   C CD2 1 
ATOM   7124  C  CE1 A HIS   C  1 41  ? 5.892   -45.634 -73.091  0.52 40.74  ? 342  HIS   C CE1 1 
ATOM   7125  C  CE1 B HIS   C  1 41  ? 8.410   -40.213 -73.194  0.48 50.89  ? 342  HIS   C CE1 1 
ATOM   7126  N  NE2 A HIS   C  1 41  ? 4.909   -45.719 -72.213  0.52 37.22  ? 342  HIS   C NE2 1 
ATOM   7127  N  NE2 B HIS   C  1 41  ? 7.195   -40.112 -73.701  0.48 51.70  ? 342  HIS   C NE2 1 
ATOM   7128  N  N   . PRO   C  1 42  ? 9.076   -41.253 -68.756  1.00 42.77  ? 343  PRO   C N   1 
ATOM   7129  C  CA  . PRO   C  1 42  ? 9.225   -39.963 -68.070  1.00 48.03  ? 343  PRO   C CA  1 
ATOM   7130  C  C   . PRO   C  1 42  ? 9.591   -38.828 -69.033  1.00 57.48  ? 343  PRO   C C   1 
ATOM   7131  O  O   . PRO   C  1 42  ? 9.317   -37.660 -68.741  1.00 64.72  ? 343  PRO   C O   1 
ATOM   7132  C  CB  . PRO   C  1 42  ? 10.360  -40.221 -67.076  1.00 43.37  ? 343  PRO   C CB  1 
ATOM   7133  C  CG  . PRO   C  1 42  ? 11.077  -41.455 -67.574  1.00 42.42  ? 343  PRO   C CG  1 
ATOM   7134  C  CD  . PRO   C  1 42  ? 10.318  -42.038 -68.741  1.00 44.96  ? 343  PRO   C CD  1 
ATOM   7135  N  N   . ASP   C  1 51  ? 6.094   -31.778 -85.046  1.00 98.71  ? 352  ASP   C N   1 
ATOM   7136  C  CA  . ASP   C  1 51  ? 7.080   -30.708 -84.906  1.00 102.61 ? 352  ASP   C CA  1 
ATOM   7137  C  C   . ASP   C  1 51  ? 8.506   -31.256 -85.026  1.00 99.93  ? 352  ASP   C C   1 
ATOM   7138  O  O   . ASP   C  1 51  ? 8.733   -32.453 -84.833  1.00 102.17 ? 352  ASP   C O   1 
ATOM   7139  C  CB  . ASP   C  1 51  ? 6.898   -29.984 -83.573  1.00 105.53 ? 352  ASP   C CB  1 
ATOM   7140  C  CG  . ASP   C  1 51  ? 7.434   -28.568 -83.605  1.00 107.91 ? 352  ASP   C CG  1 
ATOM   7141  O  OD1 . ASP   C  1 51  ? 7.710   -28.066 -84.717  1.00 111.99 ? 352  ASP   C OD1 1 
ATOM   7142  O  OD2 . ASP   C  1 51  ? 7.581   -27.959 -82.523  1.00 104.73 ? 352  ASP   C OD2 1 
ATOM   7143  N  N   . VAL   C  1 52  ? 9.466   -30.379 -85.340  1.00 90.22  ? 353  VAL   C N   1 
ATOM   7144  C  CA  . VAL   C  1 52  ? 10.806  -30.783 -85.758  1.00 75.42  ? 353  VAL   C CA  1 
ATOM   7145  C  C   . VAL   C  1 52  ? 11.837  -29.791 -85.234  1.00 63.40  ? 353  VAL   C C   1 
ATOM   7146  O  O   . VAL   C  1 52  ? 11.502  -28.710 -84.744  1.00 67.87  ? 353  VAL   C O   1 
ATOM   7147  C  CB  . VAL   C  1 52  ? 10.921  -30.888 -87.294  1.00 74.34  ? 353  VAL   C CB  1 
ATOM   7148  C  CG1 . VAL   C  1 52  ? 10.147  -32.088 -87.799  1.00 75.46  ? 353  VAL   C CG1 1 
ATOM   7149  C  CG2 . VAL   C  1 52  ? 10.428  -29.597 -87.958  1.00 66.30  ? 353  VAL   C CG2 1 
ATOM   7150  N  N   . ALA   C  1 53  ? 13.112  -30.157 -85.379  1.00 51.81  ? 354  ALA   C N   1 
ATOM   7151  C  CA  . ALA   C  1 53  ? 14.215  -29.358 -84.861  1.00 50.48  ? 354  ALA   C CA  1 
ATOM   7152  C  C   . ALA   C  1 53  ? 14.494  -28.147 -85.745  1.00 59.09  ? 354  ALA   C C   1 
ATOM   7153  O  O   . ALA   C  1 53  ? 14.386  -28.213 -86.973  1.00 54.76  ? 354  ALA   C O   1 
ATOM   7154  C  CB  . ALA   C  1 53  ? 15.481  -30.209 -84.749  1.00 49.05  ? 354  ALA   C CB  1 
ATOM   7155  N  N   . THR   C  1 54  ? 14.868  -27.038 -85.110  1.00 67.38  ? 355  THR   C N   1 
ATOM   7156  C  CA  . THR   C  1 54  ? 15.228  -25.841 -85.853  1.00 71.43  ? 355  THR   C CA  1 
ATOM   7157  C  C   . THR   C  1 54  ? 16.635  -25.978 -86.431  1.00 72.33  ? 355  THR   C C   1 
ATOM   7158  O  O   . THR   C  1 54  ? 17.400  -26.880 -86.078  1.00 72.36  ? 355  THR   C O   1 
ATOM   7159  C  CB  . THR   C  1 54  ? 15.147  -24.600 -84.965  1.00 65.58  ? 355  THR   C CB  1 
ATOM   7160  O  OG1 . THR   C  1 54  ? 16.228  -24.616 -84.024  1.00 68.36  ? 355  THR   C OG1 1 
ATOM   7161  C  CG2 . THR   C  1 54  ? 13.827  -24.571 -84.214  1.00 65.87  ? 355  THR   C CG2 1 
ATOM   7162  N  N   . LYS   C  1 55  ? 16.973  -25.057 -87.336  1.00 66.48  ? 356  LYS   C N   1 
ATOM   7163  C  CA  . LYS   C  1 55  ? 18.308  -25.048 -87.923  1.00 61.71  ? 356  LYS   C CA  1 
ATOM   7164  C  C   . LYS   C  1 55  ? 19.382  -24.998 -86.845  1.00 61.93  ? 356  LYS   C C   1 
ATOM   7165  O  O   . LYS   C  1 55  ? 20.340  -25.781 -86.865  1.00 55.50  ? 356  LYS   C O   1 
ATOM   7166  C  CB  . LYS   C  1 55  ? 18.452  -23.853 -88.861  1.00 59.47  ? 356  LYS   C CB  1 
ATOM   7167  C  CG  . LYS   C  1 55  ? 18.754  -24.212 -90.293  1.00 56.56  ? 356  LYS   C CG  1 
ATOM   7168  C  CD  . LYS   C  1 55  ? 18.866  -22.951 -91.132  1.00 54.35  ? 356  LYS   C CD  1 
ATOM   7169  C  CE  . LYS   C  1 55  ? 18.297  -23.182 -92.516  1.00 60.35  ? 356  LYS   C CE  1 
ATOM   7170  N  NZ  . LYS   C  1 55  ? 18.488  -22.006 -93.403  1.00 68.21  ? 356  LYS   C NZ  1 
ATOM   7171  N  N   . ASP   C  1 56  ? 19.226  -24.084 -85.885  1.00 58.96  ? 357  ASP   C N   1 
ATOM   7172  C  CA  . ASP   C  1 56  ? 20.251  -23.844 -84.879  1.00 61.33  ? 357  ASP   C CA  1 
ATOM   7173  C  C   . ASP   C  1 56  ? 20.273  -24.905 -83.789  1.00 54.18  ? 357  ASP   C C   1 
ATOM   7174  O  O   . ASP   C  1 56  ? 21.308  -25.083 -83.144  1.00 54.02  ? 357  ASP   C O   1 
ATOM   7175  C  CB  . ASP   C  1 56  ? 20.056  -22.457 -84.263  1.00 70.35  ? 357  ASP   C CB  1 
ATOM   7176  C  CG  . ASP   C  1 56  ? 20.181  -21.346 -85.292  1.00 78.57  ? 357  ASP   C CG  1 
ATOM   7177  O  OD1 . ASP   C  1 56  ? 21.161  -21.357 -86.070  1.00 80.61  ? 357  ASP   C OD1 1 
ATOM   7178  O  OD2 . ASP   C  1 56  ? 19.291  -20.472 -85.337  1.00 82.79  ? 357  ASP   C OD2 1 
ATOM   7179  N  N   . GLN   C  1 57  ? 19.160  -25.604 -83.563  1.00 46.92  ? 358  GLN   C N   1 
ATOM   7180  C  CA  . GLN   C  1 57  ? 19.202  -26.791 -82.717  1.00 43.69  ? 358  GLN   C CA  1 
ATOM   7181  C  C   . GLN   C  1 57  ? 19.971  -27.925 -83.379  1.00 41.99  ? 358  GLN   C C   1 
ATOM   7182  O  O   . GLN   C  1 57  ? 20.629  -28.714 -82.690  1.00 43.21  ? 358  GLN   C O   1 
ATOM   7183  C  CB  . GLN   C  1 57  ? 17.789  -27.265 -82.397  1.00 50.04  ? 358  GLN   C CB  1 
ATOM   7184  C  CG  . GLN   C  1 57  ? 17.025  -26.421 -81.398  1.00 59.28  ? 358  GLN   C CG  1 
ATOM   7185  C  CD  . GLN   C  1 57  ? 15.673  -27.030 -81.084  1.00 63.89  ? 358  GLN   C CD  1 
ATOM   7186  O  OE1 . GLN   C  1 57  ? 14.809  -27.133 -81.957  1.00 59.69  ? 358  GLN   C OE1 1 
ATOM   7187  N  NE2 . GLN   C  1 57  ? 15.491  -27.466 -79.841  1.00 69.80  ? 358  GLN   C NE2 1 
ATOM   7188  N  N   . LEU   C  1 58  ? 19.892  -28.030 -84.710  1.00 32.51  ? 359  LEU   C N   1 
ATOM   7189  C  CA  . LEU   C  1 58  ? 20.434  -29.199 -85.390  1.00 34.68  ? 359  LEU   C CA  1 
ATOM   7190  C  C   . LEU   C  1 58  ? 21.958  -29.160 -85.445  1.00 34.09  ? 359  LEU   C C   1 
ATOM   7191  O  O   . LEU   C  1 58  ? 22.610  -30.202 -85.306  1.00 39.26  ? 359  LEU   C O   1 
ATOM   7192  C  CB  . LEU   C  1 58  ? 19.839  -29.309 -86.798  1.00 36.23  ? 359  LEU   C CB  1 
ATOM   7193  C  CG  . LEU   C  1 58  ? 19.969  -30.654 -87.511  1.00 35.73  ? 359  LEU   C CG  1 
ATOM   7194  C  CD1 . LEU   C  1 58  ? 19.433  -31.783 -86.624  1.00 41.86  ? 359  LEU   C CD1 1 
ATOM   7195  C  CD2 . LEU   C  1 58  ? 19.244  -30.630 -88.858  1.00 35.12  ? 359  LEU   C CD2 1 
ATOM   7196  N  N   . PHE   C  1 59  ? 22.543  -27.970 -85.634  1.00 36.85  ? 360  PHE   C N   1 
ATOM   7197  C  CA  . PHE   C  1 59  ? 23.990  -27.819 -85.779  1.00 45.91  ? 360  PHE   C CA  1 
ATOM   7198  C  C   . PHE   C  1 59  ? 24.747  -28.547 -84.667  1.00 45.24  ? 360  PHE   C C   1 
ATOM   7199  O  O   . PHE   C  1 59  ? 25.500  -29.486 -84.964  1.00 42.13  ? 360  PHE   C O   1 
ATOM   7200  C  CB  . PHE   C  1 59  ? 24.407  -26.343 -85.797  1.00 57.40  ? 360  PHE   C CB  1 
ATOM   7201  C  CG  . PHE   C  1 59  ? 24.100  -25.618 -87.083  1.00 65.55  ? 360  PHE   C CG  1 
ATOM   7202  C  CD1 . PHE   C  1 59  ? 24.621  -26.055 -88.290  1.00 66.15  ? 360  PHE   C CD1 1 
ATOM   7203  C  CD2 . PHE   C  1 59  ? 23.332  -24.460 -87.072  1.00 65.42  ? 360  PHE   C CD2 1 
ATOM   7204  C  CE1 . PHE   C  1 59  ? 24.353  -25.368 -89.470  1.00 62.21  ? 360  PHE   C CE1 1 
ATOM   7205  C  CE2 . PHE   C  1 59  ? 23.062  -23.774 -88.241  1.00 65.14  ? 360  PHE   C CE2 1 
ATOM   7206  C  CZ  . PHE   C  1 59  ? 23.570  -24.231 -89.444  1.00 61.73  ? 360  PHE   C CZ  1 
ATOM   7207  N  N   . PRO   C  1 60  ? 24.574  -28.185 -83.387  1.00 42.26  ? 361  PRO   C N   1 
ATOM   7208  C  CA  . PRO   C  1 60  ? 25.402  -28.833 -82.361  1.00 38.84  ? 361  PRO   C CA  1 
ATOM   7209  C  C   . PRO   C  1 60  ? 25.109  -30.305 -82.207  1.00 34.70  ? 361  PRO   C C   1 
ATOM   7210  O  O   . PRO   C  1 60  ? 26.012  -31.061 -81.833  1.00 40.59  ? 361  PRO   C O   1 
ATOM   7211  C  CB  . PRO   C  1 60  ? 25.064  -28.054 -81.084  1.00 41.44  ? 361  PRO   C CB  1 
ATOM   7212  C  CG  . PRO   C  1 60  ? 23.698  -27.594 -81.296  1.00 43.96  ? 361  PRO   C CG  1 
ATOM   7213  C  CD  . PRO   C  1 60  ? 23.571  -27.296 -82.768  1.00 42.92  ? 361  PRO   C CD  1 
ATOM   7214  N  N   . LEU   C  1 61  ? 23.875  -30.741 -82.465  1.00 28.33  ? 362  LEU   C N   1 
ATOM   7215  C  CA  . LEU   C  1 61  ? 23.587  -32.168 -82.397  1.00 28.30  ? 362  LEU   C CA  1 
ATOM   7216  C  C   . LEU   C  1 61  ? 24.337  -32.908 -83.490  1.00 33.24  ? 362  LEU   C C   1 
ATOM   7217  O  O   . LEU   C  1 61  ? 24.975  -33.937 -83.240  1.00 34.81  ? 362  LEU   C O   1 
ATOM   7218  C  CB  . LEU   C  1 61  ? 22.083  -32.407 -82.521  1.00 29.78  ? 362  LEU   C CB  1 
ATOM   7219  C  CG  . LEU   C  1 61  ? 21.209  -31.858 -81.394  1.00 40.35  ? 362  LEU   C CG  1 
ATOM   7220  C  CD1 . LEU   C  1 61  ? 19.741  -32.153 -81.679  1.00 37.83  ? 362  LEU   C CD1 1 
ATOM   7221  C  CD2 . LEU   C  1 61  ? 21.636  -32.446 -80.054  1.00 34.89  ? 362  LEU   C CD2 1 
ATOM   7222  N  N   . ALA   C  1 62  ? 24.274  -32.382 -84.712  1.00 31.85  ? 363  ALA   C N   1 
ATOM   7223  C  CA  . ALA   C  1 62  ? 25.005  -32.981 -85.819  1.00 29.82  ? 363  ALA   C CA  1 
ATOM   7224  C  C   . ALA   C  1 62  ? 26.493  -33.014 -85.521  1.00 30.73  ? 363  ALA   C C   1 
ATOM   7225  O  O   . ALA   C  1 62  ? 27.153  -34.044 -85.700  1.00 27.23  ? 363  ALA   C O   1 
ATOM   7226  C  CB  . ALA   C  1 62  ? 24.723  -32.202 -87.104  1.00 33.92  ? 363  ALA   C CB  1 
ATOM   7227  N  N   . LYS   C  1 63  ? 27.032  -31.897 -85.030  1.00 36.64  ? 364  LYS   C N   1 
ATOM   7228  C  CA  . LYS   C  1 63  ? 28.457  -31.832 -84.743  1.00 39.70  ? 364  LYS   C CA  1 
ATOM   7229  C  C   . LYS   C  1 63  ? 28.866  -32.907 -83.751  1.00 37.91  ? 364  LYS   C C   1 
ATOM   7230  O  O   . LYS   C  1 63  ? 29.834  -33.640 -83.981  1.00 36.00  ? 364  LYS   C O   1 
ATOM   7231  C  CB  . LYS   C  1 63  ? 28.828  -30.453 -84.205  1.00 35.11  ? 364  LYS   C CB  1 
ATOM   7232  C  CG  . LYS   C  1 63  ? 30.309  -30.334 -83.909  1.00 37.54  ? 364  LYS   C CG  1 
ATOM   7233  C  CD  . LYS   C  1 63  ? 30.677  -28.956 -83.417  1.00 50.62  ? 364  LYS   C CD  1 
ATOM   7234  C  CE  . LYS   C  1 63  ? 32.191  -28.800 -83.333  1.00 56.54  ? 364  LYS   C CE  1 
ATOM   7235  N  NZ  . LYS   C  1 63  ? 32.789  -29.681 -82.290  1.00 53.41  ? 364  LYS   C NZ  1 
ATOM   7236  N  N   . GLU   C  1 64  ? 28.141  -33.012 -82.634  1.00 31.59  ? 365  GLU   C N   1 
ATOM   7237  C  CA  . GLU   C  1 64  ? 28.523  -33.969 -81.600  1.00 34.66  ? 365  GLU   C CA  1 
ATOM   7238  C  C   . GLU   C  1 64  ? 28.500  -35.387 -82.147  1.00 31.26  ? 365  GLU   C C   1 
ATOM   7239  O  O   . GLU   C  1 64  ? 29.404  -36.184 -81.865  1.00 25.77  ? 365  GLU   C O   1 
ATOM   7240  C  CB  . GLU   C  1 64  ? 27.606  -33.841 -80.378  1.00 40.13  ? 365  GLU   C CB  1 
ATOM   7241  C  CG  . GLU   C  1 64  ? 27.960  -34.784 -79.221  1.00 56.40  ? 365  GLU   C CG  1 
ATOM   7242  C  CD  . GLU   C  1 64  ? 29.349  -34.527 -78.637  1.00 76.04  ? 365  GLU   C CD  1 
ATOM   7243  O  OE1 . GLU   C  1 64  ? 29.662  -33.357 -78.311  1.00 79.79  ? 365  GLU   C OE1 1 
ATOM   7244  O  OE2 . GLU   C  1 64  ? 30.130  -35.500 -78.511  1.00 79.44  ? 365  GLU   C OE2 1 
ATOM   7245  N  N   . PHE   C  1 65  ? 27.499  -35.714 -82.966  1.00 28.97  ? 366  PHE   C N   1 
ATOM   7246  C  CA  . PHE   C  1 65  ? 27.481  -37.039 -83.569  1.00 29.11  ? 366  PHE   C CA  1 
ATOM   7247  C  C   . PHE   C  1 65  ? 28.667  -37.245 -84.505  1.00 24.64  ? 366  PHE   C C   1 
ATOM   7248  O  O   . PHE   C  1 65  ? 29.359  -38.266 -84.430  1.00 28.88  ? 366  PHE   C O   1 
ATOM   7249  C  CB  . PHE   C  1 65  ? 26.181  -37.281 -84.320  1.00 26.94  ? 366  PHE   C CB  1 
ATOM   7250  C  CG  . PHE   C  1 65  ? 26.213  -38.535 -85.126  1.00 28.26  ? 366  PHE   C CG  1 
ATOM   7251  C  CD1 . PHE   C  1 65  ? 26.138  -39.773 -84.497  1.00 26.67  ? 366  PHE   C CD1 1 
ATOM   7252  C  CD2 . PHE   C  1 65  ? 26.367  -38.486 -86.500  1.00 27.47  ? 366  PHE   C CD2 1 
ATOM   7253  C  CE1 . PHE   C  1 65  ? 26.193  -40.931 -85.226  1.00 31.09  ? 366  PHE   C CE1 1 
ATOM   7254  C  CE2 . PHE   C  1 65  ? 26.415  -39.653 -87.244  1.00 31.56  ? 366  PHE   C CE2 1 
ATOM   7255  C  CZ  . PHE   C  1 65  ? 26.329  -40.872 -86.611  1.00 33.53  ? 366  PHE   C CZ  1 
ATOM   7256  N  N   . ILE   C  1 66  ? 28.916  -36.290 -85.401  1.00 27.60  ? 367  ILE   C N   1 
ATOM   7257  C  CA  . ILE   C  1 66  ? 30.011  -36.469 -86.351  1.00 31.77  ? 367  ILE   C CA  1 
ATOM   7258  C  C   . ILE   C  1 66  ? 31.340  -36.536 -85.610  1.00 33.51  ? 367  ILE   C C   1 
ATOM   7259  O  O   . ILE   C  1 66  ? 32.212  -37.351 -85.942  1.00 34.40  ? 367  ILE   C O   1 
ATOM   7260  C  CB  . ILE   C  1 66  ? 29.987  -35.357 -87.415  1.00 33.43  ? 367  ILE   C CB  1 
ATOM   7261  C  CG1 . ILE   C  1 66  ? 28.698  -35.456 -88.220  1.00 35.56  ? 367  ILE   C CG1 1 
ATOM   7262  C  CG2 . ILE   C  1 66  ? 31.206  -35.448 -88.350  1.00 33.33  ? 367  ILE   C CG2 1 
ATOM   7263  C  CD1 . ILE   C  1 66  ? 28.577  -36.759 -89.017  1.00 33.29  ? 367  ILE   C CD1 1 
ATOM   7264  N  N   . ASP   C  1 67  ? 31.507  -35.702 -84.579  1.00 31.45  ? 368  ASP   C N   1 
ATOM   7265  C  CA  . ASP   C  1 67  ? 32.699  -35.796 -83.738  1.00 35.58  ? 368  ASP   C CA  1 
ATOM   7266  C  C   . ASP   C  1 67  ? 32.822  -37.192 -83.150  1.00 31.83  ? 368  ASP   C C   1 
ATOM   7267  O  O   . ASP   C  1 67  ? 33.895  -37.803 -83.162  1.00 28.55  ? 368  ASP   C O   1 
ATOM   7268  C  CB  . ASP   C  1 67  ? 32.641  -34.766 -82.602  1.00 35.29  ? 368  ASP   C CB  1 
ATOM   7269  C  CG  . ASP   C  1 67  ? 32.858  -33.351 -83.078  1.00 36.62  ? 368  ASP   C CG  1 
ATOM   7270  O  OD1 . ASP   C  1 67  ? 33.219  -33.145 -84.257  1.00 39.75  ? 368  ASP   C OD1 1 
ATOM   7271  O  OD2 . ASP   C  1 67  ? 32.665  -32.437 -82.253  1.00 38.13  ? 368  ASP   C OD2 1 
ATOM   7272  N  N   . GLN   C  1 68  ? 31.713  -37.710 -82.637  1.00 25.07  ? 369  GLN   C N   1 
ATOM   7273  C  CA  . GLN   C  1 68  ? 31.717  -39.021 -82.015  1.00 32.04  ? 369  GLN   C CA  1 
ATOM   7274  C  C   . GLN   C  1 68  ? 32.013  -40.112 -83.036  1.00 33.66  ? 369  GLN   C C   1 
ATOM   7275  O  O   . GLN   C  1 68  ? 32.791  -41.035 -82.766  1.00 36.12  ? 369  GLN   C O   1 
ATOM   7276  C  CB  . GLN   C  1 68  ? 30.367  -39.230 -81.338  1.00 36.20  ? 369  GLN   C CB  1 
ATOM   7277  C  CG  . GLN   C  1 68  ? 30.192  -40.503 -80.602  1.00 46.74  ? 369  GLN   C CG  1 
ATOM   7278  C  CD  . GLN   C  1 68  ? 28.723  -40.799 -80.393  1.00 48.27  ? 369  GLN   C CD  1 
ATOM   7279  O  OE1 . GLN   C  1 68  ? 28.276  -41.941 -80.549  1.00 42.16  ? 369  GLN   C OE1 1 
ATOM   7280  N  NE2 . GLN   C  1 68  ? 27.955  -39.760 -80.056  1.00 44.11  ? 369  GLN   C NE2 1 
ATOM   7281  N  N   . TYR   C  1 69  ? 31.423  -40.010 -84.227  1.00 28.56  ? 370  TYR   C N   1 
ATOM   7282  C  CA  . TYR   C  1 69  ? 31.730  -40.978 -85.275  1.00 30.78  ? 370  TYR   C CA  1 
ATOM   7283  C  C   . TYR   C  1 69  ? 33.207  -40.939 -85.647  1.00 34.36  ? 370  TYR   C C   1 
ATOM   7284  O  O   . TYR   C  1 69  ? 33.845  -41.985 -85.822  1.00 33.79  ? 370  TYR   C O   1 
ATOM   7285  C  CB  . TYR   C  1 69  ? 30.881  -40.719 -86.514  1.00 29.02  ? 370  TYR   C CB  1 
ATOM   7286  C  CG  . TYR   C  1 69  ? 31.353  -41.542 -87.681  1.00 37.44  ? 370  TYR   C CG  1 
ATOM   7287  C  CD1 . TYR   C  1 69  ? 31.055  -42.896 -87.748  1.00 43.55  ? 370  TYR   C CD1 1 
ATOM   7288  C  CD2 . TYR   C  1 69  ? 32.121  -40.983 -88.703  1.00 29.48  ? 370  TYR   C CD2 1 
ATOM   7289  C  CE1 . TYR   C  1 69  ? 31.485  -43.669 -88.797  1.00 38.45  ? 370  TYR   C CE1 1 
ATOM   7290  C  CE2 . TYR   C  1 69  ? 32.564  -41.764 -89.767  1.00 31.51  ? 370  TYR   C CE2 1 
ATOM   7291  C  CZ  . TYR   C  1 69  ? 32.238  -43.110 -89.803  1.00 37.55  ? 370  TYR   C CZ  1 
ATOM   7292  O  OH  . TYR   C  1 69  ? 32.648  -43.927 -90.837  1.00 40.35  ? 370  TYR   C OH  1 
ATOM   7293  N  N   . TYR   C  1 70  ? 33.768  -39.744 -85.778  1.00 29.11  ? 371  TYR   C N   1 
ATOM   7294  C  CA  . TYR   C  1 70  ? 35.145  -39.674 -86.229  1.00 31.52  ? 371  TYR   C CA  1 
ATOM   7295  C  C   . TYR   C  1 70  ? 36.125  -40.040 -85.132  1.00 30.75  ? 371  TYR   C C   1 
ATOM   7296  O  O   . TYR   C  1 70  ? 37.204  -40.573 -85.421  1.00 35.79  ? 371  TYR   C O   1 
ATOM   7297  C  CB  . TYR   C  1 70  ? 35.427  -38.292 -86.806  1.00 32.10  ? 371  TYR   C CB  1 
ATOM   7298  C  CG  . TYR   C  1 70  ? 35.062  -38.285 -88.262  1.00 29.47  ? 371  TYR   C CG  1 
ATOM   7299  C  CD1 . TYR   C  1 70  ? 33.783  -37.944 -88.673  1.00 27.19  ? 371  TYR   C CD1 1 
ATOM   7300  C  CD2 . TYR   C  1 70  ? 35.969  -38.703 -89.214  1.00 31.73  ? 371  TYR   C CD2 1 
ATOM   7301  C  CE1 . TYR   C  1 70  ? 33.434  -37.975 -90.007  1.00 34.35  ? 371  TYR   C CE1 1 
ATOM   7302  C  CE2 . TYR   C  1 70  ? 35.632  -38.737 -90.555  1.00 32.57  ? 371  TYR   C CE2 1 
ATOM   7303  C  CZ  . TYR   C  1 70  ? 34.365  -38.376 -90.942  1.00 35.25  ? 371  TYR   C CZ  1 
ATOM   7304  O  OH  . TYR   C  1 70  ? 34.025  -38.407 -92.268  1.00 36.45  ? 371  TYR   C OH  1 
ATOM   7305  N  N   . SER   C  1 71  ? 35.764  -39.786 -83.880  1.00 28.73  ? 372  SER   C N   1 
ATOM   7306  C  CA  . SER   C  1 71  ? 36.585  -40.258 -82.774  1.00 39.91  ? 372  SER   C CA  1 
ATOM   7307  C  C   . SER   C  1 71  ? 36.612  -41.780 -82.735  1.00 43.29  ? 372  SER   C C   1 
ATOM   7308  O  O   . SER   C  1 71  ? 37.679  -42.381 -82.571  1.00 52.52  ? 372  SER   C O   1 
ATOM   7309  C  CB  . SER   C  1 71  ? 36.063  -39.678 -81.462  1.00 38.63  ? 372  SER   C CB  1 
ATOM   7310  O  OG  . SER   C  1 71  ? 36.930  -39.987 -80.387  1.00 54.84  ? 372  SER   C OG  1 
ATOM   7311  N  N   . SER   C  1 72  ? 35.454  -42.419 -82.941  1.00 36.46  ? 373  SER   C N   1 
ATOM   7312  C  CA  . SER   C  1 72  ? 35.363  -43.875 -82.854  1.00 37.10  ? 373  SER   C CA  1 
ATOM   7313  C  C   . SER   C  1 72  ? 36.239  -44.570 -83.886  1.00 45.50  ? 373  SER   C C   1 
ATOM   7314  O  O   . SER   C  1 72  ? 36.771  -45.655 -83.618  1.00 51.40  ? 373  SER   C O   1 
ATOM   7315  C  CB  . SER   C  1 72  ? 33.922  -44.319 -83.041  1.00 35.93  ? 373  SER   C CB  1 
ATOM   7316  O  OG  . SER   C  1 72  ? 33.615  -44.347 -84.425  1.00 42.37  ? 373  SER   C OG  1 
ATOM   7317  N  N   . ILE   C  1 73  ? 36.389  -43.971 -85.065  1.00 43.90  ? 374  ILE   C N   1 
ATOM   7318  C  CA  . ILE   C  1 73  ? 37.223  -44.515 -86.120  1.00 44.50  ? 374  ILE   C CA  1 
ATOM   7319  C  C   . ILE   C  1 73  ? 38.623  -43.903 -86.098  1.00 48.20  ? 374  ILE   C C   1 
ATOM   7320  O  O   . ILE   C  1 73  ? 39.344  -43.973 -87.096  1.00 45.22  ? 374  ILE   C O   1 
ATOM   7321  C  CB  . ILE   C  1 73  ? 36.566  -44.346 -87.494  1.00 43.36  ? 374  ILE   C CB  1 
ATOM   7322  C  CG1 . ILE   C  1 73  ? 36.456  -42.862 -87.863  1.00 43.52  ? 374  ILE   C CG1 1 
ATOM   7323  C  CG2 . ILE   C  1 73  ? 35.197  -45.016 -87.501  1.00 35.19  ? 374  ILE   C CG2 1 
ATOM   7324  C  CD1 . ILE   C  1 73  ? 36.048  -42.611 -89.318  1.00 39.24  ? 374  ILE   C CD1 1 
ATOM   7325  N  N   . LYS   C  1 74  ? 39.012  -43.304 -84.970  1.00 50.49  ? 375  LYS   C N   1 
ATOM   7326  C  CA  . LYS   C  1 74  ? 40.346  -42.734 -84.768  1.00 52.43  ? 375  LYS   C CA  1 
ATOM   7327  C  C   . LYS   C  1 74  ? 40.732  -41.803 -85.914  1.00 49.04  ? 375  LYS   C C   1 
ATOM   7328  O  O   . LYS   C  1 74  ? 41.845  -41.845 -86.441  1.00 54.99  ? 375  LYS   C O   1 
ATOM   7329  C  CB  . LYS   C  1 74  ? 41.386  -43.837 -84.571  1.00 59.39  ? 375  LYS   C CB  1 
ATOM   7330  C  CG  . LYS   C  1 74  ? 41.109  -44.747 -83.375  1.00 65.04  ? 375  LYS   C CG  1 
ATOM   7331  C  CD  . LYS   C  1 74  ? 41.230  -44.003 -82.043  1.00 75.98  ? 375  LYS   C CD  1 
ATOM   7332  C  CE  . LYS   C  1 74  ? 40.901  -44.907 -80.847  1.00 75.02  ? 375  LYS   C CE  1 
ATOM   7333  N  NZ  . LYS   C  1 74  ? 39.486  -45.403 -80.857  1.00 72.57  ? 375  LYS   C NZ  1 
ATOM   7334  N  N   . ARG   C  1 75  ? 39.782  -40.953 -86.306  1.00 43.35  ? 376  ARG   C N   1 
ATOM   7335  C  CA  . ARG   C  1 75  ? 40.010  -39.934 -87.324  1.00 45.12  ? 376  ARG   C CA  1 
ATOM   7336  C  C   . ARG   C  1 75  ? 39.591  -38.554 -86.830  1.00 41.13  ? 376  ARG   C C   1 
ATOM   7337  O  O   . ARG   C  1 75  ? 39.285  -37.671 -87.645  1.00 39.37  ? 376  ARG   C O   1 
ATOM   7338  C  CB  . ARG   C  1 75  ? 39.263  -40.272 -88.619  1.00 44.46  ? 376  ARG   C CB  1 
ATOM   7339  C  CG  . ARG   C  1 75  ? 39.755  -41.504 -89.327  1.00 45.19  ? 376  ARG   C CG  1 
ATOM   7340  C  CD  . ARG   C  1 75  ? 41.062  -41.250 -90.050  1.00 51.90  ? 376  ARG   C CD  1 
ATOM   7341  N  NE  . ARG   C  1 75  ? 41.416  -42.381 -90.902  1.00 56.70  ? 376  ARG   C NE  1 
ATOM   7342  C  CZ  . ARG   C  1 75  ? 41.959  -43.510 -90.452  1.00 55.88  ? 376  ARG   C CZ  1 
ATOM   7343  N  NH1 . ARG   C  1 75  ? 42.240  -44.489 -91.301  1.00 49.14  ? 376  ARG   C NH1 1 
ATOM   7344  N  NH2 . ARG   C  1 75  ? 42.222  -43.657 -89.154  1.00 53.87  ? 376  ARG   C NH2 1 
ATOM   7345  N  N   . PHE   C  1 76  ? 39.557  -38.351 -85.512  1.00 39.29  ? 377  PHE   C N   1 
ATOM   7346  C  CA  . PHE   C  1 76  ? 39.139  -37.065 -84.972  1.00 38.01  ? 377  PHE   C CA  1 
ATOM   7347  C  C   . PHE   C  1 76  ? 40.112  -35.974 -85.395  1.00 42.53  ? 377  PHE   C C   1 
ATOM   7348  O  O   . PHE   C  1 76  ? 41.331  -36.134 -85.282  1.00 45.93  ? 377  PHE   C O   1 
ATOM   7349  C  CB  . PHE   C  1 76  ? 39.054  -37.129 -83.448  1.00 36.43  ? 377  PHE   C CB  1 
ATOM   7350  C  CG  . PHE   C  1 76  ? 38.399  -35.921 -82.828  1.00 38.07  ? 377  PHE   C CG  1 
ATOM   7351  C  CD1 . PHE   C  1 76  ? 37.040  -35.913 -82.572  1.00 34.91  ? 377  PHE   C CD1 1 
ATOM   7352  C  CD2 . PHE   C  1 76  ? 39.144  -34.798 -82.504  1.00 41.65  ? 377  PHE   C CD2 1 
ATOM   7353  C  CE1 . PHE   C  1 76  ? 36.435  -34.811 -82.010  1.00 40.67  ? 377  PHE   C CE1 1 
ATOM   7354  C  CE2 . PHE   C  1 76  ? 38.543  -33.691 -81.933  1.00 45.21  ? 377  PHE   C CE2 1 
ATOM   7355  C  CZ  . PHE   C  1 76  ? 37.189  -33.699 -81.685  1.00 39.58  ? 377  PHE   C CZ  1 
ATOM   7356  N  N   . GLY   C  1 77  ? 39.571  -34.852 -85.867  1.00 40.18  ? 378  GLY   C N   1 
ATOM   7357  C  CA  . GLY   C  1 77  ? 40.399  -33.760 -86.333  1.00 45.78  ? 378  GLY   C CA  1 
ATOM   7358  C  C   . GLY   C  1 77  ? 40.988  -33.966 -87.707  1.00 45.03  ? 378  GLY   C C   1 
ATOM   7359  O  O   . GLY   C  1 77  ? 41.655  -33.061 -88.222  1.00 52.32  ? 378  GLY   C O   1 
ATOM   7360  N  N   . SER   C  1 78  ? 40.765  -35.125 -88.319  1.00 45.08  ? 379  SER   C N   1 
ATOM   7361  C  CA  . SER   C  1 78  ? 41.346  -35.408 -89.621  1.00 47.09  ? 379  SER   C CA  1 
ATOM   7362  C  C   . SER   C  1 78  ? 40.749  -34.496 -90.687  1.00 50.61  ? 379  SER   C C   1 
ATOM   7363  O  O   . SER   C  1 78  ? 39.749  -33.802 -90.476  1.00 44.44  ? 379  SER   C O   1 
ATOM   7364  C  CB  . SER   C  1 78  ? 41.121  -36.867 -90.007  1.00 39.56  ? 379  SER   C CB  1 
ATOM   7365  O  OG  . SER   C  1 78  ? 39.739  -37.172 -90.022  1.00 38.08  ? 379  SER   C OG  1 
ATOM   7366  N  N   . LYS   C  1 79  ? 41.393  -34.505 -91.855  1.00 49.91  ? 380  LYS   C N   1 
ATOM   7367  C  CA  . LYS   C  1 79  ? 40.866  -33.759 -92.988  1.00 47.61  ? 380  LYS   C CA  1 
ATOM   7368  C  C   . LYS   C  1 79  ? 39.441  -34.197 -93.304  1.00 42.39  ? 380  LYS   C C   1 
ATOM   7369  O  O   . LYS   C  1 79  ? 38.552  -33.361 -93.494  1.00 41.37  ? 380  LYS   C O   1 
ATOM   7370  C  CB  . LYS   C  1 79  ? 41.785  -33.946 -94.202  1.00 58.81  ? 380  LYS   C CB  1 
ATOM   7371  C  CG  . LYS   C  1 79  ? 41.435  -33.084 -95.409  1.00 70.94  ? 380  LYS   C CG  1 
ATOM   7372  C  CD  . LYS   C  1 79  ? 42.031  -33.652 -96.704  1.00 82.43  ? 380  LYS   C CD  1 
ATOM   7373  C  CE  . LYS   C  1 79  ? 43.528  -33.379 -96.843  1.00 85.80  ? 380  LYS   C CE  1 
ATOM   7374  N  NZ  . LYS   C  1 79  ? 43.803  -31.975 -97.270  1.00 87.92  ? 380  LYS   C NZ  1 
ATOM   7375  N  N   . ALA   C  1 80  ? 39.202  -35.512 -93.345  1.00 33.61  ? 381  ALA   C N   1 
ATOM   7376  C  CA  . ALA   C  1 80  ? 37.862  -36.022 -93.622  1.00 39.73  ? 381  ALA   C CA  1 
ATOM   7377  C  C   . ALA   C  1 80  ? 36.864  -35.576 -92.560  1.00 42.04  ? 381  ALA   C C   1 
ATOM   7378  O  O   . ALA   C  1 80  ? 35.706  -35.270 -92.871  1.00 45.23  ? 381  ALA   C O   1 
ATOM   7379  C  CB  . ALA   C  1 80  ? 37.891  -37.548 -93.710  1.00 41.02  ? 381  ALA   C CB  1 
ATOM   7380  N  N   . HIS   C  1 81  ? 37.287  -35.560 -91.299  1.00 34.78  ? 382  HIS   C N   1 
ATOM   7381  C  CA  . HIS   C  1 81  ? 36.409  -35.099 -90.230  1.00 32.12  ? 382  HIS   C CA  1 
ATOM   7382  C  C   . HIS   C  1 81  ? 35.978  -33.655 -90.466  1.00 34.26  ? 382  HIS   C C   1 
ATOM   7383  O  O   . HIS   C  1 81  ? 34.783  -33.337 -90.425  1.00 33.07  ? 382  HIS   C O   1 
ATOM   7384  C  CB  . HIS   C  1 81  ? 37.126  -35.244 -88.885  1.00 30.87  ? 382  HIS   C CB  1 
ATOM   7385  C  CG  . HIS   C  1 81  ? 36.293  -34.861 -87.706  1.00 30.18  ? 382  HIS   C CG  1 
ATOM   7386  N  ND1 . HIS   C  1 81  ? 36.822  -34.728 -86.439  1.00 32.92  ? 382  HIS   C ND1 1 
ATOM   7387  C  CD2 . HIS   C  1 81  ? 34.968  -34.603 -87.590  1.00 30.98  ? 382  HIS   C CD2 1 
ATOM   7388  C  CE1 . HIS   C  1 81  ? 35.860  -34.399 -85.594  1.00 29.72  ? 382  HIS   C CE1 1 
ATOM   7389  N  NE2 . HIS   C  1 81  ? 34.724  -34.323 -86.264  1.00 32.57  ? 382  HIS   C NE2 1 
ATOM   7390  N  N   . MET   C  1 82  ? 36.942  -32.767 -90.724  1.00 33.22  ? 383  MET   C N   1 
ATOM   7391  C  CA  . MET   C  1 82  ? 36.623  -31.354 -90.910  1.00 37.20  ? 383  MET   C CA  1 
ATOM   7392  C  C   . MET   C  1 82  ? 35.766  -31.133 -92.151  1.00 38.82  ? 383  MET   C C   1 
ATOM   7393  O  O   . MET   C  1 82  ? 34.814  -30.343 -92.123  1.00 39.75  ? 383  MET   C O   1 
ATOM   7394  C  CB  . MET   C  1 82  ? 37.912  -30.528 -90.977  1.00 37.49  ? 383  MET   C CB  1 
ATOM   7395  C  CG  . MET   C  1 82  ? 38.702  -30.514 -89.664  1.00 47.58  ? 383  MET   C CG  1 
ATOM   7396  S  SD  . MET   C  1 82  ? 37.806  -29.810 -88.245  1.00 57.10  ? 383  MET   C SD  1 
ATOM   7397  C  CE  . MET   C  1 82  ? 37.360  -31.293 -87.360  1.00 53.93  ? 383  MET   C CE  1 
ATOM   7398  N  N   . GLU   C  1 83  ? 36.070  -31.828 -93.247  1.00 38.38  ? 384  GLU   C N   1 
ATOM   7399  C  CA  . GLU   C  1 83  ? 35.273  -31.644 -94.453  1.00 44.57  ? 384  GLU   C CA  1 
ATOM   7400  C  C   . GLU   C  1 83  ? 33.864  -32.183 -94.262  1.00 39.67  ? 384  GLU   C C   1 
ATOM   7401  O  O   . GLU   C  1 83  ? 32.895  -31.587 -94.745  1.00 45.21  ? 384  GLU   C O   1 
ATOM   7402  C  CB  . GLU   C  1 83  ? 35.961  -32.304 -95.646  1.00 45.97  ? 384  GLU   C CB  1 
ATOM   7403  C  CG  . GLU   C  1 83  ? 36.827  -31.331 -96.422  1.00 59.18  ? 384  GLU   C CG  1 
ATOM   7404  C  CD  . GLU   C  1 83  ? 37.984  -31.994 -97.143  1.00 67.72  ? 384  GLU   C CD  1 
ATOM   7405  O  OE1 . GLU   C  1 83  ? 37.888  -33.199 -97.468  1.00 71.51  ? 384  GLU   C OE1 1 
ATOM   7406  O  OE2 . GLU   C  1 83  ? 38.995  -31.300 -97.380  1.00 72.38  ? 384  GLU   C OE2 1 
ATOM   7407  N  N   . ARG   C  1 84  ? 33.729  -33.301 -93.550  1.00 36.97  ? 385  ARG   C N   1 
ATOM   7408  C  CA  . ARG   C  1 84  ? 32.400  -33.811 -93.239  1.00 33.99  ? 385  ARG   C CA  1 
ATOM   7409  C  C   . ARG   C  1 84  ? 31.612  -32.798 -92.421  1.00 33.81  ? 385  ARG   C C   1 
ATOM   7410  O  O   . ARG   C  1 84  ? 30.434  -32.542 -92.700  1.00 33.10  ? 385  ARG   C O   1 
ATOM   7411  C  CB  . ARG   C  1 84  ? 32.516  -35.137 -92.493  1.00 31.21  ? 385  ARG   C CB  1 
ATOM   7412  C  CG  . ARG   C  1 84  ? 31.189  -35.793 -92.189  1.00 29.91  ? 385  ARG   C CG  1 
ATOM   7413  C  CD  . ARG   C  1 84  ? 30.342  -35.954 -93.440  1.00 29.33  ? 385  ARG   C CD  1 
ATOM   7414  N  NE  . ARG   C  1 84  ? 29.057  -36.567 -93.108  1.00 28.89  ? 385  ARG   C NE  1 
ATOM   7415  C  CZ  . ARG   C  1 84  ? 27.929  -36.359 -93.772  1.00 33.92  ? 385  ARG   C CZ  1 
ATOM   7416  N  NH1 . ARG   C  1 84  ? 27.912  -35.552 -94.832  1.00 39.40  ? 385  ARG   C NH1 1 
ATOM   7417  N  NH2 . ARG   C  1 84  ? 26.813  -36.953 -93.371  1.00 27.97  ? 385  ARG   C NH2 1 
ATOM   7418  N  N   . LEU   C  1 85  ? 32.255  -32.202 -91.417  1.00 35.99  ? 386  LEU   C N   1 
ATOM   7419  C  CA  . LEU   C  1 85  ? 31.597  -31.193 -90.594  1.00 37.00  ? 386  LEU   C CA  1 
ATOM   7420  C  C   . LEU   C  1 85  ? 31.153  -30.010 -91.440  1.00 45.13  ? 386  LEU   C C   1 
ATOM   7421  O  O   . LEU   C  1 85  ? 30.033  -29.507 -91.286  1.00 41.84  ? 386  LEU   C O   1 
ATOM   7422  C  CB  . LEU   C  1 85  ? 32.551  -30.734 -89.498  1.00 43.56  ? 386  LEU   C CB  1 
ATOM   7423  C  CG  . LEU   C  1 85  ? 32.165  -30.763 -88.022  1.00 45.54  ? 386  LEU   C CG  1 
ATOM   7424  C  CD1 . LEU   C  1 85  ? 31.087  -31.778 -87.727  1.00 37.83  ? 386  LEU   C CD1 1 
ATOM   7425  C  CD2 . LEU   C  1 85  ? 33.409  -31.068 -87.221  1.00 46.50  ? 386  LEU   C CD2 1 
ATOM   7426  N  N   . GLU   C  1 86  ? 32.022  -29.553 -92.344  1.00 45.79  ? 387  GLU   C N   1 
ATOM   7427  C  CA  . GLU   C  1 86  ? 31.653  -28.445 -93.211  1.00 48.34  ? 387  GLU   C CA  1 
ATOM   7428  C  C   . GLU   C  1 86  ? 30.501  -28.835 -94.121  1.00 44.09  ? 387  GLU   C C   1 
ATOM   7429  O  O   . GLU   C  1 86  ? 29.535  -28.078 -94.280  1.00 36.80  ? 387  GLU   C O   1 
ATOM   7430  C  CB  . GLU   C  1 86  ? 32.863  -27.990 -94.027  1.00 56.08  ? 387  GLU   C CB  1 
ATOM   7431  C  CG  . GLU   C  1 86  ? 32.691  -26.593 -94.557  1.00 76.85  ? 387  GLU   C CG  1 
ATOM   7432  C  CD  . GLU   C  1 86  ? 31.867  -25.716 -93.605  1.00 91.58  ? 387  GLU   C CD  1 
ATOM   7433  O  OE1 . GLU   C  1 86  ? 32.363  -25.367 -92.508  1.00 93.74  ? 387  GLU   C OE1 1 
ATOM   7434  O  OE2 . GLU   C  1 86  ? 30.715  -25.378 -93.958  1.00 93.99  ? 387  GLU   C OE2 1 
ATOM   7435  N  N   . GLU   C  1 87  ? 30.577  -30.025 -94.711  1.00 41.57  ? 388  GLU   C N   1 
ATOM   7436  C  CA  . GLU   C  1 87  ? 29.504  -30.497 -95.572  1.00 39.79  ? 388  GLU   C CA  1 
ATOM   7437  C  C   . GLU   C  1 87  ? 28.182  -30.578 -94.816  1.00 39.48  ? 388  GLU   C C   1 
ATOM   7438  O  O   . GLU   C  1 87  ? 27.138  -30.172 -95.342  1.00 36.05  ? 388  GLU   C O   1 
ATOM   7439  C  CB  . GLU   C  1 87  ? 29.891  -31.854 -96.156  1.00 40.45  ? 388  GLU   C CB  1 
ATOM   7440  C  CG  . GLU   C  1 87  ? 28.860  -32.473 -97.051  1.00 46.63  ? 388  GLU   C CG  1 
ATOM   7441  C  CD  . GLU   C  1 87  ? 29.263  -33.854 -97.523  1.00 57.72  ? 388  GLU   C CD  1 
ATOM   7442  O  OE1 . GLU   C  1 87  ? 29.831  -34.630 -96.721  1.00 59.44  ? 388  GLU   C OE1 1 
ATOM   7443  O  OE2 . GLU   C  1 87  ? 29.014  -34.160 -98.706  1.00 65.91  ? 388  GLU   C OE2 1 
ATOM   7444  N  N   . VAL   C  1 88  ? 28.209  -31.090 -93.575  1.00 29.33  ? 389  VAL   C N   1 
ATOM   7445  C  CA  . VAL   C  1 88  ? 26.981  -31.227 -92.788  1.00 32.61  ? 389  VAL   C CA  1 
ATOM   7446  C  C   . VAL   C  1 88  ? 26.379  -29.860 -92.515  1.00 37.70  ? 389  VAL   C C   1 
ATOM   7447  O  O   . VAL   C  1 88  ? 25.169  -29.653 -92.667  1.00 39.58  ? 389  VAL   C O   1 
ATOM   7448  C  CB  . VAL   C  1 88  ? 27.245  -31.983 -91.468  1.00 34.16  ? 389  VAL   C CB  1 
ATOM   7449  C  CG1 . VAL   C  1 88  ? 26.087  -31.765 -90.504  1.00 34.07  ? 389  VAL   C CG1 1 
ATOM   7450  C  CG2 . VAL   C  1 88  ? 27.434  -33.475 -91.714  1.00 34.75  ? 389  VAL   C CG2 1 
ATOM   7451  N  N   . ASN   C  1 89  ? 27.217  -28.908 -92.101  1.00 39.86  ? 390  ASN   C N   1 
ATOM   7452  C  CA  . ASN   C  1 89  ? 26.723  -27.571 -91.788  1.00 37.07  ? 390  ASN   C CA  1 
ATOM   7453  C  C   . ASN   C  1 89  ? 26.163  -26.881 -93.029  1.00 38.38  ? 390  ASN   C C   1 
ATOM   7454  O  O   . ASN   C  1 89  ? 25.151  -26.175 -92.940  1.00 37.96  ? 390  ASN   C O   1 
ATOM   7455  C  CB  . ASN   C  1 89  ? 27.832  -26.733 -91.142  1.00 40.63  ? 390  ASN   C CB  1 
ATOM   7456  C  CG  . ASN   C  1 89  ? 28.254  -27.265 -89.770  1.00 57.07  ? 390  ASN   C CG  1 
ATOM   7457  O  OD1 . ASN   C  1 89  ? 27.451  -27.850 -89.020  1.00 55.87  ? 390  ASN   C OD1 1 
ATOM   7458  N  ND2 . ASN   C  1 89  ? 29.521  -27.056 -89.432  1.00 61.01  ? 390  ASN   C ND2 1 
ATOM   7459  N  N   . LYS   C  1 90  ? 26.791  -27.094 -94.194  1.00 36.01  ? 391  LYS   C N   1 
ATOM   7460  C  CA  . LYS   C  1 90  ? 26.252  -26.585 -95.456  1.00 47.81  ? 391  LYS   C CA  1 
ATOM   7461  C  C   . LYS   C  1 90  ? 24.847  -27.111 -95.709  1.00 45.33  ? 391  LYS   C C   1 
ATOM   7462  O  O   . LYS   C  1 90  ? 23.944  -26.353 -96.084  1.00 48.53  ? 391  LYS   C O   1 
ATOM   7463  C  CB  . LYS   C  1 90  ? 27.160  -26.975 -96.630  1.00 54.18  ? 391  LYS   C CB  1 
ATOM   7464  C  CG  . LYS   C  1 90  ? 28.451  -26.185 -96.752  1.00 69.78  ? 391  LYS   C CG  1 
ATOM   7465  C  CD  . LYS   C  1 90  ? 29.366  -26.777 -97.823  1.00 77.27  ? 391  LYS   C CD  1 
ATOM   7466  C  CE  . LYS   C  1 90  ? 30.730  -26.093 -97.825  1.00 82.80  ? 391  LYS   C CE  1 
ATOM   7467  N  NZ  . LYS   C  1 90  ? 31.802  -26.983 -98.365  1.00 83.60  ? 391  LYS   C NZ  1 
ATOM   7468  N  N   . GLU   C  1 91  ? 24.658  -28.424 -95.557  1.00 34.87  ? 392  GLU   C N   1 
ATOM   7469  C  CA  . GLU   C  1 91  ? 23.346  -29.024 -95.774  1.00 34.28  ? 392  GLU   C CA  1 
ATOM   7470  C  C   . GLU   C  1 91  ? 22.313  -28.472 -94.802  1.00 36.94  ? 392  GLU   C C   1 
ATOM   7471  O  O   . GLU   C  1 91  ? 21.191  -28.138 -95.196  1.00 43.49  ? 392  GLU   C O   1 
ATOM   7472  C  CB  . GLU   C  1 91  ? 23.431  -30.541 -95.637  1.00 36.87  ? 392  GLU   C CB  1 
ATOM   7473  C  CG  . GLU   C  1 91  ? 23.724  -31.249 -96.918  1.00 43.39  ? 392  GLU   C CG  1 
ATOM   7474  C  CD  . GLU   C  1 91  ? 23.791  -32.745 -96.755  1.00 50.75  ? 392  GLU   C CD  1 
ATOM   7475  O  OE1 . GLU   C  1 91  ? 22.743  -33.369 -96.507  1.00 57.37  ? 392  GLU   C OE1 1 
ATOM   7476  O  OE2 . GLU   C  1 91  ? 24.900  -33.298 -96.877  1.00 62.04  ? 392  GLU   C OE2 1 
ATOM   7477  N  N   . ILE   C  1 92  ? 22.658  -28.408 -93.517  1.00 38.91  ? 393  ILE   C N   1 
ATOM   7478  C  CA  . ILE   C  1 92  ? 21.740  -27.823 -92.546  1.00 43.50  ? 393  ILE   C CA  1 
ATOM   7479  C  C   . ILE   C  1 92  ? 21.430  -26.383 -92.929  1.00 47.30  ? 393  ILE   C C   1 
ATOM   7480  O  O   . ILE   C  1 92  ? 20.270  -25.961 -92.937  1.00 49.45  ? 393  ILE   C O   1 
ATOM   7481  C  CB  . ILE   C  1 92  ? 22.321  -27.921 -91.126  1.00 34.83  ? 393  ILE   C CB  1 
ATOM   7482  C  CG1 . ILE   C  1 92  ? 22.506  -29.392 -90.728  1.00 35.87  ? 393  ILE   C CG1 1 
ATOM   7483  C  CG2 . ILE   C  1 92  ? 21.438  -27.160 -90.120  1.00 35.16  ? 393  ILE   C CG2 1 
ATOM   7484  C  CD1 . ILE   C  1 92  ? 23.278  -29.580 -89.433  1.00 33.67  ? 393  ILE   C CD1 1 
ATOM   7485  N  N   . ASP   C  1 93  ? 22.466  -25.616 -93.276  1.00 47.64  ? 394  ASP   C N   1 
ATOM   7486  C  CA  . ASP   C  1 93  ? 22.278  -24.211 -93.631  1.00 53.43  ? 394  ASP   C CA  1 
ATOM   7487  C  C   . ASP   C  1 93  ? 21.320  -24.048 -94.808  1.00 50.79  ? 394  ASP   C C   1 
ATOM   7488  O  O   . ASP   C  1 93  ? 20.450  -23.171 -94.788  1.00 54.92  ? 394  ASP   C O   1 
ATOM   7489  C  CB  . ASP   C  1 93  ? 23.626  -23.571 -93.959  1.00 66.18  ? 394  ASP   C CB  1 
ATOM   7490  C  CG  . ASP   C  1 93  ? 23.780  -22.196 -93.354  1.00 77.29  ? 394  ASP   C CG  1 
ATOM   7491  O  OD1 . ASP   C  1 93  ? 24.438  -22.083 -92.299  1.00 82.70  ? 394  ASP   C OD1 1 
ATOM   7492  O  OD2 . ASP   C  1 93  ? 23.231  -21.230 -93.923  1.00 81.90  ? 394  ASP   C OD2 1 
ATOM   7493  N  N   . THR   C  1 94  ? 21.462  -24.880 -95.842  1.00 46.05  ? 395  THR   C N   1 
ATOM   7494  C  CA  . THR   C  1 94  ? 20.657  -24.714 -97.046  1.00 51.34  ? 395  THR   C CA  1 
ATOM   7495  C  C   . THR   C  1 94  ? 19.333  -25.465 -96.987  1.00 56.48  ? 395  THR   C C   1 
ATOM   7496  O  O   . THR   C  1 94  ? 18.316  -24.948 -97.463  1.00 62.29  ? 395  THR   C O   1 
ATOM   7497  C  CB  . THR   C  1 94  ? 21.438  -25.174 -98.281  1.00 59.45  ? 395  THR   C CB  1 
ATOM   7498  O  OG1 . THR   C  1 94  ? 21.769  -26.560 -98.154  1.00 61.35  ? 395  THR   C OG1 1 
ATOM   7499  C  CG2 . THR   C  1 94  ? 22.712  -24.357 -98.455  1.00 63.71  ? 395  THR   C CG2 1 
ATOM   7500  N  N   . THR   C  1 95  ? 19.313  -26.675 -96.424  1.00 53.19  ? 396  THR   C N   1 
ATOM   7501  C  CA  . THR   C  1 95  ? 18.131  -27.526 -96.486  1.00 46.53  ? 396  THR   C CA  1 
ATOM   7502  C  C   . THR   C  1 95  ? 17.412  -27.678 -95.153  1.00 45.68  ? 396  THR   C C   1 
ATOM   7503  O  O   . THR   C  1 95  ? 16.354  -28.312 -95.117  1.00 49.64  ? 396  THR   C O   1 
ATOM   7504  C  CB  . THR   C  1 95  ? 18.495  -28.931 -97.004  1.00 43.43  ? 396  THR   C CB  1 
ATOM   7505  O  OG1 . THR   C  1 95  ? 19.139  -29.679 -95.965  1.00 45.46  ? 396  THR   C OG1 1 
ATOM   7506  C  CG2 . THR   C  1 95  ? 19.416  -28.850 -98.218  1.00 36.95  ? 396  THR   C CG2 1 
ATOM   7507  N  N   . SER   C  1 96  ? 17.954  -27.129 -94.067  1.00 42.78  ? 397  SER   C N   1 
ATOM   7508  C  CA  . SER   C  1 96  ? 17.439  -27.253 -92.702  1.00 43.90  ? 397  SER   C CA  1 
ATOM   7509  C  C   . SER   C  1 96  ? 17.534  -28.670 -92.167  1.00 43.82  ? 397  SER   C C   1 
ATOM   7510  O  O   . SER   C  1 96  ? 16.922  -28.983 -91.145  1.00 45.05  ? 397  SER   C O   1 
ATOM   7511  C  CB  . SER   C  1 96  ? 15.995  -26.758 -92.582  1.00 52.02  ? 397  SER   C CB  1 
ATOM   7512  O  OG  . SER   C  1 96  ? 15.931  -25.358 -92.799  1.00 59.97  ? 397  SER   C OG  1 
ATOM   7513  N  N   . THR   C  1 97  ? 18.283  -29.536 -92.833  1.00 41.40  ? 398  THR   C N   1 
ATOM   7514  C  CA  . THR   C  1 97  ? 18.507  -30.899 -92.380  1.00 34.97  ? 398  THR   C CA  1 
ATOM   7515  C  C   . THR   C  1 97  ? 19.788  -31.375 -93.043  1.00 32.00  ? 398  THR   C C   1 
ATOM   7516  O  O   . THR   C  1 97  ? 20.468  -30.610 -93.731  1.00 32.91  ? 398  THR   C O   1 
ATOM   7517  C  CB  . THR   C  1 97  ? 17.322  -31.806 -92.717  1.00 34.85  ? 398  THR   C CB  1 
ATOM   7518  O  OG1 . THR   C  1 97  ? 17.521  -33.093 -92.121  1.00 41.47  ? 398  THR   C OG1 1 
ATOM   7519  C  CG2 . THR   C  1 97  ? 17.173  -31.970 -94.229  1.00 27.92  ? 398  THR   C CG2 1 
ATOM   7520  N  N   . TYR   C  1 98  ? 20.131  -32.639 -92.829  1.00 29.41  ? 399  TYR   C N   1 
ATOM   7521  C  CA  . TYR   C  1 98  ? 21.256  -33.195 -93.562  1.00 36.68  ? 399  TYR   C CA  1 
ATOM   7522  C  C   . TYR   C  1 98  ? 21.029  -34.682 -93.742  1.00 32.83  ? 399  TYR   C C   1 
ATOM   7523  O  O   . TYR   C  1 98  ? 20.067  -35.253 -93.221  1.00 31.33  ? 399  TYR   C O   1 
ATOM   7524  C  CB  . TYR   C  1 98  ? 22.589  -32.898 -92.865  1.00 34.55  ? 399  TYR   C CB  1 
ATOM   7525  C  CG  . TYR   C  1 98  ? 22.794  -33.581 -91.537  1.00 32.65  ? 399  TYR   C CG  1 
ATOM   7526  C  CD1 . TYR   C  1 98  ? 23.675  -34.651 -91.417  1.00 30.39  ? 399  TYR   C CD1 1 
ATOM   7527  C  CD2 . TYR   C  1 98  ? 22.127  -33.143 -90.394  1.00 30.40  ? 399  TYR   C CD2 1 
ATOM   7528  C  CE1 . TYR   C  1 98  ? 23.881  -35.273 -90.190  1.00 33.17  ? 399  TYR   C CE1 1 
ATOM   7529  C  CE2 . TYR   C  1 98  ? 22.320  -33.762 -89.174  1.00 30.00  ? 399  TYR   C CE2 1 
ATOM   7530  C  CZ  . TYR   C  1 98  ? 23.199  -34.826 -89.080  1.00 30.98  ? 399  TYR   C CZ  1 
ATOM   7531  O  OH  . TYR   C  1 98  ? 23.395  -35.445 -87.871  1.00 34.01  ? 399  TYR   C OH  1 
ATOM   7532  N  N   . GLN   C  1 99  ? 21.925  -35.305 -94.493  1.00 24.43  ? 400  GLN   C N   1 
ATOM   7533  C  CA  . GLN   C  1 99  ? 21.834  -36.727 -94.777  1.00 31.98  ? 400  GLN   C CA  1 
ATOM   7534  C  C   . GLN   C  1 99  ? 23.042  -37.438 -94.200  1.00 31.20  ? 400  GLN   C C   1 
ATOM   7535  O  O   . GLN   C  1 99  ? 24.179  -37.012 -94.421  1.00 30.65  ? 400  GLN   C O   1 
ATOM   7536  C  CB  . GLN   C  1 99  ? 21.753  -36.988 -96.285  1.00 34.80  ? 400  GLN   C CB  1 
ATOM   7537  C  CG  . GLN   C  1 99  ? 20.521  -36.418 -96.926  1.00 38.23  ? 400  GLN   C CG  1 
ATOM   7538  C  CD  . GLN   C  1 99  ? 19.259  -37.006 -96.336  1.00 42.29  ? 400  GLN   C CD  1 
ATOM   7539  O  OE1 . GLN   C  1 99  ? 19.139  -38.223 -96.181  1.00 43.95  ? 400  GLN   C OE1 1 
ATOM   7540  N  NE2 . GLN   C  1 99  ? 18.310  -36.142 -95.999  1.00 38.43  ? 400  GLN   C NE2 1 
ATOM   7541  N  N   . LEU   C  1 100 ? 22.795  -38.529 -93.484  1.00 26.76  ? 401  LEU   C N   1 
ATOM   7542  C  CA  . LEU   C  1 100 ? 23.888  -39.362 -93.008  1.00 24.37  ? 401  LEU   C CA  1 
ATOM   7543  C  C   . LEU   C  1 100 ? 24.526  -40.125 -94.155  1.00 28.84  ? 401  LEU   C C   1 
ATOM   7544  O  O   . LEU   C  1 100 ? 23.835  -40.635 -95.039  1.00 28.09  ? 401  LEU   C O   1 
ATOM   7545  C  CB  . LEU   C  1 100 ? 23.382  -40.357 -91.970  1.00 21.92  ? 401  LEU   C CB  1 
ATOM   7546  C  CG  . LEU   C  1 100 ? 22.865  -39.702 -90.689  1.00 28.95  ? 401  LEU   C CG  1 
ATOM   7547  C  CD1 . LEU   C  1 100 ? 22.229  -40.751 -89.797  1.00 25.82  ? 401  LEU   C CD1 1 
ATOM   7548  C  CD2 . LEU   C  1 100 ? 24.014  -39.020 -89.995  1.00 24.49  ? 401  LEU   C CD2 1 
ATOM   7549  N  N   . LYS   C  1 101 ? 25.851  -40.219 -94.127  1.00 28.29  ? 402  LYS   C N   1 
ATOM   7550  C  CA  . LYS   C  1 101 ? 26.534  -41.225 -94.924  1.00 25.94  ? 402  LYS   C CA  1 
ATOM   7551  C  C   . LYS   C  1 101 ? 26.147  -42.614 -94.430  1.00 29.05  ? 402  LYS   C C   1 
ATOM   7552  O  O   . LYS   C  1 101 ? 25.728  -42.793 -93.284  1.00 29.23  ? 402  LYS   C O   1 
ATOM   7553  C  CB  . LYS   C  1 101 ? 28.049  -41.040 -94.838  1.00 28.80  ? 402  LYS   C CB  1 
ATOM   7554  C  CG  . LYS   C  1 101 ? 28.522  -39.677 -95.299  1.00 36.91  ? 402  LYS   C CG  1 
ATOM   7555  C  CD  . LYS   C  1 101 ? 28.078  -39.428 -96.743  1.00 44.08  ? 402  LYS   C CD  1 
ATOM   7556  C  CE  . LYS   C  1 101 ? 28.524  -38.062 -97.253  1.00 55.07  ? 402  LYS   C CE  1 
ATOM   7557  N  NZ  . LYS   C  1 101 ? 30.004  -37.983 -97.383  1.00 60.47  ? 402  LYS   C NZ  1 
ATOM   7558  N  N   . ASP   C  1 102 ? 26.308  -43.608 -95.309  1.00 29.64  ? 403  ASP   C N   1 
ATOM   7559  C  CA  . ASP   C  1 102 ? 25.937  -44.982 -94.972  1.00 29.58  ? 403  ASP   C CA  1 
ATOM   7560  C  C   . ASP   C  1 102 ? 26.709  -45.472 -93.760  1.00 30.72  ? 403  ASP   C C   1 
ATOM   7561  O  O   . ASP   C  1 102 ? 26.148  -46.121 -92.872  1.00 27.04  ? 403  ASP   C O   1 
ATOM   7562  C  CB  . ASP   C  1 102 ? 26.199  -45.920 -96.155  1.00 32.61  ? 403  ASP   C CB  1 
ATOM   7563  C  CG  . ASP   C  1 102 ? 25.340  -45.601 -97.376  1.00 49.27  ? 403  ASP   C CG  1 
ATOM   7564  O  OD1 . ASP   C  1 102 ? 24.464  -44.711 -97.296  1.00 48.33  ? 403  ASP   C OD1 1 
ATOM   7565  O  OD2 . ASP   C  1 102 ? 25.549  -46.251 -98.428  1.00 53.29  ? 403  ASP   C OD2 1 
ATOM   7566  N  N   . THR   C  1 103 ? 28.015  -45.214 -93.737  1.00 27.73  ? 404  THR   C N   1 
ATOM   7567  C  CA  . THR   C  1 103 ? 28.828  -45.599 -92.589  1.00 28.35  ? 404  THR   C CA  1 
ATOM   7568  C  C   . THR   C  1 103 ? 28.302  -44.967 -91.308  1.00 29.73  ? 404  THR   C C   1 
ATOM   7569  O  O   . THR   C  1 103 ? 28.248  -45.618 -90.262  1.00 31.10  ? 404  THR   C O   1 
ATOM   7570  C  CB  . THR   C  1 103 ? 30.267  -45.158 -92.829  1.00 29.24  ? 404  THR   C CB  1 
ATOM   7571  O  OG1 . THR   C  1 103 ? 30.239  -43.795 -93.258  1.00 32.70  ? 404  THR   C OG1 1 
ATOM   7572  C  CG2 . THR   C  1 103 ? 30.908  -45.988 -93.921  1.00 29.71  ? 404  THR   C CG2 1 
ATOM   7573  N  N   . GLU   C  1 104 ? 27.922  -43.688 -91.374  1.00 27.97  ? 405  GLU   C N   1 
ATOM   7574  C  CA  . GLU   C  1 104 ? 27.408  -42.996 -90.200  1.00 29.54  ? 405  GLU   C CA  1 
ATOM   7575  C  C   . GLU   C  1 104 ? 26.071  -43.578 -89.779  1.00 31.55  ? 405  GLU   C C   1 
ATOM   7576  O  O   . GLU   C  1 104 ? 25.785  -43.701 -88.578  1.00 28.42  ? 405  GLU   C O   1 
ATOM   7577  C  CB  . GLU   C  1 104 ? 27.268  -41.496 -90.482  1.00 30.52  ? 405  GLU   C CB  1 
ATOM   7578  C  CG  . GLU   C  1 104 ? 28.561  -40.780 -90.847  1.00 28.65  ? 405  GLU   C CG  1 
ATOM   7579  C  CD  . GLU   C  1 104 ? 28.311  -39.421 -91.486  1.00 31.04  ? 405  GLU   C CD  1 
ATOM   7580  O  OE1 . GLU   C  1 104 ? 29.287  -38.685 -91.740  1.00 28.49  ? 405  GLU   C OE1 1 
ATOM   7581  O  OE2 . GLU   C  1 104 ? 27.135  -39.085 -91.726  1.00 31.37  ? 405  GLU   C OE2 1 
ATOM   7582  N  N   . LEU   C  1 105 ? 25.239  -43.942 -90.755  1.00 24.12  ? 406  LEU   C N   1 
ATOM   7583  C  CA  . LEU   C  1 105 ? 23.961  -44.562 -90.427  1.00 27.12  ? 406  LEU   C CA  1 
ATOM   7584  C  C   . LEU   C  1 105 ? 24.174  -45.881 -89.698  1.00 25.49  ? 406  LEU   C C   1 
ATOM   7585  O  O   . LEU   C  1 105 ? 23.480  -46.178 -88.724  1.00 24.00  ? 406  LEU   C O   1 
ATOM   7586  C  CB  . LEU   C  1 105 ? 23.144  -44.785 -91.692  1.00 25.50  ? 406  LEU   C CB  1 
ATOM   7587  C  CG  . LEU   C  1 105 ? 21.724  -45.304 -91.467  1.00 26.71  ? 406  LEU   C CG  1 
ATOM   7588  C  CD1 . LEU   C  1 105 ? 20.864  -44.183 -90.892  1.00 26.32  ? 406  LEU   C CD1 1 
ATOM   7589  C  CD2 . LEU   C  1 105 ? 21.144  -45.842 -92.778  1.00 25.05  ? 406  LEU   C CD2 1 
ATOM   7590  N  N   . ILE   C  1 106 ? 25.122  -46.692 -90.173  1.00 25.57  ? 407  ILE   C N   1 
ATOM   7591  C  CA  . ILE   C  1 106 ? 25.372  -47.989 -89.555  1.00 23.95  ? 407  ILE   C CA  1 
ATOM   7592  C  C   . ILE   C  1 106 ? 25.897  -47.806 -88.140  1.00 24.07  ? 407  ILE   C C   1 
ATOM   7593  O  O   . ILE   C  1 106 ? 25.397  -48.418 -87.194  1.00 21.15  ? 407  ILE   C O   1 
ATOM   7594  C  CB  . ILE   C  1 106 ? 26.353  -48.803 -90.411  1.00 21.37  ? 407  ILE   C CB  1 
ATOM   7595  C  CG1 . ILE   C  1 106 ? 25.729  -49.097 -91.785  1.00 27.79  ? 407  ILE   C CG1 1 
ATOM   7596  C  CG2 . ILE   C  1 106 ? 26.778  -50.041 -89.667  1.00 23.90  ? 407  ILE   C CG2 1 
ATOM   7597  C  CD1 . ILE   C  1 106 ? 26.701  -49.718 -92.775  1.00 31.86  ? 407  ILE   C CD1 1 
ATOM   7598  N  N   . TYR   C  1 107 ? 26.931  -46.973 -87.992  1.00 29.72  ? 408  TYR   C N   1 
ATOM   7599  C  CA  . TYR   C  1 107 ? 27.449  -46.608 -86.681  1.00 27.64  ? 408  TYR   C CA  1 
ATOM   7600  C  C   . TYR   C  1 107 ? 26.347  -46.084 -85.781  1.00 28.01  ? 408  TYR   C C   1 
ATOM   7601  O  O   . TYR   C  1 107 ? 26.253  -46.454 -84.605  1.00 27.16  ? 408  TYR   C O   1 
ATOM   7602  C  CB  . TYR   C  1 107 ? 28.536  -45.547 -86.844  1.00 22.83  ? 408  TYR   C CB  1 
ATOM   7603  C  CG  . TYR   C  1 107 ? 28.979  -44.924 -85.526  1.00 27.52  ? 408  TYR   C CG  1 
ATOM   7604  C  CD1 . TYR   C  1 107 ? 30.063  -45.439 -84.827  1.00 25.23  ? 408  TYR   C CD1 1 
ATOM   7605  C  CD2 . TYR   C  1 107 ? 28.315  -43.816 -84.990  1.00 28.99  ? 408  TYR   C CD2 1 
ATOM   7606  C  CE1 . TYR   C  1 107 ? 30.469  -44.882 -83.628  1.00 26.37  ? 408  TYR   C CE1 1 
ATOM   7607  C  CE2 . TYR   C  1 107 ? 28.706  -43.259 -83.783  1.00 25.53  ? 408  TYR   C CE2 1 
ATOM   7608  C  CZ  . TYR   C  1 107 ? 29.791  -43.798 -83.109  1.00 32.35  ? 408  TYR   C CZ  1 
ATOM   7609  O  OH  . TYR   C  1 107 ? 30.211  -43.255 -81.918  1.00 34.68  ? 408  TYR   C OH  1 
ATOM   7610  N  N   . GLY   C  1 108 ? 25.531  -45.172 -86.310  1.00 27.04  ? 409  GLY   C N   1 
ATOM   7611  C  CA  . GLY   C  1 108 ? 24.481  -44.589 -85.499  1.00 24.56  ? 409  GLY   C CA  1 
ATOM   7612  C  C   . GLY   C  1 108 ? 23.505  -45.633 -85.009  1.00 26.11  ? 409  GLY   C C   1 
ATOM   7613  O  O   . GLY   C  1 108 ? 23.154  -45.667 -83.828  1.00 24.05  ? 409  GLY   C O   1 
ATOM   7614  N  N   . ALA   C  1 109 ? 23.067  -46.518 -85.911  1.00 20.52  ? 410  ALA   C N   1 
ATOM   7615  C  CA  . ALA   C  1 109 ? 22.098  -47.538 -85.522  1.00 21.78  ? 410  ALA   C CA  1 
ATOM   7616  C  C   . ALA   C  1 109 ? 22.683  -48.486 -84.483  1.00 21.32  ? 410  ALA   C C   1 
ATOM   7617  O  O   . ALA   C  1 109 ? 22.008  -48.856 -83.510  1.00 21.61  ? 410  ALA   C O   1 
ATOM   7618  C  CB  . ALA   C  1 109 ? 21.641  -48.326 -86.754  1.00 22.16  ? 410  ALA   C CB  1 
ATOM   7619  N  N   . LYS   C  1 110 ? 23.931  -48.912 -84.689  1.00 22.32  ? 411  LYS   C N   1 
ATOM   7620  C  CA  . LYS   C  1 110 ? 24.569  -49.803 -83.731  1.00 20.25  ? 411  LYS   C CA  1 
ATOM   7621  C  C   . LYS   C  1 110 ? 24.721  -49.134 -82.385  1.00 23.50  ? 411  LYS   C C   1 
ATOM   7622  O  O   . LYS   C  1 110 ? 24.517  -49.766 -81.343  1.00 22.45  ? 411  LYS   C O   1 
ATOM   7623  C  CB  . LYS   C  1 110 ? 25.934  -50.252 -84.242  1.00 24.43  ? 411  LYS   C CB  1 
ATOM   7624  C  CG  . LYS   C  1 110 ? 25.842  -51.214 -85.419  1.00 25.13  ? 411  LYS   C CG  1 
ATOM   7625  C  CD  . LYS   C  1 110 ? 27.222  -51.612 -85.904  1.00 20.48  ? 411  LYS   C CD  1 
ATOM   7626  C  CE  . LYS   C  1 110 ? 27.111  -52.610 -87.045  1.00 29.85  ? 411  LYS   C CE  1 
ATOM   7627  N  NZ  . LYS   C  1 110 ? 28.435  -53.148 -87.458  1.00 28.29  ? 411  LYS   C NZ  1 
ATOM   7628  N  N   . HIS   C  1 111 ? 25.065  -47.856 -82.377  1.00 27.70  ? 412  HIS   C N   1 
ATOM   7629  C  CA  . HIS   C  1 111 ? 25.285  -47.227 -81.088  1.00 28.62  ? 412  HIS   C CA  1 
ATOM   7630  C  C   . HIS   C  1 111 ? 23.976  -46.911 -80.387  1.00 26.45  ? 412  HIS   C C   1 
ATOM   7631  O  O   . HIS   C  1 111 ? 23.917  -46.956 -79.156  1.00 25.67  ? 412  HIS   C O   1 
ATOM   7632  C  CB  . HIS   C  1 111 ? 26.189  -46.009 -81.259  1.00 24.89  ? 412  HIS   C CB  1 
ATOM   7633  C  CG  . HIS   C  1 111 ? 27.634  -46.382 -81.249  1.00 26.51  ? 412  HIS   C CG  1 
ATOM   7634  N  ND1 . HIS   C  1 111 ? 28.228  -47.063 -82.292  1.00 26.02  ? 412  HIS   C ND1 1 
ATOM   7635  C  CD2 . HIS   C  1 111 ? 28.582  -46.259 -80.291  1.00 27.41  ? 412  HIS   C CD2 1 
ATOM   7636  C  CE1 . HIS   C  1 111 ? 29.486  -47.322 -81.984  1.00 26.44  ? 412  HIS   C CE1 1 
ATOM   7637  N  NE2 . HIS   C  1 111 ? 29.730  -46.835 -80.779  1.00 29.00  ? 412  HIS   C NE2 1 
ATOM   7638  N  N   . ALA   C  1 112 ? 22.899  -46.682 -81.132  1.00 26.84  ? 413  ALA   C N   1 
ATOM   7639  C  CA  . ALA   C  1 112 ? 21.609  -46.556 -80.466  1.00 27.22  ? 413  ALA   C CA  1 
ATOM   7640  C  C   . ALA   C  1 112 ? 21.259  -47.836 -79.727  1.00 28.37  ? 413  ALA   C C   1 
ATOM   7641  O  O   . ALA   C  1 112 ? 20.695  -47.800 -78.628  1.00 29.10  ? 413  ALA   C O   1 
ATOM   7642  C  CB  . ALA   C  1 112 ? 20.524  -46.212 -81.468  1.00 20.15  ? 413  ALA   C CB  1 
ATOM   7643  N  N   . TRP   C  1 113 ? 21.586  -48.979 -80.313  1.00 23.45  ? 414  TRP   C N   1 
ATOM   7644  C  CA  . TRP   C  1 113 ? 21.411  -50.229 -79.589  1.00 23.76  ? 414  TRP   C CA  1 
ATOM   7645  C  C   . TRP   C  1 113 ? 22.374  -50.303 -78.415  1.00 22.78  ? 414  TRP   C C   1 
ATOM   7646  O  O   . TRP   C  1 113 ? 21.978  -50.629 -77.300  1.00 25.06  ? 414  TRP   C O   1 
ATOM   7647  C  CB  . TRP   C  1 113 ? 21.619  -51.411 -80.531  1.00 20.42  ? 414  TRP   C CB  1 
ATOM   7648  C  CG  . TRP   C  1 113 ? 21.329  -52.743 -79.938  1.00 18.39  ? 414  TRP   C CG  1 
ATOM   7649  C  CD1 . TRP   C  1 113 ? 20.727  -53.016 -78.731  1.00 23.65  ? 414  TRP   C CD1 1 
ATOM   7650  C  CD2 . TRP   C  1 113 ? 21.635  -54.004 -80.528  1.00 32.28  ? 414  TRP   C CD2 1 
ATOM   7651  N  NE1 . TRP   C  1 113 ? 20.647  -54.376 -78.545  1.00 23.01  ? 414  TRP   C NE1 1 
ATOM   7652  C  CE2 . TRP   C  1 113 ? 21.204  -55.005 -79.632  1.00 30.57  ? 414  TRP   C CE2 1 
ATOM   7653  C  CE3 . TRP   C  1 113 ? 22.225  -54.387 -81.738  1.00 23.27  ? 414  TRP   C CE3 1 
ATOM   7654  C  CZ2 . TRP   C  1 113 ? 21.356  -56.365 -79.908  1.00 26.98  ? 414  TRP   C CZ2 1 
ATOM   7655  C  CZ3 . TRP   C  1 113 ? 22.380  -55.732 -82.001  1.00 23.52  ? 414  TRP   C CZ3 1 
ATOM   7656  C  CH2 . TRP   C  1 113 ? 21.939  -56.705 -81.096  1.00 24.99  ? 414  TRP   C CH2 1 
ATOM   7657  N  N   . ARG   C  1 114 ? 23.649  -50.004 -78.660  1.00 20.69  ? 415  ARG   C N   1 
ATOM   7658  C  CA  . ARG   C  1 114 ? 24.641  -50.026 -77.604  1.00 23.96  ? 415  ARG   C CA  1 
ATOM   7659  C  C   . ARG   C  1 114 ? 24.212  -49.148 -76.443  1.00 26.27  ? 415  ARG   C C   1 
ATOM   7660  O  O   . ARG   C  1 114 ? 24.485  -49.470 -75.280  1.00 24.29  ? 415  ARG   C O   1 
ATOM   7661  C  CB  . ARG   C  1 114 ? 25.986  -49.567 -78.167  1.00 23.31  ? 415  ARG   C CB  1 
ATOM   7662  C  CG  . ARG   C  1 114 ? 27.172  -49.826 -77.263  1.00 21.50  ? 415  ARG   C CG  1 
ATOM   7663  C  CD  . ARG   C  1 114 ? 28.411  -49.101 -77.768  1.00 24.23  ? 415  ARG   C CD  1 
ATOM   7664  N  NE  . ARG   C  1 114 ? 29.617  -49.612 -77.131  1.00 20.68  ? 415  ARG   C NE  1 
ATOM   7665  C  CZ  . ARG   C  1 114 ? 30.838  -49.225 -77.455  1.00 27.41  ? 415  ARG   C CZ  1 
ATOM   7666  N  NH1 . ARG   C  1 114 ? 31.887  -49.739 -76.832  1.00 21.96  ? 415  ARG   C NH1 1 
ATOM   7667  N  NH2 . ARG   C  1 114 ? 30.999  -48.333 -78.420  1.00 23.78  ? 415  ARG   C NH2 1 
ATOM   7668  N  N   . ASN   C  1 115 ? 23.510  -48.059 -76.734  1.00 21.63  ? 416  ASN   C N   1 
ATOM   7669  C  CA  . ASN   C  1 115 ? 23.087  -47.113 -75.718  1.00 23.21  ? 416  ASN   C CA  1 
ATOM   7670  C  C   . ASN   C  1 115 ? 21.722  -47.439 -75.125  1.00 26.04  ? 416  ASN   C C   1 
ATOM   7671  O  O   . ASN   C  1 115 ? 21.265  -46.707 -74.239  1.00 23.82  ? 416  ASN   C O   1 
ATOM   7672  C  CB  . ASN   C  1 115 ? 23.070  -45.702 -76.309  1.00 21.34  ? 416  ASN   C CB  1 
ATOM   7673  C  CG  . ASN   C  1 115 ? 24.447  -45.234 -76.735  1.00 24.04  ? 416  ASN   C CG  1 
ATOM   7674  O  OD1 . ASN   C  1 115 ? 25.459  -45.754 -76.273  1.00 23.34  ? 416  ASN   C OD1 1 
ATOM   7675  N  ND2 . ASN   C  1 115 ? 24.491  -44.231 -77.607  1.00 21.15  ? 416  ASN   C ND2 1 
ATOM   7676  N  N   . ALA   C  1 116 ? 21.056  -48.503 -75.583  1.00 17.63  ? 417  ALA   C N   1 
ATOM   7677  C  CA  . ALA   C  1 116 ? 19.716  -48.793 -75.089  1.00 22.85  ? 417  ALA   C CA  1 
ATOM   7678  C  C   . ALA   C  1 116 ? 19.802  -49.326 -73.659  1.00 25.49  ? 417  ALA   C C   1 
ATOM   7679  O  O   . ALA   C  1 116 ? 20.010  -50.521 -73.441  1.00 22.70  ? 417  ALA   C O   1 
ATOM   7680  C  CB  . ALA   C  1 116 ? 18.997  -49.793 -75.992  1.00 17.09  ? 417  ALA   C CB  1 
ATOM   7681  N  N   . SER   C  1 117 ? 19.638  -48.437 -72.683  1.00 21.82  ? 418  SER   C N   1 
ATOM   7682  C  CA  A SER   C  1 117 ? 19.864  -48.824 -71.297  0.67 19.72  ? 418  SER   C CA  1 
ATOM   7683  C  CA  B SER   C  1 117 ? 19.845  -48.808 -71.286  0.33 20.24  ? 418  SER   C CA  1 
ATOM   7684  C  C   . SER   C  1 117 ? 18.934  -49.948 -70.850  1.00 22.51  ? 418  SER   C C   1 
ATOM   7685  O  O   . SER   C  1 117 ? 19.273  -50.696 -69.931  1.00 31.45  ? 418  SER   C O   1 
ATOM   7686  C  CB  A SER   C  1 117 ? 19.687  -47.615 -70.403  0.67 21.02  ? 418  SER   C CB  1 
ATOM   7687  C  CB  B SER   C  1 117 ? 19.621  -47.598 -70.389  0.33 20.94  ? 418  SER   C CB  1 
ATOM   7688  O  OG  A SER   C  1 117 ? 18.372  -47.123 -70.536  0.67 21.05  ? 418  SER   C OG  1 
ATOM   7689  O  OG  B SER   C  1 117 ? 20.473  -46.530 -70.749  0.33 21.52  ? 418  SER   C OG  1 
ATOM   7690  N  N   . ARG   C  1 118 ? 17.780  -50.098 -71.488  1.00 24.21  ? 419  ARG   C N   1 
ATOM   7691  C  CA  . ARG   C  1 118 ? 16.811  -51.108 -71.086  1.00 21.38  ? 419  ARG   C CA  1 
ATOM   7692  C  C   . ARG   C  1 118 ? 17.003  -52.454 -71.752  1.00 26.01  ? 419  ARG   C C   1 
ATOM   7693  O  O   . ARG   C  1 118 ? 16.202  -53.365 -71.499  1.00 24.63  ? 419  ARG   C O   1 
ATOM   7694  C  CB  . ARG   C  1 118 ? 15.395  -50.617 -71.370  1.00 19.71  ? 419  ARG   C CB  1 
ATOM   7695  C  CG  . ARG   C  1 118 ? 15.018  -49.428 -70.501  1.00 23.52  ? 419  ARG   C CG  1 
ATOM   7696  C  CD  . ARG   C  1 118 ? 13.618  -49.032 -70.793  1.00 19.47  ? 419  ARG   C CD  1 
ATOM   7697  N  NE  . ARG   C  1 118 ? 13.093  -48.132 -69.785  1.00 25.56  ? 419  ARG   C NE  1 
ATOM   7698  C  CZ  . ARG   C  1 118 ? 11.911  -47.552 -69.904  1.00 28.85  ? 419  ARG   C CZ  1 
ATOM   7699  N  NH1 . ARG   C  1 118 ? 11.193  -47.793 -70.986  1.00 32.92  ? 419  ARG   C NH1 1 
ATOM   7700  N  NH2 . ARG   C  1 118 ? 11.459  -46.740 -68.965  1.00 24.18  ? 419  ARG   C NH2 1 
ATOM   7701  N  N   . CYS   C  1 119 ? 18.019  -52.617 -72.593  1.00 22.16  ? 420  CYS   C N   1 
ATOM   7702  C  CA  . CYS   C  1 119 ? 18.169  -53.840 -73.374  1.00 19.63  ? 420  CYS   C CA  1 
ATOM   7703  C  C   . CYS   C  1 119 ? 19.239  -54.734 -72.758  1.00 19.75  ? 420  CYS   C C   1 
ATOM   7704  O  O   . CYS   C  1 119 ? 20.412  -54.353 -72.683  1.00 19.23  ? 420  CYS   C O   1 
ATOM   7705  C  CB  . CYS   C  1 119 ? 18.502  -53.529 -74.833  1.00 18.61  ? 420  CYS   C CB  1 
ATOM   7706  S  SG  . CYS   C  1 119 ? 18.900  -55.000 -75.825  1.00 21.68  ? 420  CYS   C SG  1 
ATOM   7707  N  N   . VAL   C  1 120 ? 18.828  -55.934 -72.339  1.00 17.38  ? 421  VAL   C N   1 
ATOM   7708  C  CA  . VAL   C  1 120 ? 19.753  -56.924 -71.799  1.00 23.22  ? 421  VAL   C CA  1 
ATOM   7709  C  C   . VAL   C  1 120 ? 20.538  -57.657 -72.876  1.00 25.95  ? 421  VAL   C C   1 
ATOM   7710  O  O   . VAL   C  1 120 ? 21.514  -58.347 -72.557  1.00 22.61  ? 421  VAL   C O   1 
ATOM   7711  C  CB  . VAL   C  1 120 ? 18.955  -57.903 -70.911  1.00 27.26  ? 421  VAL   C CB  1 
ATOM   7712  C  CG1 . VAL   C  1 120 ? 18.057  -58.814 -71.749  1.00 23.69  ? 421  VAL   C CG1 1 
ATOM   7713  C  CG2 . VAL   C  1 120 ? 19.887  -58.711 -70.002  1.00 27.56  ? 421  VAL   C CG2 1 
ATOM   7714  N  N   . GLY   C  1 121 ? 20.187  -57.497 -74.152  1.00 27.98  ? 422  GLY   C N   1 
ATOM   7715  C  CA  . GLY   C  1 121 ? 20.868  -58.275 -75.165  1.00 21.88  ? 422  GLY   C CA  1 
ATOM   7716  C  C   . GLY   C  1 121 ? 22.009  -57.565 -75.865  1.00 24.78  ? 422  GLY   C C   1 
ATOM   7717  O  O   . GLY   C  1 121 ? 22.410  -57.964 -76.961  1.00 24.81  ? 422  GLY   C O   1 
ATOM   7718  N  N   . ARG   C  1 122 ? 22.568  -56.534 -75.237  1.00 21.97  ? 423  ARG   C N   1 
ATOM   7719  C  CA  . ARG   C  1 122 ? 23.479  -55.630 -75.923  1.00 21.39  ? 423  ARG   C CA  1 
ATOM   7720  C  C   . ARG   C  1 122 ? 24.872  -56.198 -76.146  1.00 27.59  ? 423  ARG   C C   1 
ATOM   7721  O  O   . ARG   C  1 122 ? 25.661  -55.581 -76.876  1.00 26.56  ? 423  ARG   C O   1 
ATOM   7722  C  CB  . ARG   C  1 122 ? 23.585  -54.320 -75.151  1.00 18.16  ? 423  ARG   C CB  1 
ATOM   7723  C  CG  . ARG   C  1 122 ? 22.468  -53.343 -75.452  1.00 18.68  ? 423  ARG   C CG  1 
ATOM   7724  C  CD  . ARG   C  1 122 ? 22.679  -52.095 -74.645  1.00 20.44  ? 423  ARG   C CD  1 
ATOM   7725  N  NE  . ARG   C  1 122 ? 22.243  -52.265 -73.250  1.00 24.00  ? 423  ARG   C NE  1 
ATOM   7726  C  CZ  . ARG   C  1 122 ? 22.500  -51.379 -72.293  1.00 22.40  ? 423  ARG   C CZ  1 
ATOM   7727  N  NH1 . ARG   C  1 122 ? 23.209  -50.282 -72.581  1.00 18.24  ? 423  ARG   C NH1 1 
ATOM   7728  N  NH2 . ARG   C  1 122 ? 22.039  -51.573 -71.064  1.00 21.19  ? 423  ARG   C NH2 1 
ATOM   7729  N  N   . ILE   C  1 123 ? 25.203  -57.355 -75.569  1.00 19.06  ? 424  ILE   C N   1 
ATOM   7730  C  CA  . ILE   C  1 123 ? 26.491  -57.945 -75.895  1.00 20.06  ? 424  ILE   C CA  1 
ATOM   7731  C  C   . ILE   C  1 123 ? 26.603  -58.182 -77.403  1.00 24.65  ? 424  ILE   C C   1 
ATOM   7732  O  O   . ILE   C  1 123 ? 27.706  -58.295 -77.938  1.00 29.55  ? 424  ILE   C O   1 
ATOM   7733  C  CB  . ILE   C  1 123 ? 26.706  -59.245 -75.103  1.00 21.32  ? 424  ILE   C CB  1 
ATOM   7734  C  CG1 . ILE   C  1 123 ? 28.165  -59.694 -75.211  1.00 23.62  ? 424  ILE   C CG1 1 
ATOM   7735  C  CG2 . ILE   C  1 123 ? 25.784  -60.344 -75.603  1.00 19.91  ? 424  ILE   C CG2 1 
ATOM   7736  C  CD1 . ILE   C  1 123 ? 28.532  -60.816 -74.278  1.00 31.69  ? 424  ILE   C CD1 1 
ATOM   7737  N  N   . GLN   C  1 124 ? 25.476  -58.233 -78.098  1.00 25.01  ? 425  GLN   C N   1 
ATOM   7738  C  CA  . GLN   C  1 124 ? 25.393  -58.451 -79.536  1.00 25.90  ? 425  GLN   C CA  1 
ATOM   7739  C  C   . GLN   C  1 124 ? 25.418  -57.160 -80.350  1.00 29.82  ? 425  GLN   C C   1 
ATOM   7740  O  O   . GLN   C  1 124 ? 25.293  -57.227 -81.580  1.00 26.00  ? 425  GLN   C O   1 
ATOM   7741  C  CB  . GLN   C  1 124 ? 24.107  -59.225 -79.846  1.00 25.24  ? 425  GLN   C CB  1 
ATOM   7742  C  CG  . GLN   C  1 124 ? 24.112  -60.665 -79.334  1.00 33.87  ? 425  GLN   C CG  1 
ATOM   7743  C  CD  . GLN   C  1 124 ? 24.940  -61.574 -80.231  1.00 41.35  ? 425  GLN   C CD  1 
ATOM   7744  O  OE1 . GLN   C  1 124 ? 25.113  -61.293 -81.421  1.00 41.69  ? 425  GLN   C OE1 1 
ATOM   7745  N  NE2 . GLN   C  1 124 ? 25.451  -62.660 -79.670  1.00 41.41  ? 425  GLN   C NE2 1 
ATOM   7746  N  N   . TRP   C  1 125 ? 25.600  -55.999 -79.706  1.00 24.56  ? 426  TRP   C N   1 
ATOM   7747  C  CA  . TRP   C  1 125 ? 25.260  -54.733 -80.354  1.00 25.13  ? 426  TRP   C CA  1 
ATOM   7748  C  C   . TRP   C  1 125 ? 26.049  -54.504 -81.645  1.00 30.19  ? 426  TRP   C C   1 
ATOM   7749  O  O   . TRP   C  1 125 ? 25.511  -53.984 -82.626  1.00 29.43  ? 426  TRP   C O   1 
ATOM   7750  C  CB  . TRP   C  1 125 ? 25.469  -53.572 -79.387  1.00 23.80  ? 426  TRP   C CB  1 
ATOM   7751  C  CG  . TRP   C  1 125 ? 26.913  -53.250 -79.151  1.00 26.73  ? 426  TRP   C CG  1 
ATOM   7752  C  CD1 . TRP   C  1 125 ? 27.723  -53.765 -78.177  1.00 30.33  ? 426  TRP   C CD1 1 
ATOM   7753  C  CD2 . TRP   C  1 125 ? 27.718  -52.340 -79.902  1.00 21.57  ? 426  TRP   C CD2 1 
ATOM   7754  N  NE1 . TRP   C  1 125 ? 28.982  -53.237 -78.282  1.00 24.74  ? 426  TRP   C NE1 1 
ATOM   7755  C  CE2 . TRP   C  1 125 ? 29.009  -52.362 -79.336  1.00 23.47  ? 426  TRP   C CE2 1 
ATOM   7756  C  CE3 . TRP   C  1 125 ? 27.475  -51.516 -81.010  1.00 22.27  ? 426  TRP   C CE3 1 
ATOM   7757  C  CZ2 . TRP   C  1 125 ? 30.050  -51.586 -79.826  1.00 21.71  ? 426  TRP   C CZ2 1 
ATOM   7758  C  CZ3 . TRP   C  1 125 ? 28.509  -50.759 -81.502  1.00 23.37  ? 426  TRP   C CZ3 1 
ATOM   7759  C  CH2 . TRP   C  1 125 ? 29.783  -50.796 -80.912  1.00 27.99  ? 426  TRP   C CH2 1 
ATOM   7760  N  N   . SER   C  1 126 ? 27.315  -54.880 -81.681  1.00 25.96  ? 427  SER   C N   1 
ATOM   7761  C  CA  . SER   C  1 126 ? 28.080  -54.540 -82.870  1.00 26.74  ? 427  SER   C CA  1 
ATOM   7762  C  C   . SER   C  1 126 ? 27.814  -55.495 -84.020  1.00 34.24  ? 427  SER   C C   1 
ATOM   7763  O  O   . SER   C  1 126 ? 28.327  -55.277 -85.118  1.00 30.27  ? 427  SER   C O   1 
ATOM   7764  C  CB  . SER   C  1 126 ? 29.567  -54.534 -82.550  1.00 25.11  ? 427  SER   C CB  1 
ATOM   7765  O  OG  . SER   C  1 126 ? 29.970  -55.849 -82.205  1.00 32.31  ? 427  SER   C OG  1 
ATOM   7766  N  N   . LYS   C  1 127 ? 27.048  -56.552 -83.788  1.00 31.24  ? 428  LYS   C N   1 
ATOM   7767  C  CA  . LYS   C  1 127 ? 26.672  -57.485 -84.836  1.00 37.58  ? 428  LYS   C CA  1 
ATOM   7768  C  C   . LYS   C  1 127 ? 25.215  -57.214 -85.201  1.00 50.52  ? 428  LYS   C C   1 
ATOM   7769  O  O   . LYS   C  1 127 ? 24.289  -57.929 -84.822  1.00 63.78  ? 428  LYS   C O   1 
ATOM   7770  C  CB  . LYS   C  1 127 ? 26.902  -58.918 -84.365  1.00 43.35  ? 428  LYS   C CB  1 
ATOM   7771  C  CG  . LYS   C  1 127 ? 26.646  -59.984 -85.412  1.00 60.05  ? 428  LYS   C CG  1 
ATOM   7772  C  CD  . LYS   C  1 127 ? 26.801  -61.380 -84.830  1.00 65.69  ? 428  LYS   C CD  1 
ATOM   7773  C  CE  . LYS   C  1 127 ? 26.565  -62.449 -85.883  1.00 68.47  ? 428  LYS   C CE  1 
ATOM   7774  N  NZ  . LYS   C  1 127 ? 26.552  -63.812 -85.280  1.00 68.36  ? 428  LYS   C NZ  1 
ATOM   7775  N  N   . LEU   C  1 128 ? 25.025  -56.108 -85.904  1.00 39.99  ? 429  LEU   C N   1 
ATOM   7776  C  CA  . LEU   C  1 128 ? 23.703  -55.628 -86.278  1.00 27.48  ? 429  LEU   C CA  1 
ATOM   7777  C  C   . LEU   C  1 128 ? 23.689  -55.422 -87.782  1.00 24.50  ? 429  LEU   C C   1 
ATOM   7778  O  O   . LEU   C  1 128 ? 24.560  -54.739 -88.325  1.00 26.73  ? 429  LEU   C O   1 
ATOM   7779  C  CB  . LEU   C  1 128 ? 23.356  -54.321 -85.552  1.00 21.01  ? 429  LEU   C CB  1 
ATOM   7780  C  CG  . LEU   C  1 128 ? 22.052  -53.625 -85.975  1.00 22.39  ? 429  LEU   C CG  1 
ATOM   7781  C  CD1 . LEU   C  1 128 ? 20.812  -54.470 -85.644  1.00 21.12  ? 429  LEU   C CD1 1 
ATOM   7782  C  CD2 . LEU   C  1 128 ? 21.932  -52.204 -85.379  1.00 18.36  ? 429  LEU   C CD2 1 
ATOM   7783  N  N   . GLN   C  1 129 ? 22.731  -56.032 -88.454  1.00 20.89  ? 430  GLN   C N   1 
ATOM   7784  C  CA  . GLN   C  1 129 ? 22.609  -55.872 -89.890  1.00 23.59  ? 430  GLN   C CA  1 
ATOM   7785  C  C   . GLN   C  1 129 ? 21.718  -54.666 -90.125  1.00 26.50  ? 430  GLN   C C   1 
ATOM   7786  O  O   . GLN   C  1 129 ? 20.565  -54.643 -89.681  1.00 31.40  ? 430  GLN   C O   1 
ATOM   7787  C  CB  . GLN   C  1 129 ? 22.029  -57.126 -90.539  1.00 28.19  ? 430  GLN   C CB  1 
ATOM   7788  C  CG  . GLN   C  1 129 ? 22.049  -57.070 -92.065  1.00 30.11  ? 430  GLN   C CG  1 
ATOM   7789  C  CD  . GLN   C  1 129 ? 23.449  -56.879 -92.599  1.00 40.25  ? 430  GLN   C CD  1 
ATOM   7790  O  OE1 . GLN   C  1 129 ? 23.680  -56.026 -93.453  1.00 52.70  ? 430  GLN   C OE1 1 
ATOM   7791  N  NE2 . GLN   C  1 129 ? 24.398  -57.668 -92.089  1.00 36.94  ? 430  GLN   C NE2 1 
ATOM   7792  N  N   . VAL   C  1 130 ? 22.267  -53.650 -90.767  1.00 22.69  ? 431  VAL   C N   1 
ATOM   7793  C  CA  . VAL   C  1 130 ? 21.578  -52.384 -90.965  1.00 22.40  ? 431  VAL   C CA  1 
ATOM   7794  C  C   . VAL   C  1 130 ? 21.110  -52.338 -92.411  1.00 29.02  ? 431  VAL   C C   1 
ATOM   7795  O  O   . VAL   C  1 130 ? 21.921  -52.407 -93.339  1.00 28.94  ? 431  VAL   C O   1 
ATOM   7796  C  CB  . VAL   C  1 130 ? 22.496  -51.203 -90.626  1.00 23.94  ? 431  VAL   C CB  1 
ATOM   7797  C  CG1 . VAL   C  1 130 ? 21.838  -49.880 -90.978  1.00 20.63  ? 431  VAL   C CG1 1 
ATOM   7798  C  CG2 . VAL   C  1 130 ? 22.878  -51.267 -89.115  1.00 27.18  ? 431  VAL   C CG2 1 
ATOM   7799  N  N   . PHE   C  1 131 ? 19.800  -52.254 -92.600  1.00 26.02  ? 432  PHE   C N   1 
ATOM   7800  C  CA  . PHE   C  1 131 ? 19.206  -52.142 -93.926  1.00 23.57  ? 432  PHE   C CA  1 
ATOM   7801  C  C   . PHE   C  1 131 ? 18.829  -50.689 -94.142  1.00 21.96  ? 432  PHE   C C   1 
ATOM   7802  O  O   . PHE   C  1 131 ? 17.997  -50.137 -93.418  1.00 27.25  ? 432  PHE   C O   1 
ATOM   7803  C  CB  . PHE   C  1 131 ? 18.006  -53.071 -94.051  1.00 22.14  ? 432  PHE   C CB  1 
ATOM   7804  C  CG  . PHE   C  1 131 ? 18.393  -54.510 -94.056  1.00 23.57  ? 432  PHE   C CG  1 
ATOM   7805  C  CD1 . PHE   C  1 131 ? 19.199  -55.011 -95.074  1.00 29.50  ? 432  PHE   C CD1 1 
ATOM   7806  C  CD2 . PHE   C  1 131 ? 17.987  -55.358 -93.041  1.00 27.72  ? 432  PHE   C CD2 1 
ATOM   7807  C  CE1 . PHE   C  1 131 ? 19.577  -56.338 -95.085  1.00 30.14  ? 432  PHE   C CE1 1 
ATOM   7808  C  CE2 . PHE   C  1 131 ? 18.354  -56.688 -93.049  1.00 25.83  ? 432  PHE   C CE2 1 
ATOM   7809  C  CZ  . PHE   C  1 131 ? 19.152  -57.180 -94.075  1.00 28.56  ? 432  PHE   C CZ  1 
ATOM   7810  N  N   . ASP   C  1 132 ? 19.490  -50.062 -95.100  1.00 23.73  ? 433  ASP   C N   1 
ATOM   7811  C  CA  . ASP   C  1 132 ? 19.271  -48.659 -95.397  1.00 19.82  ? 433  ASP   C CA  1 
ATOM   7812  C  C   . ASP   C  1 132 ? 18.067  -48.577 -96.306  1.00 24.91  ? 433  ASP   C C   1 
ATOM   7813  O  O   . ASP   C  1 132 ? 18.148  -48.949 -97.473  1.00 28.28  ? 433  ASP   C O   1 
ATOM   7814  C  CB  . ASP   C  1 132 ? 20.501  -48.068 -96.072  1.00 27.96  ? 433  ASP   C CB  1 
ATOM   7815  C  CG  . ASP   C  1 132 ? 20.379  -46.582 -96.310  1.00 28.65  ? 433  ASP   C CG  1 
ATOM   7816  O  OD1 . ASP   C  1 132 ? 21.391  -45.981 -96.721  1.00 30.16  ? 433  ASP   C OD1 1 
ATOM   7817  O  OD2 . ASP   C  1 132 ? 19.292  -46.006 -96.072  1.00 31.72  ? 433  ASP   C OD2 1 
ATOM   7818  N  N   . ALA   C  1 133 ? 16.947  -48.100 -95.791  1.00 24.53  ? 434  ALA   C N   1 
ATOM   7819  C  CA  . ALA   C  1 133 ? 15.767  -47.919 -96.624  1.00 27.38  ? 434  ALA   C CA  1 
ATOM   7820  C  C   . ALA   C  1 133 ? 15.420  -46.444 -96.799  1.00 26.36  ? 434  ALA   C C   1 
ATOM   7821  O  O   . ALA   C  1 133 ? 14.251  -46.090 -96.970  1.00 22.56  ? 434  ALA   C O   1 
ATOM   7822  C  CB  . ALA   C  1 133 ? 14.584  -48.692 -96.048  1.00 25.98  ? 434  ALA   C CB  1 
ATOM   7823  N  N   . ARG   C  1 134 ? 16.427  -45.570 -96.781  1.00 21.36  ? 435  ARG   C N   1 
ATOM   7824  C  CA  . ARG   C  1 134 ? 16.126  -44.149 -96.886  1.00 27.42  ? 435  ARG   C CA  1 
ATOM   7825  C  C   . ARG   C  1 134 ? 15.709  -43.721 -98.292  1.00 25.80  ? 435  ARG   C C   1 
ATOM   7826  O  O   . ARG   C  1 134 ? 15.260  -42.586 -98.456  1.00 25.66  ? 435  ARG   C O   1 
ATOM   7827  C  CB  . ARG   C  1 134 ? 17.320  -43.338 -96.403  1.00 23.50  ? 435  ARG   C CB  1 
ATOM   7828  C  CG  . ARG   C  1 134 ? 17.521  -43.424 -94.888  1.00 25.18  ? 435  ARG   C CG  1 
ATOM   7829  C  CD  . ARG   C  1 134 ? 18.784  -42.717 -94.511  1.00 27.15  ? 435  ARG   C CD  1 
ATOM   7830  N  NE  . ARG   C  1 134 ? 19.924  -43.371 -95.137  1.00 22.44  ? 435  ARG   C NE  1 
ATOM   7831  C  CZ  . ARG   C  1 134 ? 21.133  -42.840 -95.197  1.00 25.05  ? 435  ARG   C CZ  1 
ATOM   7832  N  NH1 . ARG   C  1 134 ? 21.359  -41.640 -94.676  1.00 24.97  ? 435  ARG   C NH1 1 
ATOM   7833  N  NH2 . ARG   C  1 134 ? 22.109  -43.506 -95.790  1.00 24.25  ? 435  ARG   C NH2 1 
ATOM   7834  N  N   . ASP   C  1 135 ? 15.797  -44.594 -99.292  1.00 21.40  ? 436  ASP   C N   1 
ATOM   7835  C  CA  . ASP   C  1 135 ? 15.266  -44.283 -100.621 1.00 22.95  ? 436  ASP   C CA  1 
ATOM   7836  C  C   . ASP   C  1 135 ? 13.792  -44.650 -100.774 1.00 25.29  ? 436  ASP   C C   1 
ATOM   7837  O  O   . ASP   C  1 135 ? 13.214  -44.427 -101.841 1.00 25.68  ? 436  ASP   C O   1 
ATOM   7838  C  CB  . ASP   C  1 135 ? 16.082  -44.991 -101.708 1.00 24.47  ? 436  ASP   C CB  1 
ATOM   7839  C  CG  . ASP   C  1 135 ? 15.995  -46.496 -101.623 1.00 34.29  ? 436  ASP   C CG  1 
ATOM   7840  O  OD1 . ASP   C  1 135 ? 16.587  -47.174 -102.492 1.00 36.24  ? 436  ASP   C OD1 1 
ATOM   7841  O  OD2 . ASP   C  1 135 ? 15.352  -47.010 -100.682 1.00 43.43  ? 436  ASP   C OD2 1 
ATOM   7842  N  N   . CYS   C  1 136 ? 13.179  -45.214 -99.744  1.00 29.57  ? 437  CYS   C N   1 
ATOM   7843  C  CA  . CYS   C  1 136 ? 11.791  -45.642 -99.831  1.00 27.01  ? 437  CYS   C CA  1 
ATOM   7844  C  C   . CYS   C  1 136 ? 10.865  -44.433 -99.919  1.00 25.97  ? 437  CYS   C C   1 
ATOM   7845  O  O   . CYS   C  1 136 ? 11.114  -43.397 -99.298  1.00 28.52  ? 437  CYS   C O   1 
ATOM   7846  C  CB  . CYS   C  1 136 ? 11.453  -46.493 -98.602  1.00 27.78  ? 437  CYS   C CB  1 
ATOM   7847  S  SG  . CYS   C  1 136 ? 9.905   -47.374 -98.638  1.00 28.22  ? 437  CYS   C SG  1 
ATOM   7848  N  N   . THR   C  1 137 ? 9.784   -44.560 -100.695 1.00 24.97  ? 438  THR   C N   1 
ATOM   7849  C  CA  . THR   C  1 137 ? 8.852   -43.453 -100.878 1.00 24.23  ? 438  THR   C CA  1 
ATOM   7850  C  C   . THR   C  1 137 ? 7.401   -43.839 -100.687 1.00 22.68  ? 438  THR   C C   1 
ATOM   7851  O  O   . THR   C  1 137 ? 6.558   -42.940 -100.605 1.00 26.64  ? 438  THR   C O   1 
ATOM   7852  C  CB  . THR   C  1 137 ? 8.974   -42.834 -102.282 1.00 24.35  ? 438  THR   C CB  1 
ATOM   7853  O  OG1 . THR   C  1 137 ? 8.484   -43.767 -103.253 1.00 28.69  ? 438  THR   C OG1 1 
ATOM   7854  C  CG2 . THR   C  1 137 ? 10.428  -42.437 -102.615 1.00 26.55  ? 438  THR   C CG2 1 
ATOM   7855  N  N   . THR   C  1 138 ? 7.073   -45.129 -100.644 1.00 24.09  ? 439  THR   C N   1 
ATOM   7856  C  CA  . THR   C  1 138 ? 5.682   -45.558 -100.565 1.00 25.18  ? 439  THR   C CA  1 
ATOM   7857  C  C   . THR   C  1 138 ? 5.529   -46.686 -99.556  1.00 24.65  ? 439  THR   C C   1 
ATOM   7858  O  O   . THR   C  1 138 ? 6.491   -47.374 -99.193  1.00 23.80  ? 439  THR   C O   1 
ATOM   7859  C  CB  . THR   C  1 138 ? 5.144   -46.045 -101.914 1.00 28.06  ? 439  THR   C CB  1 
ATOM   7860  O  OG1 . THR   C  1 138 ? 5.830   -47.247 -102.278 1.00 24.58  ? 439  THR   C OG1 1 
ATOM   7861  C  CG2 . THR   C  1 138 ? 5.345   -44.993 -102.999 1.00 24.72  ? 439  THR   C CG2 1 
ATOM   7862  N  N   . ALA   C  1 139 ? 4.279   -46.892 -99.134  1.00 25.34  ? 440  ALA   C N   1 
ATOM   7863  C  CA  . ALA   C  1 139 ? 3.983   -47.997 -98.230  1.00 24.97  ? 440  ALA   C CA  1 
ATOM   7864  C  C   . ALA   C  1 139 ? 4.292   -49.343 -98.865  1.00 27.82  ? 440  ALA   C C   1 
ATOM   7865  O  O   . ALA   C  1 139 ? 4.712   -50.273 -98.164  1.00 25.42  ? 440  ALA   C O   1 
ATOM   7866  C  CB  . ALA   C  1 139 ? 2.521   -47.953 -97.795  1.00 27.19  ? 440  ALA   C CB  1 
ATOM   7867  N  N   . HIS   C  1 140 ? 4.076   -49.480 -100.182 1.00 27.78  ? 441  HIS   C N   1 
ATOM   7868  C  CA  . HIS   C  1 140 ? 4.450   -50.728 -100.838 1.00 22.72  ? 441  HIS   C CA  1 
ATOM   7869  C  C   . HIS   C  1 140 ? 5.940   -50.973 -100.701 1.00 21.72  ? 441  HIS   C C   1 
ATOM   7870  O  O   . HIS   C  1 140 ? 6.369   -52.104 -100.436 1.00 21.46  ? 441  HIS   C O   1 
ATOM   7871  C  CB  . HIS   C  1 140 ? 4.069   -50.708 -102.321 1.00 27.04  ? 441  HIS   C CB  1 
ATOM   7872  C  CG  . HIS   C  1 140 ? 2.645   -51.071 -102.580 1.00 29.50  ? 441  HIS   C CG  1 
ATOM   7873  N  ND1 . HIS   C  1 140 ? 1.607   -50.177 -102.413 1.00 33.81  ? 441  HIS   C ND1 1 
ATOM   7874  C  CD2 . HIS   C  1 140 ? 2.082   -52.231 -102.989 1.00 29.81  ? 441  HIS   C CD2 1 
ATOM   7875  C  CE1 . HIS   C  1 140 ? 0.466   -50.772 -102.709 1.00 31.15  ? 441  HIS   C CE1 1 
ATOM   7876  N  NE2 . HIS   C  1 140 ? 0.726   -52.020 -103.059 1.00 33.41  ? 441  HIS   C NE2 1 
ATOM   7877  N  N   . GLY   C  1 141 ? 6.740   -49.911 -100.876 1.00 22.25  ? 442  GLY   C N   1 
ATOM   7878  C  CA  . GLY   C  1 141 ? 8.172   -50.042 -100.715 1.00 21.34  ? 442  GLY   C CA  1 
ATOM   7879  C  C   . GLY   C  1 141 ? 8.556   -50.452 -99.308  1.00 25.01  ? 442  GLY   C C   1 
ATOM   7880  O  O   . GLY   C  1 141 ? 9.430   -51.301 -99.122  1.00 24.59  ? 442  GLY   C O   1 
ATOM   7881  N  N   . MET   C  1 142 ? 7.915   -49.847 -98.298  1.00 23.35  ? 443  MET   C N   1 
ATOM   7882  C  CA  . MET   C  1 142 ? 8.173   -50.234 -96.908  1.00 20.00  ? 443  MET   C CA  1 
ATOM   7883  C  C   . MET   C  1 142 ? 7.859   -51.705 -96.680  1.00 19.88  ? 443  MET   C C   1 
ATOM   7884  O  O   . MET   C  1 142 ? 8.628   -52.420 -96.029  1.00 20.98  ? 443  MET   C O   1 
ATOM   7885  C  CB  . MET   C  1 142 ? 7.334   -49.382 -95.946  1.00 22.55  ? 443  MET   C CB  1 
ATOM   7886  C  CG  . MET   C  1 142 ? 7.578   -47.905 -96.033  1.00 23.74  ? 443  MET   C CG  1 
ATOM   7887  S  SD  . MET   C  1 142 ? 6.439   -46.969 -95.010  1.00 26.61  ? 443  MET   C SD  1 
ATOM   7888  C  CE  . MET   C  1 142 ? 6.979   -47.424 -93.333  1.00 19.63  ? 443  MET   C CE  1 
ATOM   7889  N  N   . PHE   C  1 143 ? 6.720   -52.166 -97.199  1.00 20.25  ? 444  PHE   C N   1 
ATOM   7890  C  CA  . PHE   C  1 143 ? 6.364   -53.578 -97.095  1.00 20.28  ? 444  PHE   C CA  1 
ATOM   7891  C  C   . PHE   C  1 143 ? 7.462   -54.463 -97.660  1.00 30.29  ? 444  PHE   C C   1 
ATOM   7892  O  O   . PHE   C  1 143 ? 7.861   -55.458 -97.037  1.00 25.51  ? 444  PHE   C O   1 
ATOM   7893  C  CB  . PHE   C  1 143 ? 5.046   -53.830 -97.824  1.00 20.85  ? 444  PHE   C CB  1 
ATOM   7894  C  CG  . PHE   C  1 143 ? 4.686   -55.277 -97.942  1.00 30.35  ? 444  PHE   C CG  1 
ATOM   7895  C  CD1 . PHE   C  1 143 ? 4.750   -55.927 -99.165  1.00 28.22  ? 444  PHE   C CD1 1 
ATOM   7896  C  CD2 . PHE   C  1 143 ? 4.288   -55.993 -96.830  1.00 27.59  ? 444  PHE   C CD2 1 
ATOM   7897  C  CE1 . PHE   C  1 143 ? 4.414   -57.266 -99.272  1.00 31.54  ? 444  PHE   C CE1 1 
ATOM   7898  C  CE2 . PHE   C  1 143 ? 3.938   -57.329 -96.931  1.00 25.11  ? 444  PHE   C CE2 1 
ATOM   7899  C  CZ  . PHE   C  1 143 ? 4.005   -57.966 -98.149  1.00 28.72  ? 444  PHE   C CZ  1 
ATOM   7900  N  N   . ASN   C  1 144 ? 7.957   -54.117 -98.851  1.00 29.29  ? 445  ASN   C N   1 
ATOM   7901  C  CA  . ASN   C  1 144 ? 9.034   -54.887 -99.449  1.00 25.16  ? 445  ASN   C CA  1 
ATOM   7902  C  C   . ASN   C  1 144 ? 10.266  -54.880 -98.553  1.00 25.35  ? 445  ASN   C C   1 
ATOM   7903  O  O   . ASN   C  1 144 ? 10.846  -55.932 -98.266  1.00 22.27  ? 445  ASN   C O   1 
ATOM   7904  C  CB  . ASN   C  1 144 ? 9.347   -54.321 -100.839 1.00 31.66  ? 445  ASN   C CB  1 
ATOM   7905  C  CG  . ASN   C  1 144 ? 10.368  -55.139 -101.583 1.00 36.63  ? 445  ASN   C CG  1 
ATOM   7906  O  OD1 . ASN   C  1 144 ? 11.420  -54.636 -101.970 1.00 44.53  ? 445  ASN   C OD1 1 
ATOM   7907  N  ND2 . ASN   C  1 144 ? 10.065  -56.411 -101.791 1.00 31.46  ? 445  ASN   C ND2 1 
ATOM   7908  N  N   . TYR   C  1 145 ? 10.668  -53.699 -98.078  1.00 22.68  ? 446  TYR   C N   1 
ATOM   7909  C  CA  . TYR   C  1 145 ? 11.802  -53.624 -97.165  1.00 28.18  ? 446  TYR   C CA  1 
ATOM   7910  C  C   . TYR   C  1 145 ? 11.559  -54.458 -95.906  1.00 23.57  ? 446  TYR   C C   1 
ATOM   7911  O  O   . TYR   C  1 145 ? 12.466  -55.135 -95.410  1.00 22.73  ? 446  TYR   C O   1 
ATOM   7912  C  CB  . TYR   C  1 145 ? 12.075  -52.168 -96.795  1.00 21.64  ? 446  TYR   C CB  1 
ATOM   7913  C  CG  . TYR   C  1 145 ? 13.086  -51.479 -97.679  1.00 24.56  ? 446  TYR   C CG  1 
ATOM   7914  C  CD1 . TYR   C  1 145 ? 12.708  -50.461 -98.550  1.00 23.59  ? 446  TYR   C CD1 1 
ATOM   7915  C  CD2 . TYR   C  1 145 ? 14.427  -51.851 -97.645  1.00 22.90  ? 446  TYR   C CD2 1 
ATOM   7916  C  CE1 . TYR   C  1 145 ? 13.651  -49.825 -99.363  1.00 22.80  ? 446  TYR   C CE1 1 
ATOM   7917  C  CE2 . TYR   C  1 145 ? 15.359  -51.227 -98.433  1.00 25.02  ? 446  TYR   C CE2 1 
ATOM   7918  C  CZ  . TYR   C  1 145 ? 14.973  -50.221 -99.294  1.00 22.58  ? 446  TYR   C CZ  1 
ATOM   7919  O  OH  . TYR   C  1 145 ? 15.936  -49.617 -100.069 1.00 28.56  ? 446  TYR   C OH  1 
ATOM   7920  N  N   . ILE   C  1 146 ? 10.335  -54.449 -95.394  1.00 19.76  ? 447  ILE   C N   1 
ATOM   7921  C  CA  . ILE   C  1 146 ? 10.078  -55.154 -94.144  1.00 23.98  ? 447  ILE   C CA  1 
ATOM   7922  C  C   . ILE   C  1 146 ? 10.089  -56.657 -94.369  1.00 26.09  ? 447  ILE   C C   1 
ATOM   7923  O  O   . ILE   C  1 146 ? 10.637  -57.415 -93.554  1.00 19.79  ? 447  ILE   C O   1 
ATOM   7924  C  CB  . ILE   C  1 146 ? 8.762   -54.668 -93.513  1.00 25.66  ? 447  ILE   C CB  1 
ATOM   7925  C  CG1 . ILE   C  1 146 ? 8.955   -53.245 -92.988  1.00 27.36  ? 447  ILE   C CG1 1 
ATOM   7926  C  CG2 . ILE   C  1 146 ? 8.335   -55.594 -92.354  1.00 25.63  ? 447  ILE   C CG2 1 
ATOM   7927  C  CD1 . ILE   C  1 146 ? 7.672   -52.570 -92.550  1.00 29.53  ? 447  ILE   C CD1 1 
ATOM   7928  N  N   . CYS   C  1 147 ? 9.514   -57.117 -95.492  1.00 27.51  ? 448  CYS   C N   1 
ATOM   7929  C  CA  . CYS   C  1 147 ? 9.562   -58.544 -95.800  1.00 19.77  ? 448  CYS   C CA  1 
ATOM   7930  C  C   . CYS   C  1 147 ? 10.997  -59.028 -95.887  1.00 21.96  ? 448  CYS   C C   1 
ATOM   7931  O  O   . CYS   C  1 147 ? 11.345  -60.080 -95.336  1.00 22.99  ? 448  CYS   C O   1 
ATOM   7932  C  CB  . CYS   C  1 147 ? 8.833   -58.841 -97.119  1.00 23.51  ? 448  CYS   C CB  1 
ATOM   7933  S  SG  . CYS   C  1 147 ? 7.063   -58.746 -96.971  1.00 31.16  ? 448  CYS   C SG  1 
ATOM   7934  N  N   . ASN   C  1 148 ? 11.837  -58.282 -96.605  1.00 19.81  ? 449  ASN   C N   1 
ATOM   7935  C  CA  . ASN   C  1 148 ? 13.243  -58.653 -96.727  1.00 24.59  ? 449  ASN   C CA  1 
ATOM   7936  C  C   . ASN   C  1 148 ? 13.915  -58.692 -95.360  1.00 22.55  ? 449  ASN   C C   1 
ATOM   7937  O  O   . ASN   C  1 148 ? 14.737  -59.574 -95.087  1.00 24.50  ? 449  ASN   C O   1 
ATOM   7938  C  CB  . ASN   C  1 148 ? 13.959  -57.666 -97.647  1.00 20.07  ? 449  ASN   C CB  1 
ATOM   7939  C  CG  . ASN   C  1 148 ? 13.478  -57.763 -99.101  1.00 27.79  ? 449  ASN   C CG  1 
ATOM   7940  O  OD1 . ASN   C  1 148 ? 12.811  -58.720 -99.479  1.00 26.80  ? 449  ASN   C OD1 1 
ATOM   7941  N  ND2 . ASN   C  1 148 ? 13.841  -56.776 -99.916  1.00 20.77  ? 449  ASN   C ND2 1 
ATOM   7942  N  N   . HIS   C  1 149 ? 13.607  -57.712 -94.515  1.00 21.73  ? 450  HIS   C N   1 
ATOM   7943  C  CA  . HIS   C  1 149 ? 14.100  -57.700 -93.140  1.00 21.39  ? 450  HIS   C CA  1 
ATOM   7944  C  C   . HIS   C  1 149 ? 13.645  -58.947 -92.401  1.00 21.77  ? 450  HIS   C C   1 
ATOM   7945  O  O   . HIS   C  1 149 ? 14.453  -59.646 -91.779  1.00 20.13  ? 450  HIS   C O   1 
ATOM   7946  C  CB  . HIS   C  1 149 ? 13.611  -56.426 -92.441  1.00 19.25  ? 450  HIS   C CB  1 
ATOM   7947  C  CG  . HIS   C  1 149 ? 13.975  -56.325 -90.981  1.00 25.26  ? 450  HIS   C CG  1 
ATOM   7948  N  ND1 . HIS   C  1 149 ? 14.389  -55.143 -90.406  1.00 22.75  ? 450  HIS   C ND1 1 
ATOM   7949  C  CD2 . HIS   C  1 149 ? 13.956  -57.240 -89.980  1.00 22.34  ? 450  HIS   C CD2 1 
ATOM   7950  C  CE1 . HIS   C  1 149 ? 14.624  -55.338 -89.119  1.00 21.15  ? 450  HIS   C CE1 1 
ATOM   7951  N  NE2 . HIS   C  1 149 ? 14.376  -56.604 -88.838  1.00 20.98  ? 450  HIS   C NE2 1 
ATOM   7952  N  N   . VAL   C  1 150 ? 12.349  -59.245 -92.458  1.00 20.31  ? 451  VAL   C N   1 
ATOM   7953  C  CA  . VAL   C  1 150 ? 11.839  -60.397 -91.727  1.00 18.89  ? 451  VAL   C CA  1 
ATOM   7954  C  C   . VAL   C  1 150 ? 12.509  -61.669 -92.206  1.00 22.13  ? 451  VAL   C C   1 
ATOM   7955  O  O   . VAL   C  1 150 ? 12.932  -62.508 -91.405  1.00 22.19  ? 451  VAL   C O   1 
ATOM   7956  C  CB  . VAL   C  1 150 ? 10.315  -60.483 -91.859  1.00 22.98  ? 451  VAL   C CB  1 
ATOM   7957  C  CG1 . VAL   C  1 150 ? 9.858   -61.835 -91.393  1.00 20.78  ? 451  VAL   C CG1 1 
ATOM   7958  C  CG2 . VAL   C  1 150 ? 9.689   -59.391 -91.004  1.00 20.32  ? 451  VAL   C CG2 1 
ATOM   7959  N  N   . LYS   C  1 151 ? 12.639  -61.826 -93.525  1.00 19.86  ? 452  LYS   C N   1 
ATOM   7960  C  CA  . LYS   C  1 151 ? 13.249  -63.036 -94.058  1.00 20.27  ? 452  LYS   C CA  1 
ATOM   7961  C  C   . LYS   C  1 151 ? 14.707  -63.148 -93.643  1.00 21.79  ? 452  LYS   C C   1 
ATOM   7962  O  O   . LYS   C  1 151 ? 15.175  -64.230 -93.273  1.00 23.59  ? 452  LYS   C O   1 
ATOM   7963  C  CB  . LYS   C  1 151 ? 13.136  -63.031 -95.591  1.00 20.64  ? 452  LYS   C CB  1 
ATOM   7964  C  CG  . LYS   C  1 151 ? 13.517  -64.348 -96.227  1.00 21.29  ? 452  LYS   C CG  1 
ATOM   7965  C  CD  . LYS   C  1 151 ? 13.193  -64.240 -97.715  1.00 25.25  ? 452  LYS   C CD  1 
ATOM   7966  C  CE  . LYS   C  1 151 ? 13.319  -65.578 -98.412  1.00 33.33  ? 452  LYS   C CE  1 
ATOM   7967  N  NZ  . LYS   C  1 151 ? 12.794  -65.516 -99.820  1.00 30.73  ? 452  LYS   C NZ  1 
ATOM   7968  N  N   . TYR   C  1 152 ? 15.444  -62.039 -93.722  1.00 20.92  ? 453  TYR   C N   1 
ATOM   7969  C  CA  . TYR   C  1 152 ? 16.852  -62.057 -93.362  1.00 24.15  ? 453  TYR   C CA  1 
ATOM   7970  C  C   . TYR   C  1 152 ? 17.027  -62.338 -91.878  1.00 22.80  ? 453  TYR   C C   1 
ATOM   7971  O  O   . TYR   C  1 152 ? 17.884  -63.134 -91.475  1.00 24.73  ? 453  TYR   C O   1 
ATOM   7972  C  CB  . TYR   C  1 152 ? 17.501  -60.718 -93.707  1.00 25.05  ? 453  TYR   C CB  1 
ATOM   7973  C  CG  . TYR   C  1 152 ? 18.911  -60.636 -93.168  1.00 27.30  ? 453  TYR   C CG  1 
ATOM   7974  C  CD1 . TYR   C  1 152 ? 19.984  -61.040 -93.949  1.00 36.67  ? 453  TYR   C CD1 1 
ATOM   7975  C  CD2 . TYR   C  1 152 ? 19.171  -60.182 -91.872  1.00 27.40  ? 453  TYR   C CD2 1 
ATOM   7976  C  CE1 . TYR   C  1 152 ? 21.268  -60.987 -93.473  1.00 35.20  ? 453  TYR   C CE1 1 
ATOM   7977  C  CE2 . TYR   C  1 152 ? 20.461  -60.141 -91.381  1.00 26.71  ? 453  TYR   C CE2 1 
ATOM   7978  C  CZ  . TYR   C  1 152 ? 21.502  -60.544 -92.196  1.00 27.96  ? 453  TYR   C CZ  1 
ATOM   7979  O  OH  . TYR   C  1 152 ? 22.797  -60.507 -91.754  1.00 35.83  ? 453  TYR   C OH  1 
ATOM   7980  N  N   . ALA   C  1 153 ? 16.264  -61.632 -91.055  1.00 21.17  ? 454  ALA   C N   1 
ATOM   7981  C  CA  . ALA   C  1 153 ? 16.401  -61.759 -89.614  1.00 22.61  ? 454  ALA   C CA  1 
ATOM   7982  C  C   . ALA   C  1 153 ? 16.017  -63.159 -89.161  1.00 27.07  ? 454  ALA   C C   1 
ATOM   7983  O  O   . ALA   C  1 153 ? 16.702  -63.758 -88.328  1.00 28.99  ? 454  ALA   C O   1 
ATOM   7984  C  CB  . ALA   C  1 153 ? 15.536  -60.696 -88.934  1.00 18.46  ? 454  ALA   C CB  1 
ATOM   7985  N  N   . THR   C  1 154 ? 14.944  -63.710 -89.736  1.00 25.98  ? 455  THR   C N   1 
ATOM   7986  C  CA  . THR   C  1 154 ? 14.455  -65.019 -89.320  1.00 19.81  ? 455  THR   C CA  1 
ATOM   7987  C  C   . THR   C  1 154 ? 15.432  -66.126 -89.698  1.00 24.64  ? 455  THR   C C   1 
ATOM   7988  O  O   . THR   C  1 154 ? 15.751  -66.992 -88.871  1.00 28.97  ? 455  THR   C O   1 
ATOM   7989  C  CB  . THR   C  1 154 ? 13.085  -65.266 -89.931  1.00 24.44  ? 455  THR   C CB  1 
ATOM   7990  O  OG1 . THR   C  1 154 ? 12.167  -64.284 -89.422  1.00 24.53  ? 455  THR   C OG1 1 
ATOM   7991  C  CG2 . THR   C  1 154 ? 12.603  -66.674 -89.596  1.00 20.47  ? 455  THR   C CG2 1 
ATOM   7992  N  N   . ASN   C  1 155 ? 15.892  -66.140 -90.957  1.00 24.13  ? 456  ASN   C N   1 
ATOM   7993  C  CA  . ASN   C  1 155 ? 16.988  -67.022 -91.365  1.00 21.36  ? 456  ASN   C CA  1 
ATOM   7994  C  C   . ASN   C  1 155 ? 16.698  -68.480 -90.995  1.00 27.72  ? 456  ASN   C C   1 
ATOM   7995  O  O   . ASN   C  1 155 ? 17.573  -69.213 -90.520  1.00 28.42  ? 456  ASN   C O   1 
ATOM   7996  C  CB  . ASN   C  1 155 ? 18.304  -66.539 -90.744  1.00 21.24  ? 456  ASN   C CB  1 
ATOM   7997  C  CG  . ASN   C  1 155 ? 19.523  -67.251 -91.316  1.00 31.82  ? 456  ASN   C CG  1 
ATOM   7998  O  OD1 . ASN   C  1 155 ? 19.531  -67.650 -92.468  1.00 31.00  ? 456  ASN   C OD1 1 
ATOM   7999  N  ND2 . ASN   C  1 155 ? 20.548  -67.420 -90.499  1.00 28.81  ? 456  ASN   C ND2 1 
ATOM   8000  N  N   . LYS   C  1 156 ? 15.437  -68.891 -91.168  1.00 22.94  ? 457  LYS   C N   1 
ATOM   8001  C  CA  . LYS   C  1 156 ? 15.002  -70.274 -90.914  1.00 22.61  ? 457  LYS   C CA  1 
ATOM   8002  C  C   . LYS   C  1 156 ? 15.226  -70.705 -89.460  1.00 23.12  ? 457  LYS   C C   1 
ATOM   8003  O  O   . LYS   C  1 156 ? 15.499  -71.876 -89.187  1.00 29.56  ? 457  LYS   C O   1 
ATOM   8004  C  CB  . LYS   C  1 156 ? 15.689  -71.256 -91.868  1.00 31.56  ? 457  LYS   C CB  1 
ATOM   8005  C  CG  . LYS   C  1 156 ? 15.360  -70.974 -93.333  1.00 33.61  ? 457  LYS   C CG  1 
ATOM   8006  C  CD  . LYS   C  1 156 ? 15.620  -72.178 -94.216  1.00 53.16  ? 457  LYS   C CD  1 
ATOM   8007  C  CE  . LYS   C  1 156 ? 17.107  -72.461 -94.349  1.00 65.66  ? 457  LYS   C CE  1 
ATOM   8008  N  NZ  . LYS   C  1 156 ? 17.521  -72.654 -95.777  1.00 73.39  ? 457  LYS   C NZ  1 
ATOM   8009  N  N   . GLY   C  1 157 ? 15.107  -69.773 -88.522  1.00 26.57  ? 458  GLY   C N   1 
ATOM   8010  C  CA  . GLY   C  1 157 ? 15.272  -70.050 -87.114  1.00 25.82  ? 458  GLY   C CA  1 
ATOM   8011  C  C   . GLY   C  1 157 ? 16.608  -69.638 -86.543  1.00 30.07  ? 458  GLY   C C   1 
ATOM   8012  O  O   . GLY   C  1 157 ? 16.727  -69.490 -85.318  1.00 25.48  ? 458  GLY   C O   1 
ATOM   8013  N  N   . ASN   C  1 158 ? 17.621  -69.454 -87.388  1.00 25.12  ? 459  ASN   C N   1 
ATOM   8014  C  CA  . ASN   C  1 158 ? 18.929  -69.015 -86.911  1.00 28.73  ? 459  ASN   C CA  1 
ATOM   8015  C  C   . ASN   C  1 158 ? 18.927  -67.492 -86.933  1.00 26.91  ? 459  ASN   C C   1 
ATOM   8016  O  O   . ASN   C  1 158 ? 19.496  -66.850 -87.816  1.00 27.96  ? 459  ASN   C O   1 
ATOM   8017  C  CB  . ASN   C  1 158 ? 20.041  -69.606 -87.765  1.00 33.04  ? 459  ASN   C CB  1 
ATOM   8018  C  CG  . ASN   C  1 158 ? 21.412  -69.325 -87.197  1.00 40.31  ? 459  ASN   C CG  1 
ATOM   8019  O  OD1 . ASN   C  1 158 ? 21.541  -68.839 -86.076  1.00 40.87  ? 459  ASN   C OD1 1 
ATOM   8020  N  ND2 . ASN   C  1 158 ? 22.447  -69.630 -87.969  1.00 37.86  ? 459  ASN   C ND2 1 
ATOM   8021  N  N   . LEU   C  1 159 ? 18.273  -66.909 -85.928  1.00 22.91  ? 460  LEU   C N   1 
ATOM   8022  C  CA  . LEU   C  1 159 ? 17.913  -65.497 -86.003  1.00 23.64  ? 460  LEU   C CA  1 
ATOM   8023  C  C   . LEU   C  1 159 ? 19.147  -64.607 -86.012  1.00 25.25  ? 460  LEU   C C   1 
ATOM   8024  O  O   . LEU   C  1 159 ? 20.167  -64.902 -85.384  1.00 23.55  ? 460  LEU   C O   1 
ATOM   8025  C  CB  . LEU   C  1 159 ? 17.004  -65.085 -84.839  1.00 23.60  ? 460  LEU   C CB  1 
ATOM   8026  C  CG  . LEU   C  1 159 ? 15.805  -66.004 -84.575  1.00 36.16  ? 460  LEU   C CG  1 
ATOM   8027  C  CD1 . LEU   C  1 159 ? 14.869  -65.401 -83.522  1.00 33.56  ? 460  LEU   C CD1 1 
ATOM   8028  C  CD2 . LEU   C  1 159 ? 15.045  -66.321 -85.850  1.00 28.93  ? 460  LEU   C CD2 1 
ATOM   8029  N  N   . ARG   C  1 160 ? 19.026  -63.496 -86.728  1.00 22.59  ? 461  ARG   C N   1 
ATOM   8030  C  CA  . ARG   C  1 160 ? 20.083  -62.511 -86.886  1.00 20.05  ? 461  ARG   C CA  1 
ATOM   8031  C  C   . ARG   C  1 160 ? 19.496  -61.140 -86.595  1.00 24.65  ? 461  ARG   C C   1 
ATOM   8032  O  O   . ARG   C  1 160 ? 18.412  -60.806 -87.086  1.00 23.06  ? 461  ARG   C O   1 
ATOM   8033  C  CB  . ARG   C  1 160 ? 20.654  -62.536 -88.311  1.00 21.84  ? 461  ARG   C CB  1 
ATOM   8034  C  CG  . ARG   C  1 160 ? 21.199  -63.874 -88.718  1.00 24.93  ? 461  ARG   C CG  1 
ATOM   8035  C  CD  . ARG   C  1 160 ? 21.784  -63.814 -90.107  1.00 27.54  ? 461  ARG   C CD  1 
ATOM   8036  N  NE  . ARG   C  1 160 ? 20.754  -63.849 -91.134  1.00 29.12  ? 461  ARG   C NE  1 
ATOM   8037  C  CZ  . ARG   C  1 160 ? 20.997  -64.220 -92.389  1.00 35.49  ? 461  ARG   C CZ  1 
ATOM   8038  N  NH1 . ARG   C  1 160 ? 22.226  -64.569 -92.739  1.00 27.56  ? 461  ARG   C NH1 1 
ATOM   8039  N  NH2 . ARG   C  1 160 ? 20.021  -64.251 -93.286  1.00 23.89  ? 461  ARG   C NH2 1 
ATOM   8040  N  N   . SER   C  1 161 ? 20.214  -60.343 -85.820  1.00 23.80  ? 462  SER   C N   1 
ATOM   8041  C  CA  A SER   C  1 161 ? 19.708  -59.027 -85.465  0.50 23.60  ? 462  SER   C CA  1 
ATOM   8042  C  CA  B SER   C  1 161 ? 19.709  -59.028 -85.465  0.50 23.59  ? 462  SER   C CA  1 
ATOM   8043  C  C   . SER   C  1 161 ? 19.769  -58.104 -86.674  1.00 23.90  ? 462  SER   C C   1 
ATOM   8044  O  O   . SER   C  1 161 ? 20.725  -58.127 -87.451  1.00 23.69  ? 462  SER   C O   1 
ATOM   8045  C  CB  A SER   C  1 161 ? 20.507  -58.436 -84.302  0.50 21.91  ? 462  SER   C CB  1 
ATOM   8046  C  CB  B SER   C  1 161 ? 20.513  -58.449 -84.303  0.50 21.90  ? 462  SER   C CB  1 
ATOM   8047  O  OG  A SER   C  1 161 ? 21.807  -58.041 -84.707  0.50 21.24  ? 462  SER   C OG  1 
ATOM   8048  O  OG  B SER   C  1 161 ? 20.483  -59.330 -83.195  0.50 23.21  ? 462  SER   C OG  1 
ATOM   8049  N  N   . ALA   C  1 162 ? 18.733  -57.299 -86.842  1.00 18.46  ? 463  ALA   C N   1 
ATOM   8050  C  CA  . ALA   C  1 162 ? 18.720  -56.425 -88.000  1.00 20.84  ? 463  ALA   C CA  1 
ATOM   8051  C  C   . ALA   C  1 162 ? 17.837  -55.235 -87.685  1.00 24.65  ? 463  ALA   C C   1 
ATOM   8052  O  O   . ALA   C  1 162 ? 16.981  -55.291 -86.800  1.00 23.35  ? 463  ALA   C O   1 
ATOM   8053  C  CB  . ALA   C  1 162 ? 18.237  -57.171 -89.262  1.00 18.92  ? 463  ALA   C CB  1 
ATOM   8054  N  N   . ILE   C  1 163 ? 18.079  -54.150 -88.412  1.00 26.64  ? 464  ILE   C N   1 
ATOM   8055  C  CA  . ILE   C  1 163 ? 17.251  -52.957 -88.349  1.00 26.07  ? 464  ILE   C CA  1 
ATOM   8056  C  C   . ILE   C  1 163 ? 17.082  -52.449 -89.775  1.00 22.97  ? 464  ILE   C C   1 
ATOM   8057  O  O   . ILE   C  1 163 ? 18.004  -52.534 -90.589  1.00 21.75  ? 464  ILE   C O   1 
ATOM   8058  C  CB  . ILE   C  1 163 ? 17.879  -51.876 -87.433  1.00 17.48  ? 464  ILE   C CB  1 
ATOM   8059  C  CG1 . ILE   C  1 163 ? 16.951  -50.660 -87.334  1.00 18.01  ? 464  ILE   C CG1 1 
ATOM   8060  C  CG2 . ILE   C  1 163 ? 19.263  -51.493 -87.946  1.00 18.73  ? 464  ILE   C CG2 1 
ATOM   8061  C  CD1 . ILE   C  1 163 ? 17.268  -49.729 -86.162  1.00 21.88  ? 464  ILE   C CD1 1 
ATOM   8062  N  N   . THR   C  1 164 ? 15.901  -51.935 -90.080  1.00 22.69  ? 465  THR   C N   1 
ATOM   8063  C  CA  . THR   C  1 164 ? 15.635  -51.303 -91.363  1.00 26.96  ? 465  THR   C CA  1 
ATOM   8064  C  C   . THR   C  1 164 ? 15.272  -49.857 -91.098  1.00 28.45  ? 465  THR   C C   1 
ATOM   8065  O  O   . THR   C  1 164 ? 14.364  -49.575 -90.307  1.00 25.51  ? 465  THR   C O   1 
ATOM   8066  C  CB  . THR   C  1 164 ? 14.518  -52.015 -92.114  1.00 26.69  ? 465  THR   C CB  1 
ATOM   8067  O  OG1 . THR   C  1 164 ? 14.963  -53.337 -92.442  1.00 29.53  ? 465  THR   C OG1 1 
ATOM   8068  C  CG2 . THR   C  1 164 ? 14.149  -51.237 -93.411  1.00 24.69  ? 465  THR   C CG2 1 
ATOM   8069  N  N   . ILE   C  1 165 ? 15.989  -48.942 -91.737  1.00 20.48  ? 466  ILE   C N   1 
ATOM   8070  C  CA  . ILE   C  1 165 ? 15.852  -47.530 -91.426  1.00 21.06  ? 466  ILE   C CA  1 
ATOM   8071  C  C   . ILE   C  1 165 ? 15.229  -46.820 -92.624  1.00 27.77  ? 466  ILE   C C   1 
ATOM   8072  O  O   . ILE   C  1 165 ? 15.828  -46.733 -93.707  1.00 22.56  ? 466  ILE   C O   1 
ATOM   8073  C  CB  . ILE   C  1 165 ? 17.192  -46.915 -91.017  1.00 25.42  ? 466  ILE   C CB  1 
ATOM   8074  C  CG1 . ILE   C  1 165 ? 17.711  -47.607 -89.738  1.00 25.21  ? 466  ILE   C CG1 1 
ATOM   8075  C  CG2 . ILE   C  1 165 ? 17.004  -45.441 -90.773  1.00 25.77  ? 466  ILE   C CG2 1 
ATOM   8076  C  CD1 . ILE   C  1 165 ? 19.197  -47.370 -89.467  1.00 21.37  ? 466  ILE   C CD1 1 
ATOM   8077  N  N   . PHE   C  1 166 ? 14.022  -46.315 -92.415  1.00 28.26  ? 467  PHE   C N   1 
ATOM   8078  C  CA  . PHE   C  1 166 ? 13.253  -45.595 -93.417  1.00 23.94  ? 467  PHE   C CA  1 
ATOM   8079  C  C   . PHE   C  1 166 ? 13.594  -44.116 -93.368  1.00 27.50  ? 467  PHE   C C   1 
ATOM   8080  O  O   . PHE   C  1 166 ? 14.315  -43.674 -92.475  1.00 24.86  ? 467  PHE   C O   1 
ATOM   8081  C  CB  . PHE   C  1 166 ? 11.775  -45.868 -93.182  1.00 19.18  ? 467  PHE   C CB  1 
ATOM   8082  C  CG  . PHE   C  1 166 ? 11.380  -47.265 -93.558  1.00 23.98  ? 467  PHE   C CG  1 
ATOM   8083  C  CD1 . PHE   C  1 166 ? 11.417  -47.666 -94.886  1.00 20.87  ? 467  PHE   C CD1 1 
ATOM   8084  C  CD2 . PHE   C  1 166 ? 11.025  -48.192 -92.585  1.00 30.99  ? 467  PHE   C CD2 1 
ATOM   8085  C  CE1 . PHE   C  1 166 ? 11.072  -48.945 -95.252  1.00 26.03  ? 467  PHE   C CE1 1 
ATOM   8086  C  CE2 . PHE   C  1 166 ? 10.671  -49.481 -92.937  1.00 30.40  ? 467  PHE   C CE2 1 
ATOM   8087  C  CZ  . PHE   C  1 166 ? 10.701  -49.868 -94.287  1.00 21.26  ? 467  PHE   C CZ  1 
ATOM   8088  N  N   . PRO   C  1 167 ? 13.130  -43.315 -94.338  1.00 26.12  ? 468  PRO   C N   1 
ATOM   8089  C  CA  . PRO   C  1 167 ? 13.584  -41.918 -94.398  1.00 25.83  ? 468  PRO   C CA  1 
ATOM   8090  C  C   . PRO   C  1 167 ? 13.292  -41.155 -93.112  1.00 24.37  ? 468  PRO   C C   1 
ATOM   8091  O  O   . PRO   C  1 167 ? 12.296  -41.394 -92.429  1.00 24.54  ? 468  PRO   C O   1 
ATOM   8092  C  CB  . PRO   C  1 167 ? 12.805  -41.333 -95.585  1.00 23.21  ? 468  PRO   C CB  1 
ATOM   8093  C  CG  . PRO   C  1 167 ? 12.540  -42.497 -96.459  1.00 20.98  ? 468  PRO   C CG  1 
ATOM   8094  C  CD  . PRO   C  1 167 ? 12.282  -43.651 -95.500  1.00 22.42  ? 468  PRO   C CD  1 
ATOM   8095  N  N   . GLN   C  1 168 ? 14.183  -40.224 -92.795  1.00 25.00  ? 469  GLN   C N   1 
ATOM   8096  C  CA  . GLN   C  1 168 ? 14.065  -39.457 -91.572  1.00 24.80  ? 469  GLN   C CA  1 
ATOM   8097  C  C   . GLN   C  1 168 ? 12.905  -38.473 -91.656  1.00 29.47  ? 469  GLN   C C   1 
ATOM   8098  O  O   . GLN   C  1 168 ? 12.358  -38.182 -92.723  1.00 25.17  ? 469  GLN   C O   1 
ATOM   8099  C  CB  . GLN   C  1 168 ? 15.348  -38.689 -91.296  1.00 25.96  ? 469  GLN   C CB  1 
ATOM   8100  C  CG  . GLN   C  1 168 ? 15.650  -37.673 -92.367  1.00 29.35  ? 469  GLN   C CG  1 
ATOM   8101  C  CD  . GLN   C  1 168 ? 17.128  -37.430 -92.505  1.00 29.65  ? 469  GLN   C CD  1 
ATOM   8102  O  OE1 . GLN   C  1 168 ? 17.917  -38.368 -92.552  1.00 32.92  ? 469  GLN   C OE1 1 
ATOM   8103  N  NE2 . GLN   C  1 168 ? 17.517  -36.169 -92.563  1.00 28.43  ? 469  GLN   C NE2 1 
ATOM   8104  N  N   . ARG   C  1 169 ? 12.544  -37.953 -90.495  1.00 25.58  ? 470  ARG   C N   1 
ATOM   8105  C  CA  . ARG   C  1 169 ? 11.511  -36.941 -90.406  1.00 25.81  ? 470  ARG   C CA  1 
ATOM   8106  C  C   . ARG   C  1 169 ? 11.978  -35.672 -91.092  1.00 28.10  ? 470  ARG   C C   1 
ATOM   8107  O  O   . ARG   C  1 169 ? 13.166  -35.332 -91.071  1.00 27.89  ? 470  ARG   C O   1 
ATOM   8108  C  CB  . ARG   C  1 169 ? 11.199  -36.681 -88.929  1.00 28.05  ? 470  ARG   C CB  1 
ATOM   8109  C  CG  . ARG   C  1 169 ? 10.192  -35.589 -88.663  1.00 36.77  ? 470  ARG   C CG  1 
ATOM   8110  C  CD  . ARG   C  1 169 ? 9.736   -35.635 -87.203  1.00 39.64  ? 470  ARG   C CD  1 
ATOM   8111  N  NE  . ARG   C  1 169 ? 9.026   -36.873 -86.909  1.00 34.56  ? 470  ARG   C NE  1 
ATOM   8112  C  CZ  . ARG   C  1 169 ? 8.698   -37.265 -85.685  1.00 52.53  ? 470  ARG   C CZ  1 
ATOM   8113  N  NH1 . ARG   C  1 169 ? 9.027   -36.508 -84.645  1.00 54.75  ? 470  ARG   C NH1 1 
ATOM   8114  N  NH2 . ARG   C  1 169 ? 8.049   -38.412 -85.496  1.00 48.15  ? 470  ARG   C NH2 1 
ATOM   8115  N  N   . THR   C  1 170 ? 11.042  -34.969 -91.726  1.00 28.11  ? 471  THR   C N   1 
ATOM   8116  C  CA  . THR   C  1 170 ? 11.400  -33.712 -92.371  1.00 28.53  ? 471  THR   C CA  1 
ATOM   8117  C  C   . THR   C  1 170 ? 10.712  -32.566 -91.655  1.00 33.26  ? 471  THR   C C   1 
ATOM   8118  O  O   . THR   C  1 170 ? 11.300  -31.964 -90.745  1.00 36.24  ? 471  THR   C O   1 
ATOM   8119  C  CB  . THR   C  1 170 ? 11.045  -33.738 -93.865  1.00 31.19  ? 471  THR   C CB  1 
ATOM   8120  O  OG1 . THR   C  1 170 ? 9.677   -34.125 -94.043  1.00 39.32  ? 471  THR   C OG1 1 
ATOM   8121  C  CG2 . THR   C  1 170 ? 11.939  -34.736 -94.588  1.00 29.97  ? 471  THR   C CG2 1 
ATOM   8122  N  N   . ASP   C  1 171 ? 9.487   -32.225 -92.043  1.00 37.78  ? 472  ASP   C N   1 
ATOM   8123  C  CA  . ASP   C  1 171 ? 8.717   -31.201 -91.358  1.00 38.26  ? 472  ASP   C CA  1 
ATOM   8124  C  C   . ASP   C  1 171 ? 7.794   -31.784 -90.297  1.00 45.21  ? 472  ASP   C C   1 
ATOM   8125  O  O   . ASP   C  1 171 ? 7.005   -31.044 -89.704  1.00 51.60  ? 472  ASP   C O   1 
ATOM   8126  C  CB  . ASP   C  1 171 ? 7.904   -30.381 -92.359  1.00 41.70  ? 472  ASP   C CB  1 
ATOM   8127  C  CG  . ASP   C  1 171 ? 7.005   -31.249 -93.235  1.00 51.04  ? 472  ASP   C CG  1 
ATOM   8128  O  OD1 . ASP   C  1 171 ? 6.781   -32.433 -92.898  1.00 49.89  ? 472  ASP   C OD1 1 
ATOM   8129  O  OD2 . ASP   C  1 171 ? 6.521   -30.741 -94.270  1.00 55.50  ? 472  ASP   C OD2 1 
ATOM   8130  N  N   . GLY   C  1 172 ? 7.866   -33.093 -90.050  1.00 42.85  ? 473  GLY   C N   1 
ATOM   8131  C  CA  . GLY   C  1 172 ? 6.935   -33.759 -89.164  1.00 33.37  ? 473  GLY   C CA  1 
ATOM   8132  C  C   . GLY   C  1 172 ? 5.587   -34.078 -89.774  1.00 36.32  ? 473  GLY   C C   1 
ATOM   8133  O  O   . GLY   C  1 172 ? 4.763   -34.730 -89.117  1.00 39.95  ? 473  GLY   C O   1 
ATOM   8134  N  N   . LYS   C  1 173 ? 5.329   -33.643 -91.006  1.00 41.38  ? 474  LYS   C N   1 
ATOM   8135  C  CA  . LYS   C  1 173 ? 4.067   -33.896 -91.688  1.00 36.34  ? 474  LYS   C CA  1 
ATOM   8136  C  C   . LYS   C  1 173 ? 4.222   -34.930 -92.793  1.00 34.84  ? 474  LYS   C C   1 
ATOM   8137  O  O   . LYS   C  1 173 ? 3.256   -35.231 -93.503  1.00 39.11  ? 474  LYS   C O   1 
ATOM   8138  C  CB  . LYS   C  1 173 ? 3.501   -32.578 -92.225  1.00 40.00  ? 474  LYS   C CB  1 
ATOM   8139  C  CG  . LYS   C  1 173 ? 3.225   -31.565 -91.106  1.00 51.24  ? 474  LYS   C CG  1 
ATOM   8140  C  CD  . LYS   C  1 173 ? 3.144   -30.122 -91.607  1.00 58.85  ? 474  LYS   C CD  1 
ATOM   8141  C  CE  . LYS   C  1 173 ? 3.211   -29.131 -90.434  1.00 65.20  ? 474  LYS   C CE  1 
ATOM   8142  N  NZ  . LYS   C  1 173 ? 2.949   -27.698 -90.815  1.00 61.66  ? 474  LYS   C NZ  1 
ATOM   8143  N  N   . HIS   C  1 174 ? 5.416   -35.495 -92.935  1.00 32.41  ? 475  HIS   C N   1 
ATOM   8144  C  CA  . HIS   C  1 174 ? 5.690   -36.532 -93.915  1.00 30.61  ? 475  HIS   C CA  1 
ATOM   8145  C  C   . HIS   C  1 174 ? 6.385   -37.715 -93.266  1.00 31.90  ? 475  HIS   C C   1 
ATOM   8146  O  O   . HIS   C  1 174 ? 7.243   -38.351 -93.883  1.00 31.23  ? 475  HIS   C O   1 
ATOM   8147  C  CB  . HIS   C  1 174 ? 6.525   -35.974 -95.060  1.00 34.41  ? 475  HIS   C CB  1 
ATOM   8148  C  CG  . HIS   C  1 174 ? 5.861   -34.838 -95.767  1.00 42.17  ? 475  HIS   C CG  1 
ATOM   8149  N  ND1 . HIS   C  1 174 ? 5.791   -33.569 -95.233  1.00 46.60  ? 475  HIS   C ND1 1 
ATOM   8150  C  CD2 . HIS   C  1 174 ? 5.216   -34.785 -96.953  1.00 41.42  ? 475  HIS   C CD2 1 
ATOM   8151  C  CE1 . HIS   C  1 174 ? 5.146   -32.778 -96.072  1.00 45.93  ? 475  HIS   C CE1 1 
ATOM   8152  N  NE2 . HIS   C  1 174 ? 4.785   -33.491 -97.123  1.00 44.23  ? 475  HIS   C NE2 1 
ATOM   8153  N  N   . ASP   C  1 175 ? 6.033   -38.004 -92.009  1.00 31.58  ? 476  ASP   C N   1 
ATOM   8154  C  CA  . ASP   C  1 175 ? 6.665   -39.086 -91.268  1.00 32.04  ? 476  ASP   C CA  1 
ATOM   8155  C  C   . ASP   C  1 175 ? 6.432   -40.426 -91.947  1.00 29.75  ? 476  ASP   C C   1 
ATOM   8156  O  O   . ASP   C  1 175 ? 5.335   -40.713 -92.424  1.00 25.38  ? 476  ASP   C O   1 
ATOM   8157  C  CB  . ASP   C  1 175 ? 6.109   -39.170 -89.839  1.00 30.65  ? 476  ASP   C CB  1 
ATOM   8158  C  CG  . ASP   C  1 175 ? 6.649   -38.092 -88.921  1.00 30.32  ? 476  ASP   C CG  1 
ATOM   8159  O  OD1 . ASP   C  1 175 ? 7.417   -37.229 -89.391  1.00 33.28  ? 476  ASP   C OD1 1 
ATOM   8160  O  OD2 . ASP   C  1 175 ? 6.296   -38.125 -87.719  1.00 34.98  ? 476  ASP   C OD2 1 
ATOM   8161  N  N   . PHE   C  1 176 ? 7.471   -41.253 -91.967  1.00 22.70  ? 477  PHE   C N   1 
ATOM   8162  C  CA  . PHE   C  1 176 ? 7.310   -42.683 -92.173  1.00 23.26  ? 477  PHE   C CA  1 
ATOM   8163  C  C   . PHE   C  1 176 ? 7.060   -43.320 -90.812  1.00 28.86  ? 477  PHE   C C   1 
ATOM   8164  O  O   . PHE   C  1 176 ? 7.756   -43.008 -89.842  1.00 26.25  ? 477  PHE   C O   1 
ATOM   8165  C  CB  . PHE   C  1 176 ? 8.551   -43.291 -92.815  1.00 20.19  ? 477  PHE   C CB  1 
ATOM   8166  C  CG  . PHE   C  1 176 ? 8.685   -42.998 -94.287  1.00 20.63  ? 477  PHE   C CG  1 
ATOM   8167  C  CD1 . PHE   C  1 176 ? 9.014   -41.725 -94.724  1.00 21.64  ? 477  PHE   C CD1 1 
ATOM   8168  C  CD2 . PHE   C  1 176 ? 8.509   -44.002 -95.223  1.00 22.03  ? 477  PHE   C CD2 1 
ATOM   8169  C  CE1 . PHE   C  1 176 ? 9.158   -41.450 -96.083  1.00 24.86  ? 477  PHE   C CE1 1 
ATOM   8170  C  CE2 . PHE   C  1 176 ? 8.648   -43.740 -96.586  1.00 29.89  ? 477  PHE   C CE2 1 
ATOM   8171  C  CZ  . PHE   C  1 176 ? 8.967   -42.463 -97.013  1.00 30.63  ? 477  PHE   C CZ  1 
ATOM   8172  N  N   . ARG   C  1 177 ? 6.062   -44.194 -90.739  1.00 20.48  ? 478  ARG   C N   1 
ATOM   8173  C  CA  . ARG   C  1 177 ? 5.728   -44.888 -89.507  1.00 25.72  ? 478  ARG   C CA  1 
ATOM   8174  C  C   . ARG   C  1 177 ? 5.297   -46.297 -89.853  1.00 27.84  ? 478  ARG   C C   1 
ATOM   8175  O  O   . ARG   C  1 177 ? 4.530   -46.502 -90.798  1.00 25.77  ? 478  ARG   C O   1 
ATOM   8176  C  CB  . ARG   C  1 177 ? 4.588   -44.205 -88.734  1.00 28.01  ? 478  ARG   C CB  1 
ATOM   8177  C  CG  . ARG   C  1 177 ? 4.897   -42.822 -88.187  1.00 28.85  ? 478  ARG   C CG  1 
ATOM   8178  C  CD  . ARG   C  1 177 ? 6.002   -42.865 -87.136  1.00 25.44  ? 478  ARG   C CD  1 
ATOM   8179  N  NE  . ARG   C  1 177 ? 5.670   -43.712 -85.994  1.00 28.57  ? 478  ARG   C NE  1 
ATOM   8180  C  CZ  . ARG   C  1 177 ? 5.017   -43.289 -84.912  1.00 34.35  ? 478  ARG   C CZ  1 
ATOM   8181  N  NH1 . ARG   C  1 177 ? 4.586   -42.038 -84.839  1.00 27.93  ? 478  ARG   C NH1 1 
ATOM   8182  N  NH2 . ARG   C  1 177 ? 4.779   -44.124 -83.909  1.00 29.23  ? 478  ARG   C NH2 1 
ATOM   8183  N  N   . VAL   C  1 178 ? 5.792   -47.267 -89.099  1.00 27.13  ? 479  VAL   C N   1 
ATOM   8184  C  CA  . VAL   C  1 178 ? 5.126   -48.555 -89.003  1.00 27.82  ? 479  VAL   C CA  1 
ATOM   8185  C  C   . VAL   C  1 178 ? 4.107   -48.411 -87.887  1.00 26.83  ? 479  VAL   C C   1 
ATOM   8186  O  O   . VAL   C  1 178 ? 4.468   -48.082 -86.755  1.00 27.91  ? 479  VAL   C O   1 
ATOM   8187  C  CB  . VAL   C  1 178 ? 6.120   -49.688 -88.719  1.00 27.47  ? 479  VAL   C CB  1 
ATOM   8188  C  CG1 . VAL   C  1 178 ? 5.383   -51.033 -88.715  1.00 23.81  ? 479  VAL   C CG1 1 
ATOM   8189  C  CG2 . VAL   C  1 178 ? 7.246   -49.687 -89.769  1.00 26.12  ? 479  VAL   C CG2 1 
ATOM   8190  N  N   . TRP   C  1 179 ? 2.828   -48.604 -88.200  1.00 29.85  ? 480  TRP   C N   1 
ATOM   8191  C  CA  . TRP   C  1 179 ? 1.840   -48.431 -87.145  1.00 28.68  ? 480  TRP   C CA  1 
ATOM   8192  C  C   . TRP   C  1 179 ? 1.820   -49.606 -86.174  1.00 27.84  ? 480  TRP   C C   1 
ATOM   8193  O  O   . TRP   C  1 179 ? 1.423   -49.429 -85.020  1.00 29.21  ? 480  TRP   C O   1 
ATOM   8194  C  CB  . TRP   C  1 179 ? 0.459   -48.187 -87.747  1.00 20.72  ? 480  TRP   C CB  1 
ATOM   8195  C  CG  . TRP   C  1 179 ? 0.289   -46.774 -88.277  1.00 21.89  ? 480  TRP   C CG  1 
ATOM   8196  C  CD1 . TRP   C  1 179 ? 1.246   -45.998 -88.863  1.00 22.98  ? 480  TRP   C CD1 1 
ATOM   8197  C  CD2 . TRP   C  1 179 ? -0.908  -45.980 -88.248  1.00 21.94  ? 480  TRP   C CD2 1 
ATOM   8198  N  NE1 . TRP   C  1 179 ? 0.714   -44.782 -89.221  1.00 23.62  ? 480  TRP   C NE1 1 
ATOM   8199  C  CE2 . TRP   C  1 179 ? -0.603  -44.745 -88.841  1.00 22.50  ? 480  TRP   C CE2 1 
ATOM   8200  C  CE3 . TRP   C  1 179 ? -2.204  -46.200 -87.782  1.00 27.70  ? 480  TRP   C CE3 1 
ATOM   8201  C  CZ2 . TRP   C  1 179 ? -1.544  -43.731 -88.974  1.00 24.90  ? 480  TRP   C CZ2 1 
ATOM   8202  C  CZ3 . TRP   C  1 179 ? -3.140  -45.195 -87.914  1.00 25.84  ? 480  TRP   C CZ3 1 
ATOM   8203  C  CH2 . TRP   C  1 179 ? -2.807  -43.978 -88.505  1.00 25.96  ? 480  TRP   C CH2 1 
ATOM   8204  N  N   . ASN   C  1 180 ? 2.248   -50.787 -86.608  1.00 30.20  ? 481  ASN   C N   1 
ATOM   8205  C  CA  . ASN   C  1 180 ? 2.411   -51.921 -85.704  1.00 22.81  ? 481  ASN   C CA  1 
ATOM   8206  C  C   . ASN   C  1 180 ? 3.413   -51.607 -84.607  1.00 26.13  ? 481  ASN   C C   1 
ATOM   8207  O  O   . ASN   C  1 180 ? 4.448   -50.987 -84.857  1.00 22.65  ? 481  ASN   C O   1 
ATOM   8208  C  CB  . ASN   C  1 180 ? 2.904   -53.122 -86.489  1.00 19.05  ? 481  ASN   C CB  1 
ATOM   8209  C  CG  . ASN   C  1 180 ? 2.052   -53.382 -87.692  1.00 22.41  ? 481  ASN   C CG  1 
ATOM   8210  O  OD1 . ASN   C  1 180 ? 2.027   -52.586 -88.633  1.00 20.63  ? 481  ASN   C OD1 1 
ATOM   8211  N  ND2 . ASN   C  1 180 ? 1.309   -54.473 -87.653  1.00 25.09  ? 481  ASN   C ND2 1 
ATOM   8212  N  N   . SER   C  1 181 ? 3.136   -52.085 -83.395  1.00 22.23  ? 482  SER   C N   1 
ATOM   8213  C  CA  . SER   C  1 181 ? 4.117   -51.898 -82.333  1.00 23.92  ? 482  SER   C CA  1 
ATOM   8214  C  C   . SER   C  1 181 ? 5.293   -52.837 -82.547  1.00 22.84  ? 482  SER   C C   1 
ATOM   8215  O  O   . SER   C  1 181 ? 6.451   -52.448 -82.366  1.00 27.91  ? 482  SER   C O   1 
ATOM   8216  C  CB  . SER   C  1 181 ? 3.466   -52.088 -80.954  1.00 22.96  ? 482  SER   C CB  1 
ATOM   8217  O  OG  . SER   C  1 181 ? 2.771   -53.318 -80.861  1.00 22.78  ? 482  SER   C OG  1 
ATOM   8218  N  N   . GLN   C  1 182 ? 5.013   -54.058 -82.995  1.00 18.92  ? 483  GLN   C N   1 
ATOM   8219  C  CA  . GLN   C  1 182 ? 6.026   -54.973 -83.493  1.00 22.06  ? 483  GLN   C CA  1 
ATOM   8220  C  C   . GLN   C  1 182 ? 5.598   -55.484 -84.858  1.00 23.76  ? 483  GLN   C C   1 
ATOM   8221  O  O   . GLN   C  1 182 ? 4.406   -55.546 -85.169  1.00 27.68  ? 483  GLN   C O   1 
ATOM   8222  C  CB  . GLN   C  1 182 ? 6.231   -56.180 -82.586  1.00 23.53  ? 483  GLN   C CB  1 
ATOM   8223  C  CG  . GLN   C  1 182 ? 6.720   -55.901 -81.206  1.00 34.47  ? 483  GLN   C CG  1 
ATOM   8224  C  CD  . GLN   C  1 182 ? 6.366   -57.056 -80.291  1.00 37.65  ? 483  GLN   C CD  1 
ATOM   8225  O  OE1 . GLN   C  1 182 ? 6.755   -58.224 -80.526  1.00 29.73  ? 483  GLN   C OE1 1 
ATOM   8226  N  NE2 . GLN   C  1 182 ? 5.586   -56.754 -79.273  1.00 28.45  ? 483  GLN   C NE2 1 
ATOM   8227  N  N   . LEU   C  1 183 ? 6.579   -55.920 -85.647  1.00 23.77  ? 484  LEU   C N   1 
ATOM   8228  C  CA  . LEU   C  1 183 ? 6.268   -56.359 -87.008  1.00 29.45  ? 484  LEU   C CA  1 
ATOM   8229  C  C   . LEU   C  1 183 ? 5.350   -57.568 -86.992  1.00 31.12  ? 484  LEU   C C   1 
ATOM   8230  O  O   . LEU   C  1 183 ? 4.460   -57.702 -87.841  1.00 26.70  ? 484  LEU   C O   1 
ATOM   8231  C  CB  . LEU   C  1 183 ? 7.546   -56.689 -87.771  1.00 20.53  ? 484  LEU   C CB  1 
ATOM   8232  C  CG  . LEU   C  1 183 ? 8.518   -55.531 -87.977  1.00 17.93  ? 484  LEU   C CG  1 
ATOM   8233  C  CD1 . LEU   C  1 183 ? 9.749   -56.024 -88.730  1.00 19.56  ? 484  LEU   C CD1 1 
ATOM   8234  C  CD2 . LEU   C  1 183 ? 7.827   -54.399 -88.715  1.00 22.29  ? 484  LEU   C CD2 1 
ATOM   8235  N  N   . ILE   C  1 184 ? 5.562   -58.469 -86.046  1.00 18.49  ? 485  ILE   C N   1 
ATOM   8236  C  CA  . ILE   C  1 184 ? 4.761   -59.675 -85.929  1.00 22.12  ? 485  ILE   C CA  1 
ATOM   8237  C  C   . ILE   C  1 184 ? 4.156   -59.653 -84.539  1.00 25.55  ? 485  ILE   C C   1 
ATOM   8238  O  O   . ILE   C  1 184 ? 4.886   -59.692 -83.547  1.00 22.95  ? 485  ILE   C O   1 
ATOM   8239  C  CB  . ILE   C  1 184 ? 5.592   -60.941 -86.145  1.00 22.95  ? 485  ILE   C CB  1 
ATOM   8240  C  CG1 . ILE   C  1 184 ? 6.208   -60.929 -87.548  1.00 29.05  ? 485  ILE   C CG1 1 
ATOM   8241  C  CG2 . ILE   C  1 184 ? 4.732   -62.181 -85.894  1.00 19.48  ? 485  ILE   C CG2 1 
ATOM   8242  C  CD1 . ILE   C  1 184 ? 7.082   -62.106 -87.817  1.00 34.95  ? 485  ILE   C CD1 1 
ATOM   8243  N  N   . ARG   C  1 185 ? 2.834   -59.534 -84.471  1.00 22.34  ? 486  ARG   C N   1 
ATOM   8244  C  CA  . ARG   C  1 185 ? 2.066   -59.703 -83.251  1.00 27.74  ? 486  ARG   C CA  1 
ATOM   8245  C  C   . ARG   C  1 185 ? 0.764   -60.376 -83.627  1.00 30.15  ? 486  ARG   C C   1 
ATOM   8246  O  O   . ARG   C  1 185 ? 0.373   -60.428 -84.799  1.00 27.73  ? 486  ARG   C O   1 
ATOM   8247  C  CB  . ARG   C  1 185 ? 1.743   -58.380 -82.539  1.00 22.23  ? 486  ARG   C CB  1 
ATOM   8248  C  CG  . ARG   C  1 185 ? 2.939   -57.517 -82.208  1.00 23.46  ? 486  ARG   C CG  1 
ATOM   8249  C  CD  . ARG   C  1 185 ? 2.554   -56.499 -81.162  1.00 24.58  ? 486  ARG   C CD  1 
ATOM   8250  N  NE  . ARG   C  1 185 ? 2.278   -57.129 -79.880  1.00 34.55  ? 486  ARG   C NE  1 
ATOM   8251  C  CZ  . ARG   C  1 185 ? 2.064   -56.452 -78.753  1.00 38.76  ? 486  ARG   C CZ  1 
ATOM   8252  N  NH1 . ARG   C  1 185 ? 2.092   -55.128 -78.759  1.00 26.48  ? 486  ARG   C NH1 1 
ATOM   8253  N  NH2 . ARG   C  1 185 ? 1.812   -57.097 -77.623  1.00 31.84  ? 486  ARG   C NH2 1 
ATOM   8254  N  N   . TYR   C  1 186 ? 0.078   -60.863 -82.618  1.00 20.66  ? 487  TYR   C N   1 
ATOM   8255  C  CA  . TYR   C  1 186 ? -1.194  -61.519 -82.822  1.00 22.04  ? 487  TYR   C CA  1 
ATOM   8256  C  C   . TYR   C  1 186 ? -2.337  -60.562 -82.529  1.00 26.26  ? 487  TYR   C C   1 
ATOM   8257  O  O   . TYR   C  1 186 ? -2.257  -59.735 -81.614  1.00 28.12  ? 487  TYR   C O   1 
ATOM   8258  C  CB  . TYR   C  1 186 ? -1.296  -62.748 -81.935  1.00 21.76  ? 487  TYR   C CB  1 
ATOM   8259  C  CG  . TYR   C  1 186 ? -0.282  -63.820 -82.250  1.00 27.40  ? 487  TYR   C CG  1 
ATOM   8260  C  CD1 . TYR   C  1 186 ? 0.612   -64.264 -81.280  1.00 24.02  ? 487  TYR   C CD1 1 
ATOM   8261  C  CD2 . TYR   C  1 186 ? -0.225  -64.400 -83.520  1.00 26.93  ? 487  TYR   C CD2 1 
ATOM   8262  C  CE1 . TYR   C  1 186 ? 1.525   -65.268 -81.563  1.00 32.00  ? 487  TYR   C CE1 1 
ATOM   8263  C  CE2 . TYR   C  1 186 ? 0.686   -65.410 -83.809  1.00 23.41  ? 487  TYR   C CE2 1 
ATOM   8264  C  CZ  . TYR   C  1 186 ? 1.554   -65.842 -82.826  1.00 25.50  ? 487  TYR   C CZ  1 
ATOM   8265  O  OH  . TYR   C  1 186 ? 2.460   -66.844 -83.110  1.00 25.62  ? 487  TYR   C OH  1 
ATOM   8266  N  N   . ALA   C  1 187 ? -3.404  -60.695 -83.303  1.00 28.97  ? 488  ALA   C N   1 
ATOM   8267  C  CA  . ALA   C  1 187 ? -4.574  -59.860 -83.135  1.00 29.18  ? 488  ALA   C CA  1 
ATOM   8268  C  C   . ALA   C  1 187 ? -5.248  -60.150 -81.803  1.00 31.57  ? 488  ALA   C C   1 
ATOM   8269  O  O   . ALA   C  1 187 ? -5.029  -61.187 -81.177  1.00 28.18  ? 488  ALA   C O   1 
ATOM   8270  C  CB  . ALA   C  1 187 ? -5.572  -60.094 -84.269  1.00 30.02  ? 488  ALA   C CB  1 
ATOM   8271  N  N   . GLY   C  1 188 ? -6.074  -59.209 -81.385  1.00 27.65  ? 489  GLY   C N   1 
ATOM   8272  C  CA  . GLY   C  1 188 ? -6.921  -59.391 -80.220  1.00 32.17  ? 489  GLY   C CA  1 
ATOM   8273  C  C   . GLY   C  1 188 ? -8.310  -58.913 -80.572  1.00 36.36  ? 489  GLY   C C   1 
ATOM   8274  O  O   . GLY   C  1 188 ? -8.477  -57.919 -81.279  1.00 30.58  ? 489  GLY   C O   1 
ATOM   8275  N  N   . TYR   C  1 189 ? -9.310  -59.647 -80.098  1.00 40.16  ? 490  TYR   C N   1 
ATOM   8276  C  CA  . TYR   C  1 189 ? -10.697 -59.330 -80.401  1.00 34.30  ? 490  TYR   C CA  1 
ATOM   8277  C  C   . TYR   C  1 189 ? -11.487 -59.303 -79.109  1.00 40.63  ? 490  TYR   C C   1 
ATOM   8278  O  O   . TYR   C  1 189 ? -11.617 -60.335 -78.444  1.00 39.99  ? 490  TYR   C O   1 
ATOM   8279  C  CB  . TYR   C  1 189 ? -11.302 -60.353 -81.351  1.00 30.80  ? 490  TYR   C CB  1 
ATOM   8280  C  CG  . TYR   C  1 189 ? -10.455 -60.660 -82.548  1.00 32.15  ? 490  TYR   C CG  1 
ATOM   8281  C  CD1 . TYR   C  1 189 ? -9.547  -61.714 -82.531  1.00 27.04  ? 490  TYR   C CD1 1 
ATOM   8282  C  CD2 . TYR   C  1 189 ? -10.566 -59.906 -83.709  1.00 34.41  ? 490  TYR   C CD2 1 
ATOM   8283  C  CE1 . TYR   C  1 189 ? -8.774  -62.003 -83.656  1.00 32.64  ? 490  TYR   C CE1 1 
ATOM   8284  C  CE2 . TYR   C  1 189 ? -9.803  -60.187 -84.823  1.00 32.46  ? 490  TYR   C CE2 1 
ATOM   8285  C  CZ  . TYR   C  1 189 ? -8.913  -61.237 -84.796  1.00 33.32  ? 490  TYR   C CZ  1 
ATOM   8286  O  OH  . TYR   C  1 189 ? -8.157  -61.518 -85.914  1.00 33.97  ? 490  TYR   C OH  1 
ATOM   8287  N  N   . LYS   C  1 190 ? -12.018 -58.135 -78.760  1.00 44.74  ? 491  LYS   C N   1 
ATOM   8288  C  CA  . LYS   C  1 190 ? -12.969 -58.064 -77.662  1.00 42.02  ? 491  LYS   C CA  1 
ATOM   8289  C  C   . LYS   C  1 190 ? -14.271 -58.731 -78.084  1.00 43.94  ? 491  LYS   C C   1 
ATOM   8290  O  O   . LYS   C  1 190 ? -14.826 -58.419 -79.143  1.00 45.76  ? 491  LYS   C O   1 
ATOM   8291  C  CB  . LYS   C  1 190 ? -13.224 -56.614 -77.248  1.00 39.95  ? 491  LYS   C CB  1 
ATOM   8292  C  CG  . LYS   C  1 190 ? -13.503 -56.452 -75.744  1.00 56.15  ? 491  LYS   C CG  1 
ATOM   8293  C  CD  . LYS   C  1 190 ? -12.197 -56.471 -74.937  1.00 65.73  ? 491  LYS   C CD  1 
ATOM   8294  C  CE  . LYS   C  1 190 ? -12.420 -56.760 -73.449  1.00 71.88  ? 491  LYS   C CE  1 
ATOM   8295  N  NZ  . LYS   C  1 190 ? -13.328 -55.786 -72.767  1.00 77.04  ? 491  LYS   C NZ  1 
ATOM   8296  N  N   . GLN   C  1 191 ? -14.745 -59.675 -77.264  1.00 32.84  ? 492  GLN   C N   1 
ATOM   8297  C  CA  . GLN   C  1 191 ? -16.023 -60.319 -77.508  1.00 41.92  ? 492  GLN   C CA  1 
ATOM   8298  C  C   . GLN   C  1 191 ? -17.146 -59.521 -76.866  1.00 45.25  ? 492  GLN   C C   1 
ATOM   8299  O  O   . GLN   C  1 191 ? -16.923 -58.749 -75.925  1.00 41.19  ? 492  GLN   C O   1 
ATOM   8300  C  CB  . GLN   C  1 191 ? -16.014 -61.743 -76.951  1.00 50.76  ? 492  GLN   C CB  1 
ATOM   8301  C  CG  . GLN   C  1 191 ? -14.815 -62.568 -77.353  1.00 54.87  ? 492  GLN   C CG  1 
ATOM   8302  C  CD  . GLN   C  1 191 ? -14.912 -63.099 -78.759  1.00 62.15  ? 492  GLN   C CD  1 
ATOM   8303  O  OE1 . GLN   C  1 191 ? -15.640 -62.565 -79.594  1.00 59.81  ? 492  GLN   C OE1 1 
ATOM   8304  N  NE2 . GLN   C  1 191 ? -14.179 -64.170 -79.030  1.00 73.17  ? 492  GLN   C NE2 1 
ATOM   8305  N  N   . PRO   C  1 192 ? -18.369 -59.671 -77.367  1.00 44.94  ? 493  PRO   C N   1 
ATOM   8306  C  CA  . PRO   C  1 192 ? -19.506 -59.020 -76.701  1.00 42.51  ? 493  PRO   C CA  1 
ATOM   8307  C  C   . PRO   C  1 192 ? -19.568 -59.313 -75.205  1.00 47.42  ? 493  PRO   C C   1 
ATOM   8308  O  O   . PRO   C  1 192 ? -19.940 -58.428 -74.415  1.00 39.78  ? 493  PRO   C O   1 
ATOM   8309  C  CB  . PRO   C  1 192 ? -20.711 -59.596 -77.456  1.00 39.76  ? 493  PRO   C CB  1 
ATOM   8310  C  CG  . PRO   C  1 192 ? -20.169 -59.910 -78.830  1.00 41.36  ? 493  PRO   C CG  1 
ATOM   8311  C  CD  . PRO   C  1 192 ? -18.758 -60.354 -78.618  1.00 35.56  ? 493  PRO   C CD  1 
ATOM   8312  N  N   . ASP   C  1 193 ? -19.171 -60.516 -74.787  1.00 39.20  ? 494  ASP   C N   1 
ATOM   8313  C  CA  . ASP   C  1 193 ? -19.319 -60.922 -73.394  1.00 43.12  ? 494  ASP   C CA  1 
ATOM   8314  C  C   . ASP   C  1 193 ? -18.198 -60.393 -72.502  1.00 40.91  ? 494  ASP   C C   1 
ATOM   8315  O  O   . ASP   C  1 193 ? -18.121 -60.773 -71.327  1.00 43.61  ? 494  ASP   C O   1 
ATOM   8316  C  CB  . ASP   C  1 193 ? -19.429 -62.452 -73.304  1.00 40.36  ? 494  ASP   C CB  1 
ATOM   8317  C  CG  . ASP   C  1 193 ? -18.112 -63.168 -73.572  1.00 46.30  ? 494  ASP   C CG  1 
ATOM   8318  O  OD1 . ASP   C  1 193 ? -18.019 -64.366 -73.226  1.00 46.92  ? 494  ASP   C OD1 1 
ATOM   8319  O  OD2 . ASP   C  1 193 ? -17.169 -62.545 -74.106  1.00 48.38  ? 494  ASP   C OD2 1 
ATOM   8320  N  N   . GLY   C  1 194 ? -17.353 -59.504 -73.025  1.00 39.86  ? 495  GLY   C N   1 
ATOM   8321  C  CA  . GLY   C  1 194 ? -16.258 -58.947 -72.272  1.00 42.15  ? 495  GLY   C CA  1 
ATOM   8322  C  C   . GLY   C  1 194 ? -14.975 -59.747 -72.326  1.00 44.81  ? 495  GLY   C C   1 
ATOM   8323  O  O   . GLY   C  1 194 ? -13.914 -59.208 -71.995  1.00 44.94  ? 495  GLY   C O   1 
ATOM   8324  N  N   . SER   C  1 195 ? -15.039 -61.016 -72.724  1.00 41.84  ? 496  SER   C N   1 
ATOM   8325  C  CA  . SER   C  1 195 ? -13.820 -61.787 -72.895  1.00 42.17  ? 496  SER   C CA  1 
ATOM   8326  C  C   . SER   C  1 195 ? -13.044 -61.270 -74.106  1.00 43.47  ? 496  SER   C C   1 
ATOM   8327  O  O   . SER   C  1 195 ? -13.555 -60.506 -74.930  1.00 43.25  ? 496  SER   C O   1 
ATOM   8328  C  CB  . SER   C  1 195 ? -14.138 -63.272 -73.063  1.00 39.81  ? 496  SER   C CB  1 
ATOM   8329  O  OG  . SER   C  1 195 ? -14.696 -63.519 -74.339  1.00 40.55  ? 496  SER   C OG  1 
ATOM   8330  N  N   . THR   C  1 196 ? -11.788 -61.687 -74.203  1.00 41.28  ? 497  THR   C N   1 
ATOM   8331  C  CA  . THR   C  1 196 ? -10.927 -61.291 -75.303  1.00 42.52  ? 497  THR   C CA  1 
ATOM   8332  C  C   . THR   C  1 196 ? -10.377 -62.537 -75.971  1.00 44.35  ? 497  THR   C C   1 
ATOM   8333  O  O   . THR   C  1 196 ? -9.931  -63.467 -75.292  1.00 49.47  ? 497  THR   C O   1 
ATOM   8334  C  CB  . THR   C  1 196 ? -9.782  -60.396 -74.822  1.00 47.22  ? 497  THR   C CB  1 
ATOM   8335  O  OG1 . THR   C  1 196 ? -10.324 -59.190 -74.272  1.00 48.15  ? 497  THR   C OG1 1 
ATOM   8336  C  CG2 . THR   C  1 196 ? -8.853  -60.049 -75.981  1.00 50.40  ? 497  THR   C CG2 1 
ATOM   8337  N  N   . LEU   C  1 197 ? -10.433 -62.564 -77.294  1.00 36.39  ? 498  LEU   C N   1 
ATOM   8338  C  CA  . LEU   C  1 197 ? -9.819  -63.627 -78.072  1.00 30.80  ? 498  LEU   C CA  1 
ATOM   8339  C  C   . LEU   C  1 197 ? -8.488  -63.112 -78.589  1.00 32.22  ? 498  LEU   C C   1 
ATOM   8340  O  O   . LEU   C  1 197 ? -8.404  -61.980 -79.072  1.00 36.02  ? 498  LEU   C O   1 
ATOM   8341  C  CB  . LEU   C  1 197 ? -10.717 -64.053 -79.227  1.00 36.54  ? 498  LEU   C CB  1 
ATOM   8342  C  CG  . LEU   C  1 197 ? -10.155 -65.118 -80.170  1.00 40.74  ? 498  LEU   C CG  1 
ATOM   8343  C  CD1 . LEU   C  1 197 ? -9.740  -66.352 -79.374  1.00 37.97  ? 498  LEU   C CD1 1 
ATOM   8344  C  CD2 . LEU   C  1 197 ? -11.163 -65.465 -81.288  1.00 35.91  ? 498  LEU   C CD2 1 
ATOM   8345  N  N   . GLY   C  1 198 ? -7.451  -63.932 -78.470  1.00 29.46  ? 499  GLY   C N   1 
ATOM   8346  C  CA  . GLY   C  1 198 ? -6.130  -63.503 -78.884  1.00 24.84  ? 499  GLY   C CA  1 
ATOM   8347  C  C   . GLY   C  1 198 ? -5.483  -62.594 -77.853  1.00 31.27  ? 499  GLY   C C   1 
ATOM   8348  O  O   . GLY   C  1 198 ? -5.813  -62.631 -76.669  1.00 34.23  ? 499  GLY   C O   1 
ATOM   8349  N  N   . ASP   C  1 199 ? -4.570  -61.745 -78.326  1.00 27.35  ? 500  ASP   C N   1 
ATOM   8350  C  CA  . ASP   C  1 199 ? -3.769  -60.883 -77.474  1.00 29.74  ? 500  ASP   C CA  1 
ATOM   8351  C  C   . ASP   C  1 199 ? -4.538  -59.621 -77.072  1.00 31.02  ? 500  ASP   C C   1 
ATOM   8352  O  O   . ASP   C  1 199 ? -4.776  -58.742 -77.910  1.00 33.08  ? 500  ASP   C O   1 
ATOM   8353  C  CB  . ASP   C  1 199 ? -2.460  -60.528 -78.195  1.00 34.15  ? 500  ASP   C CB  1 
ATOM   8354  C  CG  . ASP   C  1 199 ? -1.449  -59.858 -77.280  1.00 34.31  ? 500  ASP   C CG  1 
ATOM   8355  O  OD1 . ASP   C  1 199 ? -1.887  -59.235 -76.302  1.00 32.39  ? 500  ASP   C OD1 1 
ATOM   8356  O  OD2 . ASP   C  1 199 ? -0.222  -59.945 -77.534  1.00 28.53  ? 500  ASP   C OD2 1 
ATOM   8357  N  N   . PRO   C  1 200 ? -4.889  -59.479 -75.790  1.00 30.89  ? 501  PRO   C N   1 
ATOM   8358  C  CA  . PRO   C  1 200 ? -5.627  -58.282 -75.343  1.00 30.89  ? 501  PRO   C CA  1 
ATOM   8359  C  C   . PRO   C  1 200 ? -4.879  -56.982 -75.553  1.00 30.33  ? 501  PRO   C C   1 
ATOM   8360  O  O   . PRO   C  1 200 ? -5.519  -55.930 -75.675  1.00 31.15  ? 501  PRO   C O   1 
ATOM   8361  C  CB  . PRO   C  1 200 ? -5.846  -58.545 -73.844  1.00 30.34  ? 501  PRO   C CB  1 
ATOM   8362  C  CG  . PRO   C  1 200 ? -5.750  -60.044 -73.705  1.00 31.81  ? 501  PRO   C CG  1 
ATOM   8363  C  CD  . PRO   C  1 200 ? -4.729  -60.475 -74.711  1.00 25.06  ? 501  PRO   C CD  1 
ATOM   8364  N  N   . ALA   C  1 201 ? -3.548  -57.010 -75.579  1.00 31.89  ? 502  ALA   C N   1 
ATOM   8365  C  CA  . ALA   C  1 201 ? -2.772  -55.793 -75.793  1.00 34.61  ? 502  ALA   C CA  1 
ATOM   8366  C  C   . ALA   C  1 201 ? -2.977  -55.199 -77.177  1.00 30.77  ? 502  ALA   C C   1 
ATOM   8367  O  O   . ALA   C  1 201 ? -2.609  -54.041 -77.403  1.00 32.17  ? 502  ALA   C O   1 
ATOM   8368  C  CB  . ALA   C  1 201 ? -1.280  -56.066 -75.597  1.00 32.78  ? 502  ALA   C CB  1 
ATOM   8369  N  N   . ASN   C  1 202 ? -3.531  -55.963 -78.110  1.00 25.33  ? 503  ASN   C N   1 
ATOM   8370  C  CA  . ASN   C  1 202 ? -3.571  -55.553 -79.506  1.00 28.12  ? 503  ASN   C CA  1 
ATOM   8371  C  C   . ASN   C  1 202 ? -4.987  -55.271 -79.978  1.00 29.56  ? 503  ASN   C C   1 
ATOM   8372  O  O   . ASN   C  1 202 ? -5.213  -55.084 -81.180  1.00 30.73  ? 503  ASN   C O   1 
ATOM   8373  C  CB  . ASN   C  1 202 ? -2.898  -56.625 -80.360  1.00 23.24  ? 503  ASN   C CB  1 
ATOM   8374  C  CG  . ASN   C  1 202 ? -1.404  -56.650 -80.147  1.00 26.47  ? 503  ASN   C CG  1 
ATOM   8375  O  OD1 . ASN   C  1 202 ? -0.797  -55.609 -79.906  1.00 32.59  ? 503  ASN   C OD1 1 
ATOM   8376  N  ND2 . ASN   C  1 202 ? -0.802  -57.828 -80.228  1.00 26.34  ? 503  ASN   C ND2 1 
ATOM   8377  N  N   . VAL   C  1 203 ? -5.935  -55.215 -79.045  1.00 27.21  ? 504  VAL   C N   1 
ATOM   8378  C  CA  . VAL   C  1 203 ? -7.336  -55.010 -79.384  1.00 29.06  ? 504  VAL   C CA  1 
ATOM   8379  C  C   . VAL   C  1 203 ? -7.517  -53.704 -80.150  1.00 36.28  ? 504  VAL   C C   1 
ATOM   8380  O  O   . VAL   C  1 203 ? -8.168  -53.668 -81.203  1.00 31.42  ? 504  VAL   C O   1 
ATOM   8381  C  CB  . VAL   C  1 203 ? -8.195  -55.055 -78.109  1.00 34.14  ? 504  VAL   C CB  1 
ATOM   8382  C  CG1 . VAL   C  1 203 ? -9.566  -54.439 -78.363  1.00 33.53  ? 504  VAL   C CG1 1 
ATOM   8383  C  CG2 . VAL   C  1 203 ? -8.318  -56.503 -77.604  1.00 30.28  ? 504  VAL   C CG2 1 
ATOM   8384  N  N   . GLN   C  1 204 ? -6.933  -52.613 -79.643  1.00 35.35  ? 505  GLN   C N   1 
ATOM   8385  C  CA  . GLN   C  1 204 ? -7.102  -51.320 -80.303  1.00 34.26  ? 505  GLN   C CA  1 
ATOM   8386  C  C   . GLN   C  1 204 ? -6.507  -51.340 -81.706  1.00 33.11  ? 505  GLN   C C   1 
ATOM   8387  O  O   . GLN   C  1 204 ? -7.153  -50.919 -82.672  1.00 27.28  ? 505  GLN   C O   1 
ATOM   8388  C  CB  . GLN   C  1 204 ? -6.468  -50.200 -79.480  1.00 42.18  ? 505  GLN   C CB  1 
ATOM   8389  C  CG  . GLN   C  1 204 ? -7.089  -48.837 -79.759  1.00 60.56  ? 505  GLN   C CG  1 
ATOM   8390  C  CD  . GLN   C  1 204 ? -6.177  -47.656 -79.423  1.00 66.68  ? 505  GLN   C CD  1 
ATOM   8391  O  OE1 . GLN   C  1 204 ? -5.164  -47.803 -78.738  1.00 61.86  ? 505  GLN   C OE1 1 
ATOM   8392  N  NE2 . GLN   C  1 204 ? -6.542  -46.474 -79.918  1.00 68.09  ? 505  GLN   C NE2 1 
ATOM   8393  N  N   . PHE   C  1 205 ? -5.266  -51.824 -81.835  1.00 27.13  ? 506  PHE   C N   1 
ATOM   8394  C  CA  . PHE   C  1 205 ? -4.631  -51.870 -83.146  1.00 27.15  ? 506  PHE   C CA  1 
ATOM   8395  C  C   . PHE   C  1 205 ? -5.368  -52.814 -84.085  1.00 28.69  ? 506  PHE   C C   1 
ATOM   8396  O  O   . PHE   C  1 205 ? -5.522  -52.519 -85.278  1.00 25.36  ? 506  PHE   C O   1 
ATOM   8397  C  CB  . PHE   C  1 205 ? -3.172  -52.294 -83.019  1.00 29.68  ? 506  PHE   C CB  1 
ATOM   8398  C  CG  . PHE   C  1 205 ? -2.453  -52.334 -84.330  1.00 32.17  ? 506  PHE   C CG  1 
ATOM   8399  C  CD1 . PHE   C  1 205 ? -1.938  -51.176 -84.887  1.00 33.41  ? 506  PHE   C CD1 1 
ATOM   8400  C  CD2 . PHE   C  1 205 ? -2.313  -53.526 -85.025  1.00 32.42  ? 506  PHE   C CD2 1 
ATOM   8401  C  CE1 . PHE   C  1 205 ? -1.280  -51.210 -86.117  1.00 33.20  ? 506  PHE   C CE1 1 
ATOM   8402  C  CE2 . PHE   C  1 205 ? -1.651  -53.565 -86.248  1.00 28.60  ? 506  PHE   C CE2 1 
ATOM   8403  C  CZ  . PHE   C  1 205 ? -1.141  -52.405 -86.794  1.00 27.60  ? 506  PHE   C CZ  1 
ATOM   8404  N  N   . THR   C  1 206 ? -5.825  -53.958 -83.570  1.00 26.20  ? 507  THR   C N   1 
ATOM   8405  C  CA  . THR   C  1 206 ? -6.657  -54.846 -84.374  1.00 29.77  ? 507  THR   C CA  1 
ATOM   8406  C  C   . THR   C  1 206 ? -7.889  -54.115 -84.893  1.00 33.95  ? 507  THR   C C   1 
ATOM   8407  O  O   . THR   C  1 206 ? -8.265  -54.270 -86.062  1.00 36.24  ? 507  THR   C O   1 
ATOM   8408  C  CB  . THR   C  1 206 ? -7.045  -56.079 -83.555  1.00 24.29  ? 507  THR   C CB  1 
ATOM   8409  O  OG1 . THR   C  1 206 ? -5.849  -56.748 -83.123  1.00 28.02  ? 507  THR   C OG1 1 
ATOM   8410  C  CG2 . THR   C  1 206 ? -7.897  -57.059 -84.368  1.00 25.01  ? 507  THR   C CG2 1 
ATOM   8411  N  N   . GLU   C  1 207 ? -8.521  -53.295 -84.047  1.00 31.19  ? 508  GLU   C N   1 
ATOM   8412  C  CA  . GLU   C  1 207 ? -9.709  -52.573 -84.492  1.00 32.29  ? 508  GLU   C CA  1 
ATOM   8413  C  C   . GLU   C  1 207 ? -9.372  -51.610 -85.621  1.00 30.18  ? 508  GLU   C C   1 
ATOM   8414  O  O   . GLU   C  1 207 ? -10.122 -51.500 -86.599  1.00 30.60  ? 508  GLU   C O   1 
ATOM   8415  C  CB  . GLU   C  1 207 ? -10.349 -51.827 -83.316  1.00 39.42  ? 508  GLU   C CB  1 
ATOM   8416  C  CG  . GLU   C  1 207 ? -11.125 -52.710 -82.358  1.00 50.30  ? 508  GLU   C CG  1 
ATOM   8417  C  CD  . GLU   C  1 207 ? -11.510 -51.989 -81.067  1.00 65.00  ? 508  GLU   C CD  1 
ATOM   8418  O  OE1 . GLU   C  1 207 ? -11.146 -50.801 -80.902  1.00 65.45  ? 508  GLU   C OE1 1 
ATOM   8419  O  OE2 . GLU   C  1 207 ? -12.174 -52.618 -80.211  1.00 71.47  ? 508  GLU   C OE2 1 
ATOM   8420  N  N   . ILE   C  1 208 ? -8.231  -50.925 -85.518  1.00 28.91  ? 509  ILE   C N   1 
ATOM   8421  C  CA  . ILE   C  1 208 ? -7.807  -50.033 -86.590  1.00 25.52  ? 509  ILE   C CA  1 
ATOM   8422  C  C   . ILE   C  1 208 ? -7.635  -50.814 -87.882  1.00 30.03  ? 509  ILE   C C   1 
ATOM   8423  O  O   . ILE   C  1 208 ? -8.100  -50.394 -88.945  1.00 36.44  ? 509  ILE   C O   1 
ATOM   8424  C  CB  . ILE   C  1 208 ? -6.508  -49.307 -86.202  1.00 33.29  ? 509  ILE   C CB  1 
ATOM   8425  C  CG1 . ILE   C  1 208 ? -6.759  -48.374 -85.014  1.00 37.22  ? 509  ILE   C CG1 1 
ATOM   8426  C  CG2 . ILE   C  1 208 ? -5.965  -48.548 -87.400  1.00 30.45  ? 509  ILE   C CG2 1 
ATOM   8427  C  CD1 . ILE   C  1 208 ? -5.499  -47.753 -84.453  1.00 39.08  ? 509  ILE   C CD1 1 
ATOM   8428  N  N   . CYS   C  1 209 ? -6.963  -51.968 -87.807  1.00 33.44  ? 510  CYS   C N   1 
ATOM   8429  C  CA  . CYS   C  1 209 ? -6.751  -52.787 -88.997  1.00 35.79  ? 510  CYS   C CA  1 
ATOM   8430  C  C   . CYS   C  1 209 ? -8.072  -53.198 -89.628  1.00 33.96  ? 510  CYS   C C   1 
ATOM   8431  O  O   . CYS   C  1 209 ? -8.259  -53.058 -90.839  1.00 34.01  ? 510  CYS   C O   1 
ATOM   8432  C  CB  . CYS   C  1 209 ? -5.921  -54.022 -88.654  1.00 26.71  ? 510  CYS   C CB  1 
ATOM   8433  S  SG  . CYS   C  1 209 ? -4.219  -53.656 -88.280  1.00 29.27  ? 510  CYS   C SG  1 
ATOM   8434  N  N   . ILE   C  1 210 ? -8.996  -53.721 -88.821  1.00 35.54  ? 511  ILE   C N   1 
ATOM   8435  C  CA  . ILE   C  1 210 ? -10.309 -54.082 -89.343  1.00 36.12  ? 511  ILE   C CA  1 
ATOM   8436  C  C   . ILE   C  1 210 ? -10.971 -52.878 -89.994  1.00 35.36  ? 511  ILE   C C   1 
ATOM   8437  O  O   . ILE   C  1 210 ? -11.531 -52.975 -91.091  1.00 36.74  ? 511  ILE   C O   1 
ATOM   8438  C  CB  . ILE   C  1 210 ? -11.183 -54.669 -88.223  1.00 40.24  ? 511  ILE   C CB  1 
ATOM   8439  C  CG1 . ILE   C  1 210 ? -10.634 -56.030 -87.793  1.00 39.82  ? 511  ILE   C CG1 1 
ATOM   8440  C  CG2 . ILE   C  1 210 ? -12.639 -54.755 -88.679  1.00 38.88  ? 511  ILE   C CG2 1 
ATOM   8441  C  CD1 . ILE   C  1 210 ? -11.167 -56.514 -86.456  1.00 30.23  ? 511  ILE   C CD1 1 
ATOM   8442  N  N   . GLN   C  1 211 ? -10.904 -51.720 -89.337  1.00 32.72  ? 512  GLN   C N   1 
ATOM   8443  C  CA  . GLN   C  1 211 ? -11.526 -50.525 -89.893  1.00 40.31  ? 512  GLN   C CA  1 
ATOM   8444  C  C   . GLN   C  1 211 ? -10.922 -50.162 -91.244  1.00 41.48  ? 512  GLN   C C   1 
ATOM   8445  O  O   . GLN   C  1 211 ? -11.630 -49.683 -92.133  1.00 36.34  ? 512  GLN   C O   1 
ATOM   8446  C  CB  . GLN   C  1 211 ? -11.384 -49.368 -88.914  1.00 38.64  ? 512  GLN   C CB  1 
ATOM   8447  C  CG  . GLN   C  1 211 ? -12.113 -48.120 -89.328  1.00 53.77  ? 512  GLN   C CG  1 
ATOM   8448  C  CD  . GLN   C  1 211 ? -11.708 -46.937 -88.483  1.00 74.95  ? 512  GLN   C CD  1 
ATOM   8449  O  OE1 . GLN   C  1 211 ? -10.861 -47.054 -87.594  1.00 81.15  ? 512  GLN   C OE1 1 
ATOM   8450  N  NE2 . GLN   C  1 211 ? -12.307 -45.785 -88.754  1.00 83.10  ? 512  GLN   C NE2 1 
ATOM   8451  N  N   . GLN   C  1 212 ? -9.626  -50.391 -91.417  1.00 37.72  ? 513  GLN   C N   1 
ATOM   8452  C  CA  . GLN   C  1 212 ? -8.936  -50.125 -92.669  1.00 37.47  ? 513  GLN   C CA  1 
ATOM   8453  C  C   . GLN   C  1 212 ? -9.181  -51.196 -93.720  1.00 43.03  ? 513  GLN   C C   1 
ATOM   8454  O  O   . GLN   C  1 212 ? -8.602  -51.111 -94.810  1.00 48.90  ? 513  GLN   C O   1 
ATOM   8455  C  CB  . GLN   C  1 212 ? -7.428  -49.997 -92.423  1.00 36.82  ? 513  GLN   C CB  1 
ATOM   8456  C  CG  . GLN   C  1 212 ? -7.035  -48.814 -91.564  1.00 35.12  ? 513  GLN   C CG  1 
ATOM   8457  C  CD  . GLN   C  1 212 ? -7.687  -47.537 -92.037  1.00 46.27  ? 513  GLN   C CD  1 
ATOM   8458  O  OE1 . GLN   C  1 212 ? -8.336  -46.839 -91.262  1.00 49.64  ? 513  GLN   C OE1 1 
ATOM   8459  N  NE2 . GLN   C  1 212 ? -7.524  -47.226 -93.321  1.00 40.67  ? 513  GLN   C NE2 1 
ATOM   8460  N  N   . GLY   C  1 213 ? -9.996  -52.207 -93.421  1.00 37.88  ? 514  GLY   C N   1 
ATOM   8461  C  CA  . GLY   C  1 213 ? -10.372 -53.201 -94.406  1.00 34.94  ? 514  GLY   C CA  1 
ATOM   8462  C  C   . GLY   C  1 213 ? -9.853  -54.598 -94.150  1.00 37.86  ? 514  GLY   C C   1 
ATOM   8463  O  O   . GLY   C  1 213 ? -10.181 -55.507 -94.918  1.00 37.64  ? 514  GLY   C O   1 
ATOM   8464  N  N   . TRP   C  1 214 ? -9.070  -54.813 -93.097  1.00 40.48  ? 515  TRP   C N   1 
ATOM   8465  C  CA  . TRP   C  1 214 ? -8.564  -56.149 -92.817  1.00 34.50  ? 515  TRP   C CA  1 
ATOM   8466  C  C   . TRP   C  1 214 ? -9.709  -57.099 -92.487  1.00 37.68  ? 515  TRP   C C   1 
ATOM   8467  O  O   . TRP   C  1 214 ? -10.611 -56.762 -91.712  1.00 39.02  ? 515  TRP   C O   1 
ATOM   8468  C  CB  . TRP   C  1 214 ? -7.571  -56.105 -91.660  1.00 36.70  ? 515  TRP   C CB  1 
ATOM   8469  C  CG  . TRP   C  1 214 ? -6.881  -57.403 -91.418  1.00 33.73  ? 515  TRP   C CG  1 
ATOM   8470  C  CD1 . TRP   C  1 214 ? -6.195  -58.155 -92.333  1.00 32.72  ? 515  TRP   C CD1 1 
ATOM   8471  C  CD2 . TRP   C  1 214 ? -6.779  -58.095 -90.173  1.00 37.42  ? 515  TRP   C CD2 1 
ATOM   8472  N  NE1 . TRP   C  1 214 ? -5.683  -59.279 -91.733  1.00 34.64  ? 515  TRP   C NE1 1 
ATOM   8473  C  CE2 . TRP   C  1 214 ? -6.026  -59.266 -90.406  1.00 37.75  ? 515  TRP   C CE2 1 
ATOM   8474  C  CE3 . TRP   C  1 214 ? -7.250  -57.841 -88.883  1.00 35.46  ? 515  TRP   C CE3 1 
ATOM   8475  C  CZ2 . TRP   C  1 214 ? -5.736  -60.178 -89.397  1.00 32.37  ? 515  TRP   C CZ2 1 
ATOM   8476  C  CZ3 . TRP   C  1 214 ? -6.967  -58.753 -87.882  1.00 36.86  ? 515  TRP   C CZ3 1 
ATOM   8477  C  CH2 . TRP   C  1 214 ? -6.214  -59.903 -88.142  1.00 35.20  ? 515  TRP   C CH2 1 
ATOM   8478  N  N   . LYS   C  1 215 ? -9.666  -58.291 -93.073  1.00 33.36  ? 516  LYS   C N   1 
ATOM   8479  C  CA  . LYS   C  1 215 ? -10.662 -59.314 -92.802  1.00 33.62  ? 516  LYS   C CA  1 
ATOM   8480  C  C   . LYS   C  1 215 ? -10.077 -60.266 -91.781  1.00 36.00  ? 516  LYS   C C   1 
ATOM   8481  O  O   . LYS   C  1 215 ? -9.209  -61.076 -92.124  1.00 43.83  ? 516  LYS   C O   1 
ATOM   8482  C  CB  . LYS   C  1 215 ? -11.045 -60.052 -94.082  1.00 43.14  ? 516  LYS   C CB  1 
ATOM   8483  C  CG  . LYS   C  1 215 ? -11.705 -59.163 -95.119  1.00 56.05  ? 516  LYS   C CG  1 
ATOM   8484  C  CD  . LYS   C  1 215 ? -13.112 -58.778 -94.687  1.00 65.78  ? 516  LYS   C CD  1 
ATOM   8485  C  CE  . LYS   C  1 215 ? -13.615 -57.546 -95.430  1.00 70.00  ? 516  LYS   C CE  1 
ATOM   8486  N  NZ  . LYS   C  1 215 ? -13.111 -56.272 -94.832  1.00 65.78  ? 516  LYS   C NZ  1 
ATOM   8487  N  N   . PRO   C  1 216 ? -10.485 -60.200 -90.524  1.00 39.10  ? 517  PRO   C N   1 
ATOM   8488  C  CA  . PRO   C  1 216 ? -9.804  -60.964 -89.487  1.00 38.25  ? 517  PRO   C CA  1 
ATOM   8489  C  C   . PRO   C  1 216 ? -10.243 -62.416 -89.498  1.00 41.26  ? 517  PRO   C C   1 
ATOM   8490  O  O   . PRO   C  1 216 ? -11.436 -62.714 -89.649  1.00 41.44  ? 517  PRO   C O   1 
ATOM   8491  C  CB  . PRO   C  1 216 ? -10.242 -60.262 -88.200  1.00 37.72  ? 517  PRO   C CB  1 
ATOM   8492  C  CG  . PRO   C  1 216 ? -11.625 -59.796 -88.508  1.00 40.05  ? 517  PRO   C CG  1 
ATOM   8493  C  CD  . PRO   C  1 216 ? -11.608 -59.414 -89.980  1.00 43.78  ? 517  PRO   C CD  1 
ATOM   8494  N  N   . PRO   C  1 217 ? -9.309  -63.350 -89.331  1.00 44.00  ? 518  PRO   C N   1 
ATOM   8495  C  CA  . PRO   C  1 217 ? -9.711  -64.747 -89.106  1.00 39.63  ? 518  PRO   C CA  1 
ATOM   8496  C  C   . PRO   C  1 217 ? -10.503 -64.932 -87.825  1.00 38.15  ? 518  PRO   C C   1 
ATOM   8497  O  O   . PRO   C  1 217 ? -11.289 -65.882 -87.723  1.00 44.47  ? 518  PRO   C O   1 
ATOM   8498  C  CB  . PRO   C  1 217 ? -8.370  -65.490 -89.042  1.00 36.94  ? 518  PRO   C CB  1 
ATOM   8499  C  CG  . PRO   C  1 217 ? -7.386  -64.568 -89.700  1.00 37.19  ? 518  PRO   C CG  1 
ATOM   8500  C  CD  . PRO   C  1 217 ? -7.849  -63.189 -89.368  1.00 39.48  ? 518  PRO   C CD  1 
ATOM   8501  N  N   . ARG   C  1 218 ? -10.328 -64.039 -86.849  1.00 44.03  ? 519  ARG   C N   1 
ATOM   8502  C  CA  . ARG   C  1 218 ? -10.926 -64.166 -85.518  1.00 42.47  ? 519  ARG   C CA  1 
ATOM   8503  C  C   . ARG   C  1 218 ? -10.547 -65.500 -84.870  1.00 48.17  ? 519  ARG   C C   1 
ATOM   8504  O  O   . ARG   C  1 218 ? -11.398 -66.300 -84.476  1.00 54.40  ? 519  ARG   C O   1 
ATOM   8505  C  CB  . ARG   C  1 218 ? -12.442 -63.967 -85.566  1.00 46.09  ? 519  ARG   C CB  1 
ATOM   8506  C  CG  . ARG   C  1 218 ? -12.813 -62.610 -86.132  1.00 49.47  ? 519  ARG   C CG  1 
ATOM   8507  C  CD  . ARG   C  1 218 ? -14.182 -62.117 -85.691  1.00 55.19  ? 519  ARG   C CD  1 
ATOM   8508  N  NE  . ARG   C  1 218 ? -14.186 -60.653 -85.623  1.00 69.85  ? 519  ARG   C NE  1 
ATOM   8509  C  CZ  . ARG   C  1 218 ? -14.145 -59.953 -84.490  1.00 75.68  ? 519  ARG   C CZ  1 
ATOM   8510  N  NH1 . ARG   C  1 218 ? -14.141 -58.623 -84.526  1.00 76.00  ? 519  ARG   C NH1 1 
ATOM   8511  N  NH2 . ARG   C  1 218 ? -14.125 -60.581 -83.317  1.00 76.33  ? 519  ARG   C NH2 1 
ATOM   8512  N  N   . GLY   C  1 219 ? -9.238  -65.731 -84.774  1.00 45.63  ? 520  GLY   C N   1 
ATOM   8513  C  CA  . GLY   C  1 219 ? -8.679  -66.813 -83.998  1.00 41.31  ? 520  GLY   C CA  1 
ATOM   8514  C  C   . GLY   C  1 219 ? -7.772  -66.264 -82.907  1.00 40.59  ? 520  GLY   C C   1 
ATOM   8515  O  O   . GLY   C  1 219 ? -7.656  -65.048 -82.719  1.00 35.47  ? 520  GLY   C O   1 
ATOM   8516  N  N   . ARG   C  1 220 ? -7.106  -67.182 -82.210  1.00 34.68  ? 521  ARG   C N   1 
ATOM   8517  C  CA  . ARG   C  1 220 ? -6.335  -66.793 -81.031  1.00 32.28  ? 521  ARG   C CA  1 
ATOM   8518  C  C   . ARG   C  1 220 ? -4.924  -66.319 -81.354  1.00 29.98  ? 521  ARG   C C   1 
ATOM   8519  O  O   . ARG   C  1 220 ? -4.307  -65.630 -80.533  1.00 27.70  ? 521  ARG   C O   1 
ATOM   8520  C  CB  . ARG   C  1 220 ? -6.273  -67.961 -80.051  1.00 32.58  ? 521  ARG   C CB  1 
ATOM   8521  C  CG  . ARG   C  1 220 ? -5.871  -67.573 -78.643  1.00 32.08  ? 521  ARG   C CG  1 
ATOM   8522  C  CD  . ARG   C  1 220 ? -5.981  -68.804 -77.784  1.00 37.62  ? 521  ARG   C CD  1 
ATOM   8523  N  NE  . ARG   C  1 220 ? -5.556  -68.608 -76.408  1.00 41.82  ? 521  ARG   C NE  1 
ATOM   8524  C  CZ  . ARG   C  1 220 ? -5.060  -69.589 -75.661  1.00 46.04  ? 521  ARG   C CZ  1 
ATOM   8525  N  NH1 . ARG   C  1 220 ? -4.906  -70.804 -76.186  1.00 40.70  ? 521  ARG   C NH1 1 
ATOM   8526  N  NH2 . ARG   C  1 220 ? -4.705  -69.355 -74.405  1.00 51.51  ? 521  ARG   C NH2 1 
ATOM   8527  N  N   . PHE   C  1 221 ? -4.401  -66.660 -82.528  1.00 36.73  ? 522  PHE   C N   1 
ATOM   8528  C  CA  . PHE   C  1 221 ? -3.049  -66.297 -82.905  1.00 26.69  ? 522  PHE   C CA  1 
ATOM   8529  C  C   . PHE   C  1 221 ? -3.048  -65.905 -84.382  1.00 30.02  ? 522  PHE   C C   1 
ATOM   8530  O  O   . PHE   C  1 221 ? -2.383  -66.511 -85.220  1.00 29.42  ? 522  PHE   C O   1 
ATOM   8531  C  CB  . PHE   C  1 221 ? -2.074  -67.441 -82.632  1.00 32.57  ? 522  PHE   C CB  1 
ATOM   8532  C  CG  . PHE   C  1 221 ? -2.046  -67.890 -81.200  1.00 34.33  ? 522  PHE   C CG  1 
ATOM   8533  C  CD1 . PHE   C  1 221 ? -2.678  -69.062 -80.815  1.00 35.01  ? 522  PHE   C CD1 1 
ATOM   8534  C  CD2 . PHE   C  1 221 ? -1.389  -67.139 -80.237  1.00 28.41  ? 522  PHE   C CD2 1 
ATOM   8535  C  CE1 . PHE   C  1 221 ? -2.639  -69.477 -79.489  1.00 37.18  ? 522  PHE   C CE1 1 
ATOM   8536  C  CE2 . PHE   C  1 221 ? -1.344  -67.551 -78.924  1.00 32.31  ? 522  PHE   C CE2 1 
ATOM   8537  C  CZ  . PHE   C  1 221 ? -1.977  -68.719 -78.547  1.00 36.72  ? 522  PHE   C CZ  1 
ATOM   8538  N  N   . ASP   C  1 222 ? -3.828  -64.875 -84.703  1.00 26.63  ? 523  ASP   C N   1 
ATOM   8539  C  CA  . ASP   C  1 222 ? -3.856  -64.317 -86.046  1.00 27.05  ? 523  ASP   C CA  1 
ATOM   8540  C  C   . ASP   C  1 222 ? -2.718  -63.326 -86.178  1.00 27.91  ? 523  ASP   C C   1 
ATOM   8541  O  O   . ASP   C  1 222 ? -2.714  -62.303 -85.491  1.00 30.19  ? 523  ASP   C O   1 
ATOM   8542  C  CB  . ASP   C  1 222 ? -5.171  -63.593 -86.316  1.00 29.14  ? 523  ASP   C CB  1 
ATOM   8543  C  CG  . ASP   C  1 222 ? -6.362  -64.480 -86.178  1.00 31.98  ? 523  ASP   C CG  1 
ATOM   8544  O  OD1 . ASP   C  1 222 ? -6.191  -65.714 -86.236  1.00 35.20  ? 523  ASP   C OD1 1 
ATOM   8545  O  OD2 . ASP   C  1 222 ? -7.477  -63.934 -86.022  1.00 32.64  ? 523  ASP   C OD2 1 
ATOM   8546  N  N   . VAL   C  1 223 ? -1.763  -63.603 -87.062  1.00 24.33  ? 524  VAL   C N   1 
ATOM   8547  C  CA  . VAL   C  1 223 ? -0.719  -62.616 -87.299  1.00 26.19  ? 524  VAL   C CA  1 
ATOM   8548  C  C   . VAL   C  1 223 ? -1.361  -61.370 -87.881  1.00 22.82  ? 524  VAL   C C   1 
ATOM   8549  O  O   . VAL   C  1 223 ? -2.140  -61.448 -88.833  1.00 24.76  ? 524  VAL   C O   1 
ATOM   8550  C  CB  . VAL   C  1 223 ? 0.362   -63.179 -88.228  1.00 28.26  ? 524  VAL   C CB  1 
ATOM   8551  C  CG1 . VAL   C  1 223 ? 1.375   -62.098 -88.556  1.00 23.26  ? 524  VAL   C CG1 1 
ATOM   8552  C  CG2 . VAL   C  1 223 ? 1.032   -64.394 -87.584  1.00 21.64  ? 524  VAL   C CG2 1 
ATOM   8553  N  N   . LEU   C  1 224 ? -1.066  -60.224 -87.296  1.00 25.47  ? 525  LEU   C N   1 
ATOM   8554  C  CA  . LEU   C  1 224 ? -1.696  -58.989 -87.736  1.00 25.08  ? 525  LEU   C CA  1 
ATOM   8555  C  C   . LEU   C  1 224 ? -1.117  -58.520 -89.071  1.00 21.46  ? 525  LEU   C C   1 
ATOM   8556  O  O   . LEU   C  1 224 ? 0.045   -58.788 -89.377  1.00 24.33  ? 525  LEU   C O   1 
ATOM   8557  C  CB  . LEU   C  1 224 ? -1.494  -57.907 -86.687  1.00 22.52  ? 525  LEU   C CB  1 
ATOM   8558  C  CG  . LEU   C  1 224 ? -2.454  -58.027 -85.509  1.00 25.26  ? 525  LEU   C CG  1 
ATOM   8559  C  CD1 . LEU   C  1 224 ? -1.833  -57.436 -84.239  1.00 21.88  ? 525  LEU   C CD1 1 
ATOM   8560  C  CD2 . LEU   C  1 224 ? -3.754  -57.312 -85.894  1.00 24.62  ? 525  LEU   C CD2 1 
ATOM   8561  N  N   . PRO   C  1 225 ? -1.891  -57.799 -89.875  1.00 21.90  ? 526  PRO   C N   1 
ATOM   8562  C  CA  . PRO   C  1 225 ? -1.322  -57.214 -91.084  1.00 26.15  ? 526  PRO   C CA  1 
ATOM   8563  C  C   . PRO   C  1 225 ? -0.400  -56.081 -90.696  1.00 22.77  ? 526  PRO   C C   1 
ATOM   8564  O  O   . PRO   C  1 225 ? -0.500  -55.517 -89.604  1.00 22.92  ? 526  PRO   C O   1 
ATOM   8565  C  CB  . PRO   C  1 225 ? -2.548  -56.696 -91.845  1.00 24.48  ? 526  PRO   C CB  1 
ATOM   8566  C  CG  . PRO   C  1 225 ? -3.486  -56.326 -90.759  1.00 30.20  ? 526  PRO   C CG  1 
ATOM   8567  C  CD  . PRO   C  1 225 ? -3.282  -57.360 -89.668  1.00 26.18  ? 526  PRO   C CD  1 
ATOM   8568  N  N   . LEU   C  1 226 ? 0.517   -55.757 -91.598  1.00 23.52  ? 527  LEU   C N   1 
ATOM   8569  C  CA  . LEU   C  1 226 ? 1.305   -54.545 -91.437  1.00 25.15  ? 527  LEU   C CA  1 
ATOM   8570  C  C   . LEU   C  1 226 ? 0.466   -53.349 -91.852  1.00 28.55  ? 527  LEU   C C   1 
ATOM   8571  O  O   . LEU   C  1 226 ? -0.271  -53.406 -92.837  1.00 25.60  ? 527  LEU   C O   1 
ATOM   8572  C  CB  . LEU   C  1 226 ? 2.581   -54.606 -92.263  1.00 20.14  ? 527  LEU   C CB  1 
ATOM   8573  C  CG  . LEU   C  1 226 ? 3.632   -55.628 -91.839  1.00 23.38  ? 527  LEU   C CG  1 
ATOM   8574  C  CD1 . LEU   C  1 226 ? 4.747   -55.741 -92.880  1.00 23.25  ? 527  LEU   C CD1 1 
ATOM   8575  C  CD2 . LEU   C  1 226 ? 4.213   -55.297 -90.455  1.00 21.44  ? 527  LEU   C CD2 1 
ATOM   8576  N  N   . LEU   C  1 227 ? 0.562   -52.272 -91.076  1.00 26.06  ? 528  LEU   C N   1 
ATOM   8577  C  CA  . LEU   C  1 227 ? -0.117  -51.006 -91.349  1.00 26.05  ? 528  LEU   C CA  1 
ATOM   8578  C  C   . LEU   C  1 227 ? 1.001   -49.995 -91.522  1.00 24.29  ? 528  LEU   C C   1 
ATOM   8579  O  O   . LEU   C  1 227 ? 1.622   -49.581 -90.537  1.00 22.59  ? 528  LEU   C O   1 
ATOM   8580  C  CB  . LEU   C  1 227 ? -1.035  -50.593 -90.204  1.00 28.47  ? 528  LEU   C CB  1 
ATOM   8581  C  CG  . LEU   C  1 227 ? -2.473  -50.181 -90.493  1.00 33.85  ? 528  LEU   C CG  1 
ATOM   8582  C  CD1 . LEU   C  1 227 ? -2.941  -49.216 -89.420  1.00 31.53  ? 528  LEU   C CD1 1 
ATOM   8583  C  CD2 . LEU   C  1 227 ? -2.681  -49.624 -91.907  1.00 25.74  ? 528  LEU   C CD2 1 
ATOM   8584  N  N   . LEU   C  1 228 ? 1.263   -49.598 -92.758  1.00 24.80  ? 529  LEU   C N   1 
ATOM   8585  C  CA  . LEU   C  1 228 ? 2.496   -48.910 -93.085  1.00 22.33  ? 529  LEU   C CA  1 
ATOM   8586  C  C   . LEU   C  1 228 ? 2.186   -47.529 -93.634  1.00 26.46  ? 529  LEU   C C   1 
ATOM   8587  O  O   . LEU   C  1 228 ? 1.327   -47.373 -94.513  1.00 23.01  ? 529  LEU   C O   1 
ATOM   8588  C  CB  . LEU   C  1 228 ? 3.314   -49.712 -94.096  1.00 26.40  ? 529  LEU   C CB  1 
ATOM   8589  C  CG  . LEU   C  1 228 ? 3.674   -51.123 -93.655  1.00 24.23  ? 529  LEU   C CG  1 
ATOM   8590  C  CD1 . LEU   C  1 228 ? 4.518   -51.781 -94.700  1.00 21.91  ? 529  LEU   C CD1 1 
ATOM   8591  C  CD2 . LEU   C  1 228 ? 4.389   -51.129 -92.310  1.00 22.44  ? 529  LEU   C CD2 1 
ATOM   8592  N  N   . GLN   C  1 229 ? 2.907   -46.537 -93.129  1.00 24.77  ? 530  GLN   C N   1 
ATOM   8593  C  CA  . GLN   C  1 229 ? 2.678   -45.149 -93.484  1.00 23.50  ? 530  GLN   C CA  1 
ATOM   8594  C  C   . GLN   C  1 229 ? 3.966   -44.588 -94.052  1.00 24.26  ? 530  GLN   C C   1 
ATOM   8595  O  O   . GLN   C  1 229 ? 5.004   -44.594 -93.379  1.00 24.11  ? 530  GLN   C O   1 
ATOM   8596  C  CB  . GLN   C  1 229 ? 2.218   -44.337 -92.270  1.00 26.83  ? 530  GLN   C CB  1 
ATOM   8597  C  CG  . GLN   C  1 229 ? 2.326   -42.840 -92.470  1.00 27.11  ? 530  GLN   C CG  1 
ATOM   8598  C  CD  . GLN   C  1 229 ? 1.876   -42.049 -91.265  1.00 31.08  ? 530  GLN   C CD  1 
ATOM   8599  O  OE1 . GLN   C  1 229 ? 1.952   -42.519 -90.131  1.00 33.49  ? 530  GLN   C OE1 1 
ATOM   8600  N  NE2 . GLN   C  1 229 ? 1.392   -40.842 -91.509  1.00 36.42  ? 530  GLN   C NE2 1 
ATOM   8601  N  N   . ALA   C  1 230 ? 3.896   -44.123 -95.289  1.00 24.42  ? 531  ALA   C N   1 
ATOM   8602  C  CA  . ALA   C  1 230 ? 5.031   -43.538 -95.980  1.00 27.29  ? 531  ALA   C CA  1 
ATOM   8603  C  C   . ALA   C  1 230 ? 4.749   -42.068 -96.233  1.00 29.23  ? 531  ALA   C C   1 
ATOM   8604  O  O   . ALA   C  1 230 ? 3.658   -41.710 -96.700  1.00 26.52  ? 531  ALA   C O   1 
ATOM   8605  C  CB  . ALA   C  1 230 ? 5.292   -44.258 -97.307  1.00 21.92  ? 531  ALA   C CB  1 
ATOM   8606  N  N   . ASN   C  1 231 ? 5.726   -41.223 -95.908  1.00 28.20  ? 532  ASN   C N   1 
ATOM   8607  C  CA  . ASN   C  1 231 ? 5.701   -39.826 -96.328  1.00 25.07  ? 532  ASN   C CA  1 
ATOM   8608  C  C   . ASN   C  1 231 ? 4.477   -39.094 -95.787  1.00 27.28  ? 532  ASN   C C   1 
ATOM   8609  O  O   . ASN   C  1 231 ? 3.972   -38.157 -96.408  1.00 28.52  ? 532  ASN   C O   1 
ATOM   8610  C  CB  . ASN   C  1 231 ? 5.763   -39.724 -97.856  1.00 31.21  ? 532  ASN   C CB  1 
ATOM   8611  C  CG  . ASN   C  1 231 ? 6.324   -38.408 -98.322  1.00 40.22  ? 532  ASN   C CG  1 
ATOM   8612  O  OD1 . ASN   C  1 231 ? 7.336   -37.934 -97.804  1.00 37.49  ? 532  ASN   C OD1 1 
ATOM   8613  N  ND2 . ASN   C  1 231 ? 5.652   -37.788 -99.290  1.00 40.05  ? 532  ASN   C ND2 1 
ATOM   8614  N  N   . GLY   C  1 232 ? 4.005   -39.489 -94.607  1.00 29.95  ? 533  GLY   C N   1 
ATOM   8615  C  CA  . GLY   C  1 232 ? 2.867   -38.836 -93.999  1.00 33.62  ? 533  GLY   C CA  1 
ATOM   8616  C  C   . GLY   C  1 232 ? 1.535   -39.143 -94.639  1.00 34.19  ? 533  GLY   C C   1 
ATOM   8617  O  O   . GLY   C  1 232 ? 0.529   -38.544 -94.243  1.00 35.70  ? 533  GLY   C O   1 
ATOM   8618  N  N   . ASN   C  1 233 ? 1.493   -40.041 -95.623  1.00 30.80  ? 534  ASN   C N   1 
ATOM   8619  C  CA  . ASN   C  1 233 ? 0.233   -40.445 -96.224  1.00 27.95  ? 534  ASN   C CA  1 
ATOM   8620  C  C   . ASN   C  1 233 ? -0.530  -41.371 -95.282  1.00 29.38  ? 534  ASN   C C   1 
ATOM   8621  O  O   . ASN   C  1 233 ? -0.001  -41.854 -94.283  1.00 28.43  ? 534  ASN   C O   1 
ATOM   8622  C  CB  . ASN   C  1 233 ? 0.485   -41.126 -97.566  1.00 35.39  ? 534  ASN   C CB  1 
ATOM   8623  C  CG  . ASN   C  1 233 ? 1.072   -40.172 -98.582  1.00 34.77  ? 534  ASN   C CG  1 
ATOM   8624  O  OD1 . ASN   C  1 233 ? 0.603   -39.048 -98.714  1.00 33.76  ? 534  ASN   C OD1 1 
ATOM   8625  N  ND2 . ASN   C  1 233 ? 2.120   -40.598 -99.270  1.00 36.64  ? 534  ASN   C ND2 1 
ATOM   8626  N  N   . ASP   C  1 234 ? -1.801  -41.610 -95.600  1.00 30.18  ? 535  ASP   C N   1 
ATOM   8627  C  CA  . ASP   C  1 234 ? -2.570  -42.541 -94.793  1.00 34.85  ? 535  ASP   C CA  1 
ATOM   8628  C  C   . ASP   C  1 234 ? -1.886  -43.907 -94.806  1.00 32.80  ? 535  ASP   C C   1 
ATOM   8629  O  O   . ASP   C  1 234 ? -1.253  -44.285 -95.790  1.00 29.17  ? 535  ASP   C O   1 
ATOM   8630  C  CB  . ASP   C  1 234 ? -4.001  -42.675 -95.306  1.00 34.98  ? 535  ASP   C CB  1 
ATOM   8631  C  CG  . ASP   C  1 234 ? -4.811  -41.412 -95.123  1.00 34.95  ? 535  ASP   C CG  1 
ATOM   8632  O  OD1 . ASP   C  1 234 ? -5.897  -41.316 -95.726  1.00 37.54  ? 535  ASP   C OD1 1 
ATOM   8633  O  OD2 . ASP   C  1 234 ? -4.364  -40.511 -94.386  1.00 37.50  ? 535  ASP   C OD2 1 
ATOM   8634  N  N   . PRO   C  1 235 ? -1.968  -44.656 -93.720  1.00 31.24  ? 536  PRO   C N   1 
ATOM   8635  C  CA  . PRO   C  1 235 ? -1.306  -45.962 -93.696  1.00 26.95  ? 536  PRO   C CA  1 
ATOM   8636  C  C   . PRO   C  1 235 ? -2.067  -46.970 -94.537  1.00 26.51  ? 536  PRO   C C   1 
ATOM   8637  O  O   . PRO   C  1 235 ? -3.278  -46.859 -94.734  1.00 26.06  ? 536  PRO   C O   1 
ATOM   8638  C  CB  . PRO   C  1 235 ? -1.321  -46.339 -92.208  1.00 24.49  ? 536  PRO   C CB  1 
ATOM   8639  C  CG  . PRO   C  1 235 ? -2.538  -45.609 -91.665  1.00 23.59  ? 536  PRO   C CG  1 
ATOM   8640  C  CD  . PRO   C  1 235 ? -2.544  -44.295 -92.414  1.00 30.86  ? 536  PRO   C CD  1 
ATOM   8641  N  N   . GLU   C  1 236 ? -1.341  -47.969 -95.031  1.00 23.07  ? 537  GLU   C N   1 
ATOM   8642  C  CA  . GLU   C  1 236 ? -1.921  -48.995 -95.882  1.00 23.43  ? 537  GLU   C CA  1 
ATOM   8643  C  C   . GLU   C  1 236 ? -1.645  -50.384 -95.314  1.00 23.57  ? 537  GLU   C C   1 
ATOM   8644  O  O   . GLU   C  1 236 ? -0.585  -50.640 -94.735  1.00 26.56  ? 537  GLU   C O   1 
ATOM   8645  C  CB  . GLU   C  1 236 ? -1.370  -48.876 -97.320  1.00 26.33  ? 537  GLU   C CB  1 
ATOM   8646  C  CG  . GLU   C  1 236 ? -1.535  -47.478 -97.918  1.00 30.56  ? 537  GLU   C CG  1 
ATOM   8647  C  CD  . GLU   C  1 236 ? -0.671  -47.254 -99.159  1.00 38.01  ? 537  GLU   C CD  1 
ATOM   8648  O  OE1 . GLU   C  1 236 ? -0.418  -48.236 -99.887  1.00 35.70  ? 537  GLU   C OE1 1 
ATOM   8649  O  OE2 . GLU   C  1 236 ? -0.231  -46.098 -99.393  1.00 36.30  ? 537  GLU   C OE2 1 
ATOM   8650  N  N   . LEU   C  1 237 ? -2.612  -51.284 -95.507  1.00 24.92  ? 538  LEU   C N   1 
ATOM   8651  C  CA  . LEU   C  1 237 ? -2.531  -52.646 -94.996  1.00 23.86  ? 538  LEU   C CA  1 
ATOM   8652  C  C   . LEU   C  1 237 ? -1.747  -53.554 -95.930  1.00 31.21  ? 538  LEU   C C   1 
ATOM   8653  O  O   . LEU   C  1 237 ? -1.886  -53.485 -97.155  1.00 27.80  ? 538  LEU   C O   1 
ATOM   8654  C  CB  . LEU   C  1 237 ? -3.930  -53.234 -94.815  1.00 23.88  ? 538  LEU   C CB  1 
ATOM   8655  C  CG  . LEU   C  1 237 ? -4.807  -52.624 -93.735  1.00 32.22  ? 538  LEU   C CG  1 
ATOM   8656  C  CD1 . LEU   C  1 237 ? -6.179  -53.216 -93.882  1.00 28.11  ? 538  LEU   C CD1 1 
ATOM   8657  C  CD2 . LEU   C  1 237 ? -4.224  -52.923 -92.347  1.00 36.89  ? 538  LEU   C CD2 1 
ATOM   8658  N  N   . PHE   C  1 238 ? -0.946  -54.437 -95.342  1.00 31.57  ? 539  PHE   C N   1 
ATOM   8659  C  CA  . PHE   C  1 238 ? -0.243  -55.463 -96.103  1.00 29.15  ? 539  PHE   C CA  1 
ATOM   8660  C  C   . PHE   C  1 238 ? -0.173  -56.722 -95.263  1.00 34.80  ? 539  PHE   C C   1 
ATOM   8661  O  O   . PHE   C  1 238 ? 0.130   -56.665 -94.063  1.00 31.68  ? 539  PHE   C O   1 
ATOM   8662  C  CB  . PHE   C  1 238 ? 1.177   -55.046 -96.472  1.00 24.68  ? 539  PHE   C CB  1 
ATOM   8663  C  CG  . PHE   C  1 238 ? 1.246   -53.799 -97.276  1.00 30.21  ? 539  PHE   C CG  1 
ATOM   8664  C  CD1 . PHE   C  1 238 ? 1.342   -52.571 -96.656  1.00 31.31  ? 539  PHE   C CD1 1 
ATOM   8665  C  CD2 . PHE   C  1 238 ? 1.221   -53.850 -98.656  1.00 23.55  ? 539  PHE   C CD2 1 
ATOM   8666  C  CE1 . PHE   C  1 238 ? 1.403   -51.415 -97.390  1.00 31.11  ? 539  PHE   C CE1 1 
ATOM   8667  C  CE2 . PHE   C  1 238 ? 1.285   -52.692 -99.399  1.00 30.58  ? 539  PHE   C CE2 1 
ATOM   8668  C  CZ  . PHE   C  1 238 ? 1.379   -51.474 -98.770  1.00 38.15  ? 539  PHE   C CZ  1 
ATOM   8669  N  N   . GLN   C  1 239 ? -0.435  -57.854 -95.895  1.00 28.14  ? 540  GLN   C N   1 
ATOM   8670  C  CA  . GLN   C  1 239 ? -0.326  -59.137 -95.223  1.00 34.84  ? 540  GLN   C CA  1 
ATOM   8671  C  C   . GLN   C  1 239 ? 1.096   -59.650 -95.401  1.00 31.13  ? 540  GLN   C C   1 
ATOM   8672  O  O   . GLN   C  1 239 ? 1.548   -59.847 -96.535  1.00 32.47  ? 540  GLN   C O   1 
ATOM   8673  C  CB  . GLN   C  1 239 ? -1.343  -60.131 -95.777  1.00 40.67  ? 540  GLN   C CB  1 
ATOM   8674  C  CG  . GLN   C  1 239 ? -1.104  -61.583 -95.357  1.00 47.31  ? 540  GLN   C CG  1 
ATOM   8675  C  CD  . GLN   C  1 239 ? -1.165  -62.547 -96.545  1.00 54.96  ? 540  GLN   C CD  1 
ATOM   8676  O  OE1 . GLN   C  1 239 ? -0.355  -62.464 -97.485  1.00 48.27  ? 540  GLN   C OE1 1 
ATOM   8677  N  NE2 . GLN   C  1 239 ? -2.127  -63.459 -96.508  1.00 51.63  ? 540  GLN   C NE2 1 
ATOM   8678  N  N   . ILE   C  1 240 ? 1.808   -59.822 -94.290  1.00 24.34  ? 541  ILE   C N   1 
ATOM   8679  C  CA  . ILE   C  1 240 ? 3.108   -60.499 -94.351  1.00 26.19  ? 541  ILE   C CA  1 
ATOM   8680  C  C   . ILE   C  1 240 ? 2.902   -61.890 -94.928  1.00 34.81  ? 541  ILE   C C   1 
ATOM   8681  O  O   . ILE   C  1 240 ? 1.996   -62.612 -94.471  1.00 32.47  ? 541  ILE   C O   1 
ATOM   8682  C  CB  . ILE   C  1 240 ? 3.737   -60.602 -92.956  1.00 23.63  ? 541  ILE   C CB  1 
ATOM   8683  C  CG1 . ILE   C  1 240 ? 3.856   -59.231 -92.298  1.00 30.63  ? 541  ILE   C CG1 1 
ATOM   8684  C  CG2 . ILE   C  1 240 ? 5.096   -61.249 -93.054  1.00 24.64  ? 541  ILE   C CG2 1 
ATOM   8685  C  CD1 . ILE   C  1 240 ? 4.415   -59.315 -90.880  1.00 32.13  ? 541  ILE   C CD1 1 
ATOM   8686  N  N   . PRO   C  1 241 ? 3.688   -62.317 -95.915  1.00 32.44  ? 542  PRO   C N   1 
ATOM   8687  C  CA  . PRO   C  1 241 ? 3.545   -63.676 -96.441  1.00 32.57  ? 542  PRO   C CA  1 
ATOM   8688  C  C   . PRO   C  1 241 ? 3.736   -64.694 -95.333  1.00 29.52  ? 542  PRO   C C   1 
ATOM   8689  O  O   . PRO   C  1 241 ? 4.739   -64.640 -94.603  1.00 22.87  ? 542  PRO   C O   1 
ATOM   8690  C  CB  . PRO   C  1 241 ? 4.662   -63.765 -97.486  1.00 28.11  ? 542  PRO   C CB  1 
ATOM   8691  C  CG  . PRO   C  1 241 ? 4.883   -62.351 -97.888  1.00 28.27  ? 542  PRO   C CG  1 
ATOM   8692  C  CD  . PRO   C  1 241 ? 4.759   -61.588 -96.606  1.00 29.12  ? 542  PRO   C CD  1 
ATOM   8693  N  N   . PRO   C  1 242 ? 2.784   -65.617 -95.162  1.00 25.47  ? 543  PRO   C N   1 
ATOM   8694  C  CA  . PRO   C  1 242 ? 2.825   -66.496 -93.980  1.00 27.13  ? 543  PRO   C CA  1 
ATOM   8695  C  C   . PRO   C  1 242 ? 4.077   -67.340 -93.899  1.00 33.13  ? 543  PRO   C C   1 
ATOM   8696  O  O   . PRO   C  1 242 ? 4.532   -67.655 -92.790  1.00 36.38  ? 543  PRO   C O   1 
ATOM   8697  C  CB  . PRO   C  1 242 ? 1.562   -67.354 -94.136  1.00 35.80  ? 543  PRO   C CB  1 
ATOM   8698  C  CG  . PRO   C  1 242 ? 0.642   -66.495 -94.967  1.00 40.75  ? 543  PRO   C CG  1 
ATOM   8699  C  CD  . PRO   C  1 242 ? 1.555   -65.812 -95.951  1.00 38.42  ? 543  PRO   C CD  1 
ATOM   8700  N  N   . GLU   C  1 243 ? 4.674   -67.680 -95.040  1.00 31.70  ? 544  GLU   C N   1 
ATOM   8701  C  CA  . GLU   C  1 243 ? 5.903   -68.459 -95.020  1.00 30.66  ? 544  GLU   C CA  1 
ATOM   8702  C  C   . GLU   C  1 243 ? 7.075   -67.673 -94.446  1.00 30.13  ? 544  GLU   C C   1 
ATOM   8703  O  O   . GLU   C  1 243 ? 8.105   -68.273 -94.134  1.00 31.25  ? 544  GLU   C O   1 
ATOM   8704  C  CB  . GLU   C  1 243 ? 6.243   -68.952 -96.431  1.00 31.22  ? 544  GLU   C CB  1 
ATOM   8705  C  CG  . GLU   C  1 243 ? 6.600   -67.840 -97.413  1.00 34.12  ? 544  GLU   C CG  1 
ATOM   8706  C  CD  . GLU   C  1 243 ? 5.391   -67.302 -98.168  1.00 37.57  ? 544  GLU   C CD  1 
ATOM   8707  O  OE1 . GLU   C  1 243 ? 4.247   -67.542 -97.728  1.00 37.69  ? 544  GLU   C OE1 1 
ATOM   8708  O  OE2 . GLU   C  1 243 ? 5.586   -66.654 -99.222  1.00 44.50  ? 544  GLU   C OE2 1 
ATOM   8709  N  N   . LEU   C  1 244 ? 6.961   -66.353 -94.310  1.00 26.15  ? 545  LEU   C N   1 
ATOM   8710  C  CA  . LEU   C  1 244 ? 8.025   -65.595 -93.665  1.00 28.53  ? 545  LEU   C CA  1 
ATOM   8711  C  C   . LEU   C  1 244 ? 7.825   -65.457 -92.161  1.00 27.63  ? 545  LEU   C C   1 
ATOM   8712  O  O   . LEU   C  1 244 ? 8.714   -64.939 -91.480  1.00 26.45  ? 545  LEU   C O   1 
ATOM   8713  C  CB  . LEU   C  1 244 ? 8.154   -64.194 -94.268  1.00 25.67  ? 545  LEU   C CB  1 
ATOM   8714  C  CG  . LEU   C  1 244 ? 8.371   -64.072 -95.782  1.00 29.74  ? 545  LEU   C CG  1 
ATOM   8715  C  CD1 . LEU   C  1 244 ? 8.514   -62.611 -96.116  1.00 31.21  ? 545  LEU   C CD1 1 
ATOM   8716  C  CD2 . LEU   C  1 244 ? 9.589   -64.838 -96.223  1.00 28.48  ? 545  LEU   C CD2 1 
ATOM   8717  N  N   . VAL   C  1 245 ? 6.695   -65.894 -91.627  1.00 22.86  ? 546  VAL   C N   1 
ATOM   8718  C  CA  . VAL   C  1 245 ? 6.395   -65.721 -90.206  1.00 26.09  ? 546  VAL   C CA  1 
ATOM   8719  C  C   . VAL   C  1 245 ? 6.687   -67.047 -89.520  1.00 28.50  ? 546  VAL   C C   1 
ATOM   8720  O  O   . VAL   C  1 245 ? 5.873   -67.974 -89.547  1.00 26.05  ? 546  VAL   C O   1 
ATOM   8721  C  CB  . VAL   C  1 245 ? 4.953   -65.270 -89.975  1.00 32.16  ? 546  VAL   C CB  1 
ATOM   8722  C  CG1 . VAL   C  1 245 ? 4.661   -65.215 -88.476  1.00 30.42  ? 546  VAL   C CG1 1 
ATOM   8723  C  CG2 . VAL   C  1 245 ? 4.724   -63.910 -90.613  1.00 24.59  ? 546  VAL   C CG2 1 
ATOM   8724  N  N   . LEU   C  1 246 ? 7.853   -67.145 -88.905  1.00 25.46  ? 547  LEU   C N   1 
ATOM   8725  C  CA  . LEU   C  1 246 ? 8.224   -68.368 -88.219  1.00 27.17  ? 547  LEU   C CA  1 
ATOM   8726  C  C   . LEU   C  1 246 ? 7.542   -68.416 -86.855  1.00 25.93  ? 547  LEU   C C   1 
ATOM   8727  O  O   . LEU   C  1 246 ? 7.663   -67.479 -86.061  1.00 22.89  ? 547  LEU   C O   1 
ATOM   8728  C  CB  . LEU   C  1 246 ? 9.741   -68.432 -88.068  1.00 25.27  ? 547  LEU   C CB  1 
ATOM   8729  C  CG  . LEU   C  1 246 ? 10.258  -69.653 -87.322  1.00 31.33  ? 547  LEU   C CG  1 
ATOM   8730  C  CD1 . LEU   C  1 246 ? 9.760   -70.906 -88.015  1.00 33.45  ? 547  LEU   C CD1 1 
ATOM   8731  C  CD2 . LEU   C  1 246 ? 11.765  -69.615 -87.311  1.00 35.16  ? 547  LEU   C CD2 1 
ATOM   8732  N  N   . GLU   C  1 247 ? 6.810   -69.493 -86.588  1.00 25.72  ? 548  GLU   C N   1 
ATOM   8733  C  CA  . GLU   C  1 247 ? 6.162   -69.680 -85.297  1.00 26.01  ? 548  GLU   C CA  1 
ATOM   8734  C  C   . GLU   C  1 247 ? 6.623   -70.979 -84.656  1.00 31.00  ? 548  GLU   C C   1 
ATOM   8735  O  O   . GLU   C  1 247 ? 7.113   -71.892 -85.326  1.00 28.18  ? 548  GLU   C O   1 
ATOM   8736  C  CB  . GLU   C  1 247 ? 4.637   -69.683 -85.435  1.00 31.04  ? 548  GLU   C CB  1 
ATOM   8737  C  CG  . GLU   C  1 247 ? 4.102   -68.394 -86.036  1.00 31.18  ? 548  GLU   C CG  1 
ATOM   8738  C  CD  . GLU   C  1 247 ? 2.600   -68.402 -86.198  1.00 37.65  ? 548  GLU   C CD  1 
ATOM   8739  O  OE1 . GLU   C  1 247 ? 2.085   -69.186 -87.019  1.00 40.86  ? 548  GLU   C OE1 1 
ATOM   8740  O  OE2 . GLU   C  1 247 ? 1.929   -67.628 -85.492  1.00 37.88  ? 548  GLU   C OE2 1 
ATOM   8741  N  N   . VAL   C  1 248 ? 6.466   -71.047 -83.338  1.00 30.64  ? 549  VAL   C N   1 
ATOM   8742  C  CA  . VAL   C  1 248 ? 6.868   -72.195 -82.538  1.00 26.21  ? 549  VAL   C CA  1 
ATOM   8743  C  C   . VAL   C  1 248 ? 5.642   -72.663 -81.764  1.00 23.75  ? 549  VAL   C C   1 
ATOM   8744  O  O   . VAL   C  1 248 ? 5.114   -71.917 -80.938  1.00 27.56  ? 549  VAL   C O   1 
ATOM   8745  C  CB  . VAL   C  1 248 ? 8.010   -71.850 -81.565  1.00 26.36  ? 549  VAL   C CB  1 
ATOM   8746  C  CG1 . VAL   C  1 248 ? 8.401   -73.077 -80.713  1.00 27.98  ? 549  VAL   C CG1 1 
ATOM   8747  C  CG2 . VAL   C  1 248 ? 9.206   -71.272 -82.308  1.00 25.95  ? 549  VAL   C CG2 1 
ATOM   8748  N  N   . PRO   C  1 249 ? 5.146   -73.867 -81.995  1.00 27.82  ? 550  PRO   C N   1 
ATOM   8749  C  CA  . PRO   C  1 249 ? 4.094   -74.398 -81.124  1.00 29.00  ? 550  PRO   C CA  1 
ATOM   8750  C  C   . PRO   C  1 249 ? 4.684   -74.764 -79.773  1.00 30.11  ? 550  PRO   C C   1 
ATOM   8751  O  O   . PRO   C  1 249 ? 5.776   -75.330 -79.691  1.00 29.20  ? 550  PRO   C O   1 
ATOM   8752  C  CB  . PRO   C  1 249 ? 3.588   -75.629 -81.880  1.00 31.67  ? 550  PRO   C CB  1 
ATOM   8753  C  CG  . PRO   C  1 249 ? 4.749   -76.044 -82.744  1.00 34.93  ? 550  PRO   C CG  1 
ATOM   8754  C  CD  . PRO   C  1 249 ? 5.575   -74.821 -83.033  1.00 27.84  ? 550  PRO   C CD  1 
ATOM   8755  N  N   . ILE   C  1 250 ? 3.982   -74.407 -78.706  1.00 25.84  ? 551  ILE   C N   1 
ATOM   8756  C  CA  . ILE   C  1 250 ? 4.550   -74.535 -77.367  1.00 30.81  ? 551  ILE   C CA  1 
ATOM   8757  C  C   . ILE   C  1 250 ? 4.124   -75.866 -76.769  1.00 31.14  ? 551  ILE   C C   1 
ATOM   8758  O  O   . ILE   C  1 250 ? 2.929   -76.133 -76.590  1.00 32.63  ? 551  ILE   C O   1 
ATOM   8759  C  CB  . ILE   C  1 250 ? 4.153   -73.365 -76.456  1.00 28.73  ? 551  ILE   C CB  1 
ATOM   8760  C  CG1 . ILE   C  1 250 ? 4.536   -72.028 -77.094  1.00 23.98  ? 551  ILE   C CG1 1 
ATOM   8761  C  CG2 . ILE   C  1 250 ? 4.847   -73.523 -75.085  1.00 28.97  ? 551  ILE   C CG2 1 
ATOM   8762  C  CD1 . ILE   C  1 250 ? 5.986   -71.933 -77.536  1.00 22.89  ? 551  ILE   C CD1 1 
ATOM   8763  N  N   . ARG   C  1 251 ? 5.106   -76.700 -76.472  1.00 26.20  ? 552  ARG   C N   1 
ATOM   8764  C  CA  . ARG   C  1 251 ? 4.900   -77.949 -75.766  1.00 31.35  ? 552  ARG   C CA  1 
ATOM   8765  C  C   . ARG   C  1 251 ? 5.879   -78.000 -74.597  1.00 27.10  ? 552  ARG   C C   1 
ATOM   8766  O  O   . ARG   C  1 251 ? 6.767   -77.152 -74.465  1.00 30.81  ? 552  ARG   C O   1 
ATOM   8767  C  CB  . ARG   C  1 251 ? 5.063   -79.158 -76.703  1.00 32.91  ? 552  ARG   C CB  1 
ATOM   8768  C  CG  . ARG   C  1 251 ? 6.416   -79.290 -77.387  1.00 34.41  ? 552  ARG   C CG  1 
ATOM   8769  C  CD  . ARG   C  1 251 ? 6.590   -78.363 -78.602  1.00 34.90  ? 552  ARG   C CD  1 
ATOM   8770  N  NE  . ARG   C  1 251 ? 7.649   -78.852 -79.484  1.00 41.26  ? 552  ARG   C NE  1 
ATOM   8771  C  CZ  . ARG   C  1 251 ? 8.160   -78.174 -80.511  1.00 41.03  ? 552  ARG   C CZ  1 
ATOM   8772  N  NH1 . ARG   C  1 251 ? 9.114   -78.719 -81.254  1.00 36.63  ? 552  ARG   C NH1 1 
ATOM   8773  N  NH2 . ARG   C  1 251 ? 7.725   -76.954 -80.800  1.00 32.99  ? 552  ARG   C NH2 1 
ATOM   8774  N  N   . HIS   C  1 252 ? 5.705   -79.000 -73.737  1.00 27.99  ? 553  HIS   C N   1 
ATOM   8775  C  CA  . HIS   C  1 252 ? 6.486   -79.119 -72.525  1.00 32.85  ? 553  HIS   C CA  1 
ATOM   8776  C  C   . HIS   C  1 252 ? 7.210   -80.464 -72.505  1.00 37.07  ? 553  HIS   C C   1 
ATOM   8777  O  O   . HIS   C  1 252 ? 6.636   -81.482 -72.905  1.00 32.62  ? 553  HIS   C O   1 
ATOM   8778  C  CB  . HIS   C  1 252 ? 5.565   -78.982 -71.304  1.00 28.31  ? 553  HIS   C CB  1 
ATOM   8779  C  CG  . HIS   C  1 252 ? 6.281   -78.867 -69.992  1.00 31.32  ? 553  HIS   C CG  1 
ATOM   8780  N  ND1 . HIS   C  1 252 ? 6.845   -79.950 -69.353  1.00 33.48  ? 553  HIS   C ND1 1 
ATOM   8781  C  CD2 . HIS   C  1 252 ? 6.468   -77.807 -69.170  1.00 31.71  ? 553  HIS   C CD2 1 
ATOM   8782  C  CE1 . HIS   C  1 252 ? 7.373   -79.556 -68.205  1.00 34.24  ? 553  HIS   C CE1 1 
ATOM   8783  N  NE2 . HIS   C  1 252 ? 7.160   -78.260 -68.072  1.00 31.24  ? 553  HIS   C NE2 1 
ATOM   8784  N  N   . PRO   C  1 253 ? 8.472   -80.499 -72.075  1.00 33.34  ? 554  PRO   C N   1 
ATOM   8785  C  CA  . PRO   C  1 253 ? 9.215   -81.768 -72.104  1.00 33.15  ? 554  PRO   C CA  1 
ATOM   8786  C  C   . PRO   C  1 253 ? 8.627   -82.836 -71.203  1.00 40.33  ? 554  PRO   C C   1 
ATOM   8787  O  O   . PRO   C  1 253 ? 8.835   -84.023 -71.469  1.00 41.65  ? 554  PRO   C O   1 
ATOM   8788  C  CB  . PRO   C  1 253 ? 10.618  -81.361 -71.640  1.00 38.55  ? 554  PRO   C CB  1 
ATOM   8789  C  CG  . PRO   C  1 253 ? 10.389  -80.121 -70.813  1.00 38.10  ? 554  PRO   C CG  1 
ATOM   8790  C  CD  . PRO   C  1 253 ? 9.266   -79.401 -71.499  1.00 32.72  ? 554  PRO   C CD  1 
ATOM   8791  N  N   . LYS   C  1 254 ? 7.888   -82.468 -70.160  1.00 42.57  ? 555  LYS   C N   1 
ATOM   8792  C  CA  . LYS   C  1 254 ? 7.351   -83.446 -69.224  1.00 46.61  ? 555  LYS   C CA  1 
ATOM   8793  C  C   . LYS   C  1 254 ? 5.838   -83.553 -69.255  1.00 47.01  ? 555  LYS   C C   1 
ATOM   8794  O  O   . LYS   C  1 254 ? 5.297   -84.650 -69.088  1.00 44.26  ? 555  LYS   C O   1 
ATOM   8795  C  CB  . LYS   C  1 254 ? 7.795   -83.110 -67.797  1.00 60.14  ? 555  LYS   C CB  1 
ATOM   8796  C  CG  . LYS   C  1 254 ? 9.298   -83.038 -67.632  1.00 71.59  ? 555  LYS   C CG  1 
ATOM   8797  C  CD  . LYS   C  1 254 ? 9.959   -84.341 -68.053  1.00 82.60  ? 555  LYS   C CD  1 
ATOM   8798  C  CE  . LYS   C  1 254 ? 11.459  -84.157 -68.189  1.00 88.26  ? 555  LYS   C CE  1 
ATOM   8799  N  NZ  . LYS   C  1 254 ? 11.981  -83.288 -67.093  1.00 89.13  ? 555  LYS   C NZ  1 
ATOM   8800  N  N   . PHE   C  1 255 ? 5.139   -82.443 -69.452  1.00 41.43  ? 556  PHE   C N   1 
ATOM   8801  C  CA  . PHE   C  1 255 ? 3.680   -82.428 -69.388  1.00 39.55  ? 556  PHE   C CA  1 
ATOM   8802  C  C   . PHE   C  1 255 ? 3.136   -82.627 -70.795  1.00 39.19  ? 556  PHE   C C   1 
ATOM   8803  O  O   . PHE   C  1 255 ? 3.138   -81.705 -71.613  1.00 33.96  ? 556  PHE   C O   1 
ATOM   8804  C  CB  . PHE   C  1 255 ? 3.195   -81.127 -68.763  1.00 42.94  ? 556  PHE   C CB  1 
ATOM   8805  C  CG  . PHE   C  1 255 ? 3.642   -80.948 -67.352  1.00 40.54  ? 556  PHE   C CG  1 
ATOM   8806  C  CD1 . PHE   C  1 255 ? 3.931   -79.689 -66.851  1.00 43.49  ? 556  PHE   C CD1 1 
ATOM   8807  C  CD2 . PHE   C  1 255 ? 3.781   -82.049 -66.519  1.00 40.56  ? 556  PHE   C CD2 1 
ATOM   8808  C  CE1 . PHE   C  1 255 ? 4.346   -79.528 -65.530  1.00 40.49  ? 556  PHE   C CE1 1 
ATOM   8809  C  CE2 . PHE   C  1 255 ? 4.197   -81.891 -65.201  1.00 45.67  ? 556  PHE   C CE2 1 
ATOM   8810  C  CZ  . PHE   C  1 255 ? 4.482   -80.630 -64.711  1.00 39.99  ? 556  PHE   C CZ  1 
ATOM   8811  N  N   . GLU   C  1 256 ? 2.672   -83.847 -71.075  1.00 41.32  ? 557  GLU   C N   1 
ATOM   8812  C  CA  . GLU   C  1 256 ? 2.164   -84.163 -72.404  1.00 42.68  ? 557  GLU   C CA  1 
ATOM   8813  C  C   . GLU   C  1 256 ? 0.977   -83.283 -72.757  1.00 41.71  ? 557  GLU   C C   1 
ATOM   8814  O  O   . GLU   C  1 256 ? 0.749   -82.980 -73.933  1.00 44.31  ? 557  GLU   C O   1 
ATOM   8815  C  CB  . GLU   C  1 256 ? 1.772   -85.641 -72.465  1.00 46.41  ? 557  GLU   C CB  1 
ATOM   8816  C  CG  . GLU   C  1 256 ? 1.796   -86.240 -73.852  1.00 70.60  ? 557  GLU   C CG  1 
ATOM   8817  C  CD  . GLU   C  1 256 ? 0.410   -86.615 -74.362  1.00 92.03  ? 557  GLU   C CD  1 
ATOM   8818  O  OE1 . GLU   C  1 256 ? -0.042  -86.015 -75.361  1.00 97.03  ? 557  GLU   C OE1 1 
ATOM   8819  O  OE2 . GLU   C  1 256 ? -0.233  -87.505 -73.762  1.00 98.64  ? 557  GLU   C OE2 1 
ATOM   8820  N  N   . TRP   C  1 257 ? 0.217   -82.858 -71.753  1.00 40.53  ? 558  TRP   C N   1 
ATOM   8821  C  CA  . TRP   C  1 257 ? -0.981  -82.066 -71.976  1.00 42.28  ? 558  TRP   C CA  1 
ATOM   8822  C  C   . TRP   C  1 257 ? -0.689  -80.628 -72.359  1.00 36.23  ? 558  TRP   C C   1 
ATOM   8823  O  O   . TRP   C  1 257 ? -1.609  -79.928 -72.789  1.00 41.52  ? 558  TRP   C O   1 
ATOM   8824  C  CB  . TRP   C  1 257 ? -1.855  -82.074 -70.718  1.00 43.08  ? 558  TRP   C CB  1 
ATOM   8825  C  CG  . TRP   C  1 257 ? -1.095  -81.753 -69.468  1.00 36.37  ? 558  TRP   C CG  1 
ATOM   8826  C  CD1 . TRP   C  1 257 ? -0.597  -82.645 -68.567  1.00 36.99  ? 558  TRP   C CD1 1 
ATOM   8827  C  CD2 . TRP   C  1 257 ? -0.743  -80.457 -68.985  1.00 39.00  ? 558  TRP   C CD2 1 
ATOM   8828  N  NE1 . TRP   C  1 257 ? 0.049   -81.988 -67.556  1.00 36.63  ? 558  TRP   C NE1 1 
ATOM   8829  C  CE2 . TRP   C  1 257 ? -0.034  -80.641 -67.780  1.00 39.98  ? 558  TRP   C CE2 1 
ATOM   8830  C  CE3 . TRP   C  1 257 ? -0.961  -79.156 -69.449  1.00 42.36  ? 558  TRP   C CE3 1 
ATOM   8831  C  CZ2 . TRP   C  1 257 ? 0.462   -79.574 -67.030  1.00 40.29  ? 558  TRP   C CZ2 1 
ATOM   8832  C  CZ3 . TRP   C  1 257 ? -0.467  -78.092 -68.699  1.00 47.78  ? 558  TRP   C CZ3 1 
ATOM   8833  C  CH2 . TRP   C  1 257 ? 0.234   -78.311 -67.503  1.00 43.32  ? 558  TRP   C CH2 1 
ATOM   8834  N  N   . PHE   C  1 258 ? 0.548   -80.161 -72.196  1.00 34.94  ? 559  PHE   C N   1 
ATOM   8835  C  CA  . PHE   C  1 258 ? 0.818   -78.747 -72.428  1.00 35.56  ? 559  PHE   C CA  1 
ATOM   8836  C  C   . PHE   C  1 258 ? 0.493   -78.362 -73.862  1.00 39.26  ? 559  PHE   C C   1 
ATOM   8837  O  O   . PHE   C  1 258 ? -0.094  -77.302 -74.109  1.00 31.18  ? 559  PHE   C O   1 
ATOM   8838  C  CB  . PHE   C  1 258 ? 2.270   -78.419 -72.091  1.00 33.40  ? 559  PHE   C CB  1 
ATOM   8839  C  CG  . PHE   C  1 258 ? 2.505   -76.966 -71.797  1.00 34.17  ? 559  PHE   C CG  1 
ATOM   8840  C  CD1 . PHE   C  1 258 ? 2.566   -76.510 -70.484  1.00 34.46  ? 559  PHE   C CD1 1 
ATOM   8841  C  CD2 . PHE   C  1 258 ? 2.649   -76.049 -72.831  1.00 30.14  ? 559  PHE   C CD2 1 
ATOM   8842  C  CE1 . PHE   C  1 258 ? 2.782   -75.171 -70.211  1.00 34.55  ? 559  PHE   C CE1 1 
ATOM   8843  C  CE2 . PHE   C  1 258 ? 2.853   -74.720 -72.574  1.00 35.05  ? 559  PHE   C CE2 1 
ATOM   8844  C  CZ  . PHE   C  1 258 ? 2.919   -74.270 -71.257  1.00 37.42  ? 559  PHE   C CZ  1 
ATOM   8845  N  N   . LYS   C  1 259 ? 0.827   -79.231 -74.819  1.00 37.92  ? 560  LYS   C N   1 
ATOM   8846  C  CA  . LYS   C  1 259 ? 0.509   -78.947 -76.211  1.00 37.03  ? 560  LYS   C CA  1 
ATOM   8847  C  C   . LYS   C  1 259 ? -0.990  -78.775 -76.425  1.00 37.94  ? 560  LYS   C C   1 
ATOM   8848  O  O   . LYS   C  1 259 ? -1.403  -78.094 -77.371  1.00 37.50  ? 560  LYS   C O   1 
ATOM   8849  C  CB  . LYS   C  1 259 ? 1.049   -80.059 -77.111  1.00 37.00  ? 560  LYS   C CB  1 
ATOM   8850  C  CG  . LYS   C  1 259 ? 0.483   -81.436 -76.822  1.00 40.20  ? 560  LYS   C CG  1 
ATOM   8851  C  CD  . LYS   C  1 259 ? 0.716   -82.369 -78.016  1.00 40.29  ? 560  LYS   C CD  1 
ATOM   8852  C  CE  . LYS   C  1 259 ? 0.450   -83.808 -77.646  1.00 43.25  ? 560  LYS   C CE  1 
ATOM   8853  N  NZ  . LYS   C  1 259 ? 1.406   -84.275 -76.591  1.00 51.67  ? 560  LYS   C NZ  1 
ATOM   8854  N  N   . ASP   C  1 260 ? -1.812  -79.374 -75.561  1.00 39.75  ? 561  ASP   C N   1 
ATOM   8855  C  CA  . ASP   C  1 260 ? -3.262  -79.242 -75.672  1.00 50.02  ? 561  ASP   C CA  1 
ATOM   8856  C  C   . ASP   C  1 260 ? -3.747  -77.832 -75.375  1.00 47.90  ? 561  ASP   C C   1 
ATOM   8857  O  O   . ASP   C  1 260 ? -4.878  -77.492 -75.734  1.00 48.16  ? 561  ASP   C O   1 
ATOM   8858  C  CB  . ASP   C  1 260 ? -3.975  -80.203 -74.717  1.00 57.78  ? 561  ASP   C CB  1 
ATOM   8859  C  CG  . ASP   C  1 260 ? -3.797  -81.648 -75.097  1.00 67.30  ? 561  ASP   C CG  1 
ATOM   8860  O  OD1 . ASP   C  1 260 ? -3.443  -81.921 -76.264  1.00 60.72  ? 561  ASP   C OD1 1 
ATOM   8861  O  OD2 . ASP   C  1 260 ? -4.027  -82.511 -74.219  1.00 75.78  ? 561  ASP   C OD2 1 
ATOM   8862  N  N   . LEU   C  1 261 ? -2.942  -77.018 -74.695  1.00 41.90  ? 562  LEU   C N   1 
ATOM   8863  C  CA  . LEU   C  1 261 ? -3.314  -75.623 -74.505  1.00 44.72  ? 562  LEU   C CA  1 
ATOM   8864  C  C   . LEU   C  1 261 ? -3.375  -74.848 -75.816  1.00 39.86  ? 562  LEU   C C   1 
ATOM   8865  O  O   . LEU   C  1 261 ? -3.901  -73.731 -75.822  1.00 41.43  ? 562  LEU   C O   1 
ATOM   8866  C  CB  . LEU   C  1 261 ? -2.334  -74.944 -73.550  1.00 38.28  ? 562  LEU   C CB  1 
ATOM   8867  C  CG  . LEU   C  1 261 ? -2.200  -75.631 -72.189  1.00 38.60  ? 562  LEU   C CG  1 
ATOM   8868  C  CD1 . LEU   C  1 261 ? -1.027  -75.074 -71.432  1.00 32.03  ? 562  LEU   C CD1 1 
ATOM   8869  C  CD2 . LEU   C  1 261 ? -3.471  -75.463 -71.389  1.00 39.59  ? 562  LEU   C CD2 1 
ATOM   8870  N  N   . GLY   C  1 262 ? -2.854  -75.403 -76.912  1.00 35.73  ? 563  GLY   C N   1 
ATOM   8871  C  CA  . GLY   C  1 262 ? -2.897  -74.730 -78.197  1.00 37.03  ? 563  GLY   C CA  1 
ATOM   8872  C  C   . GLY   C  1 262 ? -2.022  -73.500 -78.302  1.00 37.69  ? 563  GLY   C C   1 
ATOM   8873  O  O   . GLY   C  1 262 ? -2.266  -72.641 -79.153  1.00 40.48  ? 563  GLY   C O   1 
ATOM   8874  N  N   . LEU   C  1 263 ? -1.004  -73.382 -77.462  1.00 33.28  ? 564  LEU   C N   1 
ATOM   8875  C  CA  . LEU   C  1 263 ? -0.205  -72.173 -77.452  1.00 25.17  ? 564  LEU   C CA  1 
ATOM   8876  C  C   . LEU   C  1 263 ? 0.846   -72.212 -78.545  1.00 27.14  ? 564  LEU   C C   1 
ATOM   8877  O  O   . LEU   C  1 263 ? 1.440   -73.254 -78.835  1.00 29.47  ? 564  LEU   C O   1 
ATOM   8878  C  CB  . LEU   C  1 263 ? 0.475   -71.983 -76.096  1.00 35.48  ? 564  LEU   C CB  1 
ATOM   8879  C  CG  . LEU   C  1 263 ? -0.511  -71.891 -74.940  1.00 37.20  ? 564  LEU   C CG  1 
ATOM   8880  C  CD1 . LEU   C  1 263 ? 0.235   -71.890 -73.635  1.00 32.22  ? 564  LEU   C CD1 1 
ATOM   8881  C  CD2 . LEU   C  1 263 ? -1.364  -70.641 -75.087  1.00 36.70  ? 564  LEU   C CD2 1 
ATOM   8882  N  N   . LYS   C  1 264 ? 1.099   -71.054 -79.128  1.00 30.12  ? 565  LYS   C N   1 
ATOM   8883  C  CA  . LYS   C  1 264 ? 2.239   -70.895 -80.002  1.00 28.52  ? 565  LYS   C CA  1 
ATOM   8884  C  C   . LYS   C  1 264 ? 2.751   -69.480 -79.815  1.00 32.02  ? 565  LYS   C C   1 
ATOM   8885  O  O   . LYS   C  1 264 ? 2.119   -68.655 -79.151  1.00 31.43  ? 565  LYS   C O   1 
ATOM   8886  C  CB  . LYS   C  1 264 ? 1.860   -71.184 -81.454  1.00 30.29  ? 565  LYS   C CB  1 
ATOM   8887  C  CG  . LYS   C  1 264 ? 0.794   -70.261 -82.014  1.00 29.33  ? 565  LYS   C CG  1 
ATOM   8888  C  CD  . LYS   C  1 264 ? 0.728   -70.388 -83.536  1.00 34.97  ? 565  LYS   C CD  1 
ATOM   8889  C  CE  . LYS   C  1 264 ? -0.692  -70.438 -84.053  1.00 41.36  ? 565  LYS   C CE  1 
ATOM   8890  N  NZ  . LYS   C  1 264 ? -0.692  -70.469 -85.547  1.00 48.91  ? 565  LYS   C NZ  1 
ATOM   8891  N  N   . TRP   C  1 265 ? 3.915   -69.208 -80.392  1.00 26.00  ? 566  TRP   C N   1 
ATOM   8892  C  CA  . TRP   C  1 265 ? 4.400   -67.843 -80.455  1.00 27.11  ? 566  TRP   C CA  1 
ATOM   8893  C  C   . TRP   C  1 265 ? 5.281   -67.708 -81.690  1.00 31.45  ? 566  TRP   C C   1 
ATOM   8894  O  O   . TRP   C  1 265 ? 5.690   -68.697 -82.304  1.00 32.82  ? 566  TRP   C O   1 
ATOM   8895  C  CB  . TRP   C  1 265 ? 5.148   -67.441 -79.175  1.00 20.84  ? 566  TRP   C CB  1 
ATOM   8896  C  CG  . TRP   C  1 265 ? 5.176   -65.962 -78.959  1.00 24.46  ? 566  TRP   C CG  1 
ATOM   8897  C  CD1 . TRP   C  1 265 ? 6.241   -65.103 -79.149  1.00 22.69  ? 566  TRP   C CD1 1 
ATOM   8898  C  CD2 . TRP   C  1 265 ? 4.087   -65.156 -78.527  1.00 20.99  ? 566  TRP   C CD2 1 
ATOM   8899  N  NE1 . TRP   C  1 265 ? 5.868   -63.811 -78.843  1.00 21.13  ? 566  TRP   C NE1 1 
ATOM   8900  C  CE2 . TRP   C  1 265 ? 4.550   -63.819 -78.456  1.00 19.68  ? 566  TRP   C CE2 1 
ATOM   8901  C  CE3 . TRP   C  1 265 ? 2.765   -65.434 -78.170  1.00 26.24  ? 566  TRP   C CE3 1 
ATOM   8902  C  CZ2 . TRP   C  1 265 ? 3.729   -62.770 -78.058  1.00 20.97  ? 566  TRP   C CZ2 1 
ATOM   8903  C  CZ3 . TRP   C  1 265 ? 1.959   -64.398 -77.773  1.00 24.77  ? 566  TRP   C CZ3 1 
ATOM   8904  C  CH2 . TRP   C  1 265 ? 2.440   -63.080 -77.715  1.00 22.40  ? 566  TRP   C CH2 1 
ATOM   8905  N  N   . TYR   C  1 266 ? 5.552   -66.470 -82.064  1.00 26.32  ? 567  TYR   C N   1 
ATOM   8906  C  CA  . TYR   C  1 266 ? 6.375   -66.230 -83.236  1.00 24.70  ? 567  TYR   C CA  1 
ATOM   8907  C  C   . TYR   C  1 266 ? 7.834   -66.144 -82.814  1.00 25.80  ? 567  TYR   C C   1 
ATOM   8908  O  O   . TYR   C  1 266 ? 8.143   -65.824 -81.669  1.00 23.94  ? 567  TYR   C O   1 
ATOM   8909  C  CB  . TYR   C  1 266 ? 5.940   -64.952 -83.942  1.00 23.06  ? 567  TYR   C CB  1 
ATOM   8910  C  CG  . TYR   C  1 266 ? 5.719   -63.781 -83.014  1.00 23.67  ? 567  TYR   C CG  1 
ATOM   8911  C  CD1 . TYR   C  1 266 ? 6.762   -62.930 -82.686  1.00 28.71  ? 567  TYR   C CD1 1 
ATOM   8912  C  CD2 . TYR   C  1 266 ? 4.464   -63.520 -82.482  1.00 24.10  ? 567  TYR   C CD2 1 
ATOM   8913  C  CE1 . TYR   C  1 266 ? 6.566   -61.852 -81.844  1.00 25.80  ? 567  TYR   C CE1 1 
ATOM   8914  C  CE2 . TYR   C  1 266 ? 4.253   -62.443 -81.641  1.00 23.12  ? 567  TYR   C CE2 1 
ATOM   8915  C  CZ  . TYR   C  1 266 ? 5.310   -61.614 -81.327  1.00 24.58  ? 567  TYR   C CZ  1 
ATOM   8916  O  OH  . TYR   C  1 266 ? 5.116   -60.539 -80.498  1.00 26.69  ? 567  TYR   C OH  1 
ATOM   8917  N  N   . GLY   C  1 267 ? 8.737   -66.437 -83.743  1.00 22.85  ? 568  GLY   C N   1 
ATOM   8918  C  CA  . GLY   C  1 267 ? 10.136  -66.462 -83.357  1.00 22.01  ? 568  GLY   C CA  1 
ATOM   8919  C  C   . GLY   C  1 267 ? 10.825  -65.120 -83.355  1.00 20.82  ? 568  GLY   C C   1 
ATOM   8920  O  O   . GLY   C  1 267 ? 11.873  -64.986 -82.724  1.00 28.26  ? 568  GLY   C O   1 
ATOM   8921  N  N   . LEU   C  1 268 ? 10.286  -64.133 -84.063  1.00 20.33  ? 569  LEU   C N   1 
ATOM   8922  C  CA  . LEU   C  1 268 ? 11.038  -62.909 -84.338  1.00 23.94  ? 569  LEU   C CA  1 
ATOM   8923  C  C   . LEU   C  1 268 ? 10.490  -61.729 -83.557  1.00 26.76  ? 569  LEU   C C   1 
ATOM   8924  O  O   . LEU   C  1 268 ? 9.429   -61.195 -83.924  1.00 28.20  ? 569  LEU   C O   1 
ATOM   8925  C  CB  . LEU   C  1 268 ? 11.014  -62.589 -85.833  1.00 25.62  ? 569  LEU   C CB  1 
ATOM   8926  C  CG  . LEU   C  1 268 ? 11.895  -61.412 -86.241  1.00 24.53  ? 569  LEU   C CG  1 
ATOM   8927  C  CD1 . LEU   C  1 268 ? 13.365  -61.801 -86.074  1.00 24.09  ? 569  LEU   C CD1 1 
ATOM   8928  C  CD2 . LEU   C  1 268 ? 11.604  -60.967 -87.688  1.00 23.52  ? 569  LEU   C CD2 1 
ATOM   8929  N  N   . PRO   C  1 269 ? 11.172  -61.268 -82.504  1.00 24.56  ? 570  PRO   C N   1 
ATOM   8930  C  CA  . PRO   C  1 269 ? 10.752  -60.033 -81.823  1.00 18.31  ? 570  PRO   C CA  1 
ATOM   8931  C  C   . PRO   C  1 269 ? 11.309  -58.825 -82.566  1.00 20.66  ? 570  PRO   C C   1 
ATOM   8932  O  O   . PRO   C  1 269 ? 12.523  -58.652 -82.686  1.00 24.13  ? 570  PRO   C O   1 
ATOM   8933  C  CB  . PRO   C  1 269 ? 11.367  -60.177 -80.423  1.00 18.18  ? 570  PRO   C CB  1 
ATOM   8934  C  CG  . PRO   C  1 269 ? 12.667  -60.950 -80.692  1.00 20.07  ? 570  PRO   C CG  1 
ATOM   8935  C  CD  . PRO   C  1 269 ? 12.420  -61.824 -81.940  1.00 20.16  ? 570  PRO   C CD  1 
ATOM   8936  N  N   . ALA   C  1 270 ? 10.412  -57.994 -83.086  1.00 22.01  ? 571  ALA   C N   1 
ATOM   8937  C  CA  . ALA   C  1 270 ? 10.768  -56.972 -84.077  1.00 22.12  ? 571  ALA   C CA  1 
ATOM   8938  C  C   . ALA   C  1 270 ? 10.017  -55.694 -83.719  1.00 27.21  ? 571  ALA   C C   1 
ATOM   8939  O  O   . ALA   C  1 270 ? 8.868   -55.525 -84.120  1.00 25.93  ? 571  ALA   C O   1 
ATOM   8940  C  CB  . ALA   C  1 270 ? 10.425  -57.456 -85.479  1.00 21.74  ? 571  ALA   C CB  1 
ATOM   8941  N  N   . VAL   C  1 271 ? 10.667  -54.810 -82.966  1.00 21.88  ? 572  VAL   C N   1 
ATOM   8942  C  CA  . VAL   C  1 271 ? 10.009  -53.620 -82.440  1.00 21.43  ? 572  VAL   C CA  1 
ATOM   8943  C  C   . VAL   C  1 271 ? 9.975   -52.568 -83.531  1.00 18.23  ? 572  VAL   C C   1 
ATOM   8944  O  O   . VAL   C  1 271 ? 11.001  -52.245 -84.131  1.00 20.48  ? 572  VAL   C O   1 
ATOM   8945  C  CB  . VAL   C  1 271 ? 10.733  -53.090 -81.192  1.00 20.05  ? 572  VAL   C CB  1 
ATOM   8946  C  CG1 . VAL   C  1 271 ? 10.261  -51.655 -80.867  1.00 20.87  ? 572  VAL   C CG1 1 
ATOM   8947  C  CG2 . VAL   C  1 271 ? 10.532  -54.050 -79.969  1.00 18.63  ? 572  VAL   C CG2 1 
ATOM   8948  N  N   . SER   C  1 272 ? 8.802   -52.006 -83.773  1.00 17.79  ? 573  SER   C N   1 
ATOM   8949  C  CA  . SER   C  1 272 ? 8.639   -51.167 -84.945  1.00 25.26  ? 573  SER   C CA  1 
ATOM   8950  C  C   . SER   C  1 272 ? 7.990   -49.830 -84.633  1.00 22.97  ? 573  SER   C C   1 
ATOM   8951  O  O   . SER   C  1 272 ? 7.697   -49.075 -85.564  1.00 25.03  ? 573  SER   C O   1 
ATOM   8952  C  CB  . SER   C  1 272 ? 7.831   -51.917 -86.021  1.00 23.05  ? 573  SER   C CB  1 
ATOM   8953  O  OG  . SER   C  1 272 ? 6.579   -52.373 -85.513  1.00 19.84  ? 573  SER   C OG  1 
ATOM   8954  N  N   . ASN   C  1 273 ? 7.790   -49.484 -83.359  1.00 19.61  ? 574  ASN   C N   1 
ATOM   8955  C  CA  . ASN   C  1 273 ? 7.126   -48.224 -83.039  1.00 17.89  ? 574  ASN   C CA  1 
ATOM   8956  C  C   . ASN   C  1 273 ? 8.052   -47.229 -82.362  1.00 24.38  ? 574  ASN   C C   1 
ATOM   8957  O  O   . ASN   C  1 273 ? 7.586   -46.201 -81.880  1.00 23.92  ? 574  ASN   C O   1 
ATOM   8958  C  CB  . ASN   C  1 273 ? 5.880   -48.445 -82.177  1.00 21.74  ? 574  ASN   C CB  1 
ATOM   8959  C  CG  . ASN   C  1 273 ? 6.189   -49.122 -80.856  1.00 28.26  ? 574  ASN   C CG  1 
ATOM   8960  O  OD1 . ASN   C  1 273 ? 7.331   -49.493 -80.579  1.00 23.18  ? 574  ASN   C OD1 1 
ATOM   8961  N  ND2 . ASN   C  1 273 ? 5.163   -49.292 -80.039  1.00 26.13  ? 574  ASN   C ND2 1 
ATOM   8962  N  N   . MET   C  1 274 ? 9.351   -47.479 -82.360  1.00 19.13  ? 575  MET   C N   1 
ATOM   8963  C  CA  . MET   C  1 274 ? 10.274  -46.575 -81.706  1.00 19.58  ? 575  MET   C CA  1 
ATOM   8964  C  C   . MET   C  1 274 ? 10.888  -45.618 -82.709  1.00 23.61  ? 575  MET   C C   1 
ATOM   8965  O  O   . MET   C  1 274 ? 10.713  -45.736 -83.924  1.00 27.37  ? 575  MET   C O   1 
ATOM   8966  C  CB  . MET   C  1 274 ? 11.347  -47.361 -80.944  1.00 19.90  ? 575  MET   C CB  1 
ATOM   8967  C  CG  . MET   C  1 274 ? 10.782  -47.979 -79.643  1.00 22.92  ? 575  MET   C CG  1 
ATOM   8968  S  SD  . MET   C  1 274 ? 12.055  -48.810 -78.699  1.00 25.34  ? 575  MET   C SD  1 
ATOM   8969  C  CE  . MET   C  1 274 ? 12.682  -47.425 -77.741  1.00 20.39  ? 575  MET   C CE  1 
ATOM   8970  N  N   . LEU   C  1 275 ? 11.567  -44.617 -82.172  1.00 23.27  ? 576  LEU   C N   1 
ATOM   8971  C  CA  . LEU   C  1 275 ? 12.181  -43.570 -82.964  1.00 20.59  ? 576  LEU   C CA  1 
ATOM   8972  C  C   . LEU   C  1 275 ? 13.673  -43.652 -82.741  1.00 26.30  ? 576  LEU   C C   1 
ATOM   8973  O  O   . LEU   C  1 275 ? 14.133  -43.697 -81.594  1.00 26.45  ? 576  LEU   C O   1 
ATOM   8974  C  CB  . LEU   C  1 275 ? 11.647  -42.191 -82.573  1.00 26.00  ? 576  LEU   C CB  1 
ATOM   8975  C  CG  . LEU   C  1 275 ? 12.087  -41.017 -83.460  1.00 33.27  ? 576  LEU   C CG  1 
ATOM   8976  C  CD1 . LEU   C  1 275 ? 10.963  -39.989 -83.598  1.00 28.66  ? 576  LEU   C CD1 1 
ATOM   8977  C  CD2 . LEU   C  1 275 ? 13.344  -40.356 -82.895  1.00 26.25  ? 576  LEU   C CD2 1 
ATOM   8978  N  N   . LEU   C  1 276 ? 14.414  -43.690 -83.834  1.00 23.03  ? 577  LEU   C N   1 
ATOM   8979  C  CA  . LEU   C  1 276 ? 15.861  -43.773 -83.812  1.00 21.55  ? 577  LEU   C CA  1 
ATOM   8980  C  C   . LEU   C  1 276 ? 16.398  -42.371 -84.068  1.00 28.23  ? 577  LEU   C C   1 
ATOM   8981  O  O   . LEU   C  1 276 ? 16.105  -41.774 -85.108  1.00 23.83  ? 577  LEU   C O   1 
ATOM   8982  C  CB  . LEU   C  1 276 ? 16.347  -44.758 -84.881  1.00 23.83  ? 577  LEU   C CB  1 
ATOM   8983  C  CG  . LEU   C  1 276 ? 17.820  -44.624 -85.231  1.00 21.14  ? 577  LEU   C CG  1 
ATOM   8984  C  CD1 . LEU   C  1 276 ? 18.669  -44.912 -83.987  1.00 21.35  ? 577  LEU   C CD1 1 
ATOM   8985  C  CD2 . LEU   C  1 276 ? 18.201  -45.538 -86.395  1.00 24.88  ? 577  LEU   C CD2 1 
ATOM   8986  N  N   . GLU   C  1 277 ? 17.163  -41.838 -83.120  1.00 22.70  ? 578  GLU   C N   1 
ATOM   8987  C  CA  . GLU   C  1 277 ? 17.685  -40.485 -83.218  1.00 19.23  ? 578  GLU   C CA  1 
ATOM   8988  C  C   . GLU   C  1 277 ? 19.189  -40.573 -83.395  1.00 25.05  ? 578  GLU   C C   1 
ATOM   8989  O  O   . GLU   C  1 277 ? 19.874  -41.186 -82.574  1.00 22.94  ? 578  GLU   C O   1 
ATOM   8990  C  CB  . GLU   C  1 277 ? 17.321  -39.660 -81.980  1.00 27.09  ? 578  GLU   C CB  1 
ATOM   8991  C  CG  . GLU   C  1 277 ? 17.778  -38.230 -82.058  1.00 45.25  ? 578  GLU   C CG  1 
ATOM   8992  C  CD  . GLU   C  1 277 ? 19.067  -38.004 -81.310  1.00 63.49  ? 578  GLU   C CD  1 
ATOM   8993  O  OE1 . GLU   C  1 277 ? 19.261  -38.643 -80.252  1.00 68.91  ? 578  GLU   C OE1 1 
ATOM   8994  O  OE2 . GLU   C  1 277 ? 19.888  -37.193 -81.784  1.00 64.42  ? 578  GLU   C OE2 1 
ATOM   8995  N  N   . ILE   C  1 278 ? 19.691  -39.999 -84.486  1.00 21.88  ? 579  ILE   C N   1 
ATOM   8996  C  CA  . ILE   C  1 278 ? 21.111  -40.007 -84.805  1.00 27.31  ? 579  ILE   C CA  1 
ATOM   8997  C  C   . ILE   C  1 278 ? 21.491  -38.602 -85.228  1.00 34.85  ? 579  ILE   C C   1 
ATOM   8998  O  O   . ILE   C  1 278 ? 21.010  -38.112 -86.263  1.00 28.60  ? 579  ILE   C O   1 
ATOM   8999  C  CB  . ILE   C  1 278 ? 21.457  -40.995 -85.932  1.00 28.93  ? 579  ILE   C CB  1 
ATOM   9000  C  CG1 . ILE   C  1 278 ? 21.015  -42.412 -85.584  1.00 25.04  ? 579  ILE   C CG1 1 
ATOM   9001  C  CG2 . ILE   C  1 278 ? 22.950  -40.927 -86.233  1.00 23.07  ? 579  ILE   C CG2 1 
ATOM   9002  C  CD1 . ILE   C  1 278 ? 21.032  -43.340 -86.785  1.00 25.05  ? 579  ILE   C CD1 1 
ATOM   9003  N  N   . GLY   C  1 279 ? 22.368  -37.968 -84.451  1.00 24.72  ? 580  GLY   C N   1 
ATOM   9004  C  CA  . GLY   C  1 279 ? 22.863  -36.649 -84.807  1.00 27.91  ? 580  GLY   C CA  1 
ATOM   9005  C  C   . GLY   C  1 279 ? 21.768  -35.624 -84.945  1.00 34.72  ? 580  GLY   C C   1 
ATOM   9006  O  O   . GLY   C  1 279 ? 21.880  -34.709 -85.769  1.00 36.80  ? 580  GLY   C O   1 
ATOM   9007  N  N   . GLY   C  1 280 ? 20.696  -35.762 -84.163  1.00 28.18  ? 581  GLY   C N   1 
ATOM   9008  C  CA  . GLY   C  1 280 ? 19.564  -34.873 -84.249  1.00 28.40  ? 581  GLY   C CA  1 
ATOM   9009  C  C   . GLY   C  1 280 ? 18.581  -35.228 -85.335  1.00 29.31  ? 581  GLY   C C   1 
ATOM   9010  O  O   . GLY   C  1 280 ? 17.521  -34.599 -85.422  1.00 31.05  ? 581  GLY   C O   1 
ATOM   9011  N  N   . LEU   C  1 281 ? 18.897  -36.203 -86.171  1.00 26.69  ? 582  LEU   C N   1 
ATOM   9012  C  CA  . LEU   C  1 281 ? 17.962  -36.677 -87.175  1.00 30.79  ? 582  LEU   C CA  1 
ATOM   9013  C  C   . LEU   C  1 281 ? 17.046  -37.701 -86.541  1.00 29.43  ? 582  LEU   C C   1 
ATOM   9014  O  O   . LEU   C  1 281 ? 17.478  -38.511 -85.720  1.00 26.18  ? 582  LEU   C O   1 
ATOM   9015  C  CB  . LEU   C  1 281 ? 18.705  -37.302 -88.353  1.00 23.47  ? 582  LEU   C CB  1 
ATOM   9016  C  CG  . LEU   C  1 281 ? 19.659  -36.340 -89.034  1.00 27.81  ? 582  LEU   C CG  1 
ATOM   9017  C  CD1 . LEU   C  1 281 ? 20.387  -37.038 -90.177  1.00 33.98  ? 582  LEU   C CD1 1 
ATOM   9018  C  CD2 . LEU   C  1 281 ? 18.863  -35.132 -89.523  1.00 24.56  ? 582  LEU   C CD2 1 
ATOM   9019  N  N   . GLU   C  1 282 ? 15.781  -37.664 -86.922  1.00 26.88  ? 583  GLU   C N   1 
ATOM   9020  C  CA  . GLU   C  1 282 ? 14.760  -38.506 -86.307  1.00 27.19  ? 583  GLU   C CA  1 
ATOM   9021  C  C   . GLU   C  1 282 ? 14.248  -39.513 -87.328  1.00 30.07  ? 583  GLU   C C   1 
ATOM   9022  O  O   . GLU   C  1 282 ? 13.612  -39.132 -88.317  1.00 26.66  ? 583  GLU   C O   1 
ATOM   9023  C  CB  . GLU   C  1 282 ? 13.624  -37.644 -85.773  1.00 30.96  ? 583  GLU   C CB  1 
ATOM   9024  C  CG  . GLU   C  1 282 ? 14.071  -36.690 -84.672  1.00 38.28  ? 583  GLU   C CG  1 
ATOM   9025  C  CD  . GLU   C  1 282 ? 12.917  -35.917 -84.076  1.00 41.32  ? 583  GLU   C CD  1 
ATOM   9026  O  OE1 . GLU   C  1 282 ? 12.060  -35.428 -84.846  1.00 46.26  ? 583  GLU   C OE1 1 
ATOM   9027  O  OE2 . GLU   C  1 282 ? 12.866  -35.804 -82.835  1.00 46.70  ? 583  GLU   C OE2 1 
ATOM   9028  N  N   . PHE   C  1 283 ? 14.503  -40.788 -87.075  1.00 27.58  ? 584  PHE   C N   1 
ATOM   9029  C  CA  . PHE   C  1 283 ? 14.037  -41.869 -87.944  1.00 24.13  ? 584  PHE   C CA  1 
ATOM   9030  C  C   . PHE   C  1 283 ? 12.814  -42.502 -87.289  1.00 24.57  ? 584  PHE   C C   1 
ATOM   9031  O  O   . PHE   C  1 283 ? 12.920  -43.420 -86.475  1.00 25.17  ? 584  PHE   C O   1 
ATOM   9032  C  CB  . PHE   C  1 283 ? 15.152  -42.871 -88.190  1.00 20.24  ? 584  PHE   C CB  1 
ATOM   9033  C  CG  . PHE   C  1 283 ? 16.312  -42.283 -88.932  1.00 26.88  ? 584  PHE   C CG  1 
ATOM   9034  C  CD1 . PHE   C  1 283 ? 17.406  -41.785 -88.249  1.00 23.35  ? 584  PHE   C CD1 1 
ATOM   9035  C  CD2 . PHE   C  1 283 ? 16.280  -42.175 -90.321  1.00 23.77  ? 584  PHE   C CD2 1 
ATOM   9036  C  CE1 . PHE   C  1 283 ? 18.472  -41.230 -88.936  1.00 22.58  ? 584  PHE   C CE1 1 
ATOM   9037  C  CE2 . PHE   C  1 283 ? 17.337  -41.622 -91.008  1.00 22.97  ? 584  PHE   C CE2 1 
ATOM   9038  C  CZ  . PHE   C  1 283 ? 18.431  -41.148 -90.322  1.00 22.58  ? 584  PHE   C CZ  1 
ATOM   9039  N  N   . SER   C  1 284 ? 11.640  -41.998 -87.660  1.00 27.98  ? 585  SER   C N   1 
ATOM   9040  C  CA  . SER   C  1 284 ? 10.403  -42.417 -87.013  1.00 29.64  ? 585  SER   C CA  1 
ATOM   9041  C  C   . SER   C  1 284 ? 9.969   -43.827 -87.397  1.00 27.12  ? 585  SER   C C   1 
ATOM   9042  O  O   . SER   C  1 284 ? 9.105   -44.395 -86.720  1.00 24.46  ? 585  SER   C O   1 
ATOM   9043  C  CB  . SER   C  1 284 ? 9.291   -41.420 -87.347  1.00 29.28  ? 585  SER   C CB  1 
ATOM   9044  O  OG  . SER   C  1 284 ? 9.298   -41.113 -88.730  1.00 30.58  ? 585  SER   C OG  1 
ATOM   9045  N  N   . ALA   C  1 285 ? 10.526  -44.402 -88.461  1.00 23.44  ? 586  ALA   C N   1 
ATOM   9046  C  CA  . ALA   C  1 285 ? 10.236  -45.783 -88.829  1.00 20.01  ? 586  ALA   C CA  1 
ATOM   9047  C  C   . ALA   C  1 285 ? 11.566  -46.510 -88.930  1.00 24.07  ? 586  ALA   C C   1 
ATOM   9048  O  O   . ALA   C  1 285 ? 12.357  -46.260 -89.852  1.00 25.13  ? 586  ALA   C O   1 
ATOM   9049  C  CB  . ALA   C  1 285 ? 9.444   -45.871 -90.128  1.00 25.47  ? 586  ALA   C CB  1 
ATOM   9050  N  N   . CYS   C  1 286 ? 11.818  -47.388 -87.975  1.00 18.51  ? 587  CYS   C N   1 
ATOM   9051  C  CA  . CYS   C  1 286 ? 13.117  -48.024 -87.902  1.00 22.33  ? 587  CYS   C CA  1 
ATOM   9052  C  C   . CYS   C  1 286 ? 12.988  -49.402 -87.271  1.00 28.98  ? 587  CYS   C C   1 
ATOM   9053  O  O   . CYS   C  1 286 ? 13.677  -49.690 -86.282  1.00 30.55  ? 587  CYS   C O   1 
ATOM   9054  C  CB  . CYS   C  1 286 ? 14.073  -47.151 -87.095  1.00 26.44  ? 587  CYS   C CB  1 
ATOM   9055  S  SG  . CYS   C  1 286 ? 13.517  -46.898 -85.334  1.00 27.94  ? 587  CYS   C SG  1 
ATOM   9056  N  N   . PRO   C  1 287 ? 12.136  -50.280 -87.805  1.00 29.85  ? 588  PRO   C N   1 
ATOM   9057  C  CA  . PRO   C  1 287 ? 11.909  -51.566 -87.139  1.00 22.89  ? 588  PRO   C CA  1 
ATOM   9058  C  C   . PRO   C  1 287 ? 13.213  -52.324 -86.953  1.00 22.53  ? 588  PRO   C C   1 
ATOM   9059  O  O   . PRO   C  1 287 ? 14.066  -52.369 -87.843  1.00 23.82  ? 588  PRO   C O   1 
ATOM   9060  C  CB  . PRO   C  1 287 ? 10.955  -52.296 -88.087  1.00 24.94  ? 588  PRO   C CB  1 
ATOM   9061  C  CG  . PRO   C  1 287 ? 11.170  -51.632 -89.415  1.00 27.35  ? 588  PRO   C CG  1 
ATOM   9062  C  CD  . PRO   C  1 287 ? 11.419  -50.197 -89.090  1.00 25.83  ? 588  PRO   C CD  1 
ATOM   9063  N  N   . PHE   C  1 288 ? 13.376  -52.895 -85.761  1.00 19.98  ? 589  PHE   C N   1 
ATOM   9064  C  CA  . PHE   C  1 288 ? 14.588  -53.626 -85.426  1.00 17.28  ? 589  PHE   C CA  1 
ATOM   9065  C  C   . PHE   C  1 288 ? 14.201  -54.915 -84.723  1.00 21.11  ? 589  PHE   C C   1 
ATOM   9066  O  O   . PHE   C  1 288 ? 13.145  -55.008 -84.095  1.00 20.13  ? 589  PHE   C O   1 
ATOM   9067  C  CB  . PHE   C  1 288 ? 15.535  -52.793 -84.555  1.00 20.51  ? 589  PHE   C CB  1 
ATOM   9068  C  CG  . PHE   C  1 288 ? 14.932  -52.323 -83.239  1.00 27.53  ? 589  PHE   C CG  1 
ATOM   9069  C  CD1 . PHE   C  1 288 ? 14.905  -53.159 -82.126  1.00 24.25  ? 589  PHE   C CD1 1 
ATOM   9070  C  CD2 . PHE   C  1 288 ? 14.430  -51.029 -83.109  1.00 26.00  ? 589  PHE   C CD2 1 
ATOM   9071  C  CE1 . PHE   C  1 288 ? 14.369  -52.721 -80.909  1.00 23.65  ? 589  PHE   C CE1 1 
ATOM   9072  C  CE2 . PHE   C  1 288 ? 13.901  -50.584 -81.901  1.00 30.00  ? 589  PHE   C CE2 1 
ATOM   9073  C  CZ  . PHE   C  1 288 ? 13.871  -51.433 -80.796  1.00 22.76  ? 589  PHE   C CZ  1 
ATOM   9074  N  N   . SER   C  1 289 ? 15.063  -55.916 -84.844  1.00 22.53  ? 590  SER   C N   1 
ATOM   9075  C  CA  . SER   C  1 289 ? 14.691  -57.235 -84.399  1.00 20.62  ? 590  SER   C CA  1 
ATOM   9076  C  C   . SER   C  1 289 ? 15.934  -57.942 -83.900  1.00 19.74  ? 590  SER   C C   1 
ATOM   9077  O  O   . SER   C  1 289 ? 17.044  -57.661 -84.350  1.00 18.94  ? 590  SER   C O   1 
ATOM   9078  C  CB  . SER   C  1 289 ? 14.017  -58.022 -85.538  1.00 17.93  ? 590  SER   C CB  1 
ATOM   9079  O  OG  . SER   C  1 289 ? 14.959  -58.286 -86.553  1.00 25.20  ? 590  SER   C OG  1 
ATOM   9080  N  N   . GLY   C  1 290 ? 15.740  -58.837 -82.938  1.00 21.65  ? 591  GLY   C N   1 
ATOM   9081  C  CA  . GLY   C  1 290 ? 16.825  -59.686 -82.492  1.00 18.03  ? 591  GLY   C CA  1 
ATOM   9082  C  C   . GLY   C  1 290 ? 16.309  -61.091 -82.307  1.00 20.51  ? 591  GLY   C C   1 
ATOM   9083  O  O   . GLY   C  1 290 ? 15.775  -61.693 -83.241  1.00 25.57  ? 591  GLY   C O   1 
ATOM   9084  N  N   . TRP   C  1 291 ? 16.447  -61.627 -81.102  1.00 22.70  ? 592  TRP   C N   1 
ATOM   9085  C  CA  . TRP   C  1 291 ? 15.783  -62.867 -80.745  1.00 21.98  ? 592  TRP   C CA  1 
ATOM   9086  C  C   . TRP   C  1 291 ? 15.294  -62.765 -79.307  1.00 18.66  ? 592  TRP   C C   1 
ATOM   9087  O  O   . TRP   C  1 291 ? 15.693  -61.877 -78.549  1.00 21.97  ? 592  TRP   C O   1 
ATOM   9088  C  CB  . TRP   C  1 291 ? 16.697  -64.082 -80.924  1.00 21.04  ? 592  TRP   C CB  1 
ATOM   9089  C  CG  . TRP   C  1 291 ? 17.991  -63.954 -80.242  1.00 25.65  ? 592  TRP   C CG  1 
ATOM   9090  C  CD1 . TRP   C  1 291 ? 18.246  -64.167 -78.896  1.00 29.71  ? 592  TRP   C CD1 1 
ATOM   9091  C  CD2 . TRP   C  1 291 ? 19.231  -63.574 -80.829  1.00 26.12  ? 592  TRP   C CD2 1 
ATOM   9092  N  NE1 . TRP   C  1 291 ? 19.570  -63.947 -78.639  1.00 25.80  ? 592  TRP   C NE1 1 
ATOM   9093  C  CE2 . TRP   C  1 291 ? 20.200  -63.591 -79.806  1.00 28.26  ? 592  TRP   C CE2 1 
ATOM   9094  C  CE3 . TRP   C  1 291 ? 19.629  -63.245 -82.133  1.00 31.84  ? 592  TRP   C CE3 1 
ATOM   9095  C  CZ2 . TRP   C  1 291 ? 21.539  -63.272 -80.044  1.00 31.51  ? 592  TRP   C CZ2 1 
ATOM   9096  C  CZ3 . TRP   C  1 291 ? 20.953  -62.929 -82.365  1.00 29.37  ? 592  TRP   C CZ3 1 
ATOM   9097  C  CH2 . TRP   C  1 291 ? 21.893  -62.941 -81.329  1.00 31.20  ? 592  TRP   C CH2 1 
ATOM   9098  N  N   . TYR   C  1 292 ? 14.415  -63.692 -78.941  1.00 26.21  ? 593  TYR   C N   1 
ATOM   9099  C  CA  . TYR   C  1 292 ? 13.699  -63.602 -77.678  1.00 27.05  ? 593  TYR   C CA  1 
ATOM   9100  C  C   . TYR   C  1 292 ? 14.526  -64.106 -76.506  1.00 19.76  ? 593  TYR   C C   1 
ATOM   9101  O  O   . TYR   C  1 292 ? 15.297  -65.062 -76.621  1.00 21.59  ? 593  TYR   C O   1 
ATOM   9102  C  CB  . TYR   C  1 292 ? 12.418  -64.419 -77.739  1.00 21.02  ? 593  TYR   C CB  1 
ATOM   9103  C  CG  . TYR   C  1 292 ? 11.187  -63.647 -78.119  1.00 28.31  ? 593  TYR   C CG  1 
ATOM   9104  C  CD1 . TYR   C  1 292 ? 10.483  -63.945 -79.292  1.00 20.88  ? 593  TYR   C CD1 1 
ATOM   9105  C  CD2 . TYR   C  1 292 ? 10.710  -62.638 -77.299  1.00 24.47  ? 593  TYR   C CD2 1 
ATOM   9106  C  CE1 . TYR   C  1 292 ? 9.329   -63.247 -79.614  1.00 23.50  ? 593  TYR   C CE1 1 
ATOM   9107  C  CE2 . TYR   C  1 292 ? 9.566   -61.948 -77.610  1.00 23.40  ? 593  TYR   C CE2 1 
ATOM   9108  C  CZ  . TYR   C  1 292 ? 8.881   -62.250 -78.768  1.00 25.53  ? 593  TYR   C CZ  1 
ATOM   9109  O  OH  . TYR   C  1 292 ? 7.742   -61.536 -79.052  1.00 25.29  ? 593  TYR   C OH  1 
ATOM   9110  N  N   . MET   C  1 293 ? 14.349  -63.448 -75.375  1.00 18.31  ? 594  MET   C N   1 
ATOM   9111  C  CA  . MET   C  1 293 ? 14.601  -64.057 -74.088  1.00 18.97  ? 594  MET   C CA  1 
ATOM   9112  C  C   . MET   C  1 293 ? 13.311  -64.737 -73.667  1.00 22.88  ? 594  MET   C C   1 
ATOM   9113  O  O   . MET   C  1 293 ? 12.232  -64.151 -73.795  1.00 22.56  ? 594  MET   C O   1 
ATOM   9114  C  CB  . MET   C  1 293 ? 15.036  -63.001 -73.078  1.00 18.37  ? 594  MET   C CB  1 
ATOM   9115  C  CG  . MET   C  1 293 ? 15.452  -63.587 -71.745  1.00 20.77  ? 594  MET   C CG  1 
ATOM   9116  S  SD  . MET   C  1 293 ? 16.278  -62.319 -70.769  1.00 24.21  ? 594  MET   C SD  1 
ATOM   9117  C  CE  . MET   C  1 293 ? 14.880  -61.352 -70.214  1.00 24.32  ? 594  MET   C CE  1 
ATOM   9118  N  N   . GLY   C  1 294 ? 13.416  -65.984 -73.198  1.00 25.41  ? 595  GLY   C N   1 
ATOM   9119  C  CA  . GLY   C  1 294 ? 12.221  -66.784 -72.958  1.00 25.82  ? 595  GLY   C CA  1 
ATOM   9120  C  C   . GLY   C  1 294 ? 11.181  -66.119 -72.073  1.00 27.85  ? 595  GLY   C C   1 
ATOM   9121  O  O   . GLY   C  1 294 ? 9.974   -66.326 -72.259  1.00 22.25  ? 595  GLY   C O   1 
ATOM   9122  N  N   . THR   C  1 295 ? 11.622  -65.331 -71.086  1.00 24.19  ? 596  THR   C N   1 
ATOM   9123  C  CA  . THR   C  1 295 ? 10.666  -64.750 -70.147  1.00 24.18  ? 596  THR   C CA  1 
ATOM   9124  C  C   . THR   C  1 295 ? 9.804   -63.693 -70.805  1.00 22.23  ? 596  THR   C C   1 
ATOM   9125  O  O   . THR   C  1 295 ? 8.717   -63.395 -70.306  1.00 20.98  ? 596  THR   C O   1 
ATOM   9126  C  CB  . THR   C  1 295 ? 11.373  -64.109 -68.950  1.00 19.40  ? 596  THR   C CB  1 
ATOM   9127  O  OG1 . THR   C  1 295 ? 12.392  -63.222 -69.430  1.00 20.46  ? 596  THR   C OG1 1 
ATOM   9128  C  CG2 . THR   C  1 295 ? 11.973  -65.159 -68.034  1.00 19.90  ? 596  THR   C CG2 1 
ATOM   9129  N  N   . GLU   C  1 296 ? 10.271  -63.089 -71.892  1.00 22.69  ? 597  GLU   C N   1 
ATOM   9130  C  CA  . GLU   C  1 296 ? 9.392   -62.158 -72.591  1.00 22.89  ? 597  GLU   C CA  1 
ATOM   9131  C  C   . GLU   C  1 296 ? 8.086   -62.842 -72.960  1.00 27.19  ? 597  GLU   C C   1 
ATOM   9132  O  O   . GLU   C  1 296 ? 7.005   -62.269 -72.785  1.00 22.80  ? 597  GLU   C O   1 
ATOM   9133  C  CB  . GLU   C  1 296 ? 10.079  -61.610 -73.836  1.00 26.40  ? 597  GLU   C CB  1 
ATOM   9134  C  CG  . GLU   C  1 296 ? 11.342  -60.827 -73.566  1.00 23.60  ? 597  GLU   C CG  1 
ATOM   9135  C  CD  . GLU   C  1 296 ? 11.955  -60.337 -74.848  1.00 22.18  ? 597  GLU   C CD  1 
ATOM   9136  O  OE1 . GLU   C  1 296 ? 11.415  -59.350 -75.388  1.00 21.50  ? 597  GLU   C OE1 1 
ATOM   9137  O  OE2 . GLU   C  1 296 ? 12.939  -60.960 -75.316  1.00 22.60  ? 597  GLU   C OE2 1 
ATOM   9138  N  N   . ILE   C  1 297 ? 8.170   -64.093 -73.419  1.00 20.71  ? 598  ILE   C N   1 
ATOM   9139  C  CA  . ILE   C  1 297 ? 7.002   -64.852 -73.859  1.00 28.82  ? 598  ILE   C CA  1 
ATOM   9140  C  C   . ILE   C  1 297 ? 6.382   -65.553 -72.662  1.00 26.35  ? 598  ILE   C C   1 
ATOM   9141  O  O   . ILE   C  1 297 ? 5.200   -65.372 -72.354  1.00 27.48  ? 598  ILE   C O   1 
ATOM   9142  C  CB  . ILE   C  1 297 ? 7.385   -65.883 -74.940  1.00 25.74  ? 598  ILE   C CB  1 
ATOM   9143  C  CG1 . ILE   C  1 297 ? 8.068   -65.215 -76.143  1.00 23.55  ? 598  ILE   C CG1 1 
ATOM   9144  C  CG2 . ILE   C  1 297 ? 6.166   -66.713 -75.343  1.00 22.72  ? 598  ILE   C CG2 1 
ATOM   9145  C  CD1 . ILE   C  1 297 ? 8.739   -66.212 -77.071  1.00 19.60  ? 598  ILE   C CD1 1 
ATOM   9146  N  N   . GLY   C  1 298 ? 7.188   -66.371 -71.981  1.00 20.40  ? 599  GLY   C N   1 
ATOM   9147  C  CA  . GLY   C  1 298 ? 6.660   -67.210 -70.922  1.00 29.93  ? 599  GLY   C CA  1 
ATOM   9148  C  C   . GLY   C  1 298 ? 6.124   -66.432 -69.731  1.00 32.64  ? 599  GLY   C C   1 
ATOM   9149  O  O   . GLY   C  1 298 ? 5.123   -66.826 -69.130  1.00 32.07  ? 599  GLY   C O   1 
ATOM   9150  N  N   . VAL   C  1 299 ? 6.757   -65.318 -69.380  1.00 27.13  ? 600  VAL   C N   1 
ATOM   9151  C  CA  . VAL   C  1 299 ? 6.299   -64.556 -68.223  1.00 24.52  ? 600  VAL   C CA  1 
ATOM   9152  C  C   . VAL   C  1 299 ? 5.320   -63.466 -68.629  1.00 24.91  ? 600  VAL   C C   1 
ATOM   9153  O  O   . VAL   C  1 299 ? 4.200   -63.399 -68.118  1.00 25.60  ? 600  VAL   C O   1 
ATOM   9154  C  CB  . VAL   C  1 299 ? 7.489   -63.961 -67.463  1.00 26.46  ? 600  VAL   C CB  1 
ATOM   9155  C  CG1 . VAL   C  1 299 ? 7.000   -63.259 -66.232  1.00 32.23  ? 600  VAL   C CG1 1 
ATOM   9156  C  CG2 . VAL   C  1 299 ? 8.485   -65.066 -67.116  1.00 23.10  ? 600  VAL   C CG2 1 
ATOM   9157  N  N   . ARG   C  1 300 ? 5.721   -62.601 -69.564  1.00 24.96  ? 601  ARG   C N   1 
ATOM   9158  C  CA  . ARG   C  1 300 ? 4.917   -61.414 -69.823  1.00 23.30  ? 601  ARG   C CA  1 
ATOM   9159  C  C   . ARG   C  1 300 ? 3.794   -61.700 -70.816  1.00 28.28  ? 601  ARG   C C   1 
ATOM   9160  O  O   . ARG   C  1 300 ? 2.613   -61.492 -70.504  1.00 28.52  ? 601  ARG   C O   1 
ATOM   9161  C  CB  . ARG   C  1 300 ? 5.815   -60.263 -70.300  1.00 21.64  ? 601  ARG   C CB  1 
ATOM   9162  C  CG  . ARG   C  1 300 ? 6.996   -59.964 -69.360  1.00 22.10  ? 601  ARG   C CG  1 
ATOM   9163  C  CD  . ARG   C  1 300 ? 6.561   -59.461 -67.959  1.00 19.27  ? 601  ARG   C CD  1 
ATOM   9164  N  NE  . ARG   C  1 300 ? 5.461   -58.493 -68.039  1.00 19.77  ? 601  ARG   C NE  1 
ATOM   9165  C  CZ  . ARG   C  1 300 ? 5.623   -57.213 -68.370  1.00 20.22  ? 601  ARG   C CZ  1 
ATOM   9166  N  NH1 . ARG   C  1 300 ? 6.839   -56.735 -68.600  1.00 21.69  ? 601  ARG   C NH1 1 
ATOM   9167  N  NH2 . ARG   C  1 300 ? 4.574   -56.410 -68.470  1.00 22.30  ? 601  ARG   C NH2 1 
ATOM   9168  N  N   . ASP   C  1 301 ? 4.140   -62.175 -72.021  1.00 27.12  ? 602  ASP   C N   1 
ATOM   9169  C  CA  . ASP   C  1 301 ? 3.116   -62.438 -73.031  1.00 27.70  ? 602  ASP   C CA  1 
ATOM   9170  C  C   . ASP   C  1 301 ? 2.100   -63.463 -72.546  1.00 22.89  ? 602  ASP   C C   1 
ATOM   9171  O  O   . ASP   C  1 301 ? 0.889   -63.290 -72.735  1.00 29.92  ? 602  ASP   C O   1 
ATOM   9172  C  CB  . ASP   C  1 301 ? 3.753   -62.905 -74.346  1.00 24.61  ? 602  ASP   C CB  1 
ATOM   9173  C  CG  . ASP   C  1 301 ? 4.662   -61.860 -74.950  1.00 26.38  ? 602  ASP   C CG  1 
ATOM   9174  O  OD1 . ASP   C  1 301 ? 4.378   -60.656 -74.794  1.00 30.50  ? 602  ASP   C OD1 1 
ATOM   9175  O  OD2 . ASP   C  1 301 ? 5.671   -62.237 -75.566  1.00 28.59  ? 602  ASP   C OD2 1 
ATOM   9176  N  N   . TYR   C  1 302 ? 2.561   -64.522 -71.894  1.00 25.75  ? 603  TYR   C N   1 
ATOM   9177  C  CA  . TYR   C  1 302 ? 1.632   -65.576 -71.512  1.00 24.08  ? 603  TYR   C CA  1 
ATOM   9178  C  C   . TYR   C  1 302 ? 0.947   -65.348 -70.169  1.00 30.34  ? 603  TYR   C C   1 
ATOM   9179  O  O   . TYR   C  1 302 ? -0.203  -65.778 -70.003  1.00 31.32  ? 603  TYR   C O   1 
ATOM   9180  C  CB  . TYR   C  1 302 ? 2.352   -66.923 -71.504  1.00 25.33  ? 603  TYR   C CB  1 
ATOM   9181  C  CG  . TYR   C  1 302 ? 2.503   -67.524 -72.885  1.00 22.17  ? 603  TYR   C CG  1 
ATOM   9182  C  CD1 . TYR   C  1 302 ? 3.249   -68.679 -73.077  1.00 22.38  ? 603  TYR   C CD1 1 
ATOM   9183  C  CD2 . TYR   C  1 302 ? 1.901   -66.935 -73.990  1.00 29.07  ? 603  TYR   C CD2 1 
ATOM   9184  C  CE1 . TYR   C  1 302 ? 3.397   -69.238 -74.336  1.00 33.78  ? 603  TYR   C CE1 1 
ATOM   9185  C  CE2 . TYR   C  1 302 ? 2.044   -67.487 -75.267  1.00 29.93  ? 603  TYR   C CE2 1 
ATOM   9186  C  CZ  . TYR   C  1 302 ? 2.793   -68.639 -75.423  1.00 32.75  ? 603  TYR   C CZ  1 
ATOM   9187  O  OH  . TYR   C  1 302 ? 2.944   -69.204 -76.657  1.00 33.98  ? 603  TYR   C OH  1 
ATOM   9188  N  N   . CYS   C  1 303 ? 1.597   -64.671 -69.206  1.00 30.71  ? 604  CYS   C N   1 
ATOM   9189  C  CA  . CYS   C  1 303 ? 1.073   -64.650 -67.841  1.00 30.00  ? 604  CYS   C CA  1 
ATOM   9190  C  C   . CYS   C  1 303 ? 0.738   -63.278 -67.278  1.00 28.07  ? 604  CYS   C C   1 
ATOM   9191  O  O   . CYS   C  1 303 ? 0.188   -63.213 -66.177  1.00 28.42  ? 604  CYS   C O   1 
ATOM   9192  C  CB  . CYS   C  1 303 ? 2.051   -65.334 -66.874  1.00 25.34  ? 604  CYS   C CB  1 
ATOM   9193  S  SG  . CYS   C  1 303 ? 2.444   -67.030 -67.304  1.00 30.67  ? 604  CYS   C SG  1 
ATOM   9194  N  N   . ASP   C  1 304 ? 1.071   -62.184 -67.954  1.00 25.41  ? 605  ASP   C N   1 
ATOM   9195  C  CA  . ASP   C  1 304 ? 0.481   -60.923 -67.542  1.00 26.99  ? 605  ASP   C CA  1 
ATOM   9196  C  C   . ASP   C  1 304 ? -1.031  -61.084 -67.527  1.00 31.85  ? 605  ASP   C C   1 
ATOM   9197  O  O   . ASP   C  1 304 ? -1.610  -61.712 -68.421  1.00 30.11  ? 605  ASP   C O   1 
ATOM   9198  C  CB  . ASP   C  1 304 ? 0.867   -59.784 -68.486  1.00 24.07  ? 605  ASP   C CB  1 
ATOM   9199  C  CG  . ASP   C  1 304 ? 2.221   -59.162 -68.168  1.00 31.48  ? 605  ASP   C CG  1 
ATOM   9200  O  OD1 . ASP   C  1 304 ? 2.964   -59.663 -67.289  1.00 32.55  ? 605  ASP   C OD1 1 
ATOM   9201  O  OD2 . ASP   C  1 304 ? 2.539   -58.142 -68.823  1.00 32.22  ? 605  ASP   C OD2 1 
ATOM   9202  N  N   . ASN   C  1 305 ? -1.663  -60.538 -66.484  1.00 29.16  ? 606  ASN   C N   1 
ATOM   9203  C  CA  . ASN   C  1 305 ? -3.116  -60.607 -66.371  1.00 30.39  ? 606  ASN   C CA  1 
ATOM   9204  C  C   . ASN   C  1 305 ? -3.801  -59.965 -67.566  1.00 32.55  ? 606  ASN   C C   1 
ATOM   9205  O  O   . ASN   C  1 305 ? -4.864  -60.422 -67.995  1.00 35.46  ? 606  ASN   C O   1 
ATOM   9206  C  CB  . ASN   C  1 305 ? -3.565  -59.933 -65.075  1.00 32.84  ? 606  ASN   C CB  1 
ATOM   9207  C  CG  . ASN   C  1 305 ? -3.240  -60.769 -63.846  1.00 50.58  ? 606  ASN   C CG  1 
ATOM   9208  O  OD1 . ASN   C  1 305 ? -3.392  -61.996 -63.861  1.00 54.86  ? 606  ASN   C OD1 1 
ATOM   9209  N  ND2 . ASN   C  1 305 ? -2.787  -60.113 -62.778  1.00 52.09  ? 606  ASN   C ND2 1 
ATOM   9210  N  N   . SER   C  1 306 ? -3.208  -58.914 -68.117  1.00 30.94  ? 607  SER   C N   1 
ATOM   9211  C  CA  . SER   C  1 306 ? -3.777  -58.211 -69.255  1.00 37.17  ? 607  SER   C CA  1 
ATOM   9212  C  C   . SER   C  1 306 ? -3.322  -58.772 -70.598  1.00 37.25  ? 607  SER   C C   1 
ATOM   9213  O  O   . SER   C  1 306 ? -3.640  -58.181 -71.638  1.00 31.15  ? 607  SER   C O   1 
ATOM   9214  C  CB  . SER   C  1 306 ? -3.422  -56.728 -69.172  1.00 41.21  ? 607  SER   C CB  1 
ATOM   9215  O  OG  . SER   C  1 306 ? -2.013  -56.557 -69.191  1.00 56.26  ? 607  SER   C OG  1 
ATOM   9216  N  N   . ARG   C  1 307 ? -2.568  -59.876 -70.605  1.00 31.32  ? 608  ARG   C N   1 
ATOM   9217  C  CA  . ARG   C  1 307 ? -2.149  -60.498 -71.860  1.00 22.46  ? 608  ARG   C CA  1 
ATOM   9218  C  C   . ARG   C  1 307 ? -2.861  -61.832 -72.030  1.00 27.06  ? 608  ARG   C C   1 
ATOM   9219  O  O   . ARG   C  1 307 ? -4.070  -61.927 -71.790  1.00 32.25  ? 608  ARG   C O   1 
ATOM   9220  C  CB  . ARG   C  1 307 ? -0.627  -60.667 -71.901  1.00 25.23  ? 608  ARG   C CB  1 
ATOM   9221  C  CG  . ARG   C  1 307 ? 0.145   -59.338 -71.809  1.00 30.63  ? 608  ARG   C CG  1 
ATOM   9222  C  CD  . ARG   C  1 307 ? -0.109  -58.415 -73.016  1.00 36.57  ? 608  ARG   C CD  1 
ATOM   9223  N  NE  . ARG   C  1 307 ? 0.299   -59.039 -74.273  1.00 32.77  ? 608  ARG   C NE  1 
ATOM   9224  C  CZ  . ARG   C  1 307 ? 1.561   -59.267 -74.622  1.00 35.26  ? 608  ARG   C CZ  1 
ATOM   9225  N  NH1 . ARG   C  1 307 ? 2.555   -58.909 -73.807  1.00 25.21  ? 608  ARG   C NH1 1 
ATOM   9226  N  NH2 . ARG   C  1 307 ? 1.833   -59.856 -75.784  1.00 32.19  ? 608  ARG   C NH2 1 
ATOM   9227  N  N   . TYR   C  1 308 ? -2.151  -62.876 -72.449  1.00 26.69  ? 609  TYR   C N   1 
ATOM   9228  C  CA  . TYR   C  1 308 ? -2.864  -64.128 -72.670  1.00 27.88  ? 609  TYR   C CA  1 
ATOM   9229  C  C   . TYR   C  1 308 ? -3.318  -64.766 -71.362  1.00 32.83  ? 609  TYR   C C   1 
ATOM   9230  O  O   . TYR   C  1 308 ? -4.235  -65.593 -71.381  1.00 32.88  ? 609  TYR   C O   1 
ATOM   9231  C  CB  . TYR   C  1 308 ? -2.006  -65.093 -73.484  1.00 28.84  ? 609  TYR   C CB  1 
ATOM   9232  C  CG  . TYR   C  1 308 ? -2.127  -64.850 -74.974  1.00 30.06  ? 609  TYR   C CG  1 
ATOM   9233  C  CD1 . TYR   C  1 308 ? -1.354  -63.885 -75.612  1.00 26.69  ? 609  TYR   C CD1 1 
ATOM   9234  C  CD2 . TYR   C  1 308 ? -3.029  -65.568 -75.734  1.00 28.03  ? 609  TYR   C CD2 1 
ATOM   9235  C  CE1 . TYR   C  1 308 ? -1.470  -63.660 -76.981  1.00 27.87  ? 609  TYR   C CE1 1 
ATOM   9236  C  CE2 . TYR   C  1 308 ? -3.154  -65.348 -77.088  1.00 30.37  ? 609  TYR   C CE2 1 
ATOM   9237  C  CZ  . TYR   C  1 308 ? -2.372  -64.400 -77.706  1.00 32.68  ? 609  TYR   C CZ  1 
ATOM   9238  O  OH  . TYR   C  1 308 ? -2.511  -64.197 -79.062  1.00 30.79  ? 609  TYR   C OH  1 
ATOM   9239  N  N   . ASN   C  1 309 ? -2.702  -64.396 -70.236  1.00 29.48  ? 610  ASN   C N   1 
ATOM   9240  C  CA  . ASN   C  1 309 ? -3.227  -64.687 -68.892  1.00 29.96  ? 610  ASN   C CA  1 
ATOM   9241  C  C   . ASN   C  1 309 ? -3.547  -66.176 -68.700  1.00 28.05  ? 610  ASN   C C   1 
ATOM   9242  O  O   . ASN   C  1 309 ? -4.679  -66.565 -68.405  1.00 34.36  ? 610  ASN   C O   1 
ATOM   9243  C  CB  . ASN   C  1 309 ? -4.464  -63.820 -68.617  1.00 34.99  ? 610  ASN   C CB  1 
ATOM   9244  C  CG  . ASN   C  1 309 ? -4.986  -63.976 -67.200  1.00 34.81  ? 610  ASN   C CG  1 
ATOM   9245  O  OD1 . ASN   C  1 309 ? -4.219  -64.210 -66.270  1.00 29.19  ? 610  ASN   C OD1 1 
ATOM   9246  N  ND2 . ASN   C  1 309 ? -6.299  -63.883 -67.038  1.00 31.49  ? 610  ASN   C ND2 1 
ATOM   9247  N  N   . ILE   C  1 310 ? -2.528  -67.026 -68.861  1.00 29.04  ? 611  ILE   C N   1 
ATOM   9248  C  CA  . ILE   C  1 310 ? -2.771  -68.473 -68.895  1.00 28.97  ? 611  ILE   C CA  1 
ATOM   9249  C  C   . ILE   C  1 310 ? -2.450  -69.163 -67.581  1.00 33.23  ? 611  ILE   C C   1 
ATOM   9250  O  O   . ILE   C  1 310 ? -2.613  -70.388 -67.487  1.00 32.37  ? 611  ILE   C O   1 
ATOM   9251  C  CB  . ILE   C  1 310 ? -1.976  -69.166 -70.023  1.00 30.77  ? 611  ILE   C CB  1 
ATOM   9252  C  CG1 . ILE   C  1 310 ? -0.485  -69.179 -69.671  1.00 31.66  ? 611  ILE   C CG1 1 
ATOM   9253  C  CG2 . ILE   C  1 310 ? -2.218  -68.485 -71.366  1.00 32.44  ? 611  ILE   C CG2 1 
ATOM   9254  C  CD1 . ILE   C  1 310 ? 0.346   -70.085 -70.563  1.00 27.05  ? 611  ILE   C CD1 1 
ATOM   9255  N  N   . LEU   C  1 311 ? -1.987  -68.424 -66.567  1.00 26.96  ? 612  LEU   C N   1 
ATOM   9256  C  CA  . LEU   C  1 311 ? -1.586  -69.059 -65.314  1.00 27.31  ? 612  LEU   C CA  1 
ATOM   9257  C  C   . LEU   C  1 311 ? -2.668  -69.985 -64.770  1.00 27.41  ? 612  LEU   C C   1 
ATOM   9258  O  O   . LEU   C  1 311 ? -2.384  -71.118 -64.377  1.00 28.83  ? 612  LEU   C O   1 
ATOM   9259  C  CB  . LEU   C  1 311 ? -1.229  -67.992 -64.278  1.00 26.49  ? 612  LEU   C CB  1 
ATOM   9260  C  CG  . LEU   C  1 311 ? 0.154   -67.398 -64.471  1.00 26.65  ? 612  LEU   C CG  1 
ATOM   9261  C  CD1 . LEU   C  1 311 ? 0.376   -66.300 -63.448  1.00 36.06  ? 612  LEU   C CD1 1 
ATOM   9262  C  CD2 . LEU   C  1 311 ? 1.179   -68.502 -64.313  1.00 25.47  ? 612  LEU   C CD2 1 
ATOM   9263  N  N   . GLU   C  1 312 ? -3.918  -69.526 -64.742  1.00 32.66  ? 613  GLU   C N   1 
ATOM   9264  C  CA  . GLU   C  1 312 ? -4.954  -70.325 -64.091  1.00 40.62  ? 613  GLU   C CA  1 
ATOM   9265  C  C   . GLU   C  1 312 ? -5.229  -71.625 -64.851  1.00 38.88  ? 613  GLU   C C   1 
ATOM   9266  O  O   . GLU   C  1 312 ? -5.394  -72.688 -64.236  1.00 39.41  ? 613  GLU   C O   1 
ATOM   9267  C  CB  . GLU   C  1 312 ? -6.233  -69.501 -63.923  1.00 47.20  ? 613  GLU   C CB  1 
ATOM   9268  C  CG  . GLU   C  1 312 ? -7.398  -70.297 -63.360  1.00 63.40  ? 613  GLU   C CG  1 
ATOM   9269  C  CD  . GLU   C  1 312 ? -8.631  -69.450 -63.118  1.00 71.78  ? 613  GLU   C CD  1 
ATOM   9270  O  OE1 . GLU   C  1 312 ? -8.529  -68.208 -63.219  1.00 74.96  ? 613  GLU   C OE1 1 
ATOM   9271  O  OE2 . GLU   C  1 312 ? -9.701  -70.030 -62.830  1.00 70.35  ? 613  GLU   C OE2 1 
ATOM   9272  N  N   . GLU   C  1 313 ? -5.279  -71.570 -66.183  1.00 38.51  ? 614  GLU   C N   1 
ATOM   9273  C  CA  . GLU   C  1 313 ? -5.476  -72.803 -66.942  1.00 39.28  ? 614  GLU   C CA  1 
ATOM   9274  C  C   . GLU   C  1 313 ? -4.305  -73.755 -66.752  1.00 36.32  ? 614  GLU   C C   1 
ATOM   9275  O  O   . GLU   C  1 313 ? -4.499  -74.962 -66.585  1.00 41.47  ? 614  GLU   C O   1 
ATOM   9276  C  CB  . GLU   C  1 313 ? -5.671  -72.514 -68.430  1.00 40.55  ? 614  GLU   C CB  1 
ATOM   9277  C  CG  . GLU   C  1 313 ? -6.036  -73.774 -69.199  1.00 48.45  ? 614  GLU   C CG  1 
ATOM   9278  C  CD  . GLU   C  1 313 ? -6.270  -73.538 -70.683  1.00 67.12  ? 614  GLU   C CD  1 
ATOM   9279  O  OE1 . GLU   C  1 313 ? -6.721  -74.487 -71.369  1.00 70.11  ? 614  GLU   C OE1 1 
ATOM   9280  O  OE2 . GLU   C  1 313 ? -6.003  -72.411 -71.160  1.00 66.08  ? 614  GLU   C OE2 1 
ATOM   9281  N  N   . VAL   C  1 314 ? -3.081  -73.230 -66.762  1.00 29.50  ? 615  VAL   C N   1 
ATOM   9282  C  CA  . VAL   C  1 314 ? -1.915  -74.092 -66.611  1.00 30.34  ? 615  VAL   C CA  1 
ATOM   9283  C  C   . VAL   C  1 314 ? -1.876  -74.695 -65.220  1.00 36.76  ? 615  VAL   C C   1 
ATOM   9284  O  O   . VAL   C  1 314 ? -1.572  -75.884 -65.047  1.00 35.50  ? 615  VAL   C O   1 
ATOM   9285  C  CB  . VAL   C  1 314 ? -0.629  -73.314 -66.921  1.00 34.86  ? 615  VAL   C CB  1 
ATOM   9286  C  CG1 . VAL   C  1 314 ? 0.605   -74.121 -66.493  1.00 27.57  ? 615  VAL   C CG1 1 
ATOM   9287  C  CG2 . VAL   C  1 314 ? -0.582  -72.958 -68.408  1.00 34.43  ? 615  VAL   C CG2 1 
ATOM   9288  N  N   . ALA   C  1 315 ? -2.173  -73.888 -64.205  1.00 34.80  ? 616  ALA   C N   1 
ATOM   9289  C  CA  . ALA   C  1 315 ? -2.173  -74.408 -62.850  1.00 33.13  ? 616  ALA   C CA  1 
ATOM   9290  C  C   . ALA   C  1 315 ? -3.259  -75.459 -62.675  1.00 38.87  ? 616  ALA   C C   1 
ATOM   9291  O  O   . ALA   C  1 315 ? -3.045  -76.473 -62.004  1.00 36.52  ? 616  ALA   C O   1 
ATOM   9292  C  CB  . ALA   C  1 315 ? -2.352  -73.267 -61.862  1.00 29.88  ? 616  ALA   C CB  1 
ATOM   9293  N  N   . LYS   C  1 316 ? -4.433  -75.232 -63.275  1.00 41.20  ? 617  LYS   C N   1 
ATOM   9294  C  CA  . LYS   C  1 316 ? -5.489  -76.241 -63.244  1.00 48.86  ? 617  LYS   C CA  1 
ATOM   9295  C  C   . LYS   C  1 316 ? -4.972  -77.575 -63.760  1.00 46.65  ? 617  LYS   C C   1 
ATOM   9296  O  O   . LYS   C  1 316 ? -5.075  -78.601 -63.082  1.00 42.09  ? 617  LYS   C O   1 
ATOM   9297  C  CB  . LYS   C  1 316 ? -6.687  -75.791 -64.080  1.00 54.22  ? 617  LYS   C CB  1 
ATOM   9298  C  CG  . LYS   C  1 316 ? -7.721  -74.939 -63.376  1.00 61.74  ? 617  LYS   C CG  1 
ATOM   9299  C  CD  . LYS   C  1 316 ? -8.709  -74.398 -64.414  1.00 69.09  ? 617  LYS   C CD  1 
ATOM   9300  C  CE  . LYS   C  1 316 ? -10.030 -73.972 -63.792  1.00 71.52  ? 617  LYS   C CE  1 
ATOM   9301  N  NZ  . LYS   C  1 316 ? -9.864  -72.844 -62.839  1.00 67.05  ? 617  LYS   C NZ  1 
ATOM   9302  N  N   . LYS   C  1 317 ? -4.390  -77.575 -64.963  1.00 43.16  ? 618  LYS   C N   1 
ATOM   9303  C  CA  . LYS   C  1 317 ? -3.871  -78.822 -65.512  1.00 42.88  ? 618  LYS   C CA  1 
ATOM   9304  C  C   . LYS   C  1 317 ? -2.749  -79.397 -64.660  1.00 41.23  ? 618  LYS   C C   1 
ATOM   9305  O  O   . LYS   C  1 317 ? -2.542  -80.613 -64.672  1.00 38.17  ? 618  LYS   C O   1 
ATOM   9306  C  CB  . LYS   C  1 317 ? -3.400  -78.610 -66.954  1.00 45.61  ? 618  LYS   C CB  1 
ATOM   9307  C  CG  . LYS   C  1 317 ? -4.524  -78.191 -67.896  1.00 54.86  ? 618  LYS   C CG  1 
ATOM   9308  C  CD  . LYS   C  1 317 ? -4.407  -78.868 -69.244  1.00 60.62  ? 618  LYS   C CD  1 
ATOM   9309  C  CE  . LYS   C  1 317 ? -5.539  -78.459 -70.182  1.00 71.98  ? 618  LYS   C CE  1 
ATOM   9310  N  NZ  . LYS   C  1 317 ? -6.864  -79.002 -69.762  1.00 74.39  ? 618  LYS   C NZ  1 
ATOM   9311  N  N   . MET   C  1 318 ? -2.032  -78.563 -63.904  1.00 40.84  ? 619  MET   C N   1 
ATOM   9312  C  CA  . MET   C  1 318 ? -1.029  -79.078 -62.976  1.00 44.46  ? 619  MET   C CA  1 
ATOM   9313  C  C   . MET   C  1 318 ? -1.627  -79.609 -61.683  1.00 41.08  ? 619  MET   C C   1 
ATOM   9314  O  O   . MET   C  1 318 ? -0.879  -80.128 -60.845  1.00 41.19  ? 619  MET   C O   1 
ATOM   9315  C  CB  . MET   C  1 318 ? 0.006   -77.997 -62.666  1.00 38.04  ? 619  MET   C CB  1 
ATOM   9316  C  CG  . MET   C  1 318 ? 0.916   -77.731 -63.854  1.00 31.90  ? 619  MET   C CG  1 
ATOM   9317  S  SD  . MET   C  1 318 ? 2.047   -76.383 -63.568  1.00 36.80  ? 619  MET   C SD  1 
ATOM   9318  C  CE  . MET   C  1 318 ? 3.021   -77.048 -62.205  1.00 31.44  ? 619  MET   C CE  1 
ATOM   9319  N  N   . ASN   C  1 319 ? -2.948  -79.505 -61.516  1.00 42.77  ? 620  ASN   C N   1 
ATOM   9320  C  CA  A ASN   C  1 319 ? -3.630  -79.949 -60.300  0.50 46.41  ? 620  ASN   C CA  1 
ATOM   9321  C  CA  B ASN   C  1 319 ? -3.637  -79.943 -60.302  0.50 46.42  ? 620  ASN   C CA  1 
ATOM   9322  C  C   . ASN   C  1 319 ? -3.106  -79.205 -59.072  1.00 47.46  ? 620  ASN   C C   1 
ATOM   9323  O  O   . ASN   C  1 319 ? -2.990  -79.767 -57.982  1.00 52.54  ? 620  ASN   C O   1 
ATOM   9324  C  CB  A ASN   C  1 319 ? -3.505  -81.465 -60.113  0.50 48.31  ? 620  ASN   C CB  1 
ATOM   9325  C  CB  B ASN   C  1 319 ? -3.538  -81.460 -60.117  0.50 48.34  ? 620  ASN   C CB  1 
ATOM   9326  C  CG  A ASN   C  1 319 ? -4.042  -82.248 -61.295  0.50 51.70  ? 620  ASN   C CG  1 
ATOM   9327  C  CG  B ASN   C  1 319 ? -4.446  -81.968 -59.017  0.50 49.92  ? 620  ASN   C CG  1 
ATOM   9328  O  OD1 A ASN   C  1 319 ? -5.116  -81.950 -61.815  0.50 55.34  ? 620  ASN   C OD1 1 
ATOM   9329  O  OD1 B ASN   C  1 319 ? -5.502  -81.393 -58.763  0.50 50.92  ? 620  ASN   C OD1 1 
ATOM   9330  N  ND2 A ASN   C  1 319 ? -3.290  -83.257 -61.729  0.50 52.48  ? 620  ASN   C ND2 1 
ATOM   9331  N  ND2 B ASN   C  1 319 ? -4.031  -83.036 -58.344  0.50 53.77  ? 620  ASN   C ND2 1 
ATOM   9332  N  N   . LEU   C  1 320 ? -2.785  -77.931 -59.245  1.00 43.94  ? 621  LEU   C N   1 
ATOM   9333  C  CA  . LEU   C  1 320 ? -2.251  -77.154 -58.141  1.00 42.44  ? 621  LEU   C CA  1 
ATOM   9334  C  C   . LEU   C  1 320 ? -3.372  -76.683 -57.225  1.00 48.57  ? 621  LEU   C C   1 
ATOM   9335  O  O   . LEU   C  1 320 ? -4.504  -76.443 -57.661  1.00 44.86  ? 621  LEU   C O   1 
ATOM   9336  C  CB  . LEU   C  1 320 ? -1.459  -75.960 -58.664  1.00 38.99  ? 621  LEU   C CB  1 
ATOM   9337  C  CG  . LEU   C  1 320 ? -0.210  -76.349 -59.453  1.00 37.92  ? 621  LEU   C CG  1 
ATOM   9338  C  CD1 . LEU   C  1 320 ? 0.625   -75.110 -59.774  1.00 31.95  ? 621  LEU   C CD1 1 
ATOM   9339  C  CD2 . LEU   C  1 320 ? 0.598   -77.369 -58.665  1.00 40.38  ? 621  LEU   C CD2 1 
ATOM   9340  N  N   . ASP   C  1 321 ? -3.055  -76.578 -55.936  1.00 55.96  ? 622  ASP   C N   1 
ATOM   9341  C  CA  . ASP   C  1 321 ? -3.975  -75.962 -54.987  1.00 51.87  ? 622  ASP   C CA  1 
ATOM   9342  C  C   . ASP   C  1 321 ? -4.016  -74.468 -55.253  1.00 42.13  ? 622  ASP   C C   1 
ATOM   9343  O  O   . ASP   C  1 321 ? -3.048  -73.757 -54.971  1.00 42.03  ? 622  ASP   C O   1 
ATOM   9344  C  CB  . ASP   C  1 321 ? -3.545  -76.241 -53.554  1.00 55.19  ? 622  ASP   C CB  1 
ATOM   9345  C  CG  . ASP   C  1 321 ? -4.358  -75.450 -52.539  1.00 64.28  ? 622  ASP   C CG  1 
ATOM   9346  O  OD1 . ASP   C  1 321 ? -3.774  -75.012 -51.525  1.00 67.53  ? 622  ASP   C OD1 1 
ATOM   9347  O  OD2 . ASP   C  1 321 ? -5.572  -75.252 -52.768  1.00 62.98  ? 622  ASP   C OD2 1 
ATOM   9348  N  N   . MET   C  1 322 ? -5.126  -73.989 -55.808  1.00 41.16  ? 623  MET   C N   1 
ATOM   9349  C  CA  . MET   C  1 322 ? -5.252  -72.594 -56.204  1.00 44.20  ? 623  MET   C CA  1 
ATOM   9350  C  C   . MET   C  1 322 ? -6.156  -71.797 -55.275  1.00 44.38  ? 623  MET   C C   1 
ATOM   9351  O  O   . MET   C  1 322 ? -6.533  -70.668 -55.611  1.00 51.58  ? 623  MET   C O   1 
ATOM   9352  C  CB  . MET   C  1 322 ? -5.767  -72.502 -57.639  1.00 41.47  ? 623  MET   C CB  1 
ATOM   9353  C  CG  . MET   C  1 322 ? -5.012  -73.377 -58.616  1.00 46.35  ? 623  MET   C CG  1 
ATOM   9354  S  SD  . MET   C  1 322 ? -5.739  -73.269 -60.251  1.00 50.84  ? 623  MET   C SD  1 
ATOM   9355  C  CE  . MET   C  1 322 ? -5.930  -71.502 -60.425  1.00 42.48  ? 623  MET   C CE  1 
ATOM   9356  N  N   . ARG   C  1 323 ? -6.506  -72.348 -54.115  1.00 41.67  ? 624  ARG   C N   1 
ATOM   9357  C  CA  . ARG   C  1 323 ? -7.433  -71.670 -53.218  1.00 52.79  ? 624  ARG   C CA  1 
ATOM   9358  C  C   . ARG   C  1 323 ? -6.769  -70.608 -52.354  1.00 52.38  ? 624  ARG   C C   1 
ATOM   9359  O  O   . ARG   C  1 323 ? -7.477  -69.766 -51.790  1.00 60.24  ? 624  ARG   C O   1 
ATOM   9360  C  CB  . ARG   C  1 323 ? -8.136  -72.682 -52.318  1.00 56.89  ? 624  ARG   C CB  1 
ATOM   9361  C  CG  . ARG   C  1 323 ? -9.161  -73.551 -53.026  1.00 61.19  ? 624  ARG   C CG  1 
ATOM   9362  C  CD  . ARG   C  1 323 ? -9.694  -74.629 -52.086  1.00 70.80  ? 624  ARG   C CD  1 
ATOM   9363  N  NE  . ARG   C  1 323 ? -8.620  -75.467 -51.557  1.00 79.12  ? 624  ARG   C NE  1 
ATOM   9364  C  CZ  . ARG   C  1 323 ? -8.097  -75.341 -50.341  1.00 94.41  ? 624  ARG   C CZ  1 
ATOM   9365  N  NH1 . ARG   C  1 323 ? -8.551  -74.409 -49.510  1.00 101.15 ? 624  ARG   C NH1 1 
ATOM   9366  N  NH2 . ARG   C  1 323 ? -7.116  -76.146 -49.955  1.00 96.75  ? 624  ARG   C NH2 1 
ATOM   9367  N  N   . LYS   C  1 324 ? -5.442  -70.626 -52.223  1.00 42.63  ? 625  LYS   C N   1 
ATOM   9368  C  CA  . LYS   C  1 324 ? -4.745  -69.585 -51.478  1.00 46.28  ? 625  LYS   C CA  1 
ATOM   9369  C  C   . LYS   C  1 324 ? -3.441  -69.234 -52.181  1.00 45.33  ? 625  LYS   C C   1 
ATOM   9370  O  O   . LYS   C  1 324 ? -2.867  -70.050 -52.906  1.00 45.17  ? 625  LYS   C O   1 
ATOM   9371  C  CB  . LYS   C  1 324 ? -4.472  -70.005 -50.030  1.00 54.54  ? 625  LYS   C CB  1 
ATOM   9372  C  CG  . LYS   C  1 324 ? -3.744  -71.324 -49.914  1.00 67.16  ? 625  LYS   C CG  1 
ATOM   9373  C  CD  . LYS   C  1 324 ? -4.255  -72.150 -48.747  1.00 77.05  ? 625  LYS   C CD  1 
ATOM   9374  C  CE  . LYS   C  1 324 ? -3.520  -73.478 -48.688  1.00 80.07  ? 625  LYS   C CE  1 
ATOM   9375  N  NZ  . LYS   C  1 324 ? -2.040  -73.278 -48.747  1.00 70.75  ? 625  LYS   C NZ  1 
ATOM   9376  N  N   . THR   C  1 325 ? -2.981  -68.001 -51.954  1.00 37.35  ? 626  THR   C N   1 
ATOM   9377  C  CA  . THR   C  1 325 ? -1.817  -67.498 -52.670  1.00 42.69  ? 626  THR   C CA  1 
ATOM   9378  C  C   . THR   C  1 325 ? -0.531  -68.175 -52.215  1.00 34.31  ? 626  THR   C C   1 
ATOM   9379  O  O   . THR   C  1 325 ? 0.386   -68.382 -53.029  1.00 35.45  ? 626  THR   C O   1 
ATOM   9380  C  CB  . THR   C  1 325 ? -1.700  -65.979 -52.489  1.00 49.21  ? 626  THR   C CB  1 
ATOM   9381  O  OG1 . THR   C  1 325 ? -1.569  -65.661 -51.097  1.00 50.17  ? 626  THR   C OG1 1 
ATOM   9382  C  CG2 . THR   C  1 325 ? -2.924  -65.269 -53.064  1.00 47.20  ? 626  THR   C CG2 1 
ATOM   9383  N  N   . SER   C  1 326 ? -0.448  -68.527 -50.930  1.00 34.40  ? 627  SER   C N   1 
ATOM   9384  C  CA  . SER   C  1 326 ? 0.797   -68.992 -50.336  1.00 35.28  ? 627  SER   C CA  1 
ATOM   9385  C  C   . SER   C  1 326 ? 1.157   -70.405 -50.768  1.00 36.03  ? 627  SER   C C   1 
ATOM   9386  O  O   . SER   C  1 326 ? 2.277   -70.853 -50.499  1.00 36.66  ? 627  SER   C O   1 
ATOM   9387  C  CB  . SER   C  1 326 ? 0.721   -68.888 -48.802  1.00 31.94  ? 627  SER   C CB  1 
ATOM   9388  O  OG  . SER   C  1 326 ? -0.366  -69.630 -48.294  1.00 43.80  ? 627  SER   C OG  1 
ATOM   9389  N  N   . SER   C  1 327 ? 0.259   -71.109 -51.454  1.00 34.13  ? 628  SER   C N   1 
ATOM   9390  C  CA  . SER   C  1 327 ? 0.699   -72.324 -52.118  1.00 41.88  ? 628  SER   C CA  1 
ATOM   9391  C  C   . SER   C  1 327 ? 1.689   -72.033 -53.239  1.00 35.25  ? 628  SER   C C   1 
ATOM   9392  O  O   . SER   C  1 327 ? 2.346   -72.965 -53.710  1.00 37.25  ? 628  SER   C O   1 
ATOM   9393  C  CB  . SER   C  1 327 ? -0.502  -73.092 -52.667  1.00 43.32  ? 628  SER   C CB  1 
ATOM   9394  O  OG  . SER   C  1 327 ? -1.051  -72.434 -53.790  1.00 42.54  ? 628  SER   C OG  1 
ATOM   9395  N  N   . LEU   C  1 328 ? 1.823   -70.768 -53.654  1.00 30.28  ? 629  LEU   C N   1 
ATOM   9396  C  CA  . LEU   C  1 328 ? 2.697   -70.369 -54.762  1.00 33.24  ? 629  LEU   C CA  1 
ATOM   9397  C  C   . LEU   C  1 328 ? 2.359   -71.114 -56.050  1.00 32.59  ? 629  LEU   C C   1 
ATOM   9398  O  O   . LEU   C  1 328 ? 3.238   -71.395 -56.876  1.00 28.10  ? 629  LEU   C O   1 
ATOM   9399  C  CB  . LEU   C  1 328 ? 4.175   -70.548 -54.410  1.00 30.42  ? 629  LEU   C CB  1 
ATOM   9400  C  CG  . LEU   C  1 328 ? 4.598   -69.803 -53.135  1.00 34.22  ? 629  LEU   C CG  1 
ATOM   9401  C  CD1 . LEU   C  1 328 ? 6.099   -69.671 -53.048  1.00 27.97  ? 629  LEU   C CD1 1 
ATOM   9402  C  CD2 . LEU   C  1 328 ? 3.961   -68.429 -53.097  1.00 30.00  ? 629  LEU   C CD2 1 
ATOM   9403  N  N   . TRP   C  1 329 ? 1.077   -71.426 -56.237  1.00 35.81  ? 630  TRP   C N   1 
ATOM   9404  C  CA  . TRP   C  1 329 ? 0.659   -72.079 -57.471  1.00 37.23  ? 630  TRP   C CA  1 
ATOM   9405  C  C   . TRP   C  1 329 ? 0.995   -71.232 -58.692  1.00 36.10  ? 630  TRP   C C   1 
ATOM   9406  O  O   . TRP   C  1 329 ? 1.397   -71.775 -59.729  1.00 34.56  ? 630  TRP   C O   1 
ATOM   9407  C  CB  . TRP   C  1 329 ? -0.835  -72.413 -57.426  1.00 33.11  ? 630  TRP   C CB  1 
ATOM   9408  C  CG  . TRP   C  1 329 ? -1.788  -71.240 -57.334  1.00 34.64  ? 630  TRP   C CG  1 
ATOM   9409  C  CD1 . TRP   C  1 329 ? -2.316  -70.689 -56.190  1.00 37.67  ? 630  TRP   C CD1 1 
ATOM   9410  C  CD2 . TRP   C  1 329 ? -2.368  -70.523 -58.427  1.00 29.68  ? 630  TRP   C CD2 1 
ATOM   9411  N  NE1 . TRP   C  1 329 ? -3.172  -69.664 -56.515  1.00 34.77  ? 630  TRP   C NE1 1 
ATOM   9412  C  CE2 . TRP   C  1 329 ? -3.218  -69.541 -57.882  1.00 29.93  ? 630  TRP   C CE2 1 
ATOM   9413  C  CE3 . TRP   C  1 329 ? -2.251  -70.618 -59.819  1.00 30.63  ? 630  TRP   C CE3 1 
ATOM   9414  C  CZ2 . TRP   C  1 329 ? -3.940  -68.652 -58.679  1.00 32.32  ? 630  TRP   C CZ2 1 
ATOM   9415  C  CZ3 . TRP   C  1 329 ? -2.967  -69.734 -60.610  1.00 36.42  ? 630  TRP   C CZ3 1 
ATOM   9416  C  CH2 . TRP   C  1 329 ? -3.802  -68.760 -60.036  1.00 29.09  ? 630  TRP   C CH2 1 
ATOM   9417  N  N   . LYS   C  1 330 ? 0.862   -69.902 -58.594  1.00 29.38  ? 631  LYS   C N   1 
ATOM   9418  C  CA  . LYS   C  1 330 ? 1.210   -69.063 -59.742  1.00 28.90  ? 631  LYS   C CA  1 
ATOM   9419  C  C   . LYS   C  1 330 ? 2.685   -69.190 -60.081  1.00 35.87  ? 631  LYS   C C   1 
ATOM   9420  O  O   . LYS   C  1 330 ? 3.062   -69.308 -61.259  1.00 30.28  ? 631  LYS   C O   1 
ATOM   9421  C  CB  . LYS   C  1 330 ? 0.868   -67.599 -59.479  1.00 27.33  ? 631  LYS   C CB  1 
ATOM   9422  C  CG  . LYS   C  1 330 ? -0.615  -67.302 -59.495  1.00 36.16  ? 631  LYS   C CG  1 
ATOM   9423  C  CD  . LYS   C  1 330 ? -0.855  -65.809 -59.361  1.00 36.85  ? 631  LYS   C CD  1 
ATOM   9424  C  CE  . LYS   C  1 330 ? -2.311  -65.471 -59.593  1.00 38.89  ? 631  LYS   C CE  1 
ATOM   9425  N  NZ  . LYS   C  1 330 ? -2.503  -64.007 -59.524  1.00 32.60  ? 631  LYS   C NZ  1 
ATOM   9426  N  N   . ASP   C  1 331 ? 3.534   -69.144 -59.055  1.00 25.99  ? 632  ASP   C N   1 
ATOM   9427  C  CA  . ASP   C  1 331 ? 4.973   -69.249 -59.262  1.00 28.67  ? 632  ASP   C CA  1 
ATOM   9428  C  C   . ASP   C  1 331 ? 5.333   -70.592 -59.876  1.00 29.24  ? 632  ASP   C C   1 
ATOM   9429  O  O   . ASP   C  1 331 ? 6.177   -70.666 -60.778  1.00 27.51  ? 632  ASP   C O   1 
ATOM   9430  C  CB  . ASP   C  1 331 ? 5.711   -69.069 -57.931  1.00 34.35  ? 632  ASP   C CB  1 
ATOM   9431  C  CG  . ASP   C  1 331 ? 5.171   -67.901 -57.112  1.00 31.91  ? 632  ASP   C CG  1 
ATOM   9432  O  OD1 . ASP   C  1 331 ? 4.020   -67.988 -56.641  1.00 30.43  ? 632  ASP   C OD1 1 
ATOM   9433  O  OD2 . ASP   C  1 331 ? 5.888   -66.892 -56.959  1.00 31.45  ? 632  ASP   C OD2 1 
ATOM   9434  N  N   . GLN   C  1 332 ? 4.700   -71.664 -59.386  1.00 29.52  ? 633  GLN   C N   1 
ATOM   9435  C  CA  . GLN   C  1 332 ? 4.986   -72.997 -59.893  1.00 33.13  ? 633  GLN   C CA  1 
ATOM   9436  C  C   . GLN   C  1 332 ? 4.607   -73.112 -61.361  1.00 29.26  ? 633  GLN   C C   1 
ATOM   9437  O  O   . GLN   C  1 332 ? 5.386   -73.614 -62.180  1.00 31.31  ? 633  GLN   C O   1 
ATOM   9438  C  CB  . GLN   C  1 332 ? 4.240   -74.036 -59.055  1.00 35.50  ? 633  GLN   C CB  1 
ATOM   9439  C  CG  . GLN   C  1 332 ? 5.149   -75.087 -58.451  1.00 47.88  ? 633  GLN   C CG  1 
ATOM   9440  C  CD  . GLN   C  1 332 ? 4.454   -75.904 -57.376  1.00 52.32  ? 633  GLN   C CD  1 
ATOM   9441  O  OE1 . GLN   C  1 332 ? 3.282   -75.683 -57.075  1.00 42.01  ? 633  GLN   C OE1 1 
ATOM   9442  N  NE2 . GLN   C  1 332 ? 5.178   -76.849 -56.787  1.00 67.89  ? 633  GLN   C NE2 1 
ATOM   9443  N  N   . ALA   C  1 333 ? 3.405   -72.646 -61.709  1.00 28.95  ? 634  ALA   C N   1 
ATOM   9444  C  CA  . ALA   C  1 333 ? 2.939   -72.723 -63.089  1.00 32.80  ? 634  ALA   C CA  1 
ATOM   9445  C  C   . ALA   C  1 333 ? 3.772   -71.832 -63.998  1.00 30.05  ? 634  ALA   C C   1 
ATOM   9446  O  O   . ALA   C  1 333 ? 4.091   -72.213 -65.127  1.00 32.31  ? 634  ALA   C O   1 
ATOM   9447  C  CB  . ALA   C  1 333 ? 1.464   -72.334 -63.160  1.00 33.42  ? 634  ALA   C CB  1 
ATOM   9448  N  N   . LEU   C  1 334 ? 4.131   -70.643 -63.509  1.00 29.19  ? 635  LEU   C N   1 
ATOM   9449  C  CA  . LEU   C  1 334 ? 4.963   -69.718 -64.264  1.00 24.95  ? 635  LEU   C CA  1 
ATOM   9450  C  C   . LEU   C  1 334 ? 6.268   -70.371 -64.698  1.00 31.97  ? 635  LEU   C C   1 
ATOM   9451  O  O   . LEU   C  1 334 ? 6.707   -70.204 -65.844  1.00 30.81  ? 635  LEU   C O   1 
ATOM   9452  C  CB  . LEU   C  1 334 ? 5.241   -68.483 -63.407  1.00 23.65  ? 635  LEU   C CB  1 
ATOM   9453  C  CG  . LEU   C  1 334 ? 6.143   -67.422 -64.032  1.00 31.01  ? 635  LEU   C CG  1 
ATOM   9454  C  CD1 . LEU   C  1 334 ? 5.492   -66.809 -65.249  1.00 26.26  ? 635  LEU   C CD1 1 
ATOM   9455  C  CD2 . LEU   C  1 334 ? 6.448   -66.348 -63.008  1.00 24.40  ? 635  LEU   C CD2 1 
ATOM   9456  N  N   . VAL   C  1 335 ? 6.903   -71.122 -63.797  1.00 24.40  ? 636  VAL   C N   1 
ATOM   9457  C  CA  . VAL   C  1 335 ? 8.177   -71.754 -64.129  1.00 31.22  ? 636  VAL   C CA  1 
ATOM   9458  C  C   . VAL   C  1 335 ? 7.983   -72.787 -65.228  1.00 30.70  ? 636  VAL   C C   1 
ATOM   9459  O  O   . VAL   C  1 335 ? 8.742   -72.834 -66.202  1.00 25.64  ? 636  VAL   C O   1 
ATOM   9460  C  CB  . VAL   C  1 335 ? 8.817   -72.383 -62.881  1.00 34.35  ? 636  VAL   C CB  1 
ATOM   9461  C  CG1 . VAL   C  1 335 ? 10.015  -73.182 -63.281  1.00 29.77  ? 636  VAL   C CG1 1 
ATOM   9462  C  CG2 . VAL   C  1 335 ? 9.222   -71.294 -61.874  1.00 28.70  ? 636  VAL   C CG2 1 
ATOM   9463  N  N   . GLU   C  1 336 ? 6.954   -73.624 -65.093  1.00 27.34  ? 637  GLU   C N   1 
ATOM   9464  C  CA  . GLU   C  1 336 ? 6.723   -74.660 -66.090  1.00 32.31  ? 637  GLU   C CA  1 
ATOM   9465  C  C   . GLU   C  1 336 ? 6.440   -74.064 -67.460  1.00 32.99  ? 637  GLU   C C   1 
ATOM   9466  O  O   . GLU   C  1 336 ? 6.898   -74.593 -68.475  1.00 30.30  ? 637  GLU   C O   1 
ATOM   9467  C  CB  . GLU   C  1 336 ? 5.575   -75.556 -65.651  1.00 29.55  ? 637  GLU   C CB  1 
ATOM   9468  C  CG  . GLU   C  1 336 ? 5.817   -76.168 -64.299  1.00 31.40  ? 637  GLU   C CG  1 
ATOM   9469  C  CD  . GLU   C  1 336 ? 6.897   -77.242 -64.321  1.00 37.66  ? 637  GLU   C CD  1 
ATOM   9470  O  OE1 . GLU   C  1 336 ? 7.371   -77.619 -65.413  1.00 36.36  ? 637  GLU   C OE1 1 
ATOM   9471  O  OE2 . GLU   C  1 336 ? 7.270   -77.722 -63.234  1.00 41.21  ? 637  GLU   C OE2 1 
ATOM   9472  N  N   . ILE   C  1 337 ? 5.676   -72.970 -67.502  1.00 30.64  ? 638  ILE   C N   1 
ATOM   9473  C  CA  . ILE   C  1 337 ? 5.376   -72.308 -68.764  1.00 28.07  ? 638  ILE   C CA  1 
ATOM   9474  C  C   . ILE   C  1 337 ? 6.662   -71.848 -69.417  1.00 31.57  ? 638  ILE   C C   1 
ATOM   9475  O  O   . ILE   C  1 337 ? 6.852   -71.980 -70.633  1.00 25.69  ? 638  ILE   C O   1 
ATOM   9476  C  CB  . ILE   C  1 337 ? 4.409   -71.133 -68.527  1.00 25.05  ? 638  ILE   C CB  1 
ATOM   9477  C  CG1 . ILE   C  1 337 ? 3.063   -71.654 -68.039  1.00 27.42  ? 638  ILE   C CG1 1 
ATOM   9478  C  CG2 . ILE   C  1 337 ? 4.230   -70.273 -69.800  1.00 24.70  ? 638  ILE   C CG2 1 
ATOM   9479  C  CD1 . ILE   C  1 337 ? 2.180   -70.562 -67.502  1.00 33.26  ? 638  ILE   C CD1 1 
ATOM   9480  N  N   . ASN   C  1 338 ? 7.577   -71.319 -68.616  1.00 30.64  ? 639  ASN   C N   1 
ATOM   9481  C  CA  . ASN   C  1 338 ? 8.812   -70.817 -69.184  1.00 30.70  ? 639  ASN   C CA  1 
ATOM   9482  C  C   . ASN   C  1 338 ? 9.739   -71.945 -69.582  1.00 28.34  ? 639  ASN   C C   1 
ATOM   9483  O  O   . ASN   C  1 338 ? 10.518  -71.794 -70.529  1.00 28.96  ? 639  ASN   C O   1 
ATOM   9484  C  CB  . ASN   C  1 338 ? 9.468   -69.869 -68.198  1.00 26.89  ? 639  ASN   C CB  1 
ATOM   9485  C  CG  . ASN   C  1 338 ? 8.880   -68.510 -68.295  1.00 27.27  ? 639  ASN   C CG  1 
ATOM   9486  O  OD1 . ASN   C  1 338 ? 9.325   -67.698 -69.101  1.00 25.12  ? 639  ASN   C OD1 1 
ATOM   9487  N  ND2 . ASN   C  1 338 ? 7.827   -68.261 -67.525  1.00 25.73  ? 639  ASN   C ND2 1 
ATOM   9488  N  N   . ILE   C  1 339 ? 9.661   -73.077 -68.881  1.00 27.78  ? 640  ILE   C N   1 
ATOM   9489  C  CA  . ILE   C  1 339 ? 10.352  -74.274 -69.336  1.00 25.88  ? 640  ILE   C CA  1 
ATOM   9490  C  C   . ILE   C  1 339 ? 9.830   -74.678 -70.703  1.00 30.57  ? 640  ILE   C C   1 
ATOM   9491  O  O   . ILE   C  1 339 ? 10.606  -75.002 -71.607  1.00 28.99  ? 640  ILE   C O   1 
ATOM   9492  C  CB  . ILE   C  1 339 ? 10.194  -75.409 -68.310  1.00 25.38  ? 640  ILE   C CB  1 
ATOM   9493  C  CG1 . ILE   C  1 339 ? 11.032  -75.126 -67.061  1.00 25.36  ? 640  ILE   C CG1 1 
ATOM   9494  C  CG2 . ILE   C  1 339 ? 10.571  -76.747 -68.922  1.00 26.17  ? 640  ILE   C CG2 1 
ATOM   9495  C  CD1 . ILE   C  1 339 ? 10.844  -76.156 -65.950  1.00 26.33  ? 640  ILE   C CD1 1 
ATOM   9496  N  N   . ALA   C  1 340 ? 8.509   -74.635 -70.881  1.00 28.34  ? 641  ALA   C N   1 
ATOM   9497  C  CA  . ALA   C  1 340 ? 7.915   -75.036 -72.151  1.00 33.57  ? 641  ALA   C CA  1 
ATOM   9498  C  C   . ALA   C  1 340 ? 8.366   -74.116 -73.277  1.00 35.34  ? 641  ALA   C C   1 
ATOM   9499  O  O   . ALA   C  1 340 ? 8.763   -74.582 -74.350  1.00 30.17  ? 641  ALA   C O   1 
ATOM   9500  C  CB  . ALA   C  1 340 ? 6.390   -75.041 -72.040  1.00 31.33  ? 641  ALA   C CB  1 
ATOM   9501  N  N   . VAL   C  1 341 ? 8.312   -72.802 -73.043  1.00 24.96  ? 642  VAL   C N   1 
ATOM   9502  C  CA  . VAL   C  1 341 ? 8.735   -71.843 -74.058  1.00 29.08  ? 642  VAL   C CA  1 
ATOM   9503  C  C   . VAL   C  1 341 ? 10.160  -72.143 -74.518  1.00 30.34  ? 642  VAL   C C   1 
ATOM   9504  O  O   . VAL   C  1 341 ? 10.429  -72.224 -75.719  1.00 28.53  ? 642  VAL   C O   1 
ATOM   9505  C  CB  . VAL   C  1 341 ? 8.585   -70.407 -73.525  1.00 27.51  ? 642  VAL   C CB  1 
ATOM   9506  C  CG1 . VAL   C  1 341 ? 9.269   -69.414 -74.427  1.00 22.46  ? 642  VAL   C CG1 1 
ATOM   9507  C  CG2 . VAL   C  1 341 ? 7.100   -70.064 -73.407  1.00 26.26  ? 642  VAL   C CG2 1 
ATOM   9508  N  N   . LEU   C  1 342 ? 11.087  -72.352 -73.576  1.00 24.05  ? 643  LEU   C N   1 
ATOM   9509  C  CA  . LEU   C  1 342 ? 12.480  -72.567 -73.972  1.00 25.44  ? 643  LEU   C CA  1 
ATOM   9510  C  C   . LEU   C  1 342 ? 12.652  -73.892 -74.693  1.00 26.83  ? 643  LEU   C C   1 
ATOM   9511  O  O   . LEU   C  1 342 ? 13.318  -73.966 -75.734  1.00 23.88  ? 643  LEU   C O   1 
ATOM   9512  C  CB  . LEU   C  1 342 ? 13.395  -72.520 -72.757  1.00 23.13  ? 643  LEU   C CB  1 
ATOM   9513  C  CG  . LEU   C  1 342 ? 13.483  -71.111 -72.183  1.00 24.72  ? 643  LEU   C CG  1 
ATOM   9514  C  CD1 . LEU   C  1 342 ? 13.920  -71.176 -70.710  1.00 25.99  ? 643  LEU   C CD1 1 
ATOM   9515  C  CD2 . LEU   C  1 342 ? 14.414  -70.281 -73.012  1.00 25.48  ? 643  LEU   C CD2 1 
ATOM   9516  N  N   . TYR   C  1 343 ? 12.094  -74.956 -74.125  1.00 26.08  ? 644  TYR   C N   1 
ATOM   9517  C  CA  . TYR   C  1 343 ? 12.160  -76.268 -74.748  1.00 30.47  ? 644  TYR   C CA  1 
ATOM   9518  C  C   . TYR   C  1 343 ? 11.596  -76.243 -76.159  1.00 32.68  ? 644  TYR   C C   1 
ATOM   9519  O  O   . TYR   C  1 343 ? 12.154  -76.856 -77.078  1.00 28.78  ? 644  TYR   C O   1 
ATOM   9520  C  CB  . TYR   C  1 343 ? 11.381  -77.257 -73.893  1.00 29.53  ? 644  TYR   C CB  1 
ATOM   9521  C  CG  . TYR   C  1 343 ? 11.174  -78.608 -74.514  1.00 31.29  ? 644  TYR   C CG  1 
ATOM   9522  C  CD1 . TYR   C  1 343 ? 12.226  -79.498 -74.633  1.00 33.56  ? 644  TYR   C CD1 1 
ATOM   9523  C  CD2 . TYR   C  1 343 ? 9.913   -79.014 -74.939  1.00 34.76  ? 644  TYR   C CD2 1 
ATOM   9524  C  CE1 . TYR   C  1 343 ? 12.043  -80.753 -75.179  1.00 36.05  ? 644  TYR   C CE1 1 
ATOM   9525  C  CE2 . TYR   C  1 343 ? 9.716   -80.271 -75.481  1.00 40.27  ? 644  TYR   C CE2 1 
ATOM   9526  C  CZ  . TYR   C  1 343 ? 10.790  -81.137 -75.602  1.00 38.43  ? 644  TYR   C CZ  1 
ATOM   9527  O  OH  . TYR   C  1 343 ? 10.623  -82.398 -76.135  1.00 44.28  ? 644  TYR   C OH  1 
ATOM   9528  N  N   . SER   C  1 344 ? 10.477  -75.550 -76.343  1.00 29.76  ? 645  SER   C N   1 
ATOM   9529  C  CA  . SER   C  1 344 ? 9.816   -75.550 -77.637  1.00 30.54  ? 645  SER   C CA  1 
ATOM   9530  C  C   . SER   C  1 344 ? 10.669  -74.856 -78.690  1.00 27.55  ? 645  SER   C C   1 
ATOM   9531  O  O   . SER   C  1 344 ? 10.879  -75.397 -79.784  1.00 26.94  ? 645  SER   C O   1 
ATOM   9532  C  CB  . SER   C  1 344 ? 8.447   -74.900 -77.499  1.00 27.63  ? 645  SER   C CB  1 
ATOM   9533  O  OG  . SER   C  1 344 ? 7.626   -75.716 -76.671  1.00 31.17  ? 645  SER   C OG  1 
ATOM   9534  N  N   . PHE   C  1 345 ? 11.189  -73.668 -78.368  1.00 28.80  ? 646  PHE   C N   1 
ATOM   9535  C  CA  . PHE   C  1 345 ? 12.053  -72.963 -79.310  1.00 26.71  ? 646  PHE   C CA  1 
ATOM   9536  C  C   . PHE   C  1 345 ? 13.310  -73.773 -79.591  1.00 34.96  ? 646  PHE   C C   1 
ATOM   9537  O  O   . PHE   C  1 345 ? 13.729  -73.918 -80.748  1.00 30.27  ? 646  PHE   C O   1 
ATOM   9538  C  CB  . PHE   C  1 345 ? 12.428  -71.577 -78.777  1.00 21.84  ? 646  PHE   C CB  1 
ATOM   9539  C  CG  . PHE   C  1 345 ? 11.426  -70.498 -79.085  1.00 21.28  ? 646  PHE   C CG  1 
ATOM   9540  C  CD1 . PHE   C  1 345 ? 10.130  -70.573 -78.604  1.00 26.43  ? 646  PHE   C CD1 1 
ATOM   9541  C  CD2 . PHE   C  1 345 ? 11.801  -69.377 -79.820  1.00 25.14  ? 646  PHE   C CD2 1 
ATOM   9542  C  CE1 . PHE   C  1 345 ? 9.211   -69.565 -78.865  1.00 26.92  ? 646  PHE   C CE1 1 
ATOM   9543  C  CE2 . PHE   C  1 345 ? 10.884  -68.361 -80.110  1.00 21.56  ? 646  PHE   C CE2 1 
ATOM   9544  C  CZ  . PHE   C  1 345 ? 9.589   -68.454 -79.635  1.00 27.79  ? 646  PHE   C CZ  1 
ATOM   9545  N  N   . GLN   C  1 346 ? 13.922  -74.318 -78.541  1.00 28.62  ? 647  GLN   C N   1 
ATOM   9546  C  CA  . GLN   C  1 346 ? 15.147  -75.082 -78.739  1.00 33.78  ? 647  GLN   C CA  1 
ATOM   9547  C  C   . GLN   C  1 346 ? 14.886  -76.322 -79.581  1.00 32.00  ? 647  GLN   C C   1 
ATOM   9548  O  O   . GLN   C  1 346 ? 15.701  -76.677 -80.438  1.00 36.17  ? 647  GLN   C O   1 
ATOM   9549  C  CB  . GLN   C  1 346 ? 15.765  -75.450 -77.394  1.00 33.04  ? 647  GLN   C CB  1 
ATOM   9550  C  CG  . GLN   C  1 346 ? 16.444  -74.272 -76.719  1.00 36.27  ? 647  GLN   C CG  1 
ATOM   9551  C  CD  . GLN   C  1 346 ? 16.743  -74.530 -75.254  1.00 44.32  ? 647  GLN   C CD  1 
ATOM   9552  O  OE1 . GLN   C  1 346 ? 16.436  -75.598 -74.723  1.00 47.97  ? 647  GLN   C OE1 1 
ATOM   9553  N  NE2 . GLN   C  1 346 ? 17.337  -73.546 -74.594  1.00 41.18  ? 647  GLN   C NE2 1 
ATOM   9554  N  N   . SER   C  1 347 ? 13.740  -76.973 -79.371  1.00 30.75  ? 648  SER   C N   1 
ATOM   9555  C  CA  . SER   C  1 347 ? 13.411  -78.160 -80.140  1.00 32.35  ? 648  SER   C CA  1 
ATOM   9556  C  C   . SER   C  1 347 ? 13.183  -77.829 -81.610  1.00 37.45  ? 648  SER   C C   1 
ATOM   9557  O  O   . SER   C  1 347 ? 13.533  -78.628 -82.487  1.00 32.22  ? 648  SER   C O   1 
ATOM   9558  C  CB  . SER   C  1 347 ? 12.183  -78.842 -79.543  1.00 32.87  ? 648  SER   C CB  1 
ATOM   9559  O  OG  . SER   C  1 347 ? 12.487  -79.378 -78.267  1.00 33.55  ? 648  SER   C OG  1 
ATOM   9560  N  N   . ASP   C  1 348 ? 12.617  -76.666 -81.907  1.00 32.27  ? 649  ASP   C N   1 
ATOM   9561  C  CA  . ASP   C  1 348 ? 12.441  -76.259 -83.296  1.00 30.97  ? 649  ASP   C CA  1 
ATOM   9562  C  C   . ASP   C  1 348 ? 13.650  -75.514 -83.837  1.00 32.51  ? 649  ASP   C C   1 
ATOM   9563  O  O   . ASP   C  1 348 ? 13.599  -75.017 -84.967  1.00 27.40  ? 649  ASP   C O   1 
ATOM   9564  C  CB  . ASP   C  1 348 ? 11.183  -75.406 -83.444  1.00 27.14  ? 649  ASP   C CB  1 
ATOM   9565  C  CG  . ASP   C  1 348 ? 9.915   -76.220 -83.267  1.00 33.06  ? 649  ASP   C CG  1 
ATOM   9566  O  OD1 . ASP   C  1 348 ? 10.032  -77.448 -83.095  1.00 32.53  ? 649  ASP   C OD1 1 
ATOM   9567  O  OD2 . ASP   C  1 348 ? 8.810   -75.639 -83.288  1.00 37.22  ? 649  ASP   C OD2 1 
ATOM   9568  N  N   . LYS   C  1 349 ? 14.728  -75.426 -83.051  1.00 31.72  ? 650  LYS   C N   1 
ATOM   9569  C  CA  . LYS   C  1 349 ? 15.969  -74.780 -83.471  1.00 31.13  ? 650  LYS   C CA  1 
ATOM   9570  C  C   . LYS   C  1 349 ? 15.718  -73.337 -83.890  1.00 32.18  ? 650  LYS   C C   1 
ATOM   9571  O  O   . LYS   C  1 349 ? 16.210  -72.866 -84.916  1.00 32.18  ? 650  LYS   C O   1 
ATOM   9572  C  CB  . LYS   C  1 349 ? 16.644  -75.570 -84.590  1.00 39.93  ? 650  LYS   C CB  1 
ATOM   9573  C  CG  . LYS   C  1 349 ? 16.955  -77.000 -84.199  1.00 47.40  ? 650  LYS   C CG  1 
ATOM   9574  C  CD  . LYS   C  1 349 ? 17.691  -77.731 -85.313  1.00 56.00  ? 650  LYS   C CD  1 
ATOM   9575  C  CE  . LYS   C  1 349 ? 18.748  -78.674 -84.739  1.00 66.85  ? 650  LYS   C CE  1 
ATOM   9576  N  NZ  . LYS   C  1 349 ? 19.705  -79.169 -85.776  1.00 74.97  ? 650  LYS   C NZ  1 
ATOM   9577  N  N   . VAL   C  1 350 ? 14.927  -72.635 -83.089  1.00 24.12  ? 651  VAL   C N   1 
ATOM   9578  C  CA  . VAL   C  1 350 ? 14.696  -71.212 -83.243  1.00 23.65  ? 651  VAL   C CA  1 
ATOM   9579  C  C   . VAL   C  1 350 ? 15.464  -70.535 -82.118  1.00 31.10  ? 651  VAL   C C   1 
ATOM   9580  O  O   . VAL   C  1 350 ? 15.255  -70.854 -80.940  1.00 24.53  ? 651  VAL   C O   1 
ATOM   9581  C  CB  . VAL   C  1 350 ? 13.201  -70.876 -83.172  1.00 27.59  ? 651  VAL   C CB  1 
ATOM   9582  C  CG1 . VAL   C  1 350 ? 12.980  -69.366 -83.230  1.00 25.76  ? 651  VAL   C CG1 1 
ATOM   9583  C  CG2 . VAL   C  1 350 ? 12.422  -71.612 -84.244  1.00 22.14  ? 651  VAL   C CG2 1 
ATOM   9584  N  N   . THR   C  1 351 ? 16.363  -69.626 -82.479  1.00 25.30  ? 652  THR   C N   1 
ATOM   9585  C  CA  . THR   C  1 351 ? 17.173  -68.941 -81.490  1.00 23.42  ? 652  THR   C CA  1 
ATOM   9586  C  C   . THR   C  1 351 ? 16.315  -68.392 -80.363  1.00 28.91  ? 652  THR   C C   1 
ATOM   9587  O  O   . THR   C  1 351 ? 15.301  -67.730 -80.593  1.00 25.38  ? 652  THR   C O   1 
ATOM   9588  C  CB  . THR   C  1 351 ? 17.944  -67.793 -82.123  1.00 27.31  ? 652  THR   C CB  1 
ATOM   9589  O  OG1 . THR   C  1 351 ? 18.640  -68.256 -83.284  1.00 30.42  ? 652  THR   C OG1 1 
ATOM   9590  C  CG2 . THR   C  1 351 ? 18.939  -67.230 -81.107  1.00 20.30  ? 652  THR   C CG2 1 
ATOM   9591  N  N   . ILE   C  1 352 ? 16.744  -68.671 -79.136  1.00 23.64  ? 653  ILE   C N   1 
ATOM   9592  C  CA  . ILE   C  1 352 ? 16.133  -68.112 -77.944  1.00 24.72  ? 653  ILE   C CA  1 
ATOM   9593  C  C   . ILE   C  1 352 ? 17.194  -68.154 -76.860  1.00 26.60  ? 653  ILE   C C   1 
ATOM   9594  O  O   . ILE   C  1 352 ? 18.142  -68.938 -76.926  1.00 28.91  ? 653  ILE   C O   1 
ATOM   9595  C  CB  . ILE   C  1 352 ? 14.859  -68.885 -77.528  1.00 23.35  ? 653  ILE   C CB  1 
ATOM   9596  C  CG1 . ILE   C  1 352 ? 14.022  -68.057 -76.542  1.00 24.31  ? 653  ILE   C CG1 1 
ATOM   9597  C  CG2 . ILE   C  1 352 ? 15.236  -70.244 -76.940  1.00 23.12  ? 653  ILE   C CG2 1 
ATOM   9598  C  CD1 . ILE   C  1 352 ? 12.593  -68.546 -76.404  1.00 20.30  ? 653  ILE   C CD1 1 
ATOM   9599  N  N   . VAL   C  1 353 ? 17.054  -67.285 -75.868  1.00 21.07  ? 654  VAL   C N   1 
ATOM   9600  C  CA  . VAL   C  1 353 ? 18.004  -67.235 -74.771  1.00 23.88  ? 654  VAL   C CA  1 
ATOM   9601  C  C   . VAL   C  1 353 ? 17.218  -67.242 -73.464  1.00 20.96  ? 654  VAL   C C   1 
ATOM   9602  O  O   . VAL   C  1 353 ? 16.218  -66.526 -73.330  1.00 20.70  ? 654  VAL   C O   1 
ATOM   9603  C  CB  . VAL   C  1 353 ? 18.932  -66.007 -74.888  1.00 26.82  ? 654  VAL   C CB  1 
ATOM   9604  C  CG1 . VAL   C  1 353 ? 18.168  -64.685 -74.728  1.00 21.56  ? 654  VAL   C CG1 1 
ATOM   9605  C  CG2 . VAL   C  1 353 ? 20.113  -66.117 -73.924  1.00 28.53  ? 654  VAL   C CG2 1 
ATOM   9606  N  N   . ASP   C  1 354 ? 17.632  -68.089 -72.527  1.00 20.67  ? 655  ASP   C N   1 
ATOM   9607  C  CA  . ASP   C  1 354 ? 16.966  -68.075 -71.238  1.00 26.47  ? 655  ASP   C CA  1 
ATOM   9608  C  C   . ASP   C  1 354 ? 17.477  -66.900 -70.409  1.00 31.44  ? 655  ASP   C C   1 
ATOM   9609  O  O   . ASP   C  1 354 ? 18.554  -66.347 -70.657  1.00 24.36  ? 655  ASP   C O   1 
ATOM   9610  C  CB  . ASP   C  1 354 ? 17.172  -69.392 -70.492  1.00 25.28  ? 655  ASP   C CB  1 
ATOM   9611  C  CG  . ASP   C  1 354 ? 18.609  -69.609 -70.059  1.00 33.95  ? 655  ASP   C CG  1 
ATOM   9612  O  OD1 . ASP   C  1 354 ? 19.347  -70.320 -70.772  1.00 42.06  ? 655  ASP   C OD1 1 
ATOM   9613  O  OD2 . ASP   C  1 354 ? 19.008  -69.065 -69.013  1.00 36.56  ? 655  ASP   C OD2 1 
ATOM   9614  N  N   . HIS   C  1 355 ? 16.689  -66.518 -69.402  1.00 26.19  ? 656  HIS   C N   1 
ATOM   9615  C  CA  . HIS   C  1 355 ? 17.043  -65.326 -68.646  1.00 25.91  ? 656  HIS   C CA  1 
ATOM   9616  C  C   . HIS   C  1 355 ? 18.355  -65.499 -67.883  1.00 25.18  ? 656  HIS   C C   1 
ATOM   9617  O  O   . HIS   C  1 355 ? 19.062  -64.517 -67.648  1.00 29.59  ? 656  HIS   C O   1 
ATOM   9618  C  CB  . HIS   C  1 355 ? 15.896  -64.929 -67.710  1.00 23.56  ? 656  HIS   C CB  1 
ATOM   9619  C  CG  . HIS   C  1 355 ? 15.425  -66.025 -66.803  1.00 20.45  ? 656  HIS   C CG  1 
ATOM   9620  N  ND1 . HIS   C  1 355 ? 14.616  -67.057 -67.232  1.00 24.83  ? 656  HIS   C ND1 1 
ATOM   9621  C  CD2 . HIS   C  1 355 ? 15.594  -66.209 -65.468  1.00 22.11  ? 656  HIS   C CD2 1 
ATOM   9622  C  CE1 . HIS   C  1 355 ? 14.335  -67.848 -66.208  1.00 28.61  ? 656  HIS   C CE1 1 
ATOM   9623  N  NE2 . HIS   C  1 355 ? 14.921  -67.360 -65.127  1.00 23.50  ? 656  HIS   C NE2 1 
ATOM   9624  N  N   . HIS   C  1 356 ? 18.729  -66.723 -67.519  1.00 26.18  ? 657  HIS   C N   1 
ATOM   9625  C  CA  . HIS   C  1 356 ? 20.005  -66.880 -66.826  1.00 24.08  ? 657  HIS   C CA  1 
ATOM   9626  C  C   . HIS   C  1 356 ? 21.167  -66.619 -67.766  1.00 27.76  ? 657  HIS   C C   1 
ATOM   9627  O  O   . HIS   C  1 356 ? 22.077  -65.843 -67.448  1.00 27.96  ? 657  HIS   C O   1 
ATOM   9628  C  CB  . HIS   C  1 356 ? 20.099  -68.261 -66.206  1.00 26.36  ? 657  HIS   C CB  1 
ATOM   9629  C  CG  . HIS   C  1 356 ? 18.963  -68.561 -65.294  1.00 29.69  ? 657  HIS   C CG  1 
ATOM   9630  N  ND1 . HIS   C  1 356 ? 18.837  -67.977 -64.052  1.00 28.93  ? 657  HIS   C ND1 1 
ATOM   9631  C  CD2 . HIS   C  1 356 ? 17.877  -69.354 -65.454  1.00 27.47  ? 657  HIS   C CD2 1 
ATOM   9632  C  CE1 . HIS   C  1 356 ? 17.727  -68.408 -63.480  1.00 31.53  ? 657  HIS   C CE1 1 
ATOM   9633  N  NE2 . HIS   C  1 356 ? 17.125  -69.243 -64.312  1.00 33.37  ? 657  HIS   C NE2 1 
ATOM   9634  N  N   . SER   C  1 357 ? 21.139  -67.234 -68.947  1.00 29.58  ? 658  SER   C N   1 
ATOM   9635  C  CA  A SER   C  1 357 ? 22.185  -66.979 -69.925  0.56 24.71  ? 658  SER   C CA  1 
ATOM   9636  C  CA  B SER   C  1 357 ? 22.192  -66.977 -69.919  0.44 24.75  ? 658  SER   C CA  1 
ATOM   9637  C  C   . SER   C  1 357 ? 22.232  -65.507 -70.312  1.00 20.80  ? 658  SER   C C   1 
ATOM   9638  O  O   . SER   C  1 357 ? 23.312  -64.907 -70.381  1.00 25.28  ? 658  SER   C O   1 
ATOM   9639  C  CB  A SER   C  1 357 ? 21.968  -67.846 -71.165  0.56 22.89  ? 658  SER   C CB  1 
ATOM   9640  C  CB  B SER   C  1 357 ? 21.997  -67.863 -71.151  0.44 23.34  ? 658  SER   C CB  1 
ATOM   9641  O  OG  A SER   C  1 357 ? 23.000  -67.611 -72.097  0.56 25.77  ? 658  SER   C OG  1 
ATOM   9642  O  OG  B SER   C  1 357 ? 21.938  -69.224 -70.766  0.44 26.34  ? 658  SER   C OG  1 
ATOM   9643  N  N   . ALA   C  1 358 ? 21.066  -64.904 -70.567  1.00 21.22  ? 659  ALA   C N   1 
ATOM   9644  C  CA  . ALA   C  1 358 ? 21.053  -63.536 -71.067  1.00 21.52  ? 659  ALA   C CA  1 
ATOM   9645  C  C   . ALA   C  1 358 ? 21.625  -62.573 -70.046  1.00 28.20  ? 659  ALA   C C   1 
ATOM   9646  O  O   . ALA   C  1 358 ? 22.379  -61.659 -70.404  1.00 23.97  ? 659  ALA   C O   1 
ATOM   9647  C  CB  . ALA   C  1 358 ? 19.634  -63.124 -71.458  1.00 20.25  ? 659  ALA   C CB  1 
ATOM   9648  N  N   . THR   C  1 359 ? 21.281  -62.758 -68.767  1.00 28.08  ? 660  THR   C N   1 
ATOM   9649  C  CA  . THR   C  1 359 ? 21.766  -61.823 -67.755  1.00 19.81  ? 660  THR   C CA  1 
ATOM   9650  C  C   . THR   C  1 359 ? 23.241  -62.039 -67.467  1.00 20.35  ? 660  THR   C C   1 
ATOM   9651  O  O   . THR   C  1 359 ? 23.977  -61.074 -67.250  1.00 20.47  ? 660  THR   C O   1 
ATOM   9652  C  CB  . THR   C  1 359 ? 20.944  -61.944 -66.470  1.00 22.21  ? 660  THR   C CB  1 
ATOM   9653  O  OG1 . THR   C  1 359 ? 20.950  -63.301 -66.012  1.00 21.78  ? 660  THR   C OG1 1 
ATOM   9654  C  CG2 . THR   C  1 359 ? 19.504  -61.469 -66.689  1.00 19.42  ? 660  THR   C CG2 1 
ATOM   9655  N  N   . GLU   C  1 360 ? 23.693  -63.294 -67.442  1.00 20.90  ? 661  GLU   C N   1 
ATOM   9656  C  CA  . GLU   C  1 360 ? 25.121  -63.546 -67.309  1.00 28.03  ? 661  GLU   C CA  1 
ATOM   9657  C  C   . GLU   C  1 360 ? 25.888  -62.867 -68.435  1.00 31.37  ? 661  GLU   C C   1 
ATOM   9658  O  O   . GLU   C  1 360 ? 26.920  -62.229 -68.206  1.00 28.83  ? 661  GLU   C O   1 
ATOM   9659  C  CB  . GLU   C  1 360 ? 25.397  -65.052 -67.309  1.00 27.99  ? 661  GLU   C CB  1 
ATOM   9660  C  CG  . GLU   C  1 360 ? 26.880  -65.382 -67.165  1.00 39.11  ? 661  GLU   C CG  1 
ATOM   9661  C  CD  . GLU   C  1 360 ? 27.171  -66.875 -67.174  1.00 62.98  ? 661  GLU   C CD  1 
ATOM   9662  O  OE1 . GLU   C  1 360 ? 26.209  -67.673 -67.209  1.00 69.97  ? 661  GLU   C OE1 1 
ATOM   9663  O  OE2 . GLU   C  1 360 ? 28.366  -67.252 -67.145  1.00 69.55  ? 661  GLU   C OE2 1 
ATOM   9664  N  N   . SER   C  1 361 ? 25.387  -62.986 -69.664  1.00 26.37  ? 662  SER   C N   1 
ATOM   9665  C  CA  . SER   C  1 361 ? 26.058  -62.341 -70.782  1.00 24.11  ? 662  SER   C CA  1 
ATOM   9666  C  C   . SER   C  1 361 ? 26.058  -60.836 -70.615  1.00 28.54  ? 662  SER   C C   1 
ATOM   9667  O  O   . SER   C  1 361 ? 27.067  -60.175 -70.881  1.00 26.23  ? 662  SER   C O   1 
ATOM   9668  C  CB  . SER   C  1 361 ? 25.388  -62.742 -72.095  1.00 26.65  ? 662  SER   C CB  1 
ATOM   9669  O  OG  . SER   C  1 361 ? 25.713  -64.088 -72.390  1.00 32.54  ? 662  SER   C OG  1 
ATOM   9670  N  N   . PHE   C  1 362 ? 24.940  -60.272 -70.155  1.00 25.44  ? 663  PHE   C N   1 
ATOM   9671  C  CA  . PHE   C  1 362 ? 24.882  -58.823 -70.030  1.00 23.21  ? 663  PHE   C CA  1 
ATOM   9672  C  C   . PHE   C  1 362 ? 25.880  -58.313 -68.995  1.00 27.85  ? 663  PHE   C C   1 
ATOM   9673  O  O   . PHE   C  1 362 ? 26.478  -57.243 -69.176  1.00 29.00  ? 663  PHE   C O   1 
ATOM   9674  C  CB  . PHE   C  1 362 ? 23.467  -58.373 -69.679  1.00 25.96  ? 663  PHE   C CB  1 
ATOM   9675  C  CG  . PHE   C  1 362 ? 23.374  -56.910 -69.433  1.00 27.89  ? 663  PHE   C CG  1 
ATOM   9676  C  CD1 . PHE   C  1 362 ? 23.377  -56.025 -70.498  1.00 20.43  ? 663  PHE   C CD1 1 
ATOM   9677  C  CD2 . PHE   C  1 362 ? 23.330  -56.412 -68.133  1.00 21.04  ? 663  PHE   C CD2 1 
ATOM   9678  C  CE1 . PHE   C  1 362 ? 23.323  -54.677 -70.275  1.00 20.05  ? 663  PHE   C CE1 1 
ATOM   9679  C  CE2 . PHE   C  1 362 ? 23.268  -55.060 -67.906  1.00 27.19  ? 663  PHE   C CE2 1 
ATOM   9680  C  CZ  . PHE   C  1 362 ? 23.267  -54.187 -68.975  1.00 29.99  ? 663  PHE   C CZ  1 
ATOM   9681  N  N   . ILE   C  1 363 ? 26.078  -59.059 -67.904  1.00 24.90  ? 664  ILE   C N   1 
ATOM   9682  C  CA  . ILE   C  1 363 ? 27.103  -58.678 -66.933  1.00 29.73  ? 664  ILE   C CA  1 
ATOM   9683  C  C   . ILE   C  1 363 ? 28.477  -58.661 -67.594  1.00 23.99  ? 664  ILE   C C   1 
ATOM   9684  O  O   . ILE   C  1 363 ? 29.265  -57.726 -67.402  1.00 29.05  ? 664  ILE   C O   1 
ATOM   9685  C  CB  . ILE   C  1 363 ? 27.094  -59.622 -65.717  1.00 21.50  ? 664  ILE   C CB  1 
ATOM   9686  C  CG1 . ILE   C  1 363 ? 25.812  -59.438 -64.901  1.00 30.16  ? 664  ILE   C CG1 1 
ATOM   9687  C  CG2 . ILE   C  1 363 ? 28.339  -59.381 -64.860  1.00 25.73  ? 664  ILE   C CG2 1 
ATOM   9688  C  CD1 . ILE   C  1 363 ? 25.722  -58.098 -64.218  1.00 30.57  ? 664  ILE   C CD1 1 
ATOM   9689  N  N   . LYS   C  1 364 ? 28.791  -59.700 -68.373  1.00 25.17  ? 665  LYS   C N   1 
ATOM   9690  C  CA  . LYS   C  1 364 ? 30.071  -59.704 -69.075  1.00 31.86  ? 665  LYS   C CA  1 
ATOM   9691  C  C   . LYS   C  1 364 ? 30.155  -58.524 -70.033  1.00 29.69  ? 665  LYS   C C   1 
ATOM   9692  O  O   . LYS   C  1 364 ? 31.171  -57.821 -70.079  1.00 26.48  ? 665  LYS   C O   1 
ATOM   9693  C  CB  . LYS   C  1 364 ? 30.274  -61.031 -69.807  1.00 34.97  ? 665  LYS   C CB  1 
ATOM   9694  C  CG  . LYS   C  1 364 ? 30.429  -62.204 -68.856  1.00 38.50  ? 665  LYS   C CG  1 
ATOM   9695  C  CD  . LYS   C  1 364 ? 30.585  -63.532 -69.576  1.00 53.51  ? 665  LYS   C CD  1 
ATOM   9696  C  CE  . LYS   C  1 364 ? 31.076  -64.620 -68.618  1.00 64.62  ? 665  LYS   C CE  1 
ATOM   9697  N  NZ  . LYS   C  1 364 ? 31.165  -65.963 -69.261  1.00 69.40  ? 665  LYS   C NZ  1 
ATOM   9698  N  N   . HIS   C  1 365 ? 29.070  -58.264 -70.766  1.00 26.26  ? 666  HIS   C N   1 
ATOM   9699  C  CA  . HIS   C  1 365 ? 29.019  -57.090 -71.630  1.00 26.06  ? 666  HIS   C CA  1 
ATOM   9700  C  C   . HIS   C  1 365 ? 29.217  -55.815 -70.824  1.00 30.28  ? 666  HIS   C C   1 
ATOM   9701  O  O   . HIS   C  1 365 ? 30.017  -54.942 -71.189  1.00 21.29  ? 666  HIS   C O   1 
ATOM   9702  C  CB  . HIS   C  1 365 ? 27.684  -57.050 -72.357  1.00 23.45  ? 666  HIS   C CB  1 
ATOM   9703  C  CG  . HIS   C  1 365 ? 27.414  -55.754 -73.055  1.00 26.46  ? 666  HIS   C CG  1 
ATOM   9704  N  ND1 . HIS   C  1 365 ? 28.127  -55.338 -74.160  1.00 23.06  ? 666  HIS   C ND1 1 
ATOM   9705  C  CD2 . HIS   C  1 365 ? 26.495  -54.790 -72.816  1.00 23.77  ? 666  HIS   C CD2 1 
ATOM   9706  C  CE1 . HIS   C  1 365 ? 27.660  -54.173 -74.566  1.00 24.65  ? 666  HIS   C CE1 1 
ATOM   9707  N  NE2 . HIS   C  1 365 ? 26.681  -53.810 -73.758  1.00 24.31  ? 666  HIS   C NE2 1 
ATOM   9708  N  N   . MET   C  1 366 ? 28.492  -55.689 -69.715  1.00 25.31  ? 667  MET   C N   1 
ATOM   9709  C  CA  . MET   C  1 366 ? 28.586  -54.467 -68.929  1.00 24.64  ? 667  MET   C CA  1 
ATOM   9710  C  C   . MET   C  1 366 ? 30.017  -54.236 -68.464  1.00 27.18  ? 667  MET   C C   1 
ATOM   9711  O  O   . MET   C  1 366 ? 30.565  -53.136 -68.623  1.00 26.48  ? 667  MET   C O   1 
ATOM   9712  C  CB  . MET   C  1 366 ? 27.627  -54.544 -67.750  1.00 25.93  ? 667  MET   C CB  1 
ATOM   9713  C  CG  . MET   C  1 366 ? 27.360  -53.218 -67.092  1.00 31.47  ? 667  MET   C CG  1 
ATOM   9714  S  SD  . MET   C  1 366 ? 26.392  -53.593 -65.629  1.00 33.73  ? 667  MET   C SD  1 
ATOM   9715  C  CE  . MET   C  1 366 ? 26.716  -52.146 -64.607  1.00 35.85  ? 667  MET   C CE  1 
ATOM   9716  N  N   . GLU   C  1 367 ? 30.664  -55.287 -67.949  1.00 26.68  ? 668  GLU   C N   1 
ATOM   9717  C  CA  . GLU   C  1 367 ? 32.042  -55.136 -67.491  1.00 35.04  ? 668  GLU   C CA  1 
ATOM   9718  C  C   . GLU   C  1 367 ? 32.969  -54.789 -68.647  1.00 32.87  ? 668  GLU   C C   1 
ATOM   9719  O  O   . GLU   C  1 367 ? 33.861  -53.947 -68.509  1.00 29.20  ? 668  GLU   C O   1 
ATOM   9720  C  CB  . GLU   C  1 367 ? 32.510  -56.410 -66.790  1.00 36.06  ? 668  GLU   C CB  1 
ATOM   9721  C  CG  . GLU   C  1 367 ? 31.730  -56.719 -65.525  1.00 38.30  ? 668  GLU   C CG  1 
ATOM   9722  C  CD  . GLU   C  1 367 ? 32.211  -57.981 -64.821  1.00 48.63  ? 668  GLU   C CD  1 
ATOM   9723  O  OE1 . GLU   C  1 367 ? 32.814  -58.854 -65.486  1.00 49.56  ? 668  GLU   C OE1 1 
ATOM   9724  O  OE2 . GLU   C  1 367 ? 31.984  -58.093 -63.597  1.00 48.97  ? 668  GLU   C OE2 1 
ATOM   9725  N  N   . ASN   C  1 368 ? 32.775  -55.429 -69.797  1.00 29.71  ? 669  ASN   C N   1 
ATOM   9726  C  CA  . ASN   C  1 368 ? 33.600  -55.100 -70.953  1.00 31.02  ? 669  ASN   C CA  1 
ATOM   9727  C  C   . ASN   C  1 368 ? 33.406  -53.645 -71.362  1.00 29.20  ? 669  ASN   C C   1 
ATOM   9728  O  O   . ASN   C  1 368 ? 34.380  -52.940 -71.666  1.00 28.76  ? 669  ASN   C O   1 
ATOM   9729  C  CB  . ASN   C  1 368 ? 33.266  -56.036 -72.109  1.00 32.75  ? 669  ASN   C CB  1 
ATOM   9730  C  CG  . ASN   C  1 368 ? 34.063  -55.725 -73.331  1.00 36.21  ? 669  ASN   C CG  1 
ATOM   9731  O  OD1 . ASN   C  1 368 ? 35.290  -55.738 -73.294  1.00 35.30  ? 669  ASN   C OD1 1 
ATOM   9732  N  ND2 . ASN   C  1 368 ? 33.378  -55.430 -74.425  1.00 35.39  ? 669  ASN   C ND2 1 
ATOM   9733  N  N   . GLU   C  1 369 ? 32.153  -53.178 -71.343  1.00 26.83  ? 670  GLU   C N   1 
ATOM   9734  C  CA  . GLU   C  1 369 ? 31.844  -51.789 -71.679  1.00 27.05  ? 670  GLU   C CA  1 
ATOM   9735  C  C   . GLU   C  1 369 ? 32.488  -50.808 -70.707  1.00 29.09  ? 670  GLU   C C   1 
ATOM   9736  O  O   . GLU   C  1 369 ? 33.026  -49.778 -71.124  1.00 27.91  ? 670  GLU   C O   1 
ATOM   9737  C  CB  . GLU   C  1 369 ? 30.330  -51.590 -71.707  1.00 22.73  ? 670  GLU   C CB  1 
ATOM   9738  C  CG  . GLU   C  1 369 ? 29.666  -52.275 -72.877  1.00 23.73  ? 670  GLU   C CG  1 
ATOM   9739  C  CD  . GLU   C  1 369 ? 29.888  -51.522 -74.163  1.00 26.66  ? 670  GLU   C CD  1 
ATOM   9740  O  OE1 . GLU   C  1 369 ? 28.950  -50.829 -74.626  1.00 25.76  ? 670  GLU   C OE1 1 
ATOM   9741  O  OE2 . GLU   C  1 369 ? 31.008  -51.600 -74.690  1.00 30.30  ? 670  GLU   C OE2 1 
ATOM   9742  N  N   . TYR   C  1 370 ? 32.419  -51.084 -69.403  1.00 27.91  ? 671  TYR   C N   1 
ATOM   9743  C  CA  . TYR   C  1 370 ? 33.131  -50.225 -68.467  1.00 27.93  ? 671  TYR   C CA  1 
ATOM   9744  C  C   . TYR   C  1 370 ? 34.615  -50.164 -68.804  1.00 28.92  ? 671  TYR   C C   1 
ATOM   9745  O  O   . TYR   C  1 370 ? 35.217  -49.084 -68.794  1.00 32.64  ? 671  TYR   C O   1 
ATOM   9746  C  CB  . TYR   C  1 370 ? 32.912  -50.702 -67.030  1.00 32.59  ? 671  TYR   C CB  1 
ATOM   9747  C  CG  . TYR   C  1 370 ? 31.667  -50.109 -66.419  1.00 29.37  ? 671  TYR   C CG  1 
ATOM   9748  C  CD1 . TYR   C  1 370 ? 30.419  -50.643 -66.694  1.00 27.98  ? 671  TYR   C CD1 1 
ATOM   9749  C  CD2 . TYR   C  1 370 ? 31.738  -48.998 -65.593  1.00 28.65  ? 671  TYR   C CD2 1 
ATOM   9750  C  CE1 . TYR   C  1 370 ? 29.277  -50.094 -66.166  1.00 27.96  ? 671  TYR   C CE1 1 
ATOM   9751  C  CE2 . TYR   C  1 370 ? 30.595  -48.445 -65.045  1.00 31.35  ? 671  TYR   C CE2 1 
ATOM   9752  C  CZ  . TYR   C  1 370 ? 29.374  -48.999 -65.326  1.00 34.56  ? 671  TYR   C CZ  1 
ATOM   9753  O  OH  . TYR   C  1 370 ? 28.235  -48.462 -64.788  1.00 36.48  ? 671  TYR   C OH  1 
ATOM   9754  N  N   . ARG   C  1 371 ? 35.211  -51.306 -69.147  1.00 34.70  ? 672  ARG   C N   1 
ATOM   9755  C  CA  . ARG   C  1 371 ? 36.645  -51.343 -69.415  1.00 37.54  ? 672  ARG   C CA  1 
ATOM   9756  C  C   . ARG   C  1 371 ? 37.004  -50.583 -70.689  1.00 40.13  ? 672  ARG   C C   1 
ATOM   9757  O  O   . ARG   C  1 371 ? 37.962  -49.804 -70.706  1.00 48.79  ? 672  ARG   C O   1 
ATOM   9758  C  CB  . ARG   C  1 371 ? 37.129  -52.793 -69.500  1.00 48.34  ? 672  ARG   C CB  1 
ATOM   9759  C  CG  . ARG   C  1 371 ? 37.789  -53.309 -68.210  1.00 65.19  ? 672  ARG   C CG  1 
ATOM   9760  C  CD  . ARG   C  1 371 ? 36.984  -54.428 -67.546  1.00 75.55  ? 672  ARG   C CD  1 
ATOM   9761  N  NE  . ARG   C  1 371 ? 37.182  -54.477 -66.095  1.00 79.84  ? 672  ARG   C NE  1 
ATOM   9762  C  CZ  . ARG   C  1 371 ? 36.589  -55.351 -65.281  1.00 77.72  ? 672  ARG   C CZ  1 
ATOM   9763  N  NH1 . ARG   C  1 371 ? 35.758  -56.261 -65.772  1.00 80.25  ? 672  ARG   C NH1 1 
ATOM   9764  N  NH2 . ARG   C  1 371 ? 36.826  -55.319 -63.974  1.00 69.96  ? 672  ARG   C NH2 1 
ATOM   9765  N  N   . CYS   C  1 372 ? 36.262  -50.790 -71.770  1.00 34.77  ? 673  CYS   C N   1 
ATOM   9766  C  CA  A CYS   C  1 372 ? 36.641  -50.202 -73.051  0.66 39.89  ? 673  CYS   C CA  1 
ATOM   9767  C  CA  B CYS   C  1 372 ? 36.651  -50.197 -73.041  0.34 39.41  ? 673  CYS   C CA  1 
ATOM   9768  C  C   . CYS   C  1 372 ? 35.981  -48.856 -73.316  1.00 38.72  ? 673  CYS   C C   1 
ATOM   9769  O  O   . CYS   C  1 372 ? 36.542  -48.042 -74.057  1.00 45.16  ? 673  CYS   C O   1 
ATOM   9770  C  CB  A CYS   C  1 372 ? 36.325  -51.167 -74.211  0.66 39.40  ? 673  CYS   C CB  1 
ATOM   9771  C  CB  B CYS   C  1 372 ? 36.352  -51.182 -74.173  0.34 39.92  ? 673  CYS   C CB  1 
ATOM   9772  S  SG  A CYS   C  1 372 ? 34.584  -51.316 -74.742  0.66 35.46  ? 673  CYS   C SG  1 
ATOM   9773  S  SG  B CYS   C  1 372 ? 36.921  -52.863 -73.786  0.34 47.27  ? 673  CYS   C SG  1 
ATOM   9774  N  N   . ARG   C  1 373 ? 34.820  -48.594 -72.721  1.00 31.86  ? 674  ARG   C N   1 
ATOM   9775  C  CA  . ARG   C  1 373 ? 34.066  -47.381 -72.989  1.00 23.70  ? 674  ARG   C CA  1 
ATOM   9776  C  C   . ARG   C  1 373 ? 33.936  -46.451 -71.788  1.00 32.14  ? 674  ARG   C C   1 
ATOM   9777  O  O   . ARG   C  1 373 ? 33.569  -45.285 -71.970  1.00 31.48  ? 674  ARG   C O   1 
ATOM   9778  C  CB  . ARG   C  1 373 ? 32.656  -47.745 -73.485  1.00 23.62  ? 674  ARG   C CB  1 
ATOM   9779  C  CG  . ARG   C  1 373 ? 31.996  -46.740 -74.407  1.00 27.16  ? 674  ARG   C CG  1 
ATOM   9780  C  CD  . ARG   C  1 373 ? 30.532  -47.122 -74.626  1.00 26.39  ? 674  ARG   C CD  1 
ATOM   9781  N  NE  . ARG   C  1 373 ? 29.877  -46.202 -75.544  1.00 30.42  ? 674  ARG   C NE  1 
ATOM   9782  C  CZ  . ARG   C  1 373 ? 28.564  -46.128 -75.734  1.00 28.32  ? 674  ARG   C CZ  1 
ATOM   9783  N  NH1 . ARG   C  1 373 ? 27.739  -46.914 -75.060  1.00 24.94  ? 674  ARG   C NH1 1 
ATOM   9784  N  NH2 . ARG   C  1 373 ? 28.077  -45.262 -76.606  1.00 28.28  ? 674  ARG   C NH2 1 
ATOM   9785  N  N   . GLY   C  1 374 ? 34.216  -46.917 -70.578  1.00 25.52  ? 675  GLY   C N   1 
ATOM   9786  C  CA  . GLY   C  1 374 ? 34.026  -46.083 -69.407  1.00 29.78  ? 675  GLY   C CA  1 
ATOM   9787  C  C   . GLY   C  1 374 ? 32.652  -46.174 -68.787  1.00 35.47  ? 675  GLY   C C   1 
ATOM   9788  O  O   . GLY   C  1 374 ? 32.337  -45.384 -67.888  1.00 27.41  ? 675  GLY   C O   1 
ATOM   9789  N  N   . GLY   C  1 375 ? 31.825  -47.104 -69.232  1.00 31.18  ? 676  GLY   C N   1 
ATOM   9790  C  CA  . GLY   C  1 375 ? 30.524  -47.268 -68.624  1.00 28.28  ? 676  GLY   C CA  1 
ATOM   9791  C  C   . GLY   C  1 375 ? 29.573  -47.977 -69.558  1.00 31.89  ? 676  GLY   C C   1 
ATOM   9792  O  O   . GLY   C  1 375 ? 29.899  -48.311 -70.698  1.00 33.24  ? 676  GLY   C O   1 
ATOM   9793  N  N   . CYS   C  1 376 ? 28.393  -48.206 -69.036  1.00 30.90  ? 677  CYS   C N   1 
ATOM   9794  C  CA  . CYS   C  1 376 ? 27.348  -48.899 -69.758  1.00 29.43  ? 677  CYS   C CA  1 
ATOM   9795  C  C   . CYS   C  1 376 ? 26.030  -48.495 -69.124  1.00 28.51  ? 677  CYS   C C   1 
ATOM   9796  O  O   . CYS   C  1 376 ? 25.681  -48.998 -68.056  1.00 30.55  ? 677  CYS   C O   1 
ATOM   9797  C  CB  . CYS   C  1 376 ? 27.549  -50.407 -69.694  1.00 26.96  ? 677  CYS   C CB  1 
ATOM   9798  S  SG  . CYS   C  1 376 ? 26.227  -51.324 -70.493  1.00 30.06  ? 677  CYS   C SG  1 
ATOM   9799  N  N   . PRO   C  1 377 ? 25.304  -47.560 -69.711  1.00 22.48  ? 678  PRO   C N   1 
ATOM   9800  C  CA  . PRO   C  1 377 ? 24.027  -47.161 -69.119  1.00 20.78  ? 678  PRO   C CA  1 
ATOM   9801  C  C   . PRO   C  1 377 ? 23.089  -48.361 -69.074  1.00 26.25  ? 678  PRO   C C   1 
ATOM   9802  O  O   . PRO   C  1 377 ? 22.945  -49.096 -70.052  1.00 22.05  ? 678  PRO   C O   1 
ATOM   9803  C  CB  . PRO   C  1 377 ? 23.526  -46.069 -70.069  1.00 24.86  ? 678  PRO   C CB  1 
ATOM   9804  C  CG  . PRO   C  1 377 ? 24.197  -46.404 -71.406  1.00 30.43  ? 678  PRO   C CG  1 
ATOM   9805  C  CD  . PRO   C  1 377 ? 25.563  -46.899 -71.001  1.00 27.19  ? 678  PRO   C CD  1 
ATOM   9806  N  N   . ALA   C  1 378 ? 22.465  -48.575 -67.925  1.00 23.64  ? 679  ALA   C N   1 
ATOM   9807  C  CA  . ALA   C  1 378 ? 21.648  -49.769 -67.758  1.00 24.02  ? 679  ALA   C CA  1 
ATOM   9808  C  C   . ALA   C  1 378 ? 20.496  -49.437 -66.838  1.00 23.21  ? 679  ALA   C C   1 
ATOM   9809  O  O   . ALA   C  1 378 ? 20.675  -48.778 -65.809  1.00 21.99  ? 679  ALA   C O   1 
ATOM   9810  C  CB  . ALA   C  1 378 ? 22.453  -50.937 -67.188  1.00 29.24  ? 679  ALA   C CB  1 
ATOM   9811  N  N   . ASP   C  1 379 ? 19.318  -49.879 -67.235  1.00 22.66  ? 680  ASP   C N   1 
ATOM   9812  C  CA  . ASP   C  1 379 ? 18.088  -49.607 -66.504  1.00 24.84  ? 680  ASP   C CA  1 
ATOM   9813  C  C   . ASP   C  1 379 ? 17.739  -50.877 -65.744  1.00 23.99  ? 680  ASP   C C   1 
ATOM   9814  O  O   . ASP   C  1 379 ? 17.149  -51.805 -66.304  1.00 22.97  ? 680  ASP   C O   1 
ATOM   9815  C  CB  . ASP   C  1 379 ? 16.980  -49.192 -67.467  1.00 23.75  ? 680  ASP   C CB  1 
ATOM   9816  C  CG  . ASP   C  1 379 ? 15.696  -48.813 -66.756  1.00 26.50  ? 680  ASP   C CG  1 
ATOM   9817  O  OD1 . ASP   C  1 379 ? 14.896  -48.081 -67.367  1.00 22.21  ? 680  ASP   C OD1 1 
ATOM   9818  O  OD2 . ASP   C  1 379 ? 15.501  -49.217 -65.584  1.00 27.36  ? 680  ASP   C OD2 1 
ATOM   9819  N  N   . TRP   C  1 380 ? 18.105  -50.904 -64.453  1.00 19.25  ? 681  TRP   C N   1 
ATOM   9820  C  CA  . TRP   C  1 380 ? 17.946  -52.103 -63.640  1.00 18.78  ? 681  TRP   C CA  1 
ATOM   9821  C  C   . TRP   C  1 380 ? 16.510  -52.590 -63.666  1.00 18.65  ? 681  TRP   C C   1 
ATOM   9822  O  O   . TRP   C  1 380 ? 16.255  -53.792 -63.729  1.00 19.71  ? 681  TRP   C O   1 
ATOM   9823  C  CB  . TRP   C  1 380 ? 18.385  -51.778 -62.206  1.00 19.98  ? 681  TRP   C CB  1 
ATOM   9824  C  CG  . TRP   C  1 380 ? 18.534  -52.935 -61.261  1.00 19.53  ? 681  TRP   C CG  1 
ATOM   9825  C  CD1 . TRP   C  1 380 ? 19.709  -53.522 -60.868  1.00 20.88  ? 681  TRP   C CD1 1 
ATOM   9826  C  CD2 . TRP   C  1 380 ? 17.494  -53.602 -60.537  1.00 19.66  ? 681  TRP   C CD2 1 
ATOM   9827  N  NE1 . TRP   C  1 380 ? 19.465  -54.510 -59.944  1.00 21.11  ? 681  TRP   C NE1 1 
ATOM   9828  C  CE2 . TRP   C  1 380 ? 18.113  -54.585 -59.724  1.00 24.78  ? 681  TRP   C CE2 1 
ATOM   9829  C  CE3 . TRP   C  1 380 ? 16.101  -53.473 -60.495  1.00 21.91  ? 681  TRP   C CE3 1 
ATOM   9830  C  CZ2 . TRP   C  1 380 ? 17.383  -55.436 -58.887  1.00 21.18  ? 681  TRP   C CZ2 1 
ATOM   9831  C  CZ3 . TRP   C  1 380 ? 15.376  -54.322 -59.646  1.00 19.89  ? 681  TRP   C CZ3 1 
ATOM   9832  C  CH2 . TRP   C  1 380 ? 16.021  -55.292 -58.866  1.00 20.23  ? 681  TRP   C CH2 1 
ATOM   9833  N  N   . VAL   C  1 381 ? 15.559  -51.657 -63.606  1.00 19.09  ? 682  VAL   C N   1 
ATOM   9834  C  CA  . VAL   C  1 381 ? 14.142  -51.993 -63.619  1.00 18.66  ? 682  VAL   C CA  1 
ATOM   9835  C  C   . VAL   C  1 381 ? 13.761  -52.810 -64.851  1.00 23.33  ? 682  VAL   C C   1 
ATOM   9836  O  O   . VAL   C  1 381 ? 12.875  -53.678 -64.785  1.00 22.00  ? 682  VAL   C O   1 
ATOM   9837  C  CB  . VAL   C  1 381 ? 13.326  -50.686 -63.518  1.00 19.52  ? 682  VAL   C CB  1 
ATOM   9838  C  CG1 . VAL   C  1 381 ? 11.856  -50.963 -63.722  1.00 18.87  ? 682  VAL   C CG1 1 
ATOM   9839  C  CG2 . VAL   C  1 381 ? 13.556  -49.989 -62.143  1.00 22.83  ? 682  VAL   C CG2 1 
ATOM   9840  N  N   . TRP   C  1 382 ? 14.413  -52.565 -65.986  1.00 23.21  ? 683  TRP   C N   1 
ATOM   9841  C  CA  . TRP   C  1 382 ? 14.137  -53.358 -67.177  1.00 23.06  ? 683  TRP   C CA  1 
ATOM   9842  C  C   . TRP   C  1 382 ? 15.095  -54.522 -67.345  1.00 22.27  ? 683  TRP   C C   1 
ATOM   9843  O  O   . TRP   C  1 382 ? 14.693  -55.566 -67.861  1.00 24.62  ? 683  TRP   C O   1 
ATOM   9844  C  CB  . TRP   C  1 382 ? 14.177  -52.481 -68.441  1.00 18.44  ? 683  TRP   C CB  1 
ATOM   9845  C  CG  . TRP   C  1 382 ? 12.882  -51.780 -68.690  1.00 22.09  ? 683  TRP   C CG  1 
ATOM   9846  C  CD1 . TRP   C  1 382 ? 12.256  -50.885 -67.867  1.00 23.93  ? 683  TRP   C CD1 1 
ATOM   9847  C  CD2 . TRP   C  1 382 ? 12.051  -51.916 -69.844  1.00 20.12  ? 683  TRP   C CD2 1 
ATOM   9848  N  NE1 . TRP   C  1 382 ? 11.077  -50.455 -68.443  1.00 23.33  ? 683  TRP   C NE1 1 
ATOM   9849  C  CE2 . TRP   C  1 382 ? 10.937  -51.073 -69.661  1.00 32.21  ? 683  TRP   C CE2 1 
ATOM   9850  C  CE3 . TRP   C  1 382 ? 12.147  -52.664 -71.024  1.00 23.44  ? 683  TRP   C CE3 1 
ATOM   9851  C  CZ2 . TRP   C  1 382 ? 9.927   -50.966 -70.610  1.00 29.68  ? 683  TRP   C CZ2 1 
ATOM   9852  C  CZ3 . TRP   C  1 382 ? 11.150  -52.551 -71.957  1.00 27.79  ? 683  TRP   C CZ3 1 
ATOM   9853  C  CH2 . TRP   C  1 382 ? 10.052  -51.715 -71.746  1.00 22.48  ? 683  TRP   C CH2 1 
ATOM   9854  N  N   . ILE   C  1 383 ? 16.353  -54.369 -66.931  1.00 24.40  ? 684  ILE   C N   1 
ATOM   9855  C  CA  . ILE   C  1 383 ? 17.332  -55.427 -67.161  1.00 18.75  ? 684  ILE   C CA  1 
ATOM   9856  C  C   . ILE   C  1 383 ? 16.989  -56.672 -66.350  1.00 20.46  ? 684  ILE   C C   1 
ATOM   9857  O  O   . ILE   C  1 383 ? 17.167  -57.799 -66.826  1.00 22.53  ? 684  ILE   C O   1 
ATOM   9858  C  CB  . ILE   C  1 383 ? 18.748  -54.912 -66.846  1.00 23.27  ? 684  ILE   C CB  1 
ATOM   9859  C  CG1 . ILE   C  1 383 ? 19.150  -53.831 -67.852  1.00 23.41  ? 684  ILE   C CG1 1 
ATOM   9860  C  CG2 . ILE   C  1 383 ? 19.744  -56.057 -66.850  1.00 19.85  ? 684  ILE   C CG2 1 
ATOM   9861  C  CD1 . ILE   C  1 383 ? 19.081  -54.293 -69.304  1.00 26.91  ? 684  ILE   C CD1 1 
ATOM   9862  N  N   . VAL   C  1 384 ? 16.517  -56.500 -65.112  1.00 19.20  ? 685  VAL   C N   1 
ATOM   9863  C  CA  . VAL   C  1 384 ? 16.239  -57.674 -64.271  1.00 20.49  ? 685  VAL   C CA  1 
ATOM   9864  C  C   . VAL   C  1 384 ? 15.020  -58.410 -64.817  1.00 20.14  ? 685  VAL   C C   1 
ATOM   9865  O  O   . VAL   C  1 384 ? 13.973  -57.782 -65.065  1.00 21.76  ? 685  VAL   C O   1 
ATOM   9866  C  CB  . VAL   C  1 384 ? 16.028  -57.261 -62.804  1.00 19.15  ? 685  VAL   C CB  1 
ATOM   9867  C  CG1 . VAL   C  1 384 ? 15.665  -58.477 -61.948  1.00 19.57  ? 685  VAL   C CG1 1 
ATOM   9868  C  CG2 . VAL   C  1 384 ? 17.299  -56.625 -62.246  1.00 19.40  ? 685  VAL   C CG2 1 
ATOM   9869  N  N   . PRO   C  1 385 ? 15.107  -59.723 -65.023  1.00 22.37  ? 686  PRO   C N   1 
ATOM   9870  C  CA  . PRO   C  1 385 ? 14.003  -60.446 -65.658  1.00 26.85  ? 686  PRO   C CA  1 
ATOM   9871  C  C   . PRO   C  1 385 ? 12.769  -60.448 -64.788  1.00 27.10  ? 686  PRO   C C   1 
ATOM   9872  O  O   . PRO   C  1 385 ? 12.854  -60.362 -63.547  1.00 25.89  ? 686  PRO   C O   1 
ATOM   9873  C  CB  . PRO   C  1 385 ? 14.567  -61.865 -65.831  1.00 25.44  ? 686  PRO   C CB  1 
ATOM   9874  C  CG  . PRO   C  1 385 ? 16.029  -61.662 -65.901  1.00 32.07  ? 686  PRO   C CG  1 
ATOM   9875  C  CD  . PRO   C  1 385 ? 16.326  -60.541 -64.939  1.00 24.86  ? 686  PRO   C CD  1 
ATOM   9876  N  N   . PRO   C  1 386 ? 11.583  -60.585 -65.390  1.00 27.54  ? 687  PRO   C N   1 
ATOM   9877  C  CA  . PRO   C  1 386 ? 10.334  -60.519 -64.622  1.00 24.14  ? 687  PRO   C CA  1 
ATOM   9878  C  C   . PRO   C  1 386 ? 10.043  -61.757 -63.786  1.00 25.68  ? 687  PRO   C C   1 
ATOM   9879  O  O   . PRO   C  1 386 ? 8.963   -61.844 -63.189  1.00 28.23  ? 687  PRO   C O   1 
ATOM   9880  C  CB  . PRO   C  1 386 ? 9.284   -60.341 -65.725  1.00 25.91  ? 687  PRO   C CB  1 
ATOM   9881  C  CG  . PRO   C  1 386 ? 9.866   -61.138 -66.870  1.00 19.16  ? 687  PRO   C CG  1 
ATOM   9882  C  CD  . PRO   C  1 386 ? 11.338  -60.810 -66.828  1.00 21.44  ? 687  PRO   C CD  1 
ATOM   9883  N  N   . MET   C  1 387 ? 10.935  -62.741 -63.751  1.00 24.32  ? 688  MET   C N   1 
ATOM   9884  C  CA  . MET   C  1 387 ? 10.813  -63.846 -62.809  1.00 28.34  ? 688  MET   C CA  1 
ATOM   9885  C  C   . MET   C  1 387 ? 12.200  -64.151 -62.283  1.00 32.09  ? 688  MET   C C   1 
ATOM   9886  O  O   . MET   C  1 387 ? 13.204  -63.828 -62.928  1.00 27.97  ? 688  MET   C O   1 
ATOM   9887  C  CB  . MET   C  1 387 ? 10.221  -65.118 -63.442  1.00 26.93  ? 688  MET   C CB  1 
ATOM   9888  C  CG  . MET   C  1 387 ? 11.172  -65.833 -64.396  1.00 22.03  ? 688  MET   C CG  1 
ATOM   9889  S  SD  . MET   C  1 387 ? 10.456  -67.325 -65.119  1.00 37.70  ? 688  MET   C SD  1 
ATOM   9890  C  CE  . MET   C  1 387 ? 10.549  -68.462 -63.749  1.00 38.21  ? 688  MET   C CE  1 
ATOM   9891  N  N   . SER   C  1 388 ? 12.243  -64.770 -61.103  1.00 24.42  ? 689  SER   C N   1 
ATOM   9892  C  CA  . SER   C  1 388 ? 13.491  -65.277 -60.534  1.00 29.26  ? 689  SER   C CA  1 
ATOM   9893  C  C   . SER   C  1 388 ? 14.570  -64.203 -60.475  1.00 26.70  ? 689  SER   C C   1 
ATOM   9894  O  O   . SER   C  1 388 ? 15.751  -64.472 -60.703  1.00 25.92  ? 689  SER   C O   1 
ATOM   9895  C  CB  . SER   C  1 388 ? 13.979  -66.475 -61.335  1.00 27.71  ? 689  SER   C CB  1 
ATOM   9896  O  OG  . SER   C  1 388 ? 12.975  -67.470 -61.336  1.00 35.53  ? 689  SER   C OG  1 
ATOM   9897  N  N   . GLY   C  1 389 ? 14.156  -62.977 -60.158  1.00 28.29  ? 690  GLY   C N   1 
ATOM   9898  C  CA  . GLY   C  1 389 ? 15.050  -61.837 -60.301  1.00 23.87  ? 690  GLY   C CA  1 
ATOM   9899  C  C   . GLY   C  1 389 ? 16.391  -62.034 -59.626  1.00 32.00  ? 690  GLY   C C   1 
ATOM   9900  O  O   . GLY   C  1 389 ? 17.441  -61.886 -60.256  1.00 29.60  ? 690  GLY   C O   1 
ATOM   9901  N  N   . SER   C  1 390 ? 16.379  -62.392 -58.336  1.00 21.70  ? 691  SER   C N   1 
ATOM   9902  C  CA  . SER   C  1 390 ? 17.628  -62.370 -57.602  1.00 22.07  ? 691  SER   C CA  1 
ATOM   9903  C  C   . SER   C  1 390 ? 18.480  -63.605 -57.823  1.00 22.47  ? 691  SER   C C   1 
ATOM   9904  O  O   . SER   C  1 390 ? 19.630  -63.624 -57.381  1.00 28.26  ? 691  SER   C O   1 
ATOM   9905  C  CB  . SER   C  1 390 ? 17.388  -62.194 -56.098  1.00 26.53  ? 691  SER   C CB  1 
ATOM   9906  O  OG  . SER   C  1 390 ? 16.912  -63.393 -55.543  1.00 26.81  ? 691  SER   C OG  1 
ATOM   9907  N  N   . ILE   C  1 391 ? 17.981  -64.643 -58.489  1.00 27.28  ? 692  ILE   C N   1 
ATOM   9908  C  CA  . ILE   C  1 391 ? 18.909  -65.694 -58.862  1.00 25.70  ? 692  ILE   C CA  1 
ATOM   9909  C  C   . ILE   C  1 391 ? 19.595  -65.373 -60.181  1.00 23.94  ? 692  ILE   C C   1 
ATOM   9910  O  O   . ILE   C  1 391 ? 20.444  -66.151 -60.633  1.00 26.96  ? 692  ILE   C O   1 
ATOM   9911  C  CB  . ILE   C  1 391 ? 18.218  -67.069 -58.832  1.00 31.30  ? 692  ILE   C CB  1 
ATOM   9912  C  CG1 . ILE   C  1 391 ? 17.181  -67.195 -59.925  1.00 38.85  ? 692  ILE   C CG1 1 
ATOM   9913  C  CG2 . ILE   C  1 391 ? 17.613  -67.326 -57.403  1.00 25.82  ? 692  ILE   C CG2 1 
ATOM   9914  C  CD1 . ILE   C  1 391 ? 16.728  -68.617 -60.117  1.00 43.22  ? 692  ILE   C CD1 1 
ATOM   9915  N  N   . THR   C  1 392 ? 19.296  -64.204 -60.788  1.00 25.23  ? 693  THR   C N   1 
ATOM   9916  C  CA  . THR   C  1 392 ? 20.097  -63.765 -61.926  1.00 30.12  ? 693  THR   C CA  1 
ATOM   9917  C  C   . THR   C  1 392 ? 21.133  -62.767 -61.446  1.00 28.79  ? 693  THR   C C   1 
ATOM   9918  O  O   . THR   C  1 392 ? 20.896  -62.036 -60.480  1.00 30.25  ? 693  THR   C O   1 
ATOM   9919  C  CB  . THR   C  1 392 ? 19.253  -63.107 -63.029  1.00 25.88  ? 693  THR   C CB  1 
ATOM   9920  O  OG1 . THR   C  1 392 ? 18.726  -61.854 -62.558  1.00 26.96  ? 693  THR   C OG1 1 
ATOM   9921  C  CG2 . THR   C  1 392 ? 18.117  -64.005 -63.463  1.00 26.68  ? 693  THR   C CG2 1 
ATOM   9922  N  N   . PRO   C  1 393 ? 22.296  -62.711 -62.088  1.00 28.37  ? 694  PRO   C N   1 
ATOM   9923  C  CA  . PRO   C  1 393 ? 23.361  -61.846 -61.557  1.00 22.66  ? 694  PRO   C CA  1 
ATOM   9924  C  C   . PRO   C  1 393 ? 23.044  -60.363 -61.666  1.00 25.74  ? 694  PRO   C C   1 
ATOM   9925  O  O   . PRO   C  1 393 ? 23.505  -59.587 -60.819  1.00 25.37  ? 694  PRO   C O   1 
ATOM   9926  C  CB  . PRO   C  1 393 ? 24.583  -62.243 -62.396  1.00 24.33  ? 694  PRO   C CB  1 
ATOM   9927  C  CG  . PRO   C  1 393 ? 23.970  -62.808 -63.700  1.00 23.45  ? 694  PRO   C CG  1 
ATOM   9928  C  CD  . PRO   C  1 393 ? 22.743  -63.532 -63.226  1.00 25.14  ? 694  PRO   C CD  1 
ATOM   9929  N  N   . VAL   C  1 394 ? 22.239  -59.951 -62.654  1.00 25.09  ? 695  VAL   C N   1 
ATOM   9930  C  CA  . VAL   C  1 394 ? 21.933  -58.534 -62.831  1.00 22.24  ? 695  VAL   C CA  1 
ATOM   9931  C  C   . VAL   C  1 394 ? 21.235  -57.962 -61.602  1.00 22.75  ? 695  VAL   C C   1 
ATOM   9932  O  O   . VAL   C  1 394 ? 21.330  -56.761 -61.333  1.00 20.22  ? 695  VAL   C O   1 
ATOM   9933  C  CB  . VAL   C  1 394 ? 21.084  -58.302 -64.095  1.00 20.93  ? 695  VAL   C CB  1 
ATOM   9934  C  CG1 . VAL   C  1 394 ? 21.935  -58.467 -65.393  1.00 20.04  ? 695  VAL   C CG1 1 
ATOM   9935  C  CG2 . VAL   C  1 394 ? 19.843  -59.196 -64.096  1.00 19.54  ? 695  VAL   C CG2 1 
ATOM   9936  N  N   . PHE   C  1 395 ? 20.502  -58.793 -60.866  1.00 20.51  ? 696  PHE   C N   1 
ATOM   9937  C  CA  . PHE   C  1 395 ? 19.799  -58.315 -59.674  1.00 24.16  ? 696  PHE   C CA  1 
ATOM   9938  C  C   . PHE   C  1 395 ? 20.761  -57.712 -58.664  1.00 27.96  ? 696  PHE   C C   1 
ATOM   9939  O  O   . PHE   C  1 395 ? 20.430  -56.732 -57.985  1.00 22.46  ? 696  PHE   C O   1 
ATOM   9940  C  CB  . PHE   C  1 395 ? 19.022  -59.464 -59.037  1.00 21.00  ? 696  PHE   C CB  1 
ATOM   9941  C  CG  . PHE   C  1 395 ? 18.286  -59.083 -57.807  1.00 21.27  ? 696  PHE   C CG  1 
ATOM   9942  C  CD1 . PHE   C  1 395 ? 16.961  -58.696 -57.876  1.00 23.93  ? 696  PHE   C CD1 1 
ATOM   9943  C  CD2 . PHE   C  1 395 ? 18.918  -59.117 -56.561  1.00 24.04  ? 696  PHE   C CD2 1 
ATOM   9944  C  CE1 . PHE   C  1 395 ? 16.275  -58.328 -56.718  1.00 23.51  ? 696  PHE   C CE1 1 
ATOM   9945  C  CE2 . PHE   C  1 395 ? 18.234  -58.747 -55.408  1.00 25.86  ? 696  PHE   C CE2 1 
ATOM   9946  C  CZ  . PHE   C  1 395 ? 16.914  -58.357 -55.492  1.00 23.60  ? 696  PHE   C CZ  1 
ATOM   9947  N  N   . HIS   C  1 396 ? 21.943  -58.299 -58.536  1.00 26.02  ? 697  HIS   C N   1 
ATOM   9948  C  CA  . HIS   C  1 396 ? 22.932  -57.897 -57.552  1.00 25.42  ? 697  HIS   C CA  1 
ATOM   9949  C  C   . HIS   C  1 396 ? 23.889  -56.850 -58.079  1.00 26.51  ? 697  HIS   C C   1 
ATOM   9950  O  O   . HIS   C  1 396 ? 24.798  -56.430 -57.349  1.00 23.53  ? 697  HIS   C O   1 
ATOM   9951  C  CB  . HIS   C  1 396 ? 23.692  -59.131 -57.095  1.00 23.62  ? 697  HIS   C CB  1 
ATOM   9952  C  CG  . HIS   C  1 396 ? 22.782  -60.234 -56.675  1.00 27.85  ? 697  HIS   C CG  1 
ATOM   9953  N  ND1 . HIS   C  1 396 ? 22.302  -60.344 -55.391  1.00 27.25  ? 697  HIS   C ND1 1 
ATOM   9954  C  CD2 . HIS   C  1 396 ? 22.199  -61.228 -57.384  1.00 29.13  ? 697  HIS   C CD2 1 
ATOM   9955  C  CE1 . HIS   C  1 396 ? 21.496  -61.387 -55.314  1.00 31.11  ? 697  HIS   C CE1 1 
ATOM   9956  N  NE2 . HIS   C  1 396 ? 21.415  -61.940 -56.509  1.00 31.37  ? 697  HIS   C NE2 1 
ATOM   9957  N  N   . GLN   C  1 397 ? 23.684  -56.421 -59.320  1.00 28.72  ? 698  GLN   C N   1 
ATOM   9958  C  CA  . GLN   C  1 397 ? 24.563  -55.496 -60.013  1.00 21.38  ? 698  GLN   C CA  1 
ATOM   9959  C  C   . GLN   C  1 397 ? 24.001  -54.086 -59.910  1.00 22.71  ? 698  GLN   C C   1 
ATOM   9960  O  O   . GLN   C  1 397 ? 22.921  -53.812 -60.447  1.00 27.33  ? 698  GLN   C O   1 
ATOM   9961  C  CB  . GLN   C  1 397 ? 24.676  -55.882 -61.494  1.00 21.15  ? 698  GLN   C CB  1 
ATOM   9962  C  CG  . GLN   C  1 397 ? 25.534  -54.919 -62.252  1.00 26.34  ? 698  GLN   C CG  1 
ATOM   9963  C  CD  . GLN   C  1 397 ? 26.953  -54.966 -61.760  1.00 28.02  ? 698  GLN   C CD  1 
ATOM   9964  O  OE1 . GLN   C  1 397 ? 27.565  -56.031 -61.747  1.00 27.65  ? 698  GLN   C OE1 1 
ATOM   9965  N  NE2 . GLN   C  1 397 ? 27.486  -53.818 -61.325  1.00 27.83  ? 698  GLN   C NE2 1 
ATOM   9966  N  N   . GLU   C  1 398 ? 24.730  -53.189 -59.255  1.00 21.55  ? 699  GLU   C N   1 
ATOM   9967  C  CA  . GLU   C  1 398 ? 24.383  -51.785 -59.352  1.00 21.40  ? 699  GLU   C CA  1 
ATOM   9968  C  C   . GLU   C  1 398 ? 24.605  -51.322 -60.783  1.00 22.29  ? 699  GLU   C C   1 
ATOM   9969  O  O   . GLU   C  1 398 ? 25.536  -51.766 -61.455  1.00 21.39  ? 699  GLU   C O   1 
ATOM   9970  C  CB  . GLU   C  1 398 ? 25.210  -50.937 -58.390  1.00 22.03  ? 699  GLU   C CB  1 
ATOM   9971  C  CG  . GLU   C  1 398 ? 24.815  -51.095 -56.912  1.00 25.55  ? 699  GLU   C CG  1 
ATOM   9972  C  CD  . GLU   C  1 398 ? 25.717  -50.292 -55.992  1.00 30.44  ? 699  GLU   C CD  1 
ATOM   9973  O  OE1 . GLU   C  1 398 ? 25.420  -50.198 -54.781  1.00 32.87  ? 699  GLU   C OE1 1 
ATOM   9974  O  OE2 . GLU   C  1 398 ? 26.728  -49.759 -56.491  1.00 31.40  ? 699  GLU   C OE2 1 
ATOM   9975  N  N   . MET   C  1 399 ? 23.720  -50.454 -61.251  1.00 24.54  ? 700  MET   C N   1 
ATOM   9976  C  CA  . MET   C  1 399 ? 23.758  -49.938 -62.609  1.00 24.40  ? 700  MET   C CA  1 
ATOM   9977  C  C   . MET   C  1 399 ? 23.495  -48.449 -62.552  1.00 27.57  ? 700  MET   C C   1 
ATOM   9978  O  O   . MET   C  1 399 ? 22.794  -47.960 -61.663  1.00 37.19  ? 700  MET   C O   1 
ATOM   9979  C  CB  . MET   C  1 399 ? 22.707  -50.595 -63.493  1.00 22.30  ? 700  MET   C CB  1 
ATOM   9980  C  CG  . MET   C  1 399 ? 22.853  -52.080 -63.615  1.00 27.08  ? 700  MET   C CG  1 
ATOM   9981  S  SD  . MET   C  1 399 ? 21.368  -52.773 -64.343  1.00 26.17  ? 700  MET   C SD  1 
ATOM   9982  C  CE  . MET   C  1 399 ? 21.696  -54.532 -64.111  1.00 22.92  ? 700  MET   C CE  1 
ATOM   9983  N  N   . LEU   C  1 400 ? 24.066  -47.733 -63.500  1.00 22.37  ? 701  LEU   C N   1 
ATOM   9984  C  CA  . LEU   C  1 400 ? 23.794  -46.319 -63.666  1.00 20.52  ? 701  LEU   C CA  1 
ATOM   9985  C  C   . LEU   C  1 400 ? 22.993  -46.148 -64.937  1.00 25.94  ? 701  LEU   C C   1 
ATOM   9986  O  O   . LEU   C  1 400 ? 23.344  -46.726 -65.977  1.00 24.92  ? 701  LEU   C O   1 
ATOM   9987  C  CB  . LEU   C  1 400 ? 25.090  -45.509 -63.742  1.00 24.62  ? 701  LEU   C CB  1 
ATOM   9988  C  CG  . LEU   C  1 400 ? 25.906  -45.380 -62.467  1.00 22.71  ? 701  LEU   C CG  1 
ATOM   9989  C  CD1 . LEU   C  1 400 ? 27.241  -44.732 -62.796  1.00 29.20  ? 701  LEU   C CD1 1 
ATOM   9990  C  CD2 . LEU   C  1 400 ? 25.142  -44.580 -61.408  1.00 23.23  ? 701  LEU   C CD2 1 
ATOM   9991  N  N   . ASN   C  1 401 ? 21.912  -45.383 -64.851  1.00 29.91  ? 702  ASN   C N   1 
ATOM   9992  C  CA  . ASN   C  1 401 ? 21.063  -45.139 -66.006  1.00 32.85  ? 702  ASN   C CA  1 
ATOM   9993  C  C   . ASN   C  1 401 ? 21.244  -43.699 -66.451  1.00 29.02  ? 702  ASN   C C   1 
ATOM   9994  O  O   . ASN   C  1 401 ? 21.109  -42.777 -65.645  1.00 25.62  ? 702  ASN   C O   1 
ATOM   9995  C  CB  . ASN   C  1 401 ? 19.587  -45.419 -65.718  1.00 24.62  ? 702  ASN   C CB  1 
ATOM   9996  C  CG  . ASN   C  1 401 ? 18.805  -45.582 -66.984  1.00 32.08  ? 702  ASN   C CG  1 
ATOM   9997  O  OD1 . ASN   C  1 401 ? 19.407  -45.770 -68.025  1.00 27.64  ? 702  ASN   C OD1 1 
ATOM   9998  N  ND2 . ASN   C  1 401 ? 17.482  -45.489 -66.923  1.00 29.60  ? 702  ASN   C ND2 1 
ATOM   9999  N  N   . TYR   C  1 402 ? 21.585  -43.516 -67.725  1.00 27.12  ? 703  TYR   C N   1 
ATOM   10000 C  CA  . TYR   C  1 402 ? 21.691  -42.185 -68.298  1.00 23.99  ? 703  TYR   C CA  1 
ATOM   10001 C  C   . TYR   C  1 402 ? 21.512  -42.334 -69.796  1.00 26.41  ? 703  TYR   C C   1 
ATOM   10002 O  O   . TYR   C  1 402 ? 21.592  -43.437 -70.336  1.00 23.03  ? 703  TYR   C O   1 
ATOM   10003 C  CB  . TYR   C  1 402 ? 23.023  -41.508 -67.958  1.00 21.60  ? 703  TYR   C CB  1 
ATOM   10004 C  CG  . TYR   C  1 402 ? 24.234  -42.395 -68.127  1.00 26.91  ? 703  TYR   C CG  1 
ATOM   10005 C  CD1 . TYR   C  1 402 ? 24.883  -42.496 -69.351  1.00 27.77  ? 703  TYR   C CD1 1 
ATOM   10006 C  CD2 . TYR   C  1 402 ? 24.729  -43.137 -67.062  1.00 29.13  ? 703  TYR   C CD2 1 
ATOM   10007 C  CE1 . TYR   C  1 402 ? 26.002  -43.313 -69.511  1.00 22.60  ? 703  TYR   C CE1 1 
ATOM   10008 C  CE2 . TYR   C  1 402 ? 25.834  -43.961 -67.214  1.00 27.62  ? 703  TYR   C CE2 1 
ATOM   10009 C  CZ  . TYR   C  1 402 ? 26.469  -44.040 -68.439  1.00 26.00  ? 703  TYR   C CZ  1 
ATOM   10010 O  OH  . TYR   C  1 402 ? 27.572  -44.850 -68.585  1.00 28.67  ? 703  TYR   C OH  1 
ATOM   10011 N  N   . ARG   C  1 403 ? 21.238  -41.228 -70.452  1.00 27.24  ? 704  ARG   C N   1 
ATOM   10012 C  CA  . ARG   C  1 403 ? 20.780  -41.264 -71.830  1.00 29.23  ? 704  ARG   C CA  1 
ATOM   10013 C  C   . ARG   C  1 403 ? 21.922  -40.800 -72.724  1.00 28.45  ? 704  ARG   C C   1 
ATOM   10014 O  O   . ARG   C  1 403 ? 22.350  -39.644 -72.648  1.00 28.18  ? 704  ARG   C O   1 
ATOM   10015 C  CB  . ARG   C  1 403 ? 19.534  -40.405 -71.995  1.00 42.14  ? 704  ARG   C CB  1 
ATOM   10016 C  CG  . ARG   C  1 403 ? 18.742  -40.712 -73.248  1.00 61.43  ? 704  ARG   C CG  1 
ATOM   10017 C  CD  . ARG   C  1 403 ? 17.695  -39.641 -73.475  1.00 72.86  ? 704  ARG   C CD  1 
ATOM   10018 N  NE  . ARG   C  1 403 ? 17.487  -39.352 -74.895  1.00 83.69  ? 704  ARG   C NE  1 
ATOM   10019 C  CZ  . ARG   C  1 403 ? 18.344  -38.682 -75.665  1.00 87.64  ? 704  ARG   C CZ  1 
ATOM   10020 N  NH1 . ARG   C  1 403 ? 19.489  -38.236 -75.164  1.00 94.99  ? 704  ARG   C NH1 1 
ATOM   10021 N  NH2 . ARG   C  1 403 ? 18.062  -38.464 -76.945  1.00 80.17  ? 704  ARG   C NH2 1 
ATOM   10022 N  N   . LEU   C  1 404 ? 22.432  -41.711 -73.544  1.00 23.39  ? 705  LEU   C N   1 
ATOM   10023 C  CA  . LEU   C  1 404 ? 23.416  -41.371 -74.555  1.00 26.27  ? 705  LEU   C CA  1 
ATOM   10024 C  C   . LEU   C  1 404 ? 22.748  -41.365 -75.922  1.00 24.20  ? 705  LEU   C C   1 
ATOM   10025 O  O   . LEU   C  1 404 ? 21.777  -42.086 -76.162  1.00 24.77  ? 705  LEU   C O   1 
ATOM   10026 C  CB  . LEU   C  1 404 ? 24.578  -42.366 -74.566  1.00 25.14  ? 705  LEU   C CB  1 
ATOM   10027 C  CG  . LEU   C  1 404 ? 25.385  -42.524 -73.281  1.00 28.00  ? 705  LEU   C CG  1 
ATOM   10028 C  CD1 . LEU   C  1 404 ? 26.355  -43.683 -73.458  1.00 27.90  ? 705  LEU   C CD1 1 
ATOM   10029 C  CD2 . LEU   C  1 404 ? 26.146  -41.249 -72.969  1.00 25.40  ? 705  LEU   C CD2 1 
ATOM   10030 N  N   . THR   C  1 405 ? 23.263  -40.544 -76.795  1.00 25.29  ? 706  THR   C N   1 
ATOM   10031 C  CA  A THR   C  1 405 ? 22.808  -40.555 -78.171  0.68 26.92  ? 706  THR   C CA  1 
ATOM   10032 C  CA  B THR   C  1 405 ? 22.827  -40.508 -78.188  0.32 26.56  ? 706  THR   C CA  1 
ATOM   10033 C  C   . THR   C  1 405 ? 23.931  -41.044 -79.092  1.00 23.19  ? 706  THR   C C   1 
ATOM   10034 O  O   . THR   C  1 405 ? 25.116  -40.873 -78.784  1.00 24.01  ? 706  THR   C O   1 
ATOM   10035 C  CB  A THR   C  1 405 ? 22.336  -39.154 -78.585  0.68 26.84  ? 706  THR   C CB  1 
ATOM   10036 C  CB  B THR   C  1 405 ? 22.472  -39.085 -78.632  0.32 27.46  ? 706  THR   C CB  1 
ATOM   10037 O  OG1 A THR   C  1 405 ? 21.720  -39.209 -79.871  0.68 26.49  ? 706  THR   C OG1 1 
ATOM   10038 O  OG1 B THR   C  1 405 ? 23.597  -38.226 -78.411  0.32 29.63  ? 706  THR   C OG1 1 
ATOM   10039 C  CG2 A THR   C  1 405 ? 23.491  -38.173 -78.609  0.68 30.58  ? 706  THR   C CG2 1 
ATOM   10040 C  CG2 B THR   C  1 405 ? 21.293  -38.569 -77.843  0.32 29.33  ? 706  THR   C CG2 1 
ATOM   10041 N  N   . PRO   C  1 406 ? 23.599  -41.698 -80.222  1.00 27.01  ? 707  PRO   C N   1 
ATOM   10042 C  CA  . PRO   C  1 406 ? 22.306  -42.087 -80.797  1.00 27.95  ? 707  PRO   C CA  1 
ATOM   10043 C  C   . PRO   C  1 406 ? 21.474  -42.910 -79.841  1.00 26.36  ? 707  PRO   C C   1 
ATOM   10044 O  O   . PRO   C  1 406 ? 22.018  -43.585 -78.961  1.00 21.35  ? 707  PRO   C O   1 
ATOM   10045 C  CB  . PRO   C  1 406 ? 22.700  -42.918 -82.025  1.00 26.14  ? 707  PRO   C CB  1 
ATOM   10046 C  CG  . PRO   C  1 406 ? 24.010  -42.364 -82.426  1.00 26.83  ? 707  PRO   C CG  1 
ATOM   10047 C  CD  . PRO   C  1 406 ? 24.707  -42.040 -81.126  1.00 24.81  ? 707  PRO   C CD  1 
ATOM   10048 N  N   . SER   C  1 407 ? 20.160  -42.822 -79.983  1.00 27.73  ? 708  SER   C N   1 
ATOM   10049 C  CA  . SER   C  1 407 ? 19.296  -43.462 -79.013  1.00 27.84  ? 708  SER   C CA  1 
ATOM   10050 C  C   . SER   C  1 407 ? 18.018  -43.909 -79.695  1.00 21.33  ? 708  SER   C C   1 
ATOM   10051 O  O   . SER   C  1 407 ? 17.589  -43.327 -80.689  1.00 26.76  ? 708  SER   C O   1 
ATOM   10052 C  CB  . SER   C  1 407 ? 18.964  -42.514 -77.863  1.00 40.11  ? 708  SER   C CB  1 
ATOM   10053 O  OG  . SER   C  1 407 ? 18.291  -41.382 -78.358  1.00 50.66  ? 708  SER   C OG  1 
ATOM   10054 N  N   . PHE   C  1 408 ? 17.412  -44.947 -79.143  1.00 23.01  ? 709  PHE   C N   1 
ATOM   10055 C  CA  . PHE   C  1 408 ? 16.044  -45.291 -79.480  1.00 22.54  ? 709  PHE   C CA  1 
ATOM   10056 C  C   . PHE   C  1 408 ? 15.124  -44.601 -78.486  1.00 24.23  ? 709  PHE   C C   1 
ATOM   10057 O  O   . PHE   C  1 408 ? 15.355  -44.649 -77.273  1.00 26.10  ? 709  PHE   C O   1 
ATOM   10058 C  CB  . PHE   C  1 408 ? 15.834  -46.803 -79.450  1.00 20.55  ? 709  PHE   C CB  1 
ATOM   10059 C  CG  . PHE   C  1 408 ? 16.519  -47.522 -80.551  1.00 21.76  ? 709  PHE   C CG  1 
ATOM   10060 C  CD1 . PHE   C  1 408 ? 17.621  -48.336 -80.289  1.00 18.30  ? 709  PHE   C CD1 1 
ATOM   10061 C  CD2 . PHE   C  1 408 ? 16.075  -47.386 -81.865  1.00 24.79  ? 709  PHE   C CD2 1 
ATOM   10062 C  CE1 . PHE   C  1 408 ? 18.259  -49.007 -81.322  1.00 22.79  ? 709  PHE   C CE1 1 
ATOM   10063 C  CE2 . PHE   C  1 408 ? 16.710  -48.067 -82.910  1.00 23.59  ? 709  PHE   C CE2 1 
ATOM   10064 C  CZ  . PHE   C  1 408 ? 17.798  -48.868 -82.641  1.00 20.48  ? 709  PHE   C CZ  1 
ATOM   10065 N  N   . GLU   C  1 409 ? 14.089  -43.961 -79.001  1.00 28.60  ? 710  GLU   C N   1 
ATOM   10066 C  CA  . GLU   C  1 409 ? 13.177  -43.176 -78.193  1.00 29.53  ? 710  GLU   C CA  1 
ATOM   10067 C  C   . GLU   C  1 409 ? 11.752  -43.660 -78.413  1.00 32.75  ? 710  GLU   C C   1 
ATOM   10068 O  O   . GLU   C  1 409 ? 11.402  -44.179 -79.482  1.00 24.73  ? 710  GLU   C O   1 
ATOM   10069 C  CB  . GLU   C  1 409 ? 13.267  -41.681 -78.553  1.00 35.07  ? 710  GLU   C CB  1 
ATOM   10070 C  CG  . GLU   C  1 409 ? 14.660  -41.086 -78.439  1.00 37.36  ? 710  GLU   C CG  1 
ATOM   10071 C  CD  . GLU   C  1 409 ? 15.134  -40.988 -76.996  1.00 47.88  ? 710  GLU   C CD  1 
ATOM   10072 O  OE1 . GLU   C  1 409 ? 14.282  -41.006 -76.084  1.00 51.28  ? 710  GLU   C OE1 1 
ATOM   10073 O  OE2 . GLU   C  1 409 ? 16.357  -40.899 -76.771  1.00 51.27  ? 710  GLU   C OE2 1 
ATOM   10074 N  N   . TYR   C  1 410 ? 10.924  -43.452 -77.400  1.00 24.98  ? 711  TYR   C N   1 
ATOM   10075 C  CA  . TYR   C  1 410 ? 9.491   -43.561 -77.595  1.00 26.28  ? 711  TYR   C CA  1 
ATOM   10076 C  C   . TYR   C  1 410 ? 8.981   -42.400 -78.437  1.00 30.39  ? 711  TYR   C C   1 
ATOM   10077 O  O   . TYR   C  1 410 ? 9.560   -41.308 -78.481  1.00 24.95  ? 711  TYR   C O   1 
ATOM   10078 C  CB  . TYR   C  1 410 ? 8.754   -43.560 -76.257  1.00 25.80  ? 711  TYR   C CB  1 
ATOM   10079 C  CG  . TYR   C  1 410 ? 8.981   -44.796 -75.441  1.00 43.90  ? 711  TYR   C CG  1 
ATOM   10080 C  CD1 . TYR   C  1 410 ? 9.498   -44.720 -74.158  1.00 54.85  ? 711  TYR   C CD1 1 
ATOM   10081 C  CD2 . TYR   C  1 410 ? 8.679   -46.042 -75.955  1.00 47.70  ? 711  TYR   C CD2 1 
ATOM   10082 C  CE1 . TYR   C  1 410 ? 9.695   -45.859 -73.404  1.00 52.41  ? 711  TYR   C CE1 1 
ATOM   10083 C  CE2 . TYR   C  1 410 ? 8.880   -47.177 -75.216  1.00 55.48  ? 711  TYR   C CE2 1 
ATOM   10084 C  CZ  . TYR   C  1 410 ? 9.382   -47.085 -73.940  1.00 47.99  ? 711  TYR   C CZ  1 
ATOM   10085 O  OH  . TYR   C  1 410 ? 9.570   -48.237 -73.214  1.00 40.68  ? 711  TYR   C OH  1 
ATOM   10086 N  N   . GLN   C  1 411 ? 7.854   -42.638 -79.087  1.00 29.32  ? 712  GLN   C N   1 
ATOM   10087 C  CA  . GLN   C  1 411 ? 7.184   -41.594 -79.841  1.00 26.99  ? 712  GLN   C CA  1 
ATOM   10088 C  C   . GLN   C  1 411 ? 5.694   -41.835 -79.713  1.00 26.05  ? 712  GLN   C C   1 
ATOM   10089 O  O   . GLN   C  1 411 ? 5.276   -42.941 -79.357  1.00 26.66  ? 712  GLN   C O   1 
ATOM   10090 C  CB  . GLN   C  1 411 ? 7.628   -41.607 -81.312  1.00 29.00  ? 712  GLN   C CB  1 
ATOM   10091 C  CG  . GLN   C  1 411 ? 7.454   -42.940 -81.988  1.00 20.19  ? 712  GLN   C CG  1 
ATOM   10092 C  CD  . GLN   C  1 411 ? 7.895   -42.886 -83.442  1.00 31.80  ? 712  GLN   C CD  1 
ATOM   10093 O  OE1 . GLN   C  1 411 ? 7.844   -41.829 -84.069  1.00 29.18  ? 712  GLN   C OE1 1 
ATOM   10094 N  NE2 . GLN   C  1 411 ? 8.348   -44.020 -83.976  1.00 25.84  ? 712  GLN   C NE2 1 
ATOM   10095 N  N   . PRO   C  1 412 ? 4.866   -40.828 -79.980  1.00 30.12  ? 713  PRO   C N   1 
ATOM   10096 C  CA  . PRO   C  1 412 ? 3.422   -41.044 -79.874  1.00 32.71  ? 713  PRO   C CA  1 
ATOM   10097 C  C   . PRO   C  1 412 ? 2.963   -42.137 -80.827  1.00 34.19  ? 713  PRO   C C   1 
ATOM   10098 O  O   . PRO   C  1 412 ? 3.575   -42.377 -81.873  1.00 31.44  ? 713  PRO   C O   1 
ATOM   10099 C  CB  . PRO   C  1 412 ? 2.828   -39.682 -80.252  1.00 39.54  ? 713  PRO   C CB  1 
ATOM   10100 C  CG  . PRO   C  1 412 ? 3.938   -38.698 -80.076  1.00 35.27  ? 713  PRO   C CG  1 
ATOM   10101 C  CD  . PRO   C  1 412 ? 5.189   -39.454 -80.401  1.00 33.04  ? 713  PRO   C CD  1 
ATOM   10102 N  N   . ASP   C  1 413 ? 1.896   -42.825 -80.435  1.00 30.72  ? 714  ASP   C N   1 
ATOM   10103 C  CA  . ASP   C  1 413 ? 1.260   -43.766 -81.339  1.00 36.35  ? 714  ASP   C CA  1 
ATOM   10104 C  C   . ASP   C  1 413 ? 0.718   -43.010 -82.548  1.00 38.90  ? 714  ASP   C C   1 
ATOM   10105 O  O   . ASP   C  1 413 ? 0.092   -41.953 -82.389  1.00 32.76  ? 714  ASP   C O   1 
ATOM   10106 C  CB  . ASP   C  1 413 ? 0.128   -44.517 -80.640  1.00 39.53  ? 714  ASP   C CB  1 
ATOM   10107 C  CG  . ASP   C  1 413 ? 0.636   -45.557 -79.661  1.00 52.66  ? 714  ASP   C CG  1 
ATOM   10108 O  OD1 . ASP   C  1 413 ? 1.719   -46.125 -79.905  1.00 53.40  ? 714  ASP   C OD1 1 
ATOM   10109 O  OD2 . ASP   C  1 413 ? -0.047  -45.805 -78.643  1.00 59.24  ? 714  ASP   C OD2 1 
ATOM   10110 N  N   . PRO   C  1 414 ? 0.925   -43.526 -83.760  1.00 32.76  ? 715  PRO   C N   1 
ATOM   10111 C  CA  . PRO   C  1 414 ? 0.588   -42.735 -84.955  1.00 29.08  ? 715  PRO   C CA  1 
ATOM   10112 C  C   . PRO   C  1 414 ? -0.874  -42.392 -85.045  1.00 32.80  ? 715  PRO   C C   1 
ATOM   10113 O  O   . PRO   C  1 414 ? -1.218  -41.332 -85.579  1.00 35.27  ? 715  PRO   C O   1 
ATOM   10114 C  CB  . PRO   C  1 414 ? 1.011   -43.637 -86.123  1.00 22.87  ? 715  PRO   C CB  1 
ATOM   10115 C  CG  . PRO   C  1 414 ? 1.532   -44.885 -85.533  1.00 22.00  ? 715  PRO   C CG  1 
ATOM   10116 C  CD  . PRO   C  1 414 ? 1.256   -44.923 -84.073  1.00 30.75  ? 715  PRO   C CD  1 
ATOM   10117 N  N   . TRP   C  1 415 ? -1.755  -43.251 -84.538  1.00 36.12  ? 716  TRP   C N   1 
ATOM   10118 C  CA  . TRP   C  1 415 ? -3.173  -42.938 -84.632  1.00 38.81  ? 716  TRP   C CA  1 
ATOM   10119 C  C   . TRP   C  1 415 ? -3.588  -41.795 -83.716  1.00 40.00  ? 716  TRP   C C   1 
ATOM   10120 O  O   . TRP   C  1 415 ? -4.682  -41.255 -83.894  1.00 44.89  ? 716  TRP   C O   1 
ATOM   10121 C  CB  . TRP   C  1 415 ? -4.010  -44.175 -84.334  1.00 36.54  ? 716  TRP   C CB  1 
ATOM   10122 C  CG  . TRP   C  1 415 ? -3.606  -44.898 -83.106  1.00 34.00  ? 716  TRP   C CG  1 
ATOM   10123 C  CD1 . TRP   C  1 415 ? -4.058  -44.678 -81.839  1.00 33.98  ? 716  TRP   C CD1 1 
ATOM   10124 C  CD2 . TRP   C  1 415 ? -2.665  -45.975 -83.019  1.00 38.45  ? 716  TRP   C CD2 1 
ATOM   10125 N  NE1 . TRP   C  1 415 ? -3.455  -45.554 -80.963  1.00 35.04  ? 716  TRP   C NE1 1 
ATOM   10126 C  CE2 . TRP   C  1 415 ? -2.596  -46.360 -81.660  1.00 37.25  ? 716  TRP   C CE2 1 
ATOM   10127 C  CE3 . TRP   C  1 415 ? -1.874  -46.649 -83.954  1.00 29.92  ? 716  TRP   C CE3 1 
ATOM   10128 C  CZ2 . TRP   C  1 415 ? -1.772  -47.391 -81.217  1.00 35.45  ? 716  TRP   C CZ2 1 
ATOM   10129 C  CZ3 . TRP   C  1 415 ? -1.051  -47.674 -83.510  1.00 35.77  ? 716  TRP   C CZ3 1 
ATOM   10130 C  CH2 . TRP   C  1 415 ? -1.008  -48.035 -82.149  1.00 40.62  ? 716  TRP   C CH2 1 
ATOM   10131 N  N   . ASN   C  1 416 ? -2.756  -41.399 -82.756  1.00 42.48  ? 717  ASN   C N   1 
ATOM   10132 C  CA  . ASN   C  1 416 ? -3.107  -40.238 -81.947  1.00 45.67  ? 717  ASN   C CA  1 
ATOM   10133 C  C   . ASN   C  1 416 ? -2.711  -38.928 -82.603  1.00 44.10  ? 717  ASN   C C   1 
ATOM   10134 O  O   . ASN   C  1 416 ? -3.229  -37.879 -82.223  1.00 48.61  ? 717  ASN   C O   1 
ATOM   10135 C  CB  . ASN   C  1 416 ? -2.461  -40.328 -80.570  1.00 41.84  ? 717  ASN   C CB  1 
ATOM   10136 C  CG  . ASN   C  1 416 ? -2.896  -41.550 -79.819  1.00 40.00  ? 717  ASN   C CG  1 
ATOM   10137 O  OD1 . ASN   C  1 416 ? -4.048  -41.985 -79.927  1.00 40.20  ? 717  ASN   C OD1 1 
ATOM   10138 N  ND2 . ASN   C  1 416 ? -1.976  -42.134 -79.069  1.00 36.69  ? 717  ASN   C ND2 1 
ATOM   10139 N  N   . THR   C  1 417 ? -1.812  -38.955 -83.575  1.00 40.68  ? 718  THR   C N   1 
ATOM   10140 C  CA  . THR   C  1 417 ? -1.362  -37.725 -84.198  1.00 41.50  ? 718  THR   C CA  1 
ATOM   10141 C  C   . THR   C  1 417 ? -1.627  -37.648 -85.690  1.00 36.87  ? 718  THR   C C   1 
ATOM   10142 O  O   . THR   C  1 417 ? -1.587  -36.547 -86.241  1.00 38.87  ? 718  THR   C O   1 
ATOM   10143 C  CB  . THR   C  1 417 ? 0.137   -37.529 -83.951  1.00 40.20  ? 718  THR   C CB  1 
ATOM   10144 O  OG1 . THR   C  1 417 ? 0.852   -38.644 -84.503  1.00 33.91  ? 718  THR   C OG1 1 
ATOM   10145 C  CG2 . THR   C  1 417 ? 0.404   -37.459 -82.446  1.00 34.74  ? 718  THR   C CG2 1 
ATOM   10146 N  N   . HIS   C  1 418 ? -1.912  -38.764 -86.355  1.00 35.89  ? 719  HIS   C N   1 
ATOM   10147 C  CA  . HIS   C  1 418 ? -2.046  -38.729 -87.805  1.00 34.18  ? 719  HIS   C CA  1 
ATOM   10148 C  C   . HIS   C  1 418 ? -3.299  -37.977 -88.226  1.00 37.82  ? 719  HIS   C C   1 
ATOM   10149 O  O   . HIS   C  1 418 ? -4.381  -38.172 -87.671  1.00 40.75  ? 719  HIS   C O   1 
ATOM   10150 C  CB  . HIS   C  1 418 ? -2.087  -40.133 -88.386  1.00 36.64  ? 719  HIS   C CB  1 
ATOM   10151 C  CG  . HIS   C  1 418 ? -2.308  -40.146 -89.862  1.00 37.68  ? 719  HIS   C CG  1 
ATOM   10152 N  ND1 . HIS   C  1 418 ? -1.356  -39.706 -90.754  1.00 32.54  ? 719  HIS   C ND1 1 
ATOM   10153 C  CD2 . HIS   C  1 418 ? -3.385  -40.503 -90.599  1.00 33.20  ? 719  HIS   C CD2 1 
ATOM   10154 C  CE1 . HIS   C  1 418 ? -1.828  -39.818 -91.983  1.00 37.29  ? 719  HIS   C CE1 1 
ATOM   10155 N  NE2 . HIS   C  1 418 ? -3.055  -40.304 -91.916  1.00 34.38  ? 719  HIS   C NE2 1 
ATOM   10156 N  N   . VAL   C  1 419 ? -3.148  -37.116 -89.219  1.00 41.34  ? 720  VAL   C N   1 
ATOM   10157 C  CA  . VAL   C  1 419 ? -4.260  -36.352 -89.763  1.00 51.03  ? 720  VAL   C CA  1 
ATOM   10158 C  C   . VAL   C  1 419 ? -4.689  -37.036 -91.055  1.00 40.18  ? 720  VAL   C C   1 
ATOM   10159 O  O   . VAL   C  1 419 ? -4.005  -36.948 -92.082  1.00 46.52  ? 720  VAL   C O   1 
ATOM   10160 C  CB  . VAL   C  1 419 ? -3.881  -34.880 -89.967  1.00 55.89  ? 720  VAL   C CB  1 
ATOM   10161 C  CG1 . VAL   C  1 419 ? -4.856  -34.195 -90.917  1.00 48.10  ? 720  VAL   C CG1 1 
ATOM   10162 C  CG2 . VAL   C  1 419 ? -3.855  -34.173 -88.600  1.00 57.27  ? 720  VAL   C CG2 1 
ATOM   10163 N  N   . TRP   C  1 420 ? -5.815  -37.739 -90.976  1.00 34.86  ? 721  TRP   C N   1 
ATOM   10164 C  CA  . TRP   C  1 420 ? -6.291  -38.573 -92.070  1.00 46.11  ? 721  TRP   C CA  1 
ATOM   10165 C  C   . TRP   C  1 420 ? -6.635  -37.747 -93.301  1.00 57.35  ? 721  TRP   C C   1 
ATOM   10166 O  O   . TRP   C  1 420 ? -7.268  -36.689 -93.205  1.00 56.65  ? 721  TRP   C O   1 
ATOM   10167 C  CB  . TRP   C  1 420 ? -7.506  -39.375 -91.612  1.00 45.82  ? 721  TRP   C CB  1 
ATOM   10168 C  CG  . TRP   C  1 420 ? -7.100  -40.494 -90.727  1.00 41.04  ? 721  TRP   C CG  1 
ATOM   10169 C  CD1 . TRP   C  1 420 ? -6.954  -40.464 -89.360  1.00 34.50  ? 721  TRP   C CD1 1 
ATOM   10170 C  CD2 . TRP   C  1 420 ? -6.729  -41.808 -91.143  1.00 31.40  ? 721  TRP   C CD2 1 
ATOM   10171 N  NE1 . TRP   C  1 420 ? -6.526  -41.688 -88.909  1.00 30.87  ? 721  TRP   C NE1 1 
ATOM   10172 C  CE2 . TRP   C  1 420 ? -6.381  -42.532 -89.981  1.00 35.10  ? 721  TRP   C CE2 1 
ATOM   10173 C  CE3 . TRP   C  1 420 ? -6.666  -42.448 -92.387  1.00 38.73  ? 721  TRP   C CE3 1 
ATOM   10174 C  CZ2 . TRP   C  1 420 ? -5.983  -43.865 -90.028  1.00 45.43  ? 721  TRP   C CZ2 1 
ATOM   10175 C  CZ3 . TRP   C  1 420 ? -6.263  -43.766 -92.433  1.00 42.76  ? 721  TRP   C CZ3 1 
ATOM   10176 C  CH2 . TRP   C  1 420 ? -5.927  -44.465 -91.258  1.00 45.90  ? 721  TRP   C CH2 1 
ATOM   10177 N  N   . LYS   C  1 421 ? -6.219  -38.255 -94.466  1.00 62.21  ? 722  LYS   C N   1 
ATOM   10178 C  CA  . LYS   C  1 421 ? -6.401  -37.609 -95.761  1.00 64.69  ? 722  LYS   C CA  1 
ATOM   10179 C  C   . LYS   C  1 421 ? -7.626  -38.101 -96.529  1.00 74.60  ? 722  LYS   C C   1 
ATOM   10180 O  O   . LYS   C  1 421 ? -8.327  -37.285 -97.137  1.00 77.93  ? 722  LYS   C O   1 
ATOM   10181 C  CB  . LYS   C  1 421 ? -5.157  -37.822 -96.634  1.00 63.46  ? 722  LYS   C CB  1 
ATOM   10182 C  CG  . LYS   C  1 421 ? -3.838  -37.356 -96.021  1.00 68.91  ? 722  LYS   C CG  1 
ATOM   10183 C  CD  . LYS   C  1 421 ? -2.708  -37.421 -97.055  1.00 72.75  ? 722  LYS   C CD  1 
ATOM   10184 C  CE  . LYS   C  1 421 ? -1.347  -37.070 -96.460  1.00 68.15  ? 722  LYS   C CE  1 
ATOM   10185 N  NZ  . LYS   C  1 421 ? -1.253  -35.661 -95.990  1.00 68.05  ? 722  LYS   C NZ  1 
ATOM   10186 N  N   . LEU   C  1 422 ? -7.905  -39.409 -96.516  1.00 56.23  ? 723  LEU   C N   1 
ATOM   10187 C  CA  . LEU   C  1 422 ? -8.847  -40.009 -97.460  1.00 75.26  ? 723  LEU   C CA  1 
ATOM   10188 C  C   . LEU   C  1 422 ? -10.284 -39.547 -97.197  1.00 85.84  ? 723  LEU   C C   1 
ATOM   10189 O  O   . LEU   C  1 422 ? -10.650 -39.162 -96.083  1.00 83.85  ? 723  LEU   C O   1 
ATOM   10190 C  CB  . LEU   C  1 422 ? -8.764  -41.539 -97.407  1.00 82.59  ? 723  LEU   C CB  1 
ATOM   10191 C  CG  . LEU   C  1 422 ? -9.052  -42.328 -98.698  1.00 85.96  ? 723  LEU   C CG  1 
ATOM   10192 C  CD1 . LEU   C  1 422 ? -8.162  -43.570 -98.798  1.00 87.19  ? 723  LEU   C CD1 1 
ATOM   10193 C  CD2 . LEU   C  1 422 ? -10.517 -42.727 -98.800  1.00 84.29  ? 723  LEU   C CD2 1 
ATOM   10194 N  N   . VAL   C  1 423 ? -11.112 -39.649 -98.245  1.00 93.66  ? 724  VAL   C N   1 
ATOM   10195 C  CA  . VAL   C  1 423 ? -12.438 -39.006 -98.366  1.00 87.61  ? 724  VAL   C CA  1 
ATOM   10196 C  C   . VAL   C  1 423 ? -12.461 -37.605 -97.731  1.00 88.37  ? 724  VAL   C C   1 
ATOM   10197 O  O   . VAL   C  1 423 ? -11.475 -36.859 -97.738  1.00 86.71  ? 724  VAL   C O   1 
ATOM   10198 C  CB  . VAL   C  1 423 ? -13.612 -39.894 -97.789  1.00 77.02  ? 724  VAL   C CB  1 
ATOM   10199 C  CG1 . VAL   C  1 423 ? -14.441 -40.492 -98.929  1.00 71.43  ? 724  VAL   C CG1 1 
ATOM   10200 C  CG2 . VAL   C  1 423 ? -13.131 -40.998 -96.841  1.00 69.31  ? 724  VAL   C CG2 1 
ATOM   10201 O  OXT . VAL   C  1 423 ? -13.486 -37.157 -97.216  1.00 88.01  ? 724  VAL   C OXT 1 
ATOM   10202 N  N   . PHE   D  1 4   ? 3.755   -32.110 -58.598  1.00 65.63  ? 305  PHE   D N   1 
ATOM   10203 C  CA  . PHE   D  1 4   ? 2.537   -32.664 -59.178  1.00 61.30  ? 305  PHE   D CA  1 
ATOM   10204 C  C   . PHE   D  1 4   ? 2.895   -33.711 -60.228  1.00 53.79  ? 305  PHE   D C   1 
ATOM   10205 O  O   . PHE   D  1 4   ? 2.792   -33.479 -61.428  1.00 55.65  ? 305  PHE   D O   1 
ATOM   10206 C  CB  . PHE   D  1 4   ? 1.689   -31.549 -59.774  1.00 72.65  ? 305  PHE   D CB  1 
ATOM   10207 C  CG  . PHE   D  1 4   ? 2.222   -30.177 -59.479  1.00 87.04  ? 305  PHE   D CG  1 
ATOM   10208 C  CD1 . PHE   D  1 4   ? 2.890   -29.456 -60.462  1.00 93.28  ? 305  PHE   D CD1 1 
ATOM   10209 C  CD2 . PHE   D  1 4   ? 2.081   -29.617 -58.215  1.00 88.63  ? 305  PHE   D CD2 1 
ATOM   10210 C  CE1 . PHE   D  1 4   ? 3.394   -28.198 -60.198  1.00 95.37  ? 305  PHE   D CE1 1 
ATOM   10211 C  CE2 . PHE   D  1 4   ? 2.587   -28.359 -57.943  1.00 93.29  ? 305  PHE   D CE2 1 
ATOM   10212 C  CZ  . PHE   D  1 4   ? 3.245   -27.648 -58.937  1.00 96.85  ? 305  PHE   D CZ  1 
ATOM   10213 N  N   . LEU   D  1 5   ? 3.335   -34.870 -59.757  1.00 41.49  ? 306  LEU   D N   1 
ATOM   10214 C  CA  . LEU   D  1 5   ? 3.759   -35.962 -60.613  1.00 36.95  ? 306  LEU   D CA  1 
ATOM   10215 C  C   . LEU   D  1 5   ? 2.731   -37.079 -60.563  1.00 35.15  ? 306  LEU   D C   1 
ATOM   10216 O  O   . LEU   D  1 5   ? 2.065   -37.292 -59.548  1.00 42.03  ? 306  LEU   D O   1 
ATOM   10217 C  CB  . LEU   D  1 5   ? 5.129   -36.486 -60.186  1.00 33.49  ? 306  LEU   D CB  1 
ATOM   10218 C  CG  . LEU   D  1 5   ? 6.213   -35.407 -60.137  1.00 39.62  ? 306  LEU   D CG  1 
ATOM   10219 C  CD1 . LEU   D  1 5   ? 7.440   -35.906 -59.390  1.00 36.55  ? 306  LEU   D CD1 1 
ATOM   10220 C  CD2 . LEU   D  1 5   ? 6.565   -34.960 -61.549  1.00 34.39  ? 306  LEU   D CD2 1 
ATOM   10221 N  N   . LYS   D  1 6   ? 2.603   -37.798 -61.663  1.00 28.79  ? 307  LYS   D N   1 
ATOM   10222 C  CA  . LYS   D  1 6   ? 1.650   -38.891 -61.749  1.00 33.12  ? 307  LYS   D CA  1 
ATOM   10223 C  C   . LYS   D  1 6   ? 2.399   -40.211 -61.826  1.00 32.62  ? 307  LYS   D C   1 
ATOM   10224 O  O   . LYS   D  1 6   ? 3.458   -40.301 -62.454  1.00 33.82  ? 307  LYS   D O   1 
ATOM   10225 C  CB  . LYS   D  1 6   ? 0.738   -38.741 -62.972  1.00 40.23  ? 307  LYS   D CB  1 
ATOM   10226 C  CG  . LYS   D  1 6   ? -0.235  -37.568 -62.906  1.00 48.37  ? 307  LYS   D CG  1 
ATOM   10227 C  CD  . LYS   D  1 6   ? -1.133  -37.537 -64.144  1.00 51.93  ? 307  LYS   D CD  1 
ATOM   10228 C  CE  . LYS   D  1 6   ? -2.071  -36.337 -64.137  1.00 56.30  ? 307  LYS   D CE  1 
ATOM   10229 N  NZ  . LYS   D  1 6   ? -2.919  -36.316 -62.914  1.00 59.73  ? 307  LYS   D NZ  1 
ATOM   10230 N  N   . VAL   D  1 7   ? 1.859   -41.230 -61.181  1.00 27.64  ? 308  VAL   D N   1 
ATOM   10231 C  CA  . VAL   D  1 7   ? 2.338   -42.591 -61.361  1.00 29.43  ? 308  VAL   D CA  1 
ATOM   10232 C  C   . VAL   D  1 7   ? 1.167   -43.414 -61.856  1.00 32.85  ? 308  VAL   D C   1 
ATOM   10233 O  O   . VAL   D  1 7   ? 0.020   -43.205 -61.447  1.00 35.10  ? 308  VAL   D O   1 
ATOM   10234 C  CB  . VAL   D  1 7   ? 2.941   -43.209 -60.081  1.00 30.16  ? 308  VAL   D CB  1 
ATOM   10235 C  CG1 . VAL   D  1 7   ? 4.135   -42.397 -59.613  1.00 39.61  ? 308  VAL   D CG1 1 
ATOM   10236 C  CG2 . VAL   D  1 7   ? 1.900   -43.319 -58.991  1.00 25.66  ? 308  VAL   D CG2 1 
ATOM   10237 N  N   . LYS   D  1 8   ? 1.453   -44.327 -62.762  1.00 30.97  ? 309  LYS   D N   1 
ATOM   10238 C  CA  . LYS   D  1 8   ? 0.424   -45.135 -63.373  1.00 27.06  ? 309  LYS   D CA  1 
ATOM   10239 C  C   . LYS   D  1 8   ? 0.705   -46.583 -63.041  1.00 24.50  ? 309  LYS   D C   1 
ATOM   10240 O  O   . LYS   D  1 8   ? 1.865   -47.006 -63.003  1.00 24.66  ? 309  LYS   D O   1 
ATOM   10241 C  CB  . LYS   D  1 8   ? 0.389   -44.922 -64.901  1.00 31.48  ? 309  LYS   D CB  1 
ATOM   10242 C  CG  . LYS   D  1 8   ? -0.494  -45.886 -65.662  1.00 31.71  ? 309  LYS   D CG  1 
ATOM   10243 C  CD  . LYS   D  1 8   ? -0.571  -45.459 -67.124  1.00 44.23  ? 309  LYS   D CD  1 
ATOM   10244 C  CE  . LYS   D  1 8   ? -1.498  -46.347 -67.920  1.00 48.35  ? 309  LYS   D CE  1 
ATOM   10245 N  NZ  . LYS   D  1 8   ? -1.466  -46.007 -69.369  1.00 44.19  ? 309  LYS   D NZ  1 
ATOM   10246 N  N   . ASN   D  1 9   ? -0.361  -47.327 -62.781  1.00 24.39  ? 310  ASN   D N   1 
ATOM   10247 C  CA  . ASN   D  1 9   ? -0.298  -48.774 -62.713  1.00 27.71  ? 310  ASN   D CA  1 
ATOM   10248 C  C   . ASN   D  1 9   ? -0.693  -49.311 -64.078  1.00 27.17  ? 310  ASN   D C   1 
ATOM   10249 O  O   . ASN   D  1 9   ? -1.804  -49.056 -64.551  1.00 31.24  ? 310  ASN   D O   1 
ATOM   10250 C  CB  . ASN   D  1 9   ? -1.216  -49.333 -61.629  1.00 37.61  ? 310  ASN   D CB  1 
ATOM   10251 C  CG  . ASN   D  1 9   ? -1.067  -50.825 -61.483  1.00 40.75  ? 310  ASN   D CG  1 
ATOM   10252 O  OD1 . ASN   D  1 9   ? -1.461  -51.587 -62.371  1.00 41.58  ? 310  ASN   D OD1 1 
ATOM   10253 N  ND2 . ASN   D  1 9   ? -0.470  -51.257 -60.378  1.00 38.85  ? 310  ASN   D ND2 1 
ATOM   10254 N  N   . TRP   D  1 10  ? 0.210   -50.059 -64.701  1.00 24.14  ? 311  TRP   D N   1 
ATOM   10255 C  CA  . TRP   D  1 10  ? 0.003   -50.461 -66.091  1.00 30.78  ? 311  TRP   D CA  1 
ATOM   10256 C  C   . TRP   D  1 10  ? -0.903  -51.667 -66.217  1.00 36.43  ? 311  TRP   D C   1 
ATOM   10257 O  O   . TRP   D  1 10  ? -1.375  -51.957 -67.316  1.00 33.45  ? 311  TRP   D O   1 
ATOM   10258 C  CB  . TRP   D  1 10  ? 1.355   -50.715 -66.753  1.00 25.17  ? 311  TRP   D CB  1 
ATOM   10259 C  CG  . TRP   D  1 10  ? 2.047   -49.416 -66.996  1.00 28.37  ? 311  TRP   D CG  1 
ATOM   10260 C  CD1 . TRP   D  1 10  ? 2.862   -48.741 -66.135  1.00 23.96  ? 311  TRP   D CD1 1 
ATOM   10261 C  CD2 . TRP   D  1 10  ? 1.929   -48.599 -68.163  1.00 32.07  ? 311  TRP   D CD2 1 
ATOM   10262 N  NE1 . TRP   D  1 10  ? 3.278   -47.555 -66.705  1.00 27.30  ? 311  TRP   D NE1 1 
ATOM   10263 C  CE2 . TRP   D  1 10  ? 2.719   -47.447 -67.951  1.00 29.12  ? 311  TRP   D CE2 1 
ATOM   10264 C  CE3 . TRP   D  1 10  ? 1.249   -48.740 -69.378  1.00 30.84  ? 311  TRP   D CE3 1 
ATOM   10265 C  CZ2 . TRP   D  1 10  ? 2.839   -46.440 -68.906  1.00 34.98  ? 311  TRP   D CZ2 1 
ATOM   10266 C  CZ3 . TRP   D  1 10  ? 1.372   -47.737 -70.329  1.00 37.51  ? 311  TRP   D CZ3 1 
ATOM   10267 C  CH2 . TRP   D  1 10  ? 2.164   -46.605 -70.088  1.00 44.69  ? 311  TRP   D CH2 1 
ATOM   10268 N  N   . GLU   D  1 11  ? -1.177  -52.349 -65.109  1.00 32.75  ? 312  GLU   D N   1 
ATOM   10269 C  CA  . GLU   D  1 11  ? -2.138  -53.438 -65.107  1.00 29.43  ? 312  GLU   D CA  1 
ATOM   10270 C  C   . GLU   D  1 11  ? -3.558  -52.913 -64.926  1.00 32.96  ? 312  GLU   D C   1 
ATOM   10271 O  O   . GLU   D  1 11  ? -4.479  -53.341 -65.630  1.00 34.92  ? 312  GLU   D O   1 
ATOM   10272 C  CB  . GLU   D  1 11  ? -1.763  -54.427 -64.009  1.00 29.40  ? 312  GLU   D CB  1 
ATOM   10273 C  CG  . GLU   D  1 11  ? -2.455  -55.755 -64.067  1.00 45.65  ? 312  GLU   D CG  1 
ATOM   10274 C  CD  . GLU   D  1 11  ? -2.186  -56.601 -62.832  1.00 53.87  ? 312  GLU   D CD  1 
ATOM   10275 O  OE1 . GLU   D  1 11  ? -1.322  -56.220 -62.005  1.00 47.17  ? 312  GLU   D OE1 1 
ATOM   10276 O  OE2 . GLU   D  1 11  ? -2.856  -57.647 -62.685  1.00 61.31  ? 312  GLU   D OE2 1 
ATOM   10277 N  N   . THR   D  1 12  ? -3.748  -51.956 -64.022  1.00 31.40  ? 313  THR   D N   1 
ATOM   10278 C  CA  . THR   D  1 12  ? -5.083  -51.487 -63.674  1.00 29.27  ? 313  THR   D CA  1 
ATOM   10279 C  C   . THR   D  1 12  ? -5.435  -50.156 -64.313  1.00 33.93  ? 313  THR   D C   1 
ATOM   10280 O  O   . THR   D  1 12  ? -6.606  -49.767 -64.288  1.00 33.97  ? 313  THR   D O   1 
ATOM   10281 C  CB  . THR   D  1 12  ? -5.200  -51.357 -62.155  1.00 38.89  ? 313  THR   D CB  1 
ATOM   10282 O  OG1 . THR   D  1 12  ? -4.284  -50.353 -61.706  1.00 41.85  ? 313  THR   D OG1 1 
ATOM   10283 C  CG2 . THR   D  1 12  ? -4.823  -52.671 -61.489  1.00 39.80  ? 313  THR   D CG2 1 
ATOM   10284 N  N   . GLU   D  1 13  ? -4.449  -49.448 -64.859  1.00 33.94  ? 314  GLU   D N   1 
ATOM   10285 C  CA  . GLU   D  1 13  ? -4.569  -48.096 -65.394  1.00 35.38  ? 314  GLU   D CA  1 
ATOM   10286 C  C   . GLU   D  1 13  ? -4.917  -47.069 -64.327  1.00 38.81  ? 314  GLU   D C   1 
ATOM   10287 O  O   . GLU   D  1 13  ? -5.217  -45.917 -64.657  1.00 34.82  ? 314  GLU   D O   1 
ATOM   10288 C  CB  . GLU   D  1 13  ? -5.572  -48.035 -66.552  1.00 47.41  ? 314  GLU   D CB  1 
ATOM   10289 C  CG  . GLU   D  1 13  ? -5.383  -49.164 -67.554  1.00 55.97  ? 314  GLU   D CG  1 
ATOM   10290 C  CD  . GLU   D  1 13  ? -5.887  -48.810 -68.938  1.00 66.05  ? 314  GLU   D CD  1 
ATOM   10291 O  OE1 . GLU   D  1 13  ? -5.297  -47.910 -69.575  1.00 68.90  ? 314  GLU   D OE1 1 
ATOM   10292 O  OE2 . GLU   D  1 13  ? -6.873  -49.432 -69.383  1.00 69.56  ? 314  GLU   D OE2 1 
ATOM   10293 N  N   . VAL   D  1 14  ? -4.870  -47.446 -63.048  1.00 39.49  ? 315  VAL   D N   1 
ATOM   10294 C  CA  . VAL   D  1 14  ? -5.018  -46.459 -61.989  1.00 38.94  ? 315  VAL   D CA  1 
ATOM   10295 C  C   . VAL   D  1 14  ? -3.850  -45.482 -62.045  1.00 34.87  ? 315  VAL   D C   1 
ATOM   10296 O  O   . VAL   D  1 14  ? -2.681  -45.884 -62.134  1.00 32.34  ? 315  VAL   D O   1 
ATOM   10297 C  CB  . VAL   D  1 14  ? -5.122  -47.160 -60.628  1.00 42.73  ? 315  VAL   D CB  1 
ATOM   10298 C  CG1 . VAL   D  1 14  ? -4.856  -46.183 -59.492  1.00 39.47  ? 315  VAL   D CG1 1 
ATOM   10299 C  CG2 . VAL   D  1 14  ? -6.490  -47.796 -60.477  1.00 45.54  ? 315  VAL   D CG2 1 
ATOM   10300 N  N   . VAL   D  1 15  ? -4.168  -44.188 -62.044  1.00 32.35  ? 316  VAL   D N   1 
ATOM   10301 C  CA  . VAL   D  1 15  ? -3.179  -43.120 -61.971  1.00 34.61  ? 316  VAL   D CA  1 
ATOM   10302 C  C   . VAL   D  1 15  ? -3.302  -42.451 -60.607  1.00 34.58  ? 316  VAL   D C   1 
ATOM   10303 O  O   . VAL   D  1 15  ? -4.410  -42.132 -60.164  1.00 35.25  ? 316  VAL   D O   1 
ATOM   10304 C  CB  . VAL   D  1 15  ? -3.360  -42.081 -63.088  1.00 32.36  ? 316  VAL   D CB  1 
ATOM   10305 C  CG1 . VAL   D  1 15  ? -2.231  -41.052 -63.022  1.00 34.76  ? 316  VAL   D CG1 1 
ATOM   10306 C  CG2 . VAL   D  1 15  ? -3.438  -42.745 -64.470  1.00 32.10  ? 316  VAL   D CG2 1 
ATOM   10307 N  N   . LEU   D  1 16  ? -2.164  -42.234 -59.954  1.00 28.12  ? 317  LEU   D N   1 
ATOM   10308 C  CA  . LEU   D  1 16  ? -2.074  -41.527 -58.685  1.00 34.07  ? 317  LEU   D CA  1 
ATOM   10309 C  C   . LEU   D  1 16  ? -1.255  -40.264 -58.896  1.00 37.41  ? 317  LEU   D C   1 
ATOM   10310 O  O   . LEU   D  1 16  ? -0.329  -40.241 -59.716  1.00 36.65  ? 317  LEU   D O   1 
ATOM   10311 C  CB  . LEU   D  1 16  ? -1.421  -42.393 -57.602  1.00 28.40  ? 317  LEU   D CB  1 
ATOM   10312 C  CG  . LEU   D  1 16  ? -2.115  -43.737 -57.374  1.00 33.73  ? 317  LEU   D CG  1 
ATOM   10313 C  CD1 . LEU   D  1 16  ? -1.371  -44.573 -56.370  1.00 31.48  ? 317  LEU   D CD1 1 
ATOM   10314 C  CD2 . LEU   D  1 16  ? -3.571  -43.532 -56.952  1.00 33.55  ? 317  LEU   D CD2 1 
ATOM   10315 N  N   . THR   D  1 17  ? -1.605  -39.213 -58.157  1.00 31.72  ? 318  THR   D N   1 
ATOM   10316 C  CA  . THR   D  1 17  ? -0.997  -37.901 -58.319  1.00 33.23  ? 318  THR   D CA  1 
ATOM   10317 C  C   . THR   D  1 17  ? -0.254  -37.546 -57.046  1.00 32.75  ? 318  THR   D C   1 
ATOM   10318 O  O   . THR   D  1 17  ? -0.861  -37.447 -55.976  1.00 34.78  ? 318  THR   D O   1 
ATOM   10319 C  CB  . THR   D  1 17  ? -2.045  -36.835 -58.630  1.00 40.16  ? 318  THR   D CB  1 
ATOM   10320 O  OG1 . THR   D  1 17  ? -2.879  -37.293 -59.698  1.00 41.45  ? 318  THR   D OG1 1 
ATOM   10321 C  CG2 . THR   D  1 17  ? -1.357  -35.536 -59.048  1.00 41.97  ? 318  THR   D CG2 1 
ATOM   10322 N  N   . ASP   D  1 18  ? 1.047   -37.337 -57.169  1.00 25.65  ? 319  ASP   D N   1 
ATOM   10323 C  CA  . ASP   D  1 18  ? 1.914   -37.155 -56.022  1.00 28.00  ? 319  ASP   D CA  1 
ATOM   10324 C  C   . ASP   D  1 18  ? 2.172   -35.675 -55.807  1.00 32.56  ? 319  ASP   D C   1 
ATOM   10325 O  O   . ASP   D  1 18  ? 2.693   -34.993 -56.699  1.00 33.52  ? 319  ASP   D O   1 
ATOM   10326 C  CB  . ASP   D  1 18  ? 3.230   -37.892 -56.227  1.00 28.14  ? 319  ASP   D CB  1 
ATOM   10327 C  CG  . ASP   D  1 18  ? 4.036   -37.990 -54.954  1.00 26.64  ? 319  ASP   D CG  1 
ATOM   10328 O  OD1 . ASP   D  1 18  ? 4.456   -36.948 -54.416  1.00 32.97  ? 319  ASP   D OD1 1 
ATOM   10329 O  OD2 . ASP   D  1 18  ? 4.230   -39.118 -54.480  1.00 31.05  ? 319  ASP   D OD2 1 
ATOM   10330 N  N   . THR   D  1 19  ? 1.789   -35.182 -54.636  1.00 29.67  ? 320  THR   D N   1 
ATOM   10331 C  CA  . THR   D  1 19  ? 2.235   -33.888 -54.143  1.00 31.58  ? 320  THR   D CA  1 
ATOM   10332 C  C   . THR   D  1 19  ? 3.119   -34.013 -52.916  1.00 33.44  ? 320  THR   D C   1 
ATOM   10333 O  O   . THR   D  1 19  ? 3.804   -33.047 -52.567  1.00 33.73  ? 320  THR   D O   1 
ATOM   10334 C  CB  . THR   D  1 19  ? 1.039   -32.993 -53.790  1.00 31.72  ? 320  THR   D CB  1 
ATOM   10335 O  OG1 . THR   D  1 19  ? 0.130   -33.712 -52.951  1.00 34.89  ? 320  THR   D OG1 1 
ATOM   10336 C  CG2 . THR   D  1 19  ? 0.320   -32.533 -55.046  1.00 32.91  ? 320  THR   D CG2 1 
ATOM   10337 N  N   . LEU   D  1 20  ? 3.130   -35.181 -52.267  1.00 27.39  ? 321  LEU   D N   1 
ATOM   10338 C  CA  . LEU   D  1 20  ? 3.955   -35.362 -51.078  1.00 30.84  ? 321  LEU   D CA  1 
ATOM   10339 C  C   . LEU   D  1 20  ? 5.435   -35.121 -51.368  1.00 36.08  ? 321  LEU   D C   1 
ATOM   10340 O  O   . LEU   D  1 20  ? 6.157   -34.640 -50.491  1.00 31.37  ? 321  LEU   D O   1 
ATOM   10341 C  CB  . LEU   D  1 20  ? 3.745   -36.766 -50.508  1.00 25.52  ? 321  LEU   D CB  1 
ATOM   10342 C  CG  . LEU   D  1 20  ? 4.411   -37.065 -49.163  1.00 29.60  ? 321  LEU   D CG  1 
ATOM   10343 C  CD1 . LEU   D  1 20  ? 3.906   -36.097 -48.099  1.00 34.81  ? 321  LEU   D CD1 1 
ATOM   10344 C  CD2 . LEU   D  1 20  ? 4.126   -38.486 -48.768  1.00 20.38  ? 321  LEU   D CD2 1 
ATOM   10345 N  N   . HIS   D  1 21  ? 5.902   -35.433 -52.588  1.00 27.19  ? 322  HIS   D N   1 
ATOM   10346 C  CA  . HIS   D  1 21  ? 7.319   -35.267 -52.919  1.00 27.14  ? 322  HIS   D CA  1 
ATOM   10347 C  C   . HIS   D  1 21  ? 7.796   -33.827 -52.751  1.00 33.87  ? 322  HIS   D C   1 
ATOM   10348 O  O   . HIS   D  1 21  ? 9.005   -33.592 -52.645  1.00 30.04  ? 322  HIS   D O   1 
ATOM   10349 C  CB  . HIS   D  1 21  ? 7.584   -35.705 -54.355  1.00 28.00  ? 322  HIS   D CB  1 
ATOM   10350 C  CG  . HIS   D  1 21  ? 6.948   -34.799 -55.358  1.00 26.85  ? 322  HIS   D CG  1 
ATOM   10351 N  ND1 . HIS   D  1 21  ? 7.613   -33.733 -55.922  1.00 35.85  ? 322  HIS   D ND1 1 
ATOM   10352 C  CD2 . HIS   D  1 21  ? 5.680   -34.741 -55.825  1.00 28.41  ? 322  HIS   D CD2 1 
ATOM   10353 C  CE1 . HIS   D  1 21  ? 6.793   -33.081 -56.727  1.00 36.79  ? 322  HIS   D CE1 1 
ATOM   10354 N  NE2 . HIS   D  1 21  ? 5.612   -33.672 -56.685  1.00 37.74  ? 322  HIS   D NE2 1 
ATOM   10355 N  N   . LEU   D  1 22  ? 6.885   -32.854 -52.729  1.00 33.64  ? 323  LEU   D N   1 
ATOM   10356 C  CA  . LEU   D  1 22  ? 7.299   -31.478 -52.475  1.00 37.71  ? 323  LEU   D CA  1 
ATOM   10357 C  C   . LEU   D  1 22  ? 7.924   -31.299 -51.097  1.00 40.90  ? 323  LEU   D C   1 
ATOM   10358 O  O   . LEU   D  1 22  ? 8.663   -30.335 -50.892  1.00 49.00  ? 323  LEU   D O   1 
ATOM   10359 C  CB  . LEU   D  1 22  ? 6.112   -30.530 -52.630  1.00 41.90  ? 323  LEU   D CB  1 
ATOM   10360 C  CG  . LEU   D  1 22  ? 5.519   -30.445 -54.037  1.00 48.50  ? 323  LEU   D CG  1 
ATOM   10361 C  CD1 . LEU   D  1 22  ? 4.394   -29.432 -54.057  1.00 53.53  ? 323  LEU   D CD1 1 
ATOM   10362 C  CD2 . LEU   D  1 22  ? 6.579   -30.078 -55.066  1.00 46.61  ? 323  LEU   D CD2 1 
ATOM   10363 N  N   . LYS   D  1 23  ? 7.651   -32.201 -50.156  1.00 34.22  ? 324  LYS   D N   1 
ATOM   10364 C  CA  . LYS   D  1 23  ? 8.255   -32.173 -48.828  1.00 35.81  ? 324  LYS   D CA  1 
ATOM   10365 C  C   . LYS   D  1 23  ? 9.551   -32.960 -48.748  1.00 38.11  ? 324  LYS   D C   1 
ATOM   10366 O  O   . LYS   D  1 23  ? 10.018  -33.243 -47.640  1.00 43.83  ? 324  LYS   D O   1 
ATOM   10367 C  CB  . LYS   D  1 23  ? 7.289   -32.737 -47.782  1.00 29.10  ? 324  LYS   D CB  1 
ATOM   10368 C  CG  . LYS   D  1 23  ? 6.088   -31.876 -47.525  1.00 44.82  ? 324  LYS   D CG  1 
ATOM   10369 C  CD  . LYS   D  1 23  ? 6.476   -30.586 -46.838  1.00 49.72  ? 324  LYS   D CD  1 
ATOM   10370 C  CE  . LYS   D  1 23  ? 5.707   -30.403 -45.539  1.00 55.42  ? 324  LYS   D CE  1 
ATOM   10371 N  NZ  . LYS   D  1 23  ? 5.719   -28.991 -45.067  1.00 56.22  ? 324  LYS   D NZ  1 
ATOM   10372 N  N   . SER   D  1 24  ? 10.122  -33.352 -49.879  1.00 29.02  ? 325  SER   D N   1 
ATOM   10373 C  CA  . SER   D  1 24  ? 11.338  -34.147 -49.848  1.00 35.80  ? 325  SER   D CA  1 
ATOM   10374 C  C   . SER   D  1 24  ? 12.496  -33.314 -49.309  1.00 43.02  ? 325  SER   D C   1 
ATOM   10375 O  O   . SER   D  1 24  ? 12.627  -32.127 -49.617  1.00 42.20  ? 325  SER   D O   1 
ATOM   10376 C  CB  . SER   D  1 24  ? 11.653  -34.676 -51.246  1.00 41.76  ? 325  SER   D CB  1 
ATOM   10377 O  OG  . SER   D  1 24  ? 12.945  -35.247 -51.294  1.00 52.86  ? 325  SER   D OG  1 
ATOM   10378 N  N   . THR   D  1 25  ? 13.340  -33.937 -48.488  1.00 47.44  ? 326  THR   D N   1 
ATOM   10379 C  CA  . THR   D  1 25  ? 14.422  -33.208 -47.837  1.00 55.06  ? 326  THR   D CA  1 
ATOM   10380 C  C   . THR   D  1 25  ? 15.779  -33.485 -48.465  1.00 54.52  ? 326  THR   D C   1 
ATOM   10381 O  O   . THR   D  1 25  ? 16.499  -32.550 -48.832  1.00 65.52  ? 326  THR   D O   1 
ATOM   10382 C  CB  . THR   D  1 25  ? 14.459  -33.545 -46.338  1.00 58.81  ? 326  THR   D CB  1 
ATOM   10383 O  OG1 . THR   D  1 25  ? 13.196  -34.089 -45.941  1.00 54.33  ? 326  THR   D OG1 1 
ATOM   10384 C  CG2 . THR   D  1 25  ? 14.724  -32.287 -45.519  1.00 64.48  ? 326  THR   D CG2 1 
ATOM   10385 N  N   . LEU   D  1 26  ? 16.127  -34.751 -48.630  1.00 40.04  ? 327  LEU   D N   1 
ATOM   10386 C  CA  . LEU   D  1 26  ? 17.474  -35.155 -48.991  1.00 43.62  ? 327  LEU   D CA  1 
ATOM   10387 C  C   . LEU   D  1 26  ? 17.564  -35.563 -50.460  1.00 44.57  ? 327  LEU   D C   1 
ATOM   10388 O  O   . LEU   D  1 26  ? 16.583  -36.002 -51.066  1.00 36.41  ? 327  LEU   D O   1 
ATOM   10389 C  CB  . LEU   D  1 26  ? 17.916  -36.305 -48.085  1.00 49.64  ? 327  LEU   D CB  1 
ATOM   10390 C  CG  . LEU   D  1 26  ? 17.856  -35.874 -46.610  1.00 51.48  ? 327  LEU   D CG  1 
ATOM   10391 C  CD1 . LEU   D  1 26  ? 17.396  -37.003 -45.700  1.00 53.26  ? 327  LEU   D CD1 1 
ATOM   10392 C  CD2 . LEU   D  1 26  ? 19.205  -35.322 -46.160  1.00 45.44  ? 327  LEU   D CD2 1 
ATOM   10393 N  N   . GLU   D  1 27  ? 18.757  -35.390 -51.028  1.00 39.76  ? 328  GLU   D N   1 
ATOM   10394 C  CA  . GLU   D  1 27  ? 19.024  -35.842 -52.387  1.00 35.00  ? 328  GLU   D CA  1 
ATOM   10395 C  C   . GLU   D  1 27  ? 18.841  -37.352 -52.498  1.00 32.92  ? 328  GLU   D C   1 
ATOM   10396 O  O   . GLU   D  1 27  ? 19.206  -38.114 -51.599  1.00 33.26  ? 328  GLU   D O   1 
ATOM   10397 C  CB  . GLU   D  1 27  ? 20.445  -35.440 -52.800  1.00 40.48  ? 328  GLU   D CB  1 
ATOM   10398 C  CG  . GLU   D  1 27  ? 20.639  -33.930 -52.981  1.00 36.22  ? 328  GLU   D CG  1 
ATOM   10399 C  CD  . GLU   D  1 27  ? 22.040  -33.543 -53.443  1.00 42.42  ? 328  GLU   D CD  1 
ATOM   10400 O  OE1 . GLU   D  1 27  ? 22.253  -32.352 -53.760  1.00 45.71  ? 328  GLU   D OE1 1 
ATOM   10401 O  OE2 . GLU   D  1 27  ? 22.932  -34.416 -53.487  1.00 40.65  ? 328  GLU   D OE2 1 
ATOM   10402 N  N   . THR   D  1 28  ? 18.244  -37.789 -53.603  1.00 30.67  ? 329  THR   D N   1 
ATOM   10403 C  CA  . THR   D  1 28  ? 18.150  -39.218 -53.870  1.00 26.53  ? 329  THR   D CA  1 
ATOM   10404 C  C   . THR   D  1 28  ? 19.459  -39.788 -54.377  1.00 23.68  ? 329  THR   D C   1 
ATOM   10405 O  O   . THR   D  1 28  ? 19.672  -40.996 -54.280  1.00 28.09  ? 329  THR   D O   1 
ATOM   10406 C  CB  . THR   D  1 28  ? 17.071  -39.493 -54.914  1.00 37.13  ? 329  THR   D CB  1 
ATOM   10407 O  OG1 . THR   D  1 28  ? 17.431  -38.832 -56.152  1.00 27.15  ? 329  THR   D OG1 1 
ATOM   10408 C  CG2 . THR   D  1 28  ? 15.721  -38.990 -54.413  1.00 29.99  ? 329  THR   D CG2 1 
ATOM   10409 N  N   . GLY   D  1 29  ? 20.332  -38.945 -54.908  1.00 25.76  ? 330  GLY   D N   1 
ATOM   10410 C  CA  . GLY   D  1 29  ? 21.470  -39.374 -55.676  1.00 30.05  ? 330  GLY   D CA  1 
ATOM   10411 C  C   . GLY   D  1 29  ? 21.293  -39.188 -57.169  1.00 38.32  ? 330  GLY   D C   1 
ATOM   10412 O  O   . GLY   D  1 29  ? 22.290  -39.074 -57.891  1.00 35.58  ? 330  GLY   D O   1 
ATOM   10413 N  N   . CYS   D  1 30  ? 20.050  -39.136 -57.641  1.00 35.90  ? 331  CYS   D N   1 
ATOM   10414 C  CA  . CYS   D  1 30  ? 19.788  -38.936 -59.055  1.00 29.87  ? 331  CYS   D CA  1 
ATOM   10415 C  C   . CYS   D  1 30  ? 19.959  -37.474 -59.428  1.00 33.10  ? 331  CYS   D C   1 
ATOM   10416 O  O   . CYS   D  1 30  ? 19.939  -36.582 -58.580  1.00 30.68  ? 331  CYS   D O   1 
ATOM   10417 C  CB  . CYS   D  1 30  ? 18.372  -39.377 -59.413  1.00 25.29  ? 331  CYS   D CB  1 
ATOM   10418 S  SG  . CYS   D  1 30  ? 18.033  -41.084 -59.045  1.00 30.37  ? 331  CYS   D SG  1 
ATOM   10419 N  N   . THR   D  1 31  ? 20.144  -37.242 -60.721  1.00 28.52  ? 332  THR   D N   1 
ATOM   10420 C  CA  . THR   D  1 31  ? 20.041  -35.924 -61.315  1.00 30.02  ? 332  THR   D CA  1 
ATOM   10421 C  C   . THR   D  1 31  ? 19.175  -36.037 -62.559  1.00 30.46  ? 332  THR   D C   1 
ATOM   10422 O  O   . THR   D  1 31  ? 18.762  -37.127 -62.962  1.00 33.51  ? 332  THR   D O   1 
ATOM   10423 C  CB  . THR   D  1 31  ? 21.411  -35.344 -61.697  1.00 34.63  ? 332  THR   D CB  1 
ATOM   10424 O  OG1 . THR   D  1 31  ? 21.922  -36.047 -62.838  1.00 37.34  ? 332  THR   D OG1 1 
ATOM   10425 C  CG2 . THR   D  1 31  ? 22.404  -35.467 -60.562  1.00 33.51  ? 332  THR   D CG2 1 
ATOM   10426 N  N   . GLU   D  1 32  ? 18.905  -34.889 -63.171  1.00 34.09  ? 333  GLU   D N   1 
ATOM   10427 C  CA  . GLU   D  1 32  ? 18.290  -34.866 -64.490  1.00 37.79  ? 333  GLU   D CA  1 
ATOM   10428 C  C   . GLU   D  1 32  ? 19.053  -35.717 -65.497  1.00 35.72  ? 333  GLU   D C   1 
ATOM   10429 O  O   . GLU   D  1 32  ? 18.460  -36.181 -66.473  1.00 37.64  ? 333  GLU   D O   1 
ATOM   10430 C  CB  . GLU   D  1 32  ? 18.198  -33.418 -64.995  1.00 44.39  ? 333  GLU   D CB  1 
ATOM   10431 C  CG  . GLU   D  1 32  ? 17.120  -32.578 -64.320  1.00 65.13  ? 333  GLU   D CG  1 
ATOM   10432 C  CD  . GLU   D  1 32  ? 17.503  -32.091 -62.921  1.00 82.32  ? 333  GLU   D CD  1 
ATOM   10433 O  OE1 . GLU   D  1 32  ? 18.590  -32.457 -62.419  1.00 85.20  ? 333  GLU   D OE1 1 
ATOM   10434 O  OE2 . GLU   D  1 32  ? 16.706  -31.331 -62.323  1.00 88.12  ? 333  GLU   D OE2 1 
ATOM   10435 N  N   . TYR   D  1 33  ? 20.348  -35.948 -65.279  1.00 33.14  ? 334  TYR   D N   1 
ATOM   10436 C  CA  . TYR   D  1 33  ? 21.180  -36.632 -66.257  1.00 33.47  ? 334  TYR   D CA  1 
ATOM   10437 C  C   . TYR   D  1 33  ? 21.576  -38.056 -65.882  1.00 37.10  ? 334  TYR   D C   1 
ATOM   10438 O  O   . TYR   D  1 33  ? 21.980  -38.811 -66.767  1.00 35.59  ? 334  TYR   D O   1 
ATOM   10439 C  CB  . TYR   D  1 33  ? 22.451  -35.821 -66.514  1.00 36.34  ? 334  TYR   D CB  1 
ATOM   10440 C  CG  . TYR   D  1 33  ? 22.154  -34.484 -67.137  1.00 47.01  ? 334  TYR   D CG  1 
ATOM   10441 C  CD1 . TYR   D  1 33  ? 21.995  -34.363 -68.510  1.00 60.89  ? 334  TYR   D CD1 1 
ATOM   10442 C  CD2 . TYR   D  1 33  ? 22.004  -33.348 -66.356  1.00 52.33  ? 334  TYR   D CD2 1 
ATOM   10443 C  CE1 . TYR   D  1 33  ? 21.712  -33.146 -69.087  1.00 67.52  ? 334  TYR   D CE1 1 
ATOM   10444 C  CE2 . TYR   D  1 33  ? 21.718  -32.124 -66.928  1.00 61.98  ? 334  TYR   D CE2 1 
ATOM   10445 C  CZ  . TYR   D  1 33  ? 21.576  -32.031 -68.297  1.00 70.04  ? 334  TYR   D CZ  1 
ATOM   10446 O  OH  . TYR   D  1 33  ? 21.294  -30.823 -68.890  1.00 80.38  ? 334  TYR   D OH  1 
ATOM   10447 N  N   . ILE   D  1 34  ? 21.496  -38.451 -64.617  1.00 29.53  ? 335  ILE   D N   1 
ATOM   10448 C  CA  . ILE   D  1 34  ? 21.913  -39.796 -64.225  1.00 28.90  ? 335  ILE   D CA  1 
ATOM   10449 C  C   . ILE   D  1 34  ? 20.943  -40.312 -63.177  1.00 35.98  ? 335  ILE   D C   1 
ATOM   10450 O  O   . ILE   D  1 34  ? 20.624  -39.600 -62.221  1.00 34.27  ? 335  ILE   D O   1 
ATOM   10451 C  CB  . ILE   D  1 34  ? 23.360  -39.826 -63.690  1.00 42.12  ? 335  ILE   D CB  1 
ATOM   10452 C  CG1 . ILE   D  1 34  ? 24.329  -39.205 -64.701  1.00 58.01  ? 335  ILE   D CG1 1 
ATOM   10453 C  CG2 . ILE   D  1 34  ? 23.798  -41.252 -63.438  1.00 31.91  ? 335  ILE   D CG2 1 
ATOM   10454 C  CD1 . ILE   D  1 34  ? 25.151  -38.036 -64.175  1.00 67.47  ? 335  ILE   D CD1 1 
ATOM   10455 N  N   . CYS   D  1 35  ? 20.457  -41.536 -63.354  1.00 29.39  ? 336  CYS   D N   1 
ATOM   10456 C  CA  . CYS   D  1 35  ? 19.577  -42.144 -62.366  1.00 24.35  ? 336  CYS   D CA  1 
ATOM   10457 C  C   . CYS   D  1 35  ? 20.350  -43.177 -61.560  1.00 26.90  ? 336  CYS   D C   1 
ATOM   10458 O  O   . CYS   D  1 35  ? 21.037  -44.034 -62.128  1.00 24.47  ? 336  CYS   D O   1 
ATOM   10459 C  CB  . CYS   D  1 35  ? 18.353  -42.793 -63.008  1.00 27.48  ? 336  CYS   D CB  1 
ATOM   10460 S  SG  . CYS   D  1 35  ? 17.405  -43.753 -61.802  1.00 28.02  ? 336  CYS   D SG  1 
ATOM   10461 N  N   . MET   D  1 36  ? 20.248  -43.081 -60.234  1.00 21.29  ? 337  MET   D N   1 
ATOM   10462 C  CA  . MET   D  1 36  ? 20.947  -43.983 -59.338  1.00 23.15  ? 337  MET   D CA  1 
ATOM   10463 C  C   . MET   D  1 36  ? 19.997  -44.920 -58.612  1.00 22.62  ? 337  MET   D C   1 
ATOM   10464 O  O   . MET   D  1 36  ? 20.347  -45.453 -57.554  1.00 24.59  ? 337  MET   D O   1 
ATOM   10465 C  CB  . MET   D  1 36  ? 21.774  -43.180 -58.338  1.00 28.94  ? 337  MET   D CB  1 
ATOM   10466 C  CG  . MET   D  1 36  ? 22.814  -42.337 -59.046  1.00 39.18  ? 337  MET   D CG  1 
ATOM   10467 S  SD  . MET   D  1 36  ? 24.229  -42.008 -58.003  1.00 51.51  ? 337  MET   D SD  1 
ATOM   10468 C  CE  . MET   D  1 36  ? 25.160  -40.951 -59.110  1.00 51.39  ? 337  MET   D CE  1 
ATOM   10469 N  N   . GLY   D  1 37  ? 18.810  -45.149 -59.178  1.00 25.77  ? 338  GLY   D N   1 
ATOM   10470 C  CA  . GLY   D  1 37  ? 17.787  -45.971 -58.546  1.00 21.48  ? 338  GLY   D CA  1 
ATOM   10471 C  C   . GLY   D  1 37  ? 18.208  -47.358 -58.084  1.00 25.16  ? 338  GLY   D C   1 
ATOM   10472 O  O   . GLY   D  1 37  ? 17.592  -47.909 -57.164  1.00 24.18  ? 338  GLY   D O   1 
ATOM   10473 N  N   . SER   D  1 38  ? 19.244  -47.948 -58.688  1.00 20.91  ? 339  SER   D N   1 
ATOM   10474 C  CA  . SER   D  1 38  ? 19.678  -49.283 -58.275  1.00 25.25  ? 339  SER   D CA  1 
ATOM   10475 C  C   . SER   D  1 38  ? 20.973  -49.269 -57.471  1.00 29.24  ? 339  SER   D C   1 
ATOM   10476 O  O   . SER   D  1 38  ? 21.529  -50.336 -57.202  1.00 27.06  ? 339  SER   D O   1 
ATOM   10477 C  CB  . SER   D  1 38  ? 19.839  -50.213 -59.483  1.00 21.44  ? 339  SER   D CB  1 
ATOM   10478 O  OG  . SER   D  1 38  ? 20.882  -49.786 -60.347  1.00 27.26  ? 339  SER   D OG  1 
ATOM   10479 N  N   . ILE   D  1 39  ? 21.470  -48.096 -57.095  1.00 27.31  ? 340  ILE   D N   1 
ATOM   10480 C  CA  . ILE   D  1 39  ? 22.608  -47.996 -56.189  1.00 25.64  ? 340  ILE   D CA  1 
ATOM   10481 C  C   . ILE   D  1 39  ? 22.117  -48.245 -54.766  1.00 24.88  ? 340  ILE   D C   1 
ATOM   10482 O  O   . ILE   D  1 39  ? 21.107  -47.674 -54.340  1.00 25.38  ? 340  ILE   D O   1 
ATOM   10483 C  CB  . ILE   D  1 39  ? 23.275  -46.618 -56.312  1.00 33.77  ? 340  ILE   D CB  1 
ATOM   10484 C  CG1 . ILE   D  1 39  ? 23.612  -46.308 -57.772  1.00 38.15  ? 340  ILE   D CG1 1 
ATOM   10485 C  CG2 . ILE   D  1 39  ? 24.502  -46.525 -55.408  1.00 31.02  ? 340  ILE   D CG2 1 
ATOM   10486 C  CD1 . ILE   D  1 39  ? 24.713  -47.162 -58.342  1.00 35.69  ? 340  ILE   D CD1 1 
ATOM   10487 N  N   . MET   D  1 40  ? 22.820  -49.110 -54.032  1.00 24.99  ? 341  MET   D N   1 
ATOM   10488 C  CA  . MET   D  1 40  ? 22.403  -49.452 -52.674  1.00 30.72  ? 341  MET   D CA  1 
ATOM   10489 C  C   . MET   D  1 40  ? 22.366  -48.226 -51.770  1.00 32.16  ? 341  MET   D C   1 
ATOM   10490 O  O   . MET   D  1 40  ? 21.388  -48.005 -51.040  1.00 27.46  ? 341  MET   D O   1 
ATOM   10491 C  CB  . MET   D  1 40  ? 23.351  -50.500 -52.094  1.00 41.51  ? 341  MET   D CB  1 
ATOM   10492 C  CG  . MET   D  1 40  ? 22.926  -51.056 -50.741  1.00 57.30  ? 341  MET   D CG  1 
ATOM   10493 S  SD  . MET   D  1 40  ? 21.733  -52.397 -50.880  1.00 60.02  ? 341  MET   D SD  1 
ATOM   10494 C  CE  . MET   D  1 40  ? 22.620  -53.543 -51.951  1.00 45.82  ? 341  MET   D CE  1 
ATOM   10495 N  N   . HIS   D  1 41  ? 23.444  -47.436 -51.773  1.00 32.33  ? 342  HIS   D N   1 
ATOM   10496 C  CA  A HIS   D  1 41  ? 23.559  -46.217 -50.973  0.46 38.57  ? 342  HIS   D CA  1 
ATOM   10497 C  CA  B HIS   D  1 41  ? 23.561  -46.214 -50.967  0.54 38.68  ? 342  HIS   D CA  1 
ATOM   10498 C  C   . HIS   D  1 41  ? 23.905  -45.077 -51.927  1.00 34.79  ? 342  HIS   D C   1 
ATOM   10499 O  O   . HIS   D  1 41  ? 25.073  -44.688 -52.061  1.00 32.33  ? 342  HIS   D O   1 
ATOM   10500 C  CB  A HIS   D  1 41  ? 24.622  -46.342 -49.880  0.46 41.32  ? 342  HIS   D CB  1 
ATOM   10501 C  CB  B HIS   D  1 41  ? 24.615  -46.392 -49.870  0.54 41.24  ? 342  HIS   D CB  1 
ATOM   10502 C  CG  A HIS   D  1 41  ? 24.736  -47.715 -49.287  0.46 40.72  ? 342  HIS   D CG  1 
ATOM   10503 C  CG  B HIS   D  1 41  ? 24.497  -45.428 -48.722  0.54 43.06  ? 342  HIS   D CG  1 
ATOM   10504 N  ND1 A HIS   D  1 41  ? 23.967  -48.139 -48.224  0.46 48.20  ? 342  HIS   D ND1 1 
ATOM   10505 N  ND1 B HIS   D  1 41  ? 23.315  -44.811 -48.371  0.54 42.49  ? 342  HIS   D ND1 1 
ATOM   10506 C  CD2 A HIS   D  1 41  ? 25.569  -48.743 -49.577  0.46 45.58  ? 342  HIS   D CD2 1 
ATOM   10507 C  CD2 B HIS   D  1 41  ? 25.426  -44.981 -47.844  0.54 44.03  ? 342  HIS   D CD2 1 
ATOM   10508 C  CE1 A HIS   D  1 41  ? 24.308  -49.373 -47.899  0.46 45.76  ? 342  HIS   D CE1 1 
ATOM   10509 C  CE1 B HIS   D  1 41  ? 23.523  -44.021 -47.332  0.54 40.06  ? 342  HIS   D CE1 1 
ATOM   10510 N  NE2 A HIS   D  1 41  ? 25.278  -49.762 -48.704  0.46 42.40  ? 342  HIS   D NE2 1 
ATOM   10511 N  NE2 B HIS   D  1 41  ? 24.793  -44.115 -46.986  0.54 42.37  ? 342  HIS   D NE2 1 
ATOM   10512 N  N   . PRO   D  1 42  ? 22.915  -44.514 -52.622  1.00 36.43  ? 343  PRO   D N   1 
ATOM   10513 C  CA  . PRO   D  1 42  ? 23.257  -43.543 -53.667  1.00 38.78  ? 343  PRO   D CA  1 
ATOM   10514 C  C   . PRO   D  1 42  ? 23.715  -42.203 -53.131  1.00 45.07  ? 343  PRO   D C   1 
ATOM   10515 O  O   . PRO   D  1 42  ? 24.451  -41.491 -53.836  1.00 40.37  ? 343  PRO   D O   1 
ATOM   10516 C  CB  . PRO   D  1 42  ? 21.958  -43.419 -54.471  1.00 36.80  ? 343  PRO   D CB  1 
ATOM   10517 C  CG  . PRO   D  1 42  ? 20.890  -43.749 -53.488  1.00 36.30  ? 343  PRO   D CG  1 
ATOM   10518 C  CD  . PRO   D  1 42  ? 21.461  -44.776 -52.547  1.00 43.00  ? 343  PRO   D CD  1 
ATOM   10519 N  N   . SER   D  1 43  ? 23.331  -41.825 -51.916  1.00 42.26  ? 344  SER   D N   1 
ATOM   10520 C  CA  . SER   D  1 43  ? 23.550  -40.469 -51.439  1.00 44.62  ? 344  SER   D CA  1 
ATOM   10521 C  C   . SER   D  1 43  ? 24.158  -40.482 -50.042  1.00 41.84  ? 344  SER   D C   1 
ATOM   10522 O  O   . SER   D  1 43  ? 23.781  -41.292 -49.190  1.00 35.77  ? 344  SER   D O   1 
ATOM   10523 C  CB  . SER   D  1 43  ? 22.231  -39.674 -51.444  1.00 40.48  ? 344  SER   D CB  1 
ATOM   10524 O  OG  . SER   D  1 43  ? 22.438  -38.345 -50.992  1.00 44.27  ? 344  SER   D OG  1 
ATOM   10525 N  N   . GLN   D  1 44  ? 25.108  -39.581 -49.820  1.00 40.65  ? 345  GLN   D N   1 
ATOM   10526 C  CA  . GLN   D  1 44  ? 25.617  -39.308 -48.488  1.00 50.84  ? 345  GLN   D CA  1 
ATOM   10527 C  C   . GLN   D  1 44  ? 25.039  -38.023 -47.915  1.00 53.97  ? 345  GLN   D C   1 
ATOM   10528 O  O   . GLN   D  1 44  ? 25.534  -37.530 -46.893  1.00 51.18  ? 345  GLN   D O   1 
ATOM   10529 C  CB  . GLN   D  1 44  ? 27.144  -39.241 -48.508  1.00 54.07  ? 345  GLN   D CB  1 
ATOM   10530 C  CG  . GLN   D  1 44  ? 27.792  -40.485 -49.077  1.00 59.54  ? 345  GLN   D CG  1 
ATOM   10531 C  CD  . GLN   D  1 44  ? 29.281  -40.324 -49.276  1.00 62.60  ? 345  GLN   D CD  1 
ATOM   10532 O  OE1 . GLN   D  1 44  ? 29.745  -40.020 -50.378  1.00 66.93  ? 345  GLN   D OE1 1 
ATOM   10533 N  NE2 . GLN   D  1 44  ? 30.043  -40.529 -48.210  1.00 63.77  ? 345  GLN   D NE2 1 
ATOM   10534 N  N   . HIS   D  1 45  ? 24.005  -37.472 -48.555  1.00 50.47  ? 346  HIS   D N   1 
ATOM   10535 C  CA  . HIS   D  1 45  ? 23.364  -36.247 -48.097  1.00 50.48  ? 346  HIS   D CA  1 
ATOM   10536 C  C   . HIS   D  1 45  ? 22.723  -36.481 -46.740  1.00 49.24  ? 346  HIS   D C   1 
ATOM   10537 O  O   . HIS   D  1 45  ? 21.727  -37.203 -46.644  1.00 53.42  ? 346  HIS   D O   1 
ATOM   10538 C  CB  . HIS   D  1 45  ? 22.311  -35.770 -49.101  1.00 45.56  ? 346  HIS   D CB  1 
ATOM   10539 C  CG  . HIS   D  1 45  ? 21.853  -34.362 -48.880  1.00 48.35  ? 346  HIS   D CG  1 
ATOM   10540 N  ND1 . HIS   D  1 45  ? 20.697  -33.859 -49.440  1.00 48.55  ? 346  HIS   D ND1 1 
ATOM   10541 C  CD2 . HIS   D  1 45  ? 22.399  -33.346 -48.170  1.00 49.02  ? 346  HIS   D CD2 1 
ATOM   10542 C  CE1 . HIS   D  1 45  ? 20.551  -32.594 -49.083  1.00 51.46  ? 346  HIS   D CE1 1 
ATOM   10543 N  NE2 . HIS   D  1 45  ? 21.569  -32.259 -48.311  1.00 47.67  ? 346  HIS   D NE2 1 
ATOM   10544 N  N   . ALA   D  1 46  ? 23.296  -35.896 -45.693  1.00 56.13  ? 347  ALA   D N   1 
ATOM   10545 C  CA  . ALA   D  1 46  ? 22.759  -35.959 -44.342  1.00 51.81  ? 347  ALA   D CA  1 
ATOM   10546 C  C   . ALA   D  1 46  ? 22.175  -34.605 -43.964  1.00 51.41  ? 347  ALA   D C   1 
ATOM   10547 O  O   . ALA   D  1 46  ? 22.527  -33.569 -44.531  1.00 48.55  ? 347  ALA   D O   1 
ATOM   10548 C  CB  . ALA   D  1 46  ? 23.836  -36.375 -43.334  1.00 48.74  ? 347  ALA   D CB  1 
ATOM   10549 N  N   . ARG   D  1 47  ? 21.269  -34.617 -42.988  1.00 56.55  ? 348  ARG   D N   1 
ATOM   10550 C  CA  . ARG   D  1 47  ? 20.582  -33.376 -42.652  1.00 58.71  ? 348  ARG   D CA  1 
ATOM   10551 C  C   . ARG   D  1 47  ? 21.414  -32.478 -41.734  1.00 55.54  ? 348  ARG   D C   1 
ATOM   10552 O  O   . ARG   D  1 47  ? 21.257  -31.252 -41.774  1.00 55.64  ? 348  ARG   D O   1 
ATOM   10553 C  CB  . ARG   D  1 47  ? 19.214  -33.697 -42.046  1.00 56.68  ? 348  ARG   D CB  1 
ATOM   10554 C  CG  . ARG   D  1 47  ? 18.101  -33.697 -43.083  1.00 57.12  ? 348  ARG   D CG  1 
ATOM   10555 C  CD  . ARG   D  1 47  ? 16.985  -34.659 -42.733  1.00 61.57  ? 348  ARG   D CD  1 
ATOM   10556 N  NE  . ARG   D  1 47  ? 16.419  -34.392 -41.419  1.00 69.32  ? 348  ARG   D NE  1 
ATOM   10557 C  CZ  . ARG   D  1 47  ? 15.603  -33.377 -41.153  1.00 68.69  ? 348  ARG   D CZ  1 
ATOM   10558 N  NH1 . ARG   D  1 47  ? 15.266  -32.527 -42.121  1.00 69.68  ? 348  ARG   D NH1 1 
ATOM   10559 N  NH2 . ARG   D  1 47  ? 15.128  -33.211 -39.920  1.00 51.60  ? 348  ARG   D NH2 1 
ATOM   10560 N  N   . ARG   D  1 48  ? 22.317  -33.052 -40.941  1.00 54.62  ? 349  ARG   D N   1 
ATOM   10561 C  CA  . ARG   D  1 48  ? 23.206  -32.324 -40.046  1.00 60.48  ? 349  ARG   D CA  1 
ATOM   10562 C  C   . ARG   D  1 48  ? 24.625  -32.852 -40.200  1.00 60.69  ? 349  ARG   D C   1 
ATOM   10563 O  O   . ARG   D  1 48  ? 24.822  -34.014 -40.566  1.00 63.23  ? 349  ARG   D O   1 
ATOM   10564 C  CB  . ARG   D  1 48  ? 22.746  -32.442 -38.575  1.00 56.57  ? 349  ARG   D CB  1 
ATOM   10565 C  CG  . ARG   D  1 48  ? 22.551  -33.866 -38.059  1.00 51.10  ? 349  ARG   D CG  1 
ATOM   10566 C  CD  . ARG   D  1 48  ? 23.715  -34.285 -37.184  1.00 59.73  ? 349  ARG   D CD  1 
ATOM   10567 N  NE  . ARG   D  1 48  ? 23.526  -33.910 -35.785  1.00 67.39  ? 349  ARG   D NE  1 
ATOM   10568 C  CZ  . ARG   D  1 48  ? 24.521  -33.777 -34.915  1.00 84.72  ? 349  ARG   D CZ  1 
ATOM   10569 N  NH1 . ARG   D  1 48  ? 25.771  -33.971 -35.309  1.00 92.31  ? 349  ARG   D NH1 1 
ATOM   10570 N  NH2 . ARG   D  1 48  ? 24.270  -33.444 -33.654  1.00 88.11  ? 349  ARG   D NH2 1 
ATOM   10571 N  N   . PRO   D  1 49  ? 25.635  -32.025 -39.920  1.00 65.47  ? 350  PRO   D N   1 
ATOM   10572 C  CA  . PRO   D  1 49  ? 27.014  -32.397 -40.273  1.00 72.19  ? 350  PRO   D CA  1 
ATOM   10573 C  C   . PRO   D  1 49  ? 27.624  -33.492 -39.410  1.00 89.51  ? 350  PRO   D C   1 
ATOM   10574 O  O   . PRO   D  1 49  ? 26.962  -34.081 -38.550  1.00 82.20  ? 350  PRO   D O   1 
ATOM   10575 C  CB  . PRO   D  1 49  ? 27.790  -31.082 -40.098  1.00 62.15  ? 350  PRO   D CB  1 
ATOM   10576 C  CG  . PRO   D  1 49  ? 26.756  -30.018 -39.934  1.00 63.38  ? 350  PRO   D CG  1 
ATOM   10577 C  CD  . PRO   D  1 49  ? 25.564  -30.672 -39.351  1.00 67.46  ? 350  PRO   D CD  1 
ATOM   10578 N  N   . GLU   D  1 50  ? 28.917  -33.737 -39.648  1.00 113.85 ? 351  GLU   D N   1 
ATOM   10579 C  CA  . GLU   D  1 50  ? 29.727  -34.770 -39.006  1.00 114.19 ? 351  GLU   D CA  1 
ATOM   10580 C  C   . GLU   D  1 50  ? 29.458  -34.932 -37.516  1.00 104.58 ? 351  GLU   D C   1 
ATOM   10581 O  O   . GLU   D  1 50  ? 28.858  -35.924 -37.090  1.00 103.88 ? 351  GLU   D O   1 
ATOM   10582 C  CB  . GLU   D  1 50  ? 31.220  -34.465 -39.195  1.00 124.57 ? 351  GLU   D CB  1 
ATOM   10583 C  CG  . GLU   D  1 50  ? 31.687  -34.300 -40.632  1.00 128.22 ? 351  GLU   D CG  1 
ATOM   10584 C  CD  . GLU   D  1 50  ? 32.507  -35.480 -41.122  1.00 127.90 ? 351  GLU   D CD  1 
ATOM   10585 O  OE1 . GLU   D  1 50  ? 33.017  -36.242 -40.271  1.00 126.85 ? 351  GLU   D OE1 1 
ATOM   10586 O  OE2 . GLU   D  1 50  ? 32.641  -35.647 -42.355  1.00 127.69 ? 351  GLU   D OE2 1 
ATOM   10587 N  N   . ASP   D  1 51  ? 29.917  -33.975 -36.722  1.00 97.33  ? 352  ASP   D N   1 
ATOM   10588 C  CA  . ASP   D  1 51  ? 29.938  -34.109 -35.279  1.00 96.53  ? 352  ASP   D CA  1 
ATOM   10589 C  C   . ASP   D  1 51  ? 28.792  -33.317 -34.655  1.00 93.45  ? 352  ASP   D C   1 
ATOM   10590 O  O   . ASP   D  1 51  ? 27.798  -33.013 -35.322  1.00 97.53  ? 352  ASP   D O   1 
ATOM   10591 C  CB  . ASP   D  1 51  ? 31.299  -33.655 -34.748  1.00 102.65 ? 352  ASP   D CB  1 
ATOM   10592 C  CG  . ASP   D  1 51  ? 32.222  -34.813 -34.476  1.00 106.05 ? 352  ASP   D CG  1 
ATOM   10593 O  OD1 . ASP   D  1 51  ? 33.403  -34.734 -34.873  1.00 109.36 ? 352  ASP   D OD1 1 
ATOM   10594 O  OD2 . ASP   D  1 51  ? 31.757  -35.810 -33.881  1.00 102.98 ? 352  ASP   D OD2 1 
ATOM   10595 N  N   . VAL   D  1 52  ? 28.933  -32.981 -33.373  1.00 85.34  ? 353  VAL   D N   1 
ATOM   10596 C  CA  . VAL   D  1 52  ? 27.950  -32.181 -32.648  1.00 75.60  ? 353  VAL   D CA  1 
ATOM   10597 C  C   . VAL   D  1 52  ? 27.689  -30.894 -33.420  1.00 72.71  ? 353  VAL   D C   1 
ATOM   10598 O  O   . VAL   D  1 52  ? 28.585  -30.058 -33.600  1.00 66.16  ? 353  VAL   D O   1 
ATOM   10599 C  CB  . VAL   D  1 52  ? 28.411  -31.899 -31.206  1.00 63.05  ? 353  VAL   D CB  1 
ATOM   10600 C  CG1 . VAL   D  1 52  ? 29.913  -31.725 -31.153  1.00 61.98  ? 353  VAL   D CG1 1 
ATOM   10601 C  CG2 . VAL   D  1 52  ? 27.700  -30.672 -30.637  1.00 60.87  ? 353  VAL   D CG2 1 
ATOM   10602 N  N   . ALA   D  1 53  ? 26.459  -30.751 -33.905  1.00 68.24  ? 354  ALA   D N   1 
ATOM   10603 C  CA  . ALA   D  1 53  ? 26.096  -29.606 -34.715  1.00 58.93  ? 354  ALA   D CA  1 
ATOM   10604 C  C   . ALA   D  1 53  ? 26.133  -28.332 -33.883  1.00 55.40  ? 354  ALA   D C   1 
ATOM   10605 O  O   . ALA   D  1 53  ? 25.891  -28.341 -32.669  1.00 48.21  ? 354  ALA   D O   1 
ATOM   10606 C  CB  . ALA   D  1 53  ? 24.702  -29.803 -35.317  1.00 55.83  ? 354  ALA   D CB  1 
ATOM   10607 N  N   . THR   D  1 54  ? 26.477  -27.230 -34.545  1.00 53.99  ? 355  THR   D N   1 
ATOM   10608 C  CA  . THR   D  1 54  ? 26.220  -25.922 -33.974  1.00 53.47  ? 355  THR   D CA  1 
ATOM   10609 C  C   . THR   D  1 54  ? 24.715  -25.698 -33.873  1.00 48.17  ? 355  THR   D C   1 
ATOM   10610 O  O   . THR   D  1 54  ? 23.905  -26.436 -34.447  1.00 39.38  ? 355  THR   D O   1 
ATOM   10611 C  CB  . THR   D  1 54  ? 26.843  -24.824 -34.829  1.00 50.97  ? 355  THR   D CB  1 
ATOM   10612 O  OG1 . THR   D  1 54  ? 26.418  -25.004 -36.182  1.00 46.82  ? 355  THR   D OG1 1 
ATOM   10613 C  CG2 . THR   D  1 54  ? 28.340  -24.892 -34.767  1.00 41.79  ? 355  THR   D CG2 1 
ATOM   10614 N  N   . LYS   D  1 55  ? 24.344  -24.641 -33.151  1.00 44.80  ? 356  LYS   D N   1 
ATOM   10615 C  CA  . LYS   D  1 55  ? 22.929  -24.342 -32.961  1.00 44.04  ? 356  LYS   D CA  1 
ATOM   10616 C  C   . LYS   D  1 55  ? 22.222  -24.103 -34.293  1.00 36.21  ? 356  LYS   D C   1 
ATOM   10617 O  O   . LYS   D  1 55  ? 21.133  -24.637 -34.529  1.00 36.87  ? 356  LYS   D O   1 
ATOM   10618 C  CB  . LYS   D  1 55  ? 22.768  -23.134 -32.050  1.00 52.71  ? 356  LYS   D CB  1 
ATOM   10619 C  CG  . LYS   D  1 55  ? 21.337  -22.733 -31.881  1.00 55.68  ? 356  LYS   D CG  1 
ATOM   10620 C  CD  . LYS   D  1 55  ? 21.183  -21.803 -30.720  1.00 63.67  ? 356  LYS   D CD  1 
ATOM   10621 C  CE  . LYS   D  1 55  ? 19.727  -21.684 -30.377  1.00 64.50  ? 356  LYS   D CE  1 
ATOM   10622 N  NZ  . LYS   D  1 55  ? 19.508  -20.541 -29.463  1.00 65.49  ? 356  LYS   D NZ  1 
ATOM   10623 N  N   . ASP   D  1 56  ? 22.824  -23.298 -35.174  1.00 38.56  ? 357  ASP   D N   1 
ATOM   10624 C  CA  . ASP   D  1 56  ? 22.182  -22.970 -36.444  1.00 44.97  ? 357  ASP   D CA  1 
ATOM   10625 C  C   . ASP   D  1 56  ? 22.113  -24.161 -37.389  1.00 44.58  ? 357  ASP   D C   1 
ATOM   10626 O  O   . ASP   D  1 56  ? 21.449  -24.071 -38.428  1.00 42.43  ? 357  ASP   D O   1 
ATOM   10627 C  CB  . ASP   D  1 56  ? 22.891  -21.788 -37.127  1.00 51.01  ? 357  ASP   D CB  1 
ATOM   10628 C  CG  . ASP   D  1 56  ? 24.368  -22.045 -37.399  1.00 63.64  ? 357  ASP   D CG  1 
ATOM   10629 O  OD1 . ASP   D  1 56  ? 25.034  -21.142 -37.952  1.00 69.06  ? 357  ASP   D OD1 1 
ATOM   10630 O  OD2 . ASP   D  1 56  ? 24.866  -23.144 -37.081  1.00 72.36  ? 357  ASP   D OD2 1 
ATOM   10631 N  N   . GLN   D  1 57  ? 22.775  -25.267 -37.057  1.00 36.01  ? 358  GLN   D N   1 
ATOM   10632 C  CA  . GLN   D  1 57  ? 22.635  -26.489 -37.828  1.00 39.19  ? 358  GLN   D CA  1 
ATOM   10633 C  C   . GLN   D  1 57  ? 21.550  -27.390 -37.265  1.00 42.60  ? 358  GLN   D C   1 
ATOM   10634 O  O   . GLN   D  1 57  ? 20.770  -27.977 -38.022  1.00 39.34  ? 358  GLN   D O   1 
ATOM   10635 C  CB  . GLN   D  1 57  ? 23.969  -27.235 -37.866  1.00 47.70  ? 358  GLN   D CB  1 
ATOM   10636 C  CG  . GLN   D  1 57  ? 25.039  -26.510 -38.665  1.00 53.55  ? 358  GLN   D CG  1 
ATOM   10637 C  CD  . GLN   D  1 57  ? 26.429  -27.023 -38.370  1.00 57.17  ? 358  GLN   D CD  1 
ATOM   10638 O  OE1 . GLN   D  1 57  ? 26.645  -27.763 -37.402  1.00 57.82  ? 358  GLN   D OE1 1 
ATOM   10639 N  NE2 . GLN   D  1 57  ? 27.385  -26.630 -39.199  1.00 59.54  ? 358  GLN   D NE2 1 
ATOM   10640 N  N   . LEU   D  1 58  ? 21.478  -27.510 -35.944  1.00 39.33  ? 359  LEU   D N   1 
ATOM   10641 C  CA  . LEU   D  1 58  ? 20.523  -28.442 -35.364  1.00 35.11  ? 359  LEU   D CA  1 
ATOM   10642 C  C   . LEU   D  1 58  ? 19.144  -27.812 -35.213  1.00 32.23  ? 359  LEU   D C   1 
ATOM   10643 O  O   . LEU   D  1 58  ? 18.134  -28.460 -35.506  1.00 31.73  ? 359  LEU   D O   1 
ATOM   10644 C  CB  . LEU   D  1 58  ? 21.034  -28.945 -34.013  1.00 36.23  ? 359  LEU   D CB  1 
ATOM   10645 C  CG  . LEU   D  1 58  ? 20.149  -29.997 -33.341  1.00 38.78  ? 359  LEU   D CG  1 
ATOM   10646 C  CD1 . LEU   D  1 58  ? 19.938  -31.193 -34.278  1.00 36.30  ? 359  LEU   D CD1 1 
ATOM   10647 C  CD2 . LEU   D  1 58  ? 20.714  -30.440 -31.974  1.00 37.63  ? 359  LEU   D CD2 1 
ATOM   10648 N  N   . PHE   D  1 59  ? 19.073  -26.562 -34.756  1.00 36.61  ? 360  PHE   D N   1 
ATOM   10649 C  CA  . PHE   D  1 59  ? 17.758  -25.994 -34.465  1.00 38.64  ? 360  PHE   D CA  1 
ATOM   10650 C  C   . PHE   D  1 59  ? 16.819  -25.996 -35.666  1.00 31.53  ? 360  PHE   D C   1 
ATOM   10651 O  O   . PHE   D  1 59  ? 15.643  -26.361 -35.493  1.00 33.48  ? 360  PHE   D O   1 
ATOM   10652 C  CB  . PHE   D  1 59  ? 17.867  -24.580 -33.888  1.00 36.92  ? 360  PHE   D CB  1 
ATOM   10653 C  CG  . PHE   D  1 59  ? 16.526  -24.015 -33.526  1.00 42.41  ? 360  PHE   D CG  1 
ATOM   10654 C  CD1 . PHE   D  1 59  ? 15.881  -24.435 -32.365  1.00 42.21  ? 360  PHE   D CD1 1 
ATOM   10655 C  CD2 . PHE   D  1 59  ? 15.865  -23.148 -34.383  1.00 39.76  ? 360  PHE   D CD2 1 
ATOM   10656 C  CE1 . PHE   D  1 59  ? 14.630  -23.958 -32.042  1.00 44.05  ? 360  PHE   D CE1 1 
ATOM   10657 C  CE2 . PHE   D  1 59  ? 14.615  -22.669 -34.069  1.00 45.90  ? 360  PHE   D CE2 1 
ATOM   10658 C  CZ  . PHE   D  1 59  ? 13.995  -23.074 -32.890  1.00 52.21  ? 360  PHE   D CZ  1 
ATOM   10659 N  N   . PRO   D  1 60  ? 17.235  -25.609 -36.880  1.00 37.37  ? 361  PRO   D N   1 
ATOM   10660 C  CA  . PRO   D  1 60  ? 16.272  -25.646 -37.999  1.00 34.01  ? 361  PRO   D CA  1 
ATOM   10661 C  C   . PRO   D  1 60  ? 15.690  -27.026 -38.240  1.00 34.48  ? 361  PRO   D C   1 
ATOM   10662 O  O   . PRO   D  1 60  ? 14.507  -27.146 -38.590  1.00 33.65  ? 361  PRO   D O   1 
ATOM   10663 C  CB  . PRO   D  1 60  ? 17.098  -25.151 -39.193  1.00 35.80  ? 361  PRO   D CB  1 
ATOM   10664 C  CG  . PRO   D  1 60  ? 18.162  -24.298 -38.572  1.00 44.12  ? 361  PRO   D CG  1 
ATOM   10665 C  CD  . PRO   D  1 60  ? 18.512  -24.989 -37.281  1.00 36.89  ? 361  PRO   D CD  1 
ATOM   10666 N  N   . LEU   D  1 61  ? 16.486  -28.080 -38.044  1.00 36.55  ? 362  LEU   D N   1 
ATOM   10667 C  CA  . LEU   D  1 61  ? 15.969  -29.439 -38.190  1.00 34.45  ? 362  LEU   D CA  1 
ATOM   10668 C  C   . LEU   D  1 61  ? 14.991  -29.767 -37.079  1.00 38.76  ? 362  LEU   D C   1 
ATOM   10669 O  O   . LEU   D  1 61  ? 13.962  -30.410 -37.315  1.00 34.96  ? 362  LEU   D O   1 
ATOM   10670 C  CB  . LEU   D  1 61  ? 17.116  -30.444 -38.179  1.00 31.94  ? 362  LEU   D CB  1 
ATOM   10671 C  CG  . LEU   D  1 61  ? 18.227  -30.103 -39.174  1.00 39.97  ? 362  LEU   D CG  1 
ATOM   10672 C  CD1 . LEU   D  1 61  ? 19.411  -31.028 -38.984  1.00 30.86  ? 362  LEU   D CD1 1 
ATOM   10673 C  CD2 . LEU   D  1 61  ? 17.698  -30.189 -40.593  1.00 41.60  ? 362  LEU   D CD2 1 
ATOM   10674 N  N   . ALA   D  1 62  ? 15.302  -29.335 -35.855  1.00 37.58  ? 363  ALA   D N   1 
ATOM   10675 C  CA  . ALA   D  1 62  ? 14.400  -29.586 -34.738  1.00 39.98  ? 363  ALA   D CA  1 
ATOM   10676 C  C   . ALA   D  1 62  ? 13.082  -28.859 -34.951  1.00 39.89  ? 363  ALA   D C   1 
ATOM   10677 O  O   . ALA   D  1 62  ? 12.003  -29.447 -34.806  1.00 32.70  ? 363  ALA   D O   1 
ATOM   10678 C  CB  . ALA   D  1 62  ? 15.055  -29.154 -33.427  1.00 36.43  ? 363  ALA   D CB  1 
ATOM   10679 N  N   . LYS   D  1 63  ? 13.159  -27.582 -35.334  1.00 35.33  ? 364  LYS   D N   1 
ATOM   10680 C  CA  . LYS   D  1 63  ? 11.951  -26.796 -35.554  1.00 37.83  ? 364  LYS   D CA  1 
ATOM   10681 C  C   . LYS   D  1 63  ? 11.078  -27.434 -36.625  1.00 38.29  ? 364  LYS   D C   1 
ATOM   10682 O  O   . LYS   D  1 63  ? 9.857   -27.542 -36.462  1.00 35.75  ? 364  LYS   D O   1 
ATOM   10683 C  CB  . LYS   D  1 63  ? 12.321  -25.363 -35.931  1.00 38.76  ? 364  LYS   D CB  1 
ATOM   10684 C  CG  . LYS   D  1 63  ? 11.108  -24.486 -36.174  1.00 49.16  ? 364  LYS   D CG  1 
ATOM   10685 C  CD  . LYS   D  1 63  ? 11.492  -23.036 -36.364  1.00 54.07  ? 364  LYS   D CD  1 
ATOM   10686 C  CE  . LYS   D  1 63  ? 10.267  -22.193 -36.669  1.00 52.99  ? 364  LYS   D CE  1 
ATOM   10687 N  NZ  . LYS   D  1 63  ? 9.529   -22.716 -37.849  1.00 44.39  ? 364  LYS   D NZ  1 
ATOM   10688 N  N   . GLU   D  1 64  ? 11.701  -27.899 -37.712  1.00 33.25  ? 365  GLU   D N   1 
ATOM   10689 C  CA  . GLU   D  1 64  ? 10.975  -28.584 -38.775  1.00 42.81  ? 365  GLU   D CA  1 
ATOM   10690 C  C   . GLU   D  1 64  ? 10.232  -29.805 -38.242  1.00 40.65  ? 365  GLU   D C   1 
ATOM   10691 O  O   . GLU   D  1 64  ? 9.048   -30.013 -38.537  1.00 35.69  ? 365  GLU   D O   1 
ATOM   10692 C  CB  . GLU   D  1 64  ? 11.954  -28.978 -39.888  1.00 45.30  ? 365  GLU   D CB  1 
ATOM   10693 C  CG  . GLU   D  1 64  ? 11.460  -30.047 -40.848  1.00 65.19  ? 365  GLU   D CG  1 
ATOM   10694 C  CD  . GLU   D  1 64  ? 12.578  -30.572 -41.742  1.00 88.24  ? 365  GLU   D CD  1 
ATOM   10695 O  OE1 . GLU   D  1 64  ? 12.420  -30.554 -42.984  1.00 94.24  ? 365  GLU   D OE1 1 
ATOM   10696 O  OE2 . GLU   D  1 64  ? 13.625  -30.990 -41.200  1.00 94.78  ? 365  GLU   D OE2 1 
ATOM   10697 N  N   . PHE   D  1 65  ? 10.918  -30.639 -37.462  1.00 27.91  ? 366  PHE   D N   1 
ATOM   10698 C  CA  . PHE   D  1 65  ? 10.247  -31.810 -36.918  1.00 31.91  ? 366  PHE   D CA  1 
ATOM   10699 C  C   . PHE   D  1 65  ? 9.129   -31.417 -35.968  1.00 30.91  ? 366  PHE   D C   1 
ATOM   10700 O  O   . PHE   D  1 65  ? 8.024   -31.968 -36.031  1.00 28.85  ? 366  PHE   D O   1 
ATOM   10701 C  CB  . PHE   D  1 65  ? 11.224  -32.715 -36.187  1.00 34.38  ? 366  PHE   D CB  1 
ATOM   10702 C  CG  . PHE   D  1 65  ? 10.539  -33.803 -35.453  1.00 37.23  ? 366  PHE   D CG  1 
ATOM   10703 C  CD1 . PHE   D  1 65  ? 9.900   -34.820 -36.156  1.00 33.93  ? 366  PHE   D CD1 1 
ATOM   10704 C  CD2 . PHE   D  1 65  ? 10.470  -33.793 -34.071  1.00 31.39  ? 366  PHE   D CD2 1 
ATOM   10705 C  CE1 . PHE   D  1 65  ? 9.233   -35.829 -35.488  1.00 34.01  ? 366  PHE   D CE1 1 
ATOM   10706 C  CE2 . PHE   D  1 65  ? 9.812   -34.806 -33.394  1.00 36.29  ? 366  PHE   D CE2 1 
ATOM   10707 C  CZ  . PHE   D  1 65  ? 9.190   -35.823 -34.097  1.00 34.03  ? 366  PHE   D CZ  1 
ATOM   10708 N  N   . ILE   D  1 66  ? 9.407   -30.490 -35.053  1.00 32.40  ? 367  ILE   D N   1 
ATOM   10709 C  CA  . ILE   D  1 66  ? 8.379   -30.102 -34.092  1.00 38.12  ? 367  ILE   D CA  1 
ATOM   10710 C  C   . ILE   D  1 66  ? 7.207   -29.469 -34.825  1.00 37.17  ? 367  ILE   D C   1 
ATOM   10711 O  O   . ILE   D  1 66  ? 6.044   -29.815 -34.579  1.00 32.46  ? 367  ILE   D O   1 
ATOM   10712 C  CB  . ILE   D  1 66  ? 8.964   -29.168 -33.017  1.00 33.32  ? 367  ILE   D CB  1 
ATOM   10713 C  CG1 . ILE   D  1 66  ? 10.136  -29.842 -32.293  1.00 37.89  ? 367  ILE   D CG1 1 
ATOM   10714 C  CG2 . ILE   D  1 66  ? 7.885   -28.768 -32.012  1.00 31.29  ? 367  ILE   D CG2 1 
ATOM   10715 C  CD1 . ILE   D  1 66  ? 9.736   -31.022 -31.408  1.00 35.19  ? 367  ILE   D CD1 1 
ATOM   10716 N  N   . ASP   D  1 67  ? 7.501   -28.564 -35.771  1.00 38.60  ? 368  ASP   D N   1 
ATOM   10717 C  CA  . ASP   D  1 67  ? 6.473   -28.038 -36.666  1.00 41.55  ? 368  ASP   D CA  1 
ATOM   10718 C  C   . ASP   D  1 67  ? 5.657   -29.168 -37.279  1.00 37.31  ? 368  ASP   D C   1 
ATOM   10719 O  O   . ASP   D  1 67  ? 4.425   -29.178 -37.191  1.00 34.70  ? 368  ASP   D O   1 
ATOM   10720 C  CB  . ASP   D  1 67  ? 7.104   -27.184 -37.775  1.00 45.79  ? 368  ASP   D CB  1 
ATOM   10721 C  CG  . ASP   D  1 67  ? 7.547   -25.812 -37.289  1.00 50.11  ? 368  ASP   D CG  1 
ATOM   10722 O  OD1 . ASP   D  1 67  ? 7.259   -25.460 -36.125  1.00 47.41  ? 368  ASP   D OD1 1 
ATOM   10723 O  OD2 . ASP   D  1 67  ? 8.195   -25.085 -38.073  1.00 48.51  ? 368  ASP   D OD2 1 
ATOM   10724 N  N   . GLN   D  1 68  ? 6.342   -30.146 -37.885  1.00 33.51  ? 369  GLN   D N   1 
ATOM   10725 C  CA  . GLN   D  1 68  ? 5.661   -31.283 -38.496  1.00 34.10  ? 369  GLN   D CA  1 
ATOM   10726 C  C   . GLN   D  1 68  ? 4.788   -32.022 -37.484  1.00 41.84  ? 369  GLN   D C   1 
ATOM   10727 O  O   . GLN   D  1 68  ? 3.607   -32.284 -37.740  1.00 42.81  ? 369  GLN   D O   1 
ATOM   10728 C  CB  . GLN   D  1 68  ? 6.699   -32.224 -39.110  1.00 38.62  ? 369  GLN   D CB  1 
ATOM   10729 C  CG  . GLN   D  1 68  ? 6.135   -33.437 -39.812  1.00 43.51  ? 369  GLN   D CG  1 
ATOM   10730 C  CD  . GLN   D  1 68  ? 7.215   -34.450 -40.182  1.00 51.43  ? 369  GLN   D CD  1 
ATOM   10731 O  OE1 . GLN   D  1 68  ? 6.979   -35.658 -40.159  1.00 47.04  ? 369  GLN   D OE1 1 
ATOM   10732 N  NE2 . GLN   D  1 68  ? 8.406   -33.957 -40.516  1.00 57.35  ? 369  GLN   D NE2 1 
ATOM   10733 N  N   . TYR   D  1 69  ? 5.355   -32.368 -36.324  1.00 39.34  ? 370  TYR   D N   1 
ATOM   10734 C  CA  . TYR   D  1 69  ? 4.577   -33.077 -35.311  1.00 39.59  ? 370  TYR   D CA  1 
ATOM   10735 C  C   . TYR   D  1 69  ? 3.381   -32.257 -34.851  1.00 36.04  ? 370  TYR   D C   1 
ATOM   10736 O  O   . TYR   D  1 69  ? 2.279   -32.796 -34.684  1.00 34.05  ? 370  TYR   D O   1 
ATOM   10737 C  CB  . TYR   D  1 69  ? 5.443   -33.435 -34.104  1.00 37.50  ? 370  TYR   D CB  1 
ATOM   10738 C  CG  . TYR   D  1 69  ? 4.610   -33.919 -32.936  1.00 35.95  ? 370  TYR   D CG  1 
ATOM   10739 C  CD1 . TYR   D  1 69  ? 4.028   -35.182 -32.953  1.00 31.55  ? 370  TYR   D CD1 1 
ATOM   10740 C  CD2 . TYR   D  1 69  ? 4.379   -33.101 -31.829  1.00 34.17  ? 370  TYR   D CD2 1 
ATOM   10741 C  CE1 . TYR   D  1 69  ? 3.254   -35.625 -31.898  1.00 35.48  ? 370  TYR   D CE1 1 
ATOM   10742 C  CE2 . TYR   D  1 69  ? 3.609   -33.539 -30.767  1.00 39.16  ? 370  TYR   D CE2 1 
ATOM   10743 C  CZ  . TYR   D  1 69  ? 3.052   -34.802 -30.806  1.00 40.03  ? 370  TYR   D CZ  1 
ATOM   10744 O  OH  . TYR   D  1 69  ? 2.280   -35.242 -29.755  1.00 41.77  ? 370  TYR   D OH  1 
ATOM   10745 N  N   . TYR   D  1 70  ? 3.572   -30.955 -34.621  1.00 31.05  ? 371  TYR   D N   1 
ATOM   10746 C  CA  . TYR   D  1 70  ? 2.437   -30.186 -34.136  1.00 36.99  ? 371  TYR   D CA  1 
ATOM   10747 C  C   . TYR   D  1 70  ? 1.415   -29.950 -35.228  1.00 33.34  ? 371  TYR   D C   1 
ATOM   10748 O  O   . TYR   D  1 70  ? 0.216   -29.881 -34.932  1.00 37.45  ? 371  TYR   D O   1 
ATOM   10749 C  CB  . TYR   D  1 70  ? 2.895   -28.879 -33.498  1.00 37.64  ? 371  TYR   D CB  1 
ATOM   10750 C  CG  . TYR   D  1 70  ? 3.181   -29.124 -32.042  1.00 35.15  ? 371  TYR   D CG  1 
ATOM   10751 C  CD1 . TYR   D  1 70  ? 4.461   -29.429 -31.611  1.00 32.54  ? 371  TYR   D CD1 1 
ATOM   10752 C  CD2 . TYR   D  1 70  ? 2.151   -29.134 -31.109  1.00 38.79  ? 371  TYR   D CD2 1 
ATOM   10753 C  CE1 . TYR   D  1 70  ? 4.719   -29.696 -30.267  1.00 36.10  ? 371  TYR   D CE1 1 
ATOM   10754 C  CE2 . TYR   D  1 70  ? 2.397   -29.406 -29.772  1.00 33.44  ? 371  TYR   D CE2 1 
ATOM   10755 C  CZ  . TYR   D  1 70  ? 3.682   -29.682 -29.356  1.00 34.30  ? 371  TYR   D CZ  1 
ATOM   10756 O  OH  . TYR   D  1 70  ? 3.929   -29.945 -28.029  1.00 39.46  ? 371  TYR   D OH  1 
ATOM   10757 N  N   . SER   D  1 71  ? 1.860   -29.831 -36.486  1.00 37.59  ? 372  SER   D N   1 
ATOM   10758 C  CA  . SER   D  1 71  ? 0.920   -29.815 -37.605  1.00 44.12  ? 372  SER   D CA  1 
ATOM   10759 C  C   . SER   D  1 71  ? 0.116   -31.105 -37.653  1.00 42.66  ? 372  SER   D C   1 
ATOM   10760 O  O   . SER   D  1 71  ? -1.099  -31.081 -37.881  1.00 37.94  ? 372  SER   D O   1 
ATOM   10761 C  CB  . SER   D  1 71  ? 1.660   -29.619 -38.933  1.00 47.23  ? 372  SER   D CB  1 
ATOM   10762 O  OG  . SER   D  1 71  ? 2.162   -28.302 -39.086  1.00 54.20  ? 372  SER   D OG  1 
ATOM   10763 N  N   . SER   D  1 72  ? 0.785   -32.241 -37.431  1.00 41.29  ? 373  SER   D N   1 
ATOM   10764 C  CA  . SER   D  1 72  ? 0.125   -33.539 -37.515  1.00 41.38  ? 373  SER   D CA  1 
ATOM   10765 C  C   . SER   D  1 72  ? -1.035  -33.648 -36.536  1.00 45.67  ? 373  SER   D C   1 
ATOM   10766 O  O   . SER   D  1 72  ? -2.050  -34.283 -36.842  1.00 46.21  ? 373  SER   D O   1 
ATOM   10767 C  CB  . SER   D  1 72  ? 1.131   -34.659 -37.263  1.00 38.52  ? 373  SER   D CB  1 
ATOM   10768 O  OG  . SER   D  1 72  ? 1.408   -34.802 -35.876  1.00 40.99  ? 373  SER   D OG  1 
ATOM   10769 N  N   . ILE   D  1 73  ? -0.907  -33.055 -35.349  1.00 37.90  ? 374  ILE   D N   1 
ATOM   10770 C  CA  . ILE   D  1 73  ? -1.975  -33.098 -34.367  1.00 39.59  ? 374  ILE   D CA  1 
ATOM   10771 C  C   . ILE   D  1 73  ? -2.806  -31.811 -34.393  1.00 41.53  ? 374  ILE   D C   1 
ATOM   10772 O  O   . ILE   D  1 73  ? -3.543  -31.529 -33.448  1.00 46.09  ? 374  ILE   D O   1 
ATOM   10773 C  CB  . ILE   D  1 73  ? -1.443  -33.409 -32.953  1.00 42.06  ? 374  ILE   D CB  1 
ATOM   10774 C  CG1 . ILE   D  1 73  ? -0.595  -32.247 -32.416  1.00 38.43  ? 374  ILE   D CG1 1 
ATOM   10775 C  CG2 . ILE   D  1 73  ? -0.625  -34.707 -32.963  1.00 37.04  ? 374  ILE   D CG2 1 
ATOM   10776 C  CD1 . ILE   D  1 73  ? -0.170  -32.398 -30.968  1.00 36.53  ? 374  ILE   D CD1 1 
ATOM   10777 N  N   . LYS   D  1 74  ? -2.707  -31.034 -35.473  1.00 48.37  ? 375  LYS   D N   1 
ATOM   10778 C  CA  . LYS   D  1 74  ? -3.575  -29.871 -35.703  1.00 53.24  ? 375  LYS   D CA  1 
ATOM   10779 C  C   . LYS   D  1 74  ? -3.377  -28.811 -34.627  1.00 45.39  ? 375  LYS   D C   1 
ATOM   10780 O  O   . LYS   D  1 74  ? -4.318  -28.144 -34.198  1.00 41.63  ? 375  LYS   D O   1 
ATOM   10781 C  CB  . LYS   D  1 74  ? -5.045  -30.285 -35.791  1.00 61.65  ? 375  LYS   D CB  1 
ATOM   10782 C  CG  . LYS   D  1 74  ? -5.289  -31.412 -36.762  1.00 69.04  ? 375  LYS   D CG  1 
ATOM   10783 C  CD  . LYS   D  1 74  ? -6.512  -32.227 -36.384  1.00 78.97  ? 375  LYS   D CD  1 
ATOM   10784 C  CE  . LYS   D  1 74  ? -6.796  -33.252 -37.469  1.00 85.68  ? 375  LYS   D CE  1 
ATOM   10785 N  NZ  . LYS   D  1 74  ? -6.578  -32.655 -38.819  1.00 84.58  ? 375  LYS   D NZ  1 
ATOM   10786 N  N   . ARG   D  1 75  ? -2.133  -28.651 -34.196  1.00 46.00  ? 376  ARG   D N   1 
ATOM   10787 C  CA  . ARG   D  1 75  ? -1.775  -27.709 -33.146  1.00 44.29  ? 376  ARG   D CA  1 
ATOM   10788 C  C   . ARG   D  1 75  ? -0.640  -26.802 -33.603  1.00 48.36  ? 376  ARG   D C   1 
ATOM   10789 O  O   . ARG   D  1 75  ? 0.174   -26.353 -32.788  1.00 43.57  ? 376  ARG   D O   1 
ATOM   10790 C  CB  . ARG   D  1 75  ? -1.401  -28.454 -31.867  1.00 41.42  ? 376  ARG   D CB  1 
ATOM   10791 C  CG  . ARG   D  1 75  ? -2.508  -29.340 -31.343  1.00 42.28  ? 376  ARG   D CG  1 
ATOM   10792 C  CD  . ARG   D  1 75  ? -3.780  -28.534 -31.161  1.00 58.46  ? 376  ARG   D CD  1 
ATOM   10793 N  NE  . ARG   D  1 75  ? -4.303  -28.641 -29.804  1.00 76.50  ? 376  ARG   D NE  1 
ATOM   10794 C  CZ  . ARG   D  1 75  ? -5.278  -29.468 -29.443  1.00 82.54  ? 376  ARG   D CZ  1 
ATOM   10795 N  NH1 . ARG   D  1 75  ? -5.687  -29.491 -28.179  1.00 85.23  ? 376  ARG   D NH1 1 
ATOM   10796 N  NH2 . ARG   D  1 75  ? -5.846  -30.263 -30.344  1.00 79.47  ? 376  ARG   D NH2 1 
ATOM   10797 N  N   . PHE   D  1 76  ? -0.565  -26.534 -34.908  1.00 47.67  ? 377  PHE   D N   1 
ATOM   10798 C  CA  . PHE   D  1 76  ? 0.486   -25.666 -35.415  1.00 50.26  ? 377  PHE   D CA  1 
ATOM   10799 C  C   . PHE   D  1 76  ? 0.299   -24.259 -34.855  1.00 54.58  ? 377  PHE   D C   1 
ATOM   10800 O  O   . PHE   D  1 76  ? -0.779  -23.671 -34.960  1.00 49.42  ? 377  PHE   D O   1 
ATOM   10801 C  CB  . PHE   D  1 76  ? 0.490   -25.645 -36.948  1.00 55.64  ? 377  PHE   D CB  1 
ATOM   10802 C  CG  . PHE   D  1 76  ? 1.656   -24.897 -37.526  1.00 60.18  ? 377  PHE   D CG  1 
ATOM   10803 C  CD1 . PHE   D  1 76  ? 1.592   -23.529 -37.719  1.00 62.99  ? 377  PHE   D CD1 1 
ATOM   10804 C  CD2 . PHE   D  1 76  ? 2.835   -25.556 -37.832  1.00 62.39  ? 377  PHE   D CD2 1 
ATOM   10805 C  CE1 . PHE   D  1 76  ? 2.671   -22.834 -38.223  1.00 64.06  ? 377  PHE   D CE1 1 
ATOM   10806 C  CE2 . PHE   D  1 76  ? 3.917   -24.867 -38.338  1.00 58.96  ? 377  PHE   D CE2 1 
ATOM   10807 C  CZ  . PHE   D  1 76  ? 3.832   -23.503 -38.536  1.00 57.47  ? 377  PHE   D CZ  1 
ATOM   10808 N  N   . GLY   D  1 77  ? 1.351   -23.733 -34.231  1.00 56.70  ? 378  GLY   D N   1 
ATOM   10809 C  CA  . GLY   D  1 77  ? 1.288   -22.435 -33.599  1.00 50.74  ? 378  GLY   D CA  1 
ATOM   10810 C  C   . GLY   D  1 77  ? 0.562   -22.408 -32.275  1.00 49.59  ? 378  GLY   D C   1 
ATOM   10811 O  O   . GLY   D  1 77  ? 0.424   -21.328 -31.688  1.00 51.09  ? 378  GLY   D O   1 
ATOM   10812 N  N   . SER   D  1 78  ? 0.088   -23.555 -31.792  1.00 45.60  ? 379  SER   D N   1 
ATOM   10813 C  CA  . SER   D  1 78  ? -0.556  -23.626 -30.494  1.00 40.67  ? 379  SER   D CA  1 
ATOM   10814 C  C   . SER   D  1 78  ? 0.421   -23.217 -29.401  1.00 44.39  ? 379  SER   D C   1 
ATOM   10815 O  O   . SER   D  1 78  ? 1.638   -23.153 -29.602  1.00 40.39  ? 379  SER   D O   1 
ATOM   10816 C  CB  . SER   D  1 78  ? -1.055  -25.040 -30.215  1.00 39.83  ? 379  SER   D CB  1 
ATOM   10817 O  OG  . SER   D  1 78  ? 0.043   -25.928 -30.075  1.00 42.47  ? 379  SER   D OG  1 
ATOM   10818 N  N   . LYS   D  1 79  ? -0.133  -22.967 -28.216  1.00 41.21  ? 380  LYS   D N   1 
ATOM   10819 C  CA  . LYS   D  1 79  ? 0.708   -22.672 -27.069  1.00 50.05  ? 380  LYS   D CA  1 
ATOM   10820 C  C   . LYS   D  1 79  ? 1.748   -23.771 -26.855  1.00 49.39  ? 380  LYS   D C   1 
ATOM   10821 O  O   . LYS   D  1 79  ? 2.942   -23.485 -26.713  1.00 52.14  ? 380  LYS   D O   1 
ATOM   10822 C  CB  . LYS   D  1 79  ? -0.157  -22.475 -25.824  1.00 52.98  ? 380  LYS   D CB  1 
ATOM   10823 C  CG  . LYS   D  1 79  ? 0.604   -21.883 -24.652  1.00 62.12  ? 380  LYS   D CG  1 
ATOM   10824 C  CD  . LYS   D  1 79  ? -0.291  -21.653 -23.435  1.00 66.27  ? 380  LYS   D CD  1 
ATOM   10825 C  CE  . LYS   D  1 79  ? -1.437  -20.703 -23.756  1.00 65.47  ? 380  LYS   D CE  1 
ATOM   10826 N  NZ  . LYS   D  1 79  ? -0.978  -19.335 -24.138  1.00 58.98  ? 380  LYS   D NZ  1 
ATOM   10827 N  N   . ALA   D  1 80  ? 1.319   -25.037 -26.849  1.00 46.77  ? 381  ALA   D N   1 
ATOM   10828 C  CA  . ALA   D  1 80  ? 2.267   -26.128 -26.624  1.00 43.32  ? 381  ALA   D CA  1 
ATOM   10829 C  C   . ALA   D  1 80  ? 3.348   -26.148 -27.694  1.00 44.77  ? 381  ALA   D C   1 
ATOM   10830 O  O   . ALA   D  1 80  ? 4.519   -26.428 -27.404  1.00 41.02  ? 381  ALA   D O   1 
ATOM   10831 C  CB  . ALA   D  1 80  ? 1.539   -27.470 -26.588  1.00 40.21  ? 381  ALA   D CB  1 
ATOM   10832 N  N   . HIS   D  1 81  ? 2.972   -25.854 -28.938  1.00 48.35  ? 382  HIS   D N   1 
ATOM   10833 C  CA  . HIS   D  1 81  ? 3.944   -25.837 -30.026  1.00 44.56  ? 382  HIS   D CA  1 
ATOM   10834 C  C   . HIS   D  1 81  ? 4.996   -24.758 -29.797  1.00 44.77  ? 382  HIS   D C   1 
ATOM   10835 O  O   . HIS   D  1 81  ? 6.201   -25.024 -29.882  1.00 39.56  ? 382  HIS   D O   1 
ATOM   10836 C  CB  . HIS   D  1 81  ? 3.222   -25.628 -31.356  1.00 42.22  ? 382  HIS   D CB  1 
ATOM   10837 C  CG  . HIS   D  1 81  ? 4.128   -25.620 -32.546  1.00 46.66  ? 382  HIS   D CG  1 
ATOM   10838 N  ND1 . HIS   D  1 81  ? 3.671   -25.366 -33.820  1.00 51.10  ? 382  HIS   D ND1 1 
ATOM   10839 C  CD2 . HIS   D  1 81  ? 5.460   -25.836 -32.660  1.00 46.29  ? 382  HIS   D CD2 1 
ATOM   10840 C  CE1 . HIS   D  1 81  ? 4.682   -25.426 -34.669  1.00 50.67  ? 382  HIS   D CE1 1 
ATOM   10841 N  NE2 . HIS   D  1 81  ? 5.780   -25.705 -33.989  1.00 48.94  ? 382  HIS   D NE2 1 
ATOM   10842 N  N   . MET   D  1 82  ? 4.558   -23.534 -29.486  1.00 38.18  ? 383  MET   D N   1 
ATOM   10843 C  CA  . MET   D  1 82  ? 5.507   -22.439 -29.312  1.00 42.55  ? 383  MET   D CA  1 
ATOM   10844 C  C   . MET   D  1 82  ? 6.375   -22.666 -28.086  1.00 47.55  ? 383  MET   D C   1 
ATOM   10845 O  O   . MET   D  1 82  ? 7.586   -22.417 -28.120  1.00 49.01  ? 383  MET   D O   1 
ATOM   10846 C  CB  . MET   D  1 82  ? 4.771   -21.097 -29.206  1.00 44.44  ? 383  MET   D CB  1 
ATOM   10847 C  CG  . MET   D  1 82  ? 3.955   -20.757 -30.424  1.00 47.08  ? 383  MET   D CG  1 
ATOM   10848 S  SD  . MET   D  1 82  ? 4.892   -21.100 -31.929  1.00 59.96  ? 383  MET   D SD  1 
ATOM   10849 C  CE  . MET   D  1 82  ? 6.224   -19.909 -31.802  1.00 57.18  ? 383  MET   D CE  1 
ATOM   10850 N  N   . GLU   D  1 83  ? 5.772   -23.134 -26.994  1.00 46.79  ? 384  GLU   D N   1 
ATOM   10851 C  CA  . GLU   D  1 83  ? 6.565   -23.496 -25.830  1.00 50.94  ? 384  GLU   D CA  1 
ATOM   10852 C  C   . GLU   D  1 83  ? 7.589   -24.555 -26.197  1.00 46.63  ? 384  GLU   D C   1 
ATOM   10853 O  O   . GLU   D  1 83  ? 8.749   -24.479 -25.778  1.00 46.64  ? 384  GLU   D O   1 
ATOM   10854 C  CB  . GLU   D  1 83  ? 5.659   -23.989 -24.701  1.00 55.39  ? 384  GLU   D CB  1 
ATOM   10855 C  CG  . GLU   D  1 83  ? 4.694   -22.953 -24.172  1.00 70.05  ? 384  GLU   D CG  1 
ATOM   10856 C  CD  . GLU   D  1 83  ? 3.868   -23.472 -23.011  1.00 77.34  ? 384  GLU   D CD  1 
ATOM   10857 O  OE1 . GLU   D  1 83  ? 4.177   -24.576 -22.511  1.00 80.83  ? 384  GLU   D OE1 1 
ATOM   10858 O  OE2 . GLU   D  1 83  ? 2.914   -22.776 -22.598  1.00 78.41  ? 384  GLU   D OE2 1 
ATOM   10859 N  N   . ARG   D  1 84  ? 7.183   -25.538 -27.007  1.00 41.63  ? 385  ARG   D N   1 
ATOM   10860 C  CA  . ARG   D  1 84  ? 8.104   -26.607 -27.373  1.00 40.69  ? 385  ARG   D CA  1 
ATOM   10861 C  C   . ARG   D  1 84  ? 9.304   -26.055 -28.137  1.00 41.04  ? 385  ARG   D C   1 
ATOM   10862 O  O   . ARG   D  1 84  ? 10.454  -26.397 -27.839  1.00 43.28  ? 385  ARG   D O   1 
ATOM   10863 C  CB  . ARG   D  1 84  ? 7.369   -27.669 -28.187  1.00 42.09  ? 385  ARG   D CB  1 
ATOM   10864 C  CG  . ARG   D  1 84  ? 8.178   -28.926 -28.413  1.00 35.55  ? 385  ARG   D CG  1 
ATOM   10865 C  CD  . ARG   D  1 84  ? 8.378   -29.737 -27.134  1.00 37.48  ? 385  ARG   D CD  1 
ATOM   10866 N  NE  . ARG   D  1 84  ? 9.222   -30.883 -27.452  1.00 39.20  ? 385  ARG   D NE  1 
ATOM   10867 C  CZ  . ARG   D  1 84  ? 10.448  -31.070 -26.978  1.00 43.53  ? 385  ARG   D CZ  1 
ATOM   10868 N  NH1 . ARG   D  1 84  ? 10.970  -30.215 -26.099  1.00 48.56  ? 385  ARG   D NH1 1 
ATOM   10869 N  NH2 . ARG   D  1 84  ? 11.138  -32.134 -27.359  1.00 33.56  ? 385  ARG   D NH2 1 
ATOM   10870 N  N   . LEU   D  1 85  ? 9.056   -25.166 -29.097  1.00 40.07  ? 386  LEU   D N   1 
ATOM   10871 C  CA  . LEU   D  1 85  ? 10.153  -24.521 -29.808  1.00 37.97  ? 386  LEU   D CA  1 
ATOM   10872 C  C   . LEU   D  1 85  ? 11.088  -23.801 -28.847  1.00 40.55  ? 386  LEU   D C   1 
ATOM   10873 O  O   . LEU   D  1 85  ? 12.315  -23.917 -28.955  1.00 38.56  ? 386  LEU   D O   1 
ATOM   10874 C  CB  . LEU   D  1 85  ? 9.593   -23.560 -30.849  1.00 43.57  ? 386  LEU   D CB  1 
ATOM   10875 C  CG  . LEU   D  1 85  ? 8.866   -24.276 -31.986  1.00 42.38  ? 386  LEU   D CG  1 
ATOM   10876 C  CD1 . LEU   D  1 85  ? 8.366   -23.276 -33.017  1.00 42.85  ? 386  LEU   D CD1 1 
ATOM   10877 C  CD2 . LEU   D  1 85  ? 9.795   -25.286 -32.633  1.00 40.21  ? 386  LEU   D CD2 1 
ATOM   10878 N  N   . GLU   D  1 86  ? 10.522  -23.058 -27.890  1.00 44.43  ? 387  GLU   D N   1 
ATOM   10879 C  CA  . GLU   D  1 86  ? 11.329  -22.372 -26.886  1.00 46.79  ? 387  GLU   D CA  1 
ATOM   10880 C  C   . GLU   D  1 86  ? 12.120  -23.362 -26.044  1.00 44.46  ? 387  GLU   D C   1 
ATOM   10881 O  O   . GLU   D  1 86  ? 13.293  -23.131 -25.723  1.00 40.58  ? 387  GLU   D O   1 
ATOM   10882 C  CB  . GLU   D  1 86  ? 10.426  -21.526 -25.989  1.00 54.23  ? 387  GLU   D CB  1 
ATOM   10883 C  CG  . GLU   D  1 86  ? 9.952   -20.228 -26.609  1.00 67.36  ? 387  GLU   D CG  1 
ATOM   10884 C  CD  . GLU   D  1 86  ? 11.070  -19.211 -26.745  1.00 77.68  ? 387  GLU   D CD  1 
ATOM   10885 O  OE1 . GLU   D  1 86  ? 11.578  -19.029 -27.871  1.00 77.23  ? 387  GLU   D OE1 1 
ATOM   10886 O  OE2 . GLU   D  1 86  ? 11.448  -18.603 -25.720  1.00 82.90  ? 387  GLU   D OE2 1 
ATOM   10887 N  N   . GLU   D  1 87  ? 11.483  -24.468 -25.667  1.00 41.03  ? 388  GLU   D N   1 
ATOM   10888 C  CA  . GLU   D  1 87  ? 12.145  -25.483 -24.863  1.00 38.30  ? 388  GLU   D CA  1 
ATOM   10889 C  C   . GLU   D  1 87  ? 13.302  -26.103 -25.634  1.00 41.35  ? 388  GLU   D C   1 
ATOM   10890 O  O   . GLU   D  1 87  ? 14.419  -26.230 -25.113  1.00 40.25  ? 388  GLU   D O   1 
ATOM   10891 C  CB  . GLU   D  1 87  ? 11.119  -26.541 -24.453  1.00 38.70  ? 388  GLU   D CB  1 
ATOM   10892 C  CG  . GLU   D  1 87  ? 11.627  -27.619 -23.518  1.00 50.84  ? 388  GLU   D CG  1 
ATOM   10893 C  CD  . GLU   D  1 87  ? 10.502  -28.511 -23.018  1.00 62.96  ? 388  GLU   D CD  1 
ATOM   10894 O  OE1 . GLU   D  1 87  ? 9.509   -28.681 -23.765  1.00 53.73  ? 388  GLU   D OE1 1 
ATOM   10895 O  OE2 . GLU   D  1 87  ? 10.608  -29.024 -21.875  1.00 68.08  ? 388  GLU   D OE2 1 
ATOM   10896 N  N   . VAL   D  1 88  ? 13.052  -26.483 -26.887  1.00 36.46  ? 389  VAL   D N   1 
ATOM   10897 C  CA  . VAL   D  1 88  ? 14.108  -27.057 -27.712  1.00 36.02  ? 389  VAL   D CA  1 
ATOM   10898 C  C   . VAL   D  1 88  ? 15.227  -26.047 -27.905  1.00 35.02  ? 389  VAL   D C   1 
ATOM   10899 O  O   . VAL   D  1 88  ? 16.416  -26.382 -27.820  1.00 33.35  ? 389  VAL   D O   1 
ATOM   10900 C  CB  . VAL   D  1 88  ? 13.518  -27.535 -29.048  1.00 38.81  ? 389  VAL   D CB  1 
ATOM   10901 C  CG1 . VAL   D  1 88  ? 14.625  -27.944 -29.998  1.00 34.75  ? 389  VAL   D CG1 1 
ATOM   10902 C  CG2 . VAL   D  1 88  ? 12.565  -28.693 -28.777  1.00 36.53  ? 389  VAL   D CG2 1 
ATOM   10903 N  N   . ASN   D  1 89  ? 14.856  -24.786 -28.115  1.00 33.49  ? 390  ASN   D N   1 
ATOM   10904 C  CA  . ASN   D  1 89  ? 15.821  -23.700 -28.239  1.00 40.36  ? 390  ASN   D CA  1 
ATOM   10905 C  C   . ASN   D  1 89  ? 16.784  -23.652 -27.051  1.00 48.12  ? 390  ASN   D C   1 
ATOM   10906 O  O   . ASN   D  1 89  ? 18.004  -23.570 -27.236  1.00 42.13  ? 390  ASN   D O   1 
ATOM   10907 C  CB  . ASN   D  1 89  ? 15.064  -22.380 -28.377  1.00 48.65  ? 390  ASN   D CB  1 
ATOM   10908 C  CG  . ASN   D  1 89  ? 15.804  -21.374 -29.218  1.00 72.50  ? 390  ASN   D CG  1 
ATOM   10909 O  OD1 . ASN   D  1 89  ? 17.006  -21.183 -29.056  1.00 72.61  ? 390  ASN   D OD1 1 
ATOM   10910 N  ND2 . ASN   D  1 89  ? 15.088  -20.725 -30.134  1.00 85.76  ? 390  ASN   D ND2 1 
ATOM   10911 N  N   . LYS   D  1 90  ? 16.256  -23.685 -25.814  1.00 40.61  ? 391  LYS   D N   1 
ATOM   10912 C  CA  . LYS   D  1 90  ? 17.144  -23.582 -24.661  1.00 39.51  ? 391  LYS   D CA  1 
ATOM   10913 C  C   . LYS   D  1 90  ? 17.881  -24.885 -24.394  1.00 40.15  ? 391  LYS   D C   1 
ATOM   10914 O  O   . LYS   D  1 90  ? 19.016  -24.857 -23.908  1.00 46.24  ? 391  LYS   D O   1 
ATOM   10915 C  CB  . LYS   D  1 90  ? 16.373  -23.160 -23.408  1.00 55.30  ? 391  LYS   D CB  1 
ATOM   10916 C  CG  . LYS   D  1 90  ? 15.416  -24.219 -22.904  1.00 67.65  ? 391  LYS   D CG  1 
ATOM   10917 C  CD  . LYS   D  1 90  ? 15.289  -24.213 -21.391  1.00 74.38  ? 391  LYS   D CD  1 
ATOM   10918 C  CE  . LYS   D  1 90  ? 14.889  -25.600 -20.900  1.00 70.42  ? 391  LYS   D CE  1 
ATOM   10919 N  NZ  . LYS   D  1 90  ? 15.957  -26.609 -21.179  1.00 59.28  ? 391  LYS   D NZ  1 
ATOM   10920 N  N   . GLU   D  1 91  ? 17.258  -26.028 -24.690  1.00 41.56  ? 392  GLU   D N   1 
ATOM   10921 C  CA  . GLU   D  1 91  ? 17.960  -27.300 -24.575  1.00 40.14  ? 392  GLU   D CA  1 
ATOM   10922 C  C   . GLU   D  1 91  ? 19.193  -27.315 -25.463  1.00 40.94  ? 392  GLU   D C   1 
ATOM   10923 O  O   . GLU   D  1 91  ? 20.282  -27.714 -25.035  1.00 41.00  ? 392  GLU   D O   1 
ATOM   10924 C  CB  . GLU   D  1 91  ? 17.034  -28.455 -24.950  1.00 36.89  ? 392  GLU   D CB  1 
ATOM   10925 C  CG  . GLU   D  1 91  ? 16.172  -28.997 -23.824  1.00 39.43  ? 392  GLU   D CG  1 
ATOM   10926 C  CD  . GLU   D  1 91  ? 15.464  -30.266 -24.233  1.00 53.64  ? 392  GLU   D CD  1 
ATOM   10927 O  OE1 . GLU   D  1 91  ? 16.108  -31.338 -24.240  1.00 62.05  ? 392  GLU   D OE1 1 
ATOM   10928 O  OE2 . GLU   D  1 91  ? 14.268  -30.194 -24.575  1.00 60.69  ? 392  GLU   D OE2 1 
ATOM   10929 N  N   . ILE   D  1 92  ? 19.034  -26.893 -26.715  1.00 42.56  ? 393  ILE   D N   1 
ATOM   10930 C  CA  . ILE   D  1 92  ? 20.173  -26.827 -27.619  1.00 44.05  ? 393  ILE   D CA  1 
ATOM   10931 C  C   . ILE   D  1 92  ? 21.163  -25.777 -27.132  1.00 44.94  ? 393  ILE   D C   1 
ATOM   10932 O  O   . ILE   D  1 92  ? 22.374  -26.017 -27.091  1.00 45.81  ? 393  ILE   D O   1 
ATOM   10933 C  CB  . ILE   D  1 92  ? 19.685  -26.565 -29.056  1.00 41.50  ? 393  ILE   D CB  1 
ATOM   10934 C  CG1 . ILE   D  1 92  ? 18.915  -27.789 -29.558  1.00 38.04  ? 393  ILE   D CG1 1 
ATOM   10935 C  CG2 . ILE   D  1 92  ? 20.857  -26.215 -29.978  1.00 47.19  ? 393  ILE   D CG2 1 
ATOM   10936 C  CD1 . ILE   D  1 92  ? 18.169  -27.580 -30.859  1.00 38.72  ? 393  ILE   D CD1 1 
ATOM   10937 N  N   . ASP   D  1 93  ? 20.653  -24.626 -26.683  1.00 46.55  ? 394  ASP   D N   1 
ATOM   10938 C  CA  . ASP   D  1 93  ? 21.504  -23.586 -26.108  1.00 54.11  ? 394  ASP   D CA  1 
ATOM   10939 C  C   . ASP   D  1 93  ? 22.372  -24.106 -24.970  1.00 57.68  ? 394  ASP   D C   1 
ATOM   10940 O  O   . ASP   D  1 93  ? 23.514  -23.667 -24.805  1.00 65.92  ? 394  ASP   D O   1 
ATOM   10941 C  CB  . ASP   D  1 93  ? 20.646  -22.428 -25.603  1.00 63.22  ? 394  ASP   D CB  1 
ATOM   10942 C  CG  . ASP   D  1 93  ? 20.283  -21.469 -26.694  1.00 72.44  ? 394  ASP   D CG  1 
ATOM   10943 O  OD1 . ASP   D  1 93  ? 21.099  -21.319 -27.626  1.00 72.86  ? 394  ASP   D OD1 1 
ATOM   10944 O  OD2 . ASP   D  1 93  ? 19.190  -20.869 -26.627  1.00 77.82  ? 394  ASP   D OD2 1 
ATOM   10945 N  N   . THR   D  1 94  ? 21.851  -25.037 -24.170  1.00 46.90  ? 395  THR   D N   1 
ATOM   10946 C  CA  . THR   D  1 94  ? 22.552  -25.451 -22.968  1.00 54.08  ? 395  THR   D CA  1 
ATOM   10947 C  C   . THR   D  1 94  ? 23.167  -26.840 -23.050  1.00 58.26  ? 395  THR   D C   1 
ATOM   10948 O  O   . THR   D  1 94  ? 24.018  -27.166 -22.217  1.00 62.41  ? 395  THR   D O   1 
ATOM   10949 C  CB  . THR   D  1 94  ? 21.605  -25.376 -21.758  1.00 53.15  ? 395  THR   D CB  1 
ATOM   10950 O  OG1 . THR   D  1 94  ? 20.427  -26.140 -22.024  1.00 62.45  ? 395  THR   D OG1 1 
ATOM   10951 C  CG2 . THR   D  1 94  ? 21.196  -23.940 -21.507  1.00 53.69  ? 395  THR   D CG2 1 
ATOM   10952 N  N   . THR   D  1 95  ? 22.772  -27.664 -24.019  1.00 51.66  ? 396  THR   D N   1 
ATOM   10953 C  CA  . THR   D  1 95  ? 23.325  -29.006 -24.144  1.00 45.29  ? 396  THR   D CA  1 
ATOM   10954 C  C   . THR   D  1 95  ? 23.757  -29.361 -25.559  1.00 45.50  ? 396  THR   D C   1 
ATOM   10955 O  O   . THR   D  1 95  ? 24.181  -30.501 -25.784  1.00 53.20  ? 396  THR   D O   1 
ATOM   10956 C  CB  . THR   D  1 95  ? 22.313  -30.063 -23.659  1.00 41.59  ? 396  THR   D CB  1 
ATOM   10957 O  OG1 . THR   D  1 95  ? 21.261  -30.203 -24.624  1.00 45.16  ? 396  THR   D OG1 1 
ATOM   10958 C  CG2 . THR   D  1 95  ? 21.700  -29.671 -22.327  1.00 39.58  ? 396  THR   D CG2 1 
ATOM   10959 N  N   . SER   D  1 96  ? 23.628  -28.447 -26.523  1.00 37.51  ? 397  SER   D N   1 
ATOM   10960 C  CA  . SER   D  1 96  ? 23.993  -28.718 -27.918  1.00 41.38  ? 397  SER   D CA  1 
ATOM   10961 C  C   . SER   D  1 96  ? 23.054  -29.742 -28.541  1.00 43.36  ? 397  SER   D C   1 
ATOM   10962 O  O   . SER   D  1 96  ? 23.192  -30.068 -29.723  1.00 44.06  ? 397  SER   D O   1 
ATOM   10963 C  CB  . SER   D  1 96  ? 25.448  -29.192 -28.048  1.00 45.89  ? 397  SER   D CB  1 
ATOM   10964 O  OG  . SER   D  1 96  ? 26.340  -28.088 -28.021  1.00 49.75  ? 397  SER   D OG  1 
ATOM   10965 N  N   . THR   D  1 97  ? 22.088  -30.245 -27.780  1.00 41.11  ? 398  THR   D N   1 
ATOM   10966 C  CA  . THR   D  1 97  ? 21.118  -31.175 -28.345  1.00 37.13  ? 398  THR   D CA  1 
ATOM   10967 C  C   . THR   D  1 97  ? 19.776  -30.910 -27.675  1.00 30.63  ? 398  THR   D C   1 
ATOM   10968 O  O   . THR   D  1 97  ? 19.598  -29.899 -26.988  1.00 32.65  ? 398  THR   D O   1 
ATOM   10969 C  CB  . THR   D  1 97  ? 21.611  -32.615 -28.178  1.00 32.90  ? 398  THR   D CB  1 
ATOM   10970 O  OG1 . THR   D  1 97  ? 20.741  -33.506 -28.890  1.00 34.66  ? 398  THR   D OG1 1 
ATOM   10971 C  CG2 . THR   D  1 97  ? 21.650  -32.988 -26.702  1.00 33.92  ? 398  THR   D CG2 1 
ATOM   10972 N  N   . TYR   D  1 98  ? 18.811  -31.794 -27.903  1.00 32.75  ? 399  TYR   D N   1 
ATOM   10973 C  CA  . TYR   D  1 98  ? 17.525  -31.682 -27.226  1.00 37.35  ? 399  TYR   D CA  1 
ATOM   10974 C  C   . TYR   D  1 98  ? 16.911  -33.066 -27.141  1.00 33.84  ? 399  TYR   D C   1 
ATOM   10975 O  O   . TYR   D  1 98  ? 17.366  -34.007 -27.794  1.00 29.24  ? 399  TYR   D O   1 
ATOM   10976 C  CB  . TYR   D  1 98  ? 16.586  -30.695 -27.930  1.00 33.80  ? 399  TYR   D CB  1 
ATOM   10977 C  CG  . TYR   D  1 98  ? 16.052  -31.190 -29.251  1.00 33.07  ? 399  TYR   D CG  1 
ATOM   10978 C  CD1 . TYR   D  1 98  ? 14.743  -31.628 -29.368  1.00 26.78  ? 399  TYR   D CD1 1 
ATOM   10979 C  CD2 . TYR   D  1 98  ? 16.858  -31.216 -30.376  1.00 27.02  ? 399  TYR   D CD2 1 
ATOM   10980 C  CE1 . TYR   D  1 98  ? 14.253  -32.072 -30.563  1.00 30.23  ? 399  TYR   D CE1 1 
ATOM   10981 C  CE2 . TYR   D  1 98  ? 16.374  -31.658 -31.583  1.00 32.95  ? 399  TYR   D CE2 1 
ATOM   10982 C  CZ  . TYR   D  1 98  ? 15.070  -32.081 -31.668  1.00 34.50  ? 399  TYR   D CZ  1 
ATOM   10983 O  OH  . TYR   D  1 98  ? 14.581  -32.526 -32.865  1.00 38.23  ? 399  TYR   D OH  1 
ATOM   10984 N  N   . GLN   D  1 99  ? 15.877  -33.188 -26.313  1.00 32.07  ? 400  GLN   D N   1 
ATOM   10985 C  CA  . GLN   D  1 99  ? 15.280  -34.482 -26.004  1.00 30.85  ? 400  GLN   D CA  1 
ATOM   10986 C  C   . GLN   D  1 99  ? 13.845  -34.513 -26.508  1.00 33.49  ? 400  GLN   D C   1 
ATOM   10987 O  O   . GLN   D  1 99  ? 13.067  -33.593 -26.235  1.00 31.33  ? 400  GLN   D O   1 
ATOM   10988 C  CB  . GLN   D  1 99  ? 15.334  -34.768 -24.494  1.00 30.22  ? 400  GLN   D CB  1 
ATOM   10989 C  CG  . GLN   D  1 99  ? 16.748  -34.790 -23.909  1.00 35.14  ? 400  GLN   D CG  1 
ATOM   10990 C  CD  . GLN   D  1 99  ? 17.667  -35.804 -24.590  1.00 41.20  ? 400  GLN   D CD  1 
ATOM   10991 O  OE1 . GLN   D  1 99  ? 17.287  -36.956 -24.818  1.00 41.67  ? 400  GLN   D OE1 1 
ATOM   10992 N  NE2 . GLN   D  1 99  ? 18.884  -35.372 -24.923  1.00 41.68  ? 400  GLN   D NE2 1 
ATOM   10993 N  N   . LEU   D  1 100 ? 13.502  -35.567 -27.245  1.00 31.49  ? 401  LEU   D N   1 
ATOM   10994 C  CA  . LEU   D  1 100 ? 12.133  -35.736 -27.710  1.00 32.91  ? 401  LEU   D CA  1 
ATOM   10995 C  C   . LEU   D  1 100 ? 11.207  -36.094 -26.560  1.00 30.58  ? 401  LEU   D C   1 
ATOM   10996 O  O   . LEU   D  1 100 ? 11.554  -36.890 -25.685  1.00 32.17  ? 401  LEU   D O   1 
ATOM   10997 C  CB  . LEU   D  1 100 ? 12.056  -36.837 -28.769  1.00 29.11  ? 401  LEU   D CB  1 
ATOM   10998 C  CG  . LEU   D  1 100 ? 12.897  -36.583 -30.013  1.00 29.09  ? 401  LEU   D CG  1 
ATOM   10999 C  CD1 . LEU   D  1 100 ? 12.759  -37.756 -30.965  1.00 24.88  ? 401  LEU   D CD1 1 
ATOM   11000 C  CD2 . LEU   D  1 100 ? 12.448  -35.294 -30.664  1.00 28.90  ? 401  LEU   D CD2 1 
ATOM   11001 N  N   . LYS   D  1 101 ? 10.015  -35.509 -26.571  1.00 27.09  ? 402  LYS   D N   1 
ATOM   11002 C  CA  . LYS   D  1 101 ? 8.928   -36.042 -25.767  1.00 24.66  ? 402  LYS   D CA  1 
ATOM   11003 C  C   . LYS   D  1 101 ? 8.566   -37.448 -26.246  1.00 26.96  ? 402  LYS   D C   1 
ATOM   11004 O  O   . LYS   D  1 101 ? 8.782   -37.804 -27.407  1.00 25.52  ? 402  LYS   D O   1 
ATOM   11005 C  CB  . LYS   D  1 101 ? 7.712   -35.121 -25.862  1.00 31.18  ? 402  LYS   D CB  1 
ATOM   11006 C  CG  . LYS   D  1 101 ? 7.947   -33.741 -25.309  1.00 37.35  ? 402  LYS   D CG  1 
ATOM   11007 C  CD  . LYS   D  1 101 ? 8.308   -33.820 -23.831  1.00 40.30  ? 402  LYS   D CD  1 
ATOM   11008 C  CE  . LYS   D  1 101 ? 8.191   -32.470 -23.126  1.00 56.98  ? 402  LYS   D CE  1 
ATOM   11009 N  NZ  . LYS   D  1 101 ? 9.489   -31.744 -23.109  1.00 59.96  ? 402  LYS   D NZ  1 
ATOM   11010 N  N   . ASP   D  1 102 ? 7.997   -38.249 -25.335  1.00 27.92  ? 403  ASP   D N   1 
ATOM   11011 C  CA  . ASP   D  1 102 ? 7.587   -39.612 -25.679  1.00 29.69  ? 403  ASP   D CA  1 
ATOM   11012 C  C   . ASP   D  1 102 ? 6.657   -39.637 -26.886  1.00 29.33  ? 403  ASP   D C   1 
ATOM   11013 O  O   . ASP   D  1 102 ? 6.808   -40.480 -27.777  1.00 25.00  ? 403  ASP   D O   1 
ATOM   11014 C  CB  . ASP   D  1 102 ? 6.896   -40.269 -24.490  1.00 38.65  ? 403  ASP   D CB  1 
ATOM   11015 C  CG  . ASP   D  1 102 ? 7.802   -40.397 -23.296  1.00 53.03  ? 403  ASP   D CG  1 
ATOM   11016 O  OD1 . ASP   D  1 102 ? 8.897   -39.796 -23.327  1.00 58.96  ? 403  ASP   D OD1 1 
ATOM   11017 O  OD2 . ASP   D  1 102 ? 7.422   -41.103 -22.331  1.00 57.13  ? 403  ASP   D OD2 1 
ATOM   11018 N  N   . THR   D  1 103 ? 5.661   -38.748 -26.900  1.00 29.91  ? 404  THR   D N   1 
ATOM   11019 C  CA  . THR   D  1 103 ? 4.756   -38.633 -28.038  1.00 32.35  ? 404  THR   D CA  1 
ATOM   11020 C  C   . THR   D  1 103 ? 5.517   -38.326 -29.319  1.00 29.09  ? 404  THR   D C   1 
ATOM   11021 O  O   . THR   D  1 103 ? 5.199   -38.862 -30.382  1.00 30.63  ? 404  THR   D O   1 
ATOM   11022 C  CB  . THR   D  1 103 ? 3.729   -37.529 -27.779  1.00 36.16  ? 404  THR   D CB  1 
ATOM   11023 O  OG1 . THR   D  1 103 ? 4.422   -36.307 -27.488  1.00 39.29  ? 404  THR   D OG1 1 
ATOM   11024 C  CG2 . THR   D  1 103 ? 2.827   -37.876 -26.602  1.00 38.71  ? 404  THR   D CG2 1 
ATOM   11025 N  N   . GLU   D  1 104 ? 6.517   -37.449 -29.234  1.00 27.09  ? 405  GLU   D N   1 
ATOM   11026 C  CA  . GLU   D  1 104 ? 7.296   -37.097 -30.412  1.00 28.61  ? 405  GLU   D CA  1 
ATOM   11027 C  C   . GLU   D  1 104 ? 8.138   -38.277 -30.871  1.00 28.16  ? 405  GLU   D C   1 
ATOM   11028 O  O   . GLU   D  1 104 ? 8.243   -38.544 -32.073  1.00 25.44  ? 405  GLU   D O   1 
ATOM   11029 C  CB  . GLU   D  1 104 ? 8.178   -35.890 -30.097  1.00 28.45  ? 405  GLU   D CB  1 
ATOM   11030 C  CG  . GLU   D  1 104 ? 7.387   -34.662 -29.671  1.00 32.56  ? 405  GLU   D CG  1 
ATOM   11031 C  CD  . GLU   D  1 104 ? 8.264   -33.574 -29.098  1.00 32.54  ? 405  GLU   D CD  1 
ATOM   11032 O  OE1 . GLU   D  1 104 ? 7.767   -32.453 -28.899  1.00 33.43  ? 405  GLU   D OE1 1 
ATOM   11033 O  OE2 . GLU   D  1 104 ? 9.456   -33.835 -28.850  1.00 35.05  ? 405  GLU   D OE2 1 
ATOM   11034 N  N   . LEU   D  1 105 ? 8.756   -38.977 -29.921  1.00 26.26  ? 406  LEU   D N   1 
ATOM   11035 C  CA  . LEU   D  1 105 ? 9.523   -40.169 -30.239  1.00 26.39  ? 406  LEU   D CA  1 
ATOM   11036 C  C   . LEU   D  1 105 ? 8.652   -41.180 -30.954  1.00 28.64  ? 406  LEU   D C   1 
ATOM   11037 O  O   . LEU   D  1 105 ? 9.044   -41.741 -31.983  1.00 29.03  ? 406  LEU   D O   1 
ATOM   11038 C  CB  . LEU   D  1 105 ? 10.093  -40.780 -28.960  1.00 28.49  ? 406  LEU   D CB  1 
ATOM   11039 C  CG  . LEU   D  1 105 ? 11.003  -41.987 -29.152  1.00 25.06  ? 406  LEU   D CG  1 
ATOM   11040 C  CD1 . LEU   D  1 105 ? 12.299  -41.541 -29.831  1.00 37.66  ? 406  LEU   D CD1 1 
ATOM   11041 C  CD2 . LEU   D  1 105 ? 11.282  -42.659 -27.803  1.00 27.67  ? 406  LEU   D CD2 1 
ATOM   11042 N  N   . ILE   D  1 106 ? 7.453   -41.418 -30.428  1.00 25.58  ? 407  ILE   D N   1 
ATOM   11043 C  CA  . ILE   D  1 106 ? 6.580   -42.401 -31.053  1.00 21.62  ? 407  ILE   D CA  1 
ATOM   11044 C  C   . ILE   D  1 106 ? 6.197   -41.942 -32.451  1.00 28.97  ? 407  ILE   D C   1 
ATOM   11045 O  O   . ILE   D  1 106 ? 6.330   -42.691 -33.425  1.00 30.12  ? 407  ILE   D O   1 
ATOM   11046 C  CB  . ILE   D  1 106 ? 5.344   -42.652 -30.180  1.00 24.68  ? 407  ILE   D CB  1 
ATOM   11047 C  CG1 . ILE   D  1 106 ? 5.762   -43.351 -28.884  1.00 24.11  ? 407  ILE   D CG1 1 
ATOM   11048 C  CG2 . ILE   D  1 106 ? 4.305   -43.443 -30.964  1.00 21.35  ? 407  ILE   D CG2 1 
ATOM   11049 C  CD1 . ILE   D  1 106 ? 4.679   -43.345 -27.817  1.00 26.27  ? 407  ILE   D CD1 1 
ATOM   11050 N  N   . TYR   D  1 107 ? 5.718   -40.698 -32.562  1.00 28.77  ? 408  TYR   D N   1 
ATOM   11051 C  CA  . TYR   D  1 107 ? 5.397   -40.114 -33.860  1.00 29.70  ? 408  TYR   D CA  1 
ATOM   11052 C  C   . TYR   D  1 107 ? 6.557   -40.265 -34.837  1.00 25.51  ? 408  TYR   D C   1 
ATOM   11053 O  O   . TYR   D  1 107 ? 6.372   -40.688 -35.984  1.00 26.02  ? 408  TYR   D O   1 
ATOM   11054 C  CB  . TYR   D  1 107 ? 5.032   -38.634 -33.687  1.00 29.31  ? 408  TYR   D CB  1 
ATOM   11055 C  CG  . TYR   D  1 107 ? 4.884   -37.916 -35.010  1.00 27.25  ? 408  TYR   D CG  1 
ATOM   11056 C  CD1 . TYR   D  1 107 ? 3.705   -37.990 -35.728  1.00 25.20  ? 408  TYR   D CD1 1 
ATOM   11057 C  CD2 . TYR   D  1 107 ? 5.941   -37.193 -35.555  1.00 33.02  ? 408  TYR   D CD2 1 
ATOM   11058 C  CE1 . TYR   D  1 107 ? 3.568   -37.341 -36.948  1.00 26.65  ? 408  TYR   D CE1 1 
ATOM   11059 C  CE2 . TYR   D  1 107 ? 5.820   -36.550 -36.775  1.00 36.04  ? 408  TYR   D CE2 1 
ATOM   11060 C  CZ  . TYR   D  1 107 ? 4.632   -36.630 -37.472  1.00 36.25  ? 408  TYR   D CZ  1 
ATOM   11061 O  OH  . TYR   D  1 107 ? 4.509   -35.991 -38.694  1.00 43.15  ? 408  TYR   D OH  1 
ATOM   11062 N  N   . GLY   D  1 108 ? 7.767   -39.930 -34.388  1.00 24.73  ? 409  GLY   D N   1 
ATOM   11063 C  CA  . GLY   D  1 108 ? 8.910   -39.945 -35.282  1.00 23.05  ? 409  GLY   D CA  1 
ATOM   11064 C  C   . GLY   D  1 108 ? 9.279   -41.336 -35.756  1.00 31.31  ? 409  GLY   D C   1 
ATOM   11065 O  O   . GLY   D  1 108 ? 9.568   -41.540 -36.942  1.00 22.02  ? 409  GLY   D O   1 
ATOM   11066 N  N   . ALA   D  1 109 ? 9.286   -42.311 -34.841  1.00 21.81  ? 410  ALA   D N   1 
ATOM   11067 C  CA  . ALA   D  1 109 ? 9.593   -43.683 -35.225  1.00 22.76  ? 410  ALA   D CA  1 
ATOM   11068 C  C   . ALA   D  1 109 ? 8.555   -44.219 -36.201  1.00 22.03  ? 410  ALA   D C   1 
ATOM   11069 O  O   . ALA   D  1 109 ? 8.898   -44.817 -37.226  1.00 26.66  ? 410  ALA   D O   1 
ATOM   11070 C  CB  . ALA   D  1 109 ? 9.676   -44.576 -33.975  1.00 18.65  ? 410  ALA   D CB  1 
ATOM   11071 N  N   . LYS   D  1 110 ? 7.275   -44.012 -35.901  1.00 21.48  ? 411  LYS   D N   1 
ATOM   11072 C  CA  . LYS   D  1 110 ? 6.244   -44.463 -36.824  1.00 26.89  ? 411  LYS   D CA  1 
ATOM   11073 C  C   . LYS   D  1 110 ? 6.407   -43.800 -38.182  1.00 27.28  ? 411  LYS   D C   1 
ATOM   11074 O  O   . LYS   D  1 110 ? 6.247   -44.450 -39.221  1.00 22.09  ? 411  LYS   D O   1 
ATOM   11075 C  CB  . LYS   D  1 110 ? 4.854   -44.181 -36.260  1.00 21.86  ? 411  LYS   D CB  1 
ATOM   11076 C  CG  . LYS   D  1 110 ? 4.504   -45.093 -35.083  1.00 22.23  ? 411  LYS   D CG  1 
ATOM   11077 C  CD  . LYS   D  1 110 ? 3.106   -44.826 -34.557  1.00 18.81  ? 411  LYS   D CD  1 
ATOM   11078 C  CE  . LYS   D  1 110 ? 2.776   -45.766 -33.387  1.00 22.68  ? 411  LYS   D CE  1 
ATOM   11079 N  NZ  . LYS   D  1 110 ? 1.352   -45.594 -33.004  1.00 27.77  ? 411  LYS   D NZ  1 
ATOM   11080 N  N   . HIS   D  1 111 ? 6.753   -42.518 -38.202  1.00 24.82  ? 412  HIS   D N   1 
ATOM   11081 C  CA  . HIS   D  1 111 ? 6.865   -41.872 -39.500  1.00 21.82  ? 412  HIS   D CA  1 
ATOM   11082 C  C   . HIS   D  1 111 ? 8.130   -42.260 -40.239  1.00 25.98  ? 412  HIS   D C   1 
ATOM   11083 O  O   . HIS   D  1 111 ? 8.105   -42.328 -41.476  1.00 22.83  ? 412  HIS   D O   1 
ATOM   11084 C  CB  . HIS   D  1 111 ? 6.733   -40.362 -39.358  1.00 25.07  ? 412  HIS   D CB  1 
ATOM   11085 C  CG  . HIS   D  1 111 ? 5.306   -39.936 -39.406  1.00 25.11  ? 412  HIS   D CG  1 
ATOM   11086 N  ND1 . HIS   D  1 111 ? 4.428   -40.206 -38.379  1.00 25.29  ? 412  HIS   D ND1 1 
ATOM   11087 C  CD2 . HIS   D  1 111 ? 4.567   -39.395 -40.404  1.00 24.79  ? 412  HIS   D CD2 1 
ATOM   11088 C  CE1 . HIS   D  1 111 ? 3.217   -39.801 -38.722  1.00 29.89  ? 412  HIS   D CE1 1 
ATOM   11089 N  NE2 . HIS   D  1 111 ? 3.275   -39.300 -39.943  1.00 28.98  ? 412  HIS   D NE2 1 
ATOM   11090 N  N   . ALA   D  1 112 ? 9.222   -42.553 -39.523  1.00 21.23  ? 413  ALA   D N   1 
ATOM   11091 C  CA  . ALA   D  1 112 ? 10.387  -43.107 -40.203  1.00 20.47  ? 413  ALA   D CA  1 
ATOM   11092 C  C   . ALA   D  1 112 ? 10.024  -44.390 -40.933  1.00 22.66  ? 413  ALA   D C   1 
ATOM   11093 O  O   . ALA   D  1 112 ? 10.434  -44.600 -42.082  1.00 19.91  ? 413  ALA   D O   1 
ATOM   11094 C  CB  . ALA   D  1 112 ? 11.505  -43.368 -39.211  1.00 21.35  ? 413  ALA   D CB  1 
ATOM   11095 N  N   . TRP   D  1 113 ? 9.238   -45.253 -40.286  1.00 22.00  ? 414  TRP   D N   1 
ATOM   11096 C  CA  . TRP   D  1 113 ? 8.763   -46.455 -40.959  1.00 21.48  ? 414  TRP   D CA  1 
ATOM   11097 C  C   . TRP   D  1 113 ? 7.839   -46.096 -42.113  1.00 21.63  ? 414  TRP   D C   1 
ATOM   11098 O  O   . TRP   D  1 113 ? 7.968   -46.639 -43.208  1.00 20.97  ? 414  TRP   D O   1 
ATOM   11099 C  CB  . TRP   D  1 113 ? 8.055   -47.370 -39.959  1.00 17.62  ? 414  TRP   D CB  1 
ATOM   11100 C  CG  . TRP   D  1 113 ? 7.580   -48.680 -40.563  1.00 17.60  ? 414  TRP   D CG  1 
ATOM   11101 C  CD1 . TRP   D  1 113 ? 7.899   -49.183 -41.795  1.00 20.04  ? 414  TRP   D CD1 1 
ATOM   11102 C  CD2 . TRP   D  1 113 ? 6.714   -49.643 -39.947  1.00 17.10  ? 414  TRP   D CD2 1 
ATOM   11103 N  NE1 . TRP   D  1 113 ? 7.280   -50.391 -41.980  1.00 19.75  ? 414  TRP   D NE1 1 
ATOM   11104 C  CE2 . TRP   D  1 113 ? 6.552   -50.699 -40.857  1.00 21.82  ? 414  TRP   D CE2 1 
ATOM   11105 C  CE3 . TRP   D  1 113 ? 6.068   -49.717 -38.704  1.00 19.71  ? 414  TRP   D CE3 1 
ATOM   11106 C  CZ2 . TRP   D  1 113 ? 5.756   -51.814 -40.573  1.00 17.91  ? 414  TRP   D CZ2 1 
ATOM   11107 C  CZ3 . TRP   D  1 113 ? 5.272   -50.827 -38.425  1.00 25.23  ? 414  TRP   D CZ3 1 
ATOM   11108 C  CH2 . TRP   D  1 113 ? 5.129   -51.860 -39.354  1.00 25.20  ? 414  TRP   D CH2 1 
ATOM   11109 N  N   . ARG   D  1 114 ? 6.896   -45.186 -41.878  1.00 27.10  ? 415  ARG   D N   1 
ATOM   11110 C  CA  . ARG   D  1 114 ? 5.976   -44.782 -42.931  1.00 25.26  ? 415  ARG   D CA  1 
ATOM   11111 C  C   . ARG   D  1 114 ? 6.713   -44.238 -44.141  1.00 25.88  ? 415  ARG   D C   1 
ATOM   11112 O  O   . ARG   D  1 114 ? 6.249   -44.394 -45.282  1.00 23.74  ? 415  ARG   D O   1 
ATOM   11113 C  CB  . ARG   D  1 114 ? 5.018   -43.727 -42.388  1.00 23.36  ? 415  ARG   D CB  1 
ATOM   11114 C  CG  . ARG   D  1 114 ? 3.846   -43.434 -43.283  1.00 23.97  ? 415  ARG   D CG  1 
ATOM   11115 C  CD  . ARG   D  1 114 ? 3.140   -42.158 -42.847  1.00 23.36  ? 415  ARG   D CD  1 
ATOM   11116 N  NE  . ARG   D  1 114 ? 1.841   -42.049 -43.497  1.00 23.18  ? 415  ARG   D NE  1 
ATOM   11117 C  CZ  . ARG   D  1 114 ? 0.896   -41.198 -43.133  1.00 26.14  ? 415  ARG   D CZ  1 
ATOM   11118 N  NH1 . ARG   D  1 114 ? -0.259  -41.197 -43.784  1.00 24.51  ? 415  ARG   D NH1 1 
ATOM   11119 N  NH2 . ARG   D  1 114 ? 1.097   -40.382 -42.095  1.00 24.78  ? 415  ARG   D NH2 1 
ATOM   11120 N  N   . ASN   D  1 115 ? 7.862   -43.606 -43.914  1.00 22.62  ? 416  ASN   D N   1 
ATOM   11121 C  CA  . ASN   D  1 115 ? 8.631   -42.957 -44.961  1.00 25.05  ? 416  ASN   D CA  1 
ATOM   11122 C  C   . ASN   D  1 115 ? 9.647   -43.883 -45.603  1.00 26.03  ? 416  ASN   D C   1 
ATOM   11123 O  O   . ASN   D  1 115 ? 10.372  -43.446 -46.499  1.00 24.48  ? 416  ASN   D O   1 
ATOM   11124 C  CB  . ASN   D  1 115 ? 9.350   -41.730 -44.389  1.00 18.59  ? 416  ASN   D CB  1 
ATOM   11125 C  CG  . ASN   D  1 115 ? 8.393   -40.660 -43.955  1.00 20.44  ? 416  ASN   D CG  1 
ATOM   11126 O  OD1 . ASN   D  1 115 ? 7.245   -40.639 -44.392  1.00 24.63  ? 416  ASN   D OD1 1 
ATOM   11127 N  ND2 . ASN   D  1 115 ? 8.854   -39.753 -43.082  1.00 25.45  ? 416  ASN   D ND2 1 
ATOM   11128 N  N   . ALA   D  1 116 ? 9.738   -45.131 -45.153  1.00 19.87  ? 417  ALA   D N   1 
ATOM   11129 C  CA  . ALA   D  1 116 ? 10.787  -46.027 -45.625  1.00 23.15  ? 417  ALA   D CA  1 
ATOM   11130 C  C   . ALA   D  1 116 ? 10.402  -46.532 -47.014  1.00 18.72  ? 417  ALA   D C   1 
ATOM   11131 O  O   . ALA   D  1 116 ? 9.618   -47.477 -47.160  1.00 19.99  ? 417  ALA   D O   1 
ATOM   11132 C  CB  . ALA   D  1 116 ? 11.000  -47.168 -44.637  1.00 16.81  ? 417  ALA   D CB  1 
ATOM   11133 N  N   . SER   D  1 117 ? 10.966  -45.905 -48.037  1.00 21.40  ? 418  SER   D N   1 
ATOM   11134 C  CA  A SER   D  1 117 ? 10.520  -46.192 -49.395  0.59 20.69  ? 418  SER   D CA  1 
ATOM   11135 C  CA  B SER   D  1 117 ? 10.558  -46.184 -49.412  0.41 20.87  ? 418  SER   D CA  1 
ATOM   11136 C  C   . SER   D  1 117 ? 10.772  -47.641 -49.789  1.00 23.12  ? 418  SER   D C   1 
ATOM   11137 O  O   . SER   D  1 117 ? 10.052  -48.180 -50.636  1.00 26.28  ? 418  SER   D O   1 
ATOM   11138 C  CB  A SER   D  1 117 ? 11.211  -45.256 -50.374  0.59 21.19  ? 418  SER   D CB  1 
ATOM   11139 C  CB  B SER   D  1 117 ? 11.333  -45.289 -50.374  0.41 20.57  ? 418  SER   D CB  1 
ATOM   11140 O  OG  A SER   D  1 117 ? 12.585  -45.561 -50.437  0.59 19.85  ? 418  SER   D OG  1 
ATOM   11141 O  OG  B SER   D  1 117 ? 11.188  -43.928 -50.023  0.41 21.24  ? 418  SER   D OG  1 
ATOM   11142 N  N   . ARG   D  1 118 ? 11.766  -48.290 -49.192  1.00 19.29  ? 419  ARG   D N   1 
ATOM   11143 C  CA  . ARG   D  1 118 ? 12.098  -49.656 -49.558  1.00 21.76  ? 419  ARG   D CA  1 
ATOM   11144 C  C   . ARG   D  1 118 ? 11.266  -50.716 -48.862  1.00 27.57  ? 419  ARG   D C   1 
ATOM   11145 O  O   . ARG   D  1 118 ? 11.493  -51.900 -49.123  1.00 20.65  ? 419  ARG   D O   1 
ATOM   11146 C  CB  . ARG   D  1 118 ? 13.571  -49.913 -49.277  1.00 19.38  ? 419  ARG   D CB  1 
ATOM   11147 C  CG  . ARG   D  1 118 ? 14.460  -49.053 -50.168  1.00 21.89  ? 419  ARG   D CG  1 
ATOM   11148 C  CD  . ARG   D  1 118 ? 15.905  -49.251 -49.794  1.00 21.41  ? 419  ARG   D CD  1 
ATOM   11149 N  NE  . ARG   D  1 118 ? 16.781  -48.763 -50.842  1.00 25.57  ? 419  ARG   D NE  1 
ATOM   11150 C  CZ  . ARG   D  1 118 ? 18.100  -48.720 -50.730  1.00 30.81  ? 419  ARG   D CZ  1 
ATOM   11151 N  NH1 . ARG   D  1 118 ? 18.667  -49.130 -49.603  1.00 27.98  ? 419  ARG   D NH1 1 
ATOM   11152 N  NH2 . ARG   D  1 118 ? 18.845  -48.271 -51.727  1.00 29.02  ? 419  ARG   D NH2 1 
ATOM   11153 N  N   . CYS   D  1 119 ? 10.326  -50.348 -47.988  1.00 21.37  ? 420  CYS   D N   1 
ATOM   11154 C  CA  . CYS   D  1 119 ? 9.639   -51.324 -47.160  1.00 17.82  ? 420  CYS   D CA  1 
ATOM   11155 C  C   . CYS   D  1 119 ? 8.262   -51.608 -47.734  1.00 15.19  ? 420  CYS   D C   1 
ATOM   11156 O  O   . CYS   D  1 119 ? 7.408   -50.718 -47.779  1.00 18.06  ? 420  CYS   D O   1 
ATOM   11157 C  CB  . CYS   D  1 119 ? 9.524   -50.843 -45.704  1.00 19.35  ? 420  CYS   D CB  1 
ATOM   11158 S  SG  . CYS   D  1 119 ? 8.498   -51.923 -44.689  1.00 22.89  ? 420  CYS   D SG  1 
ATOM   11159 N  N   . VAL   D  1 120 ? 8.038   -52.866 -48.123  1.00 21.15  ? 421  VAL   D N   1 
ATOM   11160 C  CA  . VAL   D  1 120 ? 6.745   -53.309 -48.646  1.00 21.41  ? 421  VAL   D CA  1 
ATOM   11161 C  C   . VAL   D  1 120 ? 5.721   -53.527 -47.550  1.00 24.02  ? 421  VAL   D C   1 
ATOM   11162 O  O   . VAL   D  1 120 ? 4.528   -53.661 -47.848  1.00 21.26  ? 421  VAL   D O   1 
ATOM   11163 C  CB  . VAL   D  1 120 ? 6.926   -54.601 -49.480  1.00 23.01  ? 421  VAL   D CB  1 
ATOM   11164 C  CG1 . VAL   D  1 120 ? 7.214   -55.797 -48.580  1.00 21.17  ? 421  VAL   D CG1 1 
ATOM   11165 C  CG2 . VAL   D  1 120 ? 5.708   -54.888 -50.354  1.00 25.77  ? 421  VAL   D CG2 1 
ATOM   11166 N  N   . GLY   D  1 121 ? 6.142   -53.556 -46.284  1.00 25.59  ? 422  GLY   D N   1 
ATOM   11167 C  CA  . GLY   D  1 121 ? 5.210   -53.838 -45.215  1.00 26.85  ? 422  GLY   D CA  1 
ATOM   11168 C  C   . GLY   D  1 121 ? 4.547   -52.628 -44.588  1.00 29.56  ? 422  GLY   D C   1 
ATOM   11169 O  O   . GLY   D  1 121 ? 3.912   -52.769 -43.542  1.00 23.51  ? 422  GLY   D O   1 
ATOM   11170 N  N   . ARG   D  1 122 ? 4.640   -51.448 -45.203  1.00 26.18  ? 423  ARG   D N   1 
ATOM   11171 C  CA  . ARG   D  1 122 ? 4.271   -50.222 -44.503  1.00 23.52  ? 423  ARG   D CA  1 
ATOM   11172 C  C   . ARG   D  1 122 ? 2.776   -50.019 -44.331  1.00 29.01  ? 423  ARG   D C   1 
ATOM   11173 O  O   . ARG   D  1 122 ? 2.390   -49.041 -43.682  1.00 23.10  ? 423  ARG   D O   1 
ATOM   11174 C  CB  . ARG   D  1 122 ? 4.843   -49.007 -45.225  1.00 21.39  ? 423  ARG   D CB  1 
ATOM   11175 C  CG  . ARG   D  1 122 ? 6.327   -48.790 -44.999  1.00 22.24  ? 423  ARG   D CG  1 
ATOM   11176 C  CD  . ARG   D  1 122 ? 6.751   -47.622 -45.833  1.00 19.83  ? 423  ARG   D CD  1 
ATOM   11177 N  NE  . ARG   D  1 122 ? 6.881   -47.997 -47.241  1.00 22.04  ? 423  ARG   D NE  1 
ATOM   11178 C  CZ  . ARG   D  1 122 ? 6.958   -47.124 -48.239  1.00 24.27  ? 423  ARG   D CZ  1 
ATOM   11179 N  NH1 . ARG   D  1 122 ? 6.884   -45.824 -47.980  1.00 19.51  ? 423  ARG   D NH1 1 
ATOM   11180 N  NH2 . ARG   D  1 122 ? 7.116   -47.551 -49.491  1.00 19.98  ? 423  ARG   D NH2 1 
ATOM   11181 N  N   . ILE   D  1 123 ? 1.913   -50.885 -44.868  1.00 20.08  ? 424  ILE   D N   1 
ATOM   11182 C  CA  . ILE   D  1 123 ? 0.506   -50.717 -44.537  1.00 24.57  ? 424  ILE   D CA  1 
ATOM   11183 C  C   . ILE   D  1 123 ? 0.300   -50.795 -43.019  1.00 29.99  ? 424  ILE   D C   1 
ATOM   11184 O  O   . ILE   D  1 123 ? -0.662  -50.232 -42.481  1.00 20.60  ? 424  ILE   D O   1 
ATOM   11185 C  CB  . ILE   D  1 123 ? -0.357  -51.749 -45.280  1.00 28.00  ? 424  ILE   D CB  1 
ATOM   11186 C  CG1 . ILE   D  1 123 ? -1.815  -51.269 -45.307  1.00 28.20  ? 424  ILE   D CG1 1 
ATOM   11187 C  CG2 . ILE   D  1 123 ? -0.223  -53.138 -44.641  1.00 25.83  ? 424  ILE   D CG2 1 
ATOM   11188 C  CD1 . ILE   D  1 123 ? -2.689  -52.076 -46.216  1.00 34.30  ? 424  ILE   D CD1 1 
ATOM   11189 N  N   . GLN   D  1 124 ? 1.233   -51.419 -42.314  1.00 22.70  ? 425  GLN   D N   1 
ATOM   11190 C  CA  . GLN   D  1 124 ? 1.194   -51.602 -40.870  1.00 32.20  ? 425  GLN   D CA  1 
ATOM   11191 C  C   . GLN   D  1 124 ? 1.766   -50.429 -40.075  1.00 28.48  ? 425  GLN   D C   1 
ATOM   11192 O  O   . GLN   D  1 124 ? 1.772   -50.500 -38.841  1.00 26.18  ? 425  GLN   D O   1 
ATOM   11193 C  CB  . GLN   D  1 124 ? 1.980   -52.870 -40.502  1.00 30.15  ? 425  GLN   D CB  1 
ATOM   11194 C  CG  . GLN   D  1 124 ? 1.367   -54.161 -41.001  1.00 34.73  ? 425  GLN   D CG  1 
ATOM   11195 C  CD  . GLN   D  1 124 ? 0.179   -54.559 -40.159  1.00 44.64  ? 425  GLN   D CD  1 
ATOM   11196 O  OE1 . GLN   D  1 124 ? 0.169   -54.340 -38.945  1.00 46.15  ? 425  GLN   D OE1 1 
ATOM   11197 N  NE2 . GLN   D  1 124 ? -0.838  -55.132 -40.795  1.00 41.27  ? 425  GLN   D NE2 1 
ATOM   11198 N  N   . TRP   D  1 125 ? 2.240   -49.366 -40.739  1.00 25.06  ? 426  TRP   D N   1 
ATOM   11199 C  CA  . TRP   D  1 125 ? 3.204   -48.447 -40.124  1.00 19.16  ? 426  TRP   D CA  1 
ATOM   11200 C  C   . TRP   D  1 125 ? 2.700   -47.847 -38.813  1.00 22.78  ? 426  TRP   D C   1 
ATOM   11201 O  O   . TRP   D  1 125 ? 3.494   -47.588 -37.902  1.00 32.10  ? 426  TRP   D O   1 
ATOM   11202 C  CB  . TRP   D  1 125 ? 3.559   -47.320 -41.090  1.00 23.20  ? 426  TRP   D CB  1 
ATOM   11203 C  CG  . TRP   D  1 125 ? 2.412   -46.372 -41.335  1.00 23.56  ? 426  TRP   D CG  1 
ATOM   11204 C  CD1 . TRP   D  1 125 ? 1.455   -46.488 -42.294  1.00 25.90  ? 426  TRP   D CD1 1 
ATOM   11205 C  CD2 . TRP   D  1 125 ? 2.109   -45.170 -40.609  1.00 21.65  ? 426  TRP   D CD2 1 
ATOM   11206 N  NE1 . TRP   D  1 125 ? 0.573   -45.438 -42.209  1.00 27.62  ? 426  TRP   D NE1 1 
ATOM   11207 C  CE2 . TRP   D  1 125 ? 0.950   -44.617 -41.183  1.00 25.07  ? 426  TRP   D CE2 1 
ATOM   11208 C  CE3 . TRP   D  1 125 ? 2.700   -44.517 -39.522  1.00 25.59  ? 426  TRP   D CE3 1 
ATOM   11209 C  CZ2 . TRP   D  1 125 ? 0.376   -43.439 -40.722  1.00 23.17  ? 426  TRP   D CZ2 1 
ATOM   11210 C  CZ3 . TRP   D  1 125 ? 2.123   -43.344 -39.056  1.00 28.48  ? 426  TRP   D CZ3 1 
ATOM   11211 C  CH2 . TRP   D  1 125 ? 0.970   -42.820 -39.652  1.00 27.57  ? 426  TRP   D CH2 1 
ATOM   11212 N  N   . SER   D  1 126 ? 1.405   -47.568 -38.706  1.00 26.90  ? 427  SER   D N   1 
ATOM   11213 C  CA  . SER   D  1 126 ? 0.941   -46.900 -37.500  1.00 35.67  ? 427  SER   D CA  1 
ATOM   11214 C  C   . SER   D  1 126 ? 0.758   -47.867 -36.338  1.00 32.78  ? 427  SER   D C   1 
ATOM   11215 O  O   . SER   D  1 126 ? 0.583   -47.423 -35.196  1.00 30.91  ? 427  SER   D O   1 
ATOM   11216 C  CB  . SER   D  1 126 ? -0.362  -46.151 -37.779  1.00 32.73  ? 427  SER   D CB  1 
ATOM   11217 O  OG  . SER   D  1 126 ? -1.401  -47.061 -38.077  1.00 34.90  ? 427  SER   D OG  1 
ATOM   11218 N  N   . LYS   D  1 127 ? 0.803   -49.168 -36.610  1.00 30.83  ? 428  LYS   D N   1 
ATOM   11219 C  CA  . LYS   D  1 127 ? 0.702   -50.202 -35.583  1.00 35.62  ? 428  LYS   D CA  1 
ATOM   11220 C  C   . LYS   D  1 127 ? 2.116   -50.681 -35.257  1.00 49.04  ? 428  LYS   D C   1 
ATOM   11221 O  O   . LYS   D  1 127 ? 2.586   -51.727 -35.705  1.00 66.97  ? 428  LYS   D O   1 
ATOM   11222 C  CB  . LYS   D  1 127 ? -0.206  -51.331 -36.075  1.00 33.32  ? 428  LYS   D CB  1 
ATOM   11223 C  CG  . LYS   D  1 127 ? -0.350  -52.537 -35.157  1.00 59.32  ? 428  LYS   D CG  1 
ATOM   11224 C  CD  . LYS   D  1 127 ? -1.188  -53.638 -35.819  1.00 65.05  ? 428  LYS   D CD  1 
ATOM   11225 C  CE  . LYS   D  1 127 ? -1.539  -54.747 -34.831  1.00 67.87  ? 428  LYS   D CE  1 
ATOM   11226 N  NZ  . LYS   D  1 127 ? -2.949  -55.227 -34.978  1.00 70.04  ? 428  LYS   D NZ  1 
ATOM   11227 N  N   . LEU   D  1 128 ? 2.821   -49.846 -34.509  1.00 33.36  ? 429  LEU   D N   1 
ATOM   11228 C  CA  . LEU   D  1 128 ? 4.226   -50.061 -34.201  1.00 18.38  ? 429  LEU   D CA  1 
ATOM   11229 C  C   . LEU   D  1 128 ? 4.393   -49.862 -32.710  1.00 23.12  ? 429  LEU   D C   1 
ATOM   11230 O  O   . LEU   D  1 128 ? 3.979   -48.830 -32.184  1.00 25.29  ? 429  LEU   D O   1 
ATOM   11231 C  CB  . LEU   D  1 128 ? 5.141   -49.081 -34.947  1.00 16.89  ? 429  LEU   D CB  1 
ATOM   11232 C  CG  . LEU   D  1 128 ? 6.602   -49.146 -34.479  1.00 18.25  ? 429  LEU   D CG  1 
ATOM   11233 C  CD1 . LEU   D  1 128 ? 7.225   -50.474 -34.891  1.00 16.13  ? 429  LEU   D CD1 1 
ATOM   11234 C  CD2 . LEU   D  1 128 ? 7.446   -47.977 -35.001  1.00 19.10  ? 429  LEU   D CD2 1 
ATOM   11235 N  N   . GLN   D  1 129 ? 4.965   -50.837 -32.026  1.00 22.40  ? 430  GLN   D N   1 
ATOM   11236 C  CA  . GLN   D  1 129 ? 5.184   -50.694 -30.594  1.00 22.78  ? 430  GLN   D CA  1 
ATOM   11237 C  C   . GLN   D  1 129 ? 6.544   -50.038 -30.408  1.00 20.65  ? 430  GLN   D C   1 
ATOM   11238 O  O   . GLN   D  1 129 ? 7.546   -50.525 -30.940  1.00 28.99  ? 430  GLN   D O   1 
ATOM   11239 C  CB  . GLN   D  1 129 ? 5.105   -52.050 -29.896  1.00 23.46  ? 430  GLN   D CB  1 
ATOM   11240 C  CG  . GLN   D  1 129 ? 5.235   -51.969 -28.383  1.00 32.73  ? 430  GLN   D CG  1 
ATOM   11241 C  CD  . GLN   D  1 129 ? 4.134   -51.157 -27.754  1.00 38.36  ? 430  GLN   D CD  1 
ATOM   11242 O  OE1 . GLN   D  1 129 ? 3.006   -51.131 -28.243  1.00 43.72  ? 430  GLN   D OE1 1 
ATOM   11243 N  NE2 . GLN   D  1 129 ? 4.458   -50.476 -26.667  1.00 51.71  ? 430  GLN   D NE2 1 
ATOM   11244 N  N   . VAL   D  1 130 ? 6.578   -48.918 -29.697  1.00 23.22  ? 431  VAL   D N   1 
ATOM   11245 C  CA  . VAL   D  1 130 ? 7.808   -48.156 -29.512  1.00 23.18  ? 431  VAL   D CA  1 
ATOM   11246 C  C   . VAL   D  1 130 ? 8.266   -48.320 -28.066  1.00 25.46  ? 431  VAL   D C   1 
ATOM   11247 O  O   . VAL   D  1 130 ? 7.561   -47.923 -27.133  1.00 29.64  ? 431  VAL   D O   1 
ATOM   11248 C  CB  . VAL   D  1 130 ? 7.619   -46.675 -29.869  1.00 21.43  ? 431  VAL   D CB  1 
ATOM   11249 C  CG1 . VAL   D  1 130 ? 8.902   -45.895 -29.572  1.00 24.97  ? 431  VAL   D CG1 1 
ATOM   11250 C  CG2 . VAL   D  1 130 ? 7.198   -46.533 -31.355  1.00 20.32  ? 431  VAL   D CG2 1 
ATOM   11251 N  N   . PHE   D  1 131 ? 9.452   -48.890 -27.883  1.00 26.26  ? 432  PHE   D N   1 
ATOM   11252 C  CA  . PHE   D  1 131 ? 10.054  -49.030 -26.566  1.00 26.75  ? 432  PHE   D CA  1 
ATOM   11253 C  C   . PHE   D  1 131 ? 11.115  -47.956 -26.415  1.00 22.58  ? 432  PHE   D C   1 
ATOM   11254 O  O   . PHE   D  1 131 ? 12.124  -47.963 -27.122  1.00 26.77  ? 432  PHE   D O   1 
ATOM   11255 C  CB  . PHE   D  1 131 ? 10.637  -50.423 -26.378  1.00 21.98  ? 432  PHE   D CB  1 
ATOM   11256 C  CG  . PHE   D  1 131 ? 9.609   -51.495 -26.435  1.00 26.21  ? 432  PHE   D CG  1 
ATOM   11257 C  CD1 . PHE   D  1 131 ? 8.593   -51.544 -25.491  1.00 24.36  ? 432  PHE   D CD1 1 
ATOM   11258 C  CD2 . PHE   D  1 131 ? 9.643   -52.453 -27.438  1.00 23.84  ? 432  PHE   D CD2 1 
ATOM   11259 C  CE1 . PHE   D  1 131 ? 7.634   -52.542 -25.541  1.00 32.08  ? 432  PHE   D CE1 1 
ATOM   11260 C  CE2 . PHE   D  1 131 ? 8.690   -53.447 -27.493  1.00 28.79  ? 432  PHE   D CE2 1 
ATOM   11261 C  CZ  . PHE   D  1 131 ? 7.682   -53.498 -26.550  1.00 28.10  ? 432  PHE   D CZ  1 
ATOM   11262 N  N   . ASP   D  1 132 ? 10.870  -47.029 -25.502  1.00 24.90  ? 433  ASP   D N   1 
ATOM   11263 C  CA  . ASP   D  1 132 ? 11.800  -45.946 -25.227  1.00 27.81  ? 433  ASP   D CA  1 
ATOM   11264 C  C   . ASP   D  1 132 ? 12.877  -46.496 -24.306  1.00 32.22  ? 433  ASP   D C   1 
ATOM   11265 O  O   . ASP   D  1 132 ? 12.613  -46.798 -23.141  1.00 29.33  ? 433  ASP   D O   1 
ATOM   11266 C  CB  . ASP   D  1 132 ? 11.048  -44.776 -24.599  1.00 27.21  ? 433  ASP   D CB  1 
ATOM   11267 C  CG  . ASP   D  1 132 ? 11.938  -43.598 -24.261  1.00 29.51  ? 433  ASP   D CG  1 
ATOM   11268 O  OD1 . ASP   D  1 132 ? 11.364  -42.582 -23.828  1.00 34.79  ? 433  ASP   D OD1 1 
ATOM   11269 O  OD2 . ASP   D  1 132 ? 13.179  -43.659 -24.428  1.00 26.42  ? 433  ASP   D OD2 1 
ATOM   11270 N  N   . ALA   D  1 133 ? 14.083  -46.660 -24.828  1.00 32.17  ? 434  ALA   D N   1 
ATOM   11271 C  CA  . ALA   D  1 133 ? 15.203  -47.118 -24.023  1.00 24.46  ? 434  ALA   D CA  1 
ATOM   11272 C  C   . ALA   D  1 133 ? 16.250  -46.022 -23.868  1.00 26.01  ? 434  ALA   D C   1 
ATOM   11273 O  O   . ALA   D  1 133 ? 17.440  -46.307 -23.700  1.00 23.21  ? 434  ALA   D O   1 
ATOM   11274 C  CB  . ALA   D  1 133 ? 15.809  -48.389 -24.624  1.00 20.48  ? 434  ALA   D CB  1 
ATOM   11275 N  N   . ARG   D  1 134 ? 15.818  -44.759 -23.913  1.00 21.32  ? 435  ARG   D N   1 
ATOM   11276 C  CA  . ARG   D  1 134 ? 16.779  -43.665 -23.826  1.00 24.05  ? 435  ARG   D CA  1 
ATOM   11277 C  C   . ARG   D  1 134 ? 17.363  -43.481 -22.424  1.00 24.36  ? 435  ARG   D C   1 
ATOM   11278 O  O   . ARG   D  1 134 ? 18.277  -42.665 -22.252  1.00 26.15  ? 435  ARG   D O   1 
ATOM   11279 C  CB  . ARG   D  1 134 ? 16.120  -42.385 -24.304  1.00 24.94  ? 435  ARG   D CB  1 
ATOM   11280 C  CG  . ARG   D  1 134 ? 15.775  -42.435 -25.794  1.00 24.57  ? 435  ARG   D CG  1 
ATOM   11281 C  CD  . ARG   D  1 134 ? 14.999  -41.204 -26.178  1.00 25.86  ? 435  ARG   D CD  1 
ATOM   11282 N  NE  . ARG   D  1 134 ? 13.698  -41.176 -25.530  1.00 25.20  ? 435  ARG   D NE  1 
ATOM   11283 C  CZ  . ARG   D  1 134 ? 12.919  -40.103 -25.476  1.00 27.68  ? 435  ARG   D CZ  1 
ATOM   11284 N  NH1 . ARG   D  1 134 ? 13.314  -38.956 -26.024  1.00 29.29  ? 435  ARG   D NH1 1 
ATOM   11285 N  NH2 . ARG   D  1 134 ? 11.745  -40.170 -24.866  1.00 25.00  ? 435  ARG   D NH2 1 
ATOM   11286 N  N   . ASP   D  1 135 ? 16.894  -44.230 -21.431  1.00 22.98  ? 436  ASP   D N   1 
ATOM   11287 C  CA  . ASP   D  1 135 ? 17.477  -44.175 -20.093  1.00 25.53  ? 436  ASP   D CA  1 
ATOM   11288 C  C   . ASP   D  1 135 ? 18.586  -45.202 -19.917  1.00 31.88  ? 436  ASP   D C   1 
ATOM   11289 O  O   . ASP   D  1 135 ? 19.203  -45.268 -18.847  1.00 32.41  ? 436  ASP   D O   1 
ATOM   11290 C  CB  . ASP   D  1 135 ? 16.392  -44.380 -19.037  1.00 25.22  ? 436  ASP   D CB  1 
ATOM   11291 C  CG  . ASP   D  1 135 ? 15.808  -45.785 -19.062  1.00 37.99  ? 436  ASP   D CG  1 
ATOM   11292 O  OD1 . ASP   D  1 135 ? 15.043  -46.133 -18.140  1.00 34.99  ? 436  ASP   D OD1 1 
ATOM   11293 O  OD2 . ASP   D  1 135 ? 16.114  -46.548 -20.002  1.00 39.66  ? 436  ASP   D OD2 1 
ATOM   11294 N  N   . CYS   D  1 136 ? 18.844  -45.999 -20.948  1.00 28.70  ? 437  CYS   D N   1 
ATOM   11295 C  CA  . CYS   D  1 136 ? 19.827  -47.067 -20.870  1.00 27.27  ? 437  CYS   D CA  1 
ATOM   11296 C  C   . CYS   D  1 136 ? 21.243  -46.492 -20.783  1.00 33.91  ? 437  CYS   D C   1 
ATOM   11297 O  O   . CYS   D  1 136 ? 21.556  -45.476 -21.410  1.00 35.02  ? 437  CYS   D O   1 
ATOM   11298 C  CB  . CYS   D  1 136 ? 19.670  -47.969 -22.098  1.00 25.85  ? 437  CYS   D CB  1 
ATOM   11299 S  SG  . CYS   D  1 136 ? 20.679  -49.423 -22.097  1.00 31.69  ? 437  CYS   D SG  1 
ATOM   11300 N  N   . THR   D  1 137 ? 22.108  -47.130 -19.984  1.00 29.31  ? 438  THR   D N   1 
ATOM   11301 C  CA  . THR   D  1 137 ? 23.473  -46.635 -19.831  1.00 25.63  ? 438  THR   D CA  1 
ATOM   11302 C  C   . THR   D  1 137 ? 24.565  -47.663 -20.075  1.00 26.34  ? 438  THR   D C   1 
ATOM   11303 O  O   . THR   D  1 137 ? 25.724  -47.264 -20.216  1.00 31.78  ? 438  THR   D O   1 
ATOM   11304 C  CB  . THR   D  1 137 ? 23.688  -46.040 -18.427  1.00 33.45  ? 438  THR   D CB  1 
ATOM   11305 O  OG1 . THR   D  1 137 ? 23.668  -47.081 -17.438  1.00 35.41  ? 438  THR   D OG1 1 
ATOM   11306 C  CG2 . THR   D  1 137 ? 22.613  -45.008 -18.106  1.00 30.72  ? 438  THR   D CG2 1 
ATOM   11307 N  N   . THR   D  1 138 ? 24.260  -48.956 -20.117  1.00 27.68  ? 439  THR   D N   1 
ATOM   11308 C  CA  . THR   D  1 138 ? 25.299  -49.970 -20.238  1.00 24.53  ? 439  THR   D CA  1 
ATOM   11309 C  C   . THR   D  1 138 ? 24.859  -51.028 -21.235  1.00 23.75  ? 439  THR   D C   1 
ATOM   11310 O  O   . THR   D  1 138 ? 23.666  -51.190 -21.521  1.00 24.97  ? 439  THR   D O   1 
ATOM   11311 C  CB  . THR   D  1 138 ? 25.598  -50.664 -18.901  1.00 28.51  ? 439  THR   D CB  1 
ATOM   11312 O  OG1 . THR   D  1 138 ? 24.468  -51.471 -18.554  1.00 28.54  ? 439  THR   D OG1 1 
ATOM   11313 C  CG2 . THR   D  1 138 ? 25.857  -49.646 -17.797  1.00 26.10  ? 439  THR   D CG2 1 
ATOM   11314 N  N   . ALA   D  1 139 ? 25.843  -51.768 -21.754  1.00 30.92  ? 440  ALA   D N   1 
ATOM   11315 C  CA  . ALA   D  1 139 ? 25.522  -52.858 -22.667  1.00 31.81  ? 440  ALA   D CA  1 
ATOM   11316 C  C   . ALA   D  1 139 ? 24.613  -53.879 -22.001  1.00 26.67  ? 440  ALA   D C   1 
ATOM   11317 O  O   . ALA   D  1 139 ? 23.767  -54.486 -22.667  1.00 22.66  ? 440  ALA   D O   1 
ATOM   11318 C  CB  . ALA   D  1 139 ? 26.805  -53.526 -23.169  1.00 33.05  ? 440  ALA   D CB  1 
ATOM   11319 N  N   . HIS   D  1 140 ? 24.771  -54.080 -20.687  1.00 28.04  ? 441  HIS   D N   1 
ATOM   11320 C  CA  . HIS   D  1 140 ? 23.880  -54.988 -19.969  1.00 26.73  ? 441  HIS   D CA  1 
ATOM   11321 C  C   . HIS   D  1 140 ? 22.442  -54.504 -20.034  1.00 23.09  ? 441  HIS   D C   1 
ATOM   11322 O  O   . HIS   D  1 140 ? 21.527  -55.292 -20.282  1.00 28.15  ? 441  HIS   D O   1 
ATOM   11323 C  CB  . HIS   D  1 140 ? 24.312  -55.128 -18.506  1.00 24.94  ? 441  HIS   D CB  1 
ATOM   11324 C  CG  . HIS   D  1 140 ? 25.352  -56.175 -18.270  1.00 27.45  ? 441  HIS   D CG  1 
ATOM   11325 N  ND1 . HIS   D  1 140 ? 26.700  -55.923 -18.385  1.00 34.80  ? 441  HIS   D ND1 1 
ATOM   11326 C  CD2 . HIS   D  1 140 ? 25.243  -57.470 -17.887  1.00 32.88  ? 441  HIS   D CD2 1 
ATOM   11327 C  CE1 . HIS   D  1 140 ? 27.379  -57.020 -18.093  1.00 37.28  ? 441  HIS   D CE1 1 
ATOM   11328 N  NE2 . HIS   D  1 140 ? 26.517  -57.973 -17.788  1.00 37.32  ? 441  HIS   D NE2 1 
ATOM   11329 N  N   . GLY   D  1 141 ? 22.217  -53.213 -19.764  1.00 22.98  ? 442  GLY   D N   1 
ATOM   11330 C  CA  . GLY   D  1 141 ? 20.881  -52.663 -19.951  1.00 25.98  ? 442  GLY   D CA  1 
ATOM   11331 C  C   . GLY   D  1 141 ? 20.378  -52.805 -21.381  1.00 25.26  ? 442  GLY   D C   1 
ATOM   11332 O  O   . GLY   D  1 141 ? 19.198  -53.095 -21.611  1.00 24.42  ? 442  GLY   D O   1 
ATOM   11333 N  N   . MET   D  1 142 ? 21.264  -52.595 -22.361  1.00 25.51  ? 443  MET   D N   1 
ATOM   11334 C  CA  . MET   D  1 142 ? 20.884  -52.802 -23.760  1.00 23.03  ? 443  MET   D CA  1 
ATOM   11335 C  C   . MET   D  1 142 ? 20.427  -54.233 -23.992  1.00 25.26  ? 443  MET   D C   1 
ATOM   11336 O  O   . MET   D  1 142 ? 19.428  -54.472 -24.678  1.00 25.39  ? 443  MET   D O   1 
ATOM   11337 C  CB  . MET   D  1 142 ? 22.052  -52.479 -24.685  1.00 28.24  ? 443  MET   D CB  1 
ATOM   11338 C  CG  . MET   D  1 142 ? 22.444  -51.038 -24.717  1.00 26.88  ? 443  MET   D CG  1 
ATOM   11339 S  SD  . MET   D  1 142 ? 23.862  -50.805 -25.825  1.00 29.53  ? 443  MET   D SD  1 
ATOM   11340 C  CE  . MET   D  1 142 ? 23.197  -51.194 -27.453  1.00 22.17  ? 443  MET   D CE  1 
ATOM   11341 N  N   . PHE   D  1 143 ? 21.151  -55.201 -23.421  1.00 31.52  ? 444  PHE   D N   1 
ATOM   11342 C  CA  . PHE   D  1 143 ? 20.755  -56.599 -23.545  1.00 26.90  ? 444  PHE   D CA  1 
ATOM   11343 C  C   . PHE   D  1 143 ? 19.366  -56.832 -22.964  1.00 32.33  ? 444  PHE   D C   1 
ATOM   11344 O  O   . PHE   D  1 143 ? 18.529  -57.509 -23.572  1.00 28.87  ? 444  PHE   D O   1 
ATOM   11345 C  CB  . PHE   D  1 143 ? 21.786  -57.481 -22.850  1.00 24.00  ? 444  PHE   D CB  1 
ATOM   11346 C  CG  . PHE   D  1 143 ? 21.375  -58.912 -22.747  1.00 29.77  ? 444  PHE   D CG  1 
ATOM   11347 C  CD1 . PHE   D  1 143 ? 21.027  -59.459 -21.522  1.00 29.24  ? 444  PHE   D CD1 1 
ATOM   11348 C  CD2 . PHE   D  1 143 ? 21.309  -59.707 -23.881  1.00 29.41  ? 444  PHE   D CD2 1 
ATOM   11349 C  CE1 . PHE   D  1 143 ? 20.642  -60.789 -21.420  1.00 29.34  ? 444  PHE   D CE1 1 
ATOM   11350 C  CE2 . PHE   D  1 143 ? 20.938  -61.032 -23.787  1.00 25.24  ? 444  PHE   D CE2 1 
ATOM   11351 C  CZ  . PHE   D  1 143 ? 20.597  -61.574 -22.558  1.00 28.85  ? 444  PHE   D CZ  1 
ATOM   11352 N  N   . ASN   D  1 144 ? 19.110  -56.280 -21.776  1.00 24.19  ? 445  ASN   D N   1 
ATOM   11353 C  CA  . ASN   D  1 144 ? 17.792  -56.400 -21.156  1.00 21.94  ? 445  ASN   D CA  1 
ATOM   11354 C  C   . ASN   D  1 144 ? 16.703  -55.835 -22.066  1.00 20.26  ? 445  ASN   D C   1 
ATOM   11355 O  O   . ASN   D  1 144 ? 15.670  -56.478 -22.305  1.00 21.64  ? 445  ASN   D O   1 
ATOM   11356 C  CB  . ASN   D  1 144 ? 17.804  -55.674 -19.806  1.00 25.72  ? 445  ASN   D CB  1 
ATOM   11357 C  CG  . ASN   D  1 144 ? 16.516  -55.853 -19.031  1.00 36.62  ? 445  ASN   D CG  1 
ATOM   11358 O  OD1 . ASN   D  1 144 ? 15.954  -56.945 -19.002  1.00 41.20  ? 445  ASN   D OD1 1 
ATOM   11359 N  ND2 . ASN   D  1 144 ? 16.048  -54.788 -18.386  1.00 36.74  ? 445  ASN   D ND2 1 
ATOM   11360 N  N   . TYR   D  1 145 ? 16.919  -54.620 -22.575  1.00 19.92  ? 446  TYR   D N   1 
ATOM   11361 C  CA  . TYR   D  1 145 ? 15.946  -54.003 -23.477  1.00 32.83  ? 446  TYR   D CA  1 
ATOM   11362 C  C   . TYR   D  1 145 ? 15.724  -54.839 -24.731  1.00 28.50  ? 446  TYR   D C   1 
ATOM   11363 O  O   . TYR   D  1 145 ? 14.590  -54.957 -25.214  1.00 18.87  ? 446  TYR   D O   1 
ATOM   11364 C  CB  . TYR   D  1 145 ? 16.404  -52.600 -23.867  1.00 22.19  ? 446  TYR   D CB  1 
ATOM   11365 C  CG  . TYR   D  1 145 ? 15.906  -51.518 -22.955  1.00 21.68  ? 446  TYR   D CG  1 
ATOM   11366 C  CD1 . TYR   D  1 145 ? 16.776  -50.815 -22.138  1.00 21.66  ? 446  TYR   D CD1 1 
ATOM   11367 C  CD2 . TYR   D  1 145 ? 14.559  -51.194 -22.915  1.00 23.29  ? 446  TYR   D CD2 1 
ATOM   11368 C  CE1 . TYR   D  1 145 ? 16.314  -49.798 -21.303  1.00 22.68  ? 446  TYR   D CE1 1 
ATOM   11369 C  CE2 . TYR   D  1 145 ? 14.091  -50.191 -22.088  1.00 23.50  ? 446  TYR   D CE2 1 
ATOM   11370 C  CZ  . TYR   D  1 145 ? 14.958  -49.499 -21.291  1.00 24.81  ? 446  TYR   D CZ  1 
ATOM   11371 O  OH  . TYR   D  1 145 ? 14.455  -48.503 -20.477  1.00 28.02  ? 446  TYR   D OH  1 
ATOM   11372 N  N   . ILE   D  1 146 ? 16.792  -55.413 -25.282  1.00 24.74  ? 447  ILE   D N   1 
ATOM   11373 C  CA  . ILE   D  1 146 ? 16.652  -56.151 -26.534  1.00 24.23  ? 447  ILE   D CA  1 
ATOM   11374 C  C   . ILE   D  1 146 ? 15.937  -57.470 -26.292  1.00 24.82  ? 447  ILE   D C   1 
ATOM   11375 O  O   . ILE   D  1 146 ? 15.107  -57.897 -27.105  1.00 26.65  ? 447  ILE   D O   1 
ATOM   11376 C  CB  . ILE   D  1 146 ? 18.026  -56.342 -27.195  1.00 26.34  ? 447  ILE   D CB  1 
ATOM   11377 C  CG1 . ILE   D  1 146 ? 18.504  -54.996 -27.739  1.00 25.63  ? 447  ILE   D CG1 1 
ATOM   11378 C  CG2 . ILE   D  1 146 ? 17.958  -57.374 -28.323  1.00 25.84  ? 447  ILE   D CG2 1 
ATOM   11379 C  CD1 . ILE   D  1 146 ? 19.964  -54.952 -28.119  1.00 19.72  ? 447  ILE   D CD1 1 
ATOM   11380 N  N   . CYS   D  1 147 ? 16.206  -58.111 -25.146  1.00 21.59  ? 448  CYS   D N   1 
ATOM   11381 C  CA  . CYS   D  1 147 ? 15.489  -59.332 -24.804  1.00 22.15  ? 448  CYS   D CA  1 
ATOM   11382 C  C   . CYS   D  1 147 ? 14.006  -59.064 -24.652  1.00 20.88  ? 448  CYS   D C   1 
ATOM   11383 O  O   . CYS   D  1 147 ? 13.174  -59.867 -25.087  1.00 26.38  ? 448  CYS   D O   1 
ATOM   11384 C  CB  . CYS   D  1 147 ? 16.028  -59.932 -23.505  1.00 30.12  ? 448  CYS   D CB  1 
ATOM   11385 S  SG  . CYS   D  1 147 ? 17.584  -60.750 -23.694  1.00 35.05  ? 448  CYS   D SG  1 
ATOM   11386 N  N   . ASN   D  1 148 ? 13.655  -57.970 -23.976  1.00 22.10  ? 449  ASN   D N   1 
ATOM   11387 C  CA  . ASN   D  1 148 ? 12.247  -57.619 -23.834  1.00 21.53  ? 449  ASN   D CA  1 
ATOM   11388 C  C   . ASN   D  1 148 ? 11.623  -57.347 -25.201  1.00 21.76  ? 449  ASN   D C   1 
ATOM   11389 O  O   . ASN   D  1 148 ? 10.504  -57.787 -25.491  1.00 23.27  ? 449  ASN   D O   1 
ATOM   11390 C  CB  . ASN   D  1 148 ? 12.116  -56.418 -22.896  1.00 19.48  ? 449  ASN   D CB  1 
ATOM   11391 C  CG  . ASN   D  1 148 ? 12.542  -56.769 -21.455  1.00 23.24  ? 449  ASN   D CG  1 
ATOM   11392 O  OD1 . ASN   D  1 148 ? 12.629  -57.945 -21.105  1.00 25.93  ? 449  ASN   D OD1 1 
ATOM   11393 N  ND2 . ASN   D  1 148 ? 12.813  -55.758 -20.634  1.00 23.84  ? 449  ASN   D ND2 1 
ATOM   11394 N  N   . HIS   D  1 149 ? 12.349  -56.645 -26.058  1.00 18.50  ? 450  HIS   D N   1 
ATOM   11395 C  CA  . HIS   D  1 149 ? 11.878  -56.411 -27.416  1.00 21.60  ? 450  HIS   D CA  1 
ATOM   11396 C  C   . HIS   D  1 149 ? 11.634  -57.736 -28.125  1.00 18.69  ? 450  HIS   D C   1 
ATOM   11397 O  O   . HIS   D  1 149 ? 10.529  -58.001 -28.614  1.00 21.42  ? 450  HIS   D O   1 
ATOM   11398 C  CB  . HIS   D  1 149 ? 12.908  -55.546 -28.139  1.00 17.45  ? 450  HIS   D CB  1 
ATOM   11399 C  CG  . HIS   D  1 149 ? 12.591  -55.269 -29.581  1.00 26.44  ? 450  HIS   D CG  1 
ATOM   11400 N  ND1 . HIS   D  1 149 ? 12.754  -54.021 -30.139  1.00 22.65  ? 450  HIS   D ND1 1 
ATOM   11401 C  CD2 . HIS   D  1 149 ? 12.169  -56.077 -30.584  1.00 22.18  ? 450  HIS   D CD2 1 
ATOM   11402 C  CE1 . HIS   D  1 149 ? 12.444  -54.071 -31.423  1.00 26.12  ? 450  HIS   D CE1 1 
ATOM   11403 N  NE2 . HIS   D  1 149 ? 12.076  -55.304 -31.715  1.00 21.93  ? 450  HIS   D NE2 1 
ATOM   11404 N  N   . VAL   D  1 150 ? 12.638  -58.613 -28.120  1.00 20.64  ? 451  VAL   D N   1 
ATOM   11405 C  CA  . VAL   D  1 150 ? 12.521  -59.884 -28.827  1.00 20.66  ? 451  VAL   D CA  1 
ATOM   11406 C  C   . VAL   D  1 150 ? 11.346  -60.687 -28.291  1.00 33.67  ? 451  VAL   D C   1 
ATOM   11407 O  O   . VAL   D  1 150 ? 10.601  -61.314 -29.059  1.00 18.76  ? 451  VAL   D O   1 
ATOM   11408 C  CB  . VAL   D  1 150 ? 13.844  -60.668 -28.728  1.00 24.12  ? 451  VAL   D CB  1 
ATOM   11409 C  CG1 . VAL   D  1 150 ? 13.648  -62.106 -29.175  1.00 19.72  ? 451  VAL   D CG1 1 
ATOM   11410 C  CG2 . VAL   D  1 150 ? 14.904  -59.994 -29.585  1.00 22.11  ? 451  VAL   D CG2 1 
ATOM   11411 N  N   . LYS   D  1 151 ? 11.151  -60.679 -26.960  1.00 31.04  ? 452  LYS   D N   1 
ATOM   11412 C  CA  . LYS   D  1 151 ? 10.058  -61.457 -26.392  1.00 24.30  ? 452  LYS   D CA  1 
ATOM   11413 C  C   . LYS   D  1 151 ? 8.710   -60.846 -26.751  1.00 22.89  ? 452  LYS   D C   1 
ATOM   11414 O  O   . LYS   D  1 151 ? 7.776   -61.570 -27.110  1.00 19.84  ? 452  LYS   D O   1 
ATOM   11415 C  CB  . LYS   D  1 151 ? 10.211  -61.580 -24.872  1.00 27.74  ? 452  LYS   D CB  1 
ATOM   11416 C  CG  . LYS   D  1 151 ? 9.224   -62.534 -24.233  1.00 23.30  ? 452  LYS   D CG  1 
ATOM   11417 C  CD  . LYS   D  1 151 ? 9.538   -62.672 -22.726  1.00 30.16  ? 452  LYS   D CD  1 
ATOM   11418 C  CE  . LYS   D  1 151 ? 8.816   -63.847 -22.086  1.00 34.75  ? 452  LYS   D CE  1 
ATOM   11419 N  NZ  . LYS   D  1 151 ? 9.286   -64.084 -20.685  1.00 36.70  ? 452  LYS   D NZ  1 
ATOM   11420 N  N   . TYR   D  1 152 ? 8.586   -59.518 -26.647  1.00 22.00  ? 453  TYR   D N   1 
ATOM   11421 C  CA  . TYR   D  1 152 ? 7.343   -58.857 -27.037  1.00 25.92  ? 453  TYR   D CA  1 
ATOM   11422 C  C   . TYR   D  1 152 ? 7.047   -59.081 -28.510  1.00 20.51  ? 453  TYR   D C   1 
ATOM   11423 O  O   . TYR   D  1 152 ? 5.933   -59.471 -28.886  1.00 26.87  ? 453  TYR   D O   1 
ATOM   11424 C  CB  . TYR   D  1 152 ? 7.425   -57.352 -26.762  1.00 21.25  ? 453  TYR   D CB  1 
ATOM   11425 C  CG  . TYR   D  1 152 ? 6.217   -56.625 -27.277  1.00 25.24  ? 453  TYR   D CG  1 
ATOM   11426 C  CD1 . TYR   D  1 152 ? 5.099   -56.475 -26.478  1.00 30.23  ? 453  TYR   D CD1 1 
ATOM   11427 C  CD2 . TYR   D  1 152 ? 6.182   -56.096 -28.569  1.00 25.11  ? 453  TYR   D CD2 1 
ATOM   11428 C  CE1 . TYR   D  1 152 ? 3.985   -55.826 -26.943  1.00 32.43  ? 453  TYR   D CE1 1 
ATOM   11429 C  CE2 . TYR   D  1 152 ? 5.064   -55.454 -29.034  1.00 26.11  ? 453  TYR   D CE2 1 
ATOM   11430 C  CZ  . TYR   D  1 152 ? 3.975   -55.322 -28.212  1.00 30.83  ? 453  TYR   D CZ  1 
ATOM   11431 O  OH  . TYR   D  1 152 ? 2.856   -54.677 -28.655  1.00 37.45  ? 453  TYR   D OH  1 
ATOM   11432 N  N   . ALA   D  1 153 ? 8.032   -58.800 -29.359  1.00 25.51  ? 454  ALA   D N   1 
ATOM   11433 C  CA  . ALA   D  1 153 ? 7.832   -58.874 -30.802  1.00 22.57  ? 454  ALA   D CA  1 
ATOM   11434 C  C   . ALA   D  1 153 ? 7.516   -60.293 -31.241  1.00 23.80  ? 454  ALA   D C   1 
ATOM   11435 O  O   . ALA   D  1 153 ? 6.690   -60.499 -32.132  1.00 26.99  ? 454  ALA   D O   1 
ATOM   11436 C  CB  . ALA   D  1 153 ? 9.073   -58.360 -31.532  1.00 17.25  ? 454  ALA   D CB  1 
ATOM   11437 N  N   . THR   D  1 154 ? 8.164   -61.283 -30.634  1.00 27.08  ? 455  THR   D N   1 
ATOM   11438 C  CA  . THR   D  1 154 ? 7.913   -62.664 -31.028  1.00 28.21  ? 455  THR   D CA  1 
ATOM   11439 C  C   . THR   D  1 154 ? 6.516   -63.102 -30.626  1.00 29.01  ? 455  THR   D C   1 
ATOM   11440 O  O   . THR   D  1 154 ? 5.766   -63.634 -31.453  1.00 23.39  ? 455  THR   D O   1 
ATOM   11441 C  CB  . THR   D  1 154 ? 8.967   -63.585 -30.417  1.00 24.95  ? 455  THR   D CB  1 
ATOM   11442 O  OG1 . THR   D  1 154 ? 10.250  -63.235 -30.953  1.00 22.55  ? 455  THR   D OG1 1 
ATOM   11443 C  CG2 . THR   D  1 154 ? 8.659   -65.057 -30.728  1.00 24.36  ? 455  THR   D CG2 1 
ATOM   11444 N  N   . ASN   D  1 155 ? 6.155   -62.913 -29.350  1.00 28.15  ? 456  ASN   D N   1 
ATOM   11445 C  CA  . ASN   D  1 155 ? 4.785   -63.145 -28.899  1.00 28.17  ? 456  ASN   D CA  1 
ATOM   11446 C  C   . ASN   D  1 155 ? 4.321   -64.556 -29.265  1.00 28.99  ? 456  ASN   D C   1 
ATOM   11447 O  O   . ASN   D  1 155 ? 3.215   -64.761 -29.772  1.00 28.16  ? 456  ASN   D O   1 
ATOM   11448 C  CB  . ASN   D  1 155 ? 3.846   -62.084 -29.490  1.00 29.20  ? 456  ASN   D CB  1 
ATOM   11449 C  CG  . ASN   D  1 155 ? 2.443   -62.157 -28.921  1.00 32.55  ? 456  ASN   D CG  1 
ATOM   11450 O  OD1 . ASN   D  1 155 ? 2.256   -62.502 -27.760  1.00 29.65  ? 456  ASN   D OD1 1 
ATOM   11451 N  ND2 . ASN   D  1 155 ? 1.452   -61.842 -29.742  1.00 27.67  ? 456  ASN   D ND2 1 
ATOM   11452 N  N   . LYS   D  1 156 ? 5.204   -65.535 -29.047  1.00 23.42  ? 457  LYS   D N   1 
ATOM   11453 C  CA  . LYS   D  1 156 ? 4.897   -66.952 -29.278  1.00 24.90  ? 457  LYS   D CA  1 
ATOM   11454 C  C   . LYS   D  1 156 ? 4.481   -67.224 -30.727  1.00 28.51  ? 457  LYS   D C   1 
ATOM   11455 O  O   . LYS   D  1 156 ? 3.710   -68.148 -31.004  1.00 30.78  ? 457  LYS   D O   1 
ATOM   11456 C  CB  . LYS   D  1 156 ? 3.816   -67.450 -28.315  1.00 32.82  ? 457  LYS   D CB  1 
ATOM   11457 C  CG  . LYS   D  1 156 ? 4.181   -67.303 -26.845  1.00 35.98  ? 457  LYS   D CG  1 
ATOM   11458 C  CD  . LYS   D  1 156 ? 2.995   -67.679 -25.962  1.00 45.83  ? 457  LYS   D CD  1 
ATOM   11459 C  CE  . LYS   D  1 156 ? 3.331   -67.608 -24.480  1.00 57.25  ? 457  LYS   D CE  1 
ATOM   11460 N  NZ  . LYS   D  1 156 ? 4.397   -68.586 -24.132  1.00 61.05  ? 457  LYS   D NZ  1 
ATOM   11461 N  N   . GLY   D  1 157 ? 4.978   -66.419 -31.664  1.00 26.00  ? 458  GLY   D N   1 
ATOM   11462 C  CA  . GLY   D  1 157 ? 4.731   -66.635 -33.077  1.00 26.23  ? 458  GLY   D CA  1 
ATOM   11463 C  C   . GLY   D  1 157 ? 3.722   -65.692 -33.687  1.00 28.36  ? 458  GLY   D C   1 
ATOM   11464 O  O   . GLY   D  1 157 ? 3.645   -65.599 -34.918  1.00 27.62  ? 458  GLY   D O   1 
ATOM   11465 N  N   . ASN   D  1 158 ? 2.953   -64.989 -32.864  1.00 24.16  ? 459  ASN   D N   1 
ATOM   11466 C  CA  . ASN   D  1 158 ? 2.023   -63.972 -33.343  1.00 28.90  ? 459  ASN   D CA  1 
ATOM   11467 C  C   . ASN   D  1 158 ? 2.784   -62.647 -33.342  1.00 32.75  ? 459  ASN   D C   1 
ATOM   11468 O  O   . ASN   D  1 158 ? 2.618   -61.794 -32.468  1.00 29.34  ? 459  ASN   D O   1 
ATOM   11469 C  CB  . ASN   D  1 158 ? 0.780   -63.947 -32.460  1.00 27.94  ? 459  ASN   D CB  1 
ATOM   11470 C  CG  . ASN   D  1 158 ? -0.296  -63.026 -32.999  1.00 37.11  ? 459  ASN   D CG  1 
ATOM   11471 O  OD1 . ASN   D  1 158 ? -0.321  -62.716 -34.188  1.00 34.08  ? 459  ASN   D OD1 1 
ATOM   11472 N  ND2 . ASN   D  1 158 ? -1.199  -62.587 -32.124  1.00 37.00  ? 459  ASN   D ND2 1 
ATOM   11473 N  N   . LEU   D  1 159 ? 3.654   -62.490 -34.341  1.00 19.52  ? 460  LEU   D N   1 
ATOM   11474 C  CA  . LEU   D  1 159 ? 4.668   -61.450 -34.279  1.00 26.14  ? 460  LEU   D CA  1 
ATOM   11475 C  C   . LEU   D  1 159 ? 4.021   -60.077 -34.248  1.00 26.36  ? 460  LEU   D C   1 
ATOM   11476 O  O   . LEU   D  1 159 ? 2.935   -59.859 -34.790  1.00 27.87  ? 460  LEU   D O   1 
ATOM   11477 C  CB  . LEU   D  1 159 ? 5.633   -61.536 -35.463  1.00 23.88  ? 460  LEU   D CB  1 
ATOM   11478 C  CG  . LEU   D  1 159 ? 6.320   -62.881 -35.670  1.00 39.70  ? 460  LEU   D CG  1 
ATOM   11479 C  CD1 . LEU   D  1 159 ? 7.434   -62.770 -36.700  1.00 41.55  ? 460  LEU   D CD1 1 
ATOM   11480 C  CD2 . LEU   D  1 159 ? 6.858   -63.371 -34.375  1.00 34.89  ? 460  LEU   D CD2 1 
ATOM   11481 N  N   . ARG   D  1 160 ? 4.706   -59.146 -33.595  1.00 24.49  ? 461  ARG   D N   1 
ATOM   11482 C  CA  . ARG   D  1 160 ? 4.202   -57.802 -33.426  1.00 17.93  ? 461  ARG   D CA  1 
ATOM   11483 C  C   . ARG   D  1 160 ? 5.341   -56.862 -33.738  1.00 24.90  ? 461  ARG   D C   1 
ATOM   11484 O  O   . ARG   D  1 160 ? 6.474   -57.117 -33.327  1.00 23.02  ? 461  ARG   D O   1 
ATOM   11485 C  CB  . ARG   D  1 160 ? 3.691   -57.581 -31.993  1.00 21.93  ? 461  ARG   D CB  1 
ATOM   11486 C  CG  . ARG   D  1 160 ? 2.456   -58.371 -31.643  1.00 29.89  ? 461  ARG   D CG  1 
ATOM   11487 C  CD  . ARG   D  1 160 ? 2.001   -58.072 -30.193  1.00 26.15  ? 461  ARG   D CD  1 
ATOM   11488 N  NE  . ARG   D  1 160 ? 2.893   -58.649 -29.197  1.00 26.87  ? 461  ARG   D NE  1 
ATOM   11489 C  CZ  . ARG   D  1 160 ? 2.558   -58.811 -27.918  1.00 32.15  ? 461  ARG   D CZ  1 
ATOM   11490 N  NH1 . ARG   D  1 160 ? 1.359   -58.430 -27.493  1.00 27.12  ? 461  ARG   D NH1 1 
ATOM   11491 N  NH2 . ARG   D  1 160 ? 3.418   -59.348 -27.069  1.00 23.09  ? 461  ARG   D NH2 1 
ATOM   11492 N  N   . SER   D  1 161 ? 5.050   -55.811 -34.503  1.00 22.15  ? 462  SER   D N   1 
ATOM   11493 C  CA  . SER   D  1 161 ? 6.089   -54.877 -34.903  1.00 24.33  ? 462  SER   D CA  1 
ATOM   11494 C  C   . SER   D  1 161 ? 6.553   -54.053 -33.712  1.00 23.79  ? 462  SER   D C   1 
ATOM   11495 O  O   . SER   D  1 161 ? 5.749   -53.609 -32.891  1.00 22.20  ? 462  SER   D O   1 
ATOM   11496 C  CB  . SER   D  1 161 ? 5.569   -53.952 -35.998  1.00 19.87  ? 462  SER   D CB  1 
ATOM   11497 O  OG  . SER   D  1 161 ? 5.183   -54.727 -37.113  1.00 31.36  ? 462  SER   D OG  1 
ATOM   11498 N  N   . ALA   D  1 162 ? 7.855   -53.807 -33.638  1.00 20.38  ? 463  ALA   D N   1 
ATOM   11499 C  CA  . ALA   D  1 162 ? 8.366   -53.109 -32.473  1.00 17.42  ? 463  ALA   D CA  1 
ATOM   11500 C  C   . ALA   D  1 162 ? 9.674   -52.443 -32.830  1.00 22.40  ? 463  ALA   D C   1 
ATOM   11501 O  O   . ALA   D  1 162 ? 10.382  -52.874 -33.749  1.00 18.20  ? 463  ALA   D O   1 
ATOM   11502 C  CB  . ALA   D  1 162 ? 8.571   -54.076 -31.295  1.00 16.65  ? 463  ALA   D CB  1 
ATOM   11503 N  N   . ILE   D  1 163 ? 9.988   -51.391 -32.092  1.00 21.25  ? 464  ILE   D N   1 
ATOM   11504 C  CA  . ILE   D  1 163 ? 11.276  -50.732 -32.209  1.00 20.78  ? 464  ILE   D CA  1 
ATOM   11505 C  C   . ILE   D  1 163 ? 11.699  -50.380 -30.798  1.00 24.71  ? 464  ILE   D C   1 
ATOM   11506 O  O   . ILE   D  1 163 ? 10.868  -49.977 -29.977  1.00 19.99  ? 464  ILE   D O   1 
ATOM   11507 C  CB  . ILE   D  1 163 ? 11.216  -49.484 -33.119  1.00 18.74  ? 464  ILE   D CB  1 
ATOM   11508 C  CG1 . ILE   D  1 163 ? 12.607  -48.855 -33.268  1.00 16.04  ? 464  ILE   D CG1 1 
ATOM   11509 C  CG2 . ILE   D  1 163 ? 10.203  -48.458 -32.574  1.00 17.79  ? 464  ILE   D CG2 1 
ATOM   11510 C  CD1 . ILE   D  1 163 ? 12.697  -47.826 -34.394  1.00 18.47  ? 464  ILE   D CD1 1 
ATOM   11511 N  N   . THR   D  1 164 ? 12.979  -50.559 -30.503  1.00 20.61  ? 465  THR   D N   1 
ATOM   11512 C  CA  . THR   D  1 164 ? 13.532  -50.135 -29.229  1.00 20.54  ? 465  THR   D CA  1 
ATOM   11513 C  C   . THR   D  1 164 ? 14.580  -49.078 -29.514  1.00 24.82  ? 465  THR   D C   1 
ATOM   11514 O  O   . THR   D  1 164 ? 15.488  -49.319 -30.309  1.00 26.43  ? 465  THR   D O   1 
ATOM   11515 C  CB  . THR   D  1 164 ? 14.156  -51.305 -28.461  1.00 18.45  ? 465  THR   D CB  1 
ATOM   11516 O  OG1 . THR   D  1 164 ? 13.133  -52.247 -28.135  1.00 23.67  ? 465  THR   D OG1 1 
ATOM   11517 C  CG2 . THR   D  1 164 ? 14.819  -50.786 -27.192  1.00 21.01  ? 465  THR   D CG2 1 
ATOM   11518 N  N   . ILE   D  1 165 ? 14.459  -47.924 -28.868  1.00 24.04  ? 466  ILE   D N   1 
ATOM   11519 C  CA  . ILE   D  1 165 ? 15.225  -46.745 -29.237  1.00 27.32  ? 466  ILE   D CA  1 
ATOM   11520 C  C   . ILE   D  1 165 ? 16.122  -46.370 -28.070  1.00 21.90  ? 466  ILE   D C   1 
ATOM   11521 O  O   . ILE   D  1 165 ? 15.650  -45.916 -27.017  1.00 23.05  ? 466  ILE   D O   1 
ATOM   11522 C  CB  . ILE   D  1 165 ? 14.325  -45.575 -29.658  1.00 30.14  ? 466  ILE   D CB  1 
ATOM   11523 C  CG1 . ILE   D  1 165 ? 13.426  -45.997 -30.828  1.00 24.38  ? 466  ILE   D CG1 1 
ATOM   11524 C  CG2 . ILE   D  1 165 ? 15.188  -44.391 -30.077  1.00 27.57  ? 466  ILE   D CG2 1 
ATOM   11525 C  CD1 . ILE   D  1 165 ? 12.342  -44.985 -31.175  1.00 21.40  ? 466  ILE   D CD1 1 
ATOM   11526 N  N   . PHE   D  1 166 ? 17.411  -46.550 -28.269  1.00 24.70  ? 467  PHE   D N   1 
ATOM   11527 C  CA  . PHE   D  1 166 ? 18.449  -46.280 -27.292  1.00 25.15  ? 467  PHE   D CA  1 
ATOM   11528 C  C   . PHE   D  1 166 ? 18.877  -44.826 -27.365  1.00 29.41  ? 467  PHE   D C   1 
ATOM   11529 O  O   . PHE   D  1 166 ? 18.465  -44.100 -28.268  1.00 28.14  ? 467  PHE   D O   1 
ATOM   11530 C  CB  . PHE   D  1 166 ? 19.614  -47.226 -27.548  1.00 23.44  ? 467  PHE   D CB  1 
ATOM   11531 C  CG  . PHE   D  1 166 ? 19.303  -48.643 -27.185  1.00 27.10  ? 467  PHE   D CG  1 
ATOM   11532 C  CD1 . PHE   D  1 166 ? 19.164  -49.007 -25.856  1.00 24.15  ? 467  PHE   D CD1 1 
ATOM   11533 C  CD2 . PHE   D  1 166 ? 19.117  -49.598 -28.161  1.00 28.37  ? 467  PHE   D CD2 1 
ATOM   11534 C  CE1 . PHE   D  1 166 ? 18.878  -50.296 -25.514  1.00 26.08  ? 467  PHE   D CE1 1 
ATOM   11535 C  CE2 . PHE   D  1 166 ? 18.830  -50.897 -27.822  1.00 30.97  ? 467  PHE   D CE2 1 
ATOM   11536 C  CZ  . PHE   D  1 166 ? 18.711  -51.251 -26.497  1.00 20.60  ? 467  PHE   D CZ  1 
ATOM   11537 N  N   . PRO   D  1 167 ? 19.680  -44.361 -26.398  1.00 31.39  ? 468  PRO   D N   1 
ATOM   11538 C  CA  . PRO   D  1 167 ? 20.074  -42.947 -26.376  1.00 30.38  ? 468  PRO   D CA  1 
ATOM   11539 C  C   . PRO   D  1 167 ? 20.613  -42.456 -27.712  1.00 31.08  ? 468  PRO   D C   1 
ATOM   11540 O  O   . PRO   D  1 167 ? 21.351  -43.156 -28.409  1.00 29.46  ? 468  PRO   D O   1 
ATOM   11541 C  CB  . PRO   D  1 167 ? 21.154  -42.906 -25.299  1.00 33.20  ? 468  PRO   D CB  1 
ATOM   11542 C  CG  . PRO   D  1 167 ? 20.725  -43.958 -24.332  1.00 30.78  ? 468  PRO   D CG  1 
ATOM   11543 C  CD  . PRO   D  1 167 ? 20.102  -45.053 -25.162  1.00 31.63  ? 468  PRO   D CD  1 
ATOM   11544 N  N   . GLN   D  1 168 ? 20.234  -41.232 -28.056  1.00 26.75  ? 469  GLN   D N   1 
ATOM   11545 C  CA  . GLN   D  1 168 ? 20.659  -40.630 -29.301  1.00 28.50  ? 469  GLN   D CA  1 
ATOM   11546 C  C   . GLN   D  1 168 ? 22.143  -40.310 -29.248  1.00 34.05  ? 469  GLN   D C   1 
ATOM   11547 O  O   . GLN   D  1 168 ? 22.761  -40.247 -28.177  1.00 29.94  ? 469  GLN   D O   1 
ATOM   11548 C  CB  . GLN   D  1 168 ? 19.879  -39.353 -29.570  1.00 22.34  ? 469  GLN   D CB  1 
ATOM   11549 C  CG  . GLN   D  1 168 ? 20.179  -38.275 -28.564  1.00 28.70  ? 469  GLN   D CG  1 
ATOM   11550 C  CD  . GLN   D  1 168 ? 18.996  -37.371 -28.339  1.00 31.30  ? 469  GLN   D CD  1 
ATOM   11551 O  OE1 . GLN   D  1 168 ? 17.855  -37.832 -28.279  1.00 32.80  ? 469  GLN   D OE1 1 
ATOM   11552 N  NE2 . GLN   D  1 168 ? 19.252  -36.073 -28.237  1.00 29.82  ? 469  GLN   D NE2 1 
ATOM   11553 N  N   . ARG   D  1 169 ? 22.710  -40.105 -30.430  1.00 28.42  ? 470  ARG   D N   1 
ATOM   11554 C  CA  . ARG   D  1 169 ? 24.105  -39.713 -30.527  1.00 33.76  ? 470  ARG   D CA  1 
ATOM   11555 C  C   . ARG   D  1 169 ? 24.303  -38.349 -29.884  1.00 32.01  ? 470  ARG   D C   1 
ATOM   11556 O  O   . ARG   D  1 169 ? 23.430  -37.480 -29.945  1.00 35.14  ? 470  ARG   D O   1 
ATOM   11557 C  CB  . ARG   D  1 169 ? 24.529  -39.693 -31.996  1.00 44.21  ? 470  ARG   D CB  1 
ATOM   11558 C  CG  . ARG   D  1 169 ? 25.825  -38.963 -32.275  1.00 53.48  ? 470  ARG   D CG  1 
ATOM   11559 C  CD  . ARG   D  1 169 ? 26.267  -39.240 -33.694  1.00 58.51  ? 470  ARG   D CD  1 
ATOM   11560 N  NE  . ARG   D  1 169 ? 26.503  -40.663 -33.873  1.00 52.85  ? 470  ARG   D NE  1 
ATOM   11561 C  CZ  . ARG   D  1 169 ? 26.363  -41.296 -35.025  1.00 62.88  ? 470  ARG   D CZ  1 
ATOM   11562 N  NH1 . ARG   D  1 169 ? 25.972  -40.630 -36.103  1.00 65.19  ? 470  ARG   D NH1 1 
ATOM   11563 N  NH2 . ARG   D  1 169 ? 26.603  -42.598 -35.093  1.00 67.77  ? 470  ARG   D NH2 1 
ATOM   11564 N  N   . THR   D  1 170 ? 25.444  -38.171 -29.228  1.00 38.92  ? 471  THR   D N   1 
ATOM   11565 C  CA  . THR   D  1 170 ? 25.747  -36.868 -28.655  1.00 39.37  ? 471  THR   D CA  1 
ATOM   11566 C  C   . THR   D  1 170 ? 26.897  -36.247 -29.429  1.00 43.20  ? 471  THR   D C   1 
ATOM   11567 O  O   . THR   D  1 170 ? 26.679  -35.422 -30.321  1.00 53.60  ? 471  THR   D O   1 
ATOM   11568 C  CB  . THR   D  1 170 ? 26.088  -36.982 -27.168  1.00 41.85  ? 471  THR   D CB  1 
ATOM   11569 O  OG1 . THR   D  1 170 ? 27.143  -37.936 -26.990  1.00 42.61  ? 471  THR   D OG1 1 
ATOM   11570 C  CG2 . THR   D  1 170 ? 24.863  -37.410 -26.361  1.00 36.00  ? 471  THR   D CG2 1 
ATOM   11571 N  N   . ASP   D  1 171 ? 28.121  -36.661 -29.120  1.00 51.71  ? 472  ASP   D N   1 
ATOM   11572 C  CA  . ASP   D  1 171 ? 29.303  -36.146 -29.796  1.00 55.62  ? 472  ASP   D CA  1 
ATOM   11573 C  C   . ASP   D  1 171 ? 29.891  -37.123 -30.803  1.00 56.13  ? 472  ASP   D C   1 
ATOM   11574 O  O   . ASP   D  1 171 ? 30.940  -36.833 -31.381  1.00 62.87  ? 472  ASP   D O   1 
ATOM   11575 C  CB  . ASP   D  1 171 ? 30.371  -35.758 -28.768  1.00 56.66  ? 472  ASP   D CB  1 
ATOM   11576 C  CG  . ASP   D  1 171 ? 30.788  -36.923 -27.882  1.00 61.71  ? 472  ASP   D CG  1 
ATOM   11577 O  OD1 . ASP   D  1 171 ? 30.354  -38.068 -28.132  1.00 59.10  ? 472  ASP   D OD1 1 
ATOM   11578 O  OD2 . ASP   D  1 171 ? 31.555  -36.691 -26.924  1.00 60.25  ? 472  ASP   D OD2 1 
ATOM   11579 N  N   . GLY   D  1 172 ? 29.249  -38.268 -31.032  1.00 51.45  ? 473  GLY   D N   1 
ATOM   11580 C  CA  . GLY   D  1 172 ? 29.789  -39.273 -31.922  1.00 48.64  ? 473  GLY   D CA  1 
ATOM   11581 C  C   . GLY   D  1 172 ? 30.827  -40.180 -31.299  1.00 51.29  ? 473  GLY   D C   1 
ATOM   11582 O  O   . GLY   D  1 172 ? 31.185  -41.195 -31.904  1.00 53.72  ? 473  GLY   D O   1 
ATOM   11583 N  N   . LYS   D  1 173 ? 31.327  -39.850 -30.115  1.00 51.66  ? 474  LYS   D N   1 
ATOM   11584 C  CA  . LYS   D  1 173 ? 32.277  -40.690 -29.404  1.00 58.79  ? 474  LYS   D CA  1 
ATOM   11585 C  C   . LYS   D  1 173 ? 31.608  -41.537 -28.331  1.00 61.81  ? 474  LYS   D C   1 
ATOM   11586 O  O   . LYS   D  1 173 ? 32.278  -42.350 -27.686  1.00 60.67  ? 474  LYS   D O   1 
ATOM   11587 C  CB  . LYS   D  1 173 ? 33.380  -39.819 -28.788  1.00 63.74  ? 474  LYS   D CB  1 
ATOM   11588 C  CG  . LYS   D  1 173 ? 34.136  -38.971 -29.816  1.00 68.24  ? 474  LYS   D CG  1 
ATOM   11589 C  CD  . LYS   D  1 173 ? 35.289  -38.193 -29.182  1.00 71.27  ? 474  LYS   D CD  1 
ATOM   11590 C  CE  . LYS   D  1 173 ? 36.008  -37.315 -30.205  1.00 69.31  ? 474  LYS   D CE  1 
ATOM   11591 N  NZ  . LYS   D  1 173 ? 37.302  -36.766 -29.689  1.00 66.35  ? 474  LYS   D NZ  1 
ATOM   11592 N  N   . HIS   D  1 174 ? 30.302  -41.383 -28.140  1.00 58.33  ? 475  HIS   D N   1 
ATOM   11593 C  CA  . HIS   D  1 174 ? 29.574  -42.088 -27.100  1.00 50.06  ? 475  HIS   D CA  1 
ATOM   11594 C  C   . HIS   D  1 174 ? 28.387  -42.826 -27.685  1.00 40.76  ? 475  HIS   D C   1 
ATOM   11595 O  O   . HIS   D  1 174 ? 27.334  -42.927 -27.058  1.00 38.22  ? 475  HIS   D O   1 
ATOM   11596 C  CB  . HIS   D  1 174 ? 29.117  -41.123 -26.010  1.00 52.75  ? 475  HIS   D CB  1 
ATOM   11597 C  CG  . HIS   D  1 174 ? 30.243  -40.501 -25.247  1.00 60.98  ? 475  HIS   D CG  1 
ATOM   11598 N  ND1 . HIS   D  1 174 ? 31.112  -39.589 -25.810  1.00 61.49  ? 475  HIS   D ND1 1 
ATOM   11599 C  CD2 . HIS   D  1 174 ? 30.645  -40.663 -23.965  1.00 55.06  ? 475  HIS   D CD2 1 
ATOM   11600 C  CE1 . HIS   D  1 174 ? 31.999  -39.216 -24.905  1.00 58.15  ? 475  HIS   D CE1 1 
ATOM   11601 N  NE2 . HIS   D  1 174 ? 31.738  -39.853 -23.778  1.00 60.98  ? 475  HIS   D NE2 1 
ATOM   11602 N  N   . ASP   D  1 175 ? 28.534  -43.342 -28.901  1.00 38.28  ? 476  ASP   D N   1 
ATOM   11603 C  CA  . ASP   D  1 175 ? 27.413  -43.973 -29.581  1.00 33.43  ? 476  ASP   D CA  1 
ATOM   11604 C  C   . ASP   D  1 175 ? 26.958  -45.238 -28.876  1.00 30.62  ? 476  ASP   D C   1 
ATOM   11605 O  O   . ASP   D  1 175 ? 27.771  -46.036 -28.402  1.00 35.62  ? 476  ASP   D O   1 
ATOM   11606 C  CB  . ASP   D  1 175 ? 27.775  -44.332 -31.020  1.00 38.92  ? 476  ASP   D CB  1 
ATOM   11607 C  CG  . ASP   D  1 175 ? 27.826  -43.130 -31.932  1.00 39.27  ? 476  ASP   D CG  1 
ATOM   11608 O  OD1 . ASP   D  1 175 ? 27.667  -41.996 -31.435  1.00 37.61  ? 476  ASP   D OD1 1 
ATOM   11609 O  OD2 . ASP   D  1 175 ? 28.027  -43.335 -33.148  1.00 41.63  ? 476  ASP   D OD2 1 
ATOM   11610 N  N   . PHE   D  1 176 ? 25.645  -45.418 -28.822  1.00 26.85  ? 477  PHE   D N   1 
ATOM   11611 C  CA  . PHE   D  1 176 ? 25.062  -46.730 -28.605  1.00 27.58  ? 477  PHE   D CA  1 
ATOM   11612 C  C   . PHE   D  1 176 ? 24.973  -47.436 -29.952  1.00 26.48  ? 477  PHE   D C   1 
ATOM   11613 O  O   . PHE   D  1 176 ? 24.478  -46.857 -30.924  1.00 29.06  ? 477  PHE   D O   1 
ATOM   11614 C  CB  . PHE   D  1 176 ? 23.682  -46.601 -27.965  1.00 24.04  ? 477  PHE   D CB  1 
ATOM   11615 C  CG  . PHE   D  1 176 ? 23.739  -46.216 -26.501  1.00 26.03  ? 477  PHE   D CG  1 
ATOM   11616 C  CD1 . PHE   D  1 176 ? 24.124  -44.940 -26.121  1.00 24.89  ? 477  PHE   D CD1 1 
ATOM   11617 C  CD2 . PHE   D  1 176 ? 23.431  -47.139 -25.520  1.00 26.73  ? 477  PHE   D CD2 1 
ATOM   11618 C  CE1 . PHE   D  1 176 ? 24.196  -44.586 -24.780  1.00 30.78  ? 477  PHE   D CE1 1 
ATOM   11619 C  CE2 . PHE   D  1 176 ? 23.495  -46.796 -24.180  1.00 30.97  ? 477  PHE   D CE2 1 
ATOM   11620 C  CZ  . PHE   D  1 176 ? 23.879  -45.514 -23.813  1.00 31.32  ? 477  PHE   D CZ  1 
ATOM   11621 N  N   . ARG   D  1 177 ? 25.484  -48.665 -30.024  1.00 24.33  ? 478  ARG   D N   1 
ATOM   11622 C  CA  . ARG   D  1 177 ? 25.420  -49.429 -31.263  1.00 33.35  ? 478  ARG   D CA  1 
ATOM   11623 C  C   . ARG   D  1 177 ? 25.117  -50.881 -30.956  1.00 29.82  ? 478  ARG   D C   1 
ATOM   11624 O  O   . ARG   D  1 177 ? 25.739  -51.480 -30.076  1.00 31.87  ? 478  ARG   D O   1 
ATOM   11625 C  CB  . ARG   D  1 177 ? 26.732  -49.358 -32.061  1.00 28.67  ? 478  ARG   D CB  1 
ATOM   11626 C  CG  . ARG   D  1 177 ? 27.056  -48.003 -32.626  1.00 33.97  ? 478  ARG   D CG  1 
ATOM   11627 C  CD  . ARG   D  1 177 ? 25.992  -47.570 -33.612  1.00 35.90  ? 478  ARG   D CD  1 
ATOM   11628 N  NE  . ARG   D  1 177 ? 25.849  -48.504 -34.720  1.00 34.64  ? 478  ARG   D NE  1 
ATOM   11629 C  CZ  . ARG   D  1 177 ? 26.534  -48.434 -35.860  1.00 37.28  ? 478  ARG   D CZ  1 
ATOM   11630 N  NH1 . ARG   D  1 177 ? 27.431  -47.475 -36.054  1.00 29.63  ? 478  ARG   D NH1 1 
ATOM   11631 N  NH2 . ARG   D  1 177 ? 26.316  -49.329 -36.812  1.00 36.10  ? 478  ARG   D NH2 1 
ATOM   11632 N  N   . VAL   D  1 178 ? 24.182  -51.448 -31.690  1.00 25.04  ? 479  VAL   D N   1 
ATOM   11633 C  CA  . VAL   D  1 178 ? 24.083  -52.893 -31.783  1.00 26.56  ? 479  VAL   D CA  1 
ATOM   11634 C  C   . VAL   D  1 178 ? 24.980  -53.290 -32.946  1.00 29.82  ? 479  VAL   D C   1 
ATOM   11635 O  O   . VAL   D  1 178 ? 24.724  -52.907 -34.084  1.00 29.18  ? 479  VAL   D O   1 
ATOM   11636 C  CB  . VAL   D  1 178 ? 22.636  -53.341 -32.004  1.00 21.85  ? 479  VAL   D CB  1 
ATOM   11637 C  CG1 . VAL   D  1 178 ? 22.593  -54.839 -32.186  1.00 21.93  ? 479  VAL   D CG1 1 
ATOM   11638 C  CG2 . VAL   D  1 178 ? 21.778  -52.906 -30.821  1.00 23.49  ? 479  VAL   D CG2 1 
ATOM   11639 N  N   . TRP   D  1 179 ? 26.070  -53.998 -32.662  1.00 27.43  ? 480  TRP   D N   1 
ATOM   11640 C  CA  . TRP   D  1 179 ? 26.991  -54.320 -33.737  1.00 21.78  ? 480  TRP   D CA  1 
ATOM   11641 C  C   . TRP   D  1 179 ? 26.416  -55.371 -34.669  1.00 27.72  ? 480  TRP   D C   1 
ATOM   11642 O  O   . TRP   D  1 179 ? 26.819  -55.437 -35.830  1.00 29.85  ? 480  TRP   D O   1 
ATOM   11643 C  CB  . TRP   D  1 179 ? 28.333  -54.780 -33.174  1.00 26.83  ? 480  TRP   D CB  1 
ATOM   11644 C  CG  . TRP   D  1 179 ? 29.159  -53.660 -32.649  1.00 27.25  ? 480  TRP   D CG  1 
ATOM   11645 C  CD1 . TRP   D  1 179 ? 28.711  -52.536 -32.014  1.00 29.73  ? 480  TRP   D CD1 1 
ATOM   11646 C  CD2 . TRP   D  1 179 ? 30.582  -53.539 -32.724  1.00 30.64  ? 480  TRP   D CD2 1 
ATOM   11647 N  NE1 . TRP   D  1 179 ? 29.774  -51.728 -31.676  1.00 30.43  ? 480  TRP   D NE1 1 
ATOM   11648 C  CE2 . TRP   D  1 179 ? 30.932  -52.321 -32.102  1.00 24.88  ? 480  TRP   D CE2 1 
ATOM   11649 C  CE3 . TRP   D  1 179 ? 31.594  -54.340 -33.258  1.00 32.01  ? 480  TRP   D CE3 1 
ATOM   11650 C  CZ2 . TRP   D  1 179 ? 32.248  -51.882 -32.013  1.00 27.18  ? 480  TRP   D CZ2 1 
ATOM   11651 C  CZ3 . TRP   D  1 179 ? 32.906  -53.907 -33.156  1.00 35.02  ? 480  TRP   D CZ3 1 
ATOM   11652 C  CH2 . TRP   D  1 179 ? 33.219  -52.692 -32.537  1.00 31.91  ? 480  TRP   D CH2 1 
ATOM   11653 N  N   . ASN   D  1 180 ? 25.480  -56.183 -34.188  1.00 24.89  ? 481  ASN   D N   1 
ATOM   11654 C  CA  . ASN   D  1 180 ? 24.787  -57.113 -35.057  1.00 24.54  ? 481  ASN   D CA  1 
ATOM   11655 C  C   . ASN   D  1 180 ? 24.031  -56.352 -36.123  1.00 33.45  ? 481  ASN   D C   1 
ATOM   11656 O  O   . ASN   D  1 180 ? 23.416  -55.316 -35.850  1.00 31.71  ? 481  ASN   D O   1 
ATOM   11657 C  CB  . ASN   D  1 180 ? 23.810  -57.955 -34.264  1.00 22.73  ? 481  ASN   D CB  1 
ATOM   11658 C  CG  . ASN   D  1 180 ? 24.459  -58.583 -33.059  1.00 29.53  ? 481  ASN   D CG  1 
ATOM   11659 O  OD1 . ASN   D  1 180 ? 24.851  -57.889 -32.117  1.00 30.07  ? 481  ASN   D OD1 1 
ATOM   11660 N  ND2 . ASN   D  1 180 ? 24.587  -59.896 -33.083  1.00 31.38  ? 481  ASN   D ND2 1 
ATOM   11661 N  N   . SER   D  1 181 ? 24.055  -56.886 -37.344  1.00 22.88  ? 482  SER   D N   1 
ATOM   11662 C  CA  . SER   D  1 181 ? 23.253  -56.274 -38.401  1.00 28.09  ? 482  SER   D CA  1 
ATOM   11663 C  C   . SER   D  1 181 ? 21.770  -56.544 -38.171  1.00 25.86  ? 482  SER   D C   1 
ATOM   11664 O  O   . SER   D  1 181 ? 20.928  -55.668 -38.404  1.00 22.18  ? 482  SER   D O   1 
ATOM   11665 C  CB  . SER   D  1 181 ? 23.715  -56.782 -39.769  1.00 22.04  ? 482  SER   D CB  1 
ATOM   11666 O  OG  . SER   D  1 181 ? 23.573  -58.186 -39.851  1.00 25.64  ? 482  SER   D OG  1 
ATOM   11667 N  N   . GLN   D  1 182 ? 21.437  -57.742 -37.686  1.00 23.82  ? 483  GLN   D N   1 
ATOM   11668 C  CA  . GLN   D  1 182 ? 20.100  -58.072 -37.217  1.00 22.11  ? 483  GLN   D CA  1 
ATOM   11669 C  C   . GLN   D  1 182 ? 20.222  -58.792 -35.879  1.00 27.25  ? 483  GLN   D C   1 
ATOM   11670 O  O   . GLN   D  1 182 ? 21.215  -59.485 -35.618  1.00 24.62  ? 483  GLN   D O   1 
ATOM   11671 C  CB  . GLN   D  1 182 ? 19.330  -58.943 -38.218  1.00 25.12  ? 483  GLN   D CB  1 
ATOM   11672 C  CG  . GLN   D  1 182 ? 18.976  -58.234 -39.529  1.00 27.30  ? 483  GLN   D CG  1 
ATOM   11673 C  CD  . GLN   D  1 182 ? 19.531  -58.960 -40.759  1.00 38.12  ? 483  GLN   D CD  1 
ATOM   11674 O  OE1 . GLN   D  1 182 ? 20.293  -58.385 -41.547  1.00 47.35  ? 483  GLN   D OE1 1 
ATOM   11675 N  NE2 . GLN   D  1 182 ? 19.138  -60.210 -40.933  1.00 32.94  ? 483  GLN   D NE2 1 
ATOM   11676 N  N   . LEU   D  1 183 ? 19.206  -58.617 -35.030  1.00 20.21  ? 484  LEU   D N   1 
ATOM   11677 C  CA  . LEU   D  1 183 ? 19.291  -59.129 -33.663  1.00 22.17  ? 484  LEU   D CA  1 
ATOM   11678 C  C   . LEU   D  1 183 ? 19.524  -60.626 -33.660  1.00 28.26  ? 484  LEU   D C   1 
ATOM   11679 O  O   . LEU   D  1 183 ? 20.287  -61.144 -32.838  1.00 26.61  ? 484  LEU   D O   1 
ATOM   11680 C  CB  . LEU   D  1 183 ? 18.018  -58.798 -32.882  1.00 19.16  ? 484  LEU   D CB  1 
ATOM   11681 C  CG  . LEU   D  1 183 ? 17.701  -57.330 -32.600  1.00 21.25  ? 484  LEU   D CG  1 
ATOM   11682 C  CD1 . LEU   D  1 183 ? 16.436  -57.188 -31.773  1.00 22.65  ? 484  LEU   D CD1 1 
ATOM   11683 C  CD2 . LEU   D  1 183 ? 18.843  -56.610 -31.931  1.00 18.50  ? 484  LEU   D CD2 1 
ATOM   11684 N  N   . ILE   D  1 184 ? 18.883  -61.334 -34.583  1.00 19.35  ? 485  ILE   D N   1 
ATOM   11685 C  CA  . ILE   D  1 184 ? 19.000  -62.780 -34.692  1.00 23.55  ? 485  ILE   D CA  1 
ATOM   11686 C  C   . ILE   D  1 184 ? 19.528  -63.086 -36.089  1.00 29.54  ? 485  ILE   D C   1 
ATOM   11687 O  O   . ILE   D  1 184 ? 18.872  -62.771 -37.088  1.00 23.45  ? 485  ILE   D O   1 
ATOM   11688 C  CB  . ILE   D  1 184 ? 17.659  -63.472 -34.423  1.00 24.68  ? 485  ILE   D CB  1 
ATOM   11689 C  CG1 . ILE   D  1 184 ? 17.231  -63.211 -32.966  1.00 27.45  ? 485  ILE   D CG1 1 
ATOM   11690 C  CG2 . ILE   D  1 184 ? 17.775  -64.957 -34.653  1.00 22.97  ? 485  ILE   D CG2 1 
ATOM   11691 C  CD1 . ILE   D  1 184 ? 15.753  -63.226 -32.771  1.00 25.80  ? 485  ILE   D CD1 1 
ATOM   11692 N  N   . ARG   D  1 185 ? 20.736  -63.645 -36.158  1.00 25.97  ? 486  ARG   D N   1 
ATOM   11693 C  CA  . ARG   D  1 185 ? 21.328  -64.127 -37.404  1.00 27.71  ? 486  ARG   D CA  1 
ATOM   11694 C  C   . ARG   D  1 185 ? 22.178  -65.342 -37.074  1.00 33.60  ? 486  ARG   D C   1 
ATOM   11695 O  O   . ARG   D  1 185 ? 22.508  -65.596 -35.909  1.00 29.66  ? 486  ARG   D O   1 
ATOM   11696 C  CB  . ARG   D  1 185 ? 22.197  -63.069 -38.102  1.00 23.72  ? 486  ARG   D CB  1 
ATOM   11697 C  CG  . ARG   D  1 185 ? 21.465  -61.807 -38.531  1.00 25.59  ? 486  ARG   D CG  1 
ATOM   11698 C  CD  . ARG   D  1 185 ? 22.261  -61.036 -39.560  1.00 31.95  ? 486  ARG   D CD  1 
ATOM   11699 N  NE  . ARG   D  1 185 ? 22.278  -61.730 -40.845  1.00 32.82  ? 486  ARG   D NE  1 
ATOM   11700 C  CZ  . ARG   D  1 185 ? 22.766  -61.215 -41.969  1.00 31.05  ? 486  ARG   D CZ  1 
ATOM   11701 N  NH1 . ARG   D  1 185 ? 23.282  -59.990 -41.991  1.00 23.15  ? 486  ARG   D NH1 1 
ATOM   11702 N  NH2 . ARG   D  1 185 ? 22.741  -61.931 -43.081  1.00 28.84  ? 486  ARG   D NH2 1 
ATOM   11703 N  N   . TYR   D  1 186 ? 22.547  -66.086 -38.108  1.00 27.23  ? 487  TYR   D N   1 
ATOM   11704 C  CA  . TYR   D  1 186 ? 23.342  -67.290 -37.939  1.00 30.53  ? 487  TYR   D CA  1 
ATOM   11705 C  C   . TYR   D  1 186 ? 24.800  -66.994 -38.247  1.00 30.79  ? 487  TYR   D C   1 
ATOM   11706 O  O   . TYR   D  1 186 ? 25.112  -66.241 -39.172  1.00 32.47  ? 487  TYR   D O   1 
ATOM   11707 C  CB  . TYR   D  1 186 ? 22.824  -68.421 -38.839  1.00 24.05  ? 487  TYR   D CB  1 
ATOM   11708 C  CG  . TYR   D  1 186 ? 21.431  -68.879 -38.467  1.00 30.58  ? 487  TYR   D CG  1 
ATOM   11709 C  CD1 . TYR   D  1 186 ? 20.376  -68.784 -39.368  1.00 29.23  ? 487  TYR   D CD1 1 
ATOM   11710 C  CD2 . TYR   D  1 186 ? 21.163  -69.376 -37.187  1.00 29.49  ? 487  TYR   D CD2 1 
ATOM   11711 C  CE1 . TYR   D  1 186 ? 19.093  -69.208 -39.013  1.00 27.61  ? 487  TYR   D CE1 1 
ATOM   11712 C  CE2 . TYR   D  1 186 ? 19.900  -69.794 -36.829  1.00 28.51  ? 487  TYR   D CE2 1 
ATOM   11713 C  CZ  . TYR   D  1 186 ? 18.865  -69.706 -37.740  1.00 29.18  ? 487  TYR   D CZ  1 
ATOM   11714 O  OH  . TYR   D  1 186 ? 17.606  -70.134 -37.372  1.00 29.04  ? 487  TYR   D OH  1 
ATOM   11715 N  N   . ALA   D  1 187 ? 25.690  -67.603 -37.475  1.00 33.46  ? 488  ALA   D N   1 
ATOM   11716 C  CA  . ALA   D  1 187 ? 27.114  -67.443 -37.703  1.00 32.35  ? 488  ALA   D CA  1 
ATOM   11717 C  C   . ALA   D  1 187 ? 27.531  -68.055 -39.035  1.00 35.11  ? 488  ALA   D C   1 
ATOM   11718 O  O   . ALA   D  1 187 ? 26.841  -68.896 -39.621  1.00 33.73  ? 488  ALA   D O   1 
ATOM   11719 C  CB  . ALA   D  1 187 ? 27.920  -68.104 -36.588  1.00 30.96  ? 488  ALA   D CB  1 
ATOM   11720 N  N   . GLY   D  1 188 ? 28.696  -67.627 -39.497  1.00 31.88  ? 489  GLY   D N   1 
ATOM   11721 C  CA  . GLY   D  1 188 ? 29.323  -68.192 -40.671  1.00 31.93  ? 489  GLY   D CA  1 
ATOM   11722 C  C   . GLY   D  1 188 ? 30.793  -68.420 -40.394  1.00 36.13  ? 489  GLY   D C   1 
ATOM   11723 O  O   . GLY   D  1 188 ? 31.432  -67.616 -39.710  1.00 40.42  ? 489  GLY   D O   1 
ATOM   11724 N  N   . TYR   D  1 189 ? 31.345  -69.507 -40.912  1.00 33.85  ? 490  TYR   D N   1 
ATOM   11725 C  CA  . TYR   D  1 189 ? 32.706  -69.900 -40.582  1.00 45.07  ? 490  TYR   D CA  1 
ATOM   11726 C  C   . TYR   D  1 189 ? 33.455  -70.217 -41.862  1.00 49.15  ? 490  TYR   D C   1 
ATOM   11727 O  O   . TYR   D  1 189 ? 32.961  -70.986 -42.692  1.00 54.96  ? 490  TYR   D O   1 
ATOM   11728 C  CB  . TYR   D  1 189 ? 32.722  -71.122 -39.654  1.00 41.42  ? 490  TYR   D CB  1 
ATOM   11729 C  CG  . TYR   D  1 189 ? 31.830  -70.986 -38.441  1.00 43.01  ? 490  TYR   D CG  1 
ATOM   11730 C  CD1 . TYR   D  1 189 ? 30.555  -71.541 -38.423  1.00 39.59  ? 490  TYR   D CD1 1 
ATOM   11731 C  CD2 . TYR   D  1 189 ? 32.264  -70.301 -37.313  1.00 47.49  ? 490  TYR   D CD2 1 
ATOM   11732 C  CE1 . TYR   D  1 189 ? 29.738  -71.422 -37.306  1.00 43.98  ? 490  TYR   D CE1 1 
ATOM   11733 C  CE2 . TYR   D  1 189 ? 31.458  -70.176 -36.199  1.00 50.01  ? 490  TYR   D CE2 1 
ATOM   11734 C  CZ  . TYR   D  1 189 ? 30.198  -70.737 -36.195  1.00 47.09  ? 490  TYR   D CZ  1 
ATOM   11735 O  OH  . TYR   D  1 189 ? 29.408  -70.595 -35.070  1.00 43.20  ? 490  TYR   D OH  1 
ATOM   11736 N  N   . LYS   D  1 190 ? 34.635  -69.621 -42.021  1.00 52.67  ? 491  LYS   D N   1 
ATOM   11737 C  CA  . LYS   D  1 190 ? 35.562  -70.061 -43.057  1.00 60.09  ? 491  LYS   D CA  1 
ATOM   11738 C  C   . LYS   D  1 190 ? 36.061  -71.460 -42.714  1.00 59.42  ? 491  LYS   D C   1 
ATOM   11739 O  O   . LYS   D  1 190 ? 36.630  -71.676 -41.640  1.00 60.40  ? 491  LYS   D O   1 
ATOM   11740 C  CB  . LYS   D  1 190 ? 36.736  -69.091 -43.183  1.00 64.43  ? 491  LYS   D CB  1 
ATOM   11741 C  CG  . LYS   D  1 190 ? 36.381  -67.700 -43.695  1.00 66.68  ? 491  LYS   D CG  1 
ATOM   11742 C  CD  . LYS   D  1 190 ? 37.143  -67.375 -44.968  1.00 77.04  ? 491  LYS   D CD  1 
ATOM   11743 C  CE  . LYS   D  1 190 ? 36.610  -68.187 -46.138  1.00 82.65  ? 491  LYS   D CE  1 
ATOM   11744 N  NZ  . LYS   D  1 190 ? 35.168  -67.886 -46.376  1.00 84.75  ? 491  LYS   D NZ  1 
ATOM   11745 N  N   . GLN   D  1 191 ? 35.836  -72.406 -43.614  1.00 65.13  ? 492  GLN   D N   1 
ATOM   11746 C  CA  . GLN   D  1 191 ? 36.283  -73.777 -43.431  1.00 69.65  ? 492  GLN   D CA  1 
ATOM   11747 C  C   . GLN   D  1 191 ? 37.742  -73.941 -43.851  1.00 73.55  ? 492  GLN   D C   1 
ATOM   11748 O  O   . GLN   D  1 191 ? 38.299  -73.090 -44.551  1.00 71.40  ? 492  GLN   D O   1 
ATOM   11749 C  CB  . GLN   D  1 191 ? 35.396  -74.725 -44.235  1.00 68.16  ? 492  GLN   D CB  1 
ATOM   11750 C  CG  . GLN   D  1 191 ? 33.983  -74.877 -43.700  1.00 64.52  ? 492  GLN   D CG  1 
ATOM   11751 C  CD  . GLN   D  1 191 ? 33.927  -75.613 -42.378  1.00 66.41  ? 492  GLN   D CD  1 
ATOM   11752 O  OE1 . GLN   D  1 191 ? 34.458  -75.153 -41.367  1.00 65.47  ? 492  GLN   D OE1 1 
ATOM   11753 N  NE2 . GLN   D  1 191 ? 33.277  -76.768 -42.379  1.00 70.14  ? 492  GLN   D NE2 1 
ATOM   11754 N  N   . PRO   D  1 192 ? 38.393  -75.025 -43.413  1.00 78.30  ? 493  PRO   D N   1 
ATOM   11755 C  CA  . PRO   D  1 192 ? 39.768  -75.284 -43.883  1.00 74.25  ? 493  PRO   D CA  1 
ATOM   11756 C  C   . PRO   D  1 192 ? 39.901  -75.330 -45.400  1.00 74.97  ? 493  PRO   D C   1 
ATOM   11757 O  O   . PRO   D  1 192 ? 40.804  -74.695 -45.964  1.00 68.83  ? 493  PRO   D O   1 
ATOM   11758 C  CB  . PRO   D  1 192 ? 40.096  -76.636 -43.236  1.00 71.95  ? 493  PRO   D CB  1 
ATOM   11759 C  CG  . PRO   D  1 192 ? 39.265  -76.675 -42.005  1.00 70.80  ? 493  PRO   D CG  1 
ATOM   11760 C  CD  . PRO   D  1 192 ? 37.994  -75.940 -42.325  1.00 73.81  ? 493  PRO   D CD  1 
ATOM   11761 N  N   . ASP   D  1 193 ? 39.019  -76.063 -46.084  1.00 70.50  ? 494  ASP   D N   1 
ATOM   11762 C  CA  . ASP   D  1 193 ? 39.159  -76.231 -47.524  1.00 64.87  ? 494  ASP   D CA  1 
ATOM   11763 C  C   . ASP   D  1 193 ? 38.871  -74.949 -48.299  1.00 65.37  ? 494  ASP   D C   1 
ATOM   11764 O  O   . ASP   D  1 193 ? 39.200  -74.874 -49.488  1.00 65.95  ? 494  ASP   D O   1 
ATOM   11765 C  CB  . ASP   D  1 193 ? 38.253  -77.370 -48.005  1.00 68.22  ? 494  ASP   D CB  1 
ATOM   11766 C  CG  . ASP   D  1 193 ? 36.807  -77.190 -47.588  1.00 72.58  ? 494  ASP   D CG  1 
ATOM   11767 O  OD1 . ASP   D  1 193 ? 36.029  -78.164 -47.686  1.00 72.88  ? 494  ASP   D OD1 1 
ATOM   11768 O  OD2 . ASP   D  1 193 ? 36.441  -76.073 -47.174  1.00 73.40  ? 494  ASP   D OD2 1 
ATOM   11769 N  N   . GLY   D  1 194 ? 38.279  -73.943 -47.662  1.00 64.89  ? 495  GLY   D N   1 
ATOM   11770 C  CA  . GLY   D  1 194 ? 37.970  -72.686 -48.319  1.00 55.01  ? 495  GLY   D CA  1 
ATOM   11771 C  C   . GLY   D  1 194 ? 36.494  -72.403 -48.493  1.00 57.94  ? 495  GLY   D C   1 
ATOM   11772 O  O   . GLY   D  1 194 ? 36.134  -71.261 -48.819  1.00 59.54  ? 495  GLY   D O   1 
ATOM   11773 N  N   . SER   D  1 195 ? 35.629  -73.394 -48.292  1.00 56.09  ? 496  SER   D N   1 
ATOM   11774 C  CA  . SER   D  1 195 ? 34.188  -73.191 -48.339  1.00 56.15  ? 496  SER   D CA  1 
ATOM   11775 C  C   . SER   D  1 195 ? 33.739  -72.469 -47.065  1.00 53.76  ? 496  SER   D C   1 
ATOM   11776 O  O   . SER   D  1 195 ? 34.553  -72.073 -46.227  1.00 51.01  ? 496  SER   D O   1 
ATOM   11777 C  CB  . SER   D  1 195 ? 33.473  -74.527 -48.528  1.00 57.95  ? 496  SER   D CB  1 
ATOM   11778 O  OG  . SER   D  1 195 ? 33.694  -75.391 -47.425  1.00 59.88  ? 496  SER   D OG  1 
ATOM   11779 N  N   . THR   D  1 196 ? 32.428  -72.287 -46.904  1.00 47.48  ? 497  THR   D N   1 
ATOM   11780 C  CA  . THR   D  1 196 ? 31.869  -71.556 -45.776  1.00 45.90  ? 497  THR   D CA  1 
ATOM   11781 C  C   . THR   D  1 196 ? 30.774  -72.383 -45.123  1.00 42.80  ? 497  THR   D C   1 
ATOM   11782 O  O   . THR   D  1 196 ? 29.900  -72.922 -45.808  1.00 43.96  ? 497  THR   D O   1 
ATOM   11783 C  CB  . THR   D  1 196 ? 31.310  -70.196 -46.212  1.00 43.22  ? 497  THR   D CB  1 
ATOM   11784 O  OG1 . THR   D  1 196 ? 32.379  -69.362 -46.680  1.00 45.43  ? 497  THR   D OG1 1 
ATOM   11785 C  CG2 . THR   D  1 196 ? 30.621  -69.505 -45.040  1.00 43.62  ? 497  THR   D CG2 1 
ATOM   11786 N  N   . LEU   D  1 197 ? 30.832  -72.487 -43.802  1.00 46.22  ? 498  LEU   D N   1 
ATOM   11787 C  CA  . LEU   D  1 197 ? 29.799  -73.139 -43.011  1.00 45.23  ? 498  LEU   D CA  1 
ATOM   11788 C  C   . LEU   D  1 197 ? 28.895  -72.071 -42.406  1.00 42.37  ? 498  LEU   D C   1 
ATOM   11789 O  O   . LEU   D  1 197 ? 29.382  -71.053 -41.905  1.00 37.80  ? 498  LEU   D O   1 
ATOM   11790 C  CB  . LEU   D  1 197 ? 30.426  -73.996 -41.911  1.00 46.87  ? 498  LEU   D CB  1 
ATOM   11791 C  CG  . LEU   D  1 197 ? 29.419  -74.578 -40.925  1.00 48.77  ? 498  LEU   D CG  1 
ATOM   11792 C  CD1 . LEU   D  1 197 ? 28.549  -75.590 -41.632  1.00 56.28  ? 498  LEU   D CD1 1 
ATOM   11793 C  CD2 . LEU   D  1 197 ? 30.129  -75.198 -39.740  1.00 48.34  ? 498  LEU   D CD2 1 
ATOM   11794 N  N   . GLY   D  1 198 ? 27.582  -72.295 -42.473  1.00 36.56  ? 499  GLY   D N   1 
ATOM   11795 C  CA  . GLY   D  1 198 ? 26.643  -71.307 -41.971  1.00 32.58  ? 499  GLY   D CA  1 
ATOM   11796 C  C   . GLY   D  1 198 ? 26.369  -70.198 -42.978  1.00 33.98  ? 499  GLY   D C   1 
ATOM   11797 O  O   . GLY   D  1 198 ? 26.427  -70.399 -44.188  1.00 38.62  ? 499  GLY   D O   1 
ATOM   11798 N  N   . ASP   D  1 199 ? 26.079  -69.002 -42.459  1.00 31.11  ? 500  ASP   D N   1 
ATOM   11799 C  CA  . ASP   D  1 199 ? 25.743  -67.853 -43.295  1.00 26.56  ? 500  ASP   D CA  1 
ATOM   11800 C  C   . ASP   D  1 199 ? 27.009  -67.114 -43.718  1.00 31.15  ? 500  ASP   D C   1 
ATOM   11801 O  O   . ASP   D  1 199 ? 27.628  -66.441 -42.876  1.00 30.27  ? 500  ASP   D O   1 
ATOM   11802 C  CB  . ASP   D  1 199 ? 24.816  -66.903 -42.544  1.00 27.63  ? 500  ASP   D CB  1 
ATOM   11803 C  CG  . ASP   D  1 199 ? 24.158  -65.890 -43.462  1.00 34.35  ? 500  ASP   D CG  1 
ATOM   11804 O  OD1 . ASP   D  1 199 ? 24.695  -65.662 -44.567  1.00 38.67  ? 500  ASP   D OD1 1 
ATOM   11805 O  OD2 . ASP   D  1 199 ? 23.105  -65.326 -43.089  1.00 31.45  ? 500  ASP   D OD2 1 
ATOM   11806 N  N   . PRO   D  1 200 ? 27.390  -67.141 -45.004  1.00 36.49  ? 501  PRO   D N   1 
ATOM   11807 C  CA  . PRO   D  1 200 ? 28.624  -66.438 -45.422  1.00 29.79  ? 501  PRO   D CA  1 
ATOM   11808 C  C   . PRO   D  1 200 ? 28.592  -64.933 -45.207  1.00 30.67  ? 501  PRO   D C   1 
ATOM   11809 O  O   . PRO   D  1 200 ? 29.653  -64.322 -45.032  1.00 36.59  ? 501  PRO   D O   1 
ATOM   11810 C  CB  . PRO   D  1 200 ? 28.736  -66.795 -46.916  1.00 28.86  ? 501  PRO   D CB  1 
ATOM   11811 C  CG  . PRO   D  1 200 ? 28.011  -68.119 -47.019  1.00 32.22  ? 501  PRO   D CG  1 
ATOM   11812 C  CD  . PRO   D  1 200 ? 26.839  -67.977 -46.090  1.00 27.05  ? 501  PRO   D CD  1 
ATOM   11813 N  N   . ALA   D  1 201 ? 27.411  -64.314 -45.221  1.00 27.57  ? 502  ALA   D N   1 
ATOM   11814 C  CA  . ALA   D  1 201 ? 27.314  -62.881 -44.945  1.00 34.03  ? 502  ALA   D CA  1 
ATOM   11815 C  C   . ALA   D  1 201 ? 27.870  -62.520 -43.569  1.00 42.99  ? 502  ALA   D C   1 
ATOM   11816 O  O   . ALA   D  1 201 ? 28.376  -61.407 -43.373  1.00 37.21  ? 502  ALA   D O   1 
ATOM   11817 C  CB  . ALA   D  1 201 ? 25.855  -62.428 -45.054  1.00 31.10  ? 502  ALA   D CB  1 
ATOM   11818 N  N   . ASN   D  1 202 ? 27.806  -63.441 -42.609  1.00 40.09  ? 503  ASN   D N   1 
ATOM   11819 C  CA  . ASN   D  1 202 ? 28.161  -63.123 -41.233  1.00 34.50  ? 503  ASN   D CA  1 
ATOM   11820 C  C   . ASN   D  1 202 ? 29.541  -63.630 -40.845  1.00 39.64  ? 503  ASN   D C   1 
ATOM   11821 O  O   . ASN   D  1 202 ? 29.873  -63.654 -39.656  1.00 35.15  ? 503  ASN   D O   1 
ATOM   11822 C  CB  . ASN   D  1 202 ? 27.090  -63.667 -40.294  1.00 26.33  ? 503  ASN   D CB  1 
ATOM   11823 C  CG  . ASN   D  1 202 ? 25.761  -63.002 -40.540  1.00 25.02  ? 503  ASN   D CG  1 
ATOM   11824 O  OD1 . ASN   D  1 202 ? 25.727  -61.835 -40.928  1.00 34.37  ? 503  ASN   D OD1 1 
ATOM   11825 N  ND2 . ASN   D  1 202 ? 24.664  -63.733 -40.360  1.00 24.29  ? 503  ASN   D ND2 1 
ATOM   11826 N  N   . VAL   D  1 203 ? 30.364  -64.005 -41.826  1.00 34.94  ? 504  VAL   D N   1 
ATOM   11827 C  CA  . VAL   D  1 203 ? 31.688  -64.537 -41.512  1.00 38.92  ? 504  VAL   D CA  1 
ATOM   11828 C  C   . VAL   D  1 203 ? 32.513  -63.504 -40.752  1.00 39.34  ? 504  VAL   D C   1 
ATOM   11829 O  O   . VAL   D  1 203 ? 33.113  -63.809 -39.713  1.00 47.17  ? 504  VAL   D O   1 
ATOM   11830 C  CB  . VAL   D  1 203 ? 32.391  -65.005 -42.794  1.00 37.19  ? 504  VAL   D CB  1 
ATOM   11831 C  CG1 . VAL   D  1 203 ? 33.875  -65.180 -42.546  1.00 32.49  ? 504  VAL   D CG1 1 
ATOM   11832 C  CG2 . VAL   D  1 203 ? 31.757  -66.304 -43.270  1.00 34.68  ? 504  VAL   D CG2 1 
ATOM   11833 N  N   . GLN   D  1 204 ? 32.535  -62.263 -41.238  1.00 35.82  ? 505  GLN   D N   1 
ATOM   11834 C  CA  . GLN   D  1 204 ? 33.327  -61.233 -40.571  1.00 34.74  ? 505  GLN   D CA  1 
ATOM   11835 C  C   . GLN   D  1 204 ? 32.779  -60.931 -39.179  1.00 36.54  ? 505  GLN   D C   1 
ATOM   11836 O  O   . GLN   D  1 204 ? 33.538  -60.824 -38.210  1.00 34.65  ? 505  GLN   D O   1 
ATOM   11837 C  CB  . GLN   D  1 204 ? 33.366  -59.957 -41.409  1.00 31.21  ? 505  GLN   D CB  1 
ATOM   11838 C  CG  . GLN   D  1 204 ? 34.286  -58.902 -40.820  1.00 42.85  ? 505  GLN   D CG  1 
ATOM   11839 C  CD  . GLN   D  1 204 ? 34.140  -57.548 -41.482  1.00 47.99  ? 505  GLN   D CD  1 
ATOM   11840 O  OE1 . GLN   D  1 204 ? 33.062  -57.190 -41.962  1.00 53.14  ? 505  GLN   D OE1 1 
ATOM   11841 N  NE2 . GLN   D  1 204 ? 35.228  -56.782 -41.512  1.00 50.84  ? 505  GLN   D NE2 1 
ATOM   11842 N  N   . PHE   D  1 205 ? 31.464  -60.764 -39.059  1.00 33.80  ? 506  PHE   D N   1 
ATOM   11843 C  CA  . PHE   D  1 205 ? 30.901  -60.524 -37.741  1.00 35.60  ? 506  PHE   D CA  1 
ATOM   11844 C  C   . PHE   D  1 205 ? 31.187  -61.693 -36.802  1.00 36.13  ? 506  PHE   D C   1 
ATOM   11845 O  O   . PHE   D  1 205 ? 31.554  -61.494 -35.638  1.00 32.87  ? 506  PHE   D O   1 
ATOM   11846 C  CB  . PHE   D  1 205 ? 29.397  -60.261 -37.851  1.00 32.60  ? 506  PHE   D CB  1 
ATOM   11847 C  CG  . PHE   D  1 205 ? 28.770  -59.902 -36.545  1.00 38.32  ? 506  PHE   D CG  1 
ATOM   11848 C  CD1 . PHE   D  1 205 ? 28.988  -58.652 -35.985  1.00 37.88  ? 506  PHE   D CD1 1 
ATOM   11849 C  CD2 . PHE   D  1 205 ? 27.990  -60.820 -35.857  1.00 34.23  ? 506  PHE   D CD2 1 
ATOM   11850 C  CE1 . PHE   D  1 205 ? 28.424  -58.314 -34.765  1.00 32.52  ? 506  PHE   D CE1 1 
ATOM   11851 C  CE2 . PHE   D  1 205 ? 27.420  -60.489 -34.635  1.00 39.03  ? 506  PHE   D CE2 1 
ATOM   11852 C  CZ  . PHE   D  1 205 ? 27.638  -59.233 -34.090  1.00 33.24  ? 506  PHE   D CZ  1 
ATOM   11853 N  N   . THR   D  1 206 ? 31.054  -62.920 -37.301  1.00 27.04  ? 507  THR   D N   1 
ATOM   11854 C  CA  . THR   D  1 206 ? 31.360  -64.090 -36.489  1.00 31.96  ? 507  THR   D CA  1 
ATOM   11855 C  C   . THR   D  1 206 ? 32.804  -64.065 -35.997  1.00 37.23  ? 507  THR   D C   1 
ATOM   11856 O  O   . THR   D  1 206 ? 33.072  -64.337 -34.819  1.00 40.00  ? 507  THR   D O   1 
ATOM   11857 C  CB  . THR   D  1 206 ? 31.075  -65.362 -37.291  1.00 31.76  ? 507  THR   D CB  1 
ATOM   11858 O  OG1 . THR   D  1 206 ? 29.685  -65.376 -37.658  1.00 32.89  ? 507  THR   D OG1 1 
ATOM   11859 C  CG2 . THR   D  1 206 ? 31.404  -66.622 -36.474  1.00 29.67  ? 507  THR   D CG2 1 
ATOM   11860 N  N   . GLU   D  1 207 ? 33.746  -63.714 -36.873  1.00 34.35  ? 508  GLU   D N   1 
ATOM   11861 C  CA  . GLU   D  1 207 ? 35.149  -63.684 -36.466  1.00 37.69  ? 508  GLU   D CA  1 
ATOM   11862 C  C   . GLU   D  1 207 ? 35.389  -62.637 -35.390  1.00 34.30  ? 508  GLU   D C   1 
ATOM   11863 O  O   . GLU   D  1 207 ? 36.209  -62.849 -34.493  1.00 43.47  ? 508  GLU   D O   1 
ATOM   11864 C  CB  . GLU   D  1 207 ? 36.050  -63.429 -37.677  1.00 42.15  ? 508  GLU   D CB  1 
ATOM   11865 C  CG  . GLU   D  1 207 ? 36.104  -64.604 -38.650  1.00 57.67  ? 508  GLU   D CG  1 
ATOM   11866 C  CD  . GLU   D  1 207 ? 36.834  -64.300 -39.963  1.00 65.80  ? 508  GLU   D CD  1 
ATOM   11867 O  OE1 . GLU   D  1 207 ? 37.012  -63.106 -40.309  1.00 60.05  ? 508  GLU   D OE1 1 
ATOM   11868 O  OE2 . GLU   D  1 207 ? 37.222  -65.275 -40.650  1.00 65.00  ? 508  GLU   D OE2 1 
ATOM   11869 N  N   . ILE   D  1 208 ? 34.681  -61.507 -35.462  1.00 38.64  ? 509  ILE   D N   1 
ATOM   11870 C  CA  . ILE   D  1 208 ? 34.754  -60.514 -34.392  1.00 39.71  ? 509  ILE   D CA  1 
ATOM   11871 C  C   . ILE   D  1 208 ? 34.262  -61.117 -33.080  1.00 37.76  ? 509  ILE   D C   1 
ATOM   11872 O  O   . ILE   D  1 208 ? 34.905  -60.986 -32.031  1.00 37.82  ? 509  ILE   D O   1 
ATOM   11873 C  CB  . ILE   D  1 208 ? 33.947  -59.262 -34.772  1.00 40.72  ? 509  ILE   D CB  1 
ATOM   11874 C  CG1 . ILE   D  1 208 ? 34.580  -58.570 -35.983  1.00 46.26  ? 509  ILE   D CG1 1 
ATOM   11875 C  CG2 . ILE   D  1 208 ? 33.862  -58.322 -33.590  1.00 37.53  ? 509  ILE   D CG2 1 
ATOM   11876 C  CD1 . ILE   D  1 208 ? 33.721  -57.454 -36.581  1.00 42.39  ? 509  ILE   D CD1 1 
ATOM   11877 N  N   . CYS   D  1 209 ? 33.122  -61.807 -33.128  1.00 34.51  ? 510  CYS   D N   1 
ATOM   11878 C  CA  . CYS   D  1 209 ? 32.585  -62.439 -31.927  1.00 33.89  ? 510  CYS   D CA  1 
ATOM   11879 C  C   . CYS   D  1 209 ? 33.572  -63.432 -31.341  1.00 39.32  ? 510  CYS   D C   1 
ATOM   11880 O  O   . CYS   D  1 209 ? 33.838  -63.420 -30.130  1.00 40.24  ? 510  CYS   D O   1 
ATOM   11881 C  CB  . CYS   D  1 209 ? 31.265  -63.126 -32.250  1.00 38.03  ? 510  CYS   D CB  1 
ATOM   11882 S  SG  . CYS   D  1 209 ? 29.960  -61.944 -32.617  1.00 36.93  ? 510  CYS   D SG  1 
ATOM   11883 N  N   . ILE   D  1 210 ? 34.128  -64.303 -32.190  1.00 34.59  ? 511  ILE   D N   1 
ATOM   11884 C  CA  . ILE   D  1 210 ? 35.118  -65.269 -31.727  1.00 39.68  ? 511  ILE   D CA  1 
ATOM   11885 C  C   . ILE   D  1 210 ? 36.312  -64.547 -31.115  1.00 40.85  ? 511  ILE   D C   1 
ATOM   11886 O  O   . ILE   D  1 210 ? 36.800  -64.921 -30.040  1.00 45.29  ? 511  ILE   D O   1 
ATOM   11887 C  CB  . ILE   D  1 210 ? 35.530  -66.194 -32.883  1.00 45.89  ? 511  ILE   D CB  1 
ATOM   11888 C  CG1 . ILE   D  1 210 ? 34.307  -66.953 -33.396  1.00 48.63  ? 511  ILE   D CG1 1 
ATOM   11889 C  CG2 . ILE   D  1 210 ? 36.599  -67.174 -32.421  1.00 41.72  ? 511  ILE   D CG2 1 
ATOM   11890 C  CD1 . ILE   D  1 210 ? 34.597  -67.853 -34.580  1.00 48.00  ? 511  ILE   D CD1 1 
ATOM   11891 N  N   . GLN   D  1 211 ? 36.778  -63.486 -31.780  1.00 40.78  ? 512  GLN   D N   1 
ATOM   11892 C  CA  . GLN   D  1 211 ? 37.847  -62.649 -31.245  1.00 43.50  ? 512  GLN   D CA  1 
ATOM   11893 C  C   . GLN   D  1 211 ? 37.523  -62.178 -29.834  1.00 44.45  ? 512  GLN   D C   1 
ATOM   11894 O  O   . GLN   D  1 211 ? 38.399  -62.144 -28.962  1.00 48.95  ? 512  GLN   D O   1 
ATOM   11895 C  CB  . GLN   D  1 211 ? 38.060  -61.448 -32.167  1.00 58.06  ? 512  GLN   D CB  1 
ATOM   11896 C  CG  . GLN   D  1 211 ? 39.470  -60.912 -32.219  1.00 76.62  ? 512  GLN   D CG  1 
ATOM   11897 C  CD  . GLN   D  1 211 ? 40.062  -61.019 -33.618  1.00 95.18  ? 512  GLN   D CD  1 
ATOM   11898 O  OE1 . GLN   D  1 211 ? 39.410  -61.509 -34.544  1.00 93.73  ? 512  GLN   D OE1 1 
ATOM   11899 N  NE2 . GLN   D  1 211 ? 41.303  -60.564 -33.776  1.00 102.70 ? 512  GLN   D NE2 1 
ATOM   11900 N  N   . GLN   D  1 212 ? 36.264  -61.835 -29.587  1.00 37.54  ? 513  GLN   D N   1 
ATOM   11901 C  CA  . GLN   D  1 212 ? 35.837  -61.294 -28.309  1.00 37.89  ? 513  GLN   D CA  1 
ATOM   11902 C  C   . GLN   D  1 212 ? 35.537  -62.376 -27.283  1.00 47.24  ? 513  GLN   D C   1 
ATOM   11903 O  O   . GLN   D  1 212 ? 34.944  -62.076 -26.241  1.00 49.97  ? 513  GLN   D O   1 
ATOM   11904 C  CB  . GLN   D  1 212 ? 34.617  -60.395 -28.512  1.00 46.07  ? 513  GLN   D CB  1 
ATOM   11905 C  CG  . GLN   D  1 212 ? 34.897  -59.193 -29.405  1.00 47.13  ? 513  GLN   D CG  1 
ATOM   11906 C  CD  . GLN   D  1 212 ? 36.110  -58.412 -28.940  1.00 52.51  ? 513  GLN   D CD  1 
ATOM   11907 O  OE1 . GLN   D  1 212 ? 36.209  -58.046 -27.773  1.00 54.35  ? 513  GLN   D OE1 1 
ATOM   11908 N  NE2 . GLN   D  1 212 ? 37.046  -58.165 -29.849  1.00 64.32  ? 513  GLN   D NE2 1 
ATOM   11909 N  N   . GLY   D  1 213 ? 35.938  -63.616 -27.550  1.00 46.96  ? 514  GLY   D N   1 
ATOM   11910 C  CA  . GLY   D  1 213 ? 35.762  -64.701 -26.612  1.00 44.94  ? 514  GLY   D CA  1 
ATOM   11911 C  C   . GLY   D  1 213 ? 34.554  -65.577 -26.851  1.00 42.33  ? 514  GLY   D C   1 
ATOM   11912 O  O   . GLY   D  1 213 ? 34.305  -66.481 -26.051  1.00 49.83  ? 514  GLY   D O   1 
ATOM   11913 N  N   . TRP   D  1 214 ? 33.792  -65.347 -27.913  1.00 44.07  ? 515  TRP   D N   1 
ATOM   11914 C  CA  . TRP   D  1 214 ? 32.639  -66.198 -28.159  1.00 42.91  ? 515  TRP   D CA  1 
ATOM   11915 C  C   . TRP   D  1 214 ? 33.110  -67.594 -28.552  1.00 49.98  ? 515  TRP   D C   1 
ATOM   11916 O  O   . TRP   D  1 214 ? 34.014  -67.746 -29.381  1.00 47.40  ? 515  TRP   D O   1 
ATOM   11917 C  CB  . TRP   D  1 214 ? 31.744  -65.604 -29.244  1.00 41.86  ? 515  TRP   D CB  1 
ATOM   11918 C  CG  . TRP   D  1 214 ? 30.468  -66.370 -29.411  1.00 45.84  ? 515  TRP   D CG  1 
ATOM   11919 C  CD1 . TRP   D  1 214 ? 29.549  -66.652 -28.437  1.00 41.73  ? 515  TRP   D CD1 1 
ATOM   11920 C  CD2 . TRP   D  1 214 ? 29.966  -66.957 -30.616  1.00 41.57  ? 515  TRP   D CD2 1 
ATOM   11921 N  NE1 . TRP   D  1 214 ? 28.510  -67.380 -28.963  1.00 41.21  ? 515  TRP   D NE1 1 
ATOM   11922 C  CE2 . TRP   D  1 214 ? 28.740  -67.581 -30.298  1.00 37.41  ? 515  TRP   D CE2 1 
ATOM   11923 C  CE3 . TRP   D  1 214 ? 30.431  -67.013 -31.935  1.00 41.34  ? 515  TRP   D CE3 1 
ATOM   11924 C  CZ2 . TRP   D  1 214 ? 27.974  -68.248 -31.246  1.00 36.67  ? 515  TRP   D CZ2 1 
ATOM   11925 C  CZ3 . TRP   D  1 214 ? 29.667  -67.682 -32.880  1.00 44.51  ? 515  TRP   D CZ3 1 
ATOM   11926 C  CH2 . TRP   D  1 214 ? 28.451  -68.287 -32.532  1.00 41.16  ? 515  TRP   D CH2 1 
ATOM   11927 N  N   . LYS   D  1 215 ? 32.515  -68.614 -27.923  1.00 47.47  ? 516  LYS   D N   1 
ATOM   11928 C  CA  . LYS   D  1 215 ? 32.809  -70.003 -28.245  1.00 49.21  ? 516  LYS   D CA  1 
ATOM   11929 C  C   . LYS   D  1 215 ? 31.781  -70.481 -29.255  1.00 50.05  ? 516  LYS   D C   1 
ATOM   11930 O  O   . LYS   D  1 215 ? 30.616  -70.706 -28.906  1.00 55.44  ? 516  LYS   D O   1 
ATOM   11931 C  CB  . LYS   D  1 215 ? 32.787  -70.888 -27.000  1.00 52.94  ? 516  LYS   D CB  1 
ATOM   11932 C  CG  . LYS   D  1 215 ? 33.594  -70.342 -25.839  1.00 63.03  ? 516  LYS   D CG  1 
ATOM   11933 C  CD  . LYS   D  1 215 ? 35.040  -70.036 -26.231  1.00 64.83  ? 516  LYS   D CD  1 
ATOM   11934 C  CE  . LYS   D  1 215 ? 35.865  -69.655 -25.002  1.00 67.46  ? 516  LYS   D CE  1 
ATOM   11935 N  NZ  . LYS   D  1 215 ? 37.203  -69.116 -25.352  1.00 65.24  ? 516  LYS   D NZ  1 
ATOM   11936 N  N   . PRO   D  1 216 ? 32.168  -70.625 -30.512  1.00 47.39  ? 517  PRO   D N   1 
ATOM   11937 C  CA  . PRO   D  1 216 ? 31.217  -70.997 -31.537  1.00 47.56  ? 517  PRO   D CA  1 
ATOM   11938 C  C   . PRO   D  1 216 ? 30.930  -72.484 -31.486  1.00 48.17  ? 517  PRO   D C   1 
ATOM   11939 O  O   . PRO   D  1 216 ? 31.855  -73.303 -31.407  1.00 46.45  ? 517  PRO   D O   1 
ATOM   11940 C  CB  . PRO   D  1 216 ? 31.942  -70.615 -32.830  1.00 51.28  ? 517  PRO   D CB  1 
ATOM   11941 C  CG  . PRO   D  1 216 ? 33.388  -70.801 -32.486  1.00 54.69  ? 517  PRO   D CG  1 
ATOM   11942 C  CD  . PRO   D  1 216 ? 33.522  -70.411 -31.050  1.00 49.60  ? 517  PRO   D CD  1 
ATOM   11943 N  N   . PRO   D  1 217 ? 29.657  -72.875 -31.528  1.00 49.07  ? 518  PRO   D N   1 
ATOM   11944 C  CA  . PRO   D  1 217 ? 29.339  -74.300 -31.726  1.00 51.80  ? 518  PRO   D CA  1 
ATOM   11945 C  C   . PRO   D  1 217 ? 29.781  -74.823 -33.090  1.00 52.16  ? 518  PRO   D C   1 
ATOM   11946 O  O   . PRO   D  1 217 ? 29.861  -76.045 -33.274  1.00 50.50  ? 518  PRO   D O   1 
ATOM   11947 C  CB  . PRO   D  1 217 ? 27.810  -74.351 -31.578  1.00 48.04  ? 518  PRO   D CB  1 
ATOM   11948 C  CG  . PRO   D  1 217 ? 27.395  -73.005 -31.069  1.00 43.50  ? 518  PRO   D CG  1 
ATOM   11949 C  CD  . PRO   D  1 217 ? 28.455  -72.034 -31.482  1.00 44.95  ? 518  PRO   D CD  1 
ATOM   11950 N  N   . ARG   D  1 218 ? 30.066  -73.934 -34.045  1.00 47.74  ? 519  ARG   D N   1 
ATOM   11951 C  CA  . ARG   D  1 218 ? 30.544  -74.308 -35.380  1.00 53.57  ? 519  ARG   D CA  1 
ATOM   11952 C  C   . ARG   D  1 218 ? 29.545  -75.204 -36.107  1.00 49.98  ? 519  ARG   D C   1 
ATOM   11953 O  O   . ARG   D  1 218 ? 29.909  -76.219 -36.706  1.00 53.31  ? 519  ARG   D O   1 
ATOM   11954 C  CB  . ARG   D  1 218 ? 31.925  -74.965 -35.319  1.00 60.32  ? 519  ARG   D CB  1 
ATOM   11955 C  CG  . ARG   D  1 218 ? 33.013  -74.037 -34.807  1.00 66.40  ? 519  ARG   D CG  1 
ATOM   11956 C  CD  . ARG   D  1 218 ? 34.369  -74.371 -35.405  1.00 69.95  ? 519  ARG   D CD  1 
ATOM   11957 N  NE  . ARG   D  1 218 ? 34.896  -73.250 -36.180  1.00 77.12  ? 519  ARG   D NE  1 
ATOM   11958 C  CZ  . ARG   D  1 218 ? 35.616  -72.258 -35.662  1.00 79.72  ? 519  ARG   D CZ  1 
ATOM   11959 N  NH1 . ARG   D  1 218 ? 36.049  -71.273 -36.439  1.00 81.17  ? 519  ARG   D NH1 1 
ATOM   11960 N  NH2 . ARG   D  1 218 ? 35.904  -72.249 -34.366  1.00 77.75  ? 519  ARG   D NH2 1 
ATOM   11961 N  N   . GLY   D  1 219 ? 28.269  -74.827 -36.045  1.00 47.38  ? 520  GLY   D N   1 
ATOM   11962 C  CA  . GLY   D  1 219 ? 27.235  -75.441 -36.840  1.00 45.00  ? 520  GLY   D CA  1 
ATOM   11963 C  C   . GLY   D  1 219 ? 26.801  -74.546 -37.987  1.00 44.54  ? 520  GLY   D C   1 
ATOM   11964 O  O   . GLY   D  1 219 ? 27.354  -73.471 -38.227  1.00 40.28  ? 520  GLY   D O   1 
ATOM   11965 N  N   . ARG   D  1 220 ? 25.774  -75.007 -38.696  1.00 46.56  ? 521  ARG   D N   1 
ATOM   11966 C  CA  . ARG   D  1 220 ? 25.258  -74.267 -39.839  1.00 44.53  ? 521  ARG   D CA  1 
ATOM   11967 C  C   . ARG   D  1 220 ? 24.230  -73.211 -39.451  1.00 37.62  ? 521  ARG   D C   1 
ATOM   11968 O  O   . ARG   D  1 220 ? 23.969  -72.290 -40.238  1.00 34.18  ? 521  ARG   D O   1 
ATOM   11969 C  CB  . ARG   D  1 220 ? 24.651  -75.243 -40.852  1.00 44.08  ? 521  ARG   D CB  1 
ATOM   11970 C  CG  . ARG   D  1 220 ? 24.388  -74.620 -42.194  1.00 41.56  ? 521  ARG   D CG  1 
ATOM   11971 C  CD  . ARG   D  1 220 ? 23.829  -75.629 -43.168  1.00 54.38  ? 521  ARG   D CD  1 
ATOM   11972 N  NE  . ARG   D  1 220 ? 24.032  -75.172 -44.535  1.00 56.81  ? 521  ARG   D NE  1 
ATOM   11973 C  CZ  . ARG   D  1 220 ? 23.265  -75.511 -45.564  1.00 62.43  ? 521  ARG   D CZ  1 
ATOM   11974 N  NH1 . ARG   D  1 220 ? 22.222  -76.310 -45.381  1.00 63.08  ? 521  ARG   D NH1 1 
ATOM   11975 N  NH2 . ARG   D  1 220 ? 23.540  -75.035 -46.772  1.00 59.01  ? 521  ARG   D NH2 1 
ATOM   11976 N  N   . PHE   D  1 221 ? 23.647  -73.315 -38.259  1.00 34.97  ? 522  PHE   D N   1 
ATOM   11977 C  CA  . PHE   D  1 221 ? 22.627  -72.381 -37.808  1.00 34.92  ? 522  PHE   D CA  1 
ATOM   11978 C  C   . PHE   D  1 221 ? 22.887  -72.009 -36.346  1.00 38.41  ? 522  PHE   D C   1 
ATOM   11979 O  O   . PHE   D  1 221 ? 22.050  -72.169 -35.461  1.00 45.61  ? 522  PHE   D O   1 
ATOM   11980 C  CB  . PHE   D  1 221 ? 21.231  -72.970 -37.997  1.00 40.73  ? 522  PHE   D CB  1 
ATOM   11981 C  CG  . PHE   D  1 221 ? 20.876  -73.240 -39.439  1.00 40.88  ? 522  PHE   D CG  1 
ATOM   11982 C  CD1 . PHE   D  1 221 ? 20.951  -74.529 -39.955  1.00 41.18  ? 522  PHE   D CD1 1 
ATOM   11983 C  CD2 . PHE   D  1 221 ? 20.485  -72.206 -40.283  1.00 36.12  ? 522  PHE   D CD2 1 
ATOM   11984 C  CE1 . PHE   D  1 221 ? 20.636  -74.783 -41.284  1.00 44.00  ? 522  PHE   D CE1 1 
ATOM   11985 C  CE2 . PHE   D  1 221 ? 20.170  -72.459 -41.615  1.00 39.76  ? 522  PHE   D CE2 1 
ATOM   11986 C  CZ  . PHE   D  1 221 ? 20.249  -73.750 -42.111  1.00 41.78  ? 522  PHE   D CZ  1 
ATOM   11987 N  N   . ASP   D  1 222 ? 24.085  -71.499 -36.082  1.00 40.13  ? 523  ASP   D N   1 
ATOM   11988 C  CA  . ASP   D  1 222 ? 24.439  -71.014 -34.753  1.00 37.83  ? 523  ASP   D CA  1 
ATOM   11989 C  C   . ASP   D  1 222 ? 23.924  -69.594 -34.605  1.00 34.72  ? 523  ASP   D C   1 
ATOM   11990 O  O   . ASP   D  1 222 ? 24.421  -68.685 -35.274  1.00 29.80  ? 523  ASP   D O   1 
ATOM   11991 C  CB  . ASP   D  1 222 ? 25.949  -71.048 -34.548  1.00 41.06  ? 523  ASP   D CB  1 
ATOM   11992 C  CG  . ASP   D  1 222 ? 26.517  -72.445 -34.633  1.00 45.48  ? 523  ASP   D CG  1 
ATOM   11993 O  OD1 . ASP   D  1 222 ? 25.745  -73.414 -34.457  1.00 45.90  ? 523  ASP   D OD1 1 
ATOM   11994 O  OD2 . ASP   D  1 222 ? 27.737  -72.571 -34.871  1.00 42.36  ? 523  ASP   D OD2 1 
ATOM   11995 N  N   . VAL   D  1 223 ? 22.931  -69.394 -33.733  1.00 32.44  ? 524  VAL   D N   1 
ATOM   11996 C  CA  . VAL   D  1 223 ? 22.470  -68.036 -33.462  1.00 30.80  ? 524  VAL   D CA  1 
ATOM   11997 C  C   . VAL   D  1 223 ? 23.618  -67.242 -32.870  1.00 26.73  ? 524  VAL   D C   1 
ATOM   11998 O  O   . VAL   D  1 223 ? 24.223  -67.643 -31.870  1.00 32.32  ? 524  VAL   D O   1 
ATOM   11999 C  CB  . VAL   D  1 223 ? 21.254  -68.032 -32.526  1.00 35.04  ? 524  VAL   D CB  1 
ATOM   12000 C  CG1 . VAL   D  1 223 ? 20.934  -66.599 -32.088  1.00 29.43  ? 524  VAL   D CG1 1 
ATOM   12001 C  CG2 . VAL   D  1 223 ? 20.048  -68.666 -33.218  1.00 32.30  ? 524  VAL   D CG2 1 
ATOM   12002 N  N   . LEU   D  1 224 ? 23.936  -66.124 -33.503  1.00 23.85  ? 525  LEU   D N   1 
ATOM   12003 C  CA  . LEU   D  1 224 ? 25.045  -65.303 -33.075  1.00 28.72  ? 525  LEU   D CA  1 
ATOM   12004 C  C   . LEU   D  1 224 ? 24.740  -64.647 -31.729  1.00 28.20  ? 525  LEU   D C   1 
ATOM   12005 O  O   . LEU   D  1 224 ? 23.577  -64.383 -31.401  1.00 23.06  ? 525  LEU   D O   1 
ATOM   12006 C  CB  . LEU   D  1 224 ? 25.336  -64.228 -34.118  1.00 28.27  ? 525  LEU   D CB  1 
ATOM   12007 C  CG  . LEU   D  1 224 ? 26.097  -64.798 -35.312  1.00 36.17  ? 525  LEU   D CG  1 
ATOM   12008 C  CD1 . LEU   D  1 224 ? 25.881  -63.990 -36.578  1.00 28.27  ? 525  LEU   D CD1 1 
ATOM   12009 C  CD2 . LEU   D  1 224 ? 27.571  -64.874 -34.940  1.00 32.39  ? 525  LEU   D CD2 1 
ATOM   12010 N  N   . PRO   D  1 225 ? 25.769  -64.352 -30.947  1.00 24.57  ? 526  PRO   D N   1 
ATOM   12011 C  CA  . PRO   D  1 225 ? 25.559  -63.556 -29.739  1.00 25.70  ? 526  PRO   D CA  1 
ATOM   12012 C  C   . PRO   D  1 225 ? 25.258  -62.124 -30.135  1.00 32.39  ? 526  PRO   D C   1 
ATOM   12013 O  O   . PRO   D  1 225 ? 25.537  -61.695 -31.257  1.00 30.93  ? 526  PRO   D O   1 
ATOM   12014 C  CB  . PRO   D  1 225 ? 26.902  -63.661 -29.016  1.00 25.53  ? 526  PRO   D CB  1 
ATOM   12015 C  CG  . PRO   D  1 225 ? 27.884  -63.761 -30.143  1.00 32.53  ? 526  PRO   D CG  1 
ATOM   12016 C  CD  . PRO   D  1 225 ? 27.200  -64.584 -31.209  1.00 27.81  ? 526  PRO   D CD  1 
ATOM   12017 N  N   . LEU   D  1 226 ? 24.645  -61.393 -29.213  1.00 25.07  ? 527  LEU   D N   1 
ATOM   12018 C  CA  . LEU   D  1 226 ? 24.565  -59.948 -29.355  1.00 27.26  ? 527  LEU   D CA  1 
ATOM   12019 C  C   . LEU   D  1 226 ? 25.909  -59.325 -29.005  1.00 26.99  ? 527  LEU   D C   1 
ATOM   12020 O  O   . LEU   D  1 226 ? 26.565  -59.735 -28.045  1.00 32.27  ? 527  LEU   D O   1 
ATOM   12021 C  CB  . LEU   D  1 226 ? 23.485  -59.375 -28.448  1.00 28.39  ? 527  LEU   D CB  1 
ATOM   12022 C  CG  . LEU   D  1 226 ? 22.058  -59.752 -28.835  1.00 28.84  ? 527  LEU   D CG  1 
ATOM   12023 C  CD1 . LEU   D  1 226 ? 21.110  -59.407 -27.682  1.00 24.83  ? 527  LEU   D CD1 1 
ATOM   12024 C  CD2 . LEU   D  1 226 ? 21.636  -59.079 -30.155  1.00 22.42  ? 527  LEU   D CD2 1 
ATOM   12025 N  N   . LEU   D  1 227 ? 26.334  -58.352 -29.807  1.00 30.31  ? 528  LEU   D N   1 
ATOM   12026 C  CA  . LEU   D  1 227 ? 27.538  -57.566 -29.533  1.00 30.46  ? 528  LEU   D CA  1 
ATOM   12027 C  C   . LEU   D  1 227 ? 27.056  -56.137 -29.344  1.00 31.77  ? 528  LEU   D C   1 
ATOM   12028 O  O   . LEU   D  1 227 ? 26.737  -55.456 -30.325  1.00 27.62  ? 528  LEU   D O   1 
ATOM   12029 C  CB  . LEU   D  1 227 ? 28.551  -57.660 -30.664  1.00 33.52  ? 528  LEU   D CB  1 
ATOM   12030 C  CG  . LEU   D  1 227 ? 30.005  -58.052 -30.391  1.00 36.42  ? 528  LEU   D CG  1 
ATOM   12031 C  CD1 . LEU   D  1 227 ? 30.892  -57.557 -31.542  1.00 36.16  ? 528  LEU   D CD1 1 
ATOM   12032 C  CD2 . LEU   D  1 227 ? 30.518  -57.599 -29.026  1.00 28.74  ? 528  LEU   D CD2 1 
ATOM   12033 N  N   . LEU   D  1 228 ? 27.000  -55.691 -28.090  1.00 34.39  ? 529  LEU   D N   1 
ATOM   12034 C  CA  . LEU   D  1 228 ? 26.310  -54.464 -27.710  1.00 32.19  ? 529  LEU   D CA  1 
ATOM   12035 C  C   . LEU   D  1 228 ? 27.297  -53.418 -27.218  1.00 34.61  ? 529  LEU   D C   1 
ATOM   12036 O  O   . LEU   D  1 228 ? 28.104  -53.688 -26.317  1.00 30.89  ? 529  LEU   D O   1 
ATOM   12037 C  CB  . LEU   D  1 228 ? 25.268  -54.746 -26.635  1.00 26.96  ? 529  LEU   D CB  1 
ATOM   12038 C  CG  . LEU   D  1 228 ? 24.256  -55.786 -27.117  1.00 25.00  ? 529  LEU   D CG  1 
ATOM   12039 C  CD1 . LEU   D  1 228 ? 23.226  -56.063 -26.046  1.00 21.32  ? 529  LEU   D CD1 1 
ATOM   12040 C  CD2 . LEU   D  1 228 ? 23.582  -55.333 -28.407  1.00 23.38  ? 529  LEU   D CD2 1 
ATOM   12041 N  N   . GLN   D  1 229 ? 27.200  -52.221 -27.793  1.00 28.06  ? 530  GLN   D N   1 
ATOM   12042 C  CA  . GLN   D  1 229 ? 28.034  -51.081 -27.444  1.00 27.44  ? 530  GLN   D CA  1 
ATOM   12043 C  C   . GLN   D  1 229 ? 27.153  -49.990 -26.858  1.00 28.01  ? 530  GLN   D C   1 
ATOM   12044 O  O   . GLN   D  1 229 ? 26.212  -49.528 -27.517  1.00 27.82  ? 530  GLN   D O   1 
ATOM   12045 C  CB  . GLN   D  1 229 ? 28.771  -50.544 -28.667  1.00 30.91  ? 530  GLN   D CB  1 
ATOM   12046 C  CG  . GLN   D  1 229 ? 29.379  -49.176 -28.429  1.00 36.69  ? 530  GLN   D CG  1 
ATOM   12047 C  CD  . GLN   D  1 229 ? 30.119  -48.672 -29.638  1.00 37.03  ? 530  GLN   D CD  1 
ATOM   12048 O  OE1 . GLN   D  1 229 ? 29.922  -49.172 -30.735  1.00 38.86  ? 530  GLN   D OE1 1 
ATOM   12049 N  NE2 . GLN   D  1 229 ? 30.992  -47.694 -29.443  1.00 50.07  ? 530  GLN   D NE2 1 
ATOM   12050 N  N   . ALA   D  1 230 ? 27.459  -49.592 -25.628  1.00 30.12  ? 531  ALA   D N   1 
ATOM   12051 C  CA  . ALA   D  1 230 ? 26.772  -48.527 -24.915  1.00 31.58  ? 531  ALA   D CA  1 
ATOM   12052 C  C   . ALA   D  1 230 ? 27.733  -47.376 -24.674  1.00 33.06  ? 531  ALA   D C   1 
ATOM   12053 O  O   . ALA   D  1 230 ? 28.883  -47.592 -24.268  1.00 31.01  ? 531  ALA   D O   1 
ATOM   12054 C  CB  . ALA   D  1 230 ? 26.240  -49.006 -23.563  1.00 37.50  ? 531  ALA   D CB  1 
ATOM   12055 N  N   . ASN   D  1 231 ? 27.257  -46.159 -24.928  1.00 33.47  ? 532  ASN   D N   1 
ATOM   12056 C  CA  . ASN   D  1 231 ? 27.979  -44.943 -24.561  1.00 34.00  ? 532  ASN   D CA  1 
ATOM   12057 C  C   . ASN   D  1 231 ? 29.424  -44.957 -25.057  1.00 36.37  ? 532  ASN   D C   1 
ATOM   12058 O  O   . ASN   D  1 231 ? 30.348  -44.525 -24.361  1.00 36.53  ? 532  ASN   D O   1 
ATOM   12059 C  CB  . ASN   D  1 231 ? 27.935  -44.727 -23.052  1.00 35.71  ? 532  ASN   D CB  1 
ATOM   12060 C  CG  . ASN   D  1 231 ? 28.178  -43.281 -22.674  1.00 50.42  ? 532  ASN   D CG  1 
ATOM   12061 O  OD1 . ASN   D  1 231 ? 27.779  -42.368 -23.401  1.00 57.62  ? 532  ASN   D OD1 1 
ATOM   12062 N  ND2 . ASN   D  1 231 ? 28.847  -43.063 -21.545  1.00 50.26  ? 532  ASN   D ND2 1 
ATOM   12063 N  N   . GLY   D  1 232 ? 29.624  -45.463 -26.271  1.00 33.71  ? 533  GLY   D N   1 
ATOM   12064 C  CA  . GLY   D  1 232 ? 30.927  -45.445 -26.915  1.00 34.20  ? 533  GLY   D CA  1 
ATOM   12065 C  C   . GLY   D  1 232 ? 31.936  -46.441 -26.390  1.00 37.53  ? 533  GLY   D C   1 
ATOM   12066 O  O   . GLY   D  1 232 ? 33.042  -46.524 -26.938  1.00 37.47  ? 533  GLY   D O   1 
ATOM   12067 N  N   . ASN   D  1 233 ? 31.601  -47.203 -25.353  1.00 36.81  ? 534  ASN   D N   1 
ATOM   12068 C  CA  . ASN   D  1 233 ? 32.544  -48.149 -24.786  1.00 41.88  ? 534  ASN   D CA  1 
ATOM   12069 C  C   . ASN   D  1 233 ? 32.709  -49.359 -25.705  1.00 36.61  ? 534  ASN   D C   1 
ATOM   12070 O  O   . ASN   D  1 233 ? 31.940  -49.569 -26.647  1.00 31.59  ? 534  ASN   D O   1 
ATOM   12071 C  CB  . ASN   D  1 233 ? 32.079  -48.568 -23.393  1.00 44.45  ? 534  ASN   D CB  1 
ATOM   12072 C  CG  . ASN   D  1 233 ? 31.914  -47.378 -22.468  1.00 49.19  ? 534  ASN   D CG  1 
ATOM   12073 O  OD1 . ASN   D  1 233 ? 32.777  -46.503 -22.414  1.00 56.00  ? 534  ASN   D OD1 1 
ATOM   12074 N  ND2 . ASN   D  1 233 ? 30.793  -47.318 -21.767  1.00 46.63  ? 534  ASN   D ND2 1 
ATOM   12075 N  N   . ASP   D  1 234 ? 33.739  -50.152 -25.429  1.00 35.13  ? 535  ASP   D N   1 
ATOM   12076 C  CA  . ASP   D  1 234 ? 33.931  -51.394 -26.162  1.00 36.67  ? 535  ASP   D CA  1 
ATOM   12077 C  C   . ASP   D  1 234 ? 32.640  -52.215 -26.138  1.00 29.07  ? 535  ASP   D C   1 
ATOM   12078 O  O   . ASP   D  1 234 ? 31.929  -52.222 -25.124  1.00 33.32  ? 535  ASP   D O   1 
ATOM   12079 C  CB  . ASP   D  1 234 ? 35.073  -52.212 -25.551  1.00 47.07  ? 535  ASP   D CB  1 
ATOM   12080 C  CG  . ASP   D  1 234 ? 36.434  -51.582 -25.772  1.00 49.39  ? 535  ASP   D CG  1 
ATOM   12081 O  OD1 . ASP   D  1 234 ? 37.379  -51.960 -25.047  1.00 53.49  ? 535  ASP   D OD1 1 
ATOM   12082 O  OD2 . ASP   D  1 234 ? 36.557  -50.712 -26.659  1.00 48.56  ? 535  ASP   D OD2 1 
ATOM   12083 N  N   . PRO   D  1 235 ? 32.296  -52.902 -27.220  1.00 34.69  ? 536  PRO   D N   1 
ATOM   12084 C  CA  . PRO   D  1 235 ? 31.073  -53.707 -27.204  1.00 35.01  ? 536  PRO   D CA  1 
ATOM   12085 C  C   . PRO   D  1 235 ? 31.267  -54.955 -26.357  1.00 39.13  ? 536  PRO   D C   1 
ATOM   12086 O  O   . PRO   D  1 235 ? 32.390  -55.389 -26.096  1.00 37.54  ? 536  PRO   D O   1 
ATOM   12087 C  CB  . PRO   D  1 235 ? 30.848  -54.044 -28.681  1.00 28.64  ? 536  PRO   D CB  1 
ATOM   12088 C  CG  . PRO   D  1 235 ? 32.223  -54.022 -29.281  1.00 29.12  ? 536  PRO   D CG  1 
ATOM   12089 C  CD  . PRO   D  1 235 ? 32.999  -52.971 -28.516  1.00 29.12  ? 536  PRO   D CD  1 
ATOM   12090 N  N   . GLU   D  1 236 ? 30.144  -55.516 -25.895  1.00 26.30  ? 537  GLU   D N   1 
ATOM   12091 C  CA  . GLU   D  1 236 ? 30.161  -56.674 -25.013  1.00 26.86  ? 537  GLU   D CA  1 
ATOM   12092 C  C   . GLU   D  1 236 ? 29.270  -57.780 -25.573  1.00 34.04  ? 537  GLU   D C   1 
ATOM   12093 O  O   . GLU   D  1 236 ? 28.203  -57.507 -26.121  1.00 32.14  ? 537  GLU   D O   1 
ATOM   12094 C  CB  . GLU   D  1 236 ? 29.688  -56.279 -23.592  1.00 28.36  ? 537  GLU   D CB  1 
ATOM   12095 C  CG  . GLU   D  1 236 ? 30.556  -55.201 -22.962  1.00 36.59  ? 537  GLU   D CG  1 
ATOM   12096 C  CD  . GLU   D  1 236 ? 29.967  -54.592 -21.687  1.00 47.41  ? 537  GLU   D CD  1 
ATOM   12097 O  OE1 . GLU   D  1 236 ? 29.210  -55.281 -20.957  1.00 47.57  ? 537  GLU   D OE1 1 
ATOM   12098 O  OE2 . GLU   D  1 236 ? 30.279  -53.409 -21.418  1.00 48.95  ? 537  GLU   D OE2 1 
ATOM   12099 N  N   . LEU   D  1 237 ? 29.692  -59.031 -25.397  1.00 37.47  ? 538  LEU   D N   1 
ATOM   12100 C  CA  . LEU   D  1 237 ? 28.935  -60.175 -25.892  1.00 27.17  ? 538  LEU   D CA  1 
ATOM   12101 C  C   . LEU   D  1 237 ? 27.835  -60.598 -24.926  1.00 32.02  ? 538  LEU   D C   1 
ATOM   12102 O  O   . LEU   D  1 237 ? 28.019  -60.594 -23.707  1.00 30.34  ? 538  LEU   D O   1 
ATOM   12103 C  CB  . LEU   D  1 237 ? 29.866  -61.367 -26.125  1.00 28.50  ? 538  LEU   D CB  1 
ATOM   12104 C  CG  . LEU   D  1 237 ? 30.780  -61.236 -27.342  1.00 35.35  ? 538  LEU   D CG  1 
ATOM   12105 C  CD1 . LEU   D  1 237 ? 31.853  -62.318 -27.323  1.00 34.79  ? 538  LEU   D CD1 1 
ATOM   12106 C  CD2 . LEU   D  1 237 ? 29.961  -61.294 -28.616  1.00 32.95  ? 538  LEU   D CD2 1 
ATOM   12107 N  N   . PHE   D  1 238 ? 26.708  -61.018 -25.486  1.00 28.25  ? 539  PHE   D N   1 
ATOM   12108 C  CA  . PHE   D  1 238 ? 25.610  -61.574 -24.710  1.00 30.87  ? 539  PHE   D CA  1 
ATOM   12109 C  C   . PHE   D  1 238 ? 24.936  -62.656 -25.532  1.00 29.59  ? 539  PHE   D C   1 
ATOM   12110 O  O   . PHE   D  1 238 ? 24.687  -62.458 -26.722  1.00 32.36  ? 539  PHE   D O   1 
ATOM   12111 C  CB  . PHE   D  1 238 ? 24.571  -60.512 -24.350  1.00 31.10  ? 539  PHE   D CB  1 
ATOM   12112 C  CG  . PHE   D  1 238 ? 25.111  -59.398 -23.524  1.00 29.71  ? 539  PHE   D CG  1 
ATOM   12113 C  CD1 . PHE   D  1 238 ? 25.670  -58.277 -24.129  1.00 26.50  ? 539  PHE   D CD1 1 
ATOM   12114 C  CD2 . PHE   D  1 238 ? 25.065  -59.470 -22.138  1.00 25.43  ? 539  PHE   D CD2 1 
ATOM   12115 C  CE1 . PHE   D  1 238 ? 26.171  -57.242 -23.360  1.00 25.74  ? 539  PHE   D CE1 1 
ATOM   12116 C  CE2 . PHE   D  1 238 ? 25.563  -58.437 -21.365  1.00 26.81  ? 539  PHE   D CE2 1 
ATOM   12117 C  CZ  . PHE   D  1 238 ? 26.116  -57.320 -21.976  1.00 25.21  ? 539  PHE   D CZ  1 
ATOM   12118 N  N   . GLN   D  1 239 ? 24.617  -63.782 -24.901  1.00 36.30  ? 540  GLN   D N   1 
ATOM   12119 C  CA  . GLN   D  1 239 ? 23.858  -64.832 -25.570  1.00 35.18  ? 540  GLN   D CA  1 
ATOM   12120 C  C   . GLN   D  1 239 ? 22.367  -64.583 -25.381  1.00 30.05  ? 540  GLN   D C   1 
ATOM   12121 O  O   . GLN   D  1 239 ? 21.872  -64.572 -24.247  1.00 29.73  ? 540  GLN   D O   1 
ATOM   12122 C  CB  . GLN   D  1 239 ? 24.236  -66.210 -25.032  1.00 31.51  ? 540  GLN   D CB  1 
ATOM   12123 C  CG  . GLN   D  1 239 ? 23.411  -67.345 -25.630  1.00 41.33  ? 540  GLN   D CG  1 
ATOM   12124 C  CD  . GLN   D  1 239 ? 23.394  -68.586 -24.740  1.00 55.50  ? 540  GLN   D CD  1 
ATOM   12125 O  OE1 . GLN   D  1 239 ? 24.116  -69.548 -24.988  1.00 66.89  ? 540  GLN   D OE1 1 
ATOM   12126 N  NE2 . GLN   D  1 239 ? 22.563  -68.566 -23.705  1.00 55.20  ? 540  GLN   D NE2 1 
ATOM   12127 N  N   . ILE   D  1 240 ? 21.652  -64.397 -26.484  1.00 29.44  ? 541  ILE   D N   1 
ATOM   12128 C  CA  . ILE   D  1 240 ? 20.194  -64.314 -26.381  1.00 27.47  ? 541  ILE   D CA  1 
ATOM   12129 C  C   . ILE   D  1 240 ? 19.678  -65.614 -25.789  1.00 30.47  ? 541  ILE   D C   1 
ATOM   12130 O  O   . ILE   D  1 240 ? 20.078  -66.700 -26.253  1.00 30.67  ? 541  ILE   D O   1 
ATOM   12131 C  CB  . ILE   D  1 240 ? 19.562  -64.060 -27.759  1.00 30.60  ? 541  ILE   D CB  1 
ATOM   12132 C  CG1 . ILE   D  1 240 ? 20.178  -62.831 -28.413  1.00 32.00  ? 541  ILE   D CG1 1 
ATOM   12133 C  CG2 . ILE   D  1 240 ? 18.058  -63.879 -27.624  1.00 26.58  ? 541  ILE   D CG2 1 
ATOM   12134 C  CD1 . ILE   D  1 240 ? 19.674  -62.585 -29.820  1.00 34.74  ? 541  ILE   D CD1 1 
ATOM   12135 N  N   . PRO   D  1 241 ? 18.846  -65.576 -24.753  1.00 35.72  ? 542  PRO   D N   1 
ATOM   12136 C  CA  . PRO   D  1 241 ? 18.255  -66.810 -24.234  1.00 36.55  ? 542  PRO   D CA  1 
ATOM   12137 C  C   . PRO   D  1 241 ? 17.557  -67.568 -25.348  1.00 32.25  ? 542  PRO   D C   1 
ATOM   12138 O  O   . PRO   D  1 241 ? 16.689  -67.009 -26.040  1.00 31.54  ? 542  PRO   D O   1 
ATOM   12139 C  CB  . PRO   D  1 241 ? 17.260  -66.311 -23.175  1.00 40.17  ? 542  PRO   D CB  1 
ATOM   12140 C  CG  . PRO   D  1 241 ? 17.839  -65.014 -22.718  1.00 34.92  ? 542  PRO   D CG  1 
ATOM   12141 C  CD  . PRO   D  1 241 ? 18.485  -64.401 -23.943  1.00 33.70  ? 542  PRO   D CD  1 
ATOM   12142 N  N   . PRO   D  1 242 ? 17.939  -68.829 -25.574  1.00 35.03  ? 543  PRO   D N   1 
ATOM   12143 C  CA  . PRO   D  1 242 ? 17.421  -69.553 -26.745  1.00 31.39  ? 543  PRO   D CA  1 
ATOM   12144 C  C   . PRO   D  1 242 ? 15.911  -69.680 -26.742  1.00 35.20  ? 543  PRO   D C   1 
ATOM   12145 O  O   . PRO   D  1 242 ? 15.301  -69.724 -27.820  1.00 33.82  ? 543  PRO   D O   1 
ATOM   12146 C  CB  . PRO   D  1 242 ? 18.115  -70.918 -26.646  1.00 35.81  ? 543  PRO   D CB  1 
ATOM   12147 C  CG  . PRO   D  1 242 ? 19.336  -70.662 -25.821  1.00 38.49  ? 543  PRO   D CG  1 
ATOM   12148 C  CD  . PRO   D  1 242 ? 18.930  -69.624 -24.828  1.00 34.40  ? 543  PRO   D CD  1 
ATOM   12149 N  N   . GLU   D  1 243 ? 15.280  -69.702 -25.562  1.00 28.31  ? 544  GLU   D N   1 
ATOM   12150 C  CA  . GLU   D  1 243 ? 13.828  -69.774 -25.534  1.00 27.90  ? 544  GLU   D CA  1 
ATOM   12151 C  C   . GLU   D  1 243 ? 13.198  -68.502 -26.074  1.00 29.48  ? 544  GLU   D C   1 
ATOM   12152 O  O   . GLU   D  1 243 ? 12.012  -68.505 -26.413  1.00 32.51  ? 544  GLU   D O   1 
ATOM   12153 C  CB  . GLU   D  1 243 ? 13.326  -70.062 -24.110  1.00 29.70  ? 544  GLU   D CB  1 
ATOM   12154 C  CG  . GLU   D  1 243 ? 13.601  -68.948 -23.095  1.00 30.87  ? 544  GLU   D CG  1 
ATOM   12155 C  CD  . GLU   D  1 243 ? 14.972  -69.057 -22.467  1.00 32.92  ? 544  GLU   D CD  1 
ATOM   12156 O  OE1 . GLU   D  1 243 ? 15.792  -69.839 -22.982  1.00 35.09  ? 544  GLU   D OE1 1 
ATOM   12157 O  OE2 . GLU   D  1 243 ? 15.230  -68.379 -21.444  1.00 46.06  ? 544  GLU   D OE2 1 
ATOM   12158 N  N   . LEU   D  1 244 ? 13.959  -67.415 -26.157  1.00 24.78  ? 545  LEU   D N   1 
ATOM   12159 C  CA  . LEU   D  1 244 ? 13.454  -66.219 -26.808  1.00 24.77  ? 545  LEU   D CA  1 
ATOM   12160 C  C   . LEU   D  1 244 ? 13.598  -66.256 -28.327  1.00 28.73  ? 545  LEU   D C   1 
ATOM   12161 O  O   . LEU   D  1 244 ? 12.969  -65.432 -28.999  1.00 24.33  ? 545  LEU   D O   1 
ATOM   12162 C  CB  . LEU   D  1 244 ? 14.163  -64.978 -26.273  1.00 21.52  ? 545  LEU   D CB  1 
ATOM   12163 C  CG  . LEU   D  1 244 ? 13.852  -64.649 -24.811  1.00 36.17  ? 545  LEU   D CG  1 
ATOM   12164 C  CD1 . LEU   D  1 244 ? 14.375  -63.263 -24.451  1.00 37.70  ? 545  LEU   D CD1 1 
ATOM   12165 C  CD2 . LEU   D  1 244 ? 12.356  -64.778 -24.498  1.00 35.15  ? 545  LEU   D CD2 1 
ATOM   12166 N  N   . VAL   D  1 245 ? 14.406  -67.165 -28.880  1.00 29.35  ? 546  VAL   D N   1 
ATOM   12167 C  CA  . VAL   D  1 245 ? 14.714  -67.187 -30.317  1.00 27.41  ? 546  VAL   D CA  1 
ATOM   12168 C  C   . VAL   D  1 245 ? 13.816  -68.238 -30.954  1.00 26.76  ? 546  VAL   D C   1 
ATOM   12169 O  O   . VAL   D  1 245 ? 14.115  -69.433 -30.920  1.00 30.06  ? 546  VAL   D O   1 
ATOM   12170 C  CB  . VAL   D  1 245 ? 16.190  -67.491 -30.592  1.00 29.63  ? 546  VAL   D CB  1 
ATOM   12171 C  CG1 . VAL   D  1 245 ? 16.470  -67.476 -32.115  1.00 29.81  ? 546  VAL   D CG1 1 
ATOM   12172 C  CG2 . VAL   D  1 245 ? 17.098  -66.514 -29.874  1.00 25.97  ? 546  VAL   D CG2 1 
ATOM   12173 N  N   . LEU   D  1 246 ? 12.702  -67.793 -31.519  1.00 25.99  ? 547  LEU   D N   1 
ATOM   12174 C  CA  . LEU   D  1 246 ? 11.760  -68.695 -32.163  1.00 24.23  ? 547  LEU   D CA  1 
ATOM   12175 C  C   . LEU   D  1 246 ? 12.313  -69.083 -33.529  1.00 31.64  ? 547  LEU   D C   1 
ATOM   12176 O  O   . LEU   D  1 246 ? 12.673  -68.214 -34.326  1.00 35.22  ? 547  LEU   D O   1 
ATOM   12177 C  CB  . LEU   D  1 246 ? 10.394  -68.028 -32.286  1.00 26.43  ? 547  LEU   D CB  1 
ATOM   12178 C  CG  . LEU   D  1 246 ? 9.275   -68.794 -32.985  1.00 33.28  ? 547  LEU   D CG  1 
ATOM   12179 C  CD1 . LEU   D  1 246 ? 9.115   -70.166 -32.390  1.00 32.97  ? 547  LEU   D CD1 1 
ATOM   12180 C  CD2 . LEU   D  1 246 ? 7.981   -68.026 -32.857  1.00 29.74  ? 547  LEU   D CD2 1 
ATOM   12181 N  N   . GLU   D  1 247 ? 12.412  -70.383 -33.780  1.00 30.49  ? 548  GLU   D N   1 
ATOM   12182 C  CA  . GLU   D  1 247 ? 12.956  -70.909 -35.021  1.00 31.08  ? 548  GLU   D CA  1 
ATOM   12183 C  C   . GLU   D  1 247 ? 11.950  -71.866 -35.638  1.00 35.80  ? 548  GLU   D C   1 
ATOM   12184 O  O   . GLU   D  1 247 ? 11.158  -72.493 -34.933  1.00 35.11  ? 548  GLU   D O   1 
ATOM   12185 C  CB  . GLU   D  1 247 ? 14.299  -71.619 -34.786  1.00 30.37  ? 548  GLU   D CB  1 
ATOM   12186 C  CG  . GLU   D  1 247 ? 15.440  -70.642 -34.472  1.00 29.72  ? 548  GLU   D CG  1 
ATOM   12187 C  CD  . GLU   D  1 247 ? 16.751  -71.343 -34.179  1.00 37.33  ? 548  GLU   D CD  1 
ATOM   12188 O  OE1 . GLU   D  1 247 ? 16.824  -72.091 -33.185  1.00 43.75  ? 548  GLU   D OE1 1 
ATOM   12189 O  OE2 . GLU   D  1 247 ? 17.716  -71.146 -34.937  1.00 37.92  ? 548  GLU   D OE2 1 
ATOM   12190 N  N   . VAL   D  1 248 ? 11.974  -71.960 -36.963  1.00 32.99  ? 549  VAL   D N   1 
ATOM   12191 C  CA  . VAL   D  1 248 ? 11.039  -72.783 -37.713  1.00 33.59  ? 549  VAL   D CA  1 
ATOM   12192 C  C   . VAL   D  1 248 ? 11.841  -73.815 -38.494  1.00 31.94  ? 549  VAL   D C   1 
ATOM   12193 O  O   . VAL   D  1 248 ? 12.618  -73.446 -39.381  1.00 35.98  ? 549  VAL   D O   1 
ATOM   12194 C  CB  . VAL   D  1 248 ? 10.172  -71.943 -38.666  1.00 33.90  ? 549  VAL   D CB  1 
ATOM   12195 C  CG1 . VAL   D  1 248 ? 9.156   -72.835 -39.399  1.00 28.07  ? 549  VAL   D CG1 1 
ATOM   12196 C  CG2 . VAL   D  1 248 ? 9.492   -70.802 -37.905  1.00 28.24  ? 549  VAL   D CG2 1 
ATOM   12197 N  N   . PRO   D  1 249 ? 11.696  -75.110 -38.208  1.00 32.46  ? 550  PRO   D N   1 
ATOM   12198 C  CA  . PRO   D  1 249 ? 12.290  -76.129 -39.088  1.00 33.95  ? 550  PRO   D CA  1 
ATOM   12199 C  C   . PRO   D  1 249 ? 11.586  -76.106 -40.437  1.00 31.78  ? 550  PRO   D C   1 
ATOM   12200 O  O   . PRO   D  1 249 ? 10.357  -76.049 -40.498  1.00 34.41  ? 550  PRO   D O   1 
ATOM   12201 C  CB  . PRO   D  1 249 ? 12.029  -77.448 -38.342  1.00 30.13  ? 550  PRO   D CB  1 
ATOM   12202 C  CG  . PRO   D  1 249 ? 11.590  -77.045 -36.937  1.00 35.79  ? 550  PRO   D CG  1 
ATOM   12203 C  CD  . PRO   D  1 249 ? 10.943  -75.705 -37.089  1.00 32.46  ? 550  PRO   D CD  1 
ATOM   12204 N  N   . ILE   D  1 250 ? 12.358  -76.132 -41.520  1.00 34.10  ? 551  ILE   D N   1 
ATOM   12205 C  CA  . ILE   D  1 250 ? 11.774  -76.004 -42.855  1.00 30.35  ? 551  ILE   D CA  1 
ATOM   12206 C  C   . ILE   D  1 250 ? 11.479  -77.390 -43.405  1.00 33.61  ? 551  ILE   D C   1 
ATOM   12207 O  O   . ILE   D  1 250 ? 12.375  -78.234 -43.532  1.00 36.31  ? 551  ILE   D O   1 
ATOM   12208 C  CB  . ILE   D  1 250 ? 12.678  -75.217 -43.811  1.00 32.98  ? 551  ILE   D CB  1 
ATOM   12209 C  CG1 . ILE   D  1 250 ? 13.089  -73.877 -43.186  1.00 32.61  ? 551  ILE   D CG1 1 
ATOM   12210 C  CG2 . ILE   D  1 250 ? 11.946  -74.997 -45.156  1.00 31.85  ? 551  ILE   D CG2 1 
ATOM   12211 C  CD1 . ILE   D  1 250 ? 11.952  -72.931 -42.940  1.00 25.43  ? 551  ILE   D CD1 1 
ATOM   12212 N  N   . ARG   D  1 251 ? 10.216  -77.631 -43.709  1.00 35.76  ? 552  ARG   D N   1 
ATOM   12213 C  CA  . ARG   D  1 251 ? 9.789   -78.846 -44.376  1.00 41.50  ? 552  ARG   D CA  1 
ATOM   12214 C  C   . ARG   D  1 251 ? 8.858   -78.457 -45.518  1.00 39.43  ? 552  ARG   D C   1 
ATOM   12215 O  O   . ARG   D  1 251 ? 8.396   -77.316 -45.605  1.00 34.28  ? 552  ARG   D O   1 
ATOM   12216 C  CB  . ARG   D  1 251 ? 9.110   -79.816 -43.399  1.00 44.46  ? 552  ARG   D CB  1 
ATOM   12217 C  CG  . ARG   D  1 251 ? 7.897   -79.262 -42.673  1.00 40.29  ? 552  ARG   D CG  1 
ATOM   12218 C  CD  . ARG   D  1 251 ? 8.282   -78.491 -41.426  1.00 44.20  ? 552  ARG   D CD  1 
ATOM   12219 N  NE  . ARG   D  1 251 ? 7.124   -78.313 -40.564  1.00 46.53  ? 552  ARG   D NE  1 
ATOM   12220 C  CZ  . ARG   D  1 251 ? 7.042   -77.421 -39.583  1.00 41.13  ? 552  ARG   D CZ  1 
ATOM   12221 N  NH1 . ARG   D  1 251 ? 5.933   -77.350 -38.866  1.00 40.32  ? 552  ARG   D NH1 1 
ATOM   12222 N  NH2 . ARG   D  1 251 ? 8.055   -76.598 -39.323  1.00 32.47  ? 552  ARG   D NH2 1 
ATOM   12223 N  N   . HIS   D  1 252 ? 8.603   -79.419 -46.411  1.00 34.00  ? 553  HIS   D N   1 
ATOM   12224 C  CA  . HIS   D  1 252 ? 7.814   -79.202 -47.605  1.00 33.11  ? 553  HIS   D CA  1 
ATOM   12225 C  C   . HIS   D  1 252 ? 6.509   -79.986 -47.533  1.00 38.10  ? 553  HIS   D C   1 
ATOM   12226 O  O   . HIS   D  1 252 ? 6.501   -81.131 -47.076  1.00 35.08  ? 553  HIS   D O   1 
ATOM   12227 C  CB  . HIS   D  1 252 ? 8.604   -79.641 -48.845  1.00 34.11  ? 553  HIS   D CB  1 
ATOM   12228 C  CG  . HIS   D  1 252 ? 8.047   -79.142 -50.138  1.00 37.01  ? 553  HIS   D CG  1 
ATOM   12229 N  ND1 . HIS   D  1 252 ? 6.965   -79.728 -50.760  1.00 41.43  ? 553  HIS   D ND1 1 
ATOM   12230 C  CD2 . HIS   D  1 252 ? 8.445   -78.130 -50.947  1.00 38.12  ? 553  HIS   D CD2 1 
ATOM   12231 C  CE1 . HIS   D  1 252 ? 6.714   -79.093 -51.893  1.00 40.08  ? 553  HIS   D CE1 1 
ATOM   12232 N  NE2 . HIS   D  1 252 ? 7.596   -78.118 -52.029  1.00 39.52  ? 553  HIS   D NE2 1 
ATOM   12233 N  N   . PRO   D  1 253 ? 5.395   -79.407 -47.989  1.00 31.73  ? 554  PRO   D N   1 
ATOM   12234 C  CA  . PRO   D  1 253 ? 4.103   -80.106 -47.891  1.00 36.01  ? 554  PRO   D CA  1 
ATOM   12235 C  C   . PRO   D  1 253 ? 3.996   -81.341 -48.768  1.00 43.25  ? 554  PRO   D C   1 
ATOM   12236 O  O   . PRO   D  1 253 ? 3.076   -82.143 -48.565  1.00 48.29  ? 554  PRO   D O   1 
ATOM   12237 C  CB  . PRO   D  1 253 ? 3.096   -79.034 -48.324  1.00 39.13  ? 554  PRO   D CB  1 
ATOM   12238 C  CG  . PRO   D  1 253 ? 3.903   -78.064 -49.136  1.00 39.20  ? 554  PRO   D CG  1 
ATOM   12239 C  CD  . PRO   D  1 253 ? 5.252   -78.034 -48.495  1.00 31.75  ? 554  PRO   D CD  1 
ATOM   12240 N  N   . LYS   D  1 254 ? 4.889   -81.513 -49.733  1.00 40.49  ? 555  LYS   D N   1 
ATOM   12241 C  CA  . LYS   D  1 254 ? 4.870   -82.615 -50.683  1.00 45.80  ? 555  LYS   D CA  1 
ATOM   12242 C  C   . LYS   D  1 254 ? 6.136   -83.454 -50.629  1.00 48.23  ? 555  LYS   D C   1 
ATOM   12243 O  O   . LYS   D  1 254 ? 6.065   -84.684 -50.669  1.00 55.12  ? 555  LYS   D O   1 
ATOM   12244 C  CB  . LYS   D  1 254 ? 4.676   -82.044 -52.101  1.00 51.69  ? 555  LYS   D CB  1 
ATOM   12245 C  CG  . LYS   D  1 254 ? 4.352   -83.048 -53.193  1.00 59.64  ? 555  LYS   D CG  1 
ATOM   12246 C  CD  . LYS   D  1 254 ? 4.184   -82.340 -54.547  1.00 64.23  ? 555  LYS   D CD  1 
ATOM   12247 C  CE  . LYS   D  1 254 ? 5.452   -81.577 -54.956  1.00 63.54  ? 555  LYS   D CE  1 
ATOM   12248 N  NZ  . LYS   D  1 254 ? 5.291   -80.683 -56.155  1.00 64.65  ? 555  LYS   D NZ  1 
ATOM   12249 N  N   . PHE   D  1 255 ? 7.296   -82.815 -50.509  1.00 45.57  ? 556  PHE   D N   1 
ATOM   12250 C  CA  . PHE   D  1 255 ? 8.591   -83.488 -50.563  1.00 41.42  ? 556  PHE   D CA  1 
ATOM   12251 C  C   . PHE   D  1 255 ? 8.985   -83.897 -49.149  1.00 43.38  ? 556  PHE   D C   1 
ATOM   12252 O  O   . PHE   D  1 255 ? 9.529   -83.092 -48.385  1.00 40.93  ? 556  PHE   D O   1 
ATOM   12253 C  CB  . PHE   D  1 255 ? 9.642   -82.569 -51.173  1.00 40.82  ? 556  PHE   D CB  1 
ATOM   12254 C  CG  . PHE   D  1 255 ? 9.410   -82.248 -52.630  1.00 40.08  ? 556  PHE   D CG  1 
ATOM   12255 C  CD1 . PHE   D  1 255 ? 9.713   -80.991 -53.129  1.00 41.08  ? 556  PHE   D CD1 1 
ATOM   12256 C  CD2 . PHE   D  1 255 ? 8.912   -83.206 -53.493  1.00 40.39  ? 556  PHE   D CD2 1 
ATOM   12257 C  CE1 . PHE   D  1 255 ? 9.513   -80.691 -54.474  1.00 42.54  ? 556  PHE   D CE1 1 
ATOM   12258 C  CE2 . PHE   D  1 255 ? 8.709   -82.921 -54.830  1.00 44.12  ? 556  PHE   D CE2 1 
ATOM   12259 C  CZ  . PHE   D  1 255 ? 9.011   -81.662 -55.324  1.00 36.84  ? 556  PHE   D CZ  1 
ATOM   12260 N  N   . GLU   D  1 256 ? 8.730   -85.158 -48.798  1.00 42.51  ? 557  GLU   D N   1 
ATOM   12261 C  CA  . GLU   D  1 256 ? 9.063   -85.610 -47.451  1.00 46.12  ? 557  GLU   D CA  1 
ATOM   12262 C  C   . GLU   D  1 256 ? 10.565  -85.586 -47.198  1.00 43.56  ? 557  GLU   D C   1 
ATOM   12263 O  O   . GLU   D  1 256 ? 10.987  -85.505 -46.043  1.00 43.00  ? 557  GLU   D O   1 
ATOM   12264 C  CB  . GLU   D  1 256 ? 8.487   -87.008 -47.211  1.00 56.02  ? 557  GLU   D CB  1 
ATOM   12265 C  CG  . GLU   D  1 256 ? 6.964   -87.043 -47.286  1.00 70.06  ? 557  GLU   D CG  1 
ATOM   12266 C  CD  . GLU   D  1 256 ? 6.380   -88.424 -47.028  1.00 86.47  ? 557  GLU   D CD  1 
ATOM   12267 O  OE1 . GLU   D  1 256 ? 7.154   -89.402 -46.951  1.00 90.57  ? 557  GLU   D OE1 1 
ATOM   12268 O  OE2 . GLU   D  1 256 ? 5.140   -88.531 -46.903  1.00 91.06  ? 557  GLU   D OE2 1 
ATOM   12269 N  N   . TRP   D  1 257 ? 11.381  -85.615 -48.251  1.00 47.51  ? 558  TRP   D N   1 
ATOM   12270 C  CA  . TRP   D  1 257 ? 12.823  -85.528 -48.074  1.00 45.16  ? 558  TRP   D CA  1 
ATOM   12271 C  C   . TRP   D  1 257 ? 13.290  -84.128 -47.694  1.00 45.89  ? 558  TRP   D C   1 
ATOM   12272 O  O   . TRP   D  1 257 ? 14.433  -83.977 -47.249  1.00 45.95  ? 558  TRP   D O   1 
ATOM   12273 C  CB  . TRP   D  1 257 ? 13.535  -85.969 -49.353  1.00 48.53  ? 558  TRP   D CB  1 
ATOM   12274 C  CG  . TRP   D  1 257 ? 13.040  -85.291 -50.596  1.00 47.03  ? 558  TRP   D CG  1 
ATOM   12275 C  CD1 . TRP   D  1 257 ? 12.171  -85.807 -51.514  1.00 53.68  ? 558  TRP   D CD1 1 
ATOM   12276 C  CD2 . TRP   D  1 257 ? 13.394  -83.980 -51.074  1.00 45.58  ? 558  TRP   D CD2 1 
ATOM   12277 N  NE1 . TRP   D  1 257 ? 11.961  -84.902 -52.535  1.00 52.77  ? 558  TRP   D NE1 1 
ATOM   12278 C  CE2 . TRP   D  1 257 ? 12.700  -83.774 -52.287  1.00 42.15  ? 558  TRP   D CE2 1 
ATOM   12279 C  CE3 . TRP   D  1 257 ? 14.236  -82.968 -50.602  1.00 36.20  ? 558  TRP   D CE3 1 
ATOM   12280 C  CZ2 . TRP   D  1 257 ? 12.814  -82.595 -53.024  1.00 45.06  ? 558  TRP   D CZ2 1 
ATOM   12281 C  CZ3 . TRP   D  1 257 ? 14.340  -81.789 -51.336  1.00 40.53  ? 558  TRP   D CZ3 1 
ATOM   12282 C  CH2 . TRP   D  1 257 ? 13.635  -81.616 -52.531  1.00 42.30  ? 558  TRP   D CH2 1 
ATOM   12283 N  N   . PHE   D  1 258 ? 12.453  -83.106 -47.868  1.00 38.40  ? 559  PHE   D N   1 
ATOM   12284 C  CA  . PHE   D  1 258 ? 12.926  -81.741 -47.679  1.00 38.11  ? 559  PHE   D CA  1 
ATOM   12285 C  C   . PHE   D  1 258 ? 13.400  -81.502 -46.251  1.00 41.24  ? 559  PHE   D C   1 
ATOM   12286 O  O   . PHE   D  1 258 ? 14.362  -80.755 -46.035  1.00 36.29  ? 559  PHE   D O   1 
ATOM   12287 C  CB  . PHE   D  1 258 ? 11.826  -80.755 -48.047  1.00 32.69  ? 559  PHE   D CB  1 
ATOM   12288 C  CG  . PHE   D  1 258 ? 12.331  -79.377 -48.352  1.00 42.59  ? 559  PHE   D CG  1 
ATOM   12289 C  CD1 . PHE   D  1 258 ? 12.535  -78.979 -49.669  1.00 35.87  ? 559  PHE   D CD1 1 
ATOM   12290 C  CD2 . PHE   D  1 258 ? 12.620  -78.483 -47.329  1.00 37.53  ? 559  PHE   D CD2 1 
ATOM   12291 C  CE1 . PHE   D  1 258 ? 13.005  -77.721 -49.962  1.00 35.35  ? 559  PHE   D CE1 1 
ATOM   12292 C  CE2 . PHE   D  1 258 ? 13.096  -77.216 -47.616  1.00 38.82  ? 559  PHE   D CE2 1 
ATOM   12293 C  CZ  . PHE   D  1 258 ? 13.286  -76.828 -48.942  1.00 35.05  ? 559  PHE   D CZ  1 
ATOM   12294 N  N   . LYS   D  1 259 ? 12.743  -82.121 -45.267  1.00 41.76  ? 560  LYS   D N   1 
ATOM   12295 C  CA  . LYS   D  1 259 ? 13.167  -81.932 -43.885  1.00 47.58  ? 560  LYS   D CA  1 
ATOM   12296 C  C   . LYS   D  1 259 ? 14.605  -82.389 -43.692  1.00 49.34  ? 560  LYS   D C   1 
ATOM   12297 O  O   . LYS   D  1 259 ? 15.366  -81.765 -42.944  1.00 43.41  ? 560  LYS   D O   1 
ATOM   12298 C  CB  . LYS   D  1 259 ? 12.230  -82.677 -42.932  1.00 50.34  ? 560  LYS   D CB  1 
ATOM   12299 C  CG  . LYS   D  1 259 ? 12.106  -84.168 -43.202  1.00 54.10  ? 560  LYS   D CG  1 
ATOM   12300 C  CD  . LYS   D  1 259 ? 11.306  -84.862 -42.100  1.00 58.72  ? 560  LYS   D CD  1 
ATOM   12301 C  CE  . LYS   D  1 259 ? 11.049  -86.330 -42.431  1.00 61.55  ? 560  LYS   D CE  1 
ATOM   12302 N  NZ  . LYS   D  1 259 ? 10.290  -86.493 -43.719  1.00 63.12  ? 560  LYS   D NZ  1 
ATOM   12303 N  N   . ASP   D  1 260 ? 15.004  -83.455 -44.386  1.00 46.85  ? 561  ASP   D N   1 
ATOM   12304 C  CA  . ASP   D  1 260 ? 16.349  -83.996 -44.234  1.00 56.14  ? 561  ASP   D CA  1 
ATOM   12305 C  C   . ASP   D  1 260 ? 17.432  -83.006 -44.631  1.00 50.55  ? 561  ASP   D C   1 
ATOM   12306 O  O   . ASP   D  1 260 ? 18.598  -83.214 -44.275  1.00 53.79  ? 561  ASP   D O   1 
ATOM   12307 C  CB  . ASP   D  1 260 ? 16.496  -85.275 -45.060  1.00 68.61  ? 561  ASP   D CB  1 
ATOM   12308 C  CG  . ASP   D  1 260 ? 15.383  -86.265 -44.794  1.00 76.80  ? 561  ASP   D CG  1 
ATOM   12309 O  OD1 . ASP   D  1 260 ? 14.867  -86.284 -43.654  1.00 78.72  ? 561  ASP   D OD1 1 
ATOM   12310 O  OD2 . ASP   D  1 260 ? 15.019  -87.014 -45.725  1.00 81.97  ? 561  ASP   D OD2 1 
ATOM   12311 N  N   . LEU   D  1 261 ? 17.086  -81.941 -45.361  1.00 44.33  ? 562  LEU   D N   1 
ATOM   12312 C  CA  . LEU   D  1 261 ? 18.071  -80.903 -45.653  1.00 45.59  ? 562  LEU   D CA  1 
ATOM   12313 C  C   . LEU   D  1 261 ? 18.539  -80.199 -44.387  1.00 45.18  ? 562  LEU   D C   1 
ATOM   12314 O  O   . LEU   D  1 261 ? 19.546  -79.485 -44.426  1.00 44.59  ? 562  LEU   D O   1 
ATOM   12315 C  CB  . LEU   D  1 261 ? 17.500  -79.873 -46.631  1.00 44.98  ? 562  LEU   D CB  1 
ATOM   12316 C  CG  . LEU   D  1 261 ? 17.057  -80.404 -47.995  1.00 46.31  ? 562  LEU   D CG  1 
ATOM   12317 C  CD1 . LEU   D  1 261 ? 16.241  -79.372 -48.748  1.00 38.09  ? 562  LEU   D CD1 1 
ATOM   12318 C  CD2 . LEU   D  1 261 ? 18.261  -80.816 -48.801  1.00 49.29  ? 562  LEU   D CD2 1 
ATOM   12319 N  N   . GLY   D  1 262 ? 17.828  -80.383 -43.275  1.00 45.12  ? 563  GLY   D N   1 
ATOM   12320 C  CA  . GLY   D  1 262 ? 18.184  -79.757 -42.018  1.00 40.81  ? 563  GLY   D CA  1 
ATOM   12321 C  C   . GLY   D  1 262 ? 18.113  -78.255 -42.028  1.00 41.48  ? 563  GLY   D C   1 
ATOM   12322 O  O   . GLY   D  1 262 ? 18.829  -77.607 -41.265  1.00 40.72  ? 563  GLY   D O   1 
ATOM   12323 N  N   . LEU   D  1 263 ? 17.270  -77.677 -42.875  1.00 34.60  ? 564  LEU   D N   1 
ATOM   12324 C  CA  . LEU   D  1 263 ? 17.125  -76.234 -42.908  1.00 32.56  ? 564  LEU   D CA  1 
ATOM   12325 C  C   . LEU   D  1 263 ? 16.216  -75.756 -41.788  1.00 34.24  ? 564  LEU   D C   1 
ATOM   12326 O  O   . LEU   D  1 263 ? 15.237  -76.419 -41.428  1.00 34.06  ? 564  LEU   D O   1 
ATOM   12327 C  CB  . LEU   D  1 263 ? 16.559  -75.783 -44.251  1.00 33.36  ? 564  LEU   D CB  1 
ATOM   12328 C  CG  . LEU   D  1 263 ? 17.440  -76.175 -45.420  1.00 40.05  ? 564  LEU   D CG  1 
ATOM   12329 C  CD1 . LEU   D  1 263 ? 16.693  -75.903 -46.716  1.00 42.03  ? 564  LEU   D CD1 1 
ATOM   12330 C  CD2 . LEU   D  1 263 ? 18.763  -75.415 -45.348  1.00 38.32  ? 564  LEU   D CD2 1 
ATOM   12331 N  N   . LYS   D  1 264 ? 16.539  -74.588 -41.244  1.00 30.91  ? 565  LYS   D N   1 
ATOM   12332 C  CA  . LYS   D  1 264 ? 15.610  -73.869 -40.392  1.00 35.30  ? 565  LYS   D CA  1 
ATOM   12333 C  C   . LYS   D  1 264 ? 15.837  -72.387 -40.613  1.00 35.28  ? 565  LYS   D C   1 
ATOM   12334 O  O   . LYS   D  1 264 ? 16.811  -71.980 -41.248  1.00 37.74  ? 565  LYS   D O   1 
ATOM   12335 C  CB  . LYS   D  1 264 ? 15.782  -74.239 -38.909  1.00 40.34  ? 565  LYS   D CB  1 
ATOM   12336 C  CG  . LYS   D  1 264 ? 17.124  -73.845 -38.331  1.00 41.93  ? 565  LYS   D CG  1 
ATOM   12337 C  CD  . LYS   D  1 264 ? 17.207  -74.179 -36.836  1.00 44.01  ? 565  LYS   D CD  1 
ATOM   12338 C  CE  . LYS   D  1 264 ? 18.503  -74.903 -36.484  1.00 51.00  ? 565  LYS   D CE  1 
ATOM   12339 N  NZ  . LYS   D  1 264 ? 18.671  -75.095 -35.002  1.00 52.73  ? 565  LYS   D NZ  1 
ATOM   12340 N  N   . TRP   D  1 265 ? 14.919  -71.577 -40.098  1.00 26.88  ? 566  TRP   D N   1 
ATOM   12341 C  CA  . TRP   D  1 265 ? 15.156  -70.146 -40.041  1.00 26.19  ? 566  TRP   D CA  1 
ATOM   12342 C  C   . TRP   D  1 265 ? 14.485  -69.617 -38.791  1.00 34.61  ? 566  TRP   D C   1 
ATOM   12343 O  O   . TRP   D  1 265 ? 13.653  -70.294 -38.176  1.00 36.12  ? 566  TRP   D O   1 
ATOM   12344 C  CB  . TRP   D  1 265 ? 14.640  -69.410 -41.283  1.00 21.51  ? 566  TRP   D CB  1 
ATOM   12345 C  CG  . TRP   D  1 265 ? 15.351  -68.123 -41.514  1.00 20.68  ? 566  TRP   D CG  1 
ATOM   12346 C  CD1 . TRP   D  1 265 ? 14.860  -66.868 -41.345  1.00 20.60  ? 566  TRP   D CD1 1 
ATOM   12347 C  CD2 . TRP   D  1 265 ? 16.704  -67.971 -41.947  1.00 25.02  ? 566  TRP   D CD2 1 
ATOM   12348 N  NE1 . TRP   D  1 265 ? 15.826  -65.934 -41.650  1.00 22.06  ? 566  TRP   D NE1 1 
ATOM   12349 C  CE2 . TRP   D  1 265 ? 16.965  -66.590 -42.031  1.00 24.28  ? 566  TRP   D CE2 1 
ATOM   12350 C  CE3 . TRP   D  1 265 ? 17.719  -68.874 -42.285  1.00 24.80  ? 566  TRP   D CE3 1 
ATOM   12351 C  CZ2 . TRP   D  1 265 ? 18.199  -66.087 -42.435  1.00 26.76  ? 566  TRP   D CZ2 1 
ATOM   12352 C  CZ3 . TRP   D  1 265 ? 18.941  -68.372 -42.677  1.00 22.92  ? 566  TRP   D CZ3 1 
ATOM   12353 C  CH2 . TRP   D  1 265 ? 19.171  -66.996 -42.752  1.00 21.45  ? 566  TRP   D CH2 1 
ATOM   12354 N  N   . TYR   D  1 266 ? 14.878  -68.411 -38.406  1.00 29.88  ? 567  TYR   D N   1 
ATOM   12355 C  CA  . TYR   D  1 266 ? 14.284  -67.778 -37.243  1.00 28.93  ? 567  TYR   D CA  1 
ATOM   12356 C  C   . TYR   D  1 266 ? 13.064  -66.976 -37.660  1.00 26.36  ? 567  TYR   D C   1 
ATOM   12357 O  O   . TYR   D  1 266 ? 12.946  -66.524 -38.804  1.00 23.63  ? 567  TYR   D O   1 
ATOM   12358 C  CB  . TYR   D  1 266 ? 15.292  -66.865 -36.538  1.00 22.49  ? 567  TYR   D CB  1 
ATOM   12359 C  CG  . TYR   D  1 266 ? 16.032  -65.956 -37.485  1.00 24.49  ? 567  TYR   D CG  1 
ATOM   12360 C  CD1 . TYR   D  1 266 ? 15.552  -64.678 -37.766  1.00 23.26  ? 567  TYR   D CD1 1 
ATOM   12361 C  CD2 . TYR   D  1 266 ? 17.204  -66.367 -38.097  1.00 26.33  ? 567  TYR   D CD2 1 
ATOM   12362 C  CE1 . TYR   D  1 266 ? 16.213  -63.845 -38.621  1.00 25.74  ? 567  TYR   D CE1 1 
ATOM   12363 C  CE2 . TYR   D  1 266 ? 17.877  -65.530 -38.975  1.00 28.70  ? 567  TYR   D CE2 1 
ATOM   12364 C  CZ  . TYR   D  1 266 ? 17.374  -64.270 -39.230  1.00 30.34  ? 567  TYR   D CZ  1 
ATOM   12365 O  OH  . TYR   D  1 266 ? 18.028  -63.412 -40.090  1.00 30.78  ? 567  TYR   D OH  1 
ATOM   12366 N  N   . GLY   D  1 267 ? 12.157  -66.782 -36.702  1.00 22.51  ? 568  GLY   D N   1 
ATOM   12367 C  CA  . GLY   D  1 267 ? 10.898  -66.114 -36.989  1.00 26.60  ? 568  GLY   D CA  1 
ATOM   12368 C  C   . GLY   D  1 267 ? 10.958  -64.603 -37.050  1.00 26.58  ? 568  GLY   D C   1 
ATOM   12369 O  O   . GLY   D  1 267 ? 10.126  -63.996 -37.724  1.00 27.54  ? 568  GLY   D O   1 
ATOM   12370 N  N   . LEU   D  1 268 ? 11.933  -63.979 -36.389  1.00 24.47  ? 569  LEU   D N   1 
ATOM   12371 C  CA  . LEU   D  1 268 ? 11.884  -62.545 -36.135  1.00 22.05  ? 569  LEU   D CA  1 
ATOM   12372 C  C   . LEU   D  1 268 ? 12.908  -61.790 -36.972  1.00 24.66  ? 569  LEU   D C   1 
ATOM   12373 O  O   . LEU   D  1 268 ? 14.111  -61.857 -36.668  1.00 25.87  ? 569  LEU   D O   1 
ATOM   12374 C  CB  . LEU   D  1 268 ? 12.120  -62.276 -34.640  1.00 20.78  ? 569  LEU   D CB  1 
ATOM   12375 C  CG  . LEU   D  1 268 ? 11.908  -60.819 -34.216  1.00 24.32  ? 569  LEU   D CG  1 
ATOM   12376 C  CD1 . LEU   D  1 268 ? 10.429  -60.470 -34.319  1.00 26.95  ? 569  LEU   D CD1 1 
ATOM   12377 C  CD2 . LEU   D  1 268 ? 12.446  -60.488 -32.800  1.00 21.85  ? 569  LEU   D CD2 1 
ATOM   12378 N  N   . PRO   D  1 269 ? 12.498  -61.061 -38.017  1.00 25.11  ? 570  PRO   D N   1 
ATOM   12379 C  CA  . PRO   D  1 269 ? 13.437  -60.173 -38.719  1.00 22.44  ? 570  PRO   D CA  1 
ATOM   12380 C  C   . PRO   D  1 269 ? 13.568  -58.881 -37.929  1.00 24.07  ? 570  PRO   D C   1 
ATOM   12381 O  O   . PRO   D  1 269 ? 12.599  -58.142 -37.772  1.00 21.25  ? 570  PRO   D O   1 
ATOM   12382 C  CB  . PRO   D  1 269 ? 12.760  -59.937 -40.080  1.00 16.15  ? 570  PRO   D CB  1 
ATOM   12383 C  CG  . PRO   D  1 269 ? 11.295  -60.028 -39.806  1.00 16.18  ? 570  PRO   D CG  1 
ATOM   12384 C  CD  . PRO   D  1 269 ? 11.123  -60.919 -38.533  1.00 21.43  ? 570  PRO   D CD  1 
ATOM   12385 N  N   . ALA   D  1 270 ? 14.767  -58.598 -37.440  1.00 16.22  ? 571  ALA   D N   1 
ATOM   12386 C  CA  . ALA   D  1 270 ? 14.954  -57.482 -36.516  1.00 16.08  ? 571  ALA   D CA  1 
ATOM   12387 C  C   . ALA   D  1 270 ? 16.207  -56.724 -36.933  1.00 22.07  ? 571  ALA   D C   1 
ATOM   12388 O  O   . ALA   D  1 270 ? 17.316  -57.139 -36.596  1.00 25.72  ? 571  ALA   D O   1 
ATOM   12389 C  CB  . ALA   D  1 270 ? 15.049  -57.998 -35.081  1.00 16.46  ? 571  ALA   D CB  1 
ATOM   12390 N  N   . VAL   D  1 271 ? 16.035  -55.640 -37.690  1.00 23.03  ? 572  VAL   D N   1 
ATOM   12391 C  CA  . VAL   D  1 271 ? 17.177  -54.898 -38.212  1.00 24.74  ? 572  VAL   D CA  1 
ATOM   12392 C  C   . VAL   D  1 271 ? 17.745  -54.040 -37.098  1.00 21.78  ? 572  VAL   D C   1 
ATOM   12393 O  O   . VAL   D  1 271 ? 17.008  -53.288 -36.459  1.00 23.26  ? 572  VAL   D O   1 
ATOM   12394 C  CB  . VAL   D  1 271 ? 16.778  -54.010 -39.399  1.00 20.20  ? 572  VAL   D CB  1 
ATOM   12395 C  CG1 . VAL   D  1 271 ? 17.955  -53.055 -39.732  1.00 15.72  ? 572  VAL   D CG1 1 
ATOM   12396 C  CG2 . VAL   D  1 271 ? 16.368  -54.843 -40.600  1.00 19.28  ? 572  VAL   D CG2 1 
ATOM   12397 N  N   . SER   D  1 272 ? 19.067  -54.087 -36.916  1.00 21.95  ? 573  SER   D N   1 
ATOM   12398 C  CA  . SER   D  1 272 ? 19.652  -53.409 -35.768  1.00 26.32  ? 573  SER   D CA  1 
ATOM   12399 C  C   . SER   D  1 272 ? 20.867  -52.568 -36.127  1.00 27.32  ? 573  SER   D C   1 
ATOM   12400 O  O   . SER   D  1 272 ? 21.562  -52.099 -35.219  1.00 26.69  ? 573  SER   D O   1 
ATOM   12401 C  CB  . SER   D  1 272 ? 20.024  -54.420 -34.678  1.00 17.71  ? 573  SER   D CB  1 
ATOM   12402 O  OG  . SER   D  1 272 ? 20.777  -55.512 -35.208  1.00 20.49  ? 573  SER   D OG  1 
ATOM   12403 N  N   . ASN   D  1 273 ? 21.144  -52.339 -37.405  1.00 23.32  ? 574  ASN   D N   1 
ATOM   12404 C  CA  . ASN   D  1 273 ? 22.322  -51.570 -37.770  1.00 24.19  ? 574  ASN   D CA  1 
ATOM   12405 C  C   . ASN   D  1 273 ? 21.973  -50.256 -38.435  1.00 23.29  ? 574  ASN   D C   1 
ATOM   12406 O  O   . ASN   D  1 273 ? 22.875  -49.541 -38.871  1.00 23.87  ? 574  ASN   D O   1 
ATOM   12407 C  CB  . ASN   D  1 273 ? 23.246  -52.385 -38.668  1.00 24.60  ? 574  ASN   D CB  1 
ATOM   12408 C  CG  . ASN   D  1 273 ? 22.594  -52.802 -39.971  1.00 24.01  ? 574  ASN   D CG  1 
ATOM   12409 O  OD1 . ASN   D  1 273 ? 21.382  -52.692 -40.164  1.00 27.62  ? 574  ASN   D OD1 1 
ATOM   12410 N  ND2 . ASN   D  1 273 ? 23.406  -53.323 -40.862  1.00 29.44  ? 574  ASN   D ND2 1 
ATOM   12411 N  N   . MET   D  1 274 ? 20.698  -49.904 -38.491  1.00 18.75  ? 575  MET   D N   1 
ATOM   12412 C  CA  . MET   D  1 274 ? 20.317  -48.643 -39.098  1.00 27.60  ? 575  MET   D CA  1 
ATOM   12413 C  C   . MET   D  1 274 ? 20.250  -47.540 -38.061  1.00 28.33  ? 575  MET   D C   1 
ATOM   12414 O  O   . MET   D  1 274 ? 20.331  -47.763 -36.849  1.00 25.25  ? 575  MET   D O   1 
ATOM   12415 C  CB  . MET   D  1 274 ? 18.987  -48.780 -39.823  1.00 24.50  ? 575  MET   D CB  1 
ATOM   12416 C  CG  . MET   D  1 274 ? 19.153  -49.646 -41.047  1.00 24.59  ? 575  MET   D CG  1 
ATOM   12417 S  SD  . MET   D  1 274 ? 17.662  -49.721 -42.013  1.00 25.80  ? 575  MET   D SD  1 
ATOM   12418 C  CE  . MET   D  1 274 ? 17.948  -48.387 -43.191  1.00 23.66  ? 575  MET   D CE  1 
ATOM   12419 N  N   . LEU   D  1 275 ? 20.129  -46.325 -38.566  1.00 23.24  ? 576  LEU   D N   1 
ATOM   12420 C  CA  . LEU   D  1 275 ? 20.117  -45.125 -37.751  1.00 29.11  ? 576  LEU   D CA  1 
ATOM   12421 C  C   . LEU   D  1 275 ? 18.768  -44.461 -37.954  1.00 24.53  ? 576  LEU   D C   1 
ATOM   12422 O  O   . LEU   D  1 275 ? 18.322  -44.293 -39.094  1.00 26.40  ? 576  LEU   D O   1 
ATOM   12423 C  CB  . LEU   D  1 275 ? 21.262  -44.196 -38.162  1.00 31.67  ? 576  LEU   D CB  1 
ATOM   12424 C  CG  . LEU   D  1 275 ? 21.465  -42.862 -37.448  1.00 41.24  ? 576  LEU   D CG  1 
ATOM   12425 C  CD1 . LEU   D  1 275 ? 22.931  -42.471 -37.525  1.00 40.46  ? 576  LEU   D CD1 1 
ATOM   12426 C  CD2 . LEU   D  1 275 ? 20.618  -41.781 -38.095  1.00 38.06  ? 576  LEU   D CD2 1 
ATOM   12427 N  N   . LEU   D  1 276 ? 18.109  -44.117 -36.865  1.00 18.94  ? 577  LEU   D N   1 
ATOM   12428 C  CA  . LEU   D  1 276 ? 16.820  -43.444 -36.918  1.00 23.79  ? 577  LEU   D CA  1 
ATOM   12429 C  C   . LEU   D  1 276 ? 17.066  -41.961 -36.704  1.00 23.78  ? 577  LEU   D C   1 
ATOM   12430 O  O   . LEU   D  1 276 ? 17.591  -41.558 -35.662  1.00 26.01  ? 577  LEU   D O   1 
ATOM   12431 C  CB  . LEU   D  1 276 ? 15.871  -44.009 -35.867  1.00 19.23  ? 577  LEU   D CB  1 
ATOM   12432 C  CG  . LEU   D  1 276 ? 14.649  -43.200 -35.436  1.00 23.88  ? 577  LEU   D CG  1 
ATOM   12433 C  CD1 . LEU   D  1 276 ? 13.677  -43.005 -36.581  1.00 17.69  ? 577  LEU   D CD1 1 
ATOM   12434 C  CD2 . LEU   D  1 276 ? 13.977  -43.923 -34.283  1.00 23.07  ? 577  LEU   D CD2 1 
ATOM   12435 N  N   . GLU   D  1 277 ? 16.729  -41.157 -37.700  1.00 22.02  ? 578  GLU   D N   1 
ATOM   12436 C  CA  . GLU   D  1 277 ? 16.955  -39.721 -37.643  1.00 23.69  ? 578  GLU   D CA  1 
ATOM   12437 C  C   . GLU   D  1 277 ? 15.609  -39.030 -37.457  1.00 27.36  ? 578  GLU   D C   1 
ATOM   12438 O  O   . GLU   D  1 277 ? 14.715  -39.162 -38.299  1.00 23.39  ? 578  GLU   D O   1 
ATOM   12439 C  CB  . GLU   D  1 277 ? 17.680  -39.236 -38.900  1.00 29.73  ? 578  GLU   D CB  1 
ATOM   12440 C  CG  . GLU   D  1 277 ? 18.039  -37.763 -38.864  1.00 41.36  ? 578  GLU   D CG  1 
ATOM   12441 C  CD  . GLU   D  1 277 ? 16.920  -36.901 -39.409  1.00 55.13  ? 578  GLU   D CD  1 
ATOM   12442 O  OE1 . GLU   D  1 277 ? 16.194  -37.380 -40.313  1.00 58.26  ? 578  GLU   D OE1 1 
ATOM   12443 O  OE2 . GLU   D  1 277 ? 16.757  -35.760 -38.927  1.00 58.17  ? 578  GLU   D OE2 1 
ATOM   12444 N  N   . ILE   D  1 278 ? 15.461  -38.327 -36.335  1.00 27.97  ? 579  ILE   D N   1 
ATOM   12445 C  CA  . ILE   D  1 278 ? 14.270  -37.547 -36.027  1.00 28.17  ? 579  ILE   D CA  1 
ATOM   12446 C  C   . ILE   D  1 278 ? 14.717  -36.143 -35.650  1.00 29.97  ? 579  ILE   D C   1 
ATOM   12447 O  O   . ILE   D  1 278 ? 15.456  -35.965 -34.670  1.00 29.57  ? 579  ILE   D O   1 
ATOM   12448 C  CB  . ILE   D  1 278 ? 13.453  -38.147 -34.873  1.00 35.14  ? 579  ILE   D CB  1 
ATOM   12449 C  CG1 . ILE   D  1 278 ? 13.034  -39.593 -35.152  1.00 26.61  ? 579  ILE   D CG1 1 
ATOM   12450 C  CG2 . ILE   D  1 278 ? 12.261  -37.249 -34.568  1.00 32.30  ? 579  ILE   D CG2 1 
ATOM   12451 C  CD1 . ILE   D  1 278 ? 12.393  -40.275 -33.920  1.00 26.06  ? 579  ILE   D CD1 1 
ATOM   12452 N  N   . GLY   D  1 279 ? 14.274  -35.157 -36.425  1.00 27.55  ? 580  GLY   D N   1 
ATOM   12453 C  CA  . GLY   D  1 279 ? 14.515  -33.749 -36.142  1.00 28.60  ? 580  GLY   D CA  1 
ATOM   12454 C  C   . GLY   D  1 279 ? 15.962  -33.372 -35.923  1.00 31.58  ? 580  GLY   D C   1 
ATOM   12455 O  O   . GLY   D  1 279 ? 16.255  -32.513 -35.082  1.00 32.65  ? 580  GLY   D O   1 
ATOM   12456 N  N   . GLY   D  1 280 ? 16.876  -33.992 -36.665  1.00 28.12  ? 581  GLY   D N   1 
ATOM   12457 C  CA  . GLY   D  1 280 ? 18.292  -33.771 -36.472  1.00 32.34  ? 581  GLY   D CA  1 
ATOM   12458 C  C   . GLY   D  1 280 ? 18.924  -34.643 -35.415  1.00 37.63  ? 581  GLY   D C   1 
ATOM   12459 O  O   . GLY   D  1 280 ? 20.160  -34.684 -35.325  1.00 39.49  ? 581  GLY   D O   1 
ATOM   12460 N  N   . LEU   D  1 281 ? 18.127  -35.337 -34.611  1.00 31.95  ? 582  LEU   D N   1 
ATOM   12461 C  CA  . LEU   D  1 281 ? 18.670  -36.273 -33.643  1.00 31.86  ? 582  LEU   D CA  1 
ATOM   12462 C  C   . LEU   D  1 281 ? 18.922  -37.609 -34.314  1.00 30.91  ? 582  LEU   D C   1 
ATOM   12463 O  O   . LEU   D  1 281 ? 18.131  -38.056 -35.147  1.00 32.44  ? 582  LEU   D O   1 
ATOM   12464 C  CB  . LEU   D  1 281 ? 17.712  -36.455 -32.466  1.00 30.28  ? 582  LEU   D CB  1 
ATOM   12465 C  CG  . LEU   D  1 281 ? 17.255  -35.152 -31.823  1.00 28.72  ? 582  LEU   D CG  1 
ATOM   12466 C  CD1 . LEU   D  1 281 ? 16.252  -35.438 -30.712  1.00 31.59  ? 582  LEU   D CD1 1 
ATOM   12467 C  CD2 . LEU   D  1 281 ? 18.474  -34.413 -31.284  1.00 29.56  ? 582  LEU   D CD2 1 
ATOM   12468 N  N   . GLU   D  1 282 ? 20.019  -38.252 -33.932  1.00 29.92  ? 583  GLU   D N   1 
ATOM   12469 C  CA  . GLU   D  1 282 ? 20.465  -39.497 -34.545  1.00 25.04  ? 583  GLU   D CA  1 
ATOM   12470 C  C   . GLU   D  1 282 ? 20.450  -40.613 -33.507  1.00 32.97  ? 583  GLU   D C   1 
ATOM   12471 O  O   . GLU   D  1 282 ? 21.271  -40.625 -32.582  1.00 29.76  ? 583  GLU   D O   1 
ATOM   12472 C  CB  . GLU   D  1 282 ? 21.858  -39.331 -35.137  1.00 37.06  ? 583  GLU   D CB  1 
ATOM   12473 C  CG  . GLU   D  1 282 ? 21.948  -38.234 -36.157  1.00 41.87  ? 583  GLU   D CG  1 
ATOM   12474 C  CD  . GLU   D  1 282 ? 23.252  -38.280 -36.898  1.00 54.53  ? 583  GLU   D CD  1 
ATOM   12475 O  OE1 . GLU   D  1 282 ? 23.220  -38.216 -38.147  1.00 64.25  ? 583  GLU   D OE1 1 
ATOM   12476 O  OE2 . GLU   D  1 282 ? 24.303  -38.397 -36.228  1.00 53.11  ? 583  GLU   D OE2 1 
ATOM   12477 N  N   . PHE   D  1 283 ? 19.528  -41.547 -33.668  1.00 28.68  ? 584  PHE   D N   1 
ATOM   12478 C  CA  . PHE   D  1 283 ? 19.431  -42.712 -32.799  1.00 24.58  ? 584  PHE   D CA  1 
ATOM   12479 C  C   . PHE   D  1 283 ? 20.168  -43.852 -33.490  1.00 30.28  ? 584  PHE   D C   1 
ATOM   12480 O  O   . PHE   D  1 283 ? 19.619  -44.521 -34.375  1.00 29.07  ? 584  PHE   D O   1 
ATOM   12481 C  CB  . PHE   D  1 283 ? 17.969  -43.033 -32.523  1.00 25.14  ? 584  PHE   D CB  1 
ATOM   12482 C  CG  . PHE   D  1 283 ? 17.269  -41.940 -31.785  1.00 25.82  ? 584  PHE   D CG  1 
ATOM   12483 C  CD1 . PHE   D  1 283 ? 16.517  -40.994 -32.467  1.00 29.20  ? 584  PHE   D CD1 1 
ATOM   12484 C  CD2 . PHE   D  1 283 ? 17.393  -41.831 -30.408  1.00 25.77  ? 584  PHE   D CD2 1 
ATOM   12485 C  CE1 . PHE   D  1 283 ? 15.876  -39.976 -31.772  1.00 25.68  ? 584  PHE   D CE1 1 
ATOM   12486 C  CE2 . PHE   D  1 283 ? 16.751  -40.832 -29.713  1.00 27.69  ? 584  PHE   D CE2 1 
ATOM   12487 C  CZ  . PHE   D  1 283 ? 15.995  -39.898 -30.397  1.00 30.02  ? 584  PHE   D CZ  1 
ATOM   12488 N  N   . SER   D  1 284 ? 21.435  -44.041 -33.105  1.00 24.20  ? 585  SER   D N   1 
ATOM   12489 C  CA  . SER   D  1 284 ? 22.317  -44.988 -33.775  1.00 30.03  ? 585  SER   D CA  1 
ATOM   12490 C  C   . SER   D  1 284 ? 22.039  -46.430 -33.396  1.00 25.89  ? 585  SER   D C   1 
ATOM   12491 O  O   . SER   D  1 284 ? 22.576  -47.341 -34.038  1.00 26.71  ? 585  SER   D O   1 
ATOM   12492 C  CB  . SER   D  1 284 ? 23.778  -44.662 -33.463  1.00 32.38  ? 585  SER   D CB  1 
ATOM   12493 O  OG  . SER   D  1 284 ? 23.954  -44.402 -32.079  1.00 34.21  ? 585  SER   D OG  1 
ATOM   12494 N  N   . ALA   D  1 285 ? 21.258  -46.658 -32.352  1.00 31.27  ? 586  ALA   D N   1 
ATOM   12495 C  CA  . ALA   D  1 285 ? 20.826  -47.997 -31.976  1.00 26.88  ? 586  ALA   D CA  1 
ATOM   12496 C  C   . ALA   D  1 285 ? 19.314  -47.944 -31.862  1.00 21.80  ? 586  ALA   D C   1 
ATOM   12497 O  O   . ALA   D  1 285 ? 18.779  -47.363 -30.909  1.00 24.35  ? 586  ALA   D O   1 
ATOM   12498 C  CB  . ALA   D  1 285 ? 21.462  -48.450 -30.665  1.00 30.51  ? 586  ALA   D CB  1 
ATOM   12499 N  N   . CYS   D  1 286 ? 18.640  -48.539 -32.822  1.00 21.71  ? 587  CYS   D N   1 
ATOM   12500 C  CA  . CYS   D  1 286 ? 17.191  -48.491 -32.849  1.00 22.15  ? 587  CYS   D CA  1 
ATOM   12501 C  C   . CYS   D  1 286 ? 16.650  -49.782 -33.447  1.00 26.14  ? 587  CYS   D C   1 
ATOM   12502 O  O   . CYS   D  1 286 ? 15.953  -49.746 -34.474  1.00 25.68  ? 587  CYS   D O   1 
ATOM   12503 C  CB  . CYS   D  1 286 ? 16.740  -47.288 -33.662  1.00 23.29  ? 587  CYS   D CB  1 
ATOM   12504 S  SG  . CYS   D  1 286 ? 17.409  -47.325 -35.371  1.00 26.01  ? 587  CYS   D SG  1 
ATOM   12505 N  N   . PRO   D  1 287 ? 16.946  -50.938 -32.848  1.00 25.98  ? 588  PRO   D N   1 
ATOM   12506 C  CA  . PRO   D  1 287 ? 16.539  -52.197 -33.480  1.00 22.91  ? 588  PRO   D CA  1 
ATOM   12507 C  C   . PRO   D  1 287 ? 15.036  -52.195 -33.686  1.00 23.91  ? 588  PRO   D C   1 
ATOM   12508 O  O   . PRO   D  1 287 ? 14.276  -51.770 -32.813  1.00 27.82  ? 588  PRO   D O   1 
ATOM   12509 C  CB  . PRO   D  1 287 ? 16.985  -53.267 -32.478  1.00 24.37  ? 588  PRO   D CB  1 
ATOM   12510 C  CG  . PRO   D  1 287 ? 17.153  -52.526 -31.157  1.00 26.99  ? 588  PRO   D CG  1 
ATOM   12511 C  CD  . PRO   D  1 287 ? 17.586  -51.151 -31.534  1.00 24.49  ? 588  PRO   D CD  1 
ATOM   12512 N  N   . PHE   D  1 288 ? 14.616  -52.586 -34.889  1.00 23.87  ? 589  PHE   D N   1 
ATOM   12513 C  CA  . PHE   D  1 288 ? 13.206  -52.684 -35.212  1.00 15.90  ? 589  PHE   D CA  1 
ATOM   12514 C  C   . PHE   D  1 288 ? 12.941  -54.019 -35.889  1.00 20.56  ? 589  PHE   D C   1 
ATOM   12515 O  O   . PHE   D  1 288 ? 13.814  -54.602 -36.539  1.00 23.42  ? 589  PHE   D O   1 
ATOM   12516 C  CB  . PHE   D  1 288 ? 12.723  -51.528 -36.104  1.00 20.82  ? 589  PHE   D CB  1 
ATOM   12517 C  CG  . PHE   D  1 288 ? 13.462  -51.398 -37.419  1.00 20.99  ? 589  PHE   D CG  1 
ATOM   12518 C  CD1 . PHE   D  1 288 ? 13.061  -52.117 -38.541  1.00 24.26  ? 589  PHE   D CD1 1 
ATOM   12519 C  CD2 . PHE   D  1 288 ? 14.541  -50.534 -37.536  1.00 18.24  ? 589  PHE   D CD2 1 
ATOM   12520 C  CE1 . PHE   D  1 288 ? 13.724  -51.989 -39.738  1.00 23.54  ? 589  PHE   D CE1 1 
ATOM   12521 C  CE2 . PHE   D  1 288 ? 15.220  -50.393 -38.747  1.00 20.25  ? 589  PHE   D CE2 1 
ATOM   12522 C  CZ  . PHE   D  1 288 ? 14.806  -51.118 -39.854  1.00 16.74  ? 589  PHE   D CZ  1 
ATOM   12523 N  N   . SER   D  1 289 ? 11.727  -54.506 -35.717  1.00 21.40  ? 590  SER   D N   1 
ATOM   12524 C  CA  . SER   D  1 289 ? 11.419  -55.848 -36.150  1.00 18.80  ? 590  SER   D CA  1 
ATOM   12525 C  C   . SER   D  1 289 ? 9.981   -55.853 -36.595  1.00 18.32  ? 590  SER   D C   1 
ATOM   12526 O  O   . SER   D  1 289 ? 9.173   -55.078 -36.092  1.00 19.89  ? 590  SER   D O   1 
ATOM   12527 C  CB  . SER   D  1 289 ? 11.645  -56.868 -35.026  1.00 22.88  ? 590  SER   D CB  1 
ATOM   12528 O  OG  . SER   D  1 289 ? 10.741  -56.644 -33.970  1.00 25.49  ? 590  SER   D OG  1 
ATOM   12529 N  N   . GLY   D  1 290 ? 9.682   -56.704 -37.575  1.00 20.33  ? 591  GLY   D N   1 
ATOM   12530 C  CA  . GLY   D  1 290 ? 8.306   -56.949 -37.951  1.00 21.75  ? 591  GLY   D CA  1 
ATOM   12531 C  C   . GLY   D  1 290 ? 8.100   -58.437 -38.112  1.00 26.45  ? 591  GLY   D C   1 
ATOM   12532 O  O   . GLY   D  1 290 ? 8.344   -59.211 -37.183  1.00 25.35  ? 591  GLY   D O   1 
ATOM   12533 N  N   . TRP   D  1 291 ? 7.688   -58.863 -39.299  1.00 24.51  ? 592  TRP   D N   1 
ATOM   12534 C  CA  . TRP   D  1 291 ? 7.609   -60.279 -39.598  1.00 23.96  ? 592  TRP   D CA  1 
ATOM   12535 C  C   . TRP   D  1 291 ? 8.027   -60.476 -41.046  1.00 22.90  ? 592  TRP   D C   1 
ATOM   12536 O  O   . TRP   D  1 291 ? 8.040   -59.535 -41.833  1.00 21.28  ? 592  TRP   D O   1 
ATOM   12537 C  CB  . TRP   D  1 291 ? 6.208   -60.829 -39.336  1.00 18.76  ? 592  TRP   D CB  1 
ATOM   12538 C  CG  . TRP   D  1 291 ? 5.139   -60.058 -40.004  1.00 23.59  ? 592  TRP   D CG  1 
ATOM   12539 C  CD1 . TRP   D  1 291 ? 4.804   -60.101 -41.334  1.00 29.42  ? 592  TRP   D CD1 1 
ATOM   12540 C  CD2 . TRP   D  1 291 ? 4.245   -59.128 -39.397  1.00 26.50  ? 592  TRP   D CD2 1 
ATOM   12541 N  NE1 . TRP   D  1 291 ? 3.753   -59.252 -41.583  1.00 23.90  ? 592  TRP   D NE1 1 
ATOM   12542 C  CE2 . TRP   D  1 291 ? 3.391   -58.643 -40.413  1.00 26.24  ? 592  TRP   D CE2 1 
ATOM   12543 C  CE3 . TRP   D  1 291 ? 4.076   -58.659 -38.089  1.00 25.37  ? 592  TRP   D CE3 1 
ATOM   12544 C  CZ2 . TRP   D  1 291 ? 2.391   -57.712 -40.165  1.00 28.83  ? 592  TRP   D CZ2 1 
ATOM   12545 C  CZ3 . TRP   D  1 291 ? 3.084   -57.731 -37.844  1.00 30.22  ? 592  TRP   D CZ3 1 
ATOM   12546 C  CH2 . TRP   D  1 291 ? 2.250   -57.269 -38.877  1.00 36.46  ? 592  TRP   D CH2 1 
ATOM   12547 N  N   . TYR   D  1 292 ? 8.402   -61.699 -41.385  1.00 23.20  ? 593  TYR   D N   1 
ATOM   12548 C  CA  . TYR   D  1 292 ? 9.022   -61.943 -42.681  1.00 24.88  ? 593  TYR   D CA  1 
ATOM   12549 C  C   . TYR   D  1 292 ? 8.016   -61.973 -43.813  1.00 26.89  ? 593  TYR   D C   1 
ATOM   12550 O  O   . TYR   D  1 292 ? 6.874   -62.417 -43.655  1.00 23.44  ? 593  TYR   D O   1 
ATOM   12551 C  CB  . TYR   D  1 292 ? 9.752   -63.278 -42.709  1.00 22.52  ? 593  TYR   D CB  1 
ATOM   12552 C  CG  . TYR   D  1 292 ? 11.204  -63.177 -42.370  1.00 18.07  ? 593  TYR   D CG  1 
ATOM   12553 C  CD1 . TYR   D  1 292 ? 11.712  -63.800 -41.231  1.00 23.58  ? 593  TYR   D CD1 1 
ATOM   12554 C  CD2 . TYR   D  1 292 ? 12.070  -62.467 -43.179  1.00 20.74  ? 593  TYR   D CD2 1 
ATOM   12555 C  CE1 . TYR   D  1 292 ? 13.036  -63.732 -40.923  1.00 18.87  ? 593  TYR   D CE1 1 
ATOM   12556 C  CE2 . TYR   D  1 292 ? 13.413  -62.387 -42.872  1.00 23.62  ? 593  TYR   D CE2 1 
ATOM   12557 C  CZ  . TYR   D  1 292 ? 13.887  -63.031 -41.743  1.00 19.48  ? 593  TYR   D CZ  1 
ATOM   12558 O  OH  . TYR   D  1 292 ? 15.221  -62.949 -41.432  1.00 24.01  ? 593  TYR   D OH  1 
ATOM   12559 N  N   . MET   D  1 293 ? 8.475   -61.514 -44.970  1.00 27.37  ? 594  MET   D N   1 
ATOM   12560 C  CA  . MET   D  1 293 ? 7.945   -61.957 -46.243  1.00 18.90  ? 594  MET   D CA  1 
ATOM   12561 C  C   . MET   D  1 293 ? 8.762   -63.176 -46.652  1.00 20.45  ? 594  MET   D C   1 
ATOM   12562 O  O   . MET   D  1 293 ? 9.991   -63.163 -46.543  1.00 23.03  ? 594  MET   D O   1 
ATOM   12563 C  CB  . MET   D  1 293 ? 8.043   -60.845 -47.288  1.00 18.61  ? 594  MET   D CB  1 
ATOM   12564 C  CG  . MET   D  1 293 ? 7.324   -61.171 -48.607  1.00 18.76  ? 594  MET   D CG  1 
ATOM   12565 S  SD  . MET   D  1 293 ? 7.257   -59.711 -49.661  1.00 24.41  ? 594  MET   D SD  1 
ATOM   12566 C  CE  . MET   D  1 293 ? 8.974   -59.554 -50.155  1.00 23.01  ? 594  MET   D CE  1 
ATOM   12567 N  N   . GLY   D  1 294 ? 8.077   -64.246 -47.065  1.00 23.99  ? 595  GLY   D N   1 
ATOM   12568 C  CA  . GLY   D  1 294 ? 8.749   -65.527 -47.248  1.00 20.30  ? 595  GLY   D CA  1 
ATOM   12569 C  C   . GLY   D  1 294 ? 9.944   -65.486 -48.183  1.00 24.61  ? 595  GLY   D C   1 
ATOM   12570 O  O   . GLY   D  1 294 ? 10.921  -66.210 -47.974  1.00 25.47  ? 595  GLY   D O   1 
ATOM   12571 N  N   . THR   D  1 295 ? 9.885   -64.648 -49.227  1.00 21.36  ? 596  THR   D N   1 
ATOM   12572 C  CA  . THR   D  1 295 ? 10.970  -64.594 -50.202  1.00 24.96  ? 596  THR   D CA  1 
ATOM   12573 C  C   . THR   D  1 295 ? 12.270  -64.124 -49.579  1.00 21.99  ? 596  THR   D C   1 
ATOM   12574 O  O   . THR   D  1 295 ? 13.348  -64.477 -50.064  1.00 21.67  ? 596  THR   D O   1 
ATOM   12575 C  CB  . THR   D  1 295 ? 10.604  -63.663 -51.369  1.00 25.22  ? 596  THR   D CB  1 
ATOM   12576 O  OG1 . THR   D  1 295 ? 10.193  -62.385 -50.868  1.00 20.50  ? 596  THR   D OG1 1 
ATOM   12577 C  CG2 . THR   D  1 295 ? 9.483   -64.273 -52.241  1.00 25.05  ? 596  THR   D CG2 1 
ATOM   12578 N  N   . GLU   D  1 296 ? 12.192  -63.312 -48.520  1.00 27.03  ? 597  GLU   D N   1 
ATOM   12579 C  CA  . GLU   D  1 296 ? 13.403  -62.893 -47.822  1.00 30.74  ? 597  GLU   D CA  1 
ATOM   12580 C  C   . GLU   D  1 296 ? 14.227  -64.093 -47.384  1.00 30.03  ? 597  GLU   D C   1 
ATOM   12581 O  O   . GLU   D  1 296 ? 15.459  -64.101 -47.523  1.00 30.94  ? 597  GLU   D O   1 
ATOM   12582 C  CB  . GLU   D  1 296 ? 13.033  -62.048 -46.605  1.00 34.84  ? 597  GLU   D CB  1 
ATOM   12583 C  CG  . GLU   D  1 296 ? 12.358  -60.727 -46.909  1.00 28.35  ? 597  GLU   D CG  1 
ATOM   12584 C  CD  . GLU   D  1 296 ? 12.085  -59.956 -45.628  1.00 22.55  ? 597  GLU   D CD  1 
ATOM   12585 O  OE1 . GLU   D  1 296 ? 13.032  -59.332 -45.103  1.00 17.92  ? 597  GLU   D OE1 1 
ATOM   12586 O  OE2 . GLU   D  1 296 ? 10.928  -59.994 -45.148  1.00 18.20  ? 597  GLU   D OE2 1 
ATOM   12587 N  N   . ILE   D  1 297 ? 13.556  -65.116 -46.851  1.00 25.32  ? 598  ILE   D N   1 
ATOM   12588 C  CA  . ILE   D  1 297 ? 14.216  -66.351 -46.458  1.00 25.22  ? 598  ILE   D CA  1 
ATOM   12589 C  C   . ILE   D  1 297 ? 14.406  -67.272 -47.654  1.00 27.69  ? 598  ILE   D C   1 
ATOM   12590 O  O   . ILE   D  1 297 ? 15.517  -67.745 -47.924  1.00 25.07  ? 598  ILE   D O   1 
ATOM   12591 C  CB  . ILE   D  1 297 ? 13.401  -67.051 -45.360  1.00 23.36  ? 598  ILE   D CB  1 
ATOM   12592 C  CG1 . ILE   D  1 297 ? 13.145  -66.088 -44.184  1.00 25.88  ? 598  ILE   D CG1 1 
ATOM   12593 C  CG2 . ILE   D  1 297 ? 14.128  -68.318 -44.925  1.00 21.34  ? 598  ILE   D CG2 1 
ATOM   12594 C  CD1 . ILE   D  1 297 ? 12.045  -66.558 -43.227  1.00 23.43  ? 598  ILE   D CD1 1 
ATOM   12595 N  N   . GLY   D  1 298 ? 13.308  -67.567 -48.363  1.00 24.23  ? 599  GLY   D N   1 
ATOM   12596 C  CA  . GLY   D  1 298 ? 13.336  -68.595 -49.387  1.00 27.61  ? 599  GLY   D CA  1 
ATOM   12597 C  C   . GLY   D  1 298 ? 14.118  -68.205 -50.626  1.00 25.38  ? 599  GLY   D C   1 
ATOM   12598 O  O   . GLY   D  1 298 ? 14.729  -69.061 -51.270  1.00 29.21  ? 599  GLY   D O   1 
ATOM   12599 N  N   . VAL   D  1 299 ? 14.124  -66.921 -50.974  1.00 27.30  ? 600  VAL   D N   1 
ATOM   12600 C  CA  . VAL   D  1 299 ? 14.864  -66.485 -52.150  1.00 24.95  ? 600  VAL   D CA  1 
ATOM   12601 C  C   . VAL   D  1 299 ? 16.252  -65.987 -51.773  1.00 29.27  ? 600  VAL   D C   1 
ATOM   12602 O  O   . VAL   D  1 299 ? 17.258  -66.478 -52.295  1.00 32.27  ? 600  VAL   D O   1 
ATOM   12603 C  CB  . VAL   D  1 299 ? 14.105  -65.398 -52.929  1.00 26.19  ? 600  VAL   D CB  1 
ATOM   12604 C  CG1 . VAL   D  1 299 ? 14.871  -65.067 -54.179  1.00 24.94  ? 600  VAL   D CG1 1 
ATOM   12605 C  CG2 . VAL   D  1 299 ? 12.699  -65.871 -53.296  1.00 30.61  ? 600  VAL   D CG2 1 
ATOM   12606 N  N   . ARG   D  1 300 ? 16.328  -64.990 -50.888  1.00 27.68  ? 601  ARG   D N   1 
ATOM   12607 C  CA  . ARG   D  1 300 ? 17.614  -64.324 -50.675  1.00 23.91  ? 601  ARG   D CA  1 
ATOM   12608 C  C   . ARG   D  1 300 ? 18.485  -65.100 -49.694  1.00 27.75  ? 601  ARG   D C   1 
ATOM   12609 O  O   . ARG   D  1 300 ? 19.611  -65.487 -50.021  1.00 30.63  ? 601  ARG   D O   1 
ATOM   12610 C  CB  . ARG   D  1 300 ? 17.398  -62.884 -50.191  1.00 18.34  ? 601  ARG   D CB  1 
ATOM   12611 C  CG  . ARG   D  1 300 ? 16.515  -62.046 -51.109  1.00 19.89  ? 601  ARG   D CG  1 
ATOM   12612 C  CD  . ARG   D  1 300 ? 17.125  -61.911 -52.516  1.00 22.73  ? 601  ARG   D CD  1 
ATOM   12613 N  NE  . ARG   D  1 300 ? 18.524  -61.505 -52.426  1.00 24.51  ? 601  ARG   D NE  1 
ATOM   12614 C  CZ  . ARG   D  1 300 ? 18.915  -60.266 -52.162  1.00 22.09  ? 601  ARG   D CZ  1 
ATOM   12615 N  NH1 . ARG   D  1 300 ? 18.018  -59.301 -52.011  1.00 19.84  ? 601  ARG   D NH1 1 
ATOM   12616 N  NH2 . ARG   D  1 300 ? 20.202  -59.986 -52.084  1.00 24.11  ? 601  ARG   D NH2 1 
ATOM   12617 N  N   . ASP   D  1 301 ? 17.979  -65.326 -48.477  1.00 28.24  ? 602  ASP   D N   1 
ATOM   12618 C  CA  . ASP   D  1 301 ? 18.777  -66.014 -47.465  1.00 31.90  ? 602  ASP   D CA  1 
ATOM   12619 C  C   . ASP   D  1 301 ? 19.204  -67.389 -47.954  1.00 27.98  ? 602  ASP   D C   1 
ATOM   12620 O  O   . ASP   D  1 301 ? 20.385  -67.752 -47.889  1.00 27.70  ? 602  ASP   D O   1 
ATOM   12621 C  CB  . ASP   D  1 301 ? 17.990  -66.117 -46.150  1.00 28.07  ? 602  ASP   D CB  1 
ATOM   12622 C  CG  . ASP   D  1 301 ? 17.756  -64.750 -45.491  1.00 32.36  ? 602  ASP   D CG  1 
ATOM   12623 O  OD1 . ASP   D  1 301 ? 18.651  -63.882 -45.577  1.00 29.40  ? 602  ASP   D OD1 1 
ATOM   12624 O  OD2 . ASP   D  1 301 ? 16.677  -64.540 -44.891  1.00 30.92  ? 602  ASP   D OD2 1 
ATOM   12625 N  N   . TYR   D  1 302 ? 18.261  -68.153 -48.495  1.00 22.06  ? 603  TYR   D N   1 
ATOM   12626 C  CA  . TYR   D  1 302 ? 18.553  -69.526 -48.893  1.00 23.29  ? 603  TYR   D CA  1 
ATOM   12627 C  C   . TYR   D  1 302 ? 19.231  -69.620 -50.257  1.00 31.23  ? 603  TYR   D C   1 
ATOM   12628 O  O   . TYR   D  1 302 ? 20.109  -70.464 -50.448  1.00 29.63  ? 603  TYR   D O   1 
ATOM   12629 C  CB  . TYR   D  1 302 ? 17.265  -70.344 -48.874  1.00 29.90  ? 603  TYR   D CB  1 
ATOM   12630 C  CG  . TYR   D  1 302 ? 16.886  -70.808 -47.478  1.00 36.17  ? 603  TYR   D CG  1 
ATOM   12631 C  CD1 . TYR   D  1 302 ? 15.653  -71.385 -47.227  1.00 32.48  ? 603  TYR   D CD1 1 
ATOM   12632 C  CD2 . TYR   D  1 302 ? 17.776  -70.673 -46.418  1.00 36.33  ? 603  TYR   D CD2 1 
ATOM   12633 C  CE1 . TYR   D  1 302 ? 15.315  -71.829 -45.961  1.00 32.15  ? 603  TYR   D CE1 1 
ATOM   12634 C  CE2 . TYR   D  1 302 ? 17.450  -71.112 -45.149  1.00 35.64  ? 603  TYR   D CE2 1 
ATOM   12635 C  CZ  . TYR   D  1 302 ? 16.213  -71.686 -44.925  1.00 38.43  ? 603  TYR   D CZ  1 
ATOM   12636 O  OH  . TYR   D  1 302 ? 15.866  -72.122 -43.662  1.00 35.41  ? 603  TYR   D OH  1 
ATOM   12637 N  N   . CYS   D  1 303 ? 18.861  -68.777 -51.223  1.00 29.54  ? 604  CYS   D N   1 
ATOM   12638 C  CA  . CYS   D  1 303 ? 19.303  -69.040 -52.585  1.00 30.86  ? 604  CYS   D CA  1 
ATOM   12639 C  C   . CYS   D  1 303 ? 20.299  -68.043 -53.154  1.00 33.67  ? 604  CYS   D C   1 
ATOM   12640 O  O   . CYS   D  1 303 ? 20.858  -68.323 -54.221  1.00 32.17  ? 604  CYS   D O   1 
ATOM   12641 C  CB  . CYS   D  1 303 ? 18.097  -69.141 -53.522  1.00 30.31  ? 604  CYS   D CB  1 
ATOM   12642 S  SG  . CYS   D  1 303 ? 17.058  -70.523 -53.054  1.00 32.97  ? 604  CYS   D SG  1 
ATOM   12643 N  N   . ASP   D  1 304 ? 20.555  -66.907 -52.498  1.00 25.43  ? 605  ASP   D N   1 
ATOM   12644 C  CA  . ASP   D  1 304 ? 21.682  -66.087 -52.938  1.00 27.73  ? 605  ASP   D CA  1 
ATOM   12645 C  C   . ASP   D  1 304 ? 22.934  -66.954 -52.977  1.00 36.08  ? 605  ASP   D C   1 
ATOM   12646 O  O   . ASP   D  1 304 ? 23.154  -67.797 -52.097  1.00 34.11  ? 605  ASP   D O   1 
ATOM   12647 C  CB  . ASP   D  1 304 ? 21.923  -64.885 -52.012  1.00 24.47  ? 605  ASP   D CB  1 
ATOM   12648 C  CG  . ASP   D  1 304 ? 21.060  -63.670 -52.355  1.00 32.50  ? 605  ASP   D CG  1 
ATOM   12649 O  OD1 . ASP   D  1 304 ? 20.138  -63.782 -53.191  1.00 30.64  ? 605  ASP   D OD1 1 
ATOM   12650 O  OD2 . ASP   D  1 304 ? 21.311  -62.590 -51.764  1.00 33.83  ? 605  ASP   D OD2 1 
ATOM   12651 N  N   . ASN   D  1 305 ? 23.741  -66.763 -54.022  1.00 33.22  ? 606  ASN   D N   1 
ATOM   12652 C  CA  . ASN   D  1 305 ? 24.980  -67.522 -54.151  1.00 35.50  ? 606  ASN   D CA  1 
ATOM   12653 C  C   . ASN   D  1 305 ? 25.952  -67.220 -53.016  1.00 30.32  ? 606  ASN   D C   1 
ATOM   12654 O  O   . ASN   D  1 305 ? 26.758  -68.076 -52.645  1.00 34.21  ? 606  ASN   D O   1 
ATOM   12655 C  CB  . ASN   D  1 305 ? 25.648  -67.226 -55.494  1.00 30.44  ? 606  ASN   D CB  1 
ATOM   12656 C  CG  . ASN   D  1 305 ? 24.853  -67.761 -56.676  1.00 42.22  ? 606  ASN   D CG  1 
ATOM   12657 O  OD1 . ASN   D  1 305 ? 24.390  -66.996 -57.524  1.00 50.26  ? 606  ASN   D OD1 1 
ATOM   12658 N  ND2 . ASN   D  1 305 ? 24.695  -69.079 -56.739  1.00 47.99  ? 606  ASN   D ND2 1 
ATOM   12659 N  N   . SER   D  1 306 ? 25.924  -66.010 -52.481  1.00 38.98  ? 607  SER   D N   1 
ATOM   12660 C  CA  . SER   D  1 306 ? 26.814  -65.656 -51.388  1.00 40.63  ? 607  SER   D CA  1 
ATOM   12661 C  C   . SER   D  1 306 ? 26.143  -65.812 -50.034  1.00 37.35  ? 607  SER   D C   1 
ATOM   12662 O  O   . SER   D  1 306 ? 26.640  -65.275 -49.041  1.00 36.06  ? 607  SER   D O   1 
ATOM   12663 C  CB  . SER   D  1 306 ? 27.318  -64.228 -51.572  1.00 41.07  ? 607  SER   D CB  1 
ATOM   12664 O  OG  . SER   D  1 306 ? 26.216  -63.349 -51.543  1.00 44.35  ? 607  SER   D OG  1 
ATOM   12665 N  N   . ARG   D  1 307 ? 25.003  -66.499 -49.982  1.00 30.80  ? 608  ARG   D N   1 
ATOM   12666 C  CA  . ARG   D  1 307 ? 24.374  -66.817 -48.710  1.00 30.89  ? 608  ARG   D CA  1 
ATOM   12667 C  C   . ARG   D  1 307 ? 24.345  -68.333 -48.543  1.00 30.76  ? 608  ARG   D C   1 
ATOM   12668 O  O   . ARG   D  1 307 ? 25.367  -68.993 -48.765  1.00 27.83  ? 608  ARG   D O   1 
ATOM   12669 C  CB  . ARG   D  1 307 ? 22.983  -66.184 -48.626  1.00 25.12  ? 608  ARG   D CB  1 
ATOM   12670 C  CG  . ARG   D  1 307 ? 22.994  -64.652 -48.738  1.00 24.55  ? 608  ARG   D CG  1 
ATOM   12671 C  CD  . ARG   D  1 307 ? 23.618  -63.944 -47.526  1.00 30.87  ? 608  ARG   D CD  1 
ATOM   12672 N  NE  . ARG   D  1 307 ? 22.976  -64.329 -46.264  1.00 23.64  ? 608  ARG   D NE  1 
ATOM   12673 C  CZ  . ARG   D  1 307 ? 21.765  -63.923 -45.887  1.00 30.12  ? 608  ARG   D CZ  1 
ATOM   12674 N  NH1 . ARG   D  1 307 ? 21.049  -63.107 -46.661  1.00 25.31  ? 608  ARG   D NH1 1 
ATOM   12675 N  NH2 . ARG   D  1 307 ? 21.257  -64.341 -44.734  1.00 25.68  ? 608  ARG   D NH2 1 
ATOM   12676 N  N   . TYR   D  1 308 ? 23.208  -68.912 -48.147  1.00 28.22  ? 609  TYR   D N   1 
ATOM   12677 C  CA  . TYR   D  1 308 ? 23.205  -70.354 -47.905  1.00 28.79  ? 609  TYR   D CA  1 
ATOM   12678 C  C   . TYR   D  1 308 ? 23.265  -71.159 -49.194  1.00 31.98  ? 609  TYR   D C   1 
ATOM   12679 O  O   . TYR   D  1 308 ? 23.673  -72.323 -49.157  1.00 33.52  ? 609  TYR   D O   1 
ATOM   12680 C  CB  . TYR   D  1 308 ? 21.988  -70.762 -47.074  1.00 25.19  ? 609  TYR   D CB  1 
ATOM   12681 C  CG  . TYR   D  1 308 ? 22.222  -70.557 -45.591  1.00 35.35  ? 609  TYR   D CG  1 
ATOM   12682 C  CD1 . TYR   D  1 308 ? 21.989  -69.321 -44.995  1.00 30.37  ? 609  TYR   D CD1 1 
ATOM   12683 C  CD2 . TYR   D  1 308 ? 22.695  -71.596 -44.790  1.00 36.24  ? 609  TYR   D CD2 1 
ATOM   12684 C  CE1 . TYR   D  1 308 ? 22.200  -69.124 -43.633  1.00 31.72  ? 609  TYR   D CE1 1 
ATOM   12685 C  CE2 . TYR   D  1 308 ? 22.909  -71.408 -43.432  1.00 31.74  ? 609  TYR   D CE2 1 
ATOM   12686 C  CZ  . TYR   D  1 308 ? 22.663  -70.170 -42.867  1.00 28.50  ? 609  TYR   D CZ  1 
ATOM   12687 O  OH  . TYR   D  1 308 ? 22.879  -69.993 -41.528  1.00 33.79  ? 609  TYR   D OH  1 
ATOM   12688 N  N   . ASN   D  1 309 ? 22.878  -70.565 -50.325  1.00 34.17  ? 610  ASN   D N   1 
ATOM   12689 C  CA  . ASN   D  1 309 ? 23.190  -71.108 -51.646  1.00 30.18  ? 610  ASN   D CA  1 
ATOM   12690 C  C   . ASN   D  1 309 ? 22.703  -72.549 -51.809  1.00 27.67  ? 610  ASN   D C   1 
ATOM   12691 O  O   . ASN   D  1 309 ? 23.435  -73.425 -52.269  1.00 35.20  ? 610  ASN   D O   1 
ATOM   12692 C  CB  . ASN   D  1 309 ? 24.696  -71.012 -51.907  1.00 38.95  ? 610  ASN   D CB  1 
ATOM   12693 C  CG  . ASN   D  1 309 ? 25.075  -71.381 -53.338  1.00 40.45  ? 610  ASN   D CG  1 
ATOM   12694 O  OD1 . ASN   D  1 309 ? 24.282  -71.221 -54.273  1.00 34.60  ? 610  ASN   D OD1 1 
ATOM   12695 N  ND2 . ASN   D  1 309 ? 26.283  -71.897 -53.505  1.00 37.94  ? 610  ASN   D ND2 1 
ATOM   12696 N  N   . ILE   D  1 310 ? 21.442  -72.802 -51.443  1.00 29.84  ? 611  ILE   D N   1 
ATOM   12697 C  CA  . ILE   D  1 310 ? 20.976  -74.186 -51.378  1.00 34.21  ? 611  ILE   D CA  1 
ATOM   12698 C  C   . ILE   D  1 310 ? 20.380  -74.708 -52.686  1.00 34.57  ? 611  ILE   D C   1 
ATOM   12699 O  O   . ILE   D  1 310 ? 19.917  -75.858 -52.713  1.00 39.88  ? 611  ILE   D O   1 
ATOM   12700 C  CB  . ILE   D  1 310 ? 19.934  -74.377 -50.257  1.00 39.05  ? 611  ILE   D CB  1 
ATOM   12701 C  CG1 . ILE   D  1 310 ? 18.601  -73.735 -50.651  1.00 34.80  ? 611  ILE   D CG1 1 
ATOM   12702 C  CG2 . ILE   D  1 310 ? 20.447  -73.787 -48.955  1.00 39.98  ? 611  ILE   D CG2 1 
ATOM   12703 C  CD1 . ILE   D  1 310 ? 17.484  -74.023 -49.657  1.00 30.00  ? 611  ILE   D CD1 1 
ATOM   12704 N  N   . LEU   D  1 311 ? 20.379  -73.919 -53.766  1.00 33.82  ? 612  LEU   D N   1 
ATOM   12705 C  CA  . LEU   D  1 311 ? 19.660  -74.331 -54.975  1.00 32.09  ? 612  LEU   D CA  1 
ATOM   12706 C  C   . LEU   D  1 311 ? 20.159  -75.671 -55.499  1.00 31.14  ? 612  LEU   D C   1 
ATOM   12707 O  O   . LEU   D  1 311 ? 19.364  -76.581 -55.755  1.00 37.54  ? 612  LEU   D O   1 
ATOM   12708 C  CB  . LEU   D  1 311 ? 19.774  -73.266 -56.067  1.00 29.55  ? 612  LEU   D CB  1 
ATOM   12709 C  CG  . LEU   D  1 311 ? 18.892  -72.033 -55.902  1.00 30.19  ? 612  LEU   D CG  1 
ATOM   12710 C  CD1 . LEU   D  1 311 ? 19.229  -71.011 -56.970  1.00 29.61  ? 612  LEU   D CD1 1 
ATOM   12711 C  CD2 . LEU   D  1 311 ? 17.426  -72.411 -55.953  1.00 26.45  ? 612  LEU   D CD2 1 
ATOM   12712 N  N   . GLU   D  1 312 ? 21.474  -75.811 -55.669  1.00 33.41  ? 613  GLU   D N   1 
ATOM   12713 C  CA  . GLU   D  1 312 ? 22.018  -77.057 -56.207  1.00 39.32  ? 613  GLU   D CA  1 
ATOM   12714 C  C   . GLU   D  1 312 ? 21.561  -78.260 -55.397  1.00 47.27  ? 613  GLU   D C   1 
ATOM   12715 O  O   . GLU   D  1 312 ? 21.093  -79.261 -55.954  1.00 46.67  ? 613  GLU   D O   1 
ATOM   12716 C  CB  . GLU   D  1 312 ? 23.543  -77.003 -56.235  1.00 60.03  ? 613  GLU   D CB  1 
ATOM   12717 C  CG  . GLU   D  1 312 ? 24.122  -76.148 -57.344  1.00 71.33  ? 613  GLU   D CG  1 
ATOM   12718 C  CD  . GLU   D  1 312 ? 25.619  -75.973 -57.205  1.00 84.02  ? 613  GLU   D CD  1 
ATOM   12719 O  OE1 . GLU   D  1 312 ? 26.340  -76.186 -58.204  1.00 86.13  ? 613  GLU   D OE1 1 
ATOM   12720 O  OE2 . GLU   D  1 312 ? 26.072  -75.628 -56.088  1.00 87.86  ? 613  GLU   D OE2 1 
ATOM   12721 N  N   . GLU   D  1 313 ? 21.697  -78.180 -54.072  1.00 44.30  ? 614  GLU   D N   1 
ATOM   12722 C  CA  . GLU   D  1 313 ? 21.357  -79.318 -53.230  1.00 46.53  ? 614  GLU   D CA  1 
ATOM   12723 C  C   . GLU   D  1 313 ? 19.874  -79.653 -53.333  1.00 48.78  ? 614  GLU   D C   1 
ATOM   12724 O  O   . GLU   D  1 313 ? 19.496  -80.828 -53.387  1.00 48.30  ? 614  GLU   D O   1 
ATOM   12725 C  CB  . GLU   D  1 313 ? 21.769  -79.022 -51.790  1.00 56.81  ? 614  GLU   D CB  1 
ATOM   12726 C  CG  . GLU   D  1 313 ? 20.924  -79.690 -50.734  1.00 72.98  ? 614  GLU   D CG  1 
ATOM   12727 C  CD  . GLU   D  1 313 ? 21.674  -79.900 -49.430  1.00 88.09  ? 614  GLU   D CD  1 
ATOM   12728 O  OE1 . GLU   D  1 313 ? 21.669  -81.044 -48.921  1.00 92.70  ? 614  GLU   D OE1 1 
ATOM   12729 O  OE2 . GLU   D  1 313 ? 22.274  -78.926 -48.921  1.00 94.40  ? 614  GLU   D OE2 1 
ATOM   12730 N  N   . VAL   D  1 314 ? 19.020  -78.632 -53.412  1.00 50.80  ? 615  VAL   D N   1 
ATOM   12731 C  CA  . VAL   D  1 314 ? 17.588  -78.877 -53.538  1.00 43.14  ? 615  VAL   D CA  1 
ATOM   12732 C  C   . VAL   D  1 314 ? 17.261  -79.470 -54.903  1.00 37.76  ? 615  VAL   D C   1 
ATOM   12733 O  O   . VAL   D  1 314 ? 16.497  -80.436 -55.010  1.00 36.64  ? 615  VAL   D O   1 
ATOM   12734 C  CB  . VAL   D  1 314 ? 16.807  -77.578 -53.280  1.00 40.21  ? 615  VAL   D CB  1 
ATOM   12735 C  CG1 . VAL   D  1 314 ? 15.327  -77.745 -53.635  1.00 32.72  ? 615  VAL   D CG1 1 
ATOM   12736 C  CG2 . VAL   D  1 314 ? 16.975  -77.171 -51.836  1.00 35.48  ? 615  VAL   D CG2 1 
ATOM   12737 N  N   . ALA   D  1 315 ? 17.835  -78.903 -55.967  1.00 36.59  ? 616  ALA   D N   1 
ATOM   12738 C  CA  . ALA   D  1 315 ? 17.537  -79.391 -57.311  1.00 37.06  ? 616  ALA   D CA  1 
ATOM   12739 C  C   . ALA   D  1 315 ? 17.950  -80.845 -57.473  1.00 38.71  ? 616  ALA   D C   1 
ATOM   12740 O  O   . ALA   D  1 315 ? 17.237  -81.630 -58.110  1.00 43.16  ? 616  ALA   D O   1 
ATOM   12741 C  CB  . ALA   D  1 315 ? 18.229  -78.520 -58.359  1.00 34.66  ? 616  ALA   D CB  1 
ATOM   12742 N  N   . LYS   D  1 316 ? 19.099  -81.222 -56.905  1.00 48.18  ? 617  LYS   D N   1 
ATOM   12743 C  CA  . LYS   D  1 316 ? 19.517  -82.622 -56.905  1.00 51.49  ? 617  LYS   D CA  1 
ATOM   12744 C  C   . LYS   D  1 316 ? 18.421  -83.516 -56.340  1.00 52.57  ? 617  LYS   D C   1 
ATOM   12745 O  O   . LYS   D  1 316 ? 17.975  -84.466 -56.991  1.00 54.86  ? 617  LYS   D O   1 
ATOM   12746 C  CB  . LYS   D  1 316 ? 20.800  -82.797 -56.088  1.00 57.37  ? 617  LYS   D CB  1 
ATOM   12747 C  CG  . LYS   D  1 316 ? 22.084  -82.344 -56.759  1.00 67.87  ? 617  LYS   D CG  1 
ATOM   12748 C  CD  . LYS   D  1 316 ? 23.278  -82.698 -55.881  1.00 79.16  ? 617  LYS   D CD  1 
ATOM   12749 C  CE  . LYS   D  1 316 ? 24.595  -82.634 -56.641  1.00 87.83  ? 617  LYS   D CE  1 
ATOM   12750 N  NZ  . LYS   D  1 316 ? 25.029  -81.238 -56.929  1.00 86.50  ? 617  LYS   D NZ  1 
ATOM   12751 N  N   . LYS   D  1 317 ? 17.971  -83.211 -55.120  1.00 48.40  ? 618  LYS   D N   1 
ATOM   12752 C  CA  . LYS   D  1 317 ? 16.929  -84.013 -54.490  1.00 48.61  ? 618  LYS   D CA  1 
ATOM   12753 C  C   . LYS   D  1 317 ? 15.662  -84.051 -55.333  1.00 49.89  ? 618  LYS   D C   1 
ATOM   12754 O  O   . LYS   D  1 317 ? 14.925  -85.045 -55.306  1.00 48.98  ? 618  LYS   D O   1 
ATOM   12755 C  CB  . LYS   D  1 317 ? 16.628  -83.466 -53.096  1.00 48.06  ? 618  LYS   D CB  1 
ATOM   12756 C  CG  . LYS   D  1 317 ? 17.684  -83.794 -52.042  1.00 58.65  ? 618  LYS   D CG  1 
ATOM   12757 C  CD  . LYS   D  1 317 ? 17.312  -85.060 -51.270  1.00 70.56  ? 618  LYS   D CD  1 
ATOM   12758 C  CE  . LYS   D  1 317 ? 18.537  -85.794 -50.723  1.00 76.36  ? 618  LYS   D CE  1 
ATOM   12759 N  NZ  . LYS   D  1 317 ? 19.309  -84.993 -49.729  1.00 74.28  ? 618  LYS   D NZ  1 
ATOM   12760 N  N   . MET   D  1 318 ? 15.394  -82.987 -56.084  1.00 39.63  ? 619  MET   D N   1 
ATOM   12761 C  CA  . MET   D  1 318 ? 14.256  -82.951 -56.993  1.00 45.32  ? 619  MET   D CA  1 
ATOM   12762 C  C   . MET   D  1 318 ? 14.527  -83.664 -58.308  1.00 42.39  ? 619  MET   D C   1 
ATOM   12763 O  O   . MET   D  1 318 ? 13.607  -83.775 -59.125  1.00 42.47  ? 619  MET   D O   1 
ATOM   12764 C  CB  . MET   D  1 318 ? 13.849  -81.504 -57.279  1.00 38.09  ? 619  MET   D CB  1 
ATOM   12765 C  CG  . MET   D  1 318 ? 13.224  -80.800 -56.107  1.00 38.30  ? 619  MET   D CG  1 
ATOM   12766 S  SD  . MET   D  1 318 ? 12.828  -79.084 -56.486  1.00 39.61  ? 619  MET   D SD  1 
ATOM   12767 C  CE  . MET   D  1 318 ? 11.697  -79.281 -57.866  1.00 41.09  ? 619  MET   D CE  1 
ATOM   12768 N  N   . ASN   D  1 319 ? 15.757  -84.137 -58.526  1.00 47.59  ? 620  ASN   D N   1 
ATOM   12769 C  CA  . ASN   D  1 319 ? 16.139  -84.840 -59.755  1.00 56.56  ? 620  ASN   D CA  1 
ATOM   12770 C  C   . ASN   D  1 319 ? 15.881  -83.984 -60.990  1.00 48.21  ? 620  ASN   D C   1 
ATOM   12771 O  O   . ASN   D  1 319 ? 15.379  -84.457 -62.013  1.00 46.20  ? 620  ASN   D O   1 
ATOM   12772 C  CB  . ASN   D  1 319 ? 15.434  -86.189 -59.857  1.00 67.55  ? 620  ASN   D CB  1 
ATOM   12773 C  CG  . ASN   D  1 319 ? 15.921  -87.157 -58.812  1.00 78.11  ? 620  ASN   D CG  1 
ATOM   12774 O  OD1 . ASN   D  1 319 ? 17.122  -87.401 -58.704  1.00 84.56  ? 620  ASN   D OD1 1 
ATOM   12775 N  ND2 . ASN   D  1 319 ? 15.003  -87.695 -58.018  1.00 80.33  ? 620  ASN   D ND2 1 
ATOM   12776 N  N   . LEU   D  1 320 ? 16.234  -82.709 -60.887  1.00 45.59  ? 621  LEU   D N   1 
ATOM   12777 C  CA  . LEU   D  1 320 ? 16.110  -81.794 -62.007  1.00 46.96  ? 621  LEU   D CA  1 
ATOM   12778 C  C   . LEU   D  1 320 ? 17.310  -81.916 -62.930  1.00 52.61  ? 621  LEU   D C   1 
ATOM   12779 O  O   . LEU   D  1 320 ? 18.415  -82.264 -62.508  1.00 57.19  ? 621  LEU   D O   1 
ATOM   12780 C  CB  . LEU   D  1 320 ? 15.991  -80.356 -61.515  1.00 38.46  ? 621  LEU   D CB  1 
ATOM   12781 C  CG  . LEU   D  1 320 ? 14.863  -80.157 -60.510  1.00 41.07  ? 621  LEU   D CG  1 
ATOM   12782 C  CD1 . LEU   D  1 320 ? 14.883  -78.743 -59.950  1.00 37.68  ? 621  LEU   D CD1 1 
ATOM   12783 C  CD2 . LEU   D  1 320 ? 13.520  -80.488 -61.163  1.00 37.18  ? 621  LEU   D CD2 1 
ATOM   12784 N  N   . ASP   D  1 321 ? 17.075  -81.626 -64.201  1.00 52.37  ? 622  ASP   D N   1 
ATOM   12785 C  CA  . ASP   D  1 321 ? 18.135  -81.547 -65.200  1.00 57.15  ? 622  ASP   D CA  1 
ATOM   12786 C  C   . ASP   D  1 321 ? 18.969  -80.299 -64.925  1.00 51.83  ? 622  ASP   D C   1 
ATOM   12787 O  O   . ASP   D  1 321 ? 18.562  -79.183 -65.248  1.00 52.44  ? 622  ASP   D O   1 
ATOM   12788 C  CB  . ASP   D  1 321 ? 17.517  -81.514 -66.594  1.00 61.21  ? 622  ASP   D CB  1 
ATOM   12789 C  CG  . ASP   D  1 321 ? 18.551  -81.430 -67.684  1.00 75.33  ? 622  ASP   D CG  1 
ATOM   12790 O  OD1 . ASP   D  1 321 ? 19.748  -81.621 -67.371  1.00 71.90  ? 622  ASP   D OD1 1 
ATOM   12791 O  OD2 . ASP   D  1 321 ? 18.162  -81.183 -68.854  1.00 77.66  ? 622  ASP   D OD2 1 
ATOM   12792 N  N   . MET   D  1 322 ? 20.148  -80.477 -64.330  1.00 48.23  ? 623  MET   D N   1 
ATOM   12793 C  CA  . MET   D  1 322 ? 20.988  -79.354 -63.935  1.00 48.14  ? 623  MET   D CA  1 
ATOM   12794 C  C   . MET   D  1 322 ? 22.134  -79.104 -64.897  1.00 53.69  ? 623  MET   D C   1 
ATOM   12795 O  O   . MET   D  1 322 ? 23.047  -78.340 -64.566  1.00 61.31  ? 623  MET   D O   1 
ATOM   12796 C  CB  . MET   D  1 322 ? 21.545  -79.566 -62.531  1.00 45.57  ? 623  MET   D CB  1 
ATOM   12797 C  CG  . MET   D  1 322 ? 20.490  -79.514 -61.462  1.00 51.94  ? 623  MET   D CG  1 
ATOM   12798 S  SD  . MET   D  1 322 ? 21.087  -80.122 -59.880  1.00 55.80  ? 623  MET   D SD  1 
ATOM   12799 C  CE  . MET   D  1 322 ? 22.243  -78.827 -59.402  1.00 44.66  ? 623  MET   D CE  1 
ATOM   12800 N  N   . ARG   D  1 323 ? 22.101  -79.723 -66.079  1.00 45.10  ? 624  ARG   D N   1 
ATOM   12801 C  CA  . ARG   D  1 323 ? 23.166  -79.535 -67.056  1.00 54.44  ? 624  ARG   D CA  1 
ATOM   12802 C  C   . ARG   D  1 323 ? 23.157  -78.125 -67.627  1.00 50.12  ? 624  ARG   D C   1 
ATOM   12803 O  O   . ARG   D  1 323 ? 24.219  -77.535 -67.852  1.00 51.07  ? 624  ARG   D O   1 
ATOM   12804 C  CB  . ARG   D  1 323 ? 23.021  -80.564 -68.179  1.00 59.87  ? 624  ARG   D CB  1 
ATOM   12805 C  CG  . ARG   D  1 323 ? 23.984  -80.390 -69.347  1.00 68.47  ? 624  ARG   D CG  1 
ATOM   12806 C  CD  . ARG   D  1 323 ? 23.884  -81.555 -70.339  1.00 68.94  ? 624  ARG   D CD  1 
ATOM   12807 N  NE  . ARG   D  1 323 ? 23.327  -81.156 -71.633  1.00 82.78  ? 624  ARG   D NE  1 
ATOM   12808 C  CZ  . ARG   D  1 323 ? 24.056  -80.752 -72.671  1.00 96.32  ? 624  ARG   D CZ  1 
ATOM   12809 N  NH1 . ARG   D  1 323 ? 25.376  -80.687 -72.568  1.00 104.83 ? 624  ARG   D NH1 1 
ATOM   12810 N  NH2 . ARG   D  1 323 ? 23.471  -80.410 -73.814  1.00 96.12  ? 624  ARG   D NH2 1 
ATOM   12811 N  N   . LYS   D  1 324 ? 21.973  -77.574 -67.873  1.00 45.02  ? 625  LYS   D N   1 
ATOM   12812 C  CA  . LYS   D  1 324 ? 21.825  -76.338 -68.628  1.00 51.78  ? 625  LYS   D CA  1 
ATOM   12813 C  C   . LYS   D  1 324 ? 20.928  -75.375 -67.866  1.00 46.36  ? 625  LYS   D C   1 
ATOM   12814 O  O   . LYS   D  1 324 ? 19.984  -75.794 -67.193  1.00 49.96  ? 625  LYS   D O   1 
ATOM   12815 C  CB  . LYS   D  1 324 ? 21.229  -76.614 -70.017  1.00 52.62  ? 625  LYS   D CB  1 
ATOM   12816 C  CG  . LYS   D  1 324 ? 21.765  -75.727 -71.121  1.00 70.41  ? 625  LYS   D CG  1 
ATOM   12817 C  CD  . LYS   D  1 324 ? 22.412  -76.575 -72.205  1.00 74.01  ? 625  LYS   D CD  1 
ATOM   12818 C  CE  . LYS   D  1 324 ? 23.356  -75.757 -73.074  1.00 81.96  ? 625  LYS   D CE  1 
ATOM   12819 N  NZ  . LYS   D  1 324 ? 24.168  -76.634 -73.967  1.00 89.08  ? 625  LYS   D NZ  1 
ATOM   12820 N  N   . THR   D  1 325 ? 21.224  -74.074 -67.981  1.00 39.06  ? 626  THR   D N   1 
ATOM   12821 C  CA  . THR   D  1 325 ? 20.363  -73.080 -67.343  1.00 43.61  ? 626  THR   D CA  1 
ATOM   12822 C  C   . THR   D  1 325 ? 18.945  -73.136 -67.894  1.00 37.99  ? 626  THR   D C   1 
ATOM   12823 O  O   . THR   D  1 325 ? 17.983  -72.929 -67.148  1.00 37.60  ? 626  THR   D O   1 
ATOM   12824 C  CB  . THR   D  1 325 ? 20.930  -71.665 -67.523  1.00 44.02  ? 626  THR   D CB  1 
ATOM   12825 O  OG1 . THR   D  1 325 ? 20.988  -71.344 -68.917  1.00 46.83  ? 626  THR   D OG1 1 
ATOM   12826 C  CG2 . THR   D  1 325 ? 22.323  -71.567 -66.948  1.00 49.35  ? 626  THR   D CG2 1 
ATOM   12827 N  N   . SER   D  1 326 ? 18.796  -73.439 -69.188  1.00 39.23  ? 627  SER   D N   1 
ATOM   12828 C  CA  . SER   D  1 326 ? 17.497  -73.353 -69.840  1.00 33.26  ? 627  SER   D CA  1 
ATOM   12829 C  C   . SER   D  1 326 ? 16.509  -74.405 -69.360  1.00 39.92  ? 627  SER   D C   1 
ATOM   12830 O  O   . SER   D  1 326 ? 15.323  -74.286 -69.678  1.00 40.91  ? 627  SER   D O   1 
ATOM   12831 C  CB  . SER   D  1 326 ? 17.654  -73.453 -71.360  1.00 40.80  ? 627  SER   D CB  1 
ATOM   12832 O  OG  . SER   D  1 326 ? 18.159  -74.713 -71.733  1.00 46.55  ? 627  SER   D OG  1 
ATOM   12833 N  N   . SER   D  1 327 ? 16.947  -75.425 -68.611  1.00 37.73  ? 628  SER   D N   1 
ATOM   12834 C  CA  . SER   D  1 327 ? 15.963  -76.279 -67.957  1.00 39.94  ? 628  SER   D CA  1 
ATOM   12835 C  C   . SER   D  1 327 ? 15.211  -75.542 -66.866  1.00 38.86  ? 628  SER   D C   1 
ATOM   12836 O  O   . SER   D  1 327 ? 14.193  -76.054 -66.393  1.00 37.64  ? 628  SER   D O   1 
ATOM   12837 C  CB  . SER   D  1 327 ? 16.617  -77.515 -67.347  1.00 38.35  ? 628  SER   D CB  1 
ATOM   12838 O  OG  . SER   D  1 327 ? 17.449  -77.148 -66.268  1.00 37.00  ? 628  SER   D OG  1 
ATOM   12839 N  N   . LEU   D  1 328 ? 15.698  -74.364 -66.465  1.00 35.91  ? 629  LEU   D N   1 
ATOM   12840 C  CA  . LEU   D  1 328 ? 15.122  -73.577 -65.385  1.00 38.06  ? 629  LEU   D CA  1 
ATOM   12841 C  C   . LEU   D  1 328 ? 15.050  -74.376 -64.082  1.00 35.57  ? 629  LEU   D C   1 
ATOM   12842 O  O   . LEU   D  1 328 ? 14.113  -74.235 -63.292  1.00 30.51  ? 629  LEU   D O   1 
ATOM   12843 C  CB  . LEU   D  1 328 ? 13.753  -73.022 -65.781  1.00 35.99  ? 629  LEU   D CB  1 
ATOM   12844 C  CG  . LEU   D  1 328 ? 13.752  -72.195 -67.069  1.00 31.93  ? 629  LEU   D CG  1 
ATOM   12845 C  CD1 . LEU   D  1 328 ? 12.499  -71.363 -67.155  1.00 27.77  ? 629  LEU   D CD1 1 
ATOM   12846 C  CD2 . LEU   D  1 328 ? 14.977  -71.301 -67.137  1.00 28.67  ? 629  LEU   D CD2 1 
ATOM   12847 N  N   . TRP   D  1 329 ? 16.065  -75.218 -63.852  1.00 30.66  ? 630  TRP   D N   1 
ATOM   12848 C  CA  . TRP   D  1 329 ? 16.120  -75.990 -62.615  1.00 31.02  ? 630  TRP   D CA  1 
ATOM   12849 C  C   . TRP   D  1 329 ? 16.290  -75.091 -61.396  1.00 32.25  ? 630  TRP   D C   1 
ATOM   12850 O  O   . TRP   D  1 329 ? 15.762  -75.398 -60.318  1.00 33.25  ? 630  TRP   D O   1 
ATOM   12851 C  CB  . TRP   D  1 329 ? 17.247  -77.019 -62.681  1.00 32.49  ? 630  TRP   D CB  1 
ATOM   12852 C  CG  . TRP   D  1 329 ? 18.623  -76.431 -62.784  1.00 34.79  ? 630  TRP   D CG  1 
ATOM   12853 C  CD1 . TRP   D  1 329 ? 19.314  -76.160 -63.926  1.00 41.54  ? 630  TRP   D CD1 1 
ATOM   12854 C  CD2 . TRP   D  1 329 ? 19.483  -76.059 -61.698  1.00 39.32  ? 630  TRP   D CD2 1 
ATOM   12855 N  NE1 . TRP   D  1 329 ? 20.548  -75.637 -63.623  1.00 44.69  ? 630  TRP   D NE1 1 
ATOM   12856 C  CE2 . TRP   D  1 329 ? 20.675  -75.566 -62.260  1.00 41.23  ? 630  TRP   D CE2 1 
ATOM   12857 C  CE3 . TRP   D  1 329 ? 19.358  -76.094 -60.308  1.00 35.16  ? 630  TRP   D CE3 1 
ATOM   12858 C  CZ2 . TRP   D  1 329 ? 21.735  -75.116 -61.478  1.00 38.47  ? 630  TRP   D CZ2 1 
ATOM   12859 C  CZ3 . TRP   D  1 329 ? 20.411  -75.658 -59.530  1.00 33.59  ? 630  TRP   D CZ3 1 
ATOM   12860 C  CH2 . TRP   D  1 329 ? 21.587  -75.176 -60.117  1.00 39.18  ? 630  TRP   D CH2 1 
ATOM   12861 N  N   . LYS   D  1 330 ? 17.004  -73.975 -61.537  1.00 29.35  ? 631  LYS   D N   1 
ATOM   12862 C  CA  . LYS   D  1 330 ? 17.097  -73.050 -60.417  1.00 27.64  ? 631  LYS   D CA  1 
ATOM   12863 C  C   . LYS   D  1 330 ? 15.733  -72.461 -60.093  1.00 34.59  ? 631  LYS   D C   1 
ATOM   12864 O  O   . LYS   D  1 330 ? 15.326  -72.395 -58.924  1.00 30.24  ? 631  LYS   D O   1 
ATOM   12865 C  CB  . LYS   D  1 330 ? 18.101  -71.948 -60.724  1.00 29.89  ? 631  LYS   D CB  1 
ATOM   12866 C  CG  . LYS   D  1 330 ? 19.539  -72.407 -60.719  1.00 37.85  ? 631  LYS   D CG  1 
ATOM   12867 C  CD  . LYS   D  1 330 ? 20.484  -71.223 -60.663  1.00 35.45  ? 631  LYS   D CD  1 
ATOM   12868 C  CE  . LYS   D  1 330 ? 21.927  -71.671 -60.611  1.00 39.79  ? 631  LYS   D CE  1 
ATOM   12869 N  NZ  . LYS   D  1 330 ? 22.842  -70.506 -60.528  1.00 43.89  ? 631  LYS   D NZ  1 
ATOM   12870 N  N   . ASP   D  1 331 ? 15.008  -72.036 -61.124  1.00 28.93  ? 632  ASP   D N   1 
ATOM   12871 C  CA  . ASP   D  1 331 ? 13.686  -71.465 -60.916  1.00 28.84  ? 632  ASP   D CA  1 
ATOM   12872 C  C   . ASP   D  1 331 ? 12.738  -72.484 -60.305  1.00 29.95  ? 632  ASP   D C   1 
ATOM   12873 O  O   . ASP   D  1 331 ? 11.896  -72.135 -59.476  1.00 33.23  ? 632  ASP   D O   1 
ATOM   12874 C  CB  . ASP   D  1 331 ? 13.131  -70.964 -62.254  1.00 28.28  ? 632  ASP   D CB  1 
ATOM   12875 C  CG  . ASP   D  1 331 ? 14.168  -70.209 -63.066  1.00 29.94  ? 632  ASP   D CG  1 
ATOM   12876 O  OD1 . ASP   D  1 331 ? 15.079  -70.855 -63.624  1.00 36.15  ? 632  ASP   D OD1 1 
ATOM   12877 O  OD2 . ASP   D  1 331 ? 14.081  -68.971 -63.134  1.00 31.11  ? 632  ASP   D OD2 1 
ATOM   12878 N  N   . GLN   D  1 332 ? 12.834  -73.744 -60.739  1.00 29.96  ? 633  GLN   D N   1 
ATOM   12879 C  CA  . GLN   D  1 332 ? 11.955  -74.772 -60.203  1.00 31.90  ? 633  GLN   D CA  1 
ATOM   12880 C  C   . GLN   D  1 332 ? 12.248  -75.016 -58.737  1.00 32.93  ? 633  GLN   D C   1 
ATOM   12881 O  O   . GLN   D  1 332 ? 11.333  -75.054 -57.912  1.00 27.90  ? 633  GLN   D O   1 
ATOM   12882 C  CB  . GLN   D  1 332 ? 12.111  -76.080 -60.970  1.00 31.86  ? 633  GLN   D CB  1 
ATOM   12883 C  CG  . GLN   D  1 332 ? 11.424  -76.116 -62.293  1.00 45.22  ? 633  GLN   D CG  1 
ATOM   12884 C  CD  . GLN   D  1 332 ? 11.145  -77.530 -62.730  1.00 51.04  ? 633  GLN   D CD  1 
ATOM   12885 O  OE1 . GLN   D  1 332 ? 10.032  -78.021 -62.579  1.00 65.96  ? 633  GLN   D OE1 1 
ATOM   12886 N  NE2 . GLN   D  1 332 ? 12.161  -78.200 -63.256  1.00 46.87  ? 633  GLN   D NE2 1 
ATOM   12887 N  N   . ALA   D  1 333 ? 13.523  -75.229 -58.406  1.00 34.39  ? 634  ALA   D N   1 
ATOM   12888 C  CA  . ALA   D  1 333 ? 13.884  -75.423 -57.009  1.00 34.05  ? 634  ALA   D CA  1 
ATOM   12889 C  C   . ALA   D  1 333 ? 13.500  -74.207 -56.189  1.00 31.61  ? 634  ALA   D C   1 
ATOM   12890 O  O   . ALA   D  1 333 ? 12.981  -74.337 -55.075  1.00 28.72  ? 634  ALA   D O   1 
ATOM   12891 C  CB  . ALA   D  1 333 ? 15.378  -75.714 -56.882  1.00 34.25  ? 634  ALA   D CB  1 
ATOM   12892 N  N   . LEU   D  1 334 ? 13.702  -73.016 -56.752  1.00 32.49  ? 635  LEU   D N   1 
ATOM   12893 C  CA  . LEU   D  1 334 ? 13.404  -71.793 -56.022  1.00 33.66  ? 635  LEU   D CA  1 
ATOM   12894 C  C   . LEU   D  1 334 ? 11.954  -71.769 -55.558  1.00 36.97  ? 635  LEU   D C   1 
ATOM   12895 O  O   . LEU   D  1 334 ? 11.672  -71.415 -54.403  1.00 27.60  ? 635  LEU   D O   1 
ATOM   12896 C  CB  . LEU   D  1 334 ? 13.716  -70.575 -56.889  1.00 30.52  ? 635  LEU   D CB  1 
ATOM   12897 C  CG  . LEU   D  1 334 ? 13.457  -69.229 -56.206  1.00 30.91  ? 635  LEU   D CG  1 
ATOM   12898 C  CD1 . LEU   D  1 334 ? 14.354  -69.036 -54.980  1.00 35.88  ? 635  LEU   D CD1 1 
ATOM   12899 C  CD2 . LEU   D  1 334 ? 13.669  -68.110 -57.201  1.00 29.39  ? 635  LEU   D CD2 1 
ATOM   12900 N  N   . VAL   D  1 335 ? 11.017  -72.159 -56.430  1.00 32.61  ? 636  VAL   D N   1 
ATOM   12901 C  CA  . VAL   D  1 335 ? 9.613   -72.124 -56.032  1.00 34.91  ? 636  VAL   D CA  1 
ATOM   12902 C  C   . VAL   D  1 335 ? 9.350   -73.122 -54.905  1.00 34.57  ? 636  VAL   D C   1 
ATOM   12903 O  O   . VAL   D  1 335 ? 8.688   -72.804 -53.907  1.00 33.93  ? 636  VAL   D O   1 
ATOM   12904 C  CB  . VAL   D  1 335 ? 8.698   -72.377 -57.238  1.00 34.21  ? 636  VAL   D CB  1 
ATOM   12905 C  CG1 . VAL   D  1 335 ? 7.266   -72.495 -56.766  1.00 33.32  ? 636  VAL   D CG1 1 
ATOM   12906 C  CG2 . VAL   D  1 335 ? 8.833   -71.246 -58.240  1.00 29.34  ? 636  VAL   D CG2 1 
ATOM   12907 N  N   . GLU   D  1 336 ? 9.887   -74.334 -55.036  1.00 28.16  ? 637  GLU   D N   1 
ATOM   12908 C  CA  . GLU   D  1 336 ? 9.661   -75.356 -54.023  1.00 32.13  ? 637  GLU   D CA  1 
ATOM   12909 C  C   . GLU   D  1 336 ? 10.222  -74.929 -52.674  1.00 33.73  ? 637  GLU   D C   1 
ATOM   12910 O  O   . GLU   D  1 336 ? 9.585   -75.139 -51.636  1.00 35.94  ? 637  GLU   D O   1 
ATOM   12911 C  CB  . GLU   D  1 336 ? 10.263  -76.677 -54.478  1.00 36.20  ? 637  GLU   D CB  1 
ATOM   12912 C  CG  . GLU   D  1 336 ? 9.666   -77.183 -55.789  1.00 40.14  ? 637  GLU   D CG  1 
ATOM   12913 C  CD  . GLU   D  1 336 ? 8.184   -77.598 -55.706  1.00 49.32  ? 637  GLU   D CD  1 
ATOM   12914 O  OE1 . GLU   D  1 336 ? 7.576   -77.642 -54.609  1.00 43.50  ? 637  GLU   D OE1 1 
ATOM   12915 O  OE2 . GLU   D  1 336 ? 7.622   -77.901 -56.778  1.00 55.82  ? 637  GLU   D OE2 1 
ATOM   12916 N  N   . ILE   D  1 337 ? 11.392  -74.292 -52.670  1.00 32.84  ? 638  ILE   D N   1 
ATOM   12917 C  CA  . ILE   D  1 337 ? 11.946  -73.787 -51.420  1.00 31.51  ? 638  ILE   D CA  1 
ATOM   12918 C  C   . ILE   D  1 337 ? 11.004  -72.769 -50.800  1.00 33.81  ? 638  ILE   D C   1 
ATOM   12919 O  O   . ILE   D  1 337 ? 10.736  -72.800 -49.592  1.00 33.45  ? 638  ILE   D O   1 
ATOM   12920 C  CB  . ILE   D  1 337 ? 13.348  -73.198 -51.655  1.00 29.84  ? 638  ILE   D CB  1 
ATOM   12921 C  CG1 . ILE   D  1 337 ? 14.339  -74.333 -51.941  1.00 32.14  ? 638  ILE   D CG1 1 
ATOM   12922 C  CG2 . ILE   D  1 337 ? 13.815  -72.393 -50.429  1.00 27.66  ? 638  ILE   D CG2 1 
ATOM   12923 C  CD1 . ILE   D  1 337 ? 15.515  -73.914 -52.755  1.00 35.73  ? 638  ILE   D CD1 1 
ATOM   12924 N  N   . ASN   D  1 338 ? 10.453  -71.878 -51.618  1.00 30.73  ? 639  ASN   D N   1 
ATOM   12925 C  CA  . ASN   D  1 338 ? 9.602   -70.839 -51.060  1.00 29.36  ? 639  ASN   D CA  1 
ATOM   12926 C  C   . ASN   D  1 338 ? 8.241   -71.373 -50.656  1.00 33.25  ? 639  ASN   D C   1 
ATOM   12927 O  O   . ASN   D  1 338 ? 7.642   -70.852 -49.707  1.00 32.20  ? 639  ASN   D O   1 
ATOM   12928 C  CB  . ASN   D  1 338 ? 9.482   -69.688 -52.044  1.00 23.36  ? 639  ASN   D CB  1 
ATOM   12929 C  CG  . ASN   D  1 338 ? 10.707  -68.825 -52.019  1.00 26.31  ? 639  ASN   D CG  1 
ATOM   12930 O  OD1 . ASN   D  1 338 ? 10.778  -67.856 -51.259  1.00 28.67  ? 639  ASN   D OD1 1 
ATOM   12931 N  ND2 . ASN   D  1 338 ? 11.723  -69.226 -52.777  1.00 25.47  ? 639  ASN   D ND2 1 
ATOM   12932 N  N   . ILE   D  1 339 ? 7.748   -72.411 -51.339  1.00 27.75  ? 640  ILE   D N   1 
ATOM   12933 C  CA  . ILE   D  1 339 ? 6.583   -73.132 -50.838  1.00 30.28  ? 640  ILE   D CA  1 
ATOM   12934 C  C   . ILE   D  1 339 ? 6.882   -73.712 -49.455  1.00 36.68  ? 640  ILE   D C   1 
ATOM   12935 O  O   . ILE   D  1 339 ? 6.077   -73.596 -48.524  1.00 27.22  ? 640  ILE   D O   1 
ATOM   12936 C  CB  . ILE   D  1 339 ? 6.159   -74.230 -51.827  1.00 26.48  ? 640  ILE   D CB  1 
ATOM   12937 C  CG1 . ILE   D  1 339 ? 5.552   -73.622 -53.099  1.00 27.55  ? 640  ILE   D CG1 1 
ATOM   12938 C  CG2 . ILE   D  1 339 ? 5.178   -75.197 -51.172  1.00 29.87  ? 640  ILE   D CG2 1 
ATOM   12939 C  CD1 . ILE   D  1 339 ? 5.170   -74.665 -54.127  1.00 31.05  ? 640  ILE   D CD1 1 
ATOM   12940 N  N   . ALA   D  1 340 ? 8.056   -74.329 -49.303  1.00 29.84  ? 641  ALA   D N   1 
ATOM   12941 C  CA  . ALA   D  1 340 ? 8.425   -74.949 -48.035  1.00 29.82  ? 641  ALA   D CA  1 
ATOM   12942 C  C   . ALA   D  1 340 ? 8.515   -73.917 -46.915  1.00 34.02  ? 641  ALA   D C   1 
ATOM   12943 O  O   . ALA   D  1 340 ? 7.976   -74.125 -45.823  1.00 30.04  ? 641  ALA   D O   1 
ATOM   12944 C  CB  . ALA   D  1 340 ? 9.752   -75.697 -48.193  1.00 27.98  ? 641  ALA   D CB  1 
ATOM   12945 N  N   . VAL   D  1 341 ? 9.193   -72.795 -47.164  1.00 29.71  ? 642  VAL   D N   1 
ATOM   12946 C  CA  . VAL   D  1 341 ? 9.338   -71.780 -46.124  1.00 28.56  ? 642  VAL   D CA  1 
ATOM   12947 C  C   . VAL   D  1 341 ? 7.970   -71.332 -45.629  1.00 32.20  ? 642  VAL   D C   1 
ATOM   12948 O  O   . VAL   D  1 341 ? 7.694   -71.328 -44.419  1.00 27.05  ? 642  VAL   D O   1 
ATOM   12949 C  CB  . VAL   D  1 341 ? 10.168  -70.597 -46.646  1.00 27.65  ? 642  VAL   D CB  1 
ATOM   12950 C  CG1 . VAL   D  1 341 ? 10.047  -69.414 -45.711  1.00 25.25  ? 642  VAL   D CG1 1 
ATOM   12951 C  CG2 . VAL   D  1 341 ? 11.618  -71.019 -46.800  1.00 27.03  ? 642  VAL   D CG2 1 
ATOM   12952 N  N   . LEU   D  1 342 ? 7.080   -70.982 -46.563  1.00 30.39  ? 643  LEU   D N   1 
ATOM   12953 C  CA  . LEU   D  1 342 ? 5.744   -70.525 -46.193  1.00 33.96  ? 643  LEU   D CA  1 
ATOM   12954 C  C   . LEU   D  1 342 ? 4.971   -71.616 -45.472  1.00 39.25  ? 643  LEU   D C   1 
ATOM   12955 O  O   . LEU   D  1 342 ? 4.337   -71.371 -44.439  1.00 33.14  ? 643  LEU   D O   1 
ATOM   12956 C  CB  . LEU   D  1 342 ? 4.979   -70.080 -47.436  1.00 31.76  ? 643  LEU   D CB  1 
ATOM   12957 C  CG  . LEU   D  1 342 ? 5.467   -68.773 -48.067  1.00 30.63  ? 643  LEU   D CG  1 
ATOM   12958 C  CD1 . LEU   D  1 342 ? 4.854   -68.610 -49.463  1.00 24.83  ? 643  LEU   D CD1 1 
ATOM   12959 C  CD2 . LEU   D  1 342 ? 5.180   -67.561 -47.165  1.00 23.61  ? 643  LEU   D CD2 1 
ATOM   12960 N  N   . TYR   D  1 343 ? 4.979   -72.823 -46.032  1.00 34.08  ? 644  TYR   D N   1 
ATOM   12961 C  CA  . TYR   D  1 343 ? 4.261   -73.919 -45.403  1.00 33.94  ? 644  TYR   D CA  1 
ATOM   12962 C  C   . TYR   D  1 343 ? 4.752   -74.157 -43.978  1.00 33.35  ? 644  TYR   D C   1 
ATOM   12963 O  O   . TYR   D  1 343 ? 3.955   -74.426 -43.070  1.00 33.20  ? 644  TYR   D O   1 
ATOM   12964 C  CB  . TYR   D  1 343 ? 4.424   -75.168 -46.247  1.00 27.32  ? 644  TYR   D CB  1 
ATOM   12965 C  CG  . TYR   D  1 343 ? 3.959   -76.418 -45.566  1.00 29.35  ? 644  TYR   D CG  1 
ATOM   12966 C  CD1 . TYR   D  1 343 ? 2.612   -76.738 -45.522  1.00 34.53  ? 644  TYR   D CD1 1 
ATOM   12967 C  CD2 . TYR   D  1 343 ? 4.870   -77.294 -44.991  1.00 31.97  ? 644  TYR   D CD2 1 
ATOM   12968 C  CE1 . TYR   D  1 343 ? 2.181   -77.888 -44.916  1.00 35.22  ? 644  TYR   D CE1 1 
ATOM   12969 C  CE2 . TYR   D  1 343 ? 4.450   -78.457 -44.382  1.00 38.76  ? 644  TYR   D CE2 1 
ATOM   12970 C  CZ  . TYR   D  1 343 ? 3.106   -78.747 -44.346  1.00 39.17  ? 644  TYR   D CZ  1 
ATOM   12971 O  OH  . TYR   D  1 343 ? 2.684   -79.901 -43.743  1.00 40.23  ? 644  TYR   D OH  1 
ATOM   12972 N  N   . SER   D  1 344 ? 6.063   -74.042 -43.760  1.00 33.57  ? 645  SER   D N   1 
ATOM   12973 C  CA  . SER   D  1 344 ? 6.627   -74.374 -42.458  1.00 32.94  ? 645  SER   D CA  1 
ATOM   12974 C  C   . SER   D  1 344 ? 6.255   -73.324 -41.418  1.00 36.41  ? 645  SER   D C   1 
ATOM   12975 O  O   . SER   D  1 344 ? 5.836   -73.656 -40.299  1.00 31.90  ? 645  SER   D O   1 
ATOM   12976 C  CB  . SER   D  1 344 ? 8.144   -74.516 -42.575  1.00 30.61  ? 645  SER   D CB  1 
ATOM   12977 O  OG  . SER   D  1 344 ? 8.482   -75.667 -43.339  1.00 32.02  ? 645  SER   D OG  1 
ATOM   12978 N  N   . PHE   D  1 345 ? 6.414   -72.050 -41.770  1.00 29.08  ? 646  PHE   D N   1 
ATOM   12979 C  CA  . PHE   D  1 345 ? 6.034   -70.981 -40.859  1.00 25.30  ? 646  PHE   D CA  1 
ATOM   12980 C  C   . PHE   D  1 345 ? 4.555   -71.066 -40.513  1.00 28.73  ? 646  PHE   D C   1 
ATOM   12981 O  O   . PHE   D  1 345 ? 4.172   -70.984 -39.339  1.00 27.79  ? 646  PHE   D O   1 
ATOM   12982 C  CB  . PHE   D  1 345 ? 6.366   -69.626 -41.478  1.00 26.62  ? 646  PHE   D CB  1 
ATOM   12983 C  CG  . PHE   D  1 345 ? 7.742   -69.147 -41.172  1.00 27.74  ? 646  PHE   D CG  1 
ATOM   12984 C  CD1 . PHE   D  1 345 ? 8.855   -69.815 -41.662  1.00 27.58  ? 646  PHE   D CD1 1 
ATOM   12985 C  CD2 . PHE   D  1 345 ? 7.928   -68.013 -40.403  1.00 22.76  ? 646  PHE   D CD2 1 
ATOM   12986 C  CE1 . PHE   D  1 345 ? 10.143  -69.356 -41.368  1.00 22.35  ? 646  PHE   D CE1 1 
ATOM   12987 C  CE2 . PHE   D  1 345 ? 9.196   -67.542 -40.122  1.00 24.83  ? 646  PHE   D CE2 1 
ATOM   12988 C  CZ  . PHE   D  1 345 ? 10.307  -68.214 -40.595  1.00 21.01  ? 646  PHE   D CZ  1 
ATOM   12989 N  N   . GLN   D  1 346 ? 3.711   -71.266 -41.523  1.00 29.80  ? 647  GLN   D N   1 
ATOM   12990 C  CA  . GLN   D  1 346 ? 2.277   -71.327 -41.276  1.00 33.96  ? 647  GLN   D CA  1 
ATOM   12991 C  C   . GLN   D  1 346 ? 1.909   -72.539 -40.435  1.00 35.54  ? 647  GLN   D C   1 
ATOM   12992 O  O   . GLN   D  1 346 ? 1.012   -72.466 -39.588  1.00 35.37  ? 647  GLN   D O   1 
ATOM   12993 C  CB  . GLN   D  1 346 ? 1.527   -71.349 -42.599  1.00 33.07  ? 647  GLN   D CB  1 
ATOM   12994 C  CG  . GLN   D  1 346 ? 1.631   -70.038 -43.380  1.00 37.16  ? 647  GLN   D CG  1 
ATOM   12995 C  CD  . GLN   D  1 346 ? 1.090   -70.177 -44.786  1.00 38.76  ? 647  GLN   D CD  1 
ATOM   12996 O  OE1 . GLN   D  1 346 ? 0.906   -71.287 -45.277  1.00 42.73  ? 647  GLN   D OE1 1 
ATOM   12997 N  NE2 . GLN   D  1 346 ? 0.828   -69.054 -45.438  1.00 42.54  ? 647  GLN   D NE2 1 
ATOM   12998 N  N   . SER   D  1 347 ? 2.572   -73.669 -40.674  1.00 33.95  ? 648  SER   D N   1 
ATOM   12999 C  CA  . SER   D  1 347 ? 2.274   -74.864 -39.904  1.00 33.78  ? 648  SER   D CA  1 
ATOM   13000 C  C   . SER   D  1 347 ? 2.634   -74.662 -38.445  1.00 35.32  ? 648  SER   D C   1 
ATOM   13001 O  O   . SER   D  1 347 ? 1.976   -75.216 -37.560  1.00 36.47  ? 648  SER   D O   1 
ATOM   13002 C  CB  . SER   D  1 347 ? 3.019   -76.063 -40.485  1.00 34.58  ? 648  SER   D CB  1 
ATOM   13003 O  OG  . SER   D  1 347 ? 2.518   -76.391 -41.776  1.00 37.18  ? 648  SER   D OG  1 
ATOM   13004 N  N   . ASP   D  1 348 ? 3.658   -73.856 -38.180  1.00 33.37  ? 649  ASP   D N   1 
ATOM   13005 C  CA  . ASP   D  1 348 ? 4.071   -73.544 -36.824  1.00 30.30  ? 649  ASP   D CA  1 
ATOM   13006 C  C   . ASP   D  1 348 ? 3.373   -72.317 -36.270  1.00 34.23  ? 649  ASP   D C   1 
ATOM   13007 O  O   . ASP   D  1 348 ? 3.725   -71.861 -35.173  1.00 36.31  ? 649  ASP   D O   1 
ATOM   13008 C  CB  . ASP   D  1 348 ? 5.582   -73.356 -36.775  1.00 35.60  ? 649  ASP   D CB  1 
ATOM   13009 C  CG  . ASP   D  1 348 ? 6.311   -74.666 -36.784  1.00 38.11  ? 649  ASP   D CG  1 
ATOM   13010 O  OD1 . ASP   D  1 348 ? 5.620   -75.696 -36.898  1.00 37.74  ? 649  ASP   D OD1 1 
ATOM   13011 O  OD2 . ASP   D  1 348 ? 7.554   -74.674 -36.653  1.00 39.83  ? 649  ASP   D OD2 1 
ATOM   13012 N  N   . LYS   D  1 349 ? 2.387   -71.778 -36.990  1.00 29.30  ? 650  LYS   D N   1 
ATOM   13013 C  CA  . LYS   D  1 349 ? 1.662   -70.602 -36.520  1.00 33.37  ? 650  LYS   D CA  1 
ATOM   13014 C  C   . LYS   D  1 349 ? 2.633   -69.468 -36.211  1.00 28.40  ? 650  LYS   D C   1 
ATOM   13015 O  O   . LYS   D  1 349 ? 2.555   -68.815 -35.170  1.00 29.33  ? 650  LYS   D O   1 
ATOM   13016 C  CB  . LYS   D  1 349 ? 0.814   -70.933 -35.289  1.00 37.82  ? 650  LYS   D CB  1 
ATOM   13017 C  CG  . LYS   D  1 349 ? -0.265  -71.981 -35.523  1.00 51.52  ? 650  LYS   D CG  1 
ATOM   13018 C  CD  . LYS   D  1 349 ? -1.096  -72.185 -34.258  1.00 62.88  ? 650  LYS   D CD  1 
ATOM   13019 C  CE  . LYS   D  1 349 ? -2.370  -72.963 -34.536  1.00 73.34  ? 650  LYS   D CE  1 
ATOM   13020 N  NZ  . LYS   D  1 349 ? -2.298  -73.664 -35.844  1.00 75.20  ? 650  LYS   D NZ  1 
ATOM   13021 N  N   . VAL   D  1 350 ? 3.585   -69.252 -37.106  1.00 25.85  ? 651  VAL   D N   1 
ATOM   13022 C  CA  . VAL   D  1 350 ? 4.501   -68.127 -37.000  1.00 24.97  ? 651  VAL   D CA  1 
ATOM   13023 C  C   . VAL   D  1 350 ? 4.174   -67.154 -38.125  1.00 33.80  ? 651  VAL   D C   1 
ATOM   13024 O  O   . VAL   D  1 350 ? 4.099   -67.545 -39.299  1.00 28.74  ? 651  VAL   D O   1 
ATOM   13025 C  CB  . VAL   D  1 350 ? 5.965   -68.590 -37.048  1.00 23.72  ? 651  VAL   D CB  1 
ATOM   13026 C  CG1 . VAL   D  1 350 ? 6.890   -67.382 -37.015  1.00 21.81  ? 651  VAL   D CG1 1 
ATOM   13027 C  CG2 . VAL   D  1 350 ? 6.252   -69.533 -35.873  1.00 26.25  ? 651  VAL   D CG2 1 
ATOM   13028 N  N   . THR   D  1 351 ? 3.952   -65.897 -37.762  1.00 26.98  ? 652  THR   D N   1 
ATOM   13029 C  CA  . THR   D  1 351 ? 3.551   -64.908 -38.744  1.00 25.84  ? 652  THR   D CA  1 
ATOM   13030 C  C   . THR   D  1 351 ? 4.542   -64.860 -39.891  1.00 28.81  ? 652  THR   D C   1 
ATOM   13031 O  O   . THR   D  1 351 ? 5.759   -64.795 -39.681  1.00 25.56  ? 652  THR   D O   1 
ATOM   13032 C  CB  . THR   D  1 351 ? 3.436   -63.537 -38.101  1.00 26.61  ? 652  THR   D CB  1 
ATOM   13033 O  OG1 . THR   D  1 351 ? 2.584   -63.644 -36.963  1.00 28.45  ? 652  THR   D OG1 1 
ATOM   13034 C  CG2 . THR   D  1 351 ? 2.850   -62.525 -39.118  1.00 22.51  ? 652  THR   D CG2 1 
ATOM   13035 N  N   . ILE   D  1 352 ? 4.005   -64.944 -41.105  1.00 27.80  ? 653  ILE   D N   1 
ATOM   13036 C  CA  . ILE   D  1 352 ? 4.787   -64.765 -42.318  1.00 24.98  ? 653  ILE   D CA  1 
ATOM   13037 C  C   . ILE   D  1 352 ? 3.798   -64.333 -43.379  1.00 23.26  ? 653  ILE   D C   1 
ATOM   13038 O  O   . ILE   D  1 352 ? 2.601   -64.611 -43.284  1.00 24.95  ? 653  ILE   D O   1 
ATOM   13039 C  CB  . ILE   D  1 352 ? 5.522   -66.072 -42.715  1.00 19.75  ? 653  ILE   D CB  1 
ATOM   13040 C  CG1 . ILE   D  1 352 ? 6.622   -65.806 -43.744  1.00 23.53  ? 653  ILE   D CG1 1 
ATOM   13041 C  CG2 . ILE   D  1 352 ? 4.529   -67.095 -43.227  1.00 21.87  ? 653  ILE   D CG2 1 
ATOM   13042 C  CD1 . ILE   D  1 352 ? 7.623   -66.950 -43.825  1.00 25.25  ? 653  ILE   D CD1 1 
ATOM   13043 N  N   . VAL   D  1 353 ? 4.284   -63.649 -44.395  1.00 23.33  ? 654  VAL   D N   1 
ATOM   13044 C  CA  . VAL   D  1 353 ? 3.415   -63.219 -45.475  1.00 27.60  ? 654  VAL   D CA  1 
ATOM   13045 C  C   . VAL   D  1 353 ? 4.079   -63.606 -46.787  1.00 27.95  ? 654  VAL   D C   1 
ATOM   13046 O  O   . VAL   D  1 353 ? 5.301   -63.493 -46.931  1.00 32.85  ? 654  VAL   D O   1 
ATOM   13047 C  CB  . VAL   D  1 353 ? 3.100   -61.707 -45.388  1.00 25.42  ? 654  VAL   D CB  1 
ATOM   13048 C  CG1 . VAL   D  1 353 ? 4.360   -60.872 -45.559  1.00 20.56  ? 654  VAL   D CG1 1 
ATOM   13049 C  CG2 . VAL   D  1 353 ? 2.028   -61.314 -46.398  1.00 33.63  ? 654  VAL   D CG2 1 
ATOM   13050 N  N   . ASP   D  1 354 ? 3.291   -64.147 -47.705  1.00 26.83  ? 655  ASP   D N   1 
ATOM   13051 C  CA  . ASP   D  1 354 ? 3.849   -64.444 -49.015  1.00 27.11  ? 655  ASP   D CA  1 
ATOM   13052 C  C   . ASP   D  1 354 ? 3.925   -63.162 -49.836  1.00 30.83  ? 655  ASP   D C   1 
ATOM   13053 O  O   . ASP   D  1 354 ? 3.259   -62.166 -49.547  1.00 25.68  ? 655  ASP   D O   1 
ATOM   13054 C  CB  . ASP   D  1 354 ? 3.033   -65.512 -49.759  1.00 28.45  ? 655  ASP   D CB  1 
ATOM   13055 C  CG  . ASP   D  1 354 ? 1.617   -65.066 -50.088  1.00 37.18  ? 655  ASP   D CG  1 
ATOM   13056 O  OD1 . ASP   D  1 354 ? 0.667   -65.611 -49.491  1.00 50.65  ? 655  ASP   D OD1 1 
ATOM   13057 O  OD2 . ASP   D  1 354 ? 1.440   -64.173 -50.935  1.00 39.63  ? 655  ASP   D OD2 1 
ATOM   13058 N  N   . HIS   D  1 355 ? 4.763   -63.198 -50.870  1.00 27.88  ? 656  HIS   D N   1 
ATOM   13059 C  CA  . HIS   D  1 355 ? 5.005   -62.009 -51.669  1.00 27.53  ? 656  HIS   D CA  1 
ATOM   13060 C  C   . HIS   D  1 355 ? 3.773   -61.586 -52.458  1.00 29.72  ? 656  HIS   D C   1 
ATOM   13061 O  O   . HIS   D  1 355 ? 3.639   -60.400 -52.774  1.00 28.83  ? 656  HIS   D O   1 
ATOM   13062 C  CB  . HIS   D  1 355 ? 6.186   -62.255 -52.602  1.00 28.12  ? 656  HIS   D CB  1 
ATOM   13063 C  CG  . HIS   D  1 355 ? 6.071   -63.523 -53.392  1.00 26.67  ? 656  HIS   D CG  1 
ATOM   13064 N  ND1 . HIS   D  1 355 ? 6.240   -64.770 -52.830  1.00 26.97  ? 656  HIS   D ND1 1 
ATOM   13065 C  CD2 . HIS   D  1 355 ? 5.817   -63.733 -54.708  1.00 24.53  ? 656  HIS   D CD2 1 
ATOM   13066 C  CE1 . HIS   D  1 355 ? 6.087   -65.696 -53.763  1.00 30.96  ? 656  HIS   D CE1 1 
ATOM   13067 N  NE2 . HIS   D  1 355 ? 5.827   -65.094 -54.911  1.00 28.89  ? 656  HIS   D NE2 1 
ATOM   13068 N  N   . HIS   D  1 356 ? 2.859   -62.517 -52.758  1.00 21.11  ? 657  HIS   D N   1 
ATOM   13069 C  CA  . HIS   D  1 356 ? 1.613   -62.123 -53.410  1.00 21.80  ? 657  HIS   D CA  1 
ATOM   13070 C  C   . HIS   D  1 356 ? 0.756   -61.268 -52.484  1.00 26.54  ? 657  HIS   D C   1 
ATOM   13071 O  O   . HIS   D  1 356 ? 0.304   -60.177 -52.857  1.00 29.04  ? 657  HIS   D O   1 
ATOM   13072 C  CB  . HIS   D  1 356 ? 0.858   -63.365 -53.862  1.00 23.90  ? 657  HIS   D CB  1 
ATOM   13073 C  CG  . HIS   D  1 356 ? 1.648   -64.206 -54.806  1.00 31.94  ? 657  HIS   D CG  1 
ATOM   13074 N  ND1 . HIS   D  1 356 ? 1.959   -63.786 -56.080  1.00 28.31  ? 657  HIS   D ND1 1 
ATOM   13075 C  CD2 . HIS   D  1 356 ? 2.239   -65.414 -54.648  1.00 31.14  ? 657  HIS   D CD2 1 
ATOM   13076 C  CE1 . HIS   D  1 356 ? 2.687   -64.711 -56.677  1.00 33.03  ? 657  HIS   D CE1 1 
ATOM   13077 N  NE2 . HIS   D  1 356 ? 2.865   -65.712 -55.832  1.00 29.65  ? 657  HIS   D NE2 1 
ATOM   13078 N  N   . SER   D  1 357 ? 0.526   -61.748 -51.268  1.00 25.82  ? 658  SER   D N   1 
ATOM   13079 C  CA  . SER   D  1 357 ? -0.272  -60.989 -50.316  1.00 27.02  ? 658  SER   D CA  1 
ATOM   13080 C  C   . SER   D  1 357 ? 0.430   -59.689 -49.909  1.00 22.78  ? 658  SER   D C   1 
ATOM   13081 O  O   . SER   D  1 357 ? -0.206  -58.635 -49.789  1.00 24.51  ? 658  SER   D O   1 
ATOM   13082 C  CB  . SER   D  1 357 ? -0.559  -61.872 -49.097  1.00 29.19  ? 658  SER   D CB  1 
ATOM   13083 O  OG  . SER   D  1 357 ? -1.190  -61.122 -48.085  1.00 43.93  ? 658  SER   D OG  1 
ATOM   13084 N  N   . ALA   D  1 358 ? 1.739   -59.747 -49.688  1.00 20.60  ? 659  ALA   D N   1 
ATOM   13085 C  CA  . ALA   D  1 358 ? 2.476   -58.558 -49.264  1.00 20.91  ? 659  ALA   D CA  1 
ATOM   13086 C  C   . ALA   D  1 358 ? 2.404   -57.464 -50.321  1.00 28.14  ? 659  ALA   D C   1 
ATOM   13087 O  O   . ALA   D  1 358 ? 2.129   -56.295 -50.018  1.00 22.51  ? 659  ALA   D O   1 
ATOM   13088 C  CB  . ALA   D  1 358 ? 3.934   -58.930 -48.983  1.00 20.63  ? 659  ALA   D CB  1 
ATOM   13089 N  N   . THR   D  1 359 ? 2.644   -57.827 -51.582  1.00 24.02  ? 660  THR   D N   1 
ATOM   13090 C  CA  . THR   D  1 359 ? 2.624   -56.817 -52.627  1.00 21.14  ? 660  THR   D CA  1 
ATOM   13091 C  C   . THR   D  1 359 ? 1.219   -56.287 -52.846  1.00 22.31  ? 660  THR   D C   1 
ATOM   13092 O  O   . THR   D  1 359 ? 1.036   -55.081 -53.044  1.00 23.90  ? 660  THR   D O   1 
ATOM   13093 C  CB  . THR   D  1 359 ? 3.217   -57.378 -53.921  1.00 18.78  ? 660  THR   D CB  1 
ATOM   13094 O  OG1 . THR   D  1 359 ? 2.593   -58.627 -54.248  1.00 24.22  ? 660  THR   D OG1 1 
ATOM   13095 C  CG2 . THR   D  1 359 ? 4.710   -57.595 -53.738  1.00 19.56  ? 660  THR   D CG2 1 
ATOM   13096 N  N   . GLU   D  1 360 ? 0.209   -57.155 -52.790  1.00 19.02  ? 661  GLU   D N   1 
ATOM   13097 C  CA  . GLU   D  1 360 ? -1.158  -56.652 -52.887  1.00 23.45  ? 661  GLU   D CA  1 
ATOM   13098 C  C   . GLU   D  1 360 ? -1.441  -55.639 -51.780  1.00 31.21  ? 661  GLU   D C   1 
ATOM   13099 O  O   . GLU   D  1 360 ? -1.952  -54.543 -52.041  1.00 29.60  ? 661  GLU   D O   1 
ATOM   13100 C  CB  . GLU   D  1 360 ? -2.161  -57.806 -52.830  1.00 30.54  ? 661  GLU   D CB  1 
ATOM   13101 C  CG  . GLU   D  1 360 ? -3.595  -57.319 -52.842  1.00 36.41  ? 661  GLU   D CG  1 
ATOM   13102 C  CD  . GLU   D  1 360 ? -4.614  -58.437 -52.693  1.00 59.58  ? 661  GLU   D CD  1 
ATOM   13103 O  OE1 . GLU   D  1 360 ? -4.245  -59.536 -52.223  1.00 63.68  ? 661  GLU   D OE1 1 
ATOM   13104 O  OE2 . GLU   D  1 360 ? -5.793  -58.212 -53.050  1.00 72.10  ? 661  GLU   D OE2 1 
ATOM   13105 N  N   . SER   D  1 361 ? -1.087  -55.982 -50.535  1.00 26.47  ? 662  SER   D N   1 
ATOM   13106 C  CA  A SER   D  1 361 ? -1.293  -55.047 -49.434  0.44 29.78  ? 662  SER   D CA  1 
ATOM   13107 C  CA  B SER   D  1 361 ? -1.294  -55.049 -49.431  0.56 29.99  ? 662  SER   D CA  1 
ATOM   13108 C  C   . SER   D  1 361 ? -0.567  -53.734 -49.685  1.00 26.94  ? 662  SER   D C   1 
ATOM   13109 O  O   . SER   D  1 361 ? -1.080  -52.662 -49.354  1.00 26.72  ? 662  SER   D O   1 
ATOM   13110 C  CB  A SER   D  1 361 ? -0.838  -55.674 -48.113  0.44 30.04  ? 662  SER   D CB  1 
ATOM   13111 C  CB  B SER   D  1 361 ? -0.851  -55.678 -48.095  0.56 30.07  ? 662  SER   D CB  1 
ATOM   13112 O  OG  A SER   D  1 361 ? -1.608  -56.824 -47.816  0.44 30.47  ? 662  SER   D OG  1 
ATOM   13113 O  OG  B SER   D  1 361 ? 0.562   -55.692 -47.920  0.56 25.96  ? 662  SER   D OG  1 
ATOM   13114 N  N   . PHE   D  1 362 ? 0.618   -53.791 -50.293  1.00 28.67  ? 663  PHE   D N   1 
ATOM   13115 C  CA  . PHE   D  1 362 ? 1.360   -52.551 -50.496  1.00 28.98  ? 663  PHE   D CA  1 
ATOM   13116 C  C   . PHE   D  1 362 ? 0.691   -51.656 -51.530  1.00 32.02  ? 663  PHE   D C   1 
ATOM   13117 O  O   . PHE   D  1 362 ? 0.703   -50.426 -51.383  1.00 28.32  ? 663  PHE   D O   1 
ATOM   13118 C  CB  . PHE   D  1 362 ? 2.809   -52.826 -50.899  1.00 19.50  ? 663  PHE   D CB  1 
ATOM   13119 C  CG  . PHE   D  1 362 ? 3.606   -51.570 -51.066  1.00 24.16  ? 663  PHE   D CG  1 
ATOM   13120 C  CD1 . PHE   D  1 362 ? 4.012   -50.842 -49.947  1.00 24.61  ? 663  PHE   D CD1 1 
ATOM   13121 C  CD2 . PHE   D  1 362 ? 3.872   -51.062 -52.326  1.00 24.93  ? 663  PHE   D CD2 1 
ATOM   13122 C  CE1 . PHE   D  1 362 ? 4.713   -49.652 -50.085  1.00 28.80  ? 663  PHE   D CE1 1 
ATOM   13123 C  CE2 . PHE   D  1 362 ? 4.576   -49.879 -52.476  1.00 29.87  ? 663  PHE   D CE2 1 
ATOM   13124 C  CZ  . PHE   D  1 362 ? 5.001   -49.171 -51.353  1.00 30.94  ? 663  PHE   D CZ  1 
ATOM   13125 N  N   . ILE   D  1 363 ? 0.123   -52.247 -52.590  1.00 25.73  ? 664  ILE   D N   1 
ATOM   13126 C  CA  . ILE   D  1 363 ? -0.655  -51.465 -53.545  1.00 26.05  ? 664  ILE   D CA  1 
ATOM   13127 C  C   . ILE   D  1 363 ? -1.792  -50.754 -52.829  1.00 27.60  ? 664  ILE   D C   1 
ATOM   13128 O  O   . ILE   D  1 363 ? -2.056  -49.569 -53.059  1.00 25.26  ? 664  ILE   D O   1 
ATOM   13129 C  CB  . ILE   D  1 363 ? -1.194  -52.361 -54.681  1.00 27.02  ? 664  ILE   D CB  1 
ATOM   13130 C  CG1 . ILE   D  1 363 ? -0.050  -52.901 -55.521  1.00 23.86  ? 664  ILE   D CG1 1 
ATOM   13131 C  CG2 . ILE   D  1 363 ? -2.136  -51.570 -55.553  1.00 22.54  ? 664  ILE   D CG2 1 
ATOM   13132 C  CD1 . ILE   D  1 363 ? 0.803   -51.798 -56.139  1.00 28.57  ? 664  ILE   D CD1 1 
ATOM   13133 N  N   . LYS   D  1 364 ? -2.492  -51.479 -51.963  1.00 26.87  ? 665  LYS   D N   1 
ATOM   13134 C  CA  . LYS   D  1 364 ? -3.544  -50.863 -51.165  1.00 32.26  ? 665  LYS   D CA  1 
ATOM   13135 C  C   . LYS   D  1 364 ? -2.975  -49.753 -50.287  1.00 28.88  ? 665  LYS   D C   1 
ATOM   13136 O  O   . LYS   D  1 364 ? -3.554  -48.665 -50.181  1.00 23.01  ? 665  LYS   D O   1 
ATOM   13137 C  CB  . LYS   D  1 364 ? -4.236  -51.936 -50.327  1.00 29.45  ? 665  LYS   D CB  1 
ATOM   13138 C  CG  . LYS   D  1 364 ? -5.422  -51.433 -49.528  1.00 48.87  ? 665  LYS   D CG  1 
ATOM   13139 C  CD  . LYS   D  1 364 ? -6.389  -50.668 -50.419  1.00 64.62  ? 665  LYS   D CD  1 
ATOM   13140 C  CE  . LYS   D  1 364 ? -7.481  -49.968 -49.620  1.00 72.28  ? 665  LYS   D CE  1 
ATOM   13141 N  NZ  . LYS   D  1 364 ? -8.351  -49.149 -50.514  1.00 81.90  ? 665  LYS   D NZ  1 
ATOM   13142 N  N   . HIS   D  1 365 ? -1.817  -50.000 -49.681  1.00 23.50  ? 666  HIS   D N   1 
ATOM   13143 C  CA  . HIS   D  1 365 ? -1.180  -48.969 -48.881  1.00 23.42  ? 666  HIS   D CA  1 
ATOM   13144 C  C   . HIS   D  1 365 ? -0.880  -47.740 -49.724  1.00 30.60  ? 666  HIS   D C   1 
ATOM   13145 O  O   . HIS   D  1 365 ? -1.155  -46.608 -49.303  1.00 25.95  ? 666  HIS   D O   1 
ATOM   13146 C  CB  . HIS   D  1 365 ? 0.098   -49.505 -48.246  1.00 22.88  ? 666  HIS   D CB  1 
ATOM   13147 C  CG  . HIS   D  1 365 ? 0.833   -48.471 -47.470  1.00 23.11  ? 666  HIS   D CG  1 
ATOM   13148 N  ND1 . HIS   D  1 365 ? 0.273   -47.826 -46.390  1.00 21.17  ? 666  HIS   D ND1 1 
ATOM   13149 C  CD2 . HIS   D  1 365 ? 2.062   -47.932 -47.638  1.00 21.34  ? 666  HIS   D CD2 1 
ATOM   13150 C  CE1 . HIS   D  1 365 ? 1.135   -46.948 -45.909  1.00 27.02  ? 666  HIS   D CE1 1 
ATOM   13151 N  NE2 . HIS   D  1 365 ? 2.232   -46.997 -46.643  1.00 24.03  ? 666  HIS   D NE2 1 
ATOM   13152 N  N   . MET   D  1 366 ? -0.344  -47.943 -50.938  1.00 28.46  ? 667  MET   D N   1 
ATOM   13153 C  CA  . MET   D  1 366 ? -0.086  -46.814 -51.830  1.00 24.66  ? 667  MET   D CA  1 
ATOM   13154 C  C   . MET   D  1 366 ? -1.352  -46.013 -52.080  1.00 20.87  ? 667  MET   D C   1 
ATOM   13155 O  O   . MET   D  1 366 ? -1.349  -44.786 -51.951  1.00 24.19  ? 667  MET   D O   1 
ATOM   13156 C  CB  . MET   D  1 366 ? 0.498   -47.289 -53.164  1.00 28.29  ? 667  MET   D CB  1 
ATOM   13157 C  CG  . MET   D  1 366 ? 2.005   -47.400 -53.167  1.00 29.01  ? 667  MET   D CG  1 
ATOM   13158 S  SD  . MET   D  1 366 ? 2.641   -47.719 -54.838  1.00 37.64  ? 667  MET   D SD  1 
ATOM   13159 C  CE  . MET   D  1 366 ? 2.454   -46.129 -55.627  1.00 35.74  ? 667  MET   D CE  1 
ATOM   13160 N  N   . GLU   D  1 367 ? -2.445  -46.686 -52.458  1.00 22.31  ? 668  GLU   D N   1 
ATOM   13161 C  CA  A GLU   D  1 367 ? -3.705  -45.986 -52.678  0.50 29.68  ? 668  GLU   D CA  1 
ATOM   13162 C  CA  B GLU   D  1 367 ? -3.685  -45.950 -52.691  0.50 29.69  ? 668  GLU   D CA  1 
ATOM   13163 C  C   . GLU   D  1 367 ? -4.081  -45.157 -51.455  1.00 28.41  ? 668  GLU   D C   1 
ATOM   13164 O  O   . GLU   D  1 367 ? -4.453  -43.981 -51.565  1.00 31.61  ? 668  GLU   D O   1 
ATOM   13165 C  CB  A GLU   D  1 367 ? -4.803  -47.002 -53.014  0.50 32.83  ? 668  GLU   D CB  1 
ATOM   13166 C  CB  B GLU   D  1 367 ? -4.843  -46.864 -53.101  0.50 32.96  ? 668  GLU   D CB  1 
ATOM   13167 C  CG  A GLU   D  1 367 ? -6.221  -46.439 -53.099  0.50 36.16  ? 668  GLU   D CG  1 
ATOM   13168 C  CG  B GLU   D  1 367 ? -4.501  -48.232 -53.610  0.50 37.93  ? 668  GLU   D CG  1 
ATOM   13169 C  CD  A GLU   D  1 367 ? -7.297  -47.525 -53.035  0.50 43.82  ? 668  GLU   D CD  1 
ATOM   13170 C  CD  B GLU   D  1 367 ? -4.486  -48.346 -55.120  0.50 37.57  ? 668  GLU   D CD  1 
ATOM   13171 O  OE1 A GLU   D  1 367 ? -6.976  -48.718 -53.231  0.50 43.92  ? 668  GLU   D OE1 1 
ATOM   13172 O  OE1 B GLU   D  1 367 ? -3.524  -47.858 -55.749  0.50 38.06  ? 668  GLU   D OE1 1 
ATOM   13173 O  OE2 A GLU   D  1 367 ? -8.470  -47.182 -52.773  0.50 46.95  ? 668  GLU   D OE2 1 
ATOM   13174 O  OE2 B GLU   D  1 367 ? -5.429  -48.951 -55.671  0.50 36.77  ? 668  GLU   D OE2 1 
ATOM   13175 N  N   . ASN   D  1 368 ? -4.005  -45.776 -50.269  1.00 28.04  ? 669  ASN   D N   1 
ATOM   13176 C  CA  . ASN   D  1 368 ? -4.367  -45.074 -49.038  1.00 26.99  ? 669  ASN   D CA  1 
ATOM   13177 C  C   . ASN   D  1 368 ? -3.510  -43.838 -48.856  1.00 27.64  ? 669  ASN   D C   1 
ATOM   13178 O  O   . ASN   D  1 368 ? -4.008  -42.755 -48.526  1.00 28.89  ? 669  ASN   D O   1 
ATOM   13179 C  CB  . ASN   D  1 368 ? -4.192  -45.981 -47.822  1.00 30.16  ? 669  ASN   D CB  1 
ATOM   13180 C  CG  . ASN   D  1 368 ? -5.132  -47.154 -47.813  1.00 34.80  ? 669  ASN   D CG  1 
ATOM   13181 O  OD1 . ASN   D  1 368 ? -6.212  -47.113 -48.398  1.00 34.90  ? 669  ASN   D OD1 1 
ATOM   13182 N  ND2 . ASN   D  1 368 ? -4.723  -48.220 -47.124  1.00 34.45  ? 669  ASN   D ND2 1 
ATOM   13183 N  N   . GLU   D  1 369 ? -2.207  -43.990 -49.058  1.00 22.62  ? 670  GLU   D N   1 
ATOM   13184 C  CA  . GLU   D  1 369 ? -1.301  -42.881 -48.820  1.00 21.43  ? 670  GLU   D CA  1 
ATOM   13185 C  C   . GLU   D  1 369 ? -1.540  -41.755 -49.813  1.00 24.49  ? 670  GLU   D C   1 
ATOM   13186 O  O   . GLU   D  1 369 ? -1.554  -40.584 -49.425  1.00 32.71  ? 670  GLU   D O   1 
ATOM   13187 C  CB  . GLU   D  1 369 ? 0.143   -43.377 -48.873  1.00 19.95  ? 670  GLU   D CB  1 
ATOM   13188 C  CG  . GLU   D  1 369 ? 0.484   -44.288 -47.699  1.00 26.87  ? 670  GLU   D CG  1 
ATOM   13189 C  CD  . GLU   D  1 369 ? 0.616   -43.532 -46.371  1.00 30.40  ? 670  GLU   D CD  1 
ATOM   13190 O  OE1 . GLU   D  1 369 ? 1.757   -43.276 -45.935  1.00 24.96  ? 670  GLU   D OE1 1 
ATOM   13191 O  OE2 . GLU   D  1 369 ? -0.414  -43.190 -45.768  1.00 26.71  ? 670  GLU   D OE2 1 
ATOM   13192 N  N   . TYR   D  1 370 ? -1.754  -42.079 -51.097  1.00 26.97  ? 671  TYR   D N   1 
ATOM   13193 C  CA  . TYR   D  1 370 ? -2.034  -41.008 -52.046  1.00 22.76  ? 671  TYR   D CA  1 
ATOM   13194 C  C   . TYR   D  1 370 ? -3.348  -40.326 -51.708  1.00 28.30  ? 671  TYR   D C   1 
ATOM   13195 O  O   . TYR   D  1 370 ? -3.469  -39.101 -51.824  1.00 31.11  ? 671  TYR   D O   1 
ATOM   13196 C  CB  . TYR   D  1 370 ? -2.044  -41.544 -53.489  1.00 22.70  ? 671  TYR   D CB  1 
ATOM   13197 C  CG  . TYR   D  1 370 ? -0.650  -41.582 -54.072  1.00 28.99  ? 671  TYR   D CG  1 
ATOM   13198 C  CD1 . TYR   D  1 370 ? 0.192   -42.659 -53.828  1.00 22.11  ? 671  TYR   D CD1 1 
ATOM   13199 C  CD2 . TYR   D  1 370 ? -0.169  -40.525 -54.851  1.00 31.51  ? 671  TYR   D CD2 1 
ATOM   13200 C  CE1 . TYR   D  1 370 ? 1.490   -42.700 -54.349  1.00 23.34  ? 671  TYR   D CE1 1 
ATOM   13201 C  CE2 . TYR   D  1 370 ? 1.111   -40.547 -55.366  1.00 30.09  ? 671  TYR   D CE2 1 
ATOM   13202 C  CZ  . TYR   D  1 370 ? 1.939   -41.631 -55.111  1.00 30.78  ? 671  TYR   D CZ  1 
ATOM   13203 O  OH  . TYR   D  1 370 ? 3.212   -41.651 -55.634  1.00 36.80  ? 671  TYR   D OH  1 
ATOM   13204 N  N   . ARG   D  1 371 ? -4.338  -41.099 -51.265  1.00 29.79  ? 672  ARG   D N   1 
ATOM   13205 C  CA  . ARG   D  1 371 ? -5.625  -40.495 -50.927  1.00 35.85  ? 672  ARG   D CA  1 
ATOM   13206 C  C   . ARG   D  1 371 ? -5.503  -39.571 -49.717  1.00 36.77  ? 672  ARG   D C   1 
ATOM   13207 O  O   . ARG   D  1 371 ? -5.990  -38.437 -49.743  1.00 33.02  ? 672  ARG   D O   1 
ATOM   13208 C  CB  . ARG   D  1 371 ? -6.680  -41.574 -50.674  1.00 36.97  ? 672  ARG   D CB  1 
ATOM   13209 C  CG  . ARG   D  1 371 ? -8.072  -41.011 -50.435  1.00 54.75  ? 672  ARG   D CG  1 
ATOM   13210 C  CD  . ARG   D  1 371 ? -9.040  -42.071 -49.915  1.00 73.05  ? 672  ARG   D CD  1 
ATOM   13211 N  NE  . ARG   D  1 371 ? -8.833  -43.368 -50.562  1.00 85.04  ? 672  ARG   D NE  1 
ATOM   13212 C  CZ  . ARG   D  1 371 ? -8.481  -44.486 -49.925  1.00 85.55  ? 672  ARG   D CZ  1 
ATOM   13213 N  NH1 . ARG   D  1 371 ? -8.305  -44.487 -48.603  1.00 76.92  ? 672  ARG   D NH1 1 
ATOM   13214 N  NH2 . ARG   D  1 371 ? -8.316  -45.611 -50.615  1.00 83.50  ? 672  ARG   D NH2 1 
ATOM   13215 N  N   . CYS   D  1 372 ? -4.853  -40.023 -48.643  1.00 30.47  ? 673  CYS   D N   1 
ATOM   13216 C  CA  . CYS   D  1 372 ? -4.842  -39.179 -47.450  1.00 33.42  ? 673  CYS   D CA  1 
ATOM   13217 C  C   . CYS   D  1 372 ? -3.615  -38.281 -47.354  1.00 34.76  ? 673  CYS   D C   1 
ATOM   13218 O  O   . CYS   D  1 372 ? -3.716  -37.187 -46.799  1.00 43.93  ? 673  CYS   D O   1 
ATOM   13219 C  CB  . CYS   D  1 372 ? -4.957  -40.026 -46.175  1.00 36.35  ? 673  CYS   D CB  1 
ATOM   13220 S  SG  . CYS   D  1 372 ? -3.494  -40.989 -45.822  1.00 53.13  ? 673  CYS   D SG  1 
ATOM   13221 N  N   . ARG   D  1 373 ? -2.471  -38.687 -47.904  1.00 27.44  ? 674  ARG   D N   1 
ATOM   13222 C  CA  . ARG   D  1 373 ? -1.226  -37.952 -47.710  1.00 31.14  ? 674  ARG   D CA  1 
ATOM   13223 C  C   . ARG   D  1 373 ? -0.710  -37.285 -48.976  1.00 34.99  ? 674  ARG   D C   1 
ATOM   13224 O  O   . ARG   D  1 373 ? 0.212   -36.468 -48.893  1.00 32.44  ? 674  ARG   D O   1 
ATOM   13225 C  CB  . ARG   D  1 373 ? -0.147  -38.902 -47.167  1.00 35.09  ? 674  ARG   D CB  1 
ATOM   13226 C  CG  . ARG   D  1 373 ? 0.909   -38.273 -46.288  1.00 31.73  ? 674  ARG   D CG  1 
ATOM   13227 C  CD  . ARG   D  1 373 ? 1.992   -39.303 -45.967  1.00 27.66  ? 674  ARG   D CD  1 
ATOM   13228 N  NE  . ARG   D  1 373 ? 3.035   -38.699 -45.160  1.00 30.16  ? 674  ARG   D NE  1 
ATOM   13229 C  CZ  . ARG   D  1 373 ? 4.215   -39.255 -44.933  1.00 34.42  ? 674  ARG   D CZ  1 
ATOM   13230 N  NH1 . ARG   D  1 373 ? 4.504   -40.429 -45.461  1.00 26.74  ? 674  ARG   D NH1 1 
ATOM   13231 N  NH2 . ARG   D  1 373 ? 5.106   -38.628 -44.182  1.00 37.40  ? 674  ARG   D NH2 1 
ATOM   13232 N  N   . GLY   D  1 374 ? -1.251  -37.626 -50.142  1.00 34.65  ? 675  GLY   D N   1 
ATOM   13233 C  CA  . GLY   D  1 374 ? -0.755  -37.059 -51.374  1.00 29.35  ? 675  GLY   D CA  1 
ATOM   13234 C  C   . GLY   D  1 374 ? 0.493   -37.708 -51.918  1.00 28.18  ? 675  GLY   D C   1 
ATOM   13235 O  O   . GLY   D  1 374 ? 1.131   -37.139 -52.814  1.00 29.64  ? 675  GLY   D O   1 
ATOM   13236 N  N   . GLY   D  1 375 ? 0.873   -38.869 -51.409  1.00 23.89  ? 676  GLY   D N   1 
ATOM   13237 C  CA  . GLY   D  1 375 ? 2.015   -39.558 -51.961  1.00 21.59  ? 676  GLY   D CA  1 
ATOM   13238 C  C   . GLY   D  1 375 ? 2.470   -40.674 -51.057  1.00 32.15  ? 676  GLY   D C   1 
ATOM   13239 O  O   . GLY   D  1 375 ? 2.049   -40.805 -49.906  1.00 31.48  ? 676  GLY   D O   1 
ATOM   13240 N  N   . CYS   D  1 376 ? 3.341   -41.481 -51.614  1.00 30.45  ? 677  CYS   D N   1 
ATOM   13241 C  CA  . CYS   D  1 376 ? 3.946   -42.587 -50.880  1.00 29.69  ? 677  CYS   D CA  1 
ATOM   13242 C  C   . CYS   D  1 376 ? 5.276   -42.861 -51.557  1.00 32.43  ? 677  CYS   D C   1 
ATOM   13243 O  O   . CYS   D  1 376 ? 5.313   -43.419 -52.665  1.00 27.26  ? 677  CYS   D O   1 
ATOM   13244 C  CB  . CYS   D  1 376 ? 3.054   -43.825 -50.881  1.00 26.14  ? 677  CYS   D CB  1 
ATOM   13245 S  SG  . CYS   D  1 376 ? 3.780   -45.208 -50.000  1.00 27.04  ? 677  CYS   D SG  1 
ATOM   13246 N  N   . PRO   D  1 377 ? 6.384   -42.419 -50.966  1.00 23.58  ? 678  PRO   D N   1 
ATOM   13247 C  CA  . PRO   D  1 377 ? 7.695   -42.725 -51.544  1.00 22.33  ? 678  PRO   D CA  1 
ATOM   13248 C  C   . PRO   D  1 377 ? 7.898   -44.230 -51.581  1.00 26.21  ? 678  PRO   D C   1 
ATOM   13249 O  O   . PRO   D  1 377 ? 7.680   -44.930 -50.590  1.00 19.78  ? 678  PRO   D O   1 
ATOM   13250 C  CB  . PRO   D  1 377 ? 8.673   -42.047 -50.579  1.00 27.85  ? 678  PRO   D CB  1 
ATOM   13251 C  CG  . PRO   D  1 377 ? 7.926   -42.076 -49.238  1.00 28.89  ? 678  PRO   D CG  1 
ATOM   13252 C  CD  . PRO   D  1 377 ? 6.489   -41.809 -49.630  1.00 28.28  ? 678  PRO   D CD  1 
ATOM   13253 N  N   . ALA   D  1 378 ? 8.294   -44.734 -52.743  1.00 25.11  ? 679  ALA   D N   1 
ATOM   13254 C  CA  . ALA   D  1 378 ? 8.445   -46.173 -52.882  1.00 23.06  ? 679  ALA   D CA  1 
ATOM   13255 C  C   . ALA   D  1 378 ? 9.579   -46.457 -53.849  1.00 23.44  ? 679  ALA   D C   1 
ATOM   13256 O  O   . ALA   D  1 378 ? 9.675   -45.839 -54.919  1.00 24.16  ? 679  ALA   D O   1 
ATOM   13257 C  CB  . ALA   D  1 378 ? 7.134   -46.824 -53.341  1.00 20.21  ? 679  ALA   D CB  1 
ATOM   13258 N  N   . ASP   D  1 379 ? 10.431  -47.385 -53.452  1.00 20.45  ? 680  ASP   D N   1 
ATOM   13259 C  CA  . ASP   D  1 379 ? 11.631  -47.752 -54.193  1.00 21.85  ? 680  ASP   D CA  1 
ATOM   13260 C  C   . ASP   D  1 379 ? 11.331  -49.046 -54.943  1.00 21.28  ? 680  ASP   D C   1 
ATOM   13261 O  O   . ASP   D  1 379 ? 11.465  -50.136 -54.387  1.00 19.99  ? 680  ASP   D O   1 
ATOM   13262 C  CB  . ASP   D  1 379 ? 12.794  -47.912 -53.223  1.00 25.34  ? 680  ASP   D CB  1 
ATOM   13263 C  CG  . ASP   D  1 379 ? 14.085  -48.286 -53.894  1.00 27.98  ? 680  ASP   D CG  1 
ATOM   13264 O  OD1 . ASP   D  1 379 ? 15.148  -47.994 -53.304  1.00 25.27  ? 680  ASP   D OD1 1 
ATOM   13265 O  OD2 . ASP   D  1 379 ? 14.063  -48.859 -55.006  1.00 27.53  ? 680  ASP   D OD2 1 
ATOM   13266 N  N   . TRP   D  1 380 ? 10.976  -48.923 -56.231  1.00 21.86  ? 681  TRP   D N   1 
ATOM   13267 C  CA  . TRP   D  1 380 ? 10.573  -50.086 -57.028  1.00 20.79  ? 681  TRP   D CA  1 
ATOM   13268 C  C   . TRP   D  1 380 ? 11.590  -51.211 -56.942  1.00 17.61  ? 681  TRP   D C   1 
ATOM   13269 O  O   . TRP   D  1 380 ? 11.226  -52.381 -56.809  1.00 18.36  ? 681  TRP   D O   1 
ATOM   13270 C  CB  . TRP   D  1 380 ? 10.388  -49.663 -58.484  1.00 20.01  ? 681  TRP   D CB  1 
ATOM   13271 C  CG  . TRP   D  1 380 ? 9.654   -50.631 -59.369  1.00 20.43  ? 681  TRP   D CG  1 
ATOM   13272 C  CD1 . TRP   D  1 380 ? 8.330   -50.579 -59.725  1.00 27.63  ? 681  TRP   D CD1 1 
ATOM   13273 C  CD2 . TRP   D  1 380 ? 10.212  -51.753 -60.068  1.00 20.04  ? 681  TRP   D CD2 1 
ATOM   13274 N  NE1 . TRP   D  1 380 ? 8.033   -51.609 -60.595  1.00 22.23  ? 681  TRP   D NE1 1 
ATOM   13275 C  CE2 . TRP   D  1 380 ? 9.169   -52.347 -60.810  1.00 24.72  ? 681  TRP   D CE2 1 
ATOM   13276 C  CE3 . TRP   D  1 380 ? 11.488  -52.321 -60.129  1.00 22.73  ? 681  TRP   D CE3 1 
ATOM   13277 C  CZ2 . TRP   D  1 380 ? 9.366   -53.476 -61.608  1.00 26.27  ? 681  TRP   D CZ2 1 
ATOM   13278 C  CZ3 . TRP   D  1 380 ? 11.676  -53.448 -60.929  1.00 25.02  ? 681  TRP   D CZ3 1 
ATOM   13279 C  CH2 . TRP   D  1 380 ? 10.620  -54.009 -61.650  1.00 21.22  ? 681  TRP   D CH2 1 
ATOM   13280 N  N   . VAL   D  1 381 ? 12.875  -50.870 -57.004  1.00 17.86  ? 682  VAL   D N   1 
ATOM   13281 C  CA  . VAL   D  1 381 ? 13.938  -51.869 -56.967  1.00 21.43  ? 682  VAL   D CA  1 
ATOM   13282 C  C   . VAL   D  1 381 ? 13.857  -52.754 -55.727  1.00 26.51  ? 682  VAL   D C   1 
ATOM   13283 O  O   . VAL   D  1 381 ? 14.203  -53.943 -55.781  1.00 21.84  ? 682  VAL   D O   1 
ATOM   13284 C  CB  . VAL   D  1 381 ? 15.287  -51.138 -57.057  1.00 16.75  ? 682  VAL   D CB  1 
ATOM   13285 C  CG1 . VAL   D  1 381 ? 16.441  -52.103 -56.865  1.00 19.53  ? 682  VAL   D CG1 1 
ATOM   13286 C  CG2 . VAL   D  1 381 ? 15.393  -50.443 -58.425  1.00 16.76  ? 682  VAL   D CG2 1 
ATOM   13287 N  N   . TRP   D  1 382 ? 13.402  -52.203 -54.595  1.00 17.85  ? 683  TRP   D N   1 
ATOM   13288 C  CA  . TRP   D  1 382 ? 13.309  -52.967 -53.356  1.00 20.81  ? 683  TRP   D CA  1 
ATOM   13289 C  C   . TRP   D  1 382 ? 11.931  -53.561 -53.123  1.00 18.44  ? 683  TRP   D C   1 
ATOM   13290 O  O   . TRP   D  1 382 ? 11.815  -54.620 -52.499  1.00 20.61  ? 683  TRP   D O   1 
ATOM   13291 C  CB  . TRP   D  1 382 ? 13.684  -52.070 -52.168  1.00 22.83  ? 683  TRP   D CB  1 
ATOM   13292 C  CG  . TRP   D  1 382 ? 15.155  -52.074 -51.930  1.00 22.74  ? 683  TRP   D CG  1 
ATOM   13293 C  CD1 . TRP   D  1 382 ? 16.129  -51.606 -52.765  1.00 23.80  ? 683  TRP   D CD1 1 
ATOM   13294 C  CD2 . TRP   D  1 382 ? 15.824  -52.614 -50.792  1.00 23.57  ? 683  TRP   D CD2 1 
ATOM   13295 N  NE1 . TRP   D  1 382 ? 17.371  -51.812 -52.207  1.00 19.36  ? 683  TRP   D NE1 1 
ATOM   13296 C  CE2 . TRP   D  1 382 ? 17.208  -52.430 -50.993  1.00 26.27  ? 683  TRP   D CE2 1 
ATOM   13297 C  CE3 . TRP   D  1 382 ? 15.388  -53.237 -49.624  1.00 23.52  ? 683  TRP   D CE3 1 
ATOM   13298 C  CZ2 . TRP   D  1 382 ? 18.158  -52.849 -50.062  1.00 25.66  ? 683  TRP   D CZ2 1 
ATOM   13299 C  CZ3 . TRP   D  1 382 ? 16.340  -53.650 -48.693  1.00 27.54  ? 683  TRP   D CZ3 1 
ATOM   13300 C  CH2 . TRP   D  1 382 ? 17.705  -53.453 -48.920  1.00 25.04  ? 683  TRP   D CH2 1 
ATOM   13301 N  N   . ILE   D  1 383 ? 10.892  -52.900 -53.627  1.00 18.52  ? 684  ILE   D N   1 
ATOM   13302 C  CA  . ILE   D  1 383 ? 9.526   -53.330 -53.374  1.00 21.32  ? 684  ILE   D CA  1 
ATOM   13303 C  C   . ILE   D  1 383 ? 9.206   -54.595 -54.166  1.00 24.56  ? 684  ILE   D C   1 
ATOM   13304 O  O   . ILE   D  1 383 ? 8.543   -55.511 -53.658  1.00 22.84  ? 684  ILE   D O   1 
ATOM   13305 C  CB  . ILE   D  1 383 ? 8.564   -52.169 -53.709  1.00 22.53  ? 684  ILE   D CB  1 
ATOM   13306 C  CG1 . ILE   D  1 383 ? 8.800   -50.987 -52.757  1.00 25.76  ? 684  ILE   D CG1 1 
ATOM   13307 C  CG2 . ILE   D  1 383 ? 7.107   -52.622 -53.679  1.00 20.03  ? 684  ILE   D CG2 1 
ATOM   13308 C  CD1 . ILE   D  1 383 ? 8.445   -51.283 -51.320  1.00 21.01  ? 684  ILE   D CD1 1 
ATOM   13309 N  N   . VAL   D  1 384 ? 9.642   -54.660 -55.424  1.00 17.61  ? 685  VAL   D N   1 
ATOM   13310 C  CA  . VAL   D  1 384 ? 9.330   -55.837 -56.247  1.00 17.54  ? 685  VAL   D CA  1 
ATOM   13311 C  C   . VAL   D  1 384 ? 10.053  -57.043 -55.673  1.00 19.08  ? 685  VAL   D C   1 
ATOM   13312 O  O   . VAL   D  1 384 ? 11.268  -56.972 -55.429  1.00 22.95  ? 685  VAL   D O   1 
ATOM   13313 C  CB  . VAL   D  1 384 ? 9.741   -55.603 -57.715  1.00 19.03  ? 685  VAL   D CB  1 
ATOM   13314 C  CG1 . VAL   D  1 384 ? 9.470   -56.853 -58.532  1.00 17.65  ? 685  VAL   D CG1 1 
ATOM   13315 C  CG2 . VAL   D  1 384 ? 8.972   -54.441 -58.282  1.00 19.22  ? 685  VAL   D CG2 1 
ATOM   13316 N  N   . PRO   D  1 385 ? 9.364   -58.147 -55.432  1.00 21.57  ? 686  PRO   D N   1 
ATOM   13317 C  CA  . PRO   D  1 385 ? 9.999   -59.279 -54.774  1.00 23.18  ? 686  PRO   D CA  1 
ATOM   13318 C  C   . PRO   D  1 385 ? 11.067  -59.888 -55.660  1.00 26.03  ? 686  PRO   D C   1 
ATOM   13319 O  O   . PRO   D  1 385 ? 11.016  -59.762 -56.893  1.00 26.31  ? 686  PRO   D O   1 
ATOM   13320 C  CB  . PRO   D  1 385 ? 8.834   -60.249 -54.554  1.00 27.33  ? 686  PRO   D CB  1 
ATOM   13321 C  CG  . PRO   D  1 385 ? 7.640   -59.354 -54.466  1.00 29.12  ? 686  PRO   D CG  1 
ATOM   13322 C  CD  . PRO   D  1 385 ? 7.905   -58.313 -55.524  1.00 28.13  ? 686  PRO   D CD  1 
ATOM   13323 N  N   . PRO   D  1 386 ? 12.053  -60.558 -55.066  1.00 26.47  ? 687  PRO   D N   1 
ATOM   13324 C  CA  . PRO   D  1 386 ? 13.156  -61.122 -55.843  1.00 21.12  ? 687  PRO   D CA  1 
ATOM   13325 C  C   . PRO   D  1 386 ? 12.814  -62.399 -56.591  1.00 25.17  ? 687  PRO   D C   1 
ATOM   13326 O  O   . PRO   D  1 386 ? 13.722  -63.006 -57.168  1.00 27.81  ? 687  PRO   D O   1 
ATOM   13327 C  CB  . PRO   D  1 386 ? 14.205  -61.406 -54.761  1.00 22.70  ? 687  PRO   D CB  1 
ATOM   13328 C  CG  . PRO   D  1 386 ? 13.360  -61.790 -53.581  1.00 20.73  ? 687  PRO   D CG  1 
ATOM   13329 C  CD  . PRO   D  1 386 ? 12.187  -60.839 -53.631  1.00 22.12  ? 687  PRO   D CD  1 
ATOM   13330 N  N   . MET   D  1 387 ? 11.556  -62.846 -56.574  1.00 21.94  ? 688  MET   D N   1 
ATOM   13331 C  CA  . MET   D  1 387 ? 11.115  -63.895 -57.488  1.00 25.81  ? 688  MET   D CA  1 
ATOM   13332 C  C   . MET   D  1 387 ? 9.734   -63.530 -58.013  1.00 31.49  ? 688  MET   D C   1 
ATOM   13333 O  O   . MET   D  1 387 ? 8.997   -62.761 -57.385  1.00 26.67  ? 688  MET   D O   1 
ATOM   13334 C  CB  . MET   D  1 387 ? 11.085  -65.284 -56.829  1.00 23.13  ? 688  MET   D CB  1 
ATOM   13335 C  CG  . MET   D  1 387 ? 9.915   -65.476 -55.875  1.00 30.83  ? 688  MET   D CG  1 
ATOM   13336 S  SD  . MET   D  1 387 ? 9.850   -67.079 -55.029  1.00 35.79  ? 688  MET   D SD  1 
ATOM   13337 C  CE  . MET   D  1 387 ? 9.156   -68.117 -56.316  1.00 35.65  ? 688  MET   D CE  1 
ATOM   13338 N  N   . SER   D  1 388 ? 9.408   -64.058 -59.198  1.00 29.69  ? 689  SER   D N   1 
ATOM   13339 C  CA  . SER   D  1 388 ? 8.065   -63.931 -59.767  1.00 27.73  ? 689  SER   D CA  1 
ATOM   13340 C  C   . SER   D  1 388 ? 7.623   -62.473 -59.860  1.00 25.46  ? 689  SER   D C   1 
ATOM   13341 O  O   . SER   D  1 388 ? 6.448   -62.149 -59.677  1.00 29.26  ? 689  SER   D O   1 
ATOM   13342 C  CB  . SER   D  1 388 ? 7.068   -64.745 -58.950  1.00 36.27  ? 689  SER   D CB  1 
ATOM   13343 O  OG  . SER   D  1 388 ? 7.484   -66.086 -58.912  1.00 40.33  ? 689  SER   D OG  1 
ATOM   13344 N  N   . GLY   D  1 389 ? 8.576   -61.588 -60.129  1.00 23.93  ? 690  GLY   D N   1 
ATOM   13345 C  CA  . GLY   D  1 389 ? 8.330   -60.157 -60.098  1.00 22.99  ? 690  GLY   D CA  1 
ATOM   13346 C  C   . GLY   D  1 389 ? 7.043   -59.718 -60.770  1.00 26.24  ? 690  GLY   D C   1 
ATOM   13347 O  O   . GLY   D  1 389 ? 6.175   -59.128 -60.123  1.00 22.23  ? 690  GLY   D O   1 
ATOM   13348 N  N   . SER   D  1 390 ? 6.878   -60.041 -62.052  1.00 19.42  ? 691  SER   D N   1 
ATOM   13349 C  CA  . SER   D  1 390 ? 5.770   -59.450 -62.790  1.00 20.50  ? 691  SER   D CA  1 
ATOM   13350 C  C   . SER   D  1 390 ? 4.437   -60.134 -62.546  1.00 21.98  ? 691  SER   D C   1 
ATOM   13351 O  O   . SER   D  1 390 ? 3.416   -59.661 -63.053  1.00 27.26  ? 691  SER   D O   1 
ATOM   13352 C  CB  . SER   D  1 390 ? 6.055   -59.453 -64.289  1.00 22.81  ? 691  SER   D CB  1 
ATOM   13353 O  OG  . SER   D  1 390 ? 6.114   -60.770 -64.740  1.00 26.43  ? 691  SER   D OG  1 
ATOM   13354 N  N   . ILE   D  1 391 ? 4.383   -61.238 -61.803  1.00 24.38  ? 692  ILE   D N   1 
ATOM   13355 C  CA  . ILE   D  1 391 ? 3.059   -61.721 -61.434  1.00 29.87  ? 692  ILE   D CA  1 
ATOM   13356 C  C   . ILE   D  1 391 ? 2.611   -61.129 -60.107  1.00 29.02  ? 692  ILE   D C   1 
ATOM   13357 O  O   . ILE   D  1 391 ? 1.509   -61.440 -59.642  1.00 36.05  ? 692  ILE   D O   1 
ATOM   13358 C  CB  . ILE   D  1 391 ? 2.982   -63.262 -61.454  1.00 31.77  ? 692  ILE   D CB  1 
ATOM   13359 C  CG1 . ILE   D  1 391 ? 4.047   -63.879 -60.577  1.00 34.71  ? 692  ILE   D CG1 1 
ATOM   13360 C  CG2 . ILE   D  1 391 ? 3.122   -63.785 -62.910  1.00 35.66  ? 692  ILE   D CG2 1 
ATOM   13361 C  CD1 . ILE   D  1 391 ? 3.726   -65.286 -60.198  1.00 44.29  ? 692  ILE   D CD1 1 
ATOM   13362 N  N   . THR   D  1 392 ? 3.445   -60.222 -59.482  1.00 32.92  ? 693  THR   D N   1 
ATOM   13363 C  CA  . THR   D  1 392 ? 2.965   -59.414 -58.369  1.00 29.21  ? 693  THR   D CA  1 
ATOM   13364 C  C   . THR   D  1 392 ? 2.523   -58.049 -58.881  1.00 30.87  ? 693  THR   D C   1 
ATOM   13365 O  O   . THR   D  1 392 ? 3.041   -57.563 -59.897  1.00 25.90  ? 693  THR   D O   1 
ATOM   13366 C  CB  . THR   D  1 392 ? 4.040   -59.214 -57.294  1.00 26.05  ? 693  THR   D CB  1 
ATOM   13367 O  OG1 . THR   D  1 392 ? 5.076   -58.359 -57.789  1.00 28.20  ? 693  THR   D OG1 1 
ATOM   13368 C  CG2 . THR   D  1 392 ? 4.633   -60.549 -56.841  1.00 23.16  ? 693  THR   D CG2 1 
ATOM   13369 N  N   . PRO   D  1 393 ? 1.546   -57.414 -58.226  1.00 26.51  ? 694  PRO   D N   1 
ATOM   13370 C  CA  . PRO   D  1 393 ? 1.024   -56.153 -58.769  1.00 25.11  ? 694  PRO   D CA  1 
ATOM   13371 C  C   . PRO   D  1 393 ? 2.027   -55.025 -58.722  1.00 26.31  ? 694  PRO   D C   1 
ATOM   13372 O  O   . PRO   D  1 393 ? 1.911   -54.090 -59.521  1.00 31.34  ? 694  PRO   D O   1 
ATOM   13373 C  CB  . PRO   D  1 393 ? -0.200  -55.858 -57.886  1.00 28.63  ? 694  PRO   D CB  1 
ATOM   13374 C  CG  . PRO   D  1 393 ? 0.040   -56.645 -56.607  1.00 24.41  ? 694  PRO   D CG  1 
ATOM   13375 C  CD  . PRO   D  1 393 ? 0.741   -57.898 -57.095  1.00 24.71  ? 694  PRO   D CD  1 
ATOM   13376 N  N   . VAL   D  1 394 ? 3.026   -55.089 -57.842  1.00 25.77  ? 695  VAL   D N   1 
ATOM   13377 C  CA  . VAL   D  1 394 ? 3.925   -53.948 -57.714  1.00 24.75  ? 695  VAL   D CA  1 
ATOM   13378 C  C   . VAL   D  1 394 ? 4.842   -53.834 -58.910  1.00 20.66  ? 695  VAL   D C   1 
ATOM   13379 O  O   . VAL   D  1 394 ? 5.332   -52.744 -59.191  1.00 19.25  ? 695  VAL   D O   1 
ATOM   13380 C  CB  . VAL   D  1 394 ? 4.752   -54.001 -56.415  1.00 22.07  ? 695  VAL   D CB  1 
ATOM   13381 C  CG1 . VAL   D  1 394 ? 3.827   -53.813 -55.197  1.00 17.25  ? 695  VAL   D CG1 1 
ATOM   13382 C  CG2 . VAL   D  1 394 ? 5.547   -55.320 -56.324  1.00 19.88  ? 695  VAL   D CG2 1 
ATOM   13383 N  N   . PHE   D  1 395 ? 5.083   -54.934 -59.625  1.00 21.90  ? 696  PHE   D N   1 
ATOM   13384 C  CA  . PHE   D  1 395 ? 5.915   -54.868 -60.817  1.00 25.92  ? 696  PHE   D CA  1 
ATOM   13385 C  C   . PHE   D  1 395 ? 5.352   -53.873 -61.817  1.00 26.27  ? 696  PHE   D C   1 
ATOM   13386 O  O   . PHE   D  1 395 ? 6.106   -53.150 -62.476  1.00 20.30  ? 696  PHE   D O   1 
ATOM   13387 C  CB  . PHE   D  1 395 ? 6.029   -56.256 -61.443  1.00 31.28  ? 696  PHE   D CB  1 
ATOM   13388 C  CG  . PHE   D  1 395 ? 6.859   -56.302 -62.702  1.00 27.00  ? 696  PHE   D CG  1 
ATOM   13389 C  CD1 . PHE   D  1 395 ? 8.203   -56.663 -62.648  1.00 29.28  ? 696  PHE   D CD1 1 
ATOM   13390 C  CD2 . PHE   D  1 395 ? 6.290   -56.018 -63.934  1.00 20.86  ? 696  PHE   D CD2 1 
ATOM   13391 C  CE1 . PHE   D  1 395 ? 8.969   -56.724 -63.813  1.00 23.22  ? 696  PHE   D CE1 1 
ATOM   13392 C  CE2 . PHE   D  1 395 ? 7.042   -56.075 -65.096  1.00 28.06  ? 696  PHE   D CE2 1 
ATOM   13393 C  CZ  . PHE   D  1 395 ? 8.382   -56.427 -65.036  1.00 30.60  ? 696  PHE   D CZ  1 
ATOM   13394 N  N   . HIS   D  1 396 ? 4.030   -53.798 -61.917  1.00 20.91  ? 697  HIS   D N   1 
ATOM   13395 C  CA  . HIS   D  1 396 ? 3.351   -52.978 -62.899  1.00 23.23  ? 697  HIS   D CA  1 
ATOM   13396 C  C   . HIS   D  1 396 ? 2.992   -51.607 -62.370  1.00 28.18  ? 697  HIS   D C   1 
ATOM   13397 O  O   . HIS   D  1 396 ? 2.308   -50.844 -63.069  1.00 29.33  ? 697  HIS   D O   1 
ATOM   13398 C  CB  . HIS   D  1 396 ? 2.088   -53.703 -63.372  1.00 24.87  ? 697  HIS   D CB  1 
ATOM   13399 C  CG  . HIS   D  1 396 ? 2.355   -55.102 -63.821  1.00 28.38  ? 697  HIS   D CG  1 
ATOM   13400 N  ND1 . HIS   D  1 396 ? 2.730   -55.409 -65.114  1.00 28.45  ? 697  HIS   D ND1 1 
ATOM   13401 C  CD2 . HIS   D  1 396 ? 2.339   -56.274 -63.143  1.00 29.54  ? 697  HIS   D CD2 1 
ATOM   13402 C  CE1 . HIS   D  1 396 ? 2.918   -56.713 -65.215  1.00 30.09  ? 697  HIS   D CE1 1 
ATOM   13403 N  NE2 . HIS   D  1 396 ? 2.688   -57.260 -64.033  1.00 33.57  ? 697  HIS   D NE2 1 
ATOM   13404 N  N   . GLN   D  1 397 ? 3.428   -51.288 -61.159  1.00 22.90  ? 698  GLN   D N   1 
ATOM   13405 C  CA  . GLN   D  1 397 ? 3.103   -50.044 -60.488  1.00 22.32  ? 698  GLN   D CA  1 
ATOM   13406 C  C   . GLN   D  1 397 ? 4.275   -49.081 -60.614  1.00 21.19  ? 698  GLN   D C   1 
ATOM   13407 O  O   . GLN   D  1 397 ? 5.364   -49.356 -60.099  1.00 26.01  ? 698  GLN   D O   1 
ATOM   13408 C  CB  . GLN   D  1 397 ? 2.815   -50.316 -59.011  1.00 24.44  ? 698  GLN   D CB  1 
ATOM   13409 C  CG  . GLN   D  1 397 ? 2.561   -49.065 -58.227  1.00 21.63  ? 698  GLN   D CG  1 
ATOM   13410 C  CD  . GLN   D  1 397 ? 1.273   -48.430 -58.663  1.00 24.83  ? 698  GLN   D CD  1 
ATOM   13411 O  OE1 . GLN   D  1 397 ? 0.220   -49.069 -58.611  1.00 21.17  ? 698  GLN   D OE1 1 
ATOM   13412 N  NE2 . GLN   D  1 397 ? 1.343   -47.178 -59.120  1.00 22.12  ? 698  GLN   D NE2 1 
ATOM   13413 N  N   . GLU   D  1 398 ? 4.066   -47.955 -61.280  1.00 20.55  ? 699  GLU   D N   1 
ATOM   13414 C  CA  . GLU   D  1 398 ? 5.090   -46.923 -61.246  1.00 18.89  ? 699  GLU   D CA  1 
ATOM   13415 C  C   . GLU   D  1 398 ? 5.181   -46.362 -59.833  1.00 24.20  ? 699  GLU   D C   1 
ATOM   13416 O  O   . GLU   D  1 398 ? 4.178   -46.241 -59.133  1.00 19.78  ? 699  GLU   D O   1 
ATOM   13417 C  CB  . GLU   D  1 398 ? 4.777   -45.816 -62.234  1.00 21.31  ? 699  GLU   D CB  1 
ATOM   13418 C  CG  . GLU   D  1 398 ? 4.886   -46.284 -63.684  1.00 19.93  ? 699  GLU   D CG  1 
ATOM   13419 C  CD  . GLU   D  1 398 ? 4.508   -45.213 -64.659  1.00 27.63  ? 699  GLU   D CD  1 
ATOM   13420 O  OE1 . GLU   D  1 398 ? 4.822   -45.369 -65.868  1.00 27.23  ? 699  GLU   D OE1 1 
ATOM   13421 O  OE2 . GLU   D  1 398 ? 3.905   -44.212 -64.219  1.00 27.31  ? 699  GLU   D OE2 1 
ATOM   13422 N  N   . MET   D  1 399 ? 6.385   -46.026 -59.414  1.00 20.27  ? 700  MET   D N   1 
ATOM   13423 C  CA  . MET   D  1 399 ? 6.588   -45.465 -58.091  1.00 23.71  ? 700  MET   D CA  1 
ATOM   13424 C  C   . MET   D  1 399 ? 7.482   -44.242 -58.190  1.00 27.70  ? 700  MET   D C   1 
ATOM   13425 O  O   . MET   D  1 399 ? 8.313   -44.126 -59.096  1.00 32.93  ? 700  MET   D O   1 
ATOM   13426 C  CB  . MET   D  1 399 ? 7.198   -46.506 -57.157  1.00 22.22  ? 700  MET   D CB  1 
ATOM   13427 C  CG  . MET   D  1 399 ? 6.312   -47.712 -56.944  1.00 19.01  ? 700  MET   D CG  1 
ATOM   13428 S  SD  . MET   D  1 399 ? 7.201   -49.090 -56.187  1.00 25.89  ? 700  MET   D SD  1 
ATOM   13429 C  CE  . MET   D  1 399 ? 5.947   -50.360 -56.291  1.00 23.68  ? 700  MET   D CE  1 
ATOM   13430 N  N   . LEU   D  1 400 ? 7.272   -43.313 -57.273  1.00 26.16  ? 701  LEU   D N   1 
ATOM   13431 C  CA  . LEU   D  1 400 ? 8.167   -42.184 -57.092  1.00 22.37  ? 701  LEU   D CA  1 
ATOM   13432 C  C   . LEU   D  1 400 ? 8.956   -42.425 -55.831  1.00 26.51  ? 701  LEU   D C   1 
ATOM   13433 O  O   . LEU   D  1 400 ? 8.373   -42.738 -54.790  1.00 27.98  ? 701  LEU   D O   1 
ATOM   13434 C  CB  . LEU   D  1 400 ? 7.406   -40.869 -56.957  1.00 21.77  ? 701  LEU   D CB  1 
ATOM   13435 C  CG  . LEU   D  1 400 ? 6.711   -40.381 -58.200  1.00 31.25  ? 701  LEU   D CG  1 
ATOM   13436 C  CD1 . LEU   D  1 400 ? 5.929   -39.155 -57.826  1.00 33.84  ? 701  LEU   D CD1 1 
ATOM   13437 C  CD2 . LEU   D  1 400 ? 7.753   -40.062 -59.263  1.00 26.82  ? 701  LEU   D CD2 1 
ATOM   13438 N  N   . ASN   D  1 401 ? 10.269  -42.287 -55.917  1.00 26.88  ? 702  ASN   D N   1 
ATOM   13439 C  CA  . ASN   D  1 401 ? 11.116  -42.446 -54.750  1.00 23.31  ? 702  ASN   D CA  1 
ATOM   13440 C  C   . ASN   D  1 401 ? 11.631  -41.084 -54.328  1.00 27.60  ? 702  ASN   D C   1 
ATOM   13441 O  O   . ASN   D  1 401 ? 12.161  -40.334 -55.154  1.00 26.28  ? 702  ASN   D O   1 
ATOM   13442 C  CB  . ASN   D  1 401 ? 12.281  -43.393 -55.006  1.00 27.65  ? 702  ASN   D CB  1 
ATOM   13443 C  CG  . ASN   D  1 401 ? 12.899  -43.855 -53.719  1.00 27.77  ? 702  ASN   D CG  1 
ATOM   13444 O  OD1 . ASN   D  1 401 ? 12.324  -43.629 -52.669  1.00 27.91  ? 702  ASN   D OD1 1 
ATOM   13445 N  ND2 . ASN   D  1 401 ? 14.057  -44.472 -53.777  1.00 24.43  ? 702  ASN   D ND2 1 
ATOM   13446 N  N   . TYR   D  1 402 ? 11.441  -40.752 -53.054  1.00 27.47  ? 703  TYR   D N   1 
ATOM   13447 C  CA  . TYR   D  1 402 ? 11.980  -39.518 -52.500  1.00 18.52  ? 703  TYR   D CA  1 
ATOM   13448 C  C   . TYR   D  1 402 ? 12.145  -39.731 -51.002  1.00 25.60  ? 703  TYR   D C   1 
ATOM   13449 O  O   . TYR   D  1 402 ? 11.605  -40.681 -50.430  1.00 22.35  ? 703  TYR   D O   1 
ATOM   13450 C  CB  . TYR   D  1 402 ? 11.088  -38.301 -52.805  1.00 19.29  ? 703  TYR   D CB  1 
ATOM   13451 C  CG  . TYR   D  1 402 ? 9.601   -38.538 -52.610  1.00 26.70  ? 703  TYR   D CG  1 
ATOM   13452 C  CD1 . TYR   D  1 402 ? 8.962   -38.212 -51.408  1.00 27.52  ? 703  TYR   D CD1 1 
ATOM   13453 C  CD2 . TYR   D  1 402 ? 8.829   -39.080 -53.632  1.00 25.82  ? 703  TYR   D CD2 1 
ATOM   13454 C  CE1 . TYR   D  1 402 ? 7.588   -38.425 -51.242  1.00 19.53  ? 703  TYR   D CE1 1 
ATOM   13455 C  CE2 . TYR   D  1 402 ? 7.470   -39.295 -53.475  1.00 22.23  ? 703  TYR   D CE2 1 
ATOM   13456 C  CZ  . TYR   D  1 402 ? 6.851   -38.970 -52.283  1.00 28.47  ? 703  TYR   D CZ  1 
ATOM   13457 O  OH  . TYR   D  1 402 ? 5.496   -39.196 -52.151  1.00 31.17  ? 703  TYR   D OH  1 
ATOM   13458 N  N   . ARG   D  1 403 ? 12.907  -38.842 -50.385  1.00 25.88  ? 704  ARG   D N   1 
ATOM   13459 C  CA  . ARG   D  1 403 ? 13.396  -39.033 -49.025  1.00 29.65  ? 704  ARG   D CA  1 
ATOM   13460 C  C   . ARG   D  1 403 ? 12.684  -38.049 -48.104  1.00 36.28  ? 704  ARG   D C   1 
ATOM   13461 O  O   . ARG   D  1 403 ? 12.906  -36.833 -48.181  1.00 34.62  ? 704  ARG   D O   1 
ATOM   13462 C  CB  . ARG   D  1 403 ? 14.912  -38.862 -48.972  1.00 26.27  ? 704  ARG   D CB  1 
ATOM   13463 C  CG  . ARG   D  1 403 ? 15.664  -39.831 -49.885  1.00 27.60  ? 704  ARG   D CG  1 
ATOM   13464 C  CD  . ARG   D  1 403 ? 17.165  -39.641 -49.782  1.00 39.30  ? 704  ARG   D CD  1 
ATOM   13465 N  NE  . ARG   D  1 403 ? 17.686  -40.152 -48.514  1.00 48.33  ? 704  ARG   D NE  1 
ATOM   13466 C  CZ  . ARG   D  1 403 ? 18.923  -39.946 -48.075  1.00 55.36  ? 704  ARG   D CZ  1 
ATOM   13467 N  NH1 . ARG   D  1 403 ? 19.779  -39.228 -48.793  1.00 54.36  ? 704  ARG   D NH1 1 
ATOM   13468 N  NH2 . ARG   D  1 403 ? 19.304  -40.453 -46.913  1.00 56.66  ? 704  ARG   D NH2 1 
ATOM   13469 N  N   . LEU   D  1 404 ? 11.818  -38.584 -47.253  1.00 31.82  ? 705  LEU   D N   1 
ATOM   13470 C  CA  . LEU   D  1 404 ? 11.108  -37.805 -46.257  1.00 26.62  ? 705  LEU   D CA  1 
ATOM   13471 C  C   . LEU   D  1 404 ? 11.751  -38.027 -44.899  1.00 22.09  ? 705  LEU   D C   1 
ATOM   13472 O  O   . LEU   D  1 404 ? 12.389  -39.049 -44.652  1.00 24.88  ? 705  LEU   D O   1 
ATOM   13473 C  CB  . LEU   D  1 404 ? 9.625   -38.194 -46.214  1.00 25.82  ? 705  LEU   D CB  1 
ATOM   13474 C  CG  . LEU   D  1 404 ? 8.840   -38.014 -47.515  1.00 25.25  ? 705  LEU   D CG  1 
ATOM   13475 C  CD1 . LEU   D  1 404 ? 7.380   -38.405 -47.313  1.00 24.90  ? 705  LEU   D CD1 1 
ATOM   13476 C  CD2 . LEU   D  1 404 ? 8.957   -36.579 -48.022  1.00 20.14  ? 705  LEU   D CD2 1 
ATOM   13477 N  N   . THR   D  1 405 ? 11.598  -37.048 -44.027  1.00 26.01  ? 706  THR   D N   1 
ATOM   13478 C  CA  . THR   D  1 405 ? 12.082  -37.165 -42.669  1.00 26.81  ? 706  THR   D CA  1 
ATOM   13479 C  C   . THR   D  1 405 ? 10.887  -37.103 -41.728  1.00 31.29  ? 706  THR   D C   1 
ATOM   13480 O  O   . THR   D  1 405 ? 9.889   -36.453 -42.053  1.00 26.89  ? 706  THR   D O   1 
ATOM   13481 C  CB  . THR   D  1 405 ? 13.065  -36.033 -42.346  1.00 35.53  ? 706  THR   D CB  1 
ATOM   13482 O  OG1 . THR   D  1 405 ? 13.685  -36.274 -41.081  1.00 37.22  ? 706  THR   D OG1 1 
ATOM   13483 C  CG2 . THR   D  1 405 ? 12.334  -34.692 -42.303  1.00 32.98  ? 706  THR   D CG2 1 
ATOM   13484 N  N   . PRO   D  1 406 ? 10.921  -37.808 -40.579  1.00 30.97  ? 707  PRO   D N   1 
ATOM   13485 C  CA  . PRO   D  1 406 ? 11.962  -38.701 -40.056  1.00 27.63  ? 707  PRO   D CA  1 
ATOM   13486 C  C   . PRO   D  1 406 ? 12.239  -39.903 -40.952  1.00 26.79  ? 707  PRO   D C   1 
ATOM   13487 O  O   . PRO   D  1 406 ? 11.417  -40.275 -41.799  1.00 26.97  ? 707  PRO   D O   1 
ATOM   13488 C  CB  . PRO   D  1 406 ? 11.383  -39.173 -38.709  1.00 27.00  ? 707  PRO   D CB  1 
ATOM   13489 C  CG  . PRO   D  1 406 ? 10.360  -38.153 -38.353  1.00 25.32  ? 707  PRO   D CG  1 
ATOM   13490 C  CD  . PRO   D  1 406 ? 9.772   -37.725 -39.664  1.00 27.99  ? 707  PRO   D CD  1 
ATOM   13491 N  N   . SER   D  1 407 ? 13.390  -40.536 -40.753  1.00 18.73  ? 708  SER   D N   1 
ATOM   13492 C  CA  . SER   D  1 407 ? 13.718  -41.652 -41.621  1.00 21.15  ? 708  SER   D CA  1 
ATOM   13493 C  C   . SER   D  1 407 ? 14.683  -42.586 -40.914  1.00 18.67  ? 708  SER   D C   1 
ATOM   13494 O  O   . SER   D  1 407 ? 15.336  -42.221 -39.930  1.00 20.02  ? 708  SER   D O   1 
ATOM   13495 C  CB  . SER   D  1 407 ? 14.331  -41.161 -42.938  1.00 32.04  ? 708  SER   D CB  1 
ATOM   13496 O  OG  . SER   D  1 407 ? 15.501  -40.403 -42.678  1.00 34.65  ? 708  SER   D OG  1 
ATOM   13497 N  N   . PHE   D  1 408 ? 14.771  -43.796 -41.452  1.00 23.87  ? 709  PHE   D N   1 
ATOM   13498 C  CA  . PHE   D  1 408 ? 15.865  -44.714 -41.166  1.00 23.54  ? 709  PHE   D CA  1 
ATOM   13499 C  C   . PHE   D  1 408 ? 16.956  -44.523 -42.205  1.00 27.29  ? 709  PHE   D C   1 
ATOM   13500 O  O   . PHE   D  1 408 ? 16.672  -44.425 -43.408  1.00 27.44  ? 709  PHE   D O   1 
ATOM   13501 C  CB  . PHE   D  1 408 ? 15.371  -46.161 -41.175  1.00 20.70  ? 709  PHE   D CB  1 
ATOM   13502 C  CG  . PHE   D  1 408 ? 14.413  -46.463 -40.079  1.00 24.80  ? 709  PHE   D CG  1 
ATOM   13503 C  CD1 . PHE   D  1 408 ? 13.066  -46.605 -40.344  1.00 24.35  ? 709  PHE   D CD1 1 
ATOM   13504 C  CD2 . PHE   D  1 408 ? 14.859  -46.578 -38.762  1.00 23.98  ? 709  PHE   D CD2 1 
ATOM   13505 C  CE1 . PHE   D  1 408 ? 12.174  -46.885 -39.323  1.00 19.76  ? 709  PHE   D CE1 1 
ATOM   13506 C  CE2 . PHE   D  1 408 ? 13.984  -46.857 -37.751  1.00 19.42  ? 709  PHE   D CE2 1 
ATOM   13507 C  CZ  . PHE   D  1 408 ? 12.628  -47.014 -38.032  1.00 18.74  ? 709  PHE   D CZ  1 
ATOM   13508 N  N   . GLU   D  1 409 ? 18.200  -44.474 -41.741  1.00 25.70  ? 710  GLU   D N   1 
ATOM   13509 C  CA  . GLU   D  1 409 ? 19.343  -44.230 -42.596  1.00 24.69  ? 710  GLU   D CA  1 
ATOM   13510 C  C   . GLU   D  1 409 ? 20.354  -45.335 -42.375  1.00 28.67  ? 710  GLU   D C   1 
ATOM   13511 O  O   . GLU   D  1 409 ? 20.356  -45.993 -41.338  1.00 26.06  ? 710  GLU   D O   1 
ATOM   13512 C  CB  . GLU   D  1 409 ? 20.006  -42.881 -42.305  1.00 24.87  ? 710  GLU   D CB  1 
ATOM   13513 C  CG  . GLU   D  1 409 ? 19.092  -41.691 -42.462  1.00 33.89  ? 710  GLU   D CG  1 
ATOM   13514 C  CD  . GLU   D  1 409 ? 18.629  -41.500 -43.896  1.00 41.30  ? 710  GLU   D CD  1 
ATOM   13515 O  OE1 . GLU   D  1 409 ? 19.300  -42.012 -44.822  1.00 44.20  ? 710  GLU   D OE1 1 
ATOM   13516 O  OE2 . GLU   D  1 409 ? 17.591  -40.833 -44.093  1.00 42.29  ? 710  GLU   D OE2 1 
ATOM   13517 N  N   . TYR   D  1 410 ? 21.221  -45.530 -43.358  1.00 21.83  ? 711  TYR   D N   1 
ATOM   13518 C  CA  . TYR   D  1 410 ? 22.371  -46.388 -43.153  1.00 21.15  ? 711  TYR   D CA  1 
ATOM   13519 C  C   . TYR   D  1 410 ? 23.442  -45.653 -42.360  1.00 21.50  ? 711  TYR   D C   1 
ATOM   13520 O  O   . TYR   D  1 410 ? 23.517  -44.425 -42.366  1.00 28.07  ? 711  TYR   D O   1 
ATOM   13521 C  CB  . TYR   D  1 410 ? 22.969  -46.823 -44.491  1.00 28.27  ? 711  TYR   D CB  1 
ATOM   13522 C  CG  . TYR   D  1 410 ? 22.087  -47.730 -45.308  1.00 35.23  ? 711  TYR   D CG  1 
ATOM   13523 C  CD1 . TYR   D  1 410 ? 21.484  -47.285 -46.473  1.00 58.29  ? 711  TYR   D CD1 1 
ATOM   13524 C  CD2 . TYR   D  1 410 ? 21.876  -49.034 -44.920  1.00 48.66  ? 711  TYR   D CD2 1 
ATOM   13525 C  CE1 . TYR   D  1 410 ? 20.691  -48.128 -47.228  1.00 64.31  ? 711  TYR   D CE1 1 
ATOM   13526 C  CE2 . TYR   D  1 410 ? 21.090  -49.877 -45.657  1.00 61.51  ? 711  TYR   D CE2 1 
ATOM   13527 C  CZ  . TYR   D  1 410 ? 20.501  -49.429 -46.809  1.00 55.66  ? 711  TYR   D CZ  1 
ATOM   13528 O  OH  . TYR   D  1 410 ? 19.724  -50.306 -47.523  1.00 45.61  ? 711  TYR   D OH  1 
ATOM   13529 N  N   . GLN   D  1 411 ? 24.302  -46.422 -41.709  1.00 18.98  ? 712  GLN   D N   1 
ATOM   13530 C  CA  . GLN   D  1 411 ? 25.433  -45.881 -40.977  1.00 26.75  ? 712  GLN   D CA  1 
ATOM   13531 C  C   . GLN   D  1 411 ? 26.578  -46.858 -41.141  1.00 27.15  ? 712  GLN   D C   1 
ATOM   13532 O  O   . GLN   D  1 411 ? 26.357  -48.027 -41.478  1.00 29.14  ? 712  GLN   D O   1 
ATOM   13533 C  CB  . GLN   D  1 411 ? 25.102  -45.656 -39.487  1.00 30.44  ? 712  GLN   D CB  1 
ATOM   13534 C  CG  . GLN   D  1 411 ? 24.699  -46.913 -38.710  1.00 24.56  ? 712  GLN   D CG  1 
ATOM   13535 C  CD  . GLN   D  1 411 ? 24.191  -46.600 -37.301  1.00 22.83  ? 712  GLN   D CD  1 
ATOM   13536 O  OE1 . GLN   D  1 411 ? 24.628  -45.640 -36.669  1.00 30.53  ? 712  GLN   D OE1 1 
ATOM   13537 N  NE2 . GLN   D  1 411 ? 23.249  -47.400 -36.821  1.00 25.12  ? 712  GLN   D NE2 1 
ATOM   13538 N  N   . PRO   D  1 412 ? 27.810  -46.411 -40.954  1.00 29.98  ? 713  PRO   D N   1 
ATOM   13539 C  CA  . PRO   D  1 412 ? 28.934  -47.329 -41.130  1.00 38.92  ? 713  PRO   D CA  1 
ATOM   13540 C  C   . PRO   D  1 412 ? 28.926  -48.408 -40.058  1.00 39.29  ? 713  PRO   D C   1 
ATOM   13541 O  O   . PRO   D  1 412 ? 28.425  -48.212 -38.950  1.00 34.99  ? 713  PRO   D O   1 
ATOM   13542 C  CB  . PRO   D  1 412 ? 30.167  -46.422 -41.023  1.00 40.15  ? 713  PRO   D CB  1 
ATOM   13543 C  CG  . PRO   D  1 412 ? 29.689  -45.145 -40.422  1.00 37.75  ? 713  PRO   D CG  1 
ATOM   13544 C  CD  . PRO   D  1 412 ? 28.238  -45.018 -40.734  1.00 34.79  ? 713  PRO   D CD  1 
ATOM   13545 N  N   . ASP   D  1 413 ? 29.447  -49.573 -40.428  1.00 42.43  ? 714  ASP   D N   1 
ATOM   13546 C  CA  . ASP   D  1 413 ? 29.635  -50.655 -39.476  1.00 43.12  ? 714  ASP   D CA  1 
ATOM   13547 C  C   . ASP   D  1 413 ? 30.545  -50.191 -38.346  1.00 41.52  ? 714  ASP   D C   1 
ATOM   13548 O  O   . ASP   D  1 413 ? 31.613  -49.625 -38.614  1.00 43.23  ? 714  ASP   D O   1 
ATOM   13549 C  CB  . ASP   D  1 413 ? 30.252  -51.865 -40.174  1.00 51.26  ? 714  ASP   D CB  1 
ATOM   13550 C  CG  . ASP   D  1 413 ? 29.293  -52.546 -41.121  1.00 54.35  ? 714  ASP   D CG  1 
ATOM   13551 O  OD1 . ASP   D  1 413 ? 28.095  -52.653 -40.772  1.00 55.25  ? 714  ASP   D OD1 1 
ATOM   13552 O  OD2 . ASP   D  1 413 ? 29.740  -52.984 -42.206  1.00 55.06  ? 714  ASP   D OD2 1 
ATOM   13553 N  N   . PRO   D  1 414 ? 30.183  -50.425 -37.081  1.00 39.41  ? 715  PRO   D N   1 
ATOM   13554 C  CA  . PRO   D  1 414 ? 30.964  -49.830 -35.982  1.00 31.64  ? 715  PRO   D CA  1 
ATOM   13555 C  C   . PRO   D  1 414 ? 32.384  -50.352 -35.892  1.00 39.17  ? 715  PRO   D C   1 
ATOM   13556 O  O   . PRO   D  1 414 ? 33.255  -49.631 -35.391  1.00 44.10  ? 715  PRO   D O   1 
ATOM   13557 C  CB  . PRO   D  1 414 ? 30.146  -50.175 -34.727  1.00 33.77  ? 715  PRO   D CB  1 
ATOM   13558 C  CG  . PRO   D  1 414 ? 29.335  -51.349 -35.088  1.00 28.39  ? 715  PRO   D CG  1 
ATOM   13559 C  CD  . PRO   D  1 414 ? 29.094  -51.287 -36.596  1.00 35.71  ? 715  PRO   D CD  1 
ATOM   13560 N  N   . TRP   D  1 415 ? 32.674  -51.552 -36.401  1.00 39.46  ? 716  TRP   D N   1 
ATOM   13561 C  CA  . TRP   D  1 415 ? 34.054  -52.024 -36.332  1.00 44.31  ? 716  TRP   D CA  1 
ATOM   13562 C  C   . TRP   D  1 415 ? 34.982  -51.274 -37.283  1.00 47.47  ? 716  TRP   D C   1 
ATOM   13563 O  O   . TRP   D  1 415 ? 36.203  -51.337 -37.104  1.00 47.86  ? 716  TRP   D O   1 
ATOM   13564 C  CB  . TRP   D  1 415 ? 34.131  -53.527 -36.603  1.00 38.36  ? 716  TRP   D CB  1 
ATOM   13565 C  CG  . TRP   D  1 415 ? 33.475  -53.962 -37.856  1.00 41.04  ? 716  TRP   D CG  1 
ATOM   13566 C  CD1 . TRP   D  1 415 ? 34.026  -53.985 -39.101  1.00 46.38  ? 716  TRP   D CD1 1 
ATOM   13567 C  CD2 . TRP   D  1 415 ? 32.136  -54.455 -37.997  1.00 40.78  ? 716  TRP   D CD2 1 
ATOM   13568 N  NE1 . TRP   D  1 415 ? 33.114  -54.462 -40.012  1.00 43.55  ? 716  TRP   D NE1 1 
ATOM   13569 C  CE2 . TRP   D  1 415 ? 31.946  -54.760 -39.359  1.00 43.71  ? 716  TRP   D CE2 1 
ATOM   13570 C  CE3 . TRP   D  1 415 ? 31.078  -54.666 -37.102  1.00 41.48  ? 716  TRP   D CE3 1 
ATOM   13571 C  CZ2 . TRP   D  1 415 ? 30.745  -55.261 -39.851  1.00 45.64  ? 716  TRP   D CZ2 1 
ATOM   13572 C  CZ3 . TRP   D  1 415 ? 29.884  -55.169 -37.591  1.00 39.52  ? 716  TRP   D CZ3 1 
ATOM   13573 C  CH2 . TRP   D  1 415 ? 29.727  -55.458 -38.956  1.00 45.66  ? 716  TRP   D CH2 1 
ATOM   13574 N  N   . ASN   D  1 416 ? 34.440  -50.561 -38.278  1.00 53.97  ? 717  ASN   D N   1 
ATOM   13575 C  CA  . ASN   D  1 416 ? 35.270  -49.732 -39.149  1.00 57.21  ? 717  ASN   D CA  1 
ATOM   13576 C  C   . ASN   D  1 416 ? 35.661  -48.410 -38.506  1.00 58.15  ? 717  ASN   D C   1 
ATOM   13577 O  O   . ASN   D  1 416 ? 36.653  -47.801 -38.925  1.00 57.69  ? 717  ASN   D O   1 
ATOM   13578 C  CB  . ASN   D  1 416 ? 34.547  -49.436 -40.466  1.00 51.38  ? 717  ASN   D CB  1 
ATOM   13579 C  CG  . ASN   D  1 416 ? 34.257  -50.684 -41.264  1.00 55.27  ? 717  ASN   D CG  1 
ATOM   13580 O  OD1 . ASN   D  1 416 ? 35.006  -51.660 -41.209  1.00 61.91  ? 717  ASN   D OD1 1 
ATOM   13581 N  ND2 . ASN   D  1 416 ? 33.162  -50.664 -42.016  1.00 47.36  ? 717  ASN   D ND2 1 
ATOM   13582 N  N   . THR   D  1 417 ? 34.904  -47.955 -37.504  1.00 52.47  ? 718  THR   D N   1 
ATOM   13583 C  CA  . THR   D  1 417 ? 35.098  -46.641 -36.912  1.00 53.26  ? 718  THR   D CA  1 
ATOM   13584 C  C   . THR   D  1 417 ? 35.451  -46.672 -35.429  1.00 54.52  ? 718  THR   D C   1 
ATOM   13585 O  O   . THR   D  1 417 ? 35.904  -45.649 -34.899  1.00 50.60  ? 718  THR   D O   1 
ATOM   13586 C  CB  . THR   D  1 417 ? 33.836  -45.784 -37.104  1.00 54.18  ? 718  THR   D CB  1 
ATOM   13587 O  OG1 . THR   D  1 417 ? 32.686  -46.531 -36.690  1.00 58.44  ? 718  THR   D OG1 1 
ATOM   13588 C  CG2 . THR   D  1 417 ? 33.664  -45.383 -38.568  1.00 54.31  ? 718  THR   D CG2 1 
ATOM   13589 N  N   . HIS   D  1 418 ? 35.279  -47.801 -34.749  1.00 51.24  ? 719  HIS   D N   1 
ATOM   13590 C  CA  . HIS   D  1 418 ? 35.444  -47.836 -33.299  1.00 56.83  ? 719  HIS   D CA  1 
ATOM   13591 C  C   . HIS   D  1 418 ? 36.914  -47.934 -32.909  1.00 59.62  ? 719  HIS   D C   1 
ATOM   13592 O  O   . HIS   D  1 418 ? 37.646  -48.792 -33.413  1.00 59.83  ? 719  HIS   D O   1 
ATOM   13593 C  CB  . HIS   D  1 418 ? 34.672  -49.011 -32.704  1.00 51.16  ? 719  HIS   D CB  1 
ATOM   13594 C  CG  . HIS   D  1 418 ? 34.784  -49.113 -31.217  1.00 51.21  ? 719  HIS   D CG  1 
ATOM   13595 N  ND1 . HIS   D  1 418 ? 34.128  -48.253 -30.362  1.00 48.92  ? 719  HIS   D ND1 1 
ATOM   13596 C  CD2 . HIS   D  1 418 ? 35.478  -49.970 -30.433  1.00 48.78  ? 719  HIS   D CD2 1 
ATOM   13597 C  CE1 . HIS   D  1 418 ? 34.414  -48.576 -29.114  1.00 51.41  ? 719  HIS   D CE1 1 
ATOM   13598 N  NE2 . HIS   D  1 418 ? 35.233  -49.614 -29.129  1.00 53.93  ? 719  HIS   D NE2 1 
ATOM   13599 N  N   . VAL   D  1 419 ? 37.341  -47.055 -32.007  1.00 65.01  ? 720  VAL   D N   1 
ATOM   13600 C  CA  . VAL   D  1 419 ? 38.661  -47.146 -31.393  1.00 70.84  ? 720  VAL   D CA  1 
ATOM   13601 C  C   . VAL   D  1 419 ? 38.520  -47.891 -30.073  1.00 67.69  ? 720  VAL   D C   1 
ATOM   13602 O  O   . VAL   D  1 419 ? 37.680  -47.538 -29.236  1.00 63.41  ? 720  VAL   D O   1 
ATOM   13603 C  CB  . VAL   D  1 419 ? 39.280  -45.751 -31.189  1.00 72.27  ? 720  VAL   D CB  1 
ATOM   13604 C  CG1 . VAL   D  1 419 ? 39.916  -45.264 -32.479  1.00 71.04  ? 720  VAL   D CG1 1 
ATOM   13605 C  CG2 . VAL   D  1 419 ? 38.225  -44.756 -30.704  1.00 72.25  ? 720  VAL   D CG2 1 
ATOM   13606 N  N   . TRP   D  1 420 ? 39.333  -48.928 -29.890  1.00 71.29  ? 721  TRP   D N   1 
ATOM   13607 C  CA  . TRP   D  1 420 ? 39.214  -49.821 -28.745  1.00 69.25  ? 721  TRP   D CA  1 
ATOM   13608 C  C   . TRP   D  1 420 ? 39.987  -49.295 -27.539  1.00 74.98  ? 721  TRP   D C   1 
ATOM   13609 O  O   . TRP   D  1 420 ? 40.847  -48.418 -27.648  1.00 77.77  ? 721  TRP   D O   1 
ATOM   13610 C  CB  . TRP   D  1 420 ? 39.701  -51.220 -29.113  1.00 64.61  ? 721  TRP   D CB  1 
ATOM   13611 C  CG  . TRP   D  1 420 ? 38.799  -51.901 -30.084  1.00 68.17  ? 721  TRP   D CG  1 
ATOM   13612 C  CD1 . TRP   D  1 420 ? 38.708  -51.664 -31.425  1.00 69.36  ? 721  TRP   D CD1 1 
ATOM   13613 C  CD2 . TRP   D  1 420 ? 37.840  -52.925 -29.791  1.00 62.37  ? 721  TRP   D CD2 1 
ATOM   13614 N  NE1 . TRP   D  1 420 ? 37.756  -52.481 -31.987  1.00 62.85  ? 721  TRP   D NE1 1 
ATOM   13615 C  CE2 . TRP   D  1 420 ? 37.211  -53.268 -31.007  1.00 59.85  ? 721  TRP   D CE2 1 
ATOM   13616 C  CE3 . TRP   D  1 420 ? 37.457  -53.588 -28.620  1.00 55.28  ? 721  TRP   D CE3 1 
ATOM   13617 C  CZ2 . TRP   D  1 420 ? 36.220  -54.243 -31.085  1.00 51.42  ? 721  TRP   D CZ2 1 
ATOM   13618 C  CZ3 . TRP   D  1 420 ? 36.478  -54.559 -28.699  1.00 51.20  ? 721  TRP   D CZ3 1 
ATOM   13619 C  CH2 . TRP   D  1 420 ? 35.868  -54.876 -29.924  1.00 52.68  ? 721  TRP   D CH2 1 
ATOM   13620 N  N   . LYS   D  1 421 ? 39.664  -49.855 -26.374  1.00 78.98  ? 722  LYS   D N   1 
ATOM   13621 C  CA  . LYS   D  1 421 ? 40.242  -49.418 -25.107  1.00 83.27  ? 722  LYS   D CA  1 
ATOM   13622 C  C   . LYS   D  1 421 ? 40.964  -50.563 -24.399  1.00 83.81  ? 722  LYS   D C   1 
ATOM   13623 O  O   . LYS   D  1 421 ? 41.616  -51.399 -25.028  1.00 83.82  ? 722  LYS   D O   1 
ATOM   13624 C  CB  . LYS   D  1 421 ? 39.155  -48.850 -24.189  1.00 84.88  ? 722  LYS   D CB  1 
ATOM   13625 C  CG  . LYS   D  1 421 ? 38.008  -48.119 -24.897  1.00 85.32  ? 722  LYS   D CG  1 
ATOM   13626 C  CD  . LYS   D  1 421 ? 38.428  -46.759 -25.448  1.00 86.68  ? 722  LYS   D CD  1 
ATOM   13627 C  CE  . LYS   D  1 421 ? 37.252  -46.038 -26.120  1.00 82.31  ? 722  LYS   D CE  1 
ATOM   13628 N  NZ  . LYS   D  1 421 ? 36.158  -45.653 -25.170  1.00 74.44  ? 722  LYS   D NZ  1 
HETATM 13629 C  CHA . HEM   E  2 .   ? -13.048 -3.961  -35.712  1.00 26.36  ? 801  HEM   A CHA 1 
HETATM 13630 C  CHB . HEM   E  2 .   ? -16.879 -1.083  -36.309  1.00 25.32  ? 801  HEM   A CHB 1 
HETATM 13631 C  CHC . HEM   E  2 .   ? -17.610 -3.182  -40.601  1.00 20.22  ? 801  HEM   A CHC 1 
HETATM 13632 C  CHD . HEM   E  2 .   ? -14.326 -6.567  -39.608  1.00 19.73  ? 801  HEM   A CHD 1 
HETATM 13633 C  C1A . HEM   E  2 .   ? -13.924 -2.913  -35.577  1.00 24.58  ? 801  HEM   A C1A 1 
HETATM 13634 C  C2A . HEM   E  2 .   ? -13.815 -1.813  -34.633  1.00 28.57  ? 801  HEM   A C2A 1 
HETATM 13635 C  C3A . HEM   E  2 .   ? -14.870 -1.014  -34.804  1.00 27.77  ? 801  HEM   A C3A 1 
HETATM 13636 C  C4A . HEM   E  2 .   ? -15.694 -1.587  -35.842  1.00 28.15  ? 801  HEM   A C4A 1 
HETATM 13637 C  CMA . HEM   E  2 .   ? -15.191 0.286   -34.034  1.00 23.26  ? 801  HEM   A CMA 1 
HETATM 13638 C  CAA . HEM   E  2 .   ? -12.642 -1.578  -33.665  1.00 27.04  ? 801  HEM   A CAA 1 
HETATM 13639 C  CBA . HEM   E  2 .   ? -11.653 -0.808  -34.542  1.00 26.18  ? 801  HEM   A CBA 1 
HETATM 13640 C  CGA . HEM   E  2 .   ? -10.375 -0.445  -33.851  1.00 29.75  ? 801  HEM   A CGA 1 
HETATM 13641 O  O1A . HEM   E  2 .   ? -10.420 -0.185  -32.637  1.00 29.52  ? 801  HEM   A O1A 1 
HETATM 13642 O  O2A . HEM   E  2 .   ? -9.310  -0.400  -34.515  1.00 38.43  ? 801  HEM   A O2A 1 
HETATM 13643 C  C1B . HEM   E  2 .   ? -17.406 -1.389  -37.534  1.00 24.37  ? 801  HEM   A C1B 1 
HETATM 13644 C  C2B . HEM   E  2 .   ? -18.531 -0.728  -38.151  1.00 21.95  ? 801  HEM   A C2B 1 
HETATM 13645 C  C3B . HEM   E  2 .   ? -18.755 -1.305  -39.327  1.00 29.41  ? 801  HEM   A C3B 1 
HETATM 13646 C  C4B . HEM   E  2 .   ? -17.759 -2.357  -39.507  1.00 26.55  ? 801  HEM   A C4B 1 
HETATM 13647 C  CMB . HEM   E  2 .   ? -19.339 0.431   -37.533  1.00 23.52  ? 801  HEM   A CMB 1 
HETATM 13648 C  CAB . HEM   E  2 .   ? -19.878 -0.856  -40.298  1.00 26.06  ? 801  HEM   A CAB 1 
HETATM 13649 C  CBB . HEM   E  2 .   ? -20.212 -1.574  -41.371  1.00 24.74  ? 801  HEM   A CBB 1 
HETATM 13650 C  C1C . HEM   E  2 .   ? -16.774 -4.262  -40.742  1.00 16.77  ? 801  HEM   A C1C 1 
HETATM 13651 C  C2C . HEM   E  2 .   ? -16.631 -5.107  -41.922  1.00 27.72  ? 801  HEM   A C2C 1 
HETATM 13652 C  C3C . HEM   E  2 .   ? -15.705 -6.041  -41.641  1.00 18.84  ? 801  HEM   A C3C 1 
HETATM 13653 C  C4C . HEM   E  2 .   ? -15.260 -5.819  -40.286  1.00 21.01  ? 801  HEM   A C4C 1 
HETATM 13654 C  CMC . HEM   E  2 .   ? -17.410 -4.898  -43.239  1.00 23.01  ? 801  HEM   A CMC 1 
HETATM 13655 C  CAC . HEM   E  2 .   ? -15.173 -7.221  -42.474  1.00 20.98  ? 801  HEM   A CAC 1 
HETATM 13656 C  CBC . HEM   E  2 .   ? -15.808 -7.659  -43.565  1.00 30.99  ? 801  HEM   A CBC 1 
HETATM 13657 C  C1D . HEM   E  2 .   ? -13.691 -6.159  -38.459  1.00 19.91  ? 801  HEM   A C1D 1 
HETATM 13658 C  C2D . HEM   E  2 .   ? -12.586 -6.821  -37.811  1.00 19.92  ? 801  HEM   A C2D 1 
HETATM 13659 C  C3D . HEM   E  2 .   ? -12.233 -6.115  -36.738  1.00 19.68  ? 801  HEM   A C3D 1 
HETATM 13660 C  C4D . HEM   E  2 .   ? -13.098 -4.959  -36.667  1.00 24.42  ? 801  HEM   A C4D 1 
HETATM 13661 C  CMD . HEM   E  2 .   ? -11.916 -8.138  -38.244  1.00 19.58  ? 801  HEM   A CMD 1 
HETATM 13662 C  CAD . HEM   E  2 .   ? -11.090 -6.517  -35.776  1.00 21.46  ? 801  HEM   A CAD 1 
HETATM 13663 C  CBD . HEM   E  2 .   ? -9.806  -5.877  -36.282  1.00 21.62  ? 801  HEM   A CBD 1 
HETATM 13664 C  CGD . HEM   E  2 .   ? -8.624  -6.336  -35.463  1.00 26.38  ? 801  HEM   A CGD 1 
HETATM 13665 O  O1D . HEM   E  2 .   ? -7.580  -5.631  -35.503  1.00 26.33  ? 801  HEM   A O1D 1 
HETATM 13666 O  O2D . HEM   E  2 .   ? -8.725  -7.392  -34.776  1.00 24.36  ? 801  HEM   A O2D 1 
HETATM 13667 N  NA  . HEM   E  2 .   ? -15.086 -2.739  -36.291  1.00 27.18  ? 801  HEM   A NA  1 
HETATM 13668 N  NB  . HEM   E  2 .   ? -16.961 -2.386  -38.380  1.00 22.65  ? 801  HEM   A NB  1 
HETATM 13669 N  NC  . HEM   E  2 .   ? -15.916 -4.728  -39.796  1.00 22.36  ? 801  HEM   A NC  1 
HETATM 13670 N  ND  . HEM   E  2 .   ? -13.974 -5.016  -37.743  1.00 17.84  ? 801  HEM   A ND  1 
HETATM 13671 FE FE  . HEM   E  2 .   ? -15.682 -3.940  -37.893  1.00 22.05  ? 801  HEM   A FE  1 
HETATM 13672 N  N1  . H4B   F  3 .   ? -10.224 -1.837  -28.474  1.00 32.47  ? 802  H4B   A N1  1 
HETATM 13673 C  C2  . H4B   F  3 .   ? -10.363 -1.424  -29.765  1.00 33.39  ? 802  H4B   A C2  1 
HETATM 13674 N  N2  . H4B   F  3 .   ? -11.588 -1.305  -30.341  1.00 21.10  ? 802  H4B   A N2  1 
HETATM 13675 N  N3  . H4B   F  3 .   ? -9.279  -1.119  -30.495  1.00 27.77  ? 802  H4B   A N3  1 
HETATM 13676 C  C4  . H4B   F  3 .   ? -8.048  -1.216  -29.985  1.00 33.48  ? 802  H4B   A C4  1 
HETATM 13677 O  O4  . H4B   F  3 .   ? -7.090  -0.918  -30.713  1.00 24.26  ? 802  H4B   A O4  1 
HETATM 13678 C  C4A . H4B   F  3 .   ? -7.872  -1.643  -28.676  1.00 29.73  ? 802  H4B   A C4A 1 
HETATM 13679 C  C8A . H4B   F  3 .   ? -8.994  -1.957  -27.921  1.00 30.34  ? 802  H4B   A C8A 1 
HETATM 13680 N  N5  . H4B   F  3 .   ? -6.635  -1.759  -28.154  1.00 29.52  ? 802  H4B   A N5  1 
HETATM 13681 N  N8  . H4B   F  3 .   ? -8.877  -2.386  -26.631  1.00 24.60  ? 802  H4B   A N8  1 
HETATM 13682 C  C6  . H4B   F  3 .   ? -6.495  -2.684  -27.038  1.00 31.92  ? 802  H4B   A C6  1 
HETATM 13683 C  C7  . H4B   F  3 .   ? -7.569  -2.419  -25.988  1.00 25.04  ? 802  H4B   A C7  1 
HETATM 13684 C  C9  . H4B   F  3 .   ? -5.117  -2.608  -26.390  1.00 29.94  ? 802  H4B   A C9  1 
HETATM 13685 O  O9  . H4B   F  3 .   ? -4.833  -1.281  -25.961  1.00 26.35  ? 802  H4B   A O9  1 
HETATM 13686 C  C10 . H4B   F  3 .   ? -5.093  -3.452  -25.134  1.00 29.37  ? 802  H4B   A C10 1 
HETATM 13687 C  C11 . H4B   F  3 .   ? -3.660  -3.530  -24.626  1.00 29.05  ? 802  H4B   A C11 1 
HETATM 13688 O  O10 . H4B   F  3 .   ? -5.603  -4.749  -25.445  1.00 32.92  ? 802  H4B   A O10 1 
HETATM 13689 C  C11 . A1A0C G  4 .   ? -10.996 -0.398  -38.399  1.00 19.98  ? 803  A1A0C A C11 1 
HETATM 13690 C  C12 . A1A0C G  4 .   ? -10.299 0.775   -38.575  1.00 25.28  ? 803  A1A0C A C12 1 
HETATM 13691 C  C17 . A1A0C G  4 .   ? -8.352  -2.566  -36.793  1.00 30.02  ? 803  A1A0C A C17 1 
HETATM 13692 C  C16 . A1A0C G  4 .   ? -10.372 -1.494  -37.830  1.00 21.84  ? 803  A1A0C A C16 1 
HETATM 13693 C  C15 . A1A0C G  4 .   ? -9.044  -1.384  -37.430  1.00 22.62  ? 803  A1A0C A C15 1 
HETATM 13694 C  C14 . A1A0C G  4 .   ? -8.349  -0.195  -37.598  1.00 28.91  ? 803  A1A0C A C14 1 
HETATM 13695 C  C13 . A1A0C G  4 .   ? -8.992  0.891   -38.180  1.00 30.74  ? 803  A1A0C A C13 1 
HETATM 13696 C  C18 . A1A0C G  4 .   ? -7.102  -2.920  -37.580  1.00 24.64  ? 803  A1A0C A C18 1 
HETATM 13697 C  C20 . A1A0C G  4 .   ? -5.882  -4.912  -38.143  1.00 30.88  ? 803  A1A0C A C20 1 
HETATM 13698 C  C02 . A1A0C G  4 .   ? -14.562 0.396   -38.925  1.00 22.40  ? 803  A1A0C A C02 1 
HETATM 13699 C  C03 . A1A0C G  4 .   ? -14.909 -0.480  -39.953  1.00 18.11  ? 803  A1A0C A C03 1 
HETATM 13700 C  C04 . A1A0C G  4 .   ? -13.962 -1.353  -40.458  1.00 24.10  ? 803  A1A0C A C04 1 
HETATM 13701 C  C05 . A1A0C G  4 .   ? -12.691 -1.328  -39.935  1.00 16.79  ? 803  A1A0C A C05 1 
HETATM 13702 C  C06 . A1A0C G  4 .   ? -12.390 -0.436  -38.901  1.00 19.51  ? 803  A1A0C A C06 1 
HETATM 13703 C  C07 . A1A0C G  4 .   ? -14.297 -2.311  -41.574  1.00 30.07  ? 803  A1A0C A C07 1 
HETATM 13704 F  F12 . A1A0C G  4 .   ? -10.880 1.845   -39.130  1.00 26.88  ? 803  A1A0C A F12 1 
HETATM 13705 F  F13 . A1A0C G  4 .   ? -8.372  2.069   -38.371  1.00 27.69  ? 803  A1A0C A F13 1 
HETATM 13706 N  N01 . A1A0C G  4 .   ? -13.312 0.419   -38.436  1.00 23.34  ? 803  A1A0C A N01 1 
HETATM 13707 N  N02 . A1A0C G  4 .   ? -15.473 1.259   -38.424  1.00 22.68  ? 803  A1A0C A N02 1 
HETATM 13708 N  N19 . A1A0C G  4 .   ? -6.495  -4.144  -37.042  1.00 29.21  ? 803  A1A0C A N19 1 
HETATM 13709 C  C1  . GOL   H  5 .   ? -23.800 -9.008  -51.541  1.00 54.31  ? 804  GOL   A C1  1 
HETATM 13710 O  O1  . GOL   H  5 .   ? -24.721 -9.401  -50.545  1.00 58.03  ? 804  GOL   A O1  1 
HETATM 13711 C  C2  . GOL   H  5 .   ? -22.795 -10.131 -51.778  1.00 48.91  ? 804  GOL   A C2  1 
HETATM 13712 O  O2  . GOL   H  5 .   ? -21.786 -9.716  -52.685  1.00 38.95  ? 804  GOL   A O2  1 
HETATM 13713 C  C3  . GOL   H  5 .   ? -23.563 -11.330 -52.310  1.00 54.62  ? 804  GOL   A C3  1 
HETATM 13714 O  O3  . GOL   H  5 .   ? -24.725 -11.503 -51.530  1.00 51.15  ? 804  GOL   A O3  1 
HETATM 13715 ZN ZN  . ZN    I  6 .   ? -9.300  -15.310 -21.040  1.00 26.03  ? 805  ZN    A ZN  1 
HETATM 13716 C  C1  . GOL   J  5 .   ? 5.527   -34.467 -44.441  1.00 62.81  ? 806  GOL   A C1  1 
HETATM 13717 O  O1  . GOL   J  5 .   ? 6.632   -35.328 -44.243  1.00 62.04  ? 806  GOL   A O1  1 
HETATM 13718 C  C2  . GOL   J  5 .   ? 4.364   -34.889 -43.545  1.00 67.44  ? 806  GOL   A C2  1 
HETATM 13719 O  O2  . GOL   J  5 .   ? 4.654   -36.136 -42.960  1.00 57.92  ? 806  GOL   A O2  1 
HETATM 13720 C  C3  . GOL   J  5 .   ? 3.063   -35.003 -44.340  1.00 77.62  ? 806  GOL   A C3  1 
HETATM 13721 O  O3  . GOL   J  5 .   ? 2.110   -34.077 -43.855  1.00 83.38  ? 806  GOL   A O3  1 
HETATM 13722 C  CHA . HEM   K  2 .   ? -11.318 -3.051  -6.701   1.00 22.05  ? 801  HEM   B CHA 1 
HETATM 13723 C  CHB . HEM   K  2 .   ? -9.223  1.301   -6.302   1.00 24.28  ? 801  HEM   B CHB 1 
HETATM 13724 C  CHC . HEM   K  2 .   ? -7.650  -0.105  -1.940   1.00 25.49  ? 801  HEM   B CHC 1 
HETATM 13725 C  CHD . HEM   K  2 .   ? -8.920  -4.689  -2.806   1.00 22.41  ? 801  HEM   B CHD 1 
HETATM 13726 C  C1A . HEM   K  2 .   ? -11.016 -1.721  -6.885   1.00 24.56  ? 801  HEM   B C1A 1 
HETATM 13727 C  C2A . HEM   K  2 .   ? -11.639 -0.834  -7.843   1.00 27.81  ? 801  HEM   B C2A 1 
HETATM 13728 C  C3A . HEM   K  2 .   ? -11.077 0.377   -7.739   1.00 31.08  ? 801  HEM   B C3A 1 
HETATM 13729 C  C4A . HEM   K  2 .   ? -10.056 0.292   -6.718   1.00 28.58  ? 801  HEM   B C4A 1 
HETATM 13730 C  CMA . HEM   K  2 .   ? -11.420 1.640   -8.558   1.00 21.81  ? 801  HEM   B CMA 1 
HETATM 13731 C  CAA . HEM   K  2 .   ? -12.794 -1.252  -8.760   1.00 22.59  ? 801  HEM   B CAA 1 
HETATM 13732 C  CBA . HEM   K  2 .   ? -14.012 -1.104  -7.855   1.00 24.11  ? 801  HEM   B CBA 1 
HETATM 13733 C  CGA . HEM   K  2 .   ? -15.286 -1.296  -8.629   1.00 30.31  ? 801  HEM   B CGA 1 
HETATM 13734 O  O1A . HEM   K  2 .   ? -15.294 -0.982  -9.840   1.00 33.21  ? 801  HEM   B O1A 1 
HETATM 13735 O  O2A . HEM   K  2 .   ? -16.291 -1.746  -8.024   1.00 41.18  ? 801  HEM   B O2A 1 
HETATM 13736 C  C1B . HEM   K  2 .   ? -8.624  1.307   -5.063   1.00 28.07  ? 801  HEM   B C1B 1 
HETATM 13737 C  C2B . HEM   K  2 .   ? -7.946  2.430   -4.469   1.00 18.71  ? 801  HEM   B C2B 1 
HETATM 13738 C  C3B . HEM   K  2 .   ? -7.500  2.055   -3.262   1.00 30.23  ? 801  HEM   B C3B 1 
HETATM 13739 C  C4B . HEM   K  2 .   ? -7.898  0.668   -3.050   1.00 24.46  ? 801  HEM   B C4B 1 
HETATM 13740 C  CMB . HEM   K  2 .   ? -7.760  3.814   -5.130   1.00 17.66  ? 801  HEM   B CMB 1 
HETATM 13741 C  CAB . HEM   K  2 .   ? -6.725  3.011   -2.312   1.00 24.36  ? 801  HEM   B CAB 1 
HETATM 13742 C  CBB . HEM   K  2 .   ? -5.942  2.607   -1.311   1.00 26.67  ? 801  HEM   B CBB 1 
HETATM 13743 C  C1C . HEM   K  2 .   ? -7.862  -1.456  -1.779   1.00 27.73  ? 801  HEM   B C1C 1 
HETATM 13744 C  C2C . HEM   K  2 .   ? -7.564  -2.224  -0.585   1.00 28.53  ? 801  HEM   B C2C 1 
HETATM 13745 C  C3C . HEM   K  2 .   ? -7.926  -3.503  -0.821   1.00 26.50  ? 801  HEM   B C3C 1 
HETATM 13746 C  C4C . HEM   K  2 .   ? -8.447  -3.570  -2.172   1.00 24.66  ? 801  HEM   B C4C 1 
HETATM 13747 C  CMC . HEM   K  2 .   ? -6.967  -1.594  0.691    1.00 22.83  ? 801  HEM   B CMC 1 
HETATM 13748 C  CAC . HEM   K  2 .   ? -7.809  -4.752  0.075    1.00 26.89  ? 801  HEM   B CAC 1 
HETATM 13749 C  CBC . HEM   K  2 .   ? -6.986  -4.793  1.127    1.00 35.21  ? 801  HEM   B CBC 1 
HETATM 13750 C  C1D . HEM   K  2 .   ? -9.701  -4.645  -3.936   1.00 28.37  ? 801  HEM   B C1D 1 
HETATM 13751 C  C2D . HEM   K  2 .   ? -10.370 -5.764  -4.565   1.00 21.65  ? 801  HEM   B C2D 1 
HETATM 13752 C  C3D . HEM   K  2 .   ? -11.017 -5.312  -5.644   1.00 22.03  ? 801  HEM   B C3D 1 
HETATM 13753 C  C4D . HEM   K  2 .   ? -10.794 -3.893  -5.742   1.00 21.26  ? 801  HEM   B C4D 1 
HETATM 13754 C  CMD . HEM   K  2 .   ? -10.328 -7.226  -4.097   1.00 17.81  ? 801  HEM   B CMD 1 
HETATM 13755 C  CAD . HEM   K  2 .   ? -11.853 -6.168  -6.610   1.00 24.31  ? 801  HEM   B CAD 1 
HETATM 13756 C  CBD . HEM   K  2 .   ? -13.276 -6.339  -6.091   1.00 28.46  ? 801  HEM   B CBD 1 
HETATM 13757 C  CGD . HEM   K  2 .   ? -14.022 -7.283  -7.015   1.00 27.70  ? 801  HEM   B CGD 1 
HETATM 13758 O  O1D . HEM   K  2 .   ? -13.378 -8.133  -7.679   1.00 25.47  ? 801  HEM   B O1D 1 
HETATM 13759 O  O2D . HEM   K  2 .   ? -15.272 -7.196  -7.078   1.00 27.79  ? 801  HEM   B O2D 1 
HETATM 13760 N  NA  . HEM   K  2 .   ? -10.050 -0.996  -6.220   1.00 30.82  ? 801  HEM   B NA  1 
HETATM 13761 N  NB  . HEM   K  2 .   ? -8.577  0.237   -4.175   1.00 25.73  ? 801  HEM   B NB  1 
HETATM 13762 N  NC  . HEM   K  2 .   ? -8.392  -2.313  -2.713   1.00 24.07  ? 801  HEM   B NC  1 
HETATM 13763 N  ND  . HEM   K  2 .   ? -9.982  -3.508  -4.682   1.00 23.82  ? 801  HEM   B ND  1 
HETATM 13764 FE FE  . HEM   K  2 .   ? -8.916  -1.750  -4.631   1.00 22.58  ? 801  HEM   B FE  1 
HETATM 13765 N  N1  . H4B   L  3 .   ? -14.824 -2.725  -14.002  1.00 26.07  ? 802  H4B   B N1  1 
HETATM 13766 C  C2  . H4B   L  3 .   ? -14.911 -2.294  -12.718  1.00 26.74  ? 802  H4B   B C2  1 
HETATM 13767 N  N2  . H4B   L  3 .   ? -13.888 -1.603  -12.161  1.00 19.68  ? 802  H4B   B N2  1 
HETATM 13768 N  N3  . H4B   L  3 .   ? -16.015 -2.537  -11.987  1.00 24.12  ? 802  H4B   B N3  1 
HETATM 13769 C  C4  . H4B   L  3 .   ? -17.043 -3.222  -12.516  1.00 29.21  ? 802  H4B   B C4  1 
HETATM 13770 O  O4  . H4B   L  3 .   ? -18.055 -3.426  -11.816  1.00 20.57  ? 802  H4B   B O4  1 
HETATM 13771 C  C4A . H4B   L  3 .   ? -16.968 -3.681  -13.826  1.00 23.02  ? 802  H4B   B C4A 1 
HETATM 13772 C  C8A . H4B   L  3 .   ? -15.829 -3.418  -14.567  1.00 22.03  ? 802  H4B   B C8A 1 
HETATM 13773 N  N5  . H4B   L  3 .   ? -17.988 -4.369  -14.378  1.00 23.85  ? 802  H4B   B N5  1 
HETATM 13774 N  N8  . H4B   L  3 .   ? -15.717 -3.850  -15.858  1.00 26.67  ? 802  H4B   B N8  1 
HETATM 13775 C  C6  . H4B   L  3 .   ? -17.631 -5.263  -15.473  1.00 29.15  ? 802  H4B   B C6  1 
HETATM 13776 C  C7  . H4B   L  3 .   ? -16.847 -4.495  -16.532  1.00 25.87  ? 802  H4B   B C7  1 
HETATM 13777 C  C9  . H4B   L  3 .   ? -18.849 -5.949  -16.093  1.00 27.65  ? 802  H4B   B C9  1 
HETATM 13778 O  O9  . H4B   L  3 .   ? -19.824 -4.974  -16.463  1.00 28.48  ? 802  H4B   B O9  1 
HETATM 13779 C  C10 . H4B   L  3 .   ? -18.468 -6.738  -17.343  1.00 25.24  ? 802  H4B   B C10 1 
HETATM 13780 C  C11 . H4B   L  3 .   ? -19.685 -7.473  -17.884  1.00 22.07  ? 802  H4B   B C11 1 
HETATM 13781 O  O10 . H4B   L  3 .   ? -17.472 -7.714  -17.006  1.00 31.55  ? 802  H4B   B O10 1 
HETATM 13782 C  C11 . A1A0C M  4 .   ? -14.788 -0.871  -4.112   1.00 19.75  ? 803  A1A0C B C11 1 
HETATM 13783 C  C12 . A1A0C M  4 .   ? -15.916 -0.114  -3.932   1.00 18.49  ? 803  A1A0C B C12 1 
HETATM 13784 C  C17 . A1A0C M  4 .   ? -16.191 -4.053  -5.581   1.00 30.16  ? 803  A1A0C B C17 1 
HETATM 13785 C  C16 . A1A0C M  4 .   ? -14.856 -2.157  -4.628   1.00 20.76  ? 803  A1A0C B C16 1 
HETATM 13786 C  C15 . A1A0C M  4 .   ? -16.099 -2.657  -4.995   1.00 19.88  ? 803  A1A0C B C15 1 
HETATM 13787 C  C14 . A1A0C M  4 .   ? -17.241 -1.876  -4.818   1.00 28.37  ? 803  A1A0C B C14 1 
HETATM 13788 C  C13 . A1A0C M  4 .   ? -17.142 -0.600  -4.274   1.00 26.77  ? 803  A1A0C B C13 1 
HETATM 13789 C  C18 . A1A0C M  4 .   ? -16.929 -4.960  -4.610   1.00 29.33  ? 803  A1A0C B C18 1 
HETATM 13790 C  C20 . A1A0C M  4 .   ? -17.275 -7.266  -4.039   1.00 31.04  ? 803  A1A0C B C20 1 
HETATM 13791 C  C02 . A1A0C M  4 .   ? -11.981 1.463   -3.676   1.00 24.32  ? 803  A1A0C B C02 1 
HETATM 13792 C  C03 . A1A0C M  4 .   ? -11.260 0.857   -2.657   1.00 23.35  ? 803  A1A0C B C03 1 
HETATM 13793 C  C04 . A1A0C M  4 .   ? -11.714 -0.333  -2.136   1.00 20.52  ? 803  A1A0C B C04 1 
HETATM 13794 C  C05 . A1A0C M  4 .   ? -12.870 -0.889  -2.630   1.00 22.58  ? 803  A1A0C B C05 1 
HETATM 13795 C  C06 . A1A0C M  4 .   ? -13.533 -0.259  -3.661   1.00 19.98  ? 803  A1A0C B C06 1 
HETATM 13796 C  C07 . A1A0C M  4 .   ? -10.977 -1.030  -1.021   1.00 23.09  ? 803  A1A0C B C07 1 
HETATM 13797 F  F12 . A1A0C M  4 .   ? -15.839 1.125   -3.437   1.00 25.62  ? 803  A1A0C B F12 1 
HETATM 13798 F  F13 . A1A0C M  4 .   ? -18.195 0.205   -4.070   1.00 32.69  ? 803  A1A0C B F13 1 
HETATM 13799 N  N01 . A1A0C M  4 .   ? -13.113 0.909   -4.139   1.00 20.50  ? 803  A1A0C B N01 1 
HETATM 13800 N  N02 . A1A0C M  4 .   ? -11.557 2.623   -4.212   1.00 21.19  ? 803  A1A0C B N02 1 
HETATM 13801 N  N19 . A1A0C M  4 .   ? -17.003 -6.332  -5.149   1.00 34.26  ? 803  A1A0C B N19 1 
HETATM 13802 C  C1  . GOL   N  5 .   ? 5.121   -16.271 -5.430   1.00 63.25  ? 804  GOL   B C1  1 
HETATM 13803 O  O1  . GOL   N  5 .   ? 3.835   -16.774 -5.120   1.00 64.66  ? 804  GOL   B O1  1 
HETATM 13804 C  C2  . GOL   N  5 .   ? 5.436   -15.061 -4.548   1.00 62.87  ? 804  GOL   B C2  1 
HETATM 13805 O  O2  . GOL   N  5 .   ? 4.258   -14.431 -4.080   1.00 57.45  ? 804  GOL   B O2  1 
HETATM 13806 C  C3  . GOL   N  5 .   ? 6.341   -14.061 -5.265   1.00 61.73  ? 804  GOL   B C3  1 
HETATM 13807 O  O3  . GOL   N  5 .   ? 6.495   -12.909 -4.455   1.00 65.99  ? 804  GOL   B O3  1 
HETATM 13808 C  CHA . HEM   O  2 .   ? 14.473  -54.223 -74.774  1.00 20.14  ? 801  HEM   C CHA 1 
HETATM 13809 C  CHB . HEM   O  2 .   ? 16.578  -58.576 -75.191  1.00 22.89  ? 801  HEM   C CHB 1 
HETATM 13810 C  CHC . HEM   O  2 .   ? 18.215  -57.171 -79.539  1.00 25.06  ? 801  HEM   C CHC 1 
HETATM 13811 C  CHD . HEM   O  2 .   ? 16.877  -52.605 -78.676  1.00 20.33  ? 801  HEM   C CHD 1 
HETATM 13812 C  C1A . HEM   O  2 .   ? 14.778  -55.555 -74.601  1.00 22.76  ? 801  HEM   C C1A 1 
HETATM 13813 C  C2A . HEM   O  2 .   ? 14.152  -56.462 -73.653  1.00 25.72  ? 801  HEM   C C2A 1 
HETATM 13814 C  C3A . HEM   O  2 .   ? 14.720  -57.663 -73.766  1.00 23.93  ? 801  HEM   C C3A 1 
HETATM 13815 C  C4A . HEM   O  2 .   ? 15.747  -57.563 -74.782  1.00 22.99  ? 801  HEM   C C4A 1 
HETATM 13816 C  CMA . HEM   O  2 .   ? 14.383  -58.939 -72.971  1.00 18.00  ? 801  HEM   C CMA 1 
HETATM 13817 C  CAA . HEM   O  2 .   ? 12.991  -56.084 -72.737  1.00 24.70  ? 801  HEM   C CAA 1 
HETATM 13818 C  CBA . HEM   O  2 .   ? 11.788  -56.280 -73.652  1.00 21.93  ? 801  HEM   C CBA 1 
HETATM 13819 C  CGA . HEM   O  2 .   ? 10.507  -55.982 -72.933  1.00 32.74  ? 801  HEM   C CGA 1 
HETATM 13820 O  O1A . HEM   O  2 .   ? 10.430  -56.263 -71.715  1.00 33.25  ? 801  HEM   C O1A 1 
HETATM 13821 O  O2A . HEM   O  2 .   ? 9.556   -55.484 -73.592  1.00 41.53  ? 801  HEM   C O2A 1 
HETATM 13822 C  C1B . HEM   O  2 .   ? 17.189  -58.583 -76.425  1.00 28.94  ? 801  HEM   C C1B 1 
HETATM 13823 C  C2B . HEM   O  2 .   ? 17.870  -59.706 -77.014  1.00 18.42  ? 801  HEM   C C2B 1 
HETATM 13824 C  C3B . HEM   O  2 .   ? 18.331  -59.333 -78.210  1.00 27.16  ? 801  HEM   C C3B 1 
HETATM 13825 C  C4B . HEM   O  2 .   ? 17.949  -57.945 -78.423  1.00 24.88  ? 801  HEM   C C4B 1 
HETATM 13826 C  CMB . HEM   O  2 .   ? 18.043  -61.097 -76.378  1.00 16.97  ? 801  HEM   C CMB 1 
HETATM 13827 C  CAB . HEM   O  2 .   ? 19.108  -60.301 -79.137  1.00 23.17  ? 801  HEM   C CAB 1 
HETATM 13828 C  CBB . HEM   O  2 .   ? 19.834  -59.909 -80.186  1.00 23.65  ? 801  HEM   C CBB 1 
HETATM 13829 C  C1C . HEM   O  2 .   ? 17.974  -55.827 -79.706  1.00 27.78  ? 801  HEM   C C1C 1 
HETATM 13830 C  C2C . HEM   O  2 .   ? 18.236  -55.062 -80.915  1.00 25.20  ? 801  HEM   C C2C 1 
HETATM 13831 C  C3C . HEM   O  2 .   ? 17.853  -53.799 -80.680  1.00 25.47  ? 801  HEM   C C3C 1 
HETATM 13832 C  C4C . HEM   O  2 .   ? 17.356  -53.724 -79.315  1.00 22.10  ? 801  HEM   C C4C 1 
HETATM 13833 C  CMC . HEM   O  2 .   ? 18.817  -55.667 -82.206  1.00 23.69  ? 801  HEM   C CMC 1 
HETATM 13834 C  CAC . HEM   O  2 .   ? 17.958  -52.575 -81.608  1.00 27.55  ? 801  HEM   C CAC 1 
HETATM 13835 C  CBC . HEM   O  2 .   ? 18.952  -52.478 -82.500  1.00 31.18  ? 801  HEM   C CBC 1 
HETATM 13836 C  C1D . HEM   O  2 .   ? 16.101  -52.644 -77.538  1.00 30.01  ? 801  HEM   C C1D 1 
HETATM 13837 C  C2D . HEM   O  2 .   ? 15.429  -51.521 -76.925  1.00 24.59  ? 801  HEM   C C2D 1 
HETATM 13838 C  C3D . HEM   O  2 .   ? 14.775  -51.965 -75.843  1.00 27.08  ? 801  HEM   C C3D 1 
HETATM 13839 C  C4D . HEM   O  2 .   ? 14.996  -53.384 -75.735  1.00 25.40  ? 801  HEM   C C4D 1 
HETATM 13840 C  CMD . HEM   O  2 .   ? 15.470  -50.065 -77.424  1.00 17.27  ? 801  HEM   C CMD 1 
HETATM 13841 C  CAD . HEM   O  2 .   ? 13.927  -51.104 -74.890  1.00 21.17  ? 801  HEM   C CAD 1 
HETATM 13842 C  CBD . HEM   O  2 .   ? 12.536  -50.883 -75.481  1.00 26.48  ? 801  HEM   C CBD 1 
HETATM 13843 C  CGD . HEM   O  2 .   ? 11.733  -50.024 -74.528  1.00 28.29  ? 801  HEM   C CGD 1 
HETATM 13844 O  O1D . HEM   O  2 .   ? 10.483  -50.138 -74.497  1.00 28.48  ? 801  HEM   C O1D 1 
HETATM 13845 O  O2D . HEM   O  2 .   ? 12.342  -49.225 -73.783  1.00 25.69  ? 801  HEM   C O2D 1 
HETATM 13846 N  NA  . HEM   O  2 .   ? 15.758  -56.268 -75.261  1.00 25.79  ? 801  HEM   C NA  1 
HETATM 13847 N  NB  . HEM   O  2 .   ? 17.258  -57.515 -77.302  1.00 22.83  ? 801  HEM   C NB  1 
HETATM 13848 N  NC  . HEM   O  2 .   ? 17.445  -54.975 -78.758  1.00 22.42  ? 801  HEM   C NC  1 
HETATM 13849 N  ND  . HEM   O  2 .   ? 15.816  -53.775 -76.783  1.00 23.76  ? 801  HEM   C ND  1 
HETATM 13850 FE FE  . HEM   O  2 .   ? 16.864  -55.551 -76.867  1.00 22.73  ? 801  HEM   C FE  1 
HETATM 13851 N  N1  . H4B   P  3 .   ? 10.977  -54.564 -67.528  1.00 23.07  ? 802  H4B   C N1  1 
HETATM 13852 C  C2  . H4B   P  3 .   ? 10.884  -54.995 -68.812  1.00 28.43  ? 802  H4B   C C2  1 
HETATM 13853 N  N2  . H4B   P  3 .   ? 11.904  -55.687 -69.386  1.00 21.32  ? 802  H4B   C N2  1 
HETATM 13854 N  N3  . H4B   P  3 .   ? 9.771   -54.747 -69.533  1.00 22.81  ? 802  H4B   C N3  1 
HETATM 13855 C  C4  . H4B   P  3 .   ? 8.741   -54.071 -69.001  1.00 27.84  ? 802  H4B   C C4  1 
HETATM 13856 O  O4  . H4B   P  3 .   ? 7.723   -53.867 -69.702  1.00 21.39  ? 802  H4B   C O4  1 
HETATM 13857 C  C4A . H4B   P  3 .   ? 8.821   -53.615 -67.695  1.00 23.57  ? 802  H4B   C C4A 1 
HETATM 13858 C  C8A . H4B   P  3 .   ? 9.964   -53.879 -66.956  1.00 26.66  ? 802  H4B   C C8A 1 
HETATM 13859 N  N5  . H4B   P  3 .   ? 7.796   -52.927 -67.148  1.00 27.08  ? 802  H4B   C N5  1 
HETATM 13860 N  N8  . H4B   P  3 .   ? 10.077  -53.451 -65.661  1.00 26.41  ? 802  H4B   C N8  1 
HETATM 13861 C  C6  . H4B   P  3 .   ? 8.152   -52.050 -66.031  1.00 31.54  ? 802  H4B   C C6  1 
HETATM 13862 C  C7  . H4B   P  3 .   ? 8.940   -52.824 -64.976  1.00 23.92  ? 802  H4B   C C7  1 
HETATM 13863 C  C9  . H4B   P  3 .   ? 6.933   -51.390 -65.400  1.00 25.74  ? 802  H4B   C C9  1 
HETATM 13864 O  O9  . H4B   P  3 .   ? 5.992   -52.377 -64.997  1.00 28.62  ? 802  H4B   C O9  1 
HETATM 13865 C  C10 . H4B   P  3 .   ? 7.304   -50.558 -64.187  1.00 25.61  ? 802  H4B   C C10 1 
HETATM 13866 C  C11 . H4B   P  3 .   ? 6.055   -49.851 -63.686  1.00 23.52  ? 802  H4B   C C11 1 
HETATM 13867 O  O10 . H4B   P  3 .   ? 8.271   -49.581 -64.601  1.00 29.84  ? 802  H4B   C O10 1 
HETATM 13868 C  C11 . A1A0C Q  4 .   ? 11.068  -56.409 -77.403  1.00 22.90  ? 803  A1A0C C C11 1 
HETATM 13869 C  C12 . A1A0C Q  4 .   ? 9.925   -57.157 -77.590  1.00 20.49  ? 803  A1A0C C C12 1 
HETATM 13870 C  C17 . A1A0C Q  4 .   ? 9.682   -53.218 -75.913  1.00 28.36  ? 803  A1A0C C C17 1 
HETATM 13871 C  C16 . A1A0C Q  4 .   ? 11.008  -55.128 -76.869  1.00 21.53  ? 803  A1A0C C C16 1 
HETATM 13872 C  C15 . A1A0C Q  4 .   ? 9.770   -54.614 -76.506  1.00 23.10  ? 803  A1A0C C C15 1 
HETATM 13873 C  C14 . A1A0C Q  4 .   ? 8.623   -55.382 -76.693  1.00 26.10  ? 803  A1A0C C C14 1 
HETATM 13874 C  C13 . A1A0C Q  4 .   ? 8.705   -56.657 -77.238  1.00 25.22  ? 803  A1A0C C C13 1 
HETATM 13875 C  C18 . A1A0C Q  4 .   ? 9.006   -52.292 -76.909  1.00 28.44  ? 803  A1A0C C C18 1 
HETATM 13876 C  C20 . A1A0C Q  4 .   ? 8.580   -49.978 -77.449  1.00 28.37  ? 803  A1A0C C C20 1 
HETATM 13877 C  C02 . A1A0C Q  4 .   ? 13.861  -58.779 -77.827  1.00 25.25  ? 803  A1A0C C C02 1 
HETATM 13878 C  C03 . A1A0C Q  4 .   ? 14.585  -58.184 -78.864  1.00 21.40  ? 803  A1A0C C C03 1 
HETATM 13879 C  C04 . A1A0C Q  4 .   ? 14.142  -56.985 -79.399  1.00 24.86  ? 803  A1A0C C C04 1 
HETATM 13880 C  C05 . A1A0C Q  4 .   ? 12.992  -56.420 -78.899  1.00 22.40  ? 803  A1A0C C C05 1 
HETATM 13881 C  C06 . A1A0C Q  4 .   ? 12.318  -57.036 -77.857  1.00 21.61  ? 803  A1A0C C C06 1 
HETATM 13882 C  C07 . A1A0C Q  4 .   ? 14.882  -56.296 -80.522  1.00 26.01  ? 803  A1A0C C C07 1 
HETATM 13883 F  F12 . A1A0C Q  4 .   ? 9.978   -58.395 -78.107  1.00 25.21  ? 803  A1A0C C F12 1 
HETATM 13884 F  F13 . A1A0C Q  4 .   ? 7.632   -57.443 -77.445  1.00 32.14  ? 803  A1A0C C F13 1 
HETATM 13885 N  N01 . A1A0C Q  4 .   ? 12.740  -58.205 -77.356  1.00 21.67  ? 803  A1A0C C N01 1 
HETATM 13886 N  N02 . A1A0C Q  4 .   ? 14.263  -59.945 -77.283  1.00 21.20  ? 803  A1A0C C N02 1 
HETATM 13887 N  N19 . A1A0C Q  4 .   ? 8.968   -50.916 -76.373  1.00 34.91  ? 803  A1A0C C N19 1 
HETATM 13888 C  C1  . GOL   R  5 .   ? 29.237  -41.480 -76.537  1.00 59.46  ? 804  GOL   C C1  1 
HETATM 13889 O  O1  . GOL   R  5 .   ? 29.786  -40.268 -76.071  1.00 64.95  ? 804  GOL   C O1  1 
HETATM 13890 C  C2  . GOL   R  5 .   ? 30.367  -42.308 -77.145  1.00 58.06  ? 804  GOL   C C2  1 
HETATM 13891 O  O2  . GOL   R  5 .   ? 29.953  -43.617 -77.469  1.00 56.32  ? 804  GOL   C O2  1 
HETATM 13892 C  C3  . GOL   R  5 .   ? 31.571  -42.354 -76.209  1.00 63.45  ? 804  GOL   C C3  1 
HETATM 13893 O  O3  . GOL   R  5 .   ? 32.387  -43.453 -76.568  1.00 71.61  ? 804  GOL   C O3  1 
HETATM 13894 C  C1  . GOL   S  5 .   ? 26.975  -55.664 -90.372  1.00 50.80  ? 805  GOL   C C1  1 
HETATM 13895 O  O1  . GOL   S  5 .   ? 27.016  -55.509 -88.962  1.00 51.44  ? 805  GOL   C O1  1 
HETATM 13896 C  C2  . GOL   S  5 .   ? 27.228  -54.330 -91.070  1.00 52.83  ? 805  GOL   C C2  1 
HETATM 13897 O  O2  . GOL   S  5 .   ? 28.355  -53.695 -90.508  1.00 58.82  ? 805  GOL   C O2  1 
HETATM 13898 C  C3  . GOL   S  5 .   ? 26.020  -53.408 -90.925  1.00 41.74  ? 805  GOL   C C3  1 
HETATM 13899 O  O3  . GOL   S  5 .   ? 24.909  -53.913 -91.632  1.00 42.89  ? 805  GOL   C O3  1 
HETATM 13900 ZN ZN  . ZN    T  6 .   ? 16.500  -41.988 -60.469  1.00 26.03  ? 806  ZN    C ZN  1 
HETATM 13901 C  CHA . HEM   U  2 .   ? 12.734  -53.314 -45.823  1.00 24.97  ? 801  HEM   D CHA 1 
HETATM 13902 C  CHB . HEM   U  2 .   ? 8.891   -56.175 -45.202  1.00 23.77  ? 801  HEM   D CHB 1 
HETATM 13903 C  CHC . HEM   U  2 .   ? 8.161   -54.097 -40.900  1.00 17.14  ? 801  HEM   D CHC 1 
HETATM 13904 C  CHD . HEM   U  2 .   ? 11.468  -50.738 -41.902  1.00 19.70  ? 801  HEM   D CHD 1 
HETATM 13905 C  C1A . HEM   U  2 .   ? 11.863  -54.364 -45.948  1.00 21.19  ? 801  HEM   D C1A 1 
HETATM 13906 C  C2A . HEM   U  2 .   ? 11.955  -55.475 -46.886  1.00 27.04  ? 801  HEM   D C2A 1 
HETATM 13907 C  C3A . HEM   U  2 .   ? 10.894  -56.264 -46.697  1.00 29.84  ? 801  HEM   D C3A 1 
HETATM 13908 C  C4A . HEM   U  2 .   ? 10.081  -55.677 -45.665  1.00 25.27  ? 801  HEM   D C4A 1 
HETATM 13909 C  CMA . HEM   U  2 .   ? 10.547  -57.570 -47.437  1.00 26.60  ? 801  HEM   D CMA 1 
HETATM 13910 C  CAA . HEM   U  2 .   ? 13.112  -55.742 -47.864  1.00 25.97  ? 801  HEM   D CAA 1 
HETATM 13911 C  CBA . HEM   U  2 .   ? 14.176  -56.369 -46.962  1.00 28.65  ? 801  HEM   D CBA 1 
HETATM 13912 C  CGA . HEM   U  2 .   ? 15.390  -56.820 -47.710  1.00 28.15  ? 801  HEM   D CGA 1 
HETATM 13913 O  O1A . HEM   U  2 .   ? 15.250  -57.174 -48.890  1.00 32.12  ? 801  HEM   D O1A 1 
HETATM 13914 O  O2A . HEM   U  2 .   ? 16.497  -56.837 -47.127  1.00 35.90  ? 801  HEM   D O2A 1 
HETATM 13915 C  C1B . HEM   U  2 .   ? 8.358   -55.876 -43.973  1.00 18.58  ? 801  HEM   D C1B 1 
HETATM 13916 C  C2B . HEM   U  2 .   ? 7.248   -56.558 -43.358  1.00 22.45  ? 801  HEM   D C2B 1 
HETATM 13917 C  C3B . HEM   U  2 .   ? 7.020   -55.990 -42.166  1.00 26.37  ? 801  HEM   D C3B 1 
HETATM 13918 C  C4B . HEM   U  2 .   ? 8.005   -54.923 -41.988  1.00 24.56  ? 801  HEM   D C4B 1 
HETATM 13919 C  CMB . HEM   U  2 .   ? 6.457   -57.726 -43.986  1.00 25.31  ? 801  HEM   D CMB 1 
HETATM 13920 C  CAB . HEM   U  2 .   ? 5.893   -56.457 -41.212  1.00 24.09  ? 801  HEM   D CAB 1 
HETATM 13921 C  CBB . HEM   U  2 .   ? 5.526   -55.743 -40.142  1.00 28.28  ? 801  HEM   D CBB 1 
HETATM 13922 C  C1C . HEM   U  2 .   ? 9.006   -53.021 -40.756  1.00 20.19  ? 801  HEM   D C1C 1 
HETATM 13923 C  C2C . HEM   U  2 .   ? 9.146   -52.159 -39.588  1.00 25.59  ? 801  HEM   D C2C 1 
HETATM 13924 C  C3C . HEM   U  2 .   ? 10.079  -51.225 -39.871  1.00 22.46  ? 801  HEM   D C3C 1 
HETATM 13925 C  C4C . HEM   U  2 .   ? 10.531  -51.472 -41.217  1.00 20.00  ? 801  HEM   D C4C 1 
HETATM 13926 C  CMC . HEM   U  2 .   ? 8.358   -52.371 -38.277  1.00 22.32  ? 801  HEM   D CMC 1 
HETATM 13927 C  CAC . HEM   U  2 .   ? 10.631  -50.042 -39.037  1.00 21.59  ? 801  HEM   D CAC 1 
HETATM 13928 C  CBC . HEM   U  2 .   ? 10.039  -49.626 -37.910  1.00 36.17  ? 801  HEM   D CBC 1 
HETATM 13929 C  C1D . HEM   U  2 .   ? 12.106  -51.141 -43.053  1.00 22.23  ? 801  HEM   D C1D 1 
HETATM 13930 C  C2D . HEM   U  2 .   ? 13.217  -50.474 -43.690  1.00 20.29  ? 801  HEM   D C2D 1 
HETATM 13931 C  C3D . HEM   U  2 .   ? 13.561  -51.173 -44.773  1.00 22.00  ? 801  HEM   D C3D 1 
HETATM 13932 C  C4D . HEM   U  2 .   ? 12.687  -52.321 -44.862  1.00 25.68  ? 801  HEM   D C4D 1 
HETATM 13933 C  CMD . HEM   U  2 .   ? 13.890  -49.165 -43.238  1.00 18.24  ? 801  HEM   D CMD 1 
HETATM 13934 C  CAD . HEM   U  2 .   ? 14.704  -50.783 -45.734  1.00 21.94  ? 801  HEM   D CAD 1 
HETATM 13935 C  CBD . HEM   U  2 .   ? 15.984  -51.431 -45.223  1.00 21.58  ? 801  HEM   D CBD 1 
HETATM 13936 C  CGD . HEM   U  2 .   ? 17.167  -51.020 -46.067  1.00 30.39  ? 801  HEM   D CGD 1 
HETATM 13937 O  O1D . HEM   U  2 .   ? 18.218  -51.710 -45.983  1.00 27.78  ? 801  HEM   D O1D 1 
HETATM 13938 O  O2D . HEM   U  2 .   ? 17.059  -50.011 -46.820  1.00 26.22  ? 801  HEM   D O2D 1 
HETATM 13939 N  NA  . HEM   U  2 .   ? 10.702  -54.525 -45.231  1.00 25.67  ? 801  HEM   D NA  1 
HETATM 13940 N  NB  . HEM   U  2 .   ? 8.795   -54.880 -43.131  1.00 22.49  ? 801  HEM   D NB  1 
HETATM 13941 N  NC  . HEM   U  2 .   ? 9.866   -52.565 -41.706  1.00 20.40  ? 801  HEM   D NC  1 
HETATM 13942 N  ND  . HEM   U  2 .   ? 11.804  -52.268 -43.800  1.00 19.53  ? 801  HEM   D ND  1 
HETATM 13943 FE FE  . HEM   U  2 .   ? 10.085  -53.353 -43.621  1.00 21.34  ? 801  HEM   D FE  1 
HETATM 13944 N  N1  . H4B   V  3 .   ? 15.572  -55.469 -53.001  1.00 33.91  ? 802  H4B   D N1  1 
HETATM 13945 C  C2  . H4B   V  3 .   ? 15.457  -55.900 -51.716  1.00 32.90  ? 802  H4B   D C2  1 
HETATM 13946 N  N2  . H4B   V  3 .   ? 14.236  -56.045 -51.126  1.00 19.79  ? 802  H4B   D N2  1 
HETATM 13947 N  N3  . H4B   V  3 .   ? 16.555  -56.209 -50.995  1.00 26.42  ? 802  H4B   D N3  1 
HETATM 13948 C  C4  . H4B   V  3 .   ? 17.778  -56.080 -51.517  1.00 29.40  ? 802  H4B   D C4  1 
HETATM 13949 O  O4  . H4B   V  3 .   ? 18.762  -56.370 -50.825  1.00 22.24  ? 802  H4B   D O4  1 
HETATM 13950 C  C4A . H4B   V  3 .   ? 17.927  -55.631 -52.816  1.00 27.30  ? 802  H4B   D C4A 1 
HETATM 13951 C  C8A . H4B   V  3 .   ? 16.797  -55.325 -53.557  1.00 30.33  ? 802  H4B   D C8A 1 
HETATM 13952 N  N5  . H4B   V  3 .   ? 19.160  -55.492 -53.337  1.00 27.40  ? 802  H4B   D N5  1 
HETATM 13953 N  N8  . H4B   V  3 .   ? 16.909  -54.873 -54.835  1.00 29.65  ? 802  H4B   D N8  1 
HETATM 13954 C  C6  . H4B   V  3 .   ? 19.285  -54.577 -54.464  1.00 25.87  ? 802  H4B   D C6  1 
HETATM 13955 C  C7  . H4B   V  3 .   ? 18.204  -54.850 -55.507  1.00 24.48  ? 802  H4B   D C7  1 
HETATM 13956 C  C9  . H4B   V  3 .   ? 20.652  -54.677 -55.130  1.00 28.68  ? 802  H4B   D C9  1 
HETATM 13957 O  O9  . H4B   V  3 .   ? 20.935  -56.026 -55.493  1.00 28.81  ? 802  H4B   D O9  1 
HETATM 13958 C  C10 . H4B   V  3 .   ? 20.673  -53.843 -56.398  1.00 25.39  ? 802  H4B   D C10 1 
HETATM 13959 C  C11 . H4B   V  3 .   ? 22.089  -53.814 -56.970  1.00 27.08  ? 802  H4B   D C11 1 
HETATM 13960 O  O10 . H4B   V  3 .   ? 20.227  -52.524 -56.054  1.00 28.98  ? 802  H4B   D O10 1 
HETATM 13961 C  C11 . A1A0C W  4 .   ? 14.816  -56.912 -43.138  1.00 22.09  ? 803  A1A0C D C11 1 
HETATM 13962 C  C12 . A1A0C W  4 .   ? 15.478  -58.100 -42.939  1.00 22.33  ? 803  A1A0C D C12 1 
HETATM 13963 C  C17 . A1A0C W  4 .   ? 17.545  -54.841 -44.787  1.00 31.44  ? 803  A1A0C D C17 1 
HETATM 13964 C  C16 . A1A0C W  4 .   ? 15.471  -55.831 -43.729  1.00 22.22  ? 803  A1A0C D C16 1 
HETATM 13965 C  C15 . A1A0C W  4 .   ? 16.794  -55.976 -44.128  1.00 27.97  ? 803  A1A0C D C15 1 
HETATM 13966 C  C14 . A1A0C W  4 .   ? 17.450  -57.186 -43.936  1.00 37.61  ? 803  A1A0C D C14 1 
HETATM 13967 C  C13 . A1A0C W  4 .   ? 16.781  -58.240 -43.328  1.00 32.71  ? 803  A1A0C D C13 1 
HETATM 13968 C  C18 . A1A0C W  4 .   ? 18.443  -54.175 -43.760  1.00 27.56  ? 803  A1A0C D C18 1 
HETATM 13969 C  C20 . A1A0C W  4 .   ? 19.932  -52.368 -43.341  1.00 33.86  ? 803  A1A0C D C20 1 
HETATM 13970 C  C02 . A1A0C W  4 .   ? 11.231  -57.693 -42.587  1.00 22.54  ? 803  A1A0C D C02 1 
HETATM 13971 C  C03 . A1A0C W  4 .   ? 10.899  -56.778 -41.588  1.00 19.99  ? 803  A1A0C D C03 1 
HETATM 13972 C  C04 . A1A0C W  4 .   ? 11.864  -55.898 -41.110  1.00 21.70  ? 803  A1A0C D C04 1 
HETATM 13973 C  C05 . A1A0C W  4 .   ? 13.136  -55.941 -41.625  1.00 18.27  ? 803  A1A0C D C05 1 
HETATM 13974 C  C06 . A1A0C W  4 .   ? 13.424  -56.858 -42.634  1.00 17.67  ? 803  A1A0C D C06 1 
HETATM 13975 C  C07 . A1A0C W  4 .   ? 11.556  -54.892 -40.031  1.00 28.35  ? 803  A1A0C D C07 1 
HETATM 13976 F  F12 . A1A0C W  4 .   ? 14.865  -59.155 -42.365  1.00 26.48  ? 803  A1A0C D F12 1 
HETATM 13977 F  F13 . A1A0C W  4 .   ? 17.367  -59.426 -43.122  1.00 32.60  ? 803  A1A0C D F13 1 
HETATM 13978 N  N01 . A1A0C W  4 .   ? 12.485  -57.720 -43.068  1.00 24.12  ? 803  A1A0C D N01 1 
HETATM 13979 N  N02 . A1A0C W  4 .   ? 10.326  -58.593 -43.066  1.00 17.57  ? 803  A1A0C D N02 1 
HETATM 13980 N  N19 . A1A0C W  4 .   ? 19.323  -53.188 -44.406  1.00 32.00  ? 803  A1A0C D N19 1 
HETATM 13981 C  C1  . GOL   X  5 .   ? 1.375   -48.364 -30.286  1.00 41.69  ? 804  GOL   D C1  1 
HETATM 13982 O  O1  . GOL   X  5 .   ? 1.219   -48.240 -31.689  1.00 50.88  ? 804  GOL   D O1  1 
HETATM 13983 C  C2  . GOL   X  5 .   ? 1.807   -47.039 -29.665  1.00 42.36  ? 804  GOL   D C2  1 
HETATM 13984 O  O2  . GOL   X  5 .   ? 1.167   -45.935 -30.265  1.00 45.54  ? 804  GOL   D O2  1 
HETATM 13985 C  C3  . GOL   X  5 .   ? 3.316   -46.887 -29.777  1.00 34.10  ? 804  GOL   D C3  1 
HETATM 13986 O  O3  . GOL   X  5 .   ? 3.949   -47.656 -28.770  1.00 38.30  ? 804  GOL   D O3  1 
HETATM 13987 O  O   . HOH   Y  7 .   ? -8.669  3.633   -41.608  1.00 26.61  ? 901  HOH   A O   1 
HETATM 13988 O  O   . HOH   Y  7 .   ? -12.313 -25.216 -42.139  1.00 46.54  ? 902  HOH   A O   1 
HETATM 13989 O  O   . HOH   Y  7 .   ? -9.707  -19.315 -39.620  1.00 51.87  ? 903  HOH   A O   1 
HETATM 13990 O  O   . HOH   Y  7 .   ? -4.246  20.561  -37.642  1.00 47.69  ? 904  HOH   A O   1 
HETATM 13991 O  O   . HOH   Y  7 .   ? -8.496  10.999  -61.247  1.00 37.26  ? 905  HOH   A O   1 
HETATM 13992 O  O   . HOH   Y  7 .   ? -6.473  27.136  -34.282  1.00 53.06  ? 906  HOH   A O   1 
HETATM 13993 O  O   . HOH   Y  7 .   ? -0.929  -24.473 -48.405  1.00 75.51  ? 907  HOH   A O   1 
HETATM 13994 O  O   . HOH   Y  7 .   ? -11.028 13.946  -51.996  1.00 55.29  ? 908  HOH   A O   1 
HETATM 13995 O  O   . HOH   Y  7 .   ? -7.124  7.901   -26.955  1.00 30.73  ? 909  HOH   A O   1 
HETATM 13996 O  O   . HOH   Y  7 .   ? -1.491  -25.672 -26.862  1.00 48.84  ? 910  HOH   A O   1 
HETATM 13997 O  O   . HOH   Y  7 .   ? -10.505 -10.037 -24.756  1.00 34.13  ? 911  HOH   A O   1 
HETATM 13998 O  O   . HOH   Y  7 .   ? -0.822  -23.656 -50.903  1.00 55.20  ? 912  HOH   A O   1 
HETATM 13999 O  O   . HOH   Y  7 .   ? 2.057   -16.824 -51.937  1.00 33.94  ? 913  HOH   A O   1 
HETATM 14000 O  O   . HOH   Y  7 .   ? -13.877 3.285   -31.037  1.00 19.78  ? 914  HOH   A O   1 
HETATM 14001 O  O   . HOH   Y  7 .   ? -7.367  0.143   -33.171  1.00 35.60  ? 915  HOH   A O   1 
HETATM 14002 O  O   . HOH   Y  7 .   ? -29.106 -19.225 -27.494  1.00 51.46  ? 916  HOH   A O   1 
HETATM 14003 O  O   . HOH   Y  7 .   ? 8.944   16.754  -43.000  1.00 48.70  ? 917  HOH   A O   1 
HETATM 14004 O  O   . HOH   Y  7 .   ? 0.122   13.454  -25.150  1.00 58.79  ? 918  HOH   A O   1 
HETATM 14005 O  O   . HOH   Y  7 .   ? -1.553  -21.788 -18.173  1.00 49.54  ? 919  HOH   A O   1 
HETATM 14006 O  O   . HOH   Y  7 .   ? -15.137 -18.284 -59.775  1.00 49.26  ? 920  HOH   A O   1 
HETATM 14007 O  O   . HOH   Y  7 .   ? -23.221 -3.664  -44.240  1.00 35.42  ? 921  HOH   A O   1 
HETATM 14008 O  O   . HOH   Y  7 .   ? -17.181 16.031  -46.576  1.00 34.10  ? 922  HOH   A O   1 
HETATM 14009 O  O   . HOH   Y  7 .   ? -17.646 6.591   -41.798  1.00 20.06  ? 923  HOH   A O   1 
HETATM 14010 O  O   . HOH   Y  7 .   ? -6.220  -13.741 -64.406  1.00 33.41  ? 924  HOH   A O   1 
HETATM 14011 O  O   . HOH   Y  7 .   ? -18.252 -20.002 -39.284  1.00 30.87  ? 925  HOH   A O   1 
HETATM 14012 O  O   . HOH   Y  7 .   ? -6.080  15.293  -47.244  1.00 34.21  ? 926  HOH   A O   1 
HETATM 14013 O  O   . HOH   Y  7 .   ? -10.114 -19.689 -54.460  1.00 27.86  ? 927  HOH   A O   1 
HETATM 14014 O  O   . HOH   Y  7 .   ? 0.632   17.017  -36.756  1.00 50.16  ? 928  HOH   A O   1 
HETATM 14015 O  O   . HOH   Y  7 .   ? -23.851 11.830  -48.994  1.00 58.19  ? 929  HOH   A O   1 
HETATM 14016 O  O   . HOH   Y  7 .   ? -4.941  -26.984 -27.878  1.00 54.30  ? 930  HOH   A O   1 
HETATM 14017 O  O   . HOH   Y  7 .   ? -4.451  9.796   -58.465  1.00 28.79  ? 931  HOH   A O   1 
HETATM 14018 O  O   . HOH   Y  7 .   ? -26.470 -0.078  -53.028  1.00 50.85  ? 932  HOH   A O   1 
HETATM 14019 O  O   . HOH   Y  7 .   ? -9.626  -9.754  -35.066  1.00 41.05  ? 933  HOH   A O   1 
HETATM 14020 O  O   . HOH   Y  7 .   ? -3.796  -20.248 -49.382  1.00 36.13  ? 934  HOH   A O   1 
HETATM 14021 O  O   . HOH   Y  7 .   ? -3.235  12.797  -23.717  1.00 53.84  ? 935  HOH   A O   1 
HETATM 14022 O  O   . HOH   Y  7 .   ? -13.113 -25.078 -57.666  1.00 29.63  ? 936  HOH   A O   1 
HETATM 14023 O  O   . HOH   Y  7 .   ? -0.431  -5.667  -45.063  1.00 33.15  ? 937  HOH   A O   1 
HETATM 14024 O  O   . HOH   Y  7 .   ? -6.679  -11.201 -26.564  1.00 38.46  ? 938  HOH   A O   1 
HETATM 14025 O  O   . HOH   Y  7 .   ? 0.464   -30.461 -51.133  1.00 46.93  ? 939  HOH   A O   1 
HETATM 14026 O  O   . HOH   Y  7 .   ? -27.990 -8.866  -23.345  1.00 29.38  ? 940  HOH   A O   1 
HETATM 14027 O  O   . HOH   Y  7 .   ? -13.507 7.566   -50.126  1.00 22.75  ? 941  HOH   A O   1 
HETATM 14028 O  O   . HOH   Y  7 .   ? -22.358 -15.454 -16.487  1.00 46.36  ? 942  HOH   A O   1 
HETATM 14029 O  O   . HOH   Y  7 .   ? -6.829  -38.668 -53.939  1.00 41.99  ? 943  HOH   A O   1 
HETATM 14030 O  O   . HOH   Y  7 .   ? -3.980  13.733  -26.926  1.00 29.87  ? 944  HOH   A O   1 
HETATM 14031 O  O   . HOH   Y  7 .   ? -20.141 -25.456 -53.844  1.00 34.17  ? 945  HOH   A O   1 
HETATM 14032 O  O   . HOH   Y  7 .   ? -26.707 -9.033  -41.358  1.00 37.73  ? 946  HOH   A O   1 
HETATM 14033 O  O   . HOH   Y  7 .   ? -21.997 -12.523 -35.105  1.00 28.19  ? 947  HOH   A O   1 
HETATM 14034 O  O   . HOH   Y  7 .   ? -2.457  -20.277 -28.459  1.00 51.59  ? 948  HOH   A O   1 
HETATM 14035 O  O   . HOH   Y  7 .   ? -17.297 0.508   -46.782  1.00 24.57  ? 949  HOH   A O   1 
HETATM 14036 O  O   . HOH   Y  7 .   ? -23.974 10.611  -41.202  1.00 33.50  ? 950  HOH   A O   1 
HETATM 14037 O  O   . HOH   Y  7 .   ? -5.526  -21.085 -25.469  1.00 29.28  ? 951  HOH   A O   1 
HETATM 14038 O  O   . HOH   Y  7 .   ? -10.994 21.315  -37.351  1.00 36.65  ? 952  HOH   A O   1 
HETATM 14039 O  O   . HOH   Y  7 .   ? 1.846   11.684  -31.169  1.00 46.37  ? 953  HOH   A O   1 
HETATM 14040 O  O   . HOH   Y  7 .   ? -16.812 -14.209 -58.754  1.00 45.92  ? 954  HOH   A O   1 
HETATM 14041 O  O   . HOH   Y  7 .   ? -29.672 -6.948  -22.356  1.00 42.12  ? 955  HOH   A O   1 
HETATM 14042 O  O   . HOH   Y  7 .   ? 1.925   5.865   -33.380  1.00 45.54  ? 956  HOH   A O   1 
HETATM 14043 O  O   . HOH   Y  7 .   ? 6.936   -13.239 -58.074  1.00 47.00  ? 957  HOH   A O   1 
HETATM 14044 O  O   . HOH   Y  7 .   ? -5.159  -13.297 -35.736  1.00 41.70  ? 958  HOH   A O   1 
HETATM 14045 O  O   . HOH   Y  7 .   ? -4.837  -14.366 -60.493  1.00 37.55  ? 959  HOH   A O   1 
HETATM 14046 O  O   . HOH   Y  7 .   ? -31.883 -6.242  -24.041  1.00 39.30  ? 960  HOH   A O   1 
HETATM 14047 O  O   . HOH   Y  7 .   ? -26.622 -8.263  -49.152  1.00 48.90  ? 961  HOH   A O   1 
HETATM 14048 O  O   . HOH   Y  7 .   ? -9.159  5.011   -37.876  1.00 29.24  ? 962  HOH   A O   1 
HETATM 14049 O  O   . HOH   Y  7 .   ? -2.820  4.041   -46.298  1.00 24.17  ? 963  HOH   A O   1 
HETATM 14050 O  O   . HOH   Y  7 .   ? -13.168 -4.103  -60.252  1.00 59.86  ? 964  HOH   A O   1 
HETATM 14051 O  O   . HOH   Y  7 .   ? -16.737 -31.239 -41.115  1.00 46.14  ? 965  HOH   A O   1 
HETATM 14052 O  O   . HOH   Y  7 .   ? -3.340  12.186  -18.394  1.00 39.88  ? 966  HOH   A O   1 
HETATM 14053 O  O   . HOH   Y  7 .   ? -28.428 -8.594  -38.389  1.00 38.69  ? 967  HOH   A O   1 
HETATM 14054 O  O   . HOH   Y  7 .   ? -4.896  -18.440 -12.382  1.00 30.60  ? 968  HOH   A O   1 
HETATM 14055 O  O   . HOH   Y  7 .   ? -13.136 -21.835 -42.709  1.00 30.92  ? 969  HOH   A O   1 
HETATM 14056 O  O   . HOH   Y  7 .   ? -4.603  25.407  -29.285  1.00 77.30  ? 970  HOH   A O   1 
HETATM 14057 O  O   . HOH   Y  7 .   ? -16.078 24.902  -35.613  1.00 35.83  ? 971  HOH   A O   1 
HETATM 14058 O  O   . HOH   Y  7 .   ? -7.542  -17.111 -54.844  1.00 24.74  ? 972  HOH   A O   1 
HETATM 14059 O  O   . HOH   Y  7 .   ? -3.756  5.826   -48.172  1.00 27.89  ? 973  HOH   A O   1 
HETATM 14060 O  O   . HOH   Y  7 .   ? -26.417 1.845   -35.106  1.00 45.44  ? 974  HOH   A O   1 
HETATM 14061 O  O   . HOH   Y  7 .   ? -5.459  6.235   -39.986  1.00 31.66  ? 975  HOH   A O   1 
HETATM 14062 O  O   . HOH   Y  7 .   ? 7.147   -11.169 -50.332  1.00 60.85  ? 976  HOH   A O   1 
HETATM 14063 O  O   . HOH   Y  7 .   ? -3.885  -14.292 -31.445  1.00 42.62  ? 977  HOH   A O   1 
HETATM 14064 O  O   . HOH   Y  7 .   ? -28.622 1.485   -32.126  1.00 38.58  ? 978  HOH   A O   1 
HETATM 14065 O  O   . HOH   Y  7 .   ? -25.747 -37.562 -51.926  1.00 40.42  ? 979  HOH   A O   1 
HETATM 14066 O  O   . HOH   Y  7 .   ? -14.764 -16.233 -33.641  1.00 26.92  ? 980  HOH   A O   1 
HETATM 14067 O  O   . HOH   Y  7 .   ? 10.221  -2.825  -39.115  1.00 47.40  ? 981  HOH   A O   1 
HETATM 14068 O  O   . HOH   Y  7 .   ? -16.435 22.168  -16.307  1.00 43.62  ? 982  HOH   A O   1 
HETATM 14069 O  O   . HOH   Y  7 .   ? -22.291 15.733  -32.504  1.00 32.26  ? 983  HOH   A O   1 
HETATM 14070 O  O   . HOH   Y  7 .   ? -4.093  8.224   -40.715  1.00 33.15  ? 984  HOH   A O   1 
HETATM 14071 O  O   . HOH   Y  7 .   ? -2.476  -8.103  -39.971  1.00 30.06  ? 985  HOH   A O   1 
HETATM 14072 O  O   . HOH   Y  7 .   ? 3.018   -11.623 -47.300  1.00 39.80  ? 986  HOH   A O   1 
HETATM 14073 O  O   . HOH   Y  7 .   ? -21.763 -10.146 -55.320  1.00 50.38  ? 987  HOH   A O   1 
HETATM 14074 O  O   . HOH   Y  7 .   ? -10.441 -12.574 -25.334  1.00 37.54  ? 988  HOH   A O   1 
HETATM 14075 O  O   . HOH   Y  7 .   ? -1.341  -20.593 -47.390  1.00 42.86  ? 989  HOH   A O   1 
HETATM 14076 O  O   . HOH   Y  7 .   ? -22.003 -23.518 -54.554  1.00 39.51  ? 990  HOH   A O   1 
HETATM 14077 O  O   . HOH   Y  7 .   ? -2.413  -7.358  -47.404  1.00 23.58  ? 991  HOH   A O   1 
HETATM 14078 O  O   . HOH   Y  7 .   ? -10.555 -11.946 -65.972  1.00 53.23  ? 992  HOH   A O   1 
HETATM 14079 O  O   . HOH   Y  7 .   ? -3.372  -21.512 -53.238  1.00 55.89  ? 993  HOH   A O   1 
HETATM 14080 O  O   . HOH   Y  7 .   ? 0.232   2.208   -42.141  1.00 47.08  ? 994  HOH   A O   1 
HETATM 14081 O  O   . HOH   Y  7 .   ? -23.752 -4.318  -34.462  1.00 26.08  ? 995  HOH   A O   1 
HETATM 14082 O  O   . HOH   Y  7 .   ? -3.572  0.263   -27.767  1.00 44.52  ? 996  HOH   A O   1 
HETATM 14083 O  O   . HOH   Y  7 .   ? -14.855 -12.854 -22.047  1.00 32.38  ? 997  HOH   A O   1 
HETATM 14084 O  O   . HOH   Y  7 .   ? -10.080 21.486  -41.359  1.00 49.45  ? 998  HOH   A O   1 
HETATM 14085 O  O   . HOH   Y  7 .   ? -6.595  -6.442  -27.556  1.00 27.49  ? 999  HOH   A O   1 
HETATM 14086 O  O   . HOH   Y  7 .   ? -26.142 1.192   -20.608  1.00 42.40  ? 1000 HOH   A O   1 
HETATM 14087 O  O   . HOH   Y  7 .   ? 5.320   10.857  -55.852  1.00 42.66  ? 1001 HOH   A O   1 
HETATM 14088 O  O   . HOH   Y  7 .   ? -12.980 -4.278  -55.951  1.00 23.09  ? 1002 HOH   A O   1 
HETATM 14089 O  O   . HOH   Y  7 .   ? -2.615  18.820  -28.983  1.00 43.22  ? 1003 HOH   A O   1 
HETATM 14090 O  O   . HOH   Y  7 .   ? 8.526   -1.634  -57.333  1.00 45.21  ? 1004 HOH   A O   1 
HETATM 14091 O  O   . HOH   Y  7 .   ? -8.944  3.679   -44.666  1.00 23.64  ? 1005 HOH   A O   1 
HETATM 14092 O  O   . HOH   Y  7 .   ? -8.304  -8.611  -27.051  1.00 32.66  ? 1006 HOH   A O   1 
HETATM 14093 O  O   . HOH   Y  7 .   ? -27.275 -21.830 -27.198  1.00 31.15  ? 1007 HOH   A O   1 
HETATM 14094 O  O   . HOH   Y  7 .   ? -24.553 4.140   -45.347  1.00 28.85  ? 1008 HOH   A O   1 
HETATM 14095 O  O   . HOH   Y  7 .   ? -13.063 -13.163 -38.047  1.00 24.39  ? 1009 HOH   A O   1 
HETATM 14096 O  O   . HOH   Y  7 .   ? -22.999 -17.373 -50.923  1.00 28.99  ? 1010 HOH   A O   1 
HETATM 14097 O  O   . HOH   Y  7 .   ? -20.827 -13.668 -13.579  1.00 29.72  ? 1011 HOH   A O   1 
HETATM 14098 O  O   . HOH   Y  7 .   ? -22.725 -3.542  -48.657  1.00 27.83  ? 1012 HOH   A O   1 
HETATM 14099 O  O   . HOH   Y  7 .   ? -26.795 -0.907  -38.235  1.00 43.39  ? 1013 HOH   A O   1 
HETATM 14100 O  O   . HOH   Y  7 .   ? 0.110   13.750  -43.391  1.00 39.20  ? 1014 HOH   A O   1 
HETATM 14101 O  O   . HOH   Y  7 .   ? -5.431  -7.771  -46.770  1.00 26.26  ? 1015 HOH   A O   1 
HETATM 14102 O  O   . HOH   Y  7 .   ? -9.919  -16.075 -34.806  1.00 56.81  ? 1016 HOH   A O   1 
HETATM 14103 O  O   . HOH   Y  7 .   ? -15.607 -2.931  -32.371  1.00 23.78  ? 1017 HOH   A O   1 
HETATM 14104 O  O   . HOH   Y  7 .   ? -27.024 -11.333 -21.605  1.00 34.23  ? 1018 HOH   A O   1 
HETATM 14105 O  O   . HOH   Y  7 .   ? -1.727  17.913  -45.779  1.00 43.56  ? 1019 HOH   A O   1 
HETATM 14106 O  O   . HOH   Y  7 .   ? -2.938  8.047   -52.519  1.00 36.12  ? 1020 HOH   A O   1 
HETATM 14107 O  O   . HOH   Y  7 .   ? -30.659 -18.336 -22.732  1.00 53.80  ? 1021 HOH   A O   1 
HETATM 14108 O  O   . HOH   Y  7 .   ? -10.234 -8.415  -64.059  1.00 55.35  ? 1022 HOH   A O   1 
HETATM 14109 O  O   . HOH   Y  7 .   ? -28.268 -30.402 -44.601  1.00 42.91  ? 1023 HOH   A O   1 
HETATM 14110 O  O   . HOH   Y  7 .   ? -3.301  -17.310 -34.217  1.00 54.22  ? 1024 HOH   A O   1 
HETATM 14111 O  O   . HOH   Y  7 .   ? -26.537 2.944   -26.181  1.00 30.43  ? 1025 HOH   A O   1 
HETATM 14112 O  O   . HOH   Y  7 .   ? 3.834   -6.182  -57.231  1.00 29.29  ? 1026 HOH   A O   1 
HETATM 14113 O  O   . HOH   Y  7 .   ? 7.045   -4.848  -58.995  1.00 37.21  ? 1027 HOH   A O   1 
HETATM 14114 O  O   . HOH   Y  7 .   ? -5.317  -12.589 -51.154  1.00 26.05  ? 1028 HOH   A O   1 
HETATM 14115 O  O   . HOH   Y  7 .   ? -1.143  -18.654 -15.297  1.00 48.62  ? 1029 HOH   A O   1 
HETATM 14116 O  O   . HOH   Y  7 .   ? -3.689  -17.807 -55.823  1.00 36.07  ? 1030 HOH   A O   1 
HETATM 14117 O  O   . HOH   Y  7 .   ? -23.361 -1.933  -46.568  1.00 27.54  ? 1031 HOH   A O   1 
HETATM 14118 O  O   . HOH   Y  7 .   ? -25.363 4.493   -24.414  1.00 28.12  ? 1032 HOH   A O   1 
HETATM 14119 O  O   . HOH   Y  7 .   ? 8.135   9.830   -34.905  1.00 58.60  ? 1033 HOH   A O   1 
HETATM 14120 O  O   . HOH   Y  7 .   ? -25.246 -23.418 -31.332  1.00 34.84  ? 1034 HOH   A O   1 
HETATM 14121 O  O   . HOH   Y  7 .   ? 6.386   20.337  -43.936  1.00 52.17  ? 1035 HOH   A O   1 
HETATM 14122 O  O   . HOH   Y  7 .   ? -27.792 -12.542 -38.460  1.00 63.36  ? 1036 HOH   A O   1 
HETATM 14123 O  O   . HOH   Y  7 .   ? 4.084   2.714   -40.324  1.00 30.69  ? 1037 HOH   A O   1 
HETATM 14124 O  O   . HOH   Y  7 .   ? -22.417 -15.366 -33.889  1.00 31.69  ? 1038 HOH   A O   1 
HETATM 14125 O  O   . HOH   Y  7 .   ? -1.452  -15.260 -40.211  1.00 48.71  ? 1039 HOH   A O   1 
HETATM 14126 O  O   . HOH   Y  7 .   ? -6.260  -25.084 -57.375  1.00 37.65  ? 1040 HOH   A O   1 
HETATM 14127 O  O   . HOH   Y  7 .   ? -12.261 0.153   -27.592  1.00 23.85  ? 1041 HOH   A O   1 
HETATM 14128 O  O   . HOH   Y  7 .   ? -14.619 8.694   -60.141  1.00 43.19  ? 1042 HOH   A O   1 
HETATM 14129 O  O   . HOH   Y  7 .   ? -4.433  10.294  -24.628  1.00 35.99  ? 1043 HOH   A O   1 
HETATM 14130 O  O   . HOH   Y  7 .   ? -4.345  -28.883 -40.760  1.00 55.50  ? 1044 HOH   A O   1 
HETATM 14131 O  O   . HOH   Y  7 .   ? -20.648 -13.556 -26.096  1.00 25.80  ? 1045 HOH   A O   1 
HETATM 14132 O  O   . HOH   Y  7 .   ? -13.305 -10.731 -62.855  1.00 39.23  ? 1046 HOH   A O   1 
HETATM 14133 O  O   . HOH   Y  7 .   ? -27.541 -25.309 -29.680  1.00 43.50  ? 1047 HOH   A O   1 
HETATM 14134 O  O   . HOH   Y  7 .   ? -24.300 -23.375 -54.016  1.00 50.48  ? 1048 HOH   A O   1 
HETATM 14135 O  O   . HOH   Y  7 .   ? 5.312   -28.277 -48.665  1.00 66.12  ? 1049 HOH   A O   1 
HETATM 14136 O  O   . HOH   Y  7 .   ? -22.940 -26.011 -30.876  1.00 42.67  ? 1050 HOH   A O   1 
HETATM 14137 O  O   . HOH   Y  7 .   ? -17.204 -28.218 -40.343  1.00 40.97  ? 1051 HOH   A O   1 
HETATM 14138 O  O   . HOH   Y  7 .   ? 1.777   -3.717  -62.040  1.00 31.71  ? 1052 HOH   A O   1 
HETATM 14139 O  O   . HOH   Y  7 .   ? -24.970 9.190   -37.136  1.00 48.43  ? 1053 HOH   A O   1 
HETATM 14140 O  O   . HOH   Y  7 .   ? -2.770  7.597   -25.198  1.00 52.87  ? 1054 HOH   A O   1 
HETATM 14141 O  O   . HOH   Y  7 .   ? -26.508 -3.301  -20.909  1.00 41.05  ? 1055 HOH   A O   1 
HETATM 14142 O  O   . HOH   Y  7 .   ? -14.950 -10.898 -24.077  1.00 22.76  ? 1056 HOH   A O   1 
HETATM 14143 O  O   . HOH   Y  7 .   ? -10.346 -11.597 -29.846  1.00 31.05  ? 1057 HOH   A O   1 
HETATM 14144 O  O   . HOH   Y  7 .   ? -0.271  -16.465 -54.134  1.00 35.55  ? 1058 HOH   A O   1 
HETATM 14145 O  O   . HOH   Y  7 .   ? -7.165  -14.575 -25.153  1.00 33.26  ? 1059 HOH   A O   1 
HETATM 14146 O  O   . HOH   Y  7 .   ? -4.519  -0.146  -29.895  1.00 36.63  ? 1060 HOH   A O   1 
HETATM 14147 O  O   . HOH   Y  7 .   ? -1.578  -38.569 -42.729  1.00 58.64  ? 1061 HOH   A O   1 
HETATM 14148 O  O   . HOH   Y  7 .   ? -2.893  3.068   -36.168  1.00 36.90  ? 1062 HOH   A O   1 
HETATM 14149 O  O   . HOH   Y  7 .   ? -1.689  -14.159 -52.054  1.00 30.46  ? 1063 HOH   A O   1 
HETATM 14150 O  O   . HOH   Y  7 .   ? -12.523 8.141   -47.430  1.00 20.98  ? 1064 HOH   A O   1 
HETATM 14151 O  O   . HOH   Y  7 .   ? -4.579  4.566   -32.421  1.00 28.13  ? 1065 HOH   A O   1 
HETATM 14152 O  O   . HOH   Y  7 .   ? -12.622 -1.207  -24.118  1.00 24.30  ? 1066 HOH   A O   1 
HETATM 14153 O  O   . HOH   Y  7 .   ? -22.979 -24.475 -41.112  1.00 46.54  ? 1067 HOH   A O   1 
HETATM 14154 O  O   . HOH   Y  7 .   ? 2.629   -32.789 -40.588  1.00 57.51  ? 1068 HOH   A O   1 
HETATM 14155 O  O   . HOH   Y  7 .   ? -2.957  -2.390  -38.334  1.00 37.80  ? 1069 HOH   A O   1 
HETATM 14156 O  O   . HOH   Y  7 .   ? -20.175 23.439  -40.828  1.00 49.36  ? 1070 HOH   A O   1 
HETATM 14157 O  O   . HOH   Y  7 .   ? -29.650 -18.185 -25.091  1.00 35.99  ? 1071 HOH   A O   1 
HETATM 14158 O  O   . HOH   Y  7 .   ? -2.237  16.624  -26.440  1.00 30.59  ? 1072 HOH   A O   1 
HETATM 14159 O  O   . HOH   Y  7 .   ? 9.430   -7.690  -58.450  1.00 40.84  ? 1073 HOH   A O   1 
HETATM 14160 O  O   . HOH   Y  7 .   ? -16.105 -1.107  -30.373  1.00 24.15  ? 1074 HOH   A O   1 
HETATM 14161 O  O   . HOH   Y  7 .   ? 4.735   -11.924 -61.813  1.00 55.44  ? 1075 HOH   A O   1 
HETATM 14162 O  O   . HOH   Y  7 .   ? -15.545 9.359   -21.512  1.00 26.31  ? 1076 HOH   A O   1 
HETATM 14163 O  O   . HOH   Y  7 .   ? -24.766 -19.722 -50.719  1.00 43.87  ? 1077 HOH   A O   1 
HETATM 14164 O  O   . HOH   Y  7 .   ? 2.834   -6.151  -60.057  1.00 30.01  ? 1078 HOH   A O   1 
HETATM 14165 O  O   . HOH   Y  7 .   ? -1.481  12.444  -60.057  1.00 39.92  ? 1079 HOH   A O   1 
HETATM 14166 O  O   . HOH   Y  7 .   ? -17.029 -9.626  -57.900  1.00 31.61  ? 1080 HOH   A O   1 
HETATM 14167 O  O   . HOH   Y  7 .   ? -10.091 2.852   -36.168  1.00 28.24  ? 1081 HOH   A O   1 
HETATM 14168 O  O   . HOH   Y  7 .   ? -15.942 -22.397 -36.692  1.00 36.51  ? 1082 HOH   A O   1 
HETATM 14169 O  O   . HOH   Y  7 .   ? -27.149 5.593   -35.728  1.00 53.10  ? 1083 HOH   A O   1 
HETATM 14170 O  O   . HOH   Y  7 .   ? -11.405 2.422   -31.936  1.00 25.16  ? 1084 HOH   A O   1 
HETATM 14171 O  O   . HOH   Y  7 .   ? -11.945 -12.284 -60.356  1.00 37.74  ? 1085 HOH   A O   1 
HETATM 14172 O  O   . HOH   Y  7 .   ? 0.185   -10.914 -65.695  1.00 43.70  ? 1086 HOH   A O   1 
HETATM 14173 O  O   . HOH   Y  7 .   ? -29.878 -2.895  -27.577  1.00 37.02  ? 1087 HOH   A O   1 
HETATM 14174 O  O   . HOH   Y  7 .   ? -3.629  -23.254 -50.141  1.00 49.38  ? 1088 HOH   A O   1 
HETATM 14175 O  O   . HOH   Y  7 .   ? -28.179 -9.852  -36.069  1.00 32.01  ? 1089 HOH   A O   1 
HETATM 14176 O  O   . HOH   Y  7 .   ? -10.556 1.836   -29.313  1.00 25.24  ? 1090 HOH   A O   1 
HETATM 14177 O  O   . HOH   Y  7 .   ? 0.594   -33.816 -50.064  1.00 34.70  ? 1091 HOH   A O   1 
HETATM 14178 O  O   . HOH   Y  7 .   ? -17.553 20.116  -45.715  1.00 42.19  ? 1092 HOH   A O   1 
HETATM 14179 O  O   . HOH   Y  7 .   ? -26.969 6.537   -52.047  1.00 46.40  ? 1093 HOH   A O   1 
HETATM 14180 O  O   . HOH   Y  7 .   ? -1.692  6.620   -27.124  1.00 62.05  ? 1094 HOH   A O   1 
HETATM 14181 O  O   . HOH   Y  7 .   ? 5.336   -13.446 -50.917  1.00 46.98  ? 1095 HOH   A O   1 
HETATM 14182 O  O   . HOH   Y  7 .   ? 1.673   -19.232 -36.680  1.00 51.20  ? 1096 HOH   A O   1 
HETATM 14183 O  O   . HOH   Y  7 .   ? -25.198 8.452   -52.381  1.00 45.57  ? 1097 HOH   A O   1 
HETATM 14184 O  O   . HOH   Y  7 .   ? -15.239 11.549  -52.639  1.00 39.18  ? 1098 HOH   A O   1 
HETATM 14185 O  O   . HOH   Y  7 .   ? -4.730  10.303  -52.682  1.00 39.34  ? 1099 HOH   A O   1 
HETATM 14186 O  O   . HOH   Y  7 .   ? -20.819 -29.420 -56.586  1.00 49.12  ? 1100 HOH   A O   1 
HETATM 14187 O  O   . HOH   Y  7 .   ? -20.621 13.794  -48.858  1.00 52.33  ? 1101 HOH   A O   1 
HETATM 14188 O  O   . HOH   Y  7 .   ? 5.783   3.886   -37.683  1.00 47.29  ? 1102 HOH   A O   1 
HETATM 14189 O  O   . HOH   Y  7 .   ? -25.268 7.523   -34.804  1.00 36.30  ? 1103 HOH   A O   1 
HETATM 14190 O  O   . HOH   Y  7 .   ? -17.257 0.782   -58.195  1.00 30.19  ? 1104 HOH   A O   1 
HETATM 14191 O  O   . HOH   Y  7 .   ? -17.439 10.591  -31.954  1.00 30.48  ? 1105 HOH   A O   1 
HETATM 14192 O  O   . HOH   Y  7 .   ? -0.873  2.394   -44.628  1.00 40.35  ? 1106 HOH   A O   1 
HETATM 14193 O  O   . HOH   Y  7 .   ? 6.686   1.992   -57.079  1.00 43.27  ? 1107 HOH   A O   1 
HETATM 14194 O  O   . HOH   Y  7 .   ? -18.073 -20.074 -58.915  1.00 36.96  ? 1108 HOH   A O   1 
HETATM 14195 O  O   . HOH   Y  7 .   ? -1.179  13.195  -50.415  1.00 37.02  ? 1109 HOH   A O   1 
HETATM 14196 O  O   . HOH   Y  7 .   ? 10.053  10.541  -41.588  1.00 47.61  ? 1110 HOH   A O   1 
HETATM 14197 O  O   . HOH   Y  7 .   ? -5.490  -35.711 -42.191  1.00 60.08  ? 1111 HOH   A O   1 
HETATM 14198 O  O   . HOH   Y  7 .   ? -18.797 8.344   -31.425  1.00 25.61  ? 1112 HOH   A O   1 
HETATM 14199 O  O   . HOH   Y  7 .   ? -7.553  -6.702  -44.622  1.00 24.87  ? 1113 HOH   A O   1 
HETATM 14200 O  O   . HOH   Y  7 .   ? -25.102 -14.453 -48.864  1.00 39.79  ? 1114 HOH   A O   1 
HETATM 14201 O  O   . HOH   Y  7 .   ? -13.382 15.054  -49.927  1.00 33.42  ? 1115 HOH   A O   1 
HETATM 14202 O  O   . HOH   Y  7 .   ? -24.921 8.699   -45.051  1.00 46.10  ? 1116 HOH   A O   1 
HETATM 14203 O  O   . HOH   Y  7 .   ? -26.188 -20.144 -46.235  1.00 51.43  ? 1117 HOH   A O   1 
HETATM 14204 O  O   . HOH   Y  7 .   ? -32.315 -6.872  -35.560  1.00 42.62  ? 1118 HOH   A O   1 
HETATM 14205 O  O   . HOH   Y  7 .   ? -24.539 18.192  -46.858  1.00 60.80  ? 1119 HOH   A O   1 
HETATM 14206 O  O   . HOH   Y  7 .   ? 0.536   -3.602  -43.367  1.00 42.12  ? 1120 HOH   A O   1 
HETATM 14207 O  O   . HOH   Y  7 .   ? 0.524   15.259  -35.219  1.00 40.59  ? 1121 HOH   A O   1 
HETATM 14208 O  O   . HOH   Y  7 .   ? -1.726  3.973   -29.661  1.00 65.53  ? 1122 HOH   A O   1 
HETATM 14209 O  O   . HOH   Y  7 .   ? -32.087 -21.292 -35.645  1.00 56.69  ? 1123 HOH   A O   1 
HETATM 14210 O  O   . HOH   Y  7 .   ? -7.580  15.426  -17.390  1.00 27.71  ? 1124 HOH   A O   1 
HETATM 14211 O  O   . HOH   Y  7 .   ? -2.815  17.774  -16.149  1.00 44.74  ? 1125 HOH   A O   1 
HETATM 14212 O  O   . HOH   Y  7 .   ? -23.131 -20.737 -38.392  1.00 52.54  ? 1126 HOH   A O   1 
HETATM 14213 O  O   . HOH   Y  7 .   ? -6.652  4.474   -38.101  1.00 29.86  ? 1127 HOH   A O   1 
HETATM 14214 O  O   . HOH   Y  7 .   ? 2.463   -2.019  -38.042  1.00 54.74  ? 1128 HOH   A O   1 
HETATM 14215 O  O   . HOH   Y  7 .   ? -25.761 5.863   -38.871  1.00 69.28  ? 1129 HOH   A O   1 
HETATM 14216 O  O   . HOH   Y  7 .   ? -10.755 30.065  -28.119  1.00 53.56  ? 1130 HOH   A O   1 
HETATM 14217 O  O   . HOH   Y  7 .   ? -17.071 30.007  -30.571  1.00 44.11  ? 1131 HOH   A O   1 
HETATM 14218 O  O   . HOH   Y  7 .   ? -12.305 8.652   -60.555  1.00 36.74  ? 1132 HOH   A O   1 
HETATM 14219 O  O   . HOH   Y  7 .   ? 2.321   3.150   -62.995  1.00 49.51  ? 1133 HOH   A O   1 
HETATM 14220 O  O   . HOH   Y  7 .   ? -2.218  -15.450 -36.454  1.00 62.47  ? 1134 HOH   A O   1 
HETATM 14221 O  O   . HOH   Y  7 .   ? -5.427  -2.017  -40.098  1.00 30.58  ? 1135 HOH   A O   1 
HETATM 14222 O  O   . HOH   Y  7 .   ? -3.754  14.296  -49.699  1.00 37.05  ? 1136 HOH   A O   1 
HETATM 14223 O  O   . HOH   Y  7 .   ? -1.330  20.432  -43.441  1.00 39.23  ? 1137 HOH   A O   1 
HETATM 14224 O  O   . HOH   Y  7 .   ? -15.923 1.828   -60.578  1.00 45.43  ? 1138 HOH   A O   1 
HETATM 14225 O  O   . HOH   Y  7 .   ? -11.996 -10.052 -34.339  1.00 26.58  ? 1139 HOH   A O   1 
HETATM 14226 O  O   . HOH   Y  7 .   ? 2.415   -17.979 -28.364  1.00 48.53  ? 1140 HOH   A O   1 
HETATM 14227 O  O   . HOH   Y  7 .   ? -20.642 -21.651 -38.018  1.00 43.06  ? 1141 HOH   A O   1 
HETATM 14228 O  O   . HOH   Y  7 .   ? -17.457 18.347  -22.686  1.00 34.95  ? 1142 HOH   A O   1 
HETATM 14229 O  O   . HOH   Y  7 .   ? -15.210 28.922  -26.687  1.00 52.33  ? 1143 HOH   A O   1 
HETATM 14230 O  O   . HOH   Y  7 .   ? -28.702 5.421   -45.787  1.00 51.72  ? 1144 HOH   A O   1 
HETATM 14231 O  O   . HOH   Y  7 .   ? -8.845  30.467  -19.708  1.00 58.74  ? 1145 HOH   A O   1 
HETATM 14232 O  O   . HOH   Y  7 .   ? -11.518 -11.594 -36.570  1.00 37.11  ? 1146 HOH   A O   1 
HETATM 14233 O  O   . HOH   Y  7 .   ? -3.549  -23.003 -25.022  1.00 44.64  ? 1147 HOH   A O   1 
HETATM 14234 O  O   . HOH   Y  7 .   ? -8.178  -5.116  -62.645  1.00 43.97  ? 1148 HOH   A O   1 
HETATM 14235 O  O   . HOH   Y  7 .   ? -10.458 -11.931 -32.562  1.00 37.84  ? 1149 HOH   A O   1 
HETATM 14236 O  O   . HOH   Y  7 .   ? -0.375  3.888   -32.050  1.00 48.88  ? 1150 HOH   A O   1 
HETATM 14237 O  O   . HOH   Y  7 .   ? -24.955 24.450  -35.157  1.00 52.84  ? 1151 HOH   A O   1 
HETATM 14238 O  O   . HOH   Y  7 .   ? -13.939 5.071   -61.937  1.00 37.34  ? 1152 HOH   A O   1 
HETATM 14239 O  O   . HOH   Y  7 .   ? -3.978  18.287  -46.402  1.00 43.86  ? 1153 HOH   A O   1 
HETATM 14240 O  O   . HOH   Y  7 .   ? -27.710 -28.780 -42.126  1.00 39.56  ? 1154 HOH   A O   1 
HETATM 14241 O  O   . HOH   Y  7 .   ? -12.218 -13.727 -33.579  1.00 48.96  ? 1155 HOH   A O   1 
HETATM 14242 O  O   . HOH   Y  7 .   ? -23.767 -20.598 -41.021  1.00 49.33  ? 1156 HOH   A O   1 
HETATM 14243 O  O   . HOH   Y  7 .   ? -20.498 -19.899 -57.532  1.00 50.39  ? 1157 HOH   A O   1 
HETATM 14244 O  O   . HOH   Y  7 .   ? -4.131  -20.517 -55.921  1.00 39.81  ? 1158 HOH   A O   1 
HETATM 14245 O  O   . HOH   Y  7 .   ? -25.433 -2.769  -54.949  1.00 50.72  ? 1159 HOH   A O   1 
HETATM 14246 O  O   . HOH   Y  7 .   ? -25.323 0.500   -46.582  1.00 38.90  ? 1160 HOH   A O   1 
HETATM 14247 O  O   . HOH   Y  7 .   ? -12.577 -15.193 -35.926  1.00 43.56  ? 1161 HOH   A O   1 
HETATM 14248 O  O   . HOH   Y  7 .   ? -22.442 19.448  -46.732  1.00 48.03  ? 1162 HOH   A O   1 
HETATM 14249 O  O   . HOH   Y  7 .   ? -23.559 0.386   -37.546  1.00 36.13  ? 1163 HOH   A O   1 
HETATM 14250 O  O   . HOH   Y  7 .   ? -22.330 22.475  -40.974  1.00 54.13  ? 1164 HOH   A O   1 
HETATM 14251 O  O   . HOH   Y  7 .   ? -20.522 4.031   -56.452  1.00 55.30  ? 1165 HOH   A O   1 
HETATM 14252 O  O   . HOH   Y  7 .   ? -25.263 8.154   -40.663  1.00 38.96  ? 1166 HOH   A O   1 
HETATM 14253 O  O   . HOH   Y  7 .   ? -4.630  -23.290 -58.643  1.00 45.71  ? 1167 HOH   A O   1 
HETATM 14254 O  O   . HOH   Y  7 .   ? 5.820   21.521  -41.176  1.00 53.07  ? 1168 HOH   A O   1 
HETATM 14255 O  O   . HOH   Y  7 .   ? -4.409  -17.911 -37.326  1.00 48.08  ? 1169 HOH   A O   1 
HETATM 14256 O  O   . HOH   Y  7 .   ? -9.376  3.603   -33.846  1.00 39.06  ? 1170 HOH   A O   1 
HETATM 14257 O  O   . HOH   Y  7 .   ? -20.724 -19.255 -17.277  1.00 50.63  ? 1171 HOH   A O   1 
HETATM 14258 O  O   . HOH   Y  7 .   ? -9.440  -26.565 -37.458  1.00 54.75  ? 1172 HOH   A O   1 
HETATM 14259 O  O   . HOH   Y  7 .   ? -13.943 -20.843 -59.163  1.00 63.95  ? 1173 HOH   A O   1 
HETATM 14260 O  O   . HOH   Y  7 .   ? -29.849 -0.639  -22.055  1.00 67.28  ? 1174 HOH   A O   1 
HETATM 14261 O  O   . HOH   Y  7 .   ? -25.370 -14.029 -11.497  1.00 55.52  ? 1175 HOH   A O   1 
HETATM 14262 O  O   . HOH   Y  7 .   ? -1.441  13.489  -11.749  1.00 51.88  ? 1176 HOH   A O   1 
HETATM 14263 O  O   . HOH   Y  7 .   ? -17.352 23.961  -18.230  1.00 44.02  ? 1177 HOH   A O   1 
HETATM 14264 O  O   . HOH   Y  7 .   ? -5.695  2.899   -36.141  1.00 40.71  ? 1178 HOH   A O   1 
HETATM 14265 O  O   . HOH   Y  7 .   ? -2.901  19.085  -31.578  1.00 50.27  ? 1179 HOH   A O   1 
HETATM 14266 O  O   . HOH   Y  7 .   ? -14.327 0.838   -30.000  1.00 26.75  ? 1180 HOH   A O   1 
HETATM 14267 O  O   . HOH   Y  7 .   ? 9.342   -12.787 -50.271  1.00 58.65  ? 1181 HOH   A O   1 
HETATM 14268 O  O   . HOH   Y  7 .   ? -26.590 0.209   -49.012  1.00 46.25  ? 1182 HOH   A O   1 
HETATM 14269 O  O   . HOH   Y  7 .   ? -7.452  -10.248 -19.217  1.00 38.02  ? 1183 HOH   A O   1 
HETATM 14270 O  O   . HOH   Y  7 .   ? -19.935 -26.569 -56.480  1.00 49.53  ? 1184 HOH   A O   1 
HETATM 14271 O  O   . HOH   Y  7 .   ? -1.134  8.860   -20.267  1.00 47.27  ? 1185 HOH   A O   1 
HETATM 14272 O  O   . HOH   Y  7 .   ? -25.703 -17.678 -44.610  1.00 43.65  ? 1186 HOH   A O   1 
HETATM 14273 O  O   . HOH   Y  7 .   ? -19.207 2.345   -57.886  1.00 44.02  ? 1187 HOH   A O   1 
HETATM 14274 O  O   . HOH   Y  7 .   ? -23.985 -15.953 -45.709  1.00 38.32  ? 1188 HOH   A O   1 
HETATM 14275 O  O   . HOH   Y  7 .   ? -25.438 10.760  -43.586  1.00 48.83  ? 1189 HOH   A O   1 
HETATM 14276 O  O   . HOH   Y  7 .   ? -14.572 -26.383 -27.692  1.00 47.39  ? 1190 HOH   A O   1 
HETATM 14277 O  O   . HOH   Y  7 .   ? 4.370   12.332  -31.896  1.00 48.38  ? 1191 HOH   A O   1 
HETATM 14278 O  O   . HOH   Y  7 .   ? -20.272 6.566   -56.202  1.00 45.04  ? 1192 HOH   A O   1 
HETATM 14279 O  O   . HOH   Y  7 .   ? -4.942  14.668  -17.470  1.00 38.86  ? 1193 HOH   A O   1 
HETATM 14280 O  O   . HOH   Y  7 .   ? -23.710 -16.145 -48.351  1.00 35.24  ? 1194 HOH   A O   1 
HETATM 14281 O  O   . HOH   Y  7 .   ? -17.423 26.016  -37.594  1.00 42.63  ? 1195 HOH   A O   1 
HETATM 14282 O  O   . HOH   Y  7 .   ? -6.942  2.757   -33.146  1.00 30.02  ? 1196 HOH   A O   1 
HETATM 14283 O  O   . HOH   Y  7 .   ? -0.973  -6.778  -37.750  1.00 58.06  ? 1197 HOH   A O   1 
HETATM 14284 O  O   . HOH   Y  7 .   ? -28.667 -3.811  -22.810  1.00 38.95  ? 1198 HOH   A O   1 
HETATM 14285 O  O   . HOH   Y  7 .   ? -7.732  -11.601 -34.515  1.00 63.61  ? 1199 HOH   A O   1 
HETATM 14286 O  O   . HOH   Y  7 .   ? -26.249 -32.611 -59.410  1.00 58.93  ? 1200 HOH   A O   1 
HETATM 14287 O  O   . HOH   Y  7 .   ? -5.242  -15.840 -62.865  1.00 47.51  ? 1201 HOH   A O   1 
HETATM 14288 O  O   . HOH   Y  7 .   ? -8.129  -13.985 -65.824  1.00 49.41  ? 1202 HOH   A O   1 
HETATM 14289 O  O   . HOH   Y  7 .   ? -18.769 15.719  -48.711  1.00 42.30  ? 1203 HOH   A O   1 
HETATM 14290 O  O   . HOH   Y  7 .   ? -28.490 -11.245 -48.832  1.00 64.98  ? 1204 HOH   A O   1 
HETATM 14291 O  O   . HOH   Y  7 .   ? -2.478  2.996   -33.088  1.00 56.26  ? 1205 HOH   A O   1 
HETATM 14292 O  O   . HOH   Y  7 .   ? -2.927  -21.838 -57.850  1.00 42.96  ? 1206 HOH   A O   1 
HETATM 14293 O  O   . HOH   Y  7 .   ? 8.190   -6.958  -60.561  1.00 57.71  ? 1207 HOH   A O   1 
HETATM 14294 O  O   . HOH   Y  7 .   ? -17.582 25.113  -40.539  1.00 46.36  ? 1208 HOH   A O   1 
HETATM 14295 O  O   . HOH   Y  7 .   ? -17.442 11.115  -52.777  1.00 47.45  ? 1209 HOH   A O   1 
HETATM 14296 O  O   . HOH   Y  7 .   ? -17.219 -30.075 -33.618  1.00 58.66  ? 1210 HOH   A O   1 
HETATM 14297 O  O   . HOH   Y  7 .   ? -16.721 -3.063  -59.240  1.00 44.41  ? 1211 HOH   A O   1 
HETATM 14298 O  O   . HOH   Y  7 .   ? -3.034  -0.267  -32.237  1.00 43.15  ? 1212 HOH   A O   1 
HETATM 14299 O  O   . HOH   Y  7 .   ? -24.847 14.257  -50.181  1.00 41.16  ? 1213 HOH   A O   1 
HETATM 14300 O  O   . HOH   Y  7 .   ? -26.160 3.557   -40.240  1.00 63.36  ? 1214 HOH   A O   1 
HETATM 14301 O  O   . HOH   Y  7 .   ? -14.505 -4.764  -58.132  1.00 38.63  ? 1215 HOH   A O   1 
HETATM 14302 O  O   . HOH   Y  7 .   ? -1.905  -17.154 -57.781  1.00 41.19  ? 1216 HOH   A O   1 
HETATM 14303 O  O   . HOH   Y  7 .   ? -24.997 -15.825 -15.234  1.00 57.08  ? 1217 HOH   A O   1 
HETATM 14304 O  O   . HOH   Y  7 .   ? -33.073 -12.650 -25.505  1.00 42.99  ? 1218 HOH   A O   1 
HETATM 14305 O  O   . HOH   Y  7 .   ? -26.110 2.786   -43.499  1.00 53.36  ? 1219 HOH   A O   1 
HETATM 14306 O  O   . HOH   Y  7 .   ? -29.072 10.112  -35.635  1.00 62.52  ? 1220 HOH   A O   1 
HETATM 14307 O  O   . HOH   Y  7 .   ? -29.234 -1.534  -25.202  1.00 55.10  ? 1221 HOH   A O   1 
HETATM 14308 O  O   . HOH   Y  7 .   ? -24.084 -16.085 -53.163  1.00 40.13  ? 1222 HOH   A O   1 
HETATM 14309 O  O   . HOH   Z  7 .   ? -3.202  3.990   -8.164   1.00 36.08  ? 901  HOH   B O   1 
HETATM 14310 O  O   . HOH   Z  7 .   ? -4.165  -20.953 -0.236   1.00 46.22  ? 902  HOH   B O   1 
HETATM 14311 O  O   . HOH   Z  7 .   ? -0.307  1.226   9.331    1.00 49.86  ? 903  HOH   B O   1 
HETATM 14312 O  O   . HOH   Z  7 .   ? -28.238 6.286   -18.890  1.00 54.58  ? 904  HOH   B O   1 
HETATM 14313 O  O   . HOH   Z  7 .   ? -18.491 -18.200 2.110    1.00 49.47  ? 905  HOH   B O   1 
HETATM 14314 O  O   . HOH   Z  7 .   ? -25.025 5.002   16.324   1.00 30.78  ? 906  HOH   B O   1 
HETATM 14315 O  O   . HOH   Z  7 .   ? -20.208 -2.691  -2.713   1.00 46.55  ? 907  HOH   B O   1 
HETATM 14316 O  O   . HOH   Z  7 .   ? -2.149  2.960   8.062    1.00 47.95  ? 908  HOH   B O   1 
HETATM 14317 O  O   . HOH   Z  7 .   ? -0.513  -21.714 14.885   1.00 46.22  ? 909  HOH   B O   1 
HETATM 14318 O  O   . HOH   Z  7 .   ? -11.909 -9.924  -7.386   1.00 37.95  ? 910  HOH   B O   1 
HETATM 14319 O  O   . HOH   Z  7 .   ? -18.211 -2.120  -9.346   1.00 32.96  ? 911  HOH   B O   1 
HETATM 14320 O  O   . HOH   Z  7 .   ? -24.228 17.342  -25.739  1.00 50.27  ? 912  HOH   B O   1 
HETATM 14321 O  O   . HOH   Z  7 .   ? -22.026 8.112   18.881   1.00 37.11  ? 913  HOH   B O   1 
HETATM 14322 O  O   . HOH   Z  7 .   ? -12.391 -2.673  21.869   1.00 38.50  ? 914  HOH   B O   1 
HETATM 14323 O  O   . HOH   Z  7 .   ? -31.246 9.403   -8.267   1.00 56.23  ? 915  HOH   B O   1 
HETATM 14324 O  O   . HOH   Z  7 .   ? -18.009 8.285   18.150   1.00 37.29  ? 916  HOH   B O   1 
HETATM 14325 O  O   . HOH   Z  7 .   ? -12.053 -14.561 22.052   1.00 30.22  ? 917  HOH   B O   1 
HETATM 14326 O  O   . HOH   Z  7 .   ? -35.955 -1.236  0.101    1.00 52.48  ? 918  HOH   B O   1 
HETATM 14327 O  O   . HOH   Z  7 .   ? -5.232  -10.381 -20.301  1.00 30.18  ? 919  HOH   B O   1 
HETATM 14328 O  O   . HOH   Z  7 .   ? -22.062 11.546  8.998    1.00 48.50  ? 920  HOH   B O   1 
HETATM 14329 O  O   . HOH   Z  7 .   ? 4.536   -1.063  -6.472   1.00 32.83  ? 921  HOH   B O   1 
HETATM 14330 O  O   . HOH   Z  7 .   ? -2.131  7.174   -22.113  1.00 35.85  ? 922  HOH   B O   1 
HETATM 14331 O  O   . HOH   Z  7 .   ? -6.134  -21.640 -2.759   1.00 44.47  ? 923  HOH   B O   1 
HETATM 14332 O  O   . HOH   Z  7 .   ? -22.604 2.248   -2.411   1.00 28.74  ? 924  HOH   B O   1 
HETATM 14333 O  O   . HOH   Z  7 .   ? 0.005   -8.791  -28.504  1.00 24.06  ? 925  HOH   B O   1 
HETATM 14334 O  O   . HOH   Z  7 .   ? -2.408  2.249   1.616    1.00 30.21  ? 926  HOH   B O   1 
HETATM 14335 O  O   . HOH   Z  7 .   ? -11.575 -20.420 -29.591  1.00 23.61  ? 927  HOH   B O   1 
HETATM 14336 O  O   . HOH   Z  7 .   ? -3.799  10.648  -21.797  1.00 43.42  ? 928  HOH   B O   1 
HETATM 14337 O  O   . HOH   Z  7 .   ? -13.451 5.976   19.197   1.00 36.45  ? 929  HOH   B O   1 
HETATM 14338 O  O   . HOH   Z  7 .   ? -39.641 -0.077  1.062    1.00 57.26  ? 930  HOH   B O   1 
HETATM 14339 O  O   . HOH   Z  7 .   ? -5.773  -17.946 12.137   1.00 26.67  ? 931  HOH   B O   1 
HETATM 14340 O  O   . HOH   Z  7 .   ? -1.928  8.149   -7.942   1.00 43.42  ? 932  HOH   B O   1 
HETATM 14341 O  O   . HOH   Z  7 .   ? -22.106 4.266   -15.681  1.00 26.31  ? 933  HOH   B O   1 
HETATM 14342 O  O   . HOH   Z  7 .   ? -26.320 10.620  4.860    1.00 38.64  ? 934  HOH   B O   1 
HETATM 14343 O  O   . HOH   Z  7 .   ? -6.653  -11.093 -4.153   1.00 23.23  ? 935  HOH   B O   1 
HETATM 14344 O  O   . HOH   Z  7 .   ? 4.317   2.054   -20.543  1.00 44.41  ? 936  HOH   B O   1 
HETATM 14345 O  O   . HOH   Z  7 .   ? -2.958  2.322   5.960    1.00 27.77  ? 937  HOH   B O   1 
HETATM 14346 O  O   . HOH   Z  7 .   ? -15.974 -9.822  4.429    1.00 22.81  ? 938  HOH   B O   1 
HETATM 14347 O  O   . HOH   Z  7 .   ? -9.642  -1.302  -10.207  1.00 23.68  ? 939  HOH   B O   1 
HETATM 14348 O  O   . HOH   Z  7 .   ? -18.833 3.021   -4.702   1.00 25.69  ? 940  HOH   B O   1 
HETATM 14349 O  O   . HOH   Z  7 .   ? -27.662 8.011   -15.530  1.00 26.25  ? 941  HOH   B O   1 
HETATM 14350 O  O   . HOH   Z  7 .   ? 17.060  -11.308 6.509    1.00 50.26  ? 942  HOH   B O   1 
HETATM 14351 O  O   . HOH   Z  7 .   ? -23.920 -9.556  19.989   1.00 28.43  ? 943  HOH   B O   1 
HETATM 14352 O  O   . HOH   Z  7 .   ? -25.143 5.824   10.726   1.00 37.54  ? 944  HOH   B O   1 
HETATM 14353 O  O   . HOH   Z  7 .   ? 0.546   -6.015  -7.375   1.00 27.85  ? 945  HOH   B O   1 
HETATM 14354 O  O   . HOH   Z  7 .   ? -10.863 -2.909  13.546   1.00 21.24  ? 946  HOH   B O   1 
HETATM 14355 O  O   . HOH   Z  7 .   ? -10.482 -9.814  -17.821  1.00 31.89  ? 947  HOH   B O   1 
HETATM 14356 O  O   . HOH   Z  7 .   ? -27.753 -5.279  -5.627   1.00 48.52  ? 948  HOH   B O   1 
HETATM 14357 O  O   . HOH   Z  7 .   ? -31.537 11.601  -13.830  1.00 35.77  ? 949  HOH   B O   1 
HETATM 14358 O  O   . HOH   Z  7 .   ? -1.958  1.641   -8.078   1.00 24.51  ? 950  HOH   B O   1 
HETATM 14359 O  O   . HOH   Z  7 .   ? 4.295   -0.750  -19.386  1.00 33.49  ? 951  HOH   B O   1 
HETATM 14360 O  O   . HOH   Z  7 .   ? -16.170 -19.713 11.910   1.00 33.04  ? 952  HOH   B O   1 
HETATM 14361 O  O   . HOH   Z  7 .   ? -18.304 -11.616 -2.248   1.00 27.85  ? 953  HOH   B O   1 
HETATM 14362 O  O   . HOH   Z  7 .   ? -19.474 20.923  -20.661  1.00 39.37  ? 954  HOH   B O   1 
HETATM 14363 O  O   . HOH   Z  7 .   ? -31.683 3.521   -11.158  1.00 39.93  ? 955  HOH   B O   1 
HETATM 14364 O  O   . HOH   Z  7 .   ? -8.938  16.110  5.900    1.00 33.65  ? 956  HOH   B O   1 
HETATM 14365 O  O   . HOH   Z  7 .   ? -23.752 1.395   5.850    1.00 23.45  ? 957  HOH   B O   1 
HETATM 14366 O  O   . HOH   Z  7 .   ? -17.157 16.709  3.833    1.00 36.25  ? 958  HOH   B O   1 
HETATM 14367 O  O   . HOH   Z  7 .   ? -38.501 -5.312  4.629    1.00 37.96  ? 959  HOH   B O   1 
HETATM 14368 O  O   . HOH   Z  7 .   ? -21.359 -10.533 3.004    1.00 27.62  ? 960  HOH   B O   1 
HETATM 14369 O  O   . HOH   Z  7 .   ? -7.052  14.027  -6.252   1.00 46.48  ? 961  HOH   B O   1 
HETATM 14370 O  O   . HOH   Z  7 .   ? -26.698 5.277   -20.677  1.00 46.73  ? 962  HOH   B O   1 
HETATM 14371 O  O   . HOH   Z  7 .   ? -4.703  9.797   -18.458  1.00 29.74  ? 963  HOH   B O   1 
HETATM 14372 O  O   . HOH   Z  7 .   ? -10.627 -2.816  17.966   1.00 44.26  ? 964  HOH   B O   1 
HETATM 14373 O  O   . HOH   Z  7 .   ? -25.617 4.897   -17.754  1.00 36.53  ? 965  HOH   B O   1 
HETATM 14374 O  O   . HOH   Z  7 .   ? -20.380 -21.537 5.236    1.00 50.09  ? 966  HOH   B O   1 
HETATM 14375 O  O   . HOH   Z  7 .   ? -8.699  15.121  -1.739   1.00 33.69  ? 967  HOH   B O   1 
HETATM 14376 O  O   . HOH   Z  7 .   ? 3.392   -0.648  -1.680   1.00 36.70  ? 968  HOH   B O   1 
HETATM 14377 O  O   . HOH   Z  7 .   ? -11.441 -15.472 -16.823  1.00 37.00  ? 969  HOH   B O   1 
HETATM 14378 O  O   . HOH   Z  7 .   ? -23.913 -0.974  3.964    1.00 22.09  ? 970  HOH   B O   1 
HETATM 14379 O  O   . HOH   Z  7 .   ? -16.299 7.420   7.446    1.00 21.45  ? 971  HOH   B O   1 
HETATM 14380 O  O   . HOH   Z  7 .   ? -4.934  9.866   2.561    1.00 29.90  ? 972  HOH   B O   1 
HETATM 14381 O  O   . HOH   Z  7 .   ? -24.905 3.238   -1.692   1.00 27.69  ? 973  HOH   B O   1 
HETATM 14382 O  O   . HOH   Z  7 .   ? -1.157  7.056   10.225   1.00 43.29  ? 974  HOH   B O   1 
HETATM 14383 O  O   . HOH   Z  7 .   ? -25.636 -4.014  -0.115   1.00 40.52  ? 975  HOH   B O   1 
HETATM 14384 O  O   . HOH   Z  7 .   ? -12.332 8.416   -0.867   1.00 18.41  ? 976  HOH   B O   1 
HETATM 14385 O  O   . HOH   Z  7 .   ? 0.169   3.515   -21.697  1.00 35.86  ? 977  HOH   B O   1 
HETATM 14386 O  O   . HOH   Z  7 .   ? -2.638  -18.319 0.568    1.00 24.42  ? 978  HOH   B O   1 
HETATM 14387 O  O   . HOH   Z  7 .   ? -0.282  -8.239  -16.102  1.00 27.28  ? 979  HOH   B O   1 
HETATM 14388 O  O   . HOH   Z  7 .   ? -43.767 1.475   -12.093  1.00 37.56  ? 980  HOH   B O   1 
HETATM 14389 O  O   . HOH   Z  7 .   ? 6.384   -15.345 12.125   1.00 39.63  ? 981  HOH   B O   1 
HETATM 14390 O  O   . HOH   Z  7 .   ? -25.525 2.791   10.174   1.00 25.73  ? 982  HOH   B O   1 
HETATM 14391 O  O   . HOH   Z  7 .   ? -16.422 0.616   -13.325  1.00 25.70  ? 983  HOH   B O   1 
HETATM 14392 O  O   . HOH   Z  7 .   ? 4.807   -3.363  -20.954  1.00 33.96  ? 984  HOH   B O   1 
HETATM 14393 O  O   . HOH   Z  7 .   ? -10.090 -11.335 -12.617  1.00 28.16  ? 985  HOH   B O   1 
HETATM 14394 O  O   . HOH   Z  7 .   ? -12.921 -15.775 18.146   1.00 27.32  ? 986  HOH   B O   1 
HETATM 14395 O  O   . HOH   Z  7 .   ? -27.771 -13.342 16.887   1.00 31.07  ? 987  HOH   B O   1 
HETATM 14396 O  O   . HOH   Z  7 .   ? -10.665 -23.098 10.984   1.00 39.48  ? 988  HOH   B O   1 
HETATM 14397 O  O   . HOH   Z  7 .   ? -9.604  3.134   4.214    1.00 24.99  ? 989  HOH   B O   1 
HETATM 14398 O  O   . HOH   Z  7 .   ? -22.355 23.442  -7.470   1.00 26.63  ? 990  HOH   B O   1 
HETATM 14399 O  O   . HOH   Z  7 .   ? 5.794   -17.838 11.359   1.00 35.15  ? 991  HOH   B O   1 
HETATM 14400 O  O   . HOH   Z  7 .   ? 5.853   -12.147 -1.377   1.00 39.63  ? 992  HOH   B O   1 
HETATM 14401 O  O   . HOH   Z  7 .   ? -23.431 -8.517  -1.233   1.00 47.29  ? 993  HOH   B O   1 
HETATM 14402 O  O   . HOH   Z  7 .   ? -2.675  -24.892 -23.109  1.00 58.97  ? 994  HOH   B O   1 
HETATM 14403 O  O   . HOH   Z  7 .   ? -16.050 -17.185 9.889    1.00 25.24  ? 995  HOH   B O   1 
HETATM 14404 O  O   . HOH   Z  7 .   ? -32.533 7.004   -6.828   1.00 49.28  ? 996  HOH   B O   1 
HETATM 14405 O  O   . HOH   Z  7 .   ? -38.413 -2.152  10.816   1.00 41.26  ? 997  HOH   B O   1 
HETATM 14406 O  O   . HOH   Z  7 .   ? -24.542 -3.936  -4.611   1.00 43.52  ? 998  HOH   B O   1 
HETATM 14407 O  O   . HOH   Z  7 .   ? -9.465  -12.501 -16.858  1.00 34.00  ? 999  HOH   B O   1 
HETATM 14408 O  O   . HOH   Z  7 .   ? -2.747  -9.849  16.638   1.00 44.14  ? 1000 HOH   B O   1 
HETATM 14409 O  O   . HOH   Z  7 .   ? 6.579   -10.815 8.533    1.00 42.87  ? 1001 HOH   B O   1 
HETATM 14410 O  O   . HOH   Z  7 .   ? -10.605 -21.864 -15.965  1.00 41.57  ? 1002 HOH   B O   1 
HETATM 14411 O  O   . HOH   Z  7 .   ? -9.323  -16.928 12.628   1.00 25.92  ? 1003 HOH   B O   1 
HETATM 14412 O  O   . HOH   Z  7 .   ? -29.658 6.010   8.163    1.00 38.32  ? 1004 HOH   B O   1 
HETATM 14413 O  O   . HOH   Z  7 .   ? -13.686 -14.030 8.828    1.00 23.57  ? 1005 HOH   B O   1 
HETATM 14414 O  O   . HOH   Z  7 .   ? -21.280 -17.442 5.158    1.00 31.51  ? 1006 HOH   B O   1 
HETATM 14415 O  O   . HOH   Z  7 .   ? -26.004 1.599   -16.665  1.00 40.73  ? 1007 HOH   B O   1 
HETATM 14416 O  O   . HOH   Z  7 .   ? -13.953 -0.119  -14.885  1.00 26.75  ? 1008 HOH   B O   1 
HETATM 14417 O  O   . HOH   Z  7 .   ? -14.307 3.470   -11.464  1.00 22.34  ? 1009 HOH   B O   1 
HETATM 14418 O  O   . HOH   Z  7 .   ? 10.636  -2.828  -23.336  1.00 49.75  ? 1010 HOH   B O   1 
HETATM 14419 O  O   . HOH   Z  7 .   ? -4.011  -12.938 -8.565   1.00 21.72  ? 1011 HOH   B O   1 
HETATM 14420 O  O   . HOH   Z  7 .   ? -15.757 -8.656  -14.796  1.00 26.08  ? 1012 HOH   B O   1 
HETATM 14421 O  O   . HOH   Z  7 .   ? -27.640 5.995   -24.445  1.00 42.66  ? 1013 HOH   B O   1 
HETATM 14422 O  O   . HOH   Z  7 .   ? -21.856 -4.152  -14.845  1.00 32.80  ? 1014 HOH   B O   1 
HETATM 14423 O  O   . HOH   Z  7 .   ? -30.695 -6.957  15.226   1.00 34.04  ? 1015 HOH   B O   1 
HETATM 14424 O  O   . HOH   Z  7 .   ? -3.071  4.040   3.790    1.00 25.45  ? 1016 HOH   B O   1 
HETATM 14425 O  O   . HOH   Z  7 .   ? 2.333   -8.589  -8.546   1.00 31.35  ? 1017 HOH   B O   1 
HETATM 14426 O  O   . HOH   Z  7 .   ? 2.201   5.903   -18.290  1.00 46.37  ? 1018 HOH   B O   1 
HETATM 14427 O  O   . HOH   Z  7 .   ? -33.285 12.566  1.249    1.00 43.32  ? 1019 HOH   B O   1 
HETATM 14428 O  O   . HOH   Z  7 .   ? -18.173 1.791   2.255    1.00 20.32  ? 1020 HOH   B O   1 
HETATM 14429 O  O   . HOH   Z  7 .   ? -31.284 6.223   1.334    1.00 28.84  ? 1021 HOH   B O   1 
HETATM 14430 O  O   . HOH   Z  7 .   ? -10.892 -21.533 7.162    1.00 29.81  ? 1022 HOH   B O   1 
HETATM 14431 O  O   . HOH   Z  7 .   ? 2.788   -9.266  -25.966  1.00 42.06  ? 1023 HOH   B O   1 
HETATM 14432 O  O   . HOH   Z  7 .   ? -16.052 1.563   -10.532  1.00 25.58  ? 1024 HOH   B O   1 
HETATM 14433 O  O   . HOH   Z  7 .   ? -31.211 -8.813  12.962   1.00 47.25  ? 1025 HOH   B O   1 
HETATM 14434 O  O   . HOH   Z  7 .   ? -22.239 -18.604 19.416   1.00 48.72  ? 1026 HOH   B O   1 
HETATM 14435 O  O   . HOH   Z  7 .   ? -15.698 8.983   17.507   1.00 49.52  ? 1027 HOH   B O   1 
HETATM 14436 O  O   . HOH   Z  7 .   ? -26.704 -0.054  -14.686  1.00 40.03  ? 1028 HOH   B O   1 
HETATM 14437 O  O   . HOH   Z  7 .   ? -20.665 -3.827  -12.587  1.00 31.16  ? 1029 HOH   B O   1 
HETATM 14438 O  O   . HOH   Z  7 .   ? -23.579 -1.585  -6.218   1.00 30.58  ? 1030 HOH   B O   1 
HETATM 14439 O  O   . HOH   Z  7 .   ? 9.233   -26.201 2.574    1.00 45.60  ? 1031 HOH   B O   1 
HETATM 14440 O  O   . HOH   Z  7 .   ? -16.829 -23.545 15.259   1.00 36.52  ? 1032 HOH   B O   1 
HETATM 14441 O  O   . HOH   Z  7 .   ? 1.071   -14.324 -3.029   1.00 30.24  ? 1033 HOH   B O   1 
HETATM 14442 O  O   . HOH   Z  7 .   ? -30.713 9.529   -16.116  1.00 36.27  ? 1034 HOH   B O   1 
HETATM 14443 O  O   . HOH   Z  7 .   ? -23.510 -12.305 17.896   1.00 27.50  ? 1035 HOH   B O   1 
HETATM 14444 O  O   . HOH   Z  7 .   ? -12.594 18.409  -10.487  1.00 32.18  ? 1036 HOH   B O   1 
HETATM 14445 O  O   . HOH   Z  7 .   ? -9.657  -24.424 8.137    1.00 41.62  ? 1037 HOH   B O   1 
HETATM 14446 O  O   . HOH   Z  7 .   ? -17.564 -21.571 10.128   1.00 30.64  ? 1038 HOH   B O   1 
HETATM 14447 O  O   . HOH   Z  7 .   ? -25.374 17.959  -5.633   1.00 25.84  ? 1039 HOH   B O   1 
HETATM 14448 O  O   . HOH   Z  7 .   ? -21.212 -12.135 -0.605   1.00 40.50  ? 1040 HOH   B O   1 
HETATM 14449 O  O   . HOH   Z  7 .   ? -2.696  9.087   -16.562  1.00 33.45  ? 1041 HOH   B O   1 
HETATM 14450 O  O   . HOH   Z  7 .   ? -30.787 -11.235 15.280   1.00 43.93  ? 1042 HOH   B O   1 
HETATM 14451 O  O   . HOH   Z  7 .   ? -22.824 0.135   -9.992   1.00 24.25  ? 1043 HOH   B O   1 
HETATM 14452 O  O   . HOH   Z  7 .   ? -13.507 -9.548  -15.390  1.00 30.79  ? 1044 HOH   B O   1 
HETATM 14453 O  O   . HOH   Z  7 .   ? -17.407 7.557   4.869    1.00 21.29  ? 1045 HOH   B O   1 
HETATM 14454 O  O   . HOH   Z  7 .   ? -5.873  12.791  -8.088   1.00 36.10  ? 1046 HOH   B O   1 
HETATM 14455 O  O   . HOH   Z  7 .   ? -19.015 -15.076 23.282   1.00 38.12  ? 1047 HOH   B O   1 
HETATM 14456 O  O   . HOH   Z  7 .   ? 4.625   -5.852  6.508    1.00 42.82  ? 1048 HOH   B O   1 
HETATM 14457 O  O   . HOH   Z  7 .   ? 2.651   7.243   -8.511   1.00 54.43  ? 1049 HOH   B O   1 
HETATM 14458 O  O   . HOH   Z  7 .   ? -20.136 26.796  -8.414   1.00 46.30  ? 1050 HOH   B O   1 
HETATM 14459 O  O   . HOH   Z  7 .   ? -9.716  3.509   15.595   1.00 31.92  ? 1051 HOH   B O   1 
HETATM 14460 O  O   . HOH   Z  7 .   ? 6.892   4.813   -0.335   1.00 58.27  ? 1052 HOH   B O   1 
HETATM 14461 O  O   . HOH   Z  7 .   ? -29.502 -5.191  -1.985   1.00 33.41  ? 1053 HOH   B O   1 
HETATM 14462 O  O   . HOH   Z  7 .   ? -32.743 -13.458 14.464   1.00 49.72  ? 1054 HOH   B O   1 
HETATM 14463 O  O   . HOH   Z  7 .   ? -13.005 -1.181  -18.383  1.00 26.55  ? 1055 HOH   B O   1 
HETATM 14464 O  O   . HOH   Z  7 .   ? -12.180 -19.472 13.729   1.00 28.59  ? 1056 HOH   B O   1 
HETATM 14465 O  O   . HOH   Z  7 .   ? 15.616  -20.228 11.833   1.00 53.07  ? 1057 HOH   B O   1 
HETATM 14466 O  O   . HOH   Z  7 .   ? -3.083  11.557  9.736    1.00 47.70  ? 1058 HOH   B O   1 
HETATM 14467 O  O   . HOH   Z  7 .   ? -17.010 1.270   -6.648   1.00 32.63  ? 1059 HOH   B O   1 
HETATM 14468 O  O   . HOH   Z  7 .   ? -21.036 20.896  -26.670  1.00 43.71  ? 1060 HOH   B O   1 
HETATM 14469 O  O   . HOH   Z  7 .   ? -1.535  -21.670 -0.499   1.00 32.04  ? 1061 HOH   B O   1 
HETATM 14470 O  O   . HOH   Z  7 .   ? -15.570 -17.602 -5.263   1.00 43.00  ? 1062 HOH   B O   1 
HETATM 14471 O  O   . HOH   Z  7 .   ? -24.373 -12.849 15.152   1.00 35.41  ? 1063 HOH   B O   1 
HETATM 14472 O  O   . HOH   Z  7 .   ? -16.330 -19.637 14.534   1.00 40.70  ? 1064 HOH   B O   1 
HETATM 14473 O  O   . HOH   Z  7 .   ? -23.027 -9.194  1.393    1.00 35.98  ? 1065 HOH   B O   1 
HETATM 14474 O  O   . HOH   Z  7 .   ? -6.596  14.086  9.455    1.00 39.12  ? 1066 HOH   B O   1 
HETATM 14475 O  O   . HOH   Z  7 .   ? -18.683 -10.838 5.129    1.00 26.92  ? 1067 HOH   B O   1 
HETATM 14476 O  O   . HOH   Z  7 .   ? -11.361 -7.898  21.326   1.00 44.16  ? 1068 HOH   B O   1 
HETATM 14477 O  O   . HOH   Z  7 .   ? -36.373 5.720   -9.493   1.00 47.79  ? 1069 HOH   B O   1 
HETATM 14478 O  O   . HOH   Z  7 .   ? 4.374   -13.761 -24.783  1.00 40.10  ? 1070 HOH   B O   1 
HETATM 14479 O  O   . HOH   Z  7 .   ? -6.171  7.023   14.639   1.00 47.89  ? 1071 HOH   B O   1 
HETATM 14480 O  O   . HOH   Z  7 .   ? 10.118  -12.137 -14.865  1.00 56.31  ? 1072 HOH   B O   1 
HETATM 14481 O  O   . HOH   Z  7 .   ? 8.625   -2.331  -4.419   1.00 51.62  ? 1073 HOH   B O   1 
HETATM 14482 O  O   . HOH   Z  7 .   ? 4.379   -9.618  8.424    1.00 30.60  ? 1074 HOH   B O   1 
HETATM 14483 O  O   . HOH   Z  7 .   ? -17.390 -21.882 16.991   1.00 46.19  ? 1075 HOH   B O   1 
HETATM 14484 O  O   . HOH   Z  7 .   ? -10.337 -21.679 13.754   1.00 43.11  ? 1076 HOH   B O   1 
HETATM 14485 O  O   . HOH   Z  7 .   ? 5.563   -3.415  -4.732   1.00 45.39  ? 1077 HOH   B O   1 
HETATM 14486 O  O   . HOH   Z  7 .   ? -18.432 20.558  2.731    1.00 47.53  ? 1078 HOH   B O   1 
HETATM 14487 O  O   . HOH   Z  7 .   ? -30.695 9.342   7.117    1.00 44.89  ? 1079 HOH   B O   1 
HETATM 14488 O  O   . HOH   Z  7 .   ? -19.516 14.255  7.058    1.00 33.63  ? 1080 HOH   B O   1 
HETATM 14489 O  O   . HOH   Z  7 .   ? -14.307 11.520  -10.960  1.00 23.00  ? 1081 HOH   B O   1 
HETATM 14490 O  O   . HOH   Z  7 .   ? -29.258 12.092  4.281    1.00 46.16  ? 1082 HOH   B O   1 
HETATM 14491 O  O   . HOH   Z  7 .   ? -8.992  21.949  -0.410   1.00 53.89  ? 1083 HOH   B O   1 
HETATM 14492 O  O   . HOH   Z  7 .   ? -28.935 -1.740  -9.133   1.00 43.57  ? 1084 HOH   B O   1 
HETATM 14493 O  O   . HOH   Z  7 .   ? -28.910 6.247   17.995   1.00 48.48  ? 1085 HOH   B O   1 
HETATM 14494 O  O   . HOH   Z  7 .   ? -3.639  12.026  -7.237   1.00 42.81  ? 1086 HOH   B O   1 
HETATM 14495 O  O   . HOH   Z  7 .   ? -22.071 -20.218 8.757    1.00 37.22  ? 1087 HOH   B O   1 
HETATM 14496 O  O   . HOH   Z  7 .   ? -9.028  -10.502 -5.614   1.00 29.62  ? 1088 HOH   B O   1 
HETATM 14497 O  O   . HOH   Z  7 .   ? -9.670  -23.527 1.529    1.00 55.85  ? 1089 HOH   B O   1 
HETATM 14498 O  O   . HOH   Z  7 .   ? -7.155  -8.450  20.534   1.00 34.91  ? 1090 HOH   B O   1 
HETATM 14499 O  O   . HOH   Z  7 .   ? -13.830 -15.060 -6.568   1.00 36.79  ? 1091 HOH   B O   1 
HETATM 14500 O  O   . HOH   Z  7 .   ? -6.298  -8.554  -18.377  1.00 27.73  ? 1092 HOH   B O   1 
HETATM 14501 O  O   . HOH   Z  7 .   ? -28.306 -2.283  18.113   1.00 51.11  ? 1093 HOH   B O   1 
HETATM 14502 O  O   . HOH   Z  7 .   ? -9.946  0.809   -12.209  1.00 24.99  ? 1094 HOH   B O   1 
HETATM 14503 O  O   . HOH   Z  7 .   ? -11.916 10.208  -11.410  1.00 23.63  ? 1095 HOH   B O   1 
HETATM 14504 O  O   . HOH   Z  7 .   ? -31.187 10.906  3.322    1.00 36.54  ? 1096 HOH   B O   1 
HETATM 14505 O  O   . HOH   Z  7 .   ? -12.718 10.528  11.079   1.00 45.07  ? 1097 HOH   B O   1 
HETATM 14506 O  O   . HOH   Z  7 .   ? 10.493  -9.210  -15.240  1.00 65.09  ? 1098 HOH   B O   1 
HETATM 14507 O  O   . HOH   Z  7 .   ? -28.031 8.674   7.187    1.00 34.26  ? 1099 HOH   B O   1 
HETATM 14508 O  O   . HOH   Z  7 .   ? -33.831 1.252   13.968   1.00 36.08  ? 1100 HOH   B O   1 
HETATM 14509 O  O   . HOH   Z  7 .   ? -0.869  6.267   -4.621   1.00 42.12  ? 1101 HOH   B O   1 
HETATM 14510 O  O   . HOH   Z  7 .   ? -28.856 -16.824 16.503   1.00 44.30  ? 1102 HOH   B O   1 
HETATM 14511 O  O   . HOH   Z  7 .   ? -24.057 -20.994 15.599   1.00 62.75  ? 1103 HOH   B O   1 
HETATM 14512 O  O   . HOH   Z  7 .   ? -5.907  -13.095 -6.108   1.00 30.58  ? 1104 HOH   B O   1 
HETATM 14513 O  O   . HOH   Z  7 .   ? -9.337  -8.971  -8.025   1.00 32.87  ? 1105 HOH   B O   1 
HETATM 14514 O  O   . HOH   Z  7 .   ? -20.461 -6.671  -4.106   1.00 35.52  ? 1106 HOH   B O   1 
HETATM 14515 O  O   . HOH   Z  7 .   ? -14.535 8.655   11.206   1.00 40.80  ? 1107 HOH   B O   1 
HETATM 14516 O  O   . HOH   Z  7 .   ? -14.453 -8.009  2.381    1.00 23.72  ? 1108 HOH   B O   1 
HETATM 14517 O  O   . HOH   Z  7 .   ? 0.618   -24.261 18.103   1.00 54.04  ? 1109 HOH   B O   1 
HETATM 14518 O  O   . HOH   Z  7 .   ? 1.127   -14.475 16.592   1.00 34.92  ? 1110 HOH   B O   1 
HETATM 14519 O  O   . HOH   Z  7 .   ? -18.134 17.989  -20.256  1.00 39.49  ? 1111 HOH   B O   1 
HETATM 14520 O  O   . HOH   Z  7 .   ? -21.019 1.392   -4.342   1.00 35.71  ? 1112 HOH   B O   1 
HETATM 14521 O  O   . HOH   Z  7 .   ? -30.463 9.158   -31.336  1.00 54.96  ? 1113 HOH   B O   1 
HETATM 14522 O  O   . HOH   Z  7 .   ? -45.067 5.654   -5.056   1.00 38.30  ? 1114 HOH   B O   1 
HETATM 14523 O  O   . HOH   Z  7 .   ? -24.654 -3.002  2.274    1.00 33.51  ? 1115 HOH   B O   1 
HETATM 14524 O  O   . HOH   Z  7 .   ? -25.429 10.896  -25.358  1.00 25.45  ? 1116 HOH   B O   1 
HETATM 14525 O  O   . HOH   Z  7 .   ? -18.500 -23.057 4.118    1.00 52.52  ? 1117 HOH   B O   1 
HETATM 14526 O  O   . HOH   Z  7 .   ? -15.228 -18.521 -1.690   1.00 49.88  ? 1118 HOH   B O   1 
HETATM 14527 O  O   . HOH   Z  7 .   ? -0.007  -18.287 -5.530   1.00 52.25  ? 1119 HOH   B O   1 
HETATM 14528 O  O   . HOH   Z  7 .   ? -30.683 10.611  -26.798  1.00 46.84  ? 1120 HOH   B O   1 
HETATM 14529 O  O   . HOH   Z  7 .   ? -13.016 16.376  6.033    1.00 45.70  ? 1121 HOH   B O   1 
HETATM 14530 O  O   . HOH   Z  7 .   ? -28.045 10.290  -32.845  1.00 41.72  ? 1122 HOH   B O   1 
HETATM 14531 O  O   . HOH   Z  7 .   ? -27.539 3.764   10.335   1.00 40.82  ? 1123 HOH   B O   1 
HETATM 14532 O  O   . HOH   Z  7 .   ? -11.981 -4.309  19.676   1.00 37.36  ? 1124 HOH   B O   1 
HETATM 14533 O  O   . HOH   Z  7 .   ? -18.998 -5.012  -2.224   1.00 27.00  ? 1125 HOH   B O   1 
HETATM 14534 O  O   . HOH   Z  7 .   ? -33.531 5.875   -11.832  1.00 57.45  ? 1126 HOH   B O   1 
HETATM 14535 O  O   . HOH   Z  7 .   ? -38.181 -1.508  -0.767   1.00 40.21  ? 1127 HOH   B O   1 
HETATM 14536 O  O   . HOH   Z  7 .   ? -2.070  -17.221 16.556   1.00 41.91  ? 1128 HOH   B O   1 
HETATM 14537 O  O   . HOH   Z  7 .   ? 1.293   -2.315  8.600    1.00 53.02  ? 1129 HOH   B O   1 
HETATM 14538 O  O   . HOH   Z  7 .   ? -33.212 8.645   -5.420   1.00 44.81  ? 1130 HOH   B O   1 
HETATM 14539 O  O   . HOH   Z  7 .   ? -27.449 -3.493  20.705   1.00 52.01  ? 1131 HOH   B O   1 
HETATM 14540 O  O   . HOH   Z  7 .   ? -33.175 9.169   -11.638  1.00 53.65  ? 1132 HOH   B O   1 
HETATM 14541 O  O   . HOH   Z  7 .   ? -33.759 6.813   -17.035  1.00 50.64  ? 1133 HOH   B O   1 
HETATM 14542 O  O   . HOH   Z  7 .   ? -14.146 3.964   -21.899  1.00 46.28  ? 1134 HOH   B O   1 
HETATM 14543 O  O   . HOH   Z  7 .   ? -21.226 -16.737 -14.510  1.00 46.19  ? 1135 HOH   B O   1 
HETATM 14544 O  O   . HOH   Z  7 .   ? -9.850  -11.439 -9.617   1.00 43.96  ? 1136 HOH   B O   1 
HETATM 14545 O  O   . HOH   Z  7 .   ? 13.269  -19.734 -1.950   1.00 56.94  ? 1137 HOH   B O   1 
HETATM 14546 O  O   . HOH   Z  7 .   ? -4.100  13.624  9.212    1.00 40.25  ? 1138 HOH   B O   1 
HETATM 14547 O  O   . HOH   Z  7 .   ? -29.799 -3.989  -12.560  1.00 52.93  ? 1139 HOH   B O   1 
HETATM 14548 O  O   . HOH   Z  7 .   ? -0.949  12.837  -9.123   1.00 64.82  ? 1140 HOH   B O   1 
HETATM 14549 O  O   . HOH   Z  7 .   ? -25.259 -1.565  -13.137  1.00 49.33  ? 1141 HOH   B O   1 
HETATM 14550 O  O   . HOH   Z  7 .   ? -7.288  -12.101 -8.559   1.00 48.00  ? 1142 HOH   B O   1 
HETATM 14551 O  O   . HOH   Z  7 .   ? -30.883 23.094  -25.948  1.00 59.03  ? 1143 HOH   B O   1 
HETATM 14552 O  O   . HOH   Z  7 .   ? -29.597 3.668   12.073   1.00 53.29  ? 1144 HOH   B O   1 
HETATM 14553 O  O   . HOH   Z  7 .   ? -31.214 -4.892  -4.696   1.00 40.78  ? 1145 HOH   B O   1 
HETATM 14554 O  O   . HOH   Z  7 .   ? -6.818  20.013  6.978    1.00 70.28  ? 1146 HOH   B O   1 
HETATM 14555 O  O   . HOH   Z  7 .   ? -12.575 1.265   -12.609  1.00 25.50  ? 1147 HOH   B O   1 
HETATM 14556 O  O   . HOH   Z  7 .   ? -18.147 1.918   -8.574   1.00 34.92  ? 1148 HOH   B O   1 
HETATM 14557 O  O   . HOH   Z  7 .   ? -14.443 -5.979  20.124   1.00 39.55  ? 1149 HOH   B O   1 
HETATM 14558 O  O   . HOH   Z  7 .   ? -4.096  6.136   -5.167   1.00 35.87  ? 1150 HOH   B O   1 
HETATM 14559 O  O   . HOH   Z  7 .   ? -6.857  14.081  2.502    1.00 55.92  ? 1151 HOH   B O   1 
HETATM 14560 O  O   . HOH   Z  7 .   ? -0.264  -19.360 -0.606   1.00 38.50  ? 1152 HOH   B O   1 
HETATM 14561 O  O   . HOH   Z  7 .   ? -26.222 25.719  -17.087  1.00 49.92  ? 1153 HOH   B O   1 
HETATM 14562 O  O   . HOH   Z  7 .   ? 3.540   -13.075 15.025   1.00 43.36  ? 1154 HOH   B O   1 
HETATM 14563 O  O   . HOH   Z  7 .   ? -4.596  10.681  -4.383   1.00 50.45  ? 1155 HOH   B O   1 
HETATM 14564 O  O   . HOH   Z  7 .   ? -0.375  -3.688  9.911    1.00 32.23  ? 1156 HOH   B O   1 
HETATM 14565 O  O   . HOH   Z  7 .   ? 15.181  -17.375 1.599    1.00 46.08  ? 1157 HOH   B O   1 
HETATM 14566 O  O   . HOH   Z  7 .   ? 10.271  -7.373  -16.984  1.00 47.32  ? 1158 HOH   B O   1 
HETATM 14567 O  O   . HOH   Z  7 .   ? -9.538  -17.667 15.816   1.00 51.27  ? 1159 HOH   B O   1 
HETATM 14568 O  O   . HOH   Z  7 .   ? -0.223  -3.876  12.630   1.00 48.70  ? 1160 HOH   B O   1 
HETATM 14569 O  O   . HOH   Z  7 .   ? -27.853 2.580   -22.006  1.00 48.38  ? 1161 HOH   B O   1 
HETATM 14570 O  O   . HOH   Z  7 .   ? -12.633 -12.657 -7.816   1.00 62.78  ? 1162 HOH   B O   1 
HETATM 14571 O  O   . HOH   Z  7 .   ? 2.292   3.911   -20.025  1.00 41.95  ? 1163 HOH   B O   1 
HETATM 14572 O  O   . HOH   Z  7 .   ? -3.263  7.714   14.632   1.00 52.44  ? 1164 HOH   B O   1 
HETATM 14573 O  O   . HOH   Z  7 .   ? -26.574 11.559  7.284    1.00 50.08  ? 1165 HOH   B O   1 
HETATM 14574 O  O   . HOH   Z  7 .   ? -30.005 -1.190  16.260   1.00 53.89  ? 1166 HOH   B O   1 
HETATM 14575 O  O   . HOH   Z  7 .   ? -21.929 25.281  -5.349   1.00 40.04  ? 1167 HOH   B O   1 
HETATM 14576 O  O   . HOH   Z  7 .   ? 2.437   7.623   -20.651  1.00 56.30  ? 1168 HOH   B O   1 
HETATM 14577 O  O   . HOH   Z  7 .   ? -11.187 -24.039 5.404    1.00 49.15  ? 1169 HOH   B O   1 
HETATM 14578 O  O   . HOH   Z  7 .   ? -23.149 -21.125 18.605   1.00 54.41  ? 1170 HOH   B O   1 
HETATM 14579 O  O   . HOH   Z  7 .   ? -33.461 6.520   -8.846   1.00 55.56  ? 1171 HOH   B O   1 
HETATM 14580 O  O   . HOH   Z  7 .   ? -32.438 5.695   -19.082  1.00 59.83  ? 1172 HOH   B O   1 
HETATM 14581 O  O   . HOH   Z  7 .   ? 5.613   -14.657 14.942   1.00 44.11  ? 1173 HOH   B O   1 
HETATM 14582 O  O   . HOH   Z  7 .   ? -30.060 8.371   -18.595  1.00 42.00  ? 1174 HOH   B O   1 
HETATM 14583 O  O   . HOH   Z  7 .   ? -3.713  -22.482 -3.925   1.00 44.96  ? 1175 HOH   B O   1 
HETATM 14584 O  O   . HOH   Z  7 .   ? 6.352   -19.008 13.992   1.00 44.62  ? 1176 HOH   B O   1 
HETATM 14585 O  O   . HOH   Z  7 .   ? -27.313 9.025   -25.318  1.00 38.25  ? 1177 HOH   B O   1 
HETATM 14586 O  O   . HOH   Z  7 .   ? -30.669 5.576   10.805   1.00 42.04  ? 1178 HOH   B O   1 
HETATM 14587 O  O   . HOH   Z  7 .   ? 2.082   -13.262 -25.679  1.00 51.83  ? 1179 HOH   B O   1 
HETATM 14588 O  O   . HOH   Z  7 .   ? -8.153  9.154   13.893   1.00 55.09  ? 1180 HOH   B O   1 
HETATM 14589 O  O   . HOH   Z  7 .   ? -5.963  -16.136 16.787   1.00 51.00  ? 1181 HOH   B O   1 
HETATM 14590 O  O   . HOH   Z  7 .   ? -1.658  11.280  -15.524  1.00 43.09  ? 1182 HOH   B O   1 
HETATM 14591 O  O   . HOH   Z  7 .   ? -8.293  5.977   15.128   1.00 38.80  ? 1183 HOH   B O   1 
HETATM 14592 O  O   . HOH   Z  7 .   ? -20.283 -10.981 -3.921   1.00 46.37  ? 1184 HOH   B O   1 
HETATM 14593 O  O   . HOH   Z  7 .   ? 4.239   -8.413  5.717    1.00 40.10  ? 1185 HOH   B O   1 
HETATM 14594 O  O   . HOH   Z  7 .   ? -20.986 -0.915  -6.084   1.00 37.07  ? 1186 HOH   B O   1 
HETATM 14595 O  O   . HOH   Z  7 .   ? -19.917 0.055   -9.279   1.00 46.27  ? 1187 HOH   B O   1 
HETATM 14596 O  O   . HOH   Z  7 .   ? 4.349   -7.871  3.166    1.00 35.91  ? 1188 HOH   B O   1 
HETATM 14597 O  O   . HOH   Z  7 .   ? -33.424 10.986  -9.597   1.00 52.22  ? 1189 HOH   B O   1 
HETATM 14598 O  O   . HOH   Z  7 .   ? -22.847 13.977  13.710   1.00 44.64  ? 1190 HOH   B O   1 
HETATM 14599 O  O   . HOH   Z  7 .   ? -14.967 -17.823 17.900   1.00 47.68  ? 1191 HOH   B O   1 
HETATM 14600 O  O   . HOH   Z  7 .   ? -15.417 17.304  5.731    1.00 40.36  ? 1192 HOH   B O   1 
HETATM 14601 O  O   . HOH   Z  7 .   ? -9.388  -2.639  15.964   1.00 38.01  ? 1193 HOH   B O   1 
HETATM 14602 O  O   . HOH   Z  7 .   ? -32.775 21.535  -26.211  1.00 50.18  ? 1194 HOH   B O   1 
HETATM 14603 O  O   . HOH   Z  7 .   ? -23.943 -2.115  -9.132   1.00 54.96  ? 1195 HOH   B O   1 
HETATM 14604 O  O   . HOH   Z  7 .   ? -23.095 -15.017 -9.174   1.00 57.40  ? 1196 HOH   B O   1 
HETATM 14605 O  O   . HOH   Z  7 .   ? -33.515 0.760   -10.891  1.00 48.30  ? 1197 HOH   B O   1 
HETATM 14606 O  O   . HOH   Z  7 .   ? -9.928  10.417  13.873   1.00 49.84  ? 1198 HOH   B O   1 
HETATM 14607 O  O   . HOH   Z  7 .   ? -21.738 -4.197  -10.015  1.00 54.14  ? 1199 HOH   B O   1 
HETATM 14608 O  O   . HOH   Z  7 .   ? -10.928 -23.469 15.611   1.00 43.14  ? 1200 HOH   B O   1 
HETATM 14609 O  O   . HOH   Z  7 .   ? 3.760   -10.510 15.824   1.00 46.10  ? 1201 HOH   B O   1 
HETATM 14610 O  O   . HOH   Z  7 .   ? -14.633 12.567  10.131   1.00 34.08  ? 1202 HOH   B O   1 
HETATM 14611 O  O   . HOH   Z  7 .   ? -26.703 -2.322  -10.039  1.00 42.13  ? 1203 HOH   B O   1 
HETATM 14612 O  O   . HOH   Z  7 .   ? -13.635 -0.179  -20.836  1.00 39.92  ? 1204 HOH   B O   1 
HETATM 14613 O  O   . HOH   Z  7 .   ? -21.186 24.766  -2.436   1.00 46.20  ? 1205 HOH   B O   1 
HETATM 14614 O  O   . HOH   Z  7 .   ? -10.442 -19.051 17.347   1.00 47.36  ? 1206 HOH   B O   1 
HETATM 14615 O  O   . HOH   Z  7 .   ? -14.097 -19.680 15.830   1.00 41.55  ? 1207 HOH   B O   1 
HETATM 14616 O  O   . HOH   Z  7 .   ? -24.830 8.416   9.311    1.00 40.93  ? 1208 HOH   B O   1 
HETATM 14617 O  O   . HOH   Z  7 .   ? -1.222  -22.828 -2.811   1.00 39.46  ? 1209 HOH   B O   1 
HETATM 14618 O  O   . HOH   Z  7 .   ? -29.415 5.485   -26.225  1.00 47.26  ? 1210 HOH   B O   1 
HETATM 14619 O  O   . HOH   Z  7 .   ? -9.751  24.342  -1.513   1.00 74.15  ? 1211 HOH   B O   1 
HETATM 14620 O  O   . HOH   Z  7 .   ? -31.792 -0.355  14.428   1.00 52.15  ? 1212 HOH   B O   1 
HETATM 14621 O  O   . HOH   Z  7 .   ? 4.479   -7.875  10.548   1.00 34.66  ? 1213 HOH   B O   1 
HETATM 14622 O  O   . HOH   Z  7 .   ? -48.044 5.954   -4.524   1.00 59.71  ? 1214 HOH   B O   1 
HETATM 14623 O  O   . HOH   Z  7 .   ? -2.872  9.560   0.369    1.00 50.01  ? 1215 HOH   B O   1 
HETATM 14624 O  O   . HOH   Z  7 .   ? -13.273 -16.058 23.927   1.00 48.03  ? 1216 HOH   B O   1 
HETATM 14625 O  O   . HOH   Z  7 .   ? 5.446   -8.615  -27.338  1.00 44.40  ? 1217 HOH   B O   1 
HETATM 14626 O  O   . HOH   Z  7 .   ? -22.949 -6.386  -8.728   1.00 56.91  ? 1218 HOH   B O   1 
HETATM 14627 O  O   . HOH   Z  7 .   ? -22.426 22.239  2.471    1.00 56.31  ? 1219 HOH   B O   1 
HETATM 14628 O  O   . HOH   Z  7 .   ? -24.961 20.602  2.309    1.00 59.95  ? 1220 HOH   B O   1 
HETATM 14629 O  O   . HOH   AA 7 .   ? 21.670  -36.282 -81.341  1.00 40.53  ? 901  HOH   C O   1 
HETATM 14630 O  O   . HOH   AA 7 .   ? 23.704  -60.307 -89.731  1.00 43.47  ? 902  HOH   C O   1 
HETATM 14631 O  O   . HOH   AA 7 .   ? 5.523   -54.536 -78.666  1.00 42.73  ? 903  HOH   C O   1 
HETATM 14632 O  O   . HOH   AA 7 .   ? -5.241  -71.868 -78.298  1.00 62.85  ? 904  HOH   C O   1 
HETATM 14633 O  O   . HOH   AA 7 .   ? -2.236  -63.633 -62.546  1.00 49.85  ? 905  HOH   C O   1 
HETATM 14634 O  O   . HOH   AA 7 .   ? 1.547   -74.618 -55.787  1.00 43.13  ? 906  HOH   C O   1 
HETATM 14635 O  O   . HOH   AA 7 .   ? 31.383  -32.583 -79.850  1.00 48.29  ? 907  HOH   C O   1 
HETATM 14636 O  O   . HOH   AA 7 .   ? 13.867  -47.383 -74.257  1.00 40.59  ? 908  HOH   C O   1 
HETATM 14637 O  O   . HOH   AA 7 .   ? 15.101  -47.335 -63.868  1.00 36.09  ? 909  HOH   C O   1 
HETATM 14638 O  O   . HOH   AA 7 .   ? 29.419  -37.850 -78.658  1.00 61.68  ? 910  HOH   C O   1 
HETATM 14639 O  O   . HOH   AA 7 .   ? 3.661   -61.520 -65.827  1.00 23.51  ? 911  HOH   C O   1 
HETATM 14640 O  O   . HOH   AA 7 .   ? -5.782  -60.926 -70.236  1.00 34.66  ? 912  HOH   C O   1 
HETATM 14641 O  O   . HOH   AA 7 .   ? -7.657  -66.434 -64.728  1.00 43.71  ? 913  HOH   C O   1 
HETATM 14642 O  O   . HOH   AA 7 .   ? 7.317   -34.343 -85.623  1.00 57.21  ? 914  HOH   C O   1 
HETATM 14643 O  O   . HOH   AA 7 .   ? -2.005  -65.339 -66.043  1.00 30.36  ? 915  HOH   C O   1 
HETATM 14644 O  O   . HOH   AA 7 .   ? -10.084 -56.053 -81.686  1.00 47.77  ? 916  HOH   C O   1 
HETATM 14645 O  O   . HOH   AA 7 .   ? 31.663  -45.348 -80.208  1.00 38.95  ? 917  HOH   C O   1 
HETATM 14646 O  O   . HOH   AA 7 .   ? 7.529   -54.848 -72.261  1.00 37.77  ? 918  HOH   C O   1 
HETATM 14647 O  O   . HOH   AA 7 .   ? -4.262  -71.509 -73.197  1.00 49.26  ? 919  HOH   C O   1 
HETATM 14648 O  O   . HOH   AA 7 .   ? 3.294   -59.551 -79.073  1.00 28.63  ? 920  HOH   C O   1 
HETATM 14649 O  O   . HOH   AA 7 .   ? 6.468   -78.000 -60.858  1.00 34.82  ? 921  HOH   C O   1 
HETATM 14650 O  O   . HOH   AA 7 .   ? 18.422  -48.835 -101.965 1.00 39.65  ? 922  HOH   C O   1 
HETATM 14651 O  O   . HOH   AA 7 .   ? -5.528  -66.713 -73.259  1.00 50.08  ? 923  HOH   C O   1 
HETATM 14652 O  O   . HOH   AA 7 .   ? 14.270  -41.831 -64.713  1.00 39.06  ? 924  HOH   C O   1 
HETATM 14653 O  O   . HOH   AA 7 .   ? 9.243   -79.325 -65.104  1.00 45.16  ? 925  HOH   C O   1 
HETATM 14654 O  O   . HOH   AA 7 .   ? 2.047   -44.947 -99.375  1.00 25.62  ? 926  HOH   C O   1 
HETATM 14655 O  O   . HOH   AA 7 .   ? 25.836  -60.818 -59.839  1.00 32.33  ? 927  HOH   C O   1 
HETATM 14656 O  O   . HOH   AA 7 .   ? 14.876  -54.383 -95.016  1.00 23.22  ? 928  HOH   C O   1 
HETATM 14657 O  O   . HOH   AA 7 .   ? 23.681  -64.490 -59.398  1.00 32.50  ? 929  HOH   C O   1 
HETATM 14658 O  O   . HOH   AA 7 .   ? -0.458  -67.869 -86.391  1.00 61.07  ? 930  HOH   C O   1 
HETATM 14659 O  O   . HOH   AA 7 .   ? 14.037  -42.785 -103.630 1.00 26.73  ? 931  HOH   C O   1 
HETATM 14660 O  O   . HOH   AA 7 .   ? 26.380  -51.291 -74.139  1.00 26.44  ? 932  HOH   C O   1 
HETATM 14661 O  O   . HOH   AA 7 .   ? 23.054  -47.527 -97.923  1.00 45.02  ? 933  HOH   C O   1 
HETATM 14662 O  O   . HOH   AA 7 .   ? 3.701   -65.315 -100.345 1.00 39.42  ? 934  HOH   C O   1 
HETATM 14663 O  O   . HOH   AA 7 .   ? 24.631  -64.289 -91.869  1.00 43.25  ? 935  HOH   C O   1 
HETATM 14664 O  O   . HOH   AA 7 .   ? 30.426  -56.169 -74.967  1.00 31.77  ? 936  HOH   C O   1 
HETATM 14665 O  O   . HOH   AA 7 .   ? 21.995  -67.957 -59.652  1.00 36.87  ? 937  HOH   C O   1 
HETATM 14666 O  O   . HOH   AA 7 .   ? 16.263  -60.486 -85.702  1.00 24.86  ? 938  HOH   C O   1 
HETATM 14667 O  O   . HOH   AA 7 .   ? 19.176  -46.204 -77.292  1.00 21.18  ? 939  HOH   C O   1 
HETATM 14668 O  O   . HOH   AA 7 .   ? 25.896  -48.426 -52.968  1.00 23.78  ? 940  HOH   C O   1 
HETATM 14669 O  O   . HOH   AA 7 .   ? -3.802  -63.203 -89.736  1.00 32.76  ? 941  HOH   C O   1 
HETATM 14670 O  O   . HOH   AA 7 .   ? 43.030  -45.960 -88.316  1.00 52.68  ? 942  HOH   C O   1 
HETATM 14671 O  O   . HOH   AA 7 .   ? 19.932  -70.191 -73.282  1.00 35.58  ? 943  HOH   C O   1 
HETATM 14672 O  O   . HOH   AA 7 .   ? 0.286   -62.217 -63.794  1.00 41.02  ? 944  HOH   C O   1 
HETATM 14673 O  O   . HOH   AA 7 .   ? 20.826  -67.125 -84.080  1.00 29.04  ? 945  HOH   C O   1 
HETATM 14674 O  O   . HOH   AA 7 .   ? 29.093  -56.739 -79.936  1.00 35.51  ? 946  HOH   C O   1 
HETATM 14675 O  O   . HOH   AA 7 .   ? 20.233  -36.290 -55.932  1.00 25.78  ? 947  HOH   C O   1 
HETATM 14676 O  O   . HOH   AA 7 .   ? 26.977  -42.956 -78.549  1.00 29.04  ? 948  HOH   C O   1 
HETATM 14677 O  O   . HOH   AA 7 .   ? -2.299  -44.840 -77.795  1.00 46.02  ? 949  HOH   C O   1 
HETATM 14678 O  O   . HOH   AA 7 .   ? 9.658   -37.570 -93.338  1.00 28.50  ? 950  HOH   C O   1 
HETATM 14679 O  O   . HOH   AA 7 .   ? 3.125   -39.698 -83.819  1.00 44.36  ? 951  HOH   C O   1 
HETATM 14680 O  O   . HOH   AA 7 .   ? 12.890  -41.544 -99.705  1.00 28.94  ? 952  HOH   C O   1 
HETATM 14681 O  O   . HOH   AA 7 .   ? 32.049  -41.964 -93.616  1.00 44.94  ? 953  HOH   C O   1 
HETATM 14682 O  O   . HOH   AA 7 .   ? 23.930  -58.899 -73.342  1.00 27.46  ? 954  HOH   C O   1 
HETATM 14683 O  O   . HOH   AA 7 .   ? 30.091  -56.529 -62.108  1.00 33.56  ? 955  HOH   C O   1 
HETATM 14684 O  O   . HOH   AA 7 .   ? -1.808  -63.417 -57.087  1.00 37.23  ? 956  HOH   C O   1 
HETATM 14685 O  O   . HOH   AA 7 .   ? 23.264  -59.552 -83.065  1.00 32.01  ? 957  HOH   C O   1 
HETATM 14686 O  O   . HOH   AA 7 .   ? 4.551   -46.722 -84.533  1.00 30.20  ? 958  HOH   C O   1 
HETATM 14687 O  O   . HOH   AA 7 .   ? 28.521  -48.029 -55.719  1.00 32.05  ? 959  HOH   C O   1 
HETATM 14688 O  O   . HOH   AA 7 .   ? 0.716   -63.004 -92.232  1.00 41.42  ? 960  HOH   C O   1 
HETATM 14689 O  O   . HOH   AA 7 .   ? 33.417  -39.218 -70.036  1.00 52.03  ? 961  HOH   C O   1 
HETATM 14690 O  O   . HOH   AA 7 .   ? 8.738   -73.934 -85.298  1.00 32.57  ? 962  HOH   C O   1 
HETATM 14691 O  O   . HOH   AA 7 .   ? 20.017  -39.412 -93.702  1.00 24.49  ? 963  HOH   C O   1 
HETATM 14692 O  O   . HOH   AA 7 .   ? 6.901   -60.322 -76.853  1.00 28.44  ? 964  HOH   C O   1 
HETATM 14693 O  O   . HOH   AA 7 .   ? 3.358   -80.919 -74.102  1.00 27.32  ? 965  HOH   C O   1 
HETATM 14694 O  O   . HOH   AA 7 .   ? 35.418  -40.171 -93.622  1.00 35.89  ? 966  HOH   C O   1 
HETATM 14695 O  O   . HOH   AA 7 .   ? 20.123  -28.605 -80.112  1.00 46.68  ? 967  HOH   C O   1 
HETATM 14696 O  O   . HOH   AA 7 .   ? 23.800  -65.524 -73.484  1.00 37.01  ? 968  HOH   C O   1 
HETATM 14697 O  O   . HOH   AA 7 .   ? 4.540   -39.797 -86.697  1.00 30.95  ? 969  HOH   C O   1 
HETATM 14698 O  O   . HOH   AA 7 .   ? 20.466  -46.881 -61.074  1.00 32.97  ? 970  HOH   C O   1 
HETATM 14699 O  O   . HOH   AA 7 .   ? 21.140  -66.981 -63.044  1.00 28.59  ? 971  HOH   C O   1 
HETATM 14700 O  O   . HOH   AA 7 .   ? 41.279  -37.148 -93.317  1.00 64.43  ? 972  HOH   C O   1 
HETATM 14701 O  O   . HOH   AA 7 .   ? 9.538   -64.774 -88.973  1.00 18.11  ? 973  HOH   C O   1 
HETATM 14702 O  O   . HOH   AA 7 .   ? 15.295  -35.371 -65.493  1.00 38.98  ? 974  HOH   C O   1 
HETATM 14703 O  O   . HOH   AA 7 .   ? 1.932   -56.408 -85.531  1.00 21.36  ? 975  HOH   C O   1 
HETATM 14704 O  O   . HOH   AA 7 .   ? 5.427   -35.829 -86.729  1.00 40.91  ? 976  HOH   C O   1 
HETATM 14705 O  O   . HOH   AA 7 .   ? 30.162  -51.291 -88.220  1.00 41.40  ? 977  HOH   C O   1 
HETATM 14706 O  O   . HOH   AA 7 .   ? 9.220   -36.874 -71.270  1.00 60.37  ? 978  HOH   C O   1 
HETATM 14707 O  O   . HOH   AA 7 .   ? 31.602  -39.428 -92.799  1.00 31.46  ? 979  HOH   C O   1 
HETATM 14708 O  O   . HOH   AA 7 .   ? -12.709 -55.240 -92.277  1.00 38.58  ? 980  HOH   C O   1 
HETATM 14709 O  O   . HOH   AA 7 .   ? 1.879   -47.700 -101.493 1.00 26.57  ? 981  HOH   C O   1 
HETATM 14710 O  O   . HOH   AA 7 .   ? 33.122  -41.860 -80.261  1.00 35.99  ? 982  HOH   C O   1 
HETATM 14711 O  O   . HOH   AA 7 .   ? 16.485  -40.304 -94.123  1.00 24.61  ? 983  HOH   C O   1 
HETATM 14712 O  O   . HOH   AA 7 .   ? 23.289  -32.440 -58.118  1.00 57.78  ? 984  HOH   C O   1 
HETATM 14713 O  O   . HOH   AA 7 .   ? 13.451  -37.824 -95.122  1.00 27.42  ? 985  HOH   C O   1 
HETATM 14714 O  O   . HOH   AA 7 .   ? 15.215  -34.287 -92.704  1.00 36.27  ? 986  HOH   C O   1 
HETATM 14715 O  O   . HOH   AA 7 .   ? 17.125  -72.345 -79.771  1.00 32.26  ? 987  HOH   C O   1 
HETATM 14716 O  O   . HOH   AA 7 .   ? 23.283  -38.897 -82.004  1.00 29.11  ? 988  HOH   C O   1 
HETATM 14717 O  O   . HOH   AA 7 .   ? 1.998   -58.590 -87.339  1.00 28.26  ? 989  HOH   C O   1 
HETATM 14718 O  O   . HOH   AA 7 .   ? 24.002  -70.691 -69.922  1.00 48.89  ? 990  HOH   C O   1 
HETATM 14719 O  O   . HOH   AA 7 .   ? 0.981   -60.525 -79.849  1.00 29.59  ? 991  HOH   C O   1 
HETATM 14720 O  O   . HOH   AA 7 .   ? 11.870  -57.127 -66.581  1.00 23.51  ? 992  HOH   C O   1 
HETATM 14721 O  O   . HOH   AA 7 .   ? 19.159  -71.311 -91.009  1.00 40.60  ? 993  HOH   C O   1 
HETATM 14722 O  O   . HOH   AA 7 .   ? -5.489  -63.483 -82.833  1.00 26.64  ? 994  HOH   C O   1 
HETATM 14723 O  O   . HOH   AA 7 .   ? 2.788   -48.120 -83.127  1.00 40.18  ? 995  HOH   C O   1 
HETATM 14724 O  O   . HOH   AA 7 .   ? 11.576  -60.735 -70.014  1.00 24.29  ? 996  HOH   C O   1 
HETATM 14725 O  O   . HOH   AA 7 .   ? 25.525  -49.044 -65.379  1.00 27.61  ? 997  HOH   C O   1 
HETATM 14726 O  O   . HOH   AA 7 .   ? -12.722 -51.906 -86.046  1.00 36.53  ? 998  HOH   C O   1 
HETATM 14727 O  O   . HOH   AA 7 .   ? 8.000   -65.566 -99.696  1.00 39.24  ? 999  HOH   C O   1 
HETATM 14728 O  O   . HOH   AA 7 .   ? 25.337  -63.580 -77.138  1.00 44.58  ? 1000 HOH   C O   1 
HETATM 14729 O  O   . HOH   AA 7 .   ? 7.662   -59.164 -83.757  1.00 23.68  ? 1001 HOH   C O   1 
HETATM 14730 O  O   . HOH   AA 7 .   ? 22.984  -59.605 -87.518  1.00 30.53  ? 1002 HOH   C O   1 
HETATM 14731 O  O   . HOH   AA 7 .   ? -6.808  -64.386 -74.869  1.00 47.29  ? 1003 HOH   C O   1 
HETATM 14732 O  O   . HOH   AA 7 .   ? -14.064 -56.994 -82.368  1.00 59.98  ? 1004 HOH   C O   1 
HETATM 14733 O  O   . HOH   AA 7 .   ? 23.184  -43.435 -99.314  1.00 53.58  ? 1005 HOH   C O   1 
HETATM 14734 O  O   . HOH   AA 7 .   ? 8.349   -64.876 -86.368  1.00 19.92  ? 1006 HOH   C O   1 
HETATM 14735 O  O   . HOH   AA 7 .   ? 3.877   -42.310 -100.423 1.00 49.49  ? 1007 HOH   C O   1 
HETATM 14736 O  O   . HOH   AA 7 .   ? 16.361  -44.871 -64.532  1.00 30.85  ? 1008 HOH   C O   1 
HETATM 14737 O  O   . HOH   AA 7 .   ? 5.107   -53.615 -69.028  1.00 34.18  ? 1009 HOH   C O   1 
HETATM 14738 O  O   . HOH   AA 7 .   ? 22.708  -61.331 -85.399  1.00 27.56  ? 1010 HOH   C O   1 
HETATM 14739 O  O   . HOH   AA 7 .   ? 11.891  -63.120 -100.728 1.00 38.05  ? 1011 HOH   C O   1 
HETATM 14740 O  O   . HOH   AA 7 .   ? 12.264  -44.126 -65.941  1.00 43.19  ? 1012 HOH   C O   1 
HETATM 14741 O  O   . HOH   AA 7 .   ? 16.196  -56.075 -71.273  1.00 23.67  ? 1013 HOH   C O   1 
HETATM 14742 O  O   . HOH   AA 7 .   ? 2.908   -57.440 -71.544  1.00 26.12  ? 1014 HOH   C O   1 
HETATM 14743 O  O   . HOH   AA 7 .   ? 10.284  -39.134 -79.959  1.00 43.24  ? 1015 HOH   C O   1 
HETATM 14744 O  O   . HOH   AA 7 .   ? 15.159  -54.416 -99.544  1.00 46.27  ? 1016 HOH   C O   1 
HETATM 14745 O  O   . HOH   AA 7 .   ? 0.396   -75.222 -76.011  1.00 28.80  ? 1017 HOH   C O   1 
HETATM 14746 O  O   . HOH   AA 7 .   ? 10.022  -39.750 -76.287  1.00 40.49  ? 1018 HOH   C O   1 
HETATM 14747 O  O   . HOH   AA 7 .   ? 0.010   -53.424 -81.332  1.00 39.05  ? 1019 HOH   C O   1 
HETATM 14748 O  O   . HOH   AA 7 .   ? 25.444  -35.974 -96.785  1.00 45.04  ? 1020 HOH   C O   1 
HETATM 14749 O  O   . HOH   AA 7 .   ? 13.480  -65.692 -80.605  1.00 24.57  ? 1021 HOH   C O   1 
HETATM 14750 O  O   . HOH   AA 7 .   ? 4.072   -53.320 -66.701  1.00 31.74  ? 1022 HOH   C O   1 
HETATM 14751 O  O   . HOH   AA 7 .   ? 0.204   -75.464 -79.870  1.00 48.08  ? 1023 HOH   C O   1 
HETATM 14752 O  O   . HOH   AA 7 .   ? -1.294  -51.887 -76.340  1.00 52.15  ? 1024 HOH   C O   1 
HETATM 14753 O  O   . HOH   AA 7 .   ? 9.940   -47.416 -85.945  1.00 24.65  ? 1025 HOH   C O   1 
HETATM 14754 O  O   . HOH   AA 7 .   ? 16.101  -60.711 -97.176  1.00 32.19  ? 1026 HOH   C O   1 
HETATM 14755 O  O   . HOH   AA 7 .   ? 18.608  -71.260 -75.425  1.00 47.89  ? 1027 HOH   C O   1 
HETATM 14756 O  O   . HOH   AA 7 .   ? 22.178  -34.720 -77.497  1.00 49.02  ? 1028 HOH   C O   1 
HETATM 14757 O  O   . HOH   AA 7 .   ? -1.087  -57.275 -66.705  1.00 38.55  ? 1029 HOH   C O   1 
HETATM 14758 O  O   . HOH   AA 7 .   ? 28.167  -48.758 -72.989  1.00 24.47  ? 1030 HOH   C O   1 
HETATM 14759 O  O   . HOH   AA 7 .   ? 21.337  -51.304 -96.725  1.00 33.96  ? 1031 HOH   C O   1 
HETATM 14760 O  O   . HOH   AA 7 .   ? 7.425   -77.793 -84.310  1.00 42.73  ? 1032 HOH   C O   1 
HETATM 14761 O  O   . HOH   AA 7 .   ? 30.007  -59.438 -61.085  1.00 40.25  ? 1033 HOH   C O   1 
HETATM 14762 O  O   . HOH   AA 7 .   ? 25.429  -53.203 -94.249  1.00 43.58  ? 1034 HOH   C O   1 
HETATM 14763 O  O   . HOH   AA 7 .   ? 21.854  -44.343 -72.936  1.00 22.17  ? 1035 HOH   C O   1 
HETATM 14764 O  O   . HOH   AA 7 .   ? 0.292   -60.134 -91.778  1.00 29.78  ? 1036 HOH   C O   1 
HETATM 14765 O  O   . HOH   AA 7 .   ? 15.600  -45.948 -68.980  1.00 28.51  ? 1037 HOH   C O   1 
HETATM 14766 O  O   . HOH   AA 7 .   ? 8.365   -35.652 -91.599  1.00 28.89  ? 1038 HOH   C O   1 
HETATM 14767 O  O   . HOH   AA 7 .   ? 12.170  -43.271 -90.394  1.00 25.33  ? 1039 HOH   C O   1 
HETATM 14768 O  O   . HOH   AA 7 .   ? -5.051  -66.679 -65.323  1.00 35.61  ? 1040 HOH   C O   1 
HETATM 14769 O  O   . HOH   AA 7 .   ? 7.443   -45.671 -79.162  1.00 32.78  ? 1041 HOH   C O   1 
HETATM 14770 O  O   . HOH   AA 7 .   ? 13.469  -32.734 -86.345  1.00 44.64  ? 1042 HOH   C O   1 
HETATM 14771 O  O   . HOH   AA 7 .   ? 13.199  -75.829 -71.059  1.00 32.76  ? 1043 HOH   C O   1 
HETATM 14772 O  O   . HOH   AA 7 .   ? 9.842   -58.881 -71.001  1.00 23.82  ? 1044 HOH   C O   1 
HETATM 14773 O  O   . HOH   AA 7 .   ? 32.330  -46.572 -90.049  1.00 37.59  ? 1045 HOH   C O   1 
HETATM 14774 O  O   . HOH   AA 7 .   ? 14.879  -35.815 -88.790  1.00 29.72  ? 1046 HOH   C O   1 
HETATM 14775 O  O   . HOH   AA 7 .   ? 9.897   -40.060 -91.310  1.00 21.99  ? 1047 HOH   C O   1 
HETATM 14776 O  O   . HOH   AA 7 .   ? 3.396   -73.036 -49.184  1.00 45.69  ? 1048 HOH   C O   1 
HETATM 14777 O  O   . HOH   AA 7 .   ? -7.503  -69.874 -82.815  1.00 42.25  ? 1049 HOH   C O   1 
HETATM 14778 O  O   . HOH   AA 7 .   ? 24.245  -35.560 -81.092  1.00 32.91  ? 1050 HOH   C O   1 
HETATM 14779 O  O   . HOH   AA 7 .   ? 7.103   -46.337 -86.622  1.00 25.30  ? 1051 HOH   C O   1 
HETATM 14780 O  O   . HOH   AA 7 .   ? 1.533   -44.450 -96.743  1.00 28.34  ? 1052 HOH   C O   1 
HETATM 14781 O  O   . HOH   AA 7 .   ? 17.188  -73.370 -87.486  1.00 41.72  ? 1053 HOH   C O   1 
HETATM 14782 O  O   . HOH   AA 7 .   ? -4.879  -50.452 -96.930  1.00 35.14  ? 1054 HOH   C O   1 
HETATM 14783 O  O   . HOH   AA 7 .   ? -5.830  -68.996 -67.597  1.00 39.10  ? 1055 HOH   C O   1 
HETATM 14784 O  O   . HOH   AA 7 .   ? 23.118  -66.463 -64.913  1.00 27.56  ? 1056 HOH   C O   1 
HETATM 14785 O  O   . HOH   AA 7 .   ? 31.342  -53.996 -76.959  1.00 50.51  ? 1057 HOH   C O   1 
HETATM 14786 O  O   . HOH   AA 7 .   ? 15.732  -58.132 -69.224  1.00 24.47  ? 1058 HOH   C O   1 
HETATM 14787 O  O   . HOH   AA 7 .   ? -5.363  -68.079 -84.954  1.00 35.33  ? 1059 HOH   C O   1 
HETATM 14788 O  O   . HOH   AA 7 .   ? 9.974   -48.591 -66.645  1.00 28.96  ? 1060 HOH   C O   1 
HETATM 14789 O  O   . HOH   AA 7 .   ? 5.465   -84.032 -73.129  1.00 45.44  ? 1061 HOH   C O   1 
HETATM 14790 O  O   . HOH   AA 7 .   ? 28.441  -64.544 -72.925  1.00 54.68  ? 1062 HOH   C O   1 
HETATM 14791 O  O   . HOH   AA 7 .   ? 30.441  -54.025 -60.566  1.00 35.23  ? 1063 HOH   C O   1 
HETATM 14792 O  O   . HOH   AA 7 .   ? 19.376  -48.722 -63.192  1.00 22.80  ? 1064 HOH   C O   1 
HETATM 14793 O  O   . HOH   AA 7 .   ? -10.431 -63.069 -72.146  1.00 50.61  ? 1065 HOH   C O   1 
HETATM 14794 O  O   . HOH   AA 7 .   ? 23.007  -68.671 -91.144  1.00 45.72  ? 1066 HOH   C O   1 
HETATM 14795 O  O   . HOH   AA 7 .   ? 12.295  -47.675 -66.212  1.00 30.38  ? 1067 HOH   C O   1 
HETATM 14796 O  O   . HOH   AA 7 .   ? 30.108  -47.748 -90.012  1.00 28.34  ? 1068 HOH   C O   1 
HETATM 14797 O  O   . HOH   AA 7 .   ? 30.064  -43.490 -56.808  1.00 46.13  ? 1069 HOH   C O   1 
HETATM 14798 O  O   . HOH   AA 7 .   ? -8.056  -58.586 -95.403  1.00 35.58  ? 1070 HOH   C O   1 
HETATM 14799 O  O   . HOH   AA 7 .   ? 18.736  -50.669 -99.673  1.00 48.53  ? 1071 HOH   C O   1 
HETATM 14800 O  O   . HOH   AA 7 .   ? 8.707   -58.594 -74.892  1.00 31.56  ? 1072 HOH   C O   1 
HETATM 14801 O  O   . HOH   AA 7 .   ? 2.208   -55.686 -75.172  1.00 29.45  ? 1073 HOH   C O   1 
HETATM 14802 O  O   . HOH   AA 7 .   ? -3.542  -52.231 -79.589  1.00 34.41  ? 1074 HOH   C O   1 
HETATM 14803 O  O   . HOH   AA 7 .   ? -2.014  -44.009 -98.593  1.00 38.24  ? 1075 HOH   C O   1 
HETATM 14804 O  O   . HOH   AA 7 .   ? -2.321  -67.588 -48.732  1.00 39.98  ? 1076 HOH   C O   1 
HETATM 14805 O  O   . HOH   AA 7 .   ? 22.877  -61.128 -73.172  1.00 46.32  ? 1077 HOH   C O   1 
HETATM 14806 O  O   . HOH   AA 7 .   ? 9.379   -58.002 -68.231  1.00 24.12  ? 1078 HOH   C O   1 
HETATM 14807 O  O   . HOH   AA 7 .   ? 5.347   -50.680 -77.541  1.00 39.77  ? 1079 HOH   C O   1 
HETATM 14808 O  O   . HOH   AA 7 .   ? 1.520   -53.330 -76.601  1.00 37.24  ? 1080 HOH   C O   1 
HETATM 14809 O  O   . HOH   AA 7 .   ? 11.892  -42.162 -74.993  1.00 35.82  ? 1081 HOH   C O   1 
HETATM 14810 O  O   . HOH   AA 7 .   ? 19.864  -44.128 -75.492  1.00 29.72  ? 1082 HOH   C O   1 
HETATM 14811 O  O   . HOH   AA 7 .   ? 16.253  -33.985 -82.911  1.00 51.68  ? 1083 HOH   C O   1 
HETATM 14812 O  O   . HOH   AA 7 .   ? 1.944   -36.329 -97.326  1.00 57.92  ? 1084 HOH   C O   1 
HETATM 14813 O  O   . HOH   AA 7 .   ? 19.937  -64.212 -96.168  1.00 44.97  ? 1085 HOH   C O   1 
HETATM 14814 O  O   . HOH   AA 7 .   ? 16.021  -32.692 -89.689  1.00 38.04  ? 1086 HOH   C O   1 
HETATM 14815 O  O   . HOH   AA 7 .   ? 34.542  -36.244 -95.343  1.00 37.41  ? 1087 HOH   C O   1 
HETATM 14816 O  O   . HOH   AA 7 .   ? 9.008   -33.568 -96.820  1.00 42.14  ? 1088 HOH   C O   1 
HETATM 14817 O  O   . HOH   AA 7 .   ? 11.562  -68.864 -70.557  1.00 23.55  ? 1089 HOH   C O   1 
HETATM 14818 O  O   . HOH   AA 7 .   ? -0.941  -55.030 -71.428  1.00 44.91  ? 1090 HOH   C O   1 
HETATM 14819 O  O   . HOH   AA 7 .   ? 3.623   -37.098 -90.379  1.00 33.16  ? 1091 HOH   C O   1 
HETATM 14820 O  O   . HOH   AA 7 .   ? 26.189  -32.463 -99.357  1.00 59.58  ? 1092 HOH   C O   1 
HETATM 14821 O  O   . HOH   AA 7 .   ? 12.646  -56.091 -63.083  1.00 23.65  ? 1093 HOH   C O   1 
HETATM 14822 O  O   . HOH   AA 7 .   ? 35.129  -30.951 -83.962  1.00 46.39  ? 1094 HOH   C O   1 
HETATM 14823 O  O   . HOH   AA 7 .   ? -0.204  -58.668 -64.774  1.00 36.07  ? 1095 HOH   C O   1 
HETATM 14824 O  O   . HOH   AA 7 .   ? 15.215  -77.043 -72.487  1.00 48.98  ? 1096 HOH   C O   1 
HETATM 14825 O  O   . HOH   AA 7 .   ? 1.227   -54.272 -83.815  1.00 29.84  ? 1097 HOH   C O   1 
HETATM 14826 O  O   . HOH   AA 7 .   ? 2.128   -86.104 -69.281  1.00 49.67  ? 1098 HOH   C O   1 
HETATM 14827 O  O   . HOH   AA 7 .   ? -3.427  -69.425 -85.771  1.00 46.39  ? 1099 HOH   C O   1 
HETATM 14828 O  O   . HOH   AA 7 .   ? 32.285  -38.464 -95.597  1.00 48.93  ? 1100 HOH   C O   1 
HETATM 14829 O  O   . HOH   AA 7 .   ? -2.478  -65.739 -88.951  1.00 34.24  ? 1101 HOH   C O   1 
HETATM 14830 O  O   . HOH   AA 7 .   ? 16.900  -46.708 -75.852  1.00 29.92  ? 1102 HOH   C O   1 
HETATM 14831 O  O   . HOH   AA 7 .   ? 4.847   -58.710 -77.205  1.00 30.79  ? 1103 HOH   C O   1 
HETATM 14832 O  O   . HOH   AA 7 .   ? 6.772   -42.123 -104.990 1.00 41.75  ? 1104 HOH   C O   1 
HETATM 14833 O  O   . HOH   AA 7 .   ? -4.918  -67.945 -54.876  1.00 53.71  ? 1105 HOH   C O   1 
HETATM 14834 O  O   . HOH   AA 7 .   ? 6.497   -71.618 -88.612  1.00 33.31  ? 1106 HOH   C O   1 
HETATM 14835 O  O   . HOH   AA 7 .   ? 28.834  -63.009 -66.091  1.00 43.19  ? 1107 HOH   C O   1 
HETATM 14836 O  O   . HOH   AA 7 .   ? 22.029  -69.393 -74.270  1.00 48.94  ? 1108 HOH   C O   1 
HETATM 14837 O  O   . HOH   AA 7 .   ? -5.633  -52.311 -76.986  1.00 37.97  ? 1109 HOH   C O   1 
HETATM 14838 O  O   . HOH   AA 7 .   ? 15.736  -24.739 -95.998  1.00 59.85  ? 1110 HOH   C O   1 
HETATM 14839 O  O   . HOH   AA 7 .   ? 36.618  -54.722 -58.303  1.00 52.13  ? 1111 HOH   C O   1 
HETATM 14840 O  O   . HOH   AA 7 .   ? 16.473  -48.298 -73.466  1.00 31.94  ? 1112 HOH   C O   1 
HETATM 14841 O  O   . HOH   AA 7 .   ? -1.705  -53.541 -102.255 1.00 46.59  ? 1113 HOH   C O   1 
HETATM 14842 O  O   . HOH   AA 7 .   ? 18.588  -45.374 -72.937  1.00 36.09  ? 1114 HOH   C O   1 
HETATM 14843 O  O   . HOH   AA 7 .   ? 4.629   -40.643 -67.039  1.00 39.61  ? 1115 HOH   C O   1 
HETATM 14844 O  O   . HOH   AA 7 .   ? 7.730   -75.213 -61.260  1.00 33.68  ? 1116 HOH   C O   1 
HETATM 14845 O  O   . HOH   AA 7 .   ? 13.032  -67.906 -92.653  1.00 52.26  ? 1117 HOH   C O   1 
HETATM 14846 O  O   . HOH   AA 7 .   ? -1.870  -61.008 -91.782  1.00 44.85  ? 1118 HOH   C O   1 
HETATM 14847 O  O   . HOH   AA 7 .   ? 13.916  -67.431 -70.119  1.00 24.36  ? 1119 HOH   C O   1 
HETATM 14848 O  O   . HOH   AA 7 .   ? 19.924  -44.981 -99.150  1.00 45.24  ? 1120 HOH   C O   1 
HETATM 14849 O  O   . HOH   AA 7 .   ? 15.640  -33.347 -87.413  1.00 44.54  ? 1121 HOH   C O   1 
HETATM 14850 O  O   . HOH   AA 7 .   ? 15.474  -35.553 -95.174  1.00 38.54  ? 1122 HOH   C O   1 
HETATM 14851 O  O   . HOH   AA 7 .   ? 27.048  -42.845 -98.128  1.00 34.75  ? 1123 HOH   C O   1 
HETATM 14852 O  O   . HOH   AA 7 .   ? 22.069  -68.078 -94.040  1.00 50.45  ? 1124 HOH   C O   1 
HETATM 14853 O  O   . HOH   AA 7 .   ? 0.928   -27.883 -93.048  1.00 53.00  ? 1125 HOH   C O   1 
HETATM 14854 O  O   . HOH   AA 7 .   ? 19.357  -70.519 -79.194  1.00 33.80  ? 1126 HOH   C O   1 
HETATM 14855 O  O   . HOH   AA 7 .   ? 6.812   -52.262 -79.372  1.00 27.55  ? 1127 HOH   C O   1 
HETATM 14856 O  O   . HOH   AA 7 .   ? 0.284   -68.225 -56.047  1.00 29.51  ? 1128 HOH   C O   1 
HETATM 14857 O  O   . HOH   AA 7 .   ? 1.117   -38.275 -89.760  1.00 48.48  ? 1129 HOH   C O   1 
HETATM 14858 O  O   . HOH   AA 7 .   ? 11.667  -61.308 -59.740  1.00 41.44  ? 1130 HOH   C O   1 
HETATM 14859 O  O   . HOH   AA 7 .   ? 31.842  -60.860 -62.369  1.00 48.59  ? 1131 HOH   C O   1 
HETATM 14860 O  O   . HOH   AA 7 .   ? 0.547   -55.187 -68.315  1.00 53.62  ? 1132 HOH   C O   1 
HETATM 14861 O  O   . HOH   AA 7 .   ? 21.629  -63.474 -76.463  1.00 34.19  ? 1133 HOH   C O   1 
HETATM 14862 O  O   . HOH   AA 7 .   ? 7.484   -81.882 -79.368  1.00 46.70  ? 1134 HOH   C O   1 
HETATM 14863 O  O   . HOH   AA 7 .   ? 11.318  -65.747 -92.818  1.00 34.50  ? 1135 HOH   C O   1 
HETATM 14864 O  O   . HOH   AA 7 .   ? 11.379  -49.232 -83.806  1.00 24.11  ? 1136 HOH   C O   1 
HETATM 14865 O  O   . HOH   AA 7 .   ? 23.910  -40.071 -98.039  1.00 41.37  ? 1137 HOH   C O   1 
HETATM 14866 O  O   . HOH   AA 7 .   ? -0.097  -76.607 -55.170  1.00 40.48  ? 1138 HOH   C O   1 
HETATM 14867 O  O   . HOH   AA 7 .   ? 41.150  -39.770 -83.313  1.00 40.83  ? 1139 HOH   C O   1 
HETATM 14868 O  O   . HOH   AA 7 .   ? 36.021  -59.292 -56.211  1.00 56.38  ? 1140 HOH   C O   1 
HETATM 14869 O  O   . HOH   AA 7 .   ? 4.124   -85.423 -75.722  1.00 56.33  ? 1141 HOH   C O   1 
HETATM 14870 O  O   . HOH   AA 7 .   ? -4.766  -66.629 -88.810  1.00 49.72  ? 1142 HOH   C O   1 
HETATM 14871 O  O   . HOH   AA 7 .   ? 18.871  -71.412 -84.205  1.00 50.89  ? 1143 HOH   C O   1 
HETATM 14872 O  O   . HOH   AA 7 .   ? 41.377  -42.285 -93.994  1.00 43.75  ? 1144 HOH   C O   1 
HETATM 14873 O  O   . HOH   AA 7 .   ? 15.880  -45.875 -71.896  1.00 37.67  ? 1145 HOH   C O   1 
HETATM 14874 O  O   . HOH   AA 7 .   ? -3.883  -60.941 -93.642  1.00 49.64  ? 1146 HOH   C O   1 
HETATM 14875 O  O   . HOH   AA 7 .   ? 22.430  -65.136 -95.789  1.00 44.06  ? 1147 HOH   C O   1 
HETATM 14876 O  O   . HOH   AA 7 .   ? 25.535  -38.016 -80.944  1.00 32.89  ? 1148 HOH   C O   1 
HETATM 14877 O  O   . HOH   AA 7 .   ? 21.605  -70.782 -90.744  1.00 40.91  ? 1149 HOH   C O   1 
HETATM 14878 O  O   . HOH   AA 7 .   ? 4.013   -82.631 -76.083  1.00 34.88  ? 1150 HOH   C O   1 
HETATM 14879 O  O   . HOH   AA 7 .   ? -3.145  -40.460 -98.182  1.00 43.02  ? 1151 HOH   C O   1 
HETATM 14880 O  O   . HOH   AA 7 .   ? 14.807  -61.127 -99.644  1.00 47.20  ? 1152 HOH   C O   1 
HETATM 14881 O  O   . HOH   AA 7 .   ? 35.239  -42.033 -71.034  1.00 56.48  ? 1153 HOH   C O   1 
HETATM 14882 O  O   . HOH   AA 7 .   ? 25.956  -39.133 -76.034  1.00 46.62  ? 1154 HOH   C O   1 
HETATM 14883 O  O   . HOH   AA 7 .   ? 15.638  -42.115 -73.459  1.00 65.61  ? 1155 HOH   C O   1 
HETATM 14884 O  O   . HOH   AA 7 .   ? -12.398 -55.803 -80.868  1.00 46.26  ? 1156 HOH   C O   1 
HETATM 14885 O  O   . HOH   AA 7 .   ? 7.467   -59.114 -72.915  1.00 46.28  ? 1157 HOH   C O   1 
HETATM 14886 O  O   . HOH   AA 7 .   ? 29.157  -44.295 -96.587  1.00 42.67  ? 1158 HOH   C O   1 
HETATM 14887 O  O   . HOH   AA 7 .   ? 35.971  -49.994 -64.406  1.00 45.48  ? 1159 HOH   C O   1 
HETATM 14888 O  O   . HOH   AA 7 .   ? -19.697 -63.109 -76.608  1.00 44.89  ? 1160 HOH   C O   1 
HETATM 14889 O  O   . HOH   AA 7 .   ? 1.834   -75.945 -52.600  1.00 47.94  ? 1161 HOH   C O   1 
HETATM 14890 O  O   . HOH   AA 7 .   ? -6.230  -69.307 -70.306  1.00 47.30  ? 1162 HOH   C O   1 
HETATM 14891 O  O   . HOH   AA 7 .   ? 11.325  -51.406 -101.742 1.00 41.31  ? 1163 HOH   C O   1 
HETATM 14892 O  O   . HOH   AA 7 .   ? 21.280  -68.211 -77.239  1.00 50.30  ? 1164 HOH   C O   1 
HETATM 14893 O  O   . HOH   AA 7 .   ? 13.237  -58.589 -68.858  1.00 19.48  ? 1165 HOH   C O   1 
HETATM 14894 O  O   . HOH   AA 7 .   ? -0.098  -82.733 -64.306  1.00 53.73  ? 1166 HOH   C O   1 
HETATM 14895 O  O   . HOH   AA 7 .   ? 2.545   -67.701 -90.202  1.00 47.62  ? 1167 HOH   C O   1 
HETATM 14896 O  O   . HOH   AA 7 .   ? -7.795  -63.053 -69.830  1.00 43.81  ? 1168 HOH   C O   1 
HETATM 14897 O  O   . HOH   AA 7 .   ? -3.322  -63.328 -99.560  1.00 43.68  ? 1169 HOH   C O   1 
HETATM 14898 O  O   . HOH   AA 7 .   ? 43.054  -28.823 -97.917  1.00 56.65  ? 1170 HOH   C O   1 
HETATM 14899 O  O   . HOH   AA 7 .   ? -2.182  -59.864 -59.535  1.00 48.76  ? 1171 HOH   C O   1 
HETATM 14900 O  O   . HOH   AA 7 .   ? 20.141  -35.687 -78.822  1.00 41.44  ? 1172 HOH   C O   1 
HETATM 14901 O  O   . HOH   AA 7 .   ? 27.992  -61.211 -61.446  1.00 39.45  ? 1173 HOH   C O   1 
HETATM 14902 O  O   . HOH   AA 7 .   ? -14.707 -61.598 -69.405  1.00 54.56  ? 1174 HOH   C O   1 
HETATM 14903 O  O   . HOH   AA 7 .   ? 12.890  -77.842 -86.715  1.00 53.32  ? 1175 HOH   C O   1 
HETATM 14904 O  O   . HOH   AA 7 .   ? 17.984  -29.639 -79.041  1.00 55.78  ? 1176 HOH   C O   1 
HETATM 14905 O  O   . HOH   AA 7 .   ? -7.676  -63.825 -72.691  1.00 53.98  ? 1177 HOH   C O   1 
HETATM 14906 O  O   . HOH   AA 7 .   ? 2.855   -35.998 -100.297 1.00 49.74  ? 1178 HOH   C O   1 
HETATM 14907 O  O   . HOH   AA 7 .   ? 9.673   -81.729 -79.409  1.00 45.93  ? 1179 HOH   C O   1 
HETATM 14908 O  O   . HOH   AA 7 .   ? 11.472  -79.781 -66.769  1.00 45.45  ? 1180 HOH   C O   1 
HETATM 14909 O  O   . HOH   AA 7 .   ? -3.886  -65.448 -62.866  1.00 39.84  ? 1181 HOH   C O   1 
HETATM 14910 O  O   . HOH   AA 7 .   ? -5.107  -62.808 -92.467  1.00 41.42  ? 1182 HOH   C O   1 
HETATM 14911 O  O   . HOH   AA 7 .   ? 23.243  -63.228 -74.962  1.00 49.56  ? 1183 HOH   C O   1 
HETATM 14912 O  O   . HOH   AA 7 .   ? 26.365  -34.934 -67.510  1.00 46.74  ? 1184 HOH   C O   1 
HETATM 14913 O  O   . HOH   AA 7 .   ? 4.811   -56.375 -75.580  1.00 46.26  ? 1185 HOH   C O   1 
HETATM 14914 O  O   . HOH   AA 7 .   ? 29.982  -48.998 -87.432  1.00 40.10  ? 1186 HOH   C O   1 
HETATM 14915 O  O   . HOH   AA 7 .   ? 5.596   -46.180 -77.570  1.00 44.02  ? 1187 HOH   C O   1 
HETATM 14916 O  O   . HOH   AA 7 .   ? 16.810  -58.835 -100.786 1.00 60.04  ? 1188 HOH   C O   1 
HETATM 14917 O  O   . HOH   AA 7 .   ? -1.648  -66.240 -56.296  1.00 40.29  ? 1189 HOH   C O   1 
HETATM 14918 O  O   . HOH   AA 7 .   ? 27.848  -43.883 -55.863  1.00 59.88  ? 1190 HOH   C O   1 
HETATM 14919 O  O   . HOH   AA 7 .   ? -8.374  -69.489 -67.093  1.00 49.40  ? 1191 HOH   C O   1 
HETATM 14920 O  O   . HOH   AA 7 .   ? 19.805  -41.225 -98.488  1.00 56.69  ? 1192 HOH   C O   1 
HETATM 14921 O  O   . HOH   AA 7 .   ? 17.625  -63.283 -96.634  1.00 40.18  ? 1193 HOH   C O   1 
HETATM 14922 O  O   . HOH   AA 7 .   ? 25.912  -65.913 -63.788  1.00 39.92  ? 1194 HOH   C O   1 
HETATM 14923 O  O   . HOH   AA 7 .   ? 16.092  -38.436 -98.539  1.00 52.19  ? 1195 HOH   C O   1 
HETATM 14924 O  O   . HOH   AA 7 .   ? 6.101   -57.193 -72.374  1.00 46.87  ? 1196 HOH   C O   1 
HETATM 14925 O  O   . HOH   AA 7 .   ? 30.201  -49.446 -84.673  1.00 43.69  ? 1197 HOH   C O   1 
HETATM 14926 O  O   . HOH   AA 7 .   ? 24.643  -34.461 -78.649  1.00 38.88  ? 1198 HOH   C O   1 
HETATM 14927 O  O   . HOH   AA 7 .   ? 11.031  -39.438 -99.375  1.00 46.41  ? 1199 HOH   C O   1 
HETATM 14928 O  O   . HOH   AA 7 .   ? 15.076  -34.028 -97.085  1.00 44.90  ? 1200 HOH   C O   1 
HETATM 14929 O  O   . HOH   AA 7 .   ? -7.497  -58.113 -70.499  1.00 51.10  ? 1201 HOH   C O   1 
HETATM 14930 O  O   . HOH   AA 7 .   ? 16.323  -54.642 -97.517  1.00 34.73  ? 1202 HOH   C O   1 
HETATM 14931 O  O   . HOH   AA 7 .   ? 1.781   -55.141 -72.485  1.00 52.97  ? 1203 HOH   C O   1 
HETATM 14932 O  O   . HOH   AA 7 .   ? -7.285  -66.729 -56.316  1.00 65.54  ? 1204 HOH   C O   1 
HETATM 14933 O  O   . HOH   AA 7 .   ? 12.076  -68.598 -95.356  1.00 55.08  ? 1205 HOH   C O   1 
HETATM 14934 O  O   . HOH   AA 7 .   ? 28.917  -63.164 -77.374  1.00 50.82  ? 1206 HOH   C O   1 
HETATM 14935 O  O   . HOH   AA 7 .   ? 1.588   -75.194 -49.591  1.00 51.18  ? 1207 HOH   C O   1 
HETATM 14936 O  O   . HOH   AA 7 .   ? -7.802  -67.967 -71.870  1.00 52.96  ? 1208 HOH   C O   1 
HETATM 14937 O  O   . HOH   AA 7 .   ? 12.856  -44.654 -73.388  1.00 63.37  ? 1209 HOH   C O   1 
HETATM 14938 O  O   . HOH   AA 7 .   ? 25.639  -32.495 -68.302  1.00 58.84  ? 1210 HOH   C O   1 
HETATM 14939 O  O   . HOH   AA 7 .   ? 16.229  -43.751 -105.113 1.00 44.42  ? 1211 HOH   C O   1 
HETATM 14940 O  O   . HOH   AA 7 .   ? 11.291  -70.117 -91.465  1.00 36.21  ? 1212 HOH   C O   1 
HETATM 14941 O  O   . HOH   AA 7 .   ? 3.802   -52.812 -71.341  1.00 50.61  ? 1213 HOH   C O   1 
HETATM 14942 O  O   . HOH   AA 7 .   ? 17.641  -58.029 -98.025  1.00 52.25  ? 1214 HOH   C O   1 
HETATM 14943 O  O   . HOH   AA 7 .   ? -4.479  -51.021 -74.705  1.00 68.28  ? 1215 HOH   C O   1 
HETATM 14944 O  O   . HOH   AA 7 .   ? -12.798 -63.564 -69.735  1.00 52.53  ? 1216 HOH   C O   1 
HETATM 14945 O  O   . HOH   AA 7 .   ? 11.805  -37.457 -97.289  1.00 36.51  ? 1217 HOH   C O   1 
HETATM 14946 O  O   . HOH   AA 7 .   ? 12.266  -57.056 -60.493  1.00 36.24  ? 1218 HOH   C O   1 
HETATM 14947 O  O   . HOH   AA 7 .   ? 30.391  -49.358 -92.059  1.00 32.78  ? 1219 HOH   C O   1 
HETATM 14948 O  O   . HOH   AA 7 .   ? 13.364  -32.524 -79.416  1.00 64.20  ? 1220 HOH   C O   1 
HETATM 14949 O  O   . HOH   AA 7 .   ? 0.375   -65.543 -90.984  1.00 41.24  ? 1221 HOH   C O   1 
HETATM 14950 O  O   . HOH   AA 7 .   ? -10.967 -64.839 -67.789  1.00 49.64  ? 1222 HOH   C O   1 
HETATM 14951 O  O   . HOH   AA 7 .   ? 27.712  -63.243 -63.538  1.00 51.23  ? 1223 HOH   C O   1 
HETATM 14952 O  O   . HOH   AA 7 .   ? 23.095  -66.950 -81.769  1.00 49.30  ? 1224 HOH   C O   1 
HETATM 14953 O  O   . HOH   AA 7 .   ? 31.370  -48.590 -54.179  1.00 48.23  ? 1225 HOH   C O   1 
HETATM 14954 O  O   . HOH   AA 7 .   ? 13.385  -35.159 -98.870  1.00 54.09  ? 1226 HOH   C O   1 
HETATM 14955 O  O   . HOH   AA 7 .   ? 20.785  -55.635 -98.668  1.00 45.59  ? 1227 HOH   C O   1 
HETATM 14956 O  O   . HOH   BA 7 .   ? 14.166  -36.902 -51.906  1.00 23.47  ? 901  HOH   D O   1 
HETATM 14957 O  O   . HOH   BA 7 .   ? 21.271  -66.960 -22.954  1.00 31.39  ? 902  HOH   D O   1 
HETATM 14958 O  O   . HOH   BA 7 .   ? 17.203  -60.776 -39.947  1.00 23.98  ? 903  HOH   D O   1 
HETATM 14959 O  O   . HOH   BA 7 .   ? 25.994  -70.972 -56.496  1.00 52.50  ? 904  HOH   D O   1 
HETATM 14960 O  O   . HOH   BA 7 .   ? 18.396  -57.377 -48.378  1.00 32.35  ? 905  HOH   D O   1 
HETATM 14961 O  O   . HOH   BA 7 .   ? 17.223  -68.216 -20.182  1.00 38.77  ? 906  HOH   D O   1 
HETATM 14962 O  O   . HOH   BA 7 .   ? 14.098  -54.065 -17.246  1.00 42.51  ? 907  HOH   D O   1 
HETATM 14963 O  O   . HOH   BA 7 .   ? 34.788  -73.992 -38.481  1.00 52.57  ? 908  HOH   D O   1 
HETATM 14964 O  O   . HOH   BA 7 .   ? 26.449  -44.077 -37.034  1.00 50.28  ? 909  HOH   D O   1 
HETATM 14965 O  O   . HOH   BA 7 .   ? 27.706  -40.467 -29.530  1.00 33.89  ? 910  HOH   D O   1 
HETATM 14966 O  O   . HOH   BA 7 .   ? 8.642   -73.424 -34.854  1.00 39.33  ? 911  HOH   D O   1 
HETATM 14967 O  O   . HOH   BA 7 .   ? 15.264  -47.221 -56.812  1.00 35.29  ? 912  HOH   D O   1 
HETATM 14968 O  O   . HOH   BA 7 .   ? 24.433  -31.749 -54.718  1.00 42.16  ? 913  HOH   D O   1 
HETATM 14969 O  O   . HOH   BA 7 .   ? 22.523  -35.788 -28.407  1.00 52.74  ? 914  HOH   D O   1 
HETATM 14970 O  O   . HOH   BA 7 .   ? 22.143  -34.699 -33.471  1.00 57.78  ? 915  HOH   D O   1 
HETATM 14971 O  O   . HOH   BA 7 .   ? 8.178   -78.127 -59.183  1.00 49.07  ? 916  HOH   D O   1 
HETATM 14972 O  O   . HOH   BA 7 .   ? 21.837  -70.956 -54.594  1.00 28.84  ? 917  HOH   D O   1 
HETATM 14973 O  O   . HOH   BA 7 .   ? 32.680  -44.182 -23.573  1.00 46.49  ? 918  HOH   D O   1 
HETATM 14974 O  O   . HOH   BA 7 .   ? 15.459  -52.671 -19.555  1.00 38.68  ? 919  HOH   D O   1 
HETATM 14975 O  O   . HOH   BA 7 .   ? 3.200   -79.851 -57.240  1.00 39.86  ? 920  HOH   D O   1 
HETATM 14976 O  O   . HOH   BA 7 .   ? 25.352  -51.603 -36.424  1.00 30.63  ? 921  HOH   D O   1 
HETATM 14977 O  O   . HOH   BA 7 .   ? 5.676   -31.786 -27.690  1.00 36.78  ? 922  HOH   D O   1 
HETATM 14978 O  O   . HOH   BA 7 .   ? 2.433   -53.609 -37.353  1.00 32.30  ? 923  HOH   D O   1 
HETATM 14979 O  O   . HOH   BA 7 .   ? 23.354  -37.079 -52.952  1.00 45.16  ? 924  HOH   D O   1 
HETATM 14980 O  O   . HOH   BA 7 .   ? 8.488   -57.762 -34.674  1.00 24.16  ? 925  HOH   D O   1 
HETATM 14981 O  O   . HOH   BA 7 .   ? 0.250   -19.722 -29.769  1.00 35.25  ? 926  HOH   D O   1 
HETATM 14982 O  O   . HOH   BA 7 .   ? 3.691   -44.833 -46.298  1.00 27.11  ? 927  HOH   D O   1 
HETATM 14983 O  O   . HOH   BA 7 .   ? 18.646  -65.203 -54.634  1.00 25.11  ? 928  HOH   D O   1 
HETATM 14984 O  O   . HOH   BA 7 .   ? 20.659  -43.947 -45.693  1.00 33.15  ? 929  HOH   D O   1 
HETATM 14985 O  O   . HOH   BA 7 .   ? 1.467   -33.905 -27.764  1.00 52.73  ? 930  HOH   D O   1 
HETATM 14986 O  O   . HOH   BA 7 .   ? 22.953  -61.291 -35.209  1.00 21.59  ? 931  HOH   D O   1 
HETATM 14987 O  O   . HOH   BA 7 .   ? 22.200  -43.099 -50.023  1.00 42.54  ? 932  HOH   D O   1 
HETATM 14988 O  O   . HOH   BA 7 .   ? 26.085  -26.803 -30.201  1.00 48.63  ? 933  HOH   D O   1 
HETATM 14989 O  O   . HOH   BA 7 .   ? 12.557  -46.581 -18.477  1.00 36.24  ? 934  HOH   D O   1 
HETATM 14990 O  O   . HOH   BA 7 .   ? 7.501   -37.335 -42.295  1.00 32.46  ? 935  HOH   D O   1 
HETATM 14991 O  O   . HOH   BA 7 .   ? 2.849   -39.866 -30.525  1.00 30.41  ? 936  HOH   D O   1 
HETATM 14992 O  O   . HOH   BA 7 .   ? 19.501  -43.432 -17.088  1.00 32.94  ? 937  HOH   D O   1 
HETATM 14993 O  O   . HOH   BA 7 .   ? 12.253  -64.772 -31.381  1.00 25.18  ? 938  HOH   D O   1 
HETATM 14994 O  O   . HOH   BA 7 .   ? 33.747  -66.695 -39.116  1.00 40.31  ? 939  HOH   D O   1 
HETATM 14995 O  O   . HOH   BA 7 .   ? -0.950  -48.425 -40.200  1.00 40.40  ? 940  HOH   D O   1 
HETATM 14996 O  O   . HOH   BA 7 .   ? 9.013   -43.067 -22.764  1.00 42.11  ? 941  HOH   D O   1 
HETATM 14997 O  O   . HOH   BA 7 .   ? 1.763   -67.935 -40.288  1.00 33.15  ? 942  HOH   D O   1 
HETATM 14998 O  O   . HOH   BA 7 .   ? 20.529  -77.735 -47.457  1.00 49.94  ? 943  HOH   D O   1 
HETATM 14999 O  O   . HOH   BA 7 .   ? 18.791  -18.487 -27.508  1.00 43.82  ? 944  HOH   D O   1 
HETATM 15000 O  O   . HOH   BA 7 .   ? 19.815  -72.495 -34.233  1.00 34.25  ? 945  HOH   D O   1 
HETATM 15001 O  O   . HOH   BA 7 .   ? 24.777  -31.615 -31.902  1.00 60.14  ? 946  HOH   D O   1 
HETATM 15002 O  O   . HOH   BA 7 .   ? 12.582  -44.182 -43.473  1.00 23.05  ? 947  HOH   D O   1 
HETATM 15003 O  O   . HOH   BA 7 .   ? 22.687  -76.546 -49.868  1.00 52.61  ? 948  HOH   D O   1 
HETATM 15004 O  O   . HOH   BA 7 .   ? -1.549  -35.517 -54.384  1.00 31.14  ? 949  HOH   D O   1 
HETATM 15005 O  O   . HOH   BA 7 .   ? 8.173   -63.837 -39.745  1.00 21.39  ? 950  HOH   D O   1 
HETATM 15006 O  O   . HOH   BA 7 .   ? 16.631  -62.254 -43.657  1.00 31.29  ? 951  HOH   D O   1 
HETATM 15007 O  O   . HOH   BA 7 .   ? 15.568  -37.607 -27.060  1.00 26.77  ? 952  HOH   D O   1 
HETATM 15008 O  O   . HOH   BA 7 .   ? 20.969  -42.973 -20.989  1.00 35.49  ? 953  HOH   D O   1 
HETATM 15009 O  O   . HOH   BA 7 .   ? 20.175  -63.510 -41.564  1.00 27.85  ? 954  HOH   D O   1 
HETATM 15010 O  O   . HOH   BA 7 .   ? -2.241  -48.273 -58.280  1.00 28.67  ? 955  HOH   D O   1 
HETATM 15011 O  O   . HOH   BA 7 .   ? 19.632  -84.427 -47.201  1.00 62.35  ? 956  HOH   D O   1 
HETATM 15012 O  O   . HOH   BA 7 .   ? 16.277  -47.582 -46.261  1.00 39.82  ? 957  HOH   D O   1 
HETATM 15013 O  O   . HOH   BA 7 .   ? -4.358  -32.080 -40.077  1.00 51.77  ? 958  HOH   D O   1 
HETATM 15014 O  O   . HOH   BA 7 .   ? -2.662  -48.699 -43.183  1.00 38.30  ? 959  HOH   D O   1 
HETATM 15015 O  O   . HOH   BA 7 .   ? 3.404   -41.745 -64.932  1.00 43.26  ? 960  HOH   D O   1 
HETATM 15016 O  O   . HOH   BA 7 .   ? 22.019  -37.051 -32.111  1.00 32.66  ? 961  HOH   D O   1 
HETATM 15017 O  O   . HOH   BA 7 .   ? 0.459   -61.882 -57.089  1.00 25.14  ? 962  HOH   D O   1 
HETATM 15018 O  O   . HOH   BA 7 .   ? 26.524  -74.343 -44.565  1.00 45.70  ? 963  HOH   D O   1 
HETATM 15019 O  O   . HOH   BA 7 .   ? 14.928  -78.571 -44.050  1.00 41.66  ? 964  HOH   D O   1 
HETATM 15020 O  O   . HOH   BA 7 .   ? -3.878  -50.408 -59.108  1.00 36.52  ? 965  HOH   D O   1 
HETATM 15021 O  O   . HOH   BA 7 .   ? 1.275   -61.481 -36.220  1.00 29.30  ? 966  HOH   D O   1 
HETATM 15022 O  O   . HOH   BA 7 .   ? 20.835  -38.933 -69.138  1.00 27.22  ? 967  HOH   D O   1 
HETATM 15023 O  O   . HOH   BA 7 .   ? 10.904  -44.442 -59.484  1.00 31.04  ? 968  HOH   D O   1 
HETATM 15024 O  O   . HOH   BA 7 .   ? -0.732  -53.988 -60.705  1.00 31.54  ? 969  HOH   D O   1 
HETATM 15025 O  O   . HOH   BA 7 .   ? 34.283  -55.422 -24.237  1.00 41.71  ? 970  HOH   D O   1 
HETATM 15026 O  O   . HOH   BA 7 .   ? 21.469  -77.991 -43.346  1.00 62.72  ? 971  HOH   D O   1 
HETATM 15027 O  O   . HOH   BA 7 .   ? 29.657  -51.150 -24.236  1.00 33.25  ? 972  HOH   D O   1 
HETATM 15028 O  O   . HOH   BA 7 .   ? 27.801  -63.032 -48.182  1.00 40.19  ? 973  HOH   D O   1 
HETATM 15029 O  O   . HOH   BA 7 .   ? 3.268   -41.861 -47.622  1.00 27.70  ? 974  HOH   D O   1 
HETATM 15030 O  O   . HOH   BA 7 .   ? 23.282  -49.912 -34.195  1.00 25.08  ? 975  HOH   D O   1 
HETATM 15031 O  O   . HOH   BA 7 .   ? 20.895  -30.051 -53.727  1.00 54.07  ? 976  HOH   D O   1 
HETATM 15032 O  O   . HOH   BA 7 .   ? 22.101  -39.430 -25.719  1.00 33.19  ? 977  HOH   D O   1 
HETATM 15033 O  O   . HOH   BA 7 .   ? -0.676  -60.243 -55.343  1.00 31.38  ? 978  HOH   D O   1 
HETATM 15034 O  O   . HOH   BA 7 .   ? -2.835  -58.716 -49.288  1.00 44.08  ? 979  HOH   D O   1 
HETATM 15035 O  O   . HOH   BA 7 .   ? -2.235  -47.496 -45.508  1.00 26.55  ? 980  HOH   D O   1 
HETATM 15036 O  O   . HOH   BA 7 .   ? 3.762   -33.775 -26.890  1.00 36.73  ? 981  HOH   D O   1 
HETATM 15037 O  O   . HOH   BA 7 .   ? 21.205  -57.231 -51.533  1.00 39.25  ? 982  HOH   D O   1 
HETATM 15038 O  O   . HOH   BA 7 .   ? 21.952  -63.183 -33.381  1.00 30.00  ? 983  HOH   D O   1 
HETATM 15039 O  O   . HOH   BA 7 .   ? 10.905  -41.058 -47.786  1.00 27.76  ? 984  HOH   D O   1 
HETATM 15040 O  O   . HOH   BA 7 .   ? 13.481  -57.403 -53.959  1.00 20.23  ? 985  HOH   D O   1 
HETATM 15041 O  O   . HOH   BA 7 .   ? 12.738  -52.955 -25.568  1.00 19.36  ? 986  HOH   D O   1 
HETATM 15042 O  O   . HOH   BA 7 .   ? 18.203  -40.164 -26.648  1.00 28.88  ? 987  HOH   D O   1 
HETATM 15043 O  O   . HOH   BA 7 .   ? 28.871  -45.697 -34.134  1.00 35.77  ? 988  HOH   D O   1 
HETATM 15044 O  O   . HOH   BA 7 .   ? 27.580  -69.167 -50.319  1.00 39.03  ? 989  HOH   D O   1 
HETATM 15045 O  O   . HOH   BA 7 .   ? 15.144  -44.631 -56.247  1.00 37.40  ? 990  HOH   D O   1 
HETATM 15046 O  O   . HOH   BA 7 .   ? 27.451  -53.501 -19.329  1.00 35.03  ? 991  HOH   D O   1 
HETATM 15047 O  O   . HOH   BA 7 .   ? 30.024  -57.773 -20.272  1.00 44.56  ? 992  HOH   D O   1 
HETATM 15048 O  O   . HOH   BA 7 .   ? 25.813  -41.117 -24.784  1.00 51.91  ? 993  HOH   D O   1 
HETATM 15049 O  O   . HOH   BA 7 .   ? 4.921   -43.581 -67.902  1.00 27.39  ? 994  HOH   D O   1 
HETATM 15050 O  O   . HOH   BA 7 .   ? 12.194  -60.592 -50.473  1.00 19.41  ? 995  HOH   D O   1 
HETATM 15051 O  O   . HOH   BA 7 .   ? 17.539  -48.649 -54.550  1.00 32.82  ? 996  HOH   D O   1 
HETATM 15052 O  O   . HOH   BA 7 .   ? 9.272   -26.102 -40.351  1.00 49.73  ? 997  HOH   D O   1 
HETATM 15053 O  O   . HOH   BA 7 .   ? 14.330  -59.638 -49.588  1.00 27.53  ? 998  HOH   D O   1 
HETATM 15054 O  O   . HOH   BA 7 .   ? 28.658  -51.220 -21.520  1.00 29.83  ? 999  HOH   D O   1 
HETATM 15055 O  O   . HOH   BA 7 .   ? 12.370  -53.106 -21.114  1.00 48.89  ? 1000 HOH   D O   1 
HETATM 15056 O  O   . HOH   BA 7 .   ? 21.758  -65.545 -40.719  1.00 30.58  ? 1001 HOH   D O   1 
HETATM 15057 O  O   . HOH   BA 7 .   ? 25.950  -70.991 -38.017  1.00 34.35  ? 1002 HOH   D O   1 
HETATM 15058 O  O   . HOH   BA 7 .   ? -0.836  -57.183 -28.548  1.00 40.95  ? 1003 HOH   D O   1 
HETATM 15059 O  O   . HOH   BA 7 .   ? 5.210   -43.634 -55.395  1.00 24.40  ? 1004 HOH   D O   1 
HETATM 15060 O  O   . HOH   BA 7 .   ? 21.308  -61.823 -49.132  1.00 29.52  ? 1005 HOH   D O   1 
HETATM 15061 O  O   . HOH   BA 7 .   ? 12.512  -35.376 -38.765  1.00 31.16  ? 1006 HOH   D O   1 
HETATM 15062 O  O   . HOH   BA 7 .   ? 12.602  -32.235 -23.792  1.00 35.10  ? 1007 HOH   D O   1 
HETATM 15063 O  O   . HOH   BA 7 .   ? -4.938  -39.023 -59.123  1.00 57.71  ? 1008 HOH   D O   1 
HETATM 15064 O  O   . HOH   BA 7 .   ? 2.015   -52.901 -47.015  1.00 26.47  ? 1009 HOH   D O   1 
HETATM 15065 O  O   . HOH   BA 7 .   ? 13.137  -65.511 -34.064  1.00 22.48  ? 1010 HOH   D O   1 
HETATM 15066 O  O   . HOH   BA 7 .   ? 0.864   -66.309 -44.589  1.00 50.88  ? 1011 HOH   D O   1 
HETATM 15067 O  O   . HOH   BA 7 .   ? -0.343  -58.551 -60.889  1.00 46.22  ? 1012 HOH   D O   1 
HETATM 15068 O  O   . HOH   BA 7 .   ? 20.375  -44.850 -30.363  1.00 25.32  ? 1013 HOH   D O   1 
HETATM 15069 O  O   . HOH   BA 7 .   ? -3.855  -55.505 -46.892  1.00 50.89  ? 1014 HOH   D O   1 
HETATM 15070 O  O   . HOH   BA 7 .   ? 2.993   -53.831 -32.876  1.00 26.44  ? 1015 HOH   D O   1 
HETATM 15071 O  O   . HOH   BA 7 .   ? 19.017  -45.993 -55.019  1.00 34.61  ? 1016 HOH   D O   1 
HETATM 15072 O  O   . HOH   BA 7 .   ? -1.111  -46.074 -59.785  1.00 33.44  ? 1017 HOH   D O   1 
HETATM 15073 O  O   . HOH   BA 7 .   ? 24.333  -42.061 -41.170  1.00 45.98  ? 1018 HOH   D O   1 
HETATM 15074 O  O   . HOH   BA 7 .   ? 24.685  -58.668 -43.984  1.00 42.14  ? 1019 HOH   D O   1 
HETATM 15075 O  O   . HOH   BA 7 .   ? 10.857  -46.295 -57.386  1.00 22.63  ? 1020 HOH   D O   1 
HETATM 15076 O  O   . HOH   BA 7 .   ? 19.511  -32.278 -24.049  1.00 33.33  ? 1021 HOH   D O   1 
HETATM 15077 O  O   . HOH   BA 7 .   ? 21.065  -67.608 -28.689  1.00 37.31  ? 1022 HOH   D O   1 
HETATM 15078 O  O   . HOH   BA 7 .   ? 24.059  -43.240 -29.511  1.00 27.79  ? 1023 HOH   D O   1 
HETATM 15079 O  O   . HOH   BA 7 .   ? 20.411  -49.604 -34.765  1.00 24.69  ? 1024 HOH   D O   1 
HETATM 15080 O  O   . HOH   BA 7 .   ? -4.240  -53.653 -68.384  1.00 42.64  ? 1025 HOH   D O   1 
HETATM 15081 O  O   . HOH   BA 7 .   ? 22.589  -65.316 -28.938  1.00 30.38  ? 1026 HOH   D O   1 
HETATM 15082 O  O   . HOH   BA 7 .   ? 2.197   -36.780 -40.425  1.00 40.75  ? 1027 HOH   D O   1 
HETATM 15083 O  O   . HOH   BA 7 .   ? 26.063  -59.337 -39.378  1.00 54.67  ? 1028 HOH   D O   1 
HETATM 15084 O  O   . HOH   BA 7 .   ? 32.864  -52.486 -22.515  1.00 40.94  ? 1029 HOH   D O   1 
HETATM 15085 O  O   . HOH   BA 7 .   ? -0.873  -50.023 -32.138  1.00 44.92  ? 1030 HOH   D O   1 
HETATM 15086 O  O   . HOH   BA 7 .   ? 9.784   -82.049 -45.814  1.00 31.58  ? 1031 HOH   D O   1 
HETATM 15087 O  O   . HOH   BA 7 .   ? 15.723  -59.958 -45.463  1.00 31.37  ? 1032 HOH   D O   1 
HETATM 15088 O  O   . HOH   BA 7 .   ? 15.643  -45.710 -51.787  1.00 36.47  ? 1033 HOH   D O   1 
HETATM 15089 O  O   . HOH   BA 7 .   ? 19.255  -50.810 -54.081  1.00 31.01  ? 1034 HOH   D O   1 
HETATM 15090 O  O   . HOH   BA 7 .   ? 9.569   -56.220 -51.164  1.00 23.09  ? 1035 HOH   D O   1 
HETATM 15091 O  O   . HOH   BA 7 .   ? 2.762   -31.386 -50.574  1.00 40.32  ? 1036 HOH   D O   1 
HETATM 15092 O  O   . HOH   BA 7 .   ? 13.597  -66.191 -20.840  1.00 45.75  ? 1037 HOH   D O   1 
HETATM 15093 O  O   . HOH   BA 7 .   ? 24.542  -70.324 -31.136  1.00 39.90  ? 1038 HOH   D O   1 
HETATM 15094 O  O   . HOH   BA 7 .   ? 23.472  -73.936 -55.086  1.00 28.10  ? 1039 HOH   D O   1 
HETATM 15095 O  O   . HOH   BA 7 .   ? 16.856  -60.849 -36.777  1.00 25.96  ? 1040 HOH   D O   1 
HETATM 15096 O  O   . HOH   BA 7 .   ? -1.765  -31.935 -51.899  1.00 42.16  ? 1041 HOH   D O   1 
HETATM 15097 O  O   . HOH   BA 7 .   ? 10.163  -54.403 -49.115  1.00 27.17  ? 1042 HOH   D O   1 
HETATM 15098 O  O   . HOH   BA 7 .   ? 25.393  -40.926 -27.384  1.00 33.52  ? 1043 HOH   D O   1 
HETATM 15099 O  O   . HOH   BA 7 .   ? 13.134  -56.057 -57.316  1.00 24.13  ? 1044 HOH   D O   1 
HETATM 15100 O  O   . HOH   BA 7 .   ? 22.205  -57.781 -53.700  1.00 47.25  ? 1045 HOH   D O   1 
HETATM 15101 O  O   . HOH   BA 7 .   ? 35.371  -54.223 -42.672  1.00 52.41  ? 1046 HOH   D O   1 
HETATM 15102 O  O   . HOH   BA 7 .   ? 23.253  -76.228 -52.455  1.00 39.15  ? 1047 HOH   D O   1 
HETATM 15103 O  O   . HOH   BA 7 .   ? -0.868  -56.443 -43.289  1.00 43.00  ? 1048 HOH   D O   1 
HETATM 15104 O  O   . HOH   BA 7 .   ? 23.011  -64.891 -56.256  1.00 46.99  ? 1049 HOH   D O   1 
HETATM 15105 O  O   . HOH   BA 7 .   ? -3.934  -54.464 -54.047  1.00 41.28  ? 1050 HOH   D O   1 
HETATM 15106 O  O   . HOH   BA 7 .   ? 23.170  -49.214 -41.658  1.00 31.77  ? 1051 HOH   D O   1 
HETATM 15107 O  O   . HOH   BA 7 .   ? 11.305  -47.291 -20.689  1.00 53.52  ? 1052 HOH   D O   1 
HETATM 15108 O  O   . HOH   BA 7 .   ? 25.989  -46.422 -15.962  1.00 43.57  ? 1053 HOH   D O   1 
HETATM 15109 O  O   . HOH   BA 7 .   ? 15.211  -58.994 -52.227  1.00 25.70  ? 1054 HOH   D O   1 
HETATM 15110 O  O   . HOH   BA 7 .   ? 12.859  -71.261 -29.157  1.00 48.44  ? 1055 HOH   D O   1 
HETATM 15111 O  O   . HOH   BA 7 .   ? 10.312  -66.607 -60.065  1.00 26.00  ? 1056 HOH   D O   1 
HETATM 15112 O  O   . HOH   BA 7 .   ? 0.553   -65.640 -29.301  1.00 48.15  ? 1057 HOH   D O   1 
HETATM 15113 O  O   . HOH   BA 7 .   ? 2.270   -55.395 -34.945  1.00 26.42  ? 1058 HOH   D O   1 
HETATM 15114 O  O   . HOH   BA 7 .   ? 30.971  -68.010 -25.607  1.00 42.25  ? 1059 HOH   D O   1 
HETATM 15115 O  O   . HOH   BA 7 .   ? 11.049  -38.743 -21.782  1.00 48.71  ? 1060 HOH   D O   1 
HETATM 15116 O  O   . HOH   BA 7 .   ? 21.226  -67.479 -56.920  1.00 36.58  ? 1061 HOH   D O   1 
HETATM 15117 O  O   . HOH   BA 7 .   ? -3.926  -39.168 -56.498  1.00 42.04  ? 1062 HOH   D O   1 
HETATM 15118 O  O   . HOH   BA 7 .   ? 29.827  -60.041 -41.282  1.00 32.63  ? 1063 HOH   D O   1 
HETATM 15119 O  O   . HOH   BA 7 .   ? 22.351  -39.952 -47.108  1.00 52.17  ? 1064 HOH   D O   1 
HETATM 15120 O  O   . HOH   BA 7 .   ? 26.236  -53.775 -38.084  1.00 45.11  ? 1065 HOH   D O   1 
HETATM 15121 O  O   . HOH   BA 7 .   ? 9.800   -34.938 -44.746  1.00 32.81  ? 1066 HOH   D O   1 
HETATM 15122 O  O   . HOH   BA 7 .   ? 22.946  -60.335 -45.454  1.00 34.47  ? 1067 HOH   D O   1 
HETATM 15123 O  O   . HOH   BA 7 .   ? 27.257  -37.890 -44.624  1.00 54.53  ? 1068 HOH   D O   1 
HETATM 15124 O  O   . HOH   BA 7 .   ? 35.808  -68.112 -39.877  1.00 49.92  ? 1069 HOH   D O   1 
HETATM 15125 O  O   . HOH   BA 7 .   ? 12.277  -72.314 -31.656  1.00 33.59  ? 1070 HOH   D O   1 
HETATM 15126 O  O   . HOH   BA 7 .   ? 22.277  -34.020 -31.271  1.00 46.84  ? 1071 HOH   D O   1 
HETATM 15127 O  O   . HOH   BA 7 .   ? -5.830  -43.204 -53.986  1.00 45.46  ? 1072 HOH   D O   1 
HETATM 15128 O  O   . HOH   BA 7 .   ? -2.716  -62.874 -35.804  1.00 46.64  ? 1073 HOH   D O   1 
HETATM 15129 O  O   . HOH   BA 7 .   ? 6.888   -65.624 -50.142  1.00 27.79  ? 1074 HOH   D O   1 
HETATM 15130 O  O   . HOH   BA 7 .   ? 18.497  -42.700 -56.303  1.00 38.40  ? 1075 HOH   D O   1 
HETATM 15131 O  O   . HOH   BA 7 .   ? 10.613  -68.973 -28.912  1.00 42.83  ? 1076 HOH   D O   1 
HETATM 15132 O  O   . HOH   BA 7 .   ? 22.308  -69.588 -63.229  1.00 44.17  ? 1077 HOH   D O   1 
HETATM 15133 O  O   . HOH   BA 7 .   ? 8.409   -87.103 -50.936  1.00 46.48  ? 1078 HOH   D O   1 
HETATM 15134 O  O   . HOH   BA 7 .   ? -0.203  -37.166 -35.350  1.00 43.70  ? 1079 HOH   D O   1 
HETATM 15135 O  O   . HOH   BA 7 .   ? 26.393  -72.550 -46.150  1.00 40.24  ? 1080 HOH   D O   1 
HETATM 15136 O  O   . HOH   BA 7 .   ? 0.876   -37.603 -30.724  1.00 55.43  ? 1081 HOH   D O   1 
HETATM 15137 O  O   . HOH   BA 7 .   ? -7.857  -30.088 -39.344  1.00 50.90  ? 1082 HOH   D O   1 
HETATM 15138 O  O   . HOH   BA 7 .   ? 37.440  -71.093 -32.172  1.00 52.23  ? 1083 HOH   D O   1 
HETATM 15139 O  O   . HOH   BA 7 .   ? 32.435  -59.430 -24.486  1.00 38.27  ? 1084 HOH   D O   1 
HETATM 15140 O  O   . HOH   BA 7 .   ? -2.629  -26.826 -36.950  1.00 38.67  ? 1085 HOH   D O   1 
HETATM 15141 O  O   . HOH   BA 7 .   ? 8.730   -47.718 -23.638  1.00 32.19  ? 1086 HOH   D O   1 
HETATM 15142 O  O   . HOH   BA 7 .   ? 10.644  -86.033 -54.885  1.00 51.89  ? 1087 HOH   D O   1 
HETATM 15143 O  O   . HOH   BA 7 .   ? 23.864  -18.533 -38.557  1.00 52.27  ? 1088 HOH   D O   1 
HETATM 15144 O  O   . HOH   BA 7 .   ? 23.853  -75.242 -35.748  1.00 44.57  ? 1089 HOH   D O   1 
HETATM 15145 O  O   . HOH   BA 7 .   ? 19.135  -61.837 -43.371  1.00 29.46  ? 1090 HOH   D O   1 
HETATM 15146 O  O   . HOH   BA 7 .   ? 35.147  -49.646 -22.905  1.00 51.87  ? 1091 HOH   D O   1 
HETATM 15147 O  O   . HOH   BA 7 .   ? 30.392  -45.331 -19.644  1.00 48.58  ? 1092 HOH   D O   1 
HETATM 15148 O  O   . HOH   BA 7 .   ? 0.483   -64.739 -46.694  1.00 36.23  ? 1093 HOH   D O   1 
HETATM 15149 O  O   . HOH   BA 7 .   ? 24.396  -67.073 -28.992  1.00 42.73  ? 1094 HOH   D O   1 
HETATM 15150 O  O   . HOH   BA 7 .   ? 16.693  -19.956 -32.475  1.00 51.55  ? 1095 HOH   D O   1 
HETATM 15151 O  O   . HOH   BA 7 .   ? 31.565  -61.252 -43.824  1.00 35.74  ? 1096 HOH   D O   1 
HETATM 15152 O  O   . HOH   BA 7 .   ? 8.407   -77.371 -35.830  1.00 42.61  ? 1097 HOH   D O   1 
HETATM 15153 O  O   . HOH   BA 7 .   ? 22.628  -54.774 -43.333  1.00 38.85  ? 1098 HOH   D O   1 
HETATM 15154 O  O   . HOH   BA 7 .   ? 14.916  -87.480 -53.596  1.00 53.38  ? 1099 HOH   D O   1 
HETATM 15155 O  O   . HOH   BA 7 .   ? 18.236  -50.597 -36.830  1.00 26.03  ? 1100 HOH   D O   1 
HETATM 15156 O  O   . HOH   BA 7 .   ? 0.551   -42.761 -32.497  1.00 43.59  ? 1101 HOH   D O   1 
HETATM 15157 O  O   . HOH   BA 7 .   ? 24.585  -77.670 -38.029  1.00 38.48  ? 1102 HOH   D O   1 
HETATM 15158 O  O   . HOH   BA 7 .   ? 21.466  -36.734 -25.581  1.00 32.37  ? 1103 HOH   D O   1 
HETATM 15159 O  O   . HOH   BA 7 .   ? 14.419  -45.794 -44.841  1.00 34.76  ? 1104 HOH   D O   1 
HETATM 15160 O  O   . HOH   BA 7 .   ? 22.987  -75.105 -65.296  1.00 44.27  ? 1105 HOH   D O   1 
HETATM 15161 O  O   . HOH   BA 7 .   ? 31.032  -47.234 -32.748  1.00 56.61  ? 1106 HOH   D O   1 
HETATM 15162 O  O   . HOH   BA 7 .   ? 7.675   -37.163 -22.534  1.00 34.60  ? 1107 HOH   D O   1 
HETATM 15163 O  O   . HOH   BA 7 .   ? 8.406   -58.054 -23.349  1.00 30.71  ? 1108 HOH   D O   1 
HETATM 15164 O  O   . HOH   BA 7 .   ? 37.103  -77.904 -44.668  1.00 49.79  ? 1109 HOH   D O   1 
HETATM 15165 O  O   . HOH   BA 7 .   ? 8.510   -75.628 -58.793  1.00 40.51  ? 1110 HOH   D O   1 
HETATM 15166 O  O   . HOH   BA 7 .   ? 24.866  -59.782 -36.996  1.00 34.81  ? 1111 HOH   D O   1 
HETATM 15167 O  O   . HOH   BA 7 .   ? 20.368  -55.357 -41.408  1.00 28.02  ? 1112 HOH   D O   1 
HETATM 15168 O  O   . HOH   BA 7 .   ? 8.240   -67.880 -49.565  1.00 25.60  ? 1113 HOH   D O   1 
HETATM 15169 O  O   . HOH   BA 7 .   ? 18.212  -72.719 -64.119  1.00 27.04  ? 1114 HOH   D O   1 
HETATM 15170 O  O   . HOH   BA 7 .   ? 24.002  -61.169 -51.971  1.00 64.76  ? 1115 HOH   D O   1 
HETATM 15171 O  O   . HOH   BA 7 .   ? 24.085  -69.810 -21.368  1.00 41.37  ? 1116 HOH   D O   1 
HETATM 15172 O  O   . HOH   BA 7 .   ? 8.514   -28.848 -41.309  1.00 44.23  ? 1117 HOH   D O   1 
HETATM 15173 O  O   . HOH   BA 7 .   ? 13.810  -47.281 -47.159  1.00 28.40  ? 1118 HOH   D O   1 
HETATM 15174 O  O   . HOH   BA 7 .   ? 5.146   -71.226 -32.537  1.00 51.72  ? 1119 HOH   D O   1 
HETATM 15175 O  O   . HOH   BA 7 .   ? 5.025   -27.866 -24.742  1.00 47.25  ? 1120 HOH   D O   1 
HETATM 15176 O  O   . HOH   BA 7 .   ? 21.852  -71.586 -31.868  1.00 37.87  ? 1121 HOH   D O   1 
HETATM 15177 O  O   . HOH   BA 7 .   ? 23.786  -41.863 -45.126  1.00 61.95  ? 1122 HOH   D O   1 
HETATM 15178 O  O   . HOH   BA 7 .   ? 24.211  -63.706 -54.094  1.00 63.33  ? 1123 HOH   D O   1 
HETATM 15179 O  O   . HOH   BA 7 .   ? 0.527   -57.901 -34.893  1.00 42.41  ? 1124 HOH   D O   1 
HETATM 15180 O  O   . HOH   BA 7 .   ? 11.867  -36.234 -22.656  1.00 48.52  ? 1125 HOH   D O   1 
HETATM 15181 O  O   . HOH   BA 7 .   ? 25.407  -61.160 -49.456  1.00 49.74  ? 1126 HOH   D O   1 
HETATM 15182 O  O   . HOH   BA 7 .   ? 2.378   -57.799 -44.017  1.00 34.00  ? 1127 HOH   D O   1 
HETATM 15183 O  O   . HOH   BA 7 .   ? 16.320  -61.052 -47.676  1.00 36.59  ? 1128 HOH   D O   1 
HETATM 15184 O  O   . HOH   BA 7 .   ? 21.347  -39.249 -44.244  1.00 51.44  ? 1129 HOH   D O   1 
HETATM 15185 O  O   . HOH   BA 7 .   ? 9.715   -59.227 -21.052  1.00 41.66  ? 1130 HOH   D O   1 
HETATM 15186 O  O   . HOH   BA 7 .   ? 1.328   -75.296 -34.443  1.00 65.11  ? 1131 HOH   D O   1 
HETATM 15187 O  O   . HOH   BA 7 .   ? 21.565  -36.158 -40.211  1.00 47.84  ? 1132 HOH   D O   1 
HETATM 15188 O  O   . HOH   BA 7 .   ? 5.151   -37.357 -24.047  1.00 46.21  ? 1133 HOH   D O   1 
HETATM 15189 O  O   . HOH   BA 7 .   ? 15.463  -45.299 -48.993  1.00 37.89  ? 1134 HOH   D O   1 
HETATM 15190 O  O   . HOH   BA 7 .   ? 13.715  -43.660 -48.010  1.00 48.50  ? 1135 HOH   D O   1 
HETATM 15191 O  O   . HOH   BA 7 .   ? 3.554   -79.860 -40.620  1.00 57.29  ? 1136 HOH   D O   1 
HETATM 15192 O  O   . HOH   BA 7 .   ? 27.381  -46.104 -53.941  1.00 49.68  ? 1137 HOH   D O   1 
HETATM 15193 O  O   . HOH   BA 7 .   ? 17.671  -51.941 -18.800  1.00 47.62  ? 1138 HOH   D O   1 
HETATM 15194 O  O   . HOH   BA 7 .   ? 32.013  -35.171 -45.572  1.00 50.69  ? 1139 HOH   D O   1 
HETATM 15195 O  O   . HOH   BA 7 .   ? 31.509  -29.063 -32.354  1.00 67.67  ? 1140 HOH   D O   1 
HETATM 15196 O  O   . HOH   BA 7 .   ? 5.271   -61.380 -24.894  1.00 63.65  ? 1141 HOH   D O   1 
HETATM 15197 O  O   . HOH   BA 7 .   ? 0.491   -65.468 -40.822  1.00 41.93  ? 1142 HOH   D O   1 
HETATM 15198 O  O   . HOH   BA 7 .   ? 13.040  -47.394 -58.410  1.00 41.56  ? 1143 HOH   D O   1 
HETATM 15199 O  O   . HOH   BA 7 .   ? -3.014  -46.654 -41.028  1.00 45.76  ? 1144 HOH   D O   1 
HETATM 15200 O  O   . HOH   BA 7 .   ? 19.012  -39.594 -23.503  1.00 46.05  ? 1145 HOH   D O   1 
HETATM 15201 O  O   . HOH   BA 7 .   ? -2.829  -37.255 -35.358  1.00 55.00  ? 1146 HOH   D O   1 
HETATM 15202 O  O   . HOH   BA 7 .   ? 13.845  -29.350 -20.774  1.00 57.91  ? 1147 HOH   D O   1 
HETATM 15203 O  O   . HOH   BA 7 .   ? 20.155  -60.169 -45.091  1.00 46.19  ? 1148 HOH   D O   1 
HETATM 15204 O  O   . HOH   BA 7 .   ? -2.746  -53.225 -58.599  1.00 39.16  ? 1149 HOH   D O   1 
HETATM 15205 O  O   . HOH   BA 7 .   ? 11.441  -58.129 -51.631  1.00 26.55  ? 1150 HOH   D O   1 
HETATM 15206 O  O   . HOH   BA 7 .   ? -0.179  -24.531 -21.931  1.00 54.21  ? 1151 HOH   D O   1 
HETATM 15207 O  O   . HOH   BA 7 .   ? 2.140   -40.918 -33.169  1.00 38.72  ? 1152 HOH   D O   1 
HETATM 15208 O  O   . HOH   BA 7 .   ? 8.611   -81.325 -63.152  1.00 40.77  ? 1153 HOH   D O   1 
HETATM 15209 O  O   . HOH   BA 7 .   ? 30.154  -69.490 -49.595  1.00 49.58  ? 1154 HOH   D O   1 
HETATM 15210 O  O   . HOH   BA 7 .   ? -0.515  -74.532 -44.271  1.00 58.75  ? 1155 HOH   D O   1 
HETATM 15211 O  O   . HOH   BA 7 .   ? 17.984  -45.678 -46.647  1.00 67.67  ? 1156 HOH   D O   1 
HETATM 15212 O  O   . HOH   BA 7 .   ? 24.488  -50.533 -43.510  1.00 55.99  ? 1157 HOH   D O   1 
HETATM 15213 O  O   . HOH   BA 7 .   ? 6.305   -59.280 -23.707  1.00 44.49  ? 1158 HOH   D O   1 
HETATM 15214 O  O   . HOH   BA 7 .   ? 19.410  -45.314 -49.340  1.00 67.10  ? 1159 HOH   D O   1 
HETATM 15215 O  O   . HOH   BA 7 .   ? 3.058   -41.118 -25.564  1.00 50.34  ? 1160 HOH   D O   1 
HETATM 15216 O  O   . HOH   BA 7 .   ? 8.215   -83.305 -43.837  1.00 41.63  ? 1161 HOH   D O   1 
HETATM 15217 O  O   . HOH   BA 7 .   ? 5.350   -63.752 -25.142  1.00 52.03  ? 1162 HOH   D O   1 
HETATM 15218 O  O   . HOH   BA 7 .   ? 18.578  -59.953 -48.291  1.00 40.09  ? 1163 HOH   D O   1 
HETATM 15219 O  O   . HOH   BA 7 .   ? 1.828   -41.379 -35.829  1.00 32.20  ? 1164 HOH   D O   1 
HETATM 15220 O  O   . HOH   BA 7 .   ? 20.925  -71.853 -64.074  1.00 35.76  ? 1165 HOH   D O   1 
HETATM 15221 O  O   . HOH   BA 7 .   ? 27.914  -38.787 -53.559  1.00 56.74  ? 1166 HOH   D O   1 
HETATM 15222 O  O   . HOH   BA 7 .   ? 24.624  -66.181 -61.305  1.00 42.25  ? 1167 HOH   D O   1 
HETATM 15223 O  O   . HOH   BA 7 .   ? 20.723  -41.667 -18.724  1.00 47.65  ? 1168 HOH   D O   1 
HETATM 15224 O  O   . HOH   BA 7 .   ? -5.632  -40.563 -54.945  1.00 49.00  ? 1169 HOH   D O   1 
HETATM 15225 O  O   . HOH   BA 7 .   ? 27.501  -57.771 -41.033  1.00 50.32  ? 1170 HOH   D O   1 
HETATM 15226 O  O   . HOH   BA 7 .   ? -3.349  -62.450 -55.048  1.00 51.33  ? 1171 HOH   D O   1 
HETATM 15227 O  O   . HOH   BA 7 .   ? 7.026   -72.731 -32.795  1.00 50.17  ? 1172 HOH   D O   1 
HETATM 15228 O  O   . HOH   BA 7 .   ? 8.531   -68.149 -28.667  1.00 48.41  ? 1173 HOH   D O   1 
HETATM 15229 O  O   . HOH   BA 7 .   ? 17.280  -43.247 -15.728  1.00 41.45  ? 1174 HOH   D O   1 
HETATM 15230 O  O   . HOH   BA 7 .   ? 23.468  -60.104 -48.307  1.00 51.61  ? 1175 HOH   D O   1 
HETATM 15231 O  O   . HOH   BA 7 .   ? -7.295  -44.843 -56.080  1.00 47.89  ? 1176 HOH   D O   1 
HETATM 15232 O  O   . HOH   BA 7 .   ? 24.631  -56.363 -43.693  1.00 55.09  ? 1177 HOH   D O   1 
HETATM 15233 O  O   . HOH   BA 7 .   ? 7.958   -82.457 -40.982  1.00 48.15  ? 1178 HOH   D O   1 
HETATM 15234 O  O   . HOH   BA 7 .   ? 22.584  -57.000 -49.080  1.00 42.29  ? 1179 HOH   D O   1 
HETATM 15235 O  O   . HOH   BA 7 .   ? 20.305  -16.778 -26.163  1.00 43.70  ? 1180 HOH   D O   1 
HETATM 15236 O  O   . HOH   BA 7 .   ? -0.396  -43.128 -36.072  1.00 51.34  ? 1181 HOH   D O   1 
HETATM 15237 O  O   . HOH   BA 7 .   ? 9.123   -54.142 -22.275  1.00 38.49  ? 1182 HOH   D O   1 
HETATM 15238 O  O   . HOH   BA 7 .   ? -4.485  -52.414 -42.091  1.00 52.31  ? 1183 HOH   D O   1 
HETATM 15239 O  O   . HOH   BA 7 .   ? 11.225  -52.506 -23.399  1.00 34.22  ? 1184 HOH   D O   1 
HETATM 15240 O  O   . HOH   BA 7 .   ? 1.719   -41.081 -28.376  1.00 39.36  ? 1185 HOH   D O   1 
HETATM 15241 O  O   . HOH   BA 7 .   ? -3.261  -55.601 -56.328  1.00 53.77  ? 1186 HOH   D O   1 
HETATM 15242 O  O   . HOH   BA 7 .   ? 23.663  -39.908 -23.671  1.00 35.66  ? 1187 HOH   D O   1 
HETATM 15243 O  O   . HOH   BA 7 .   ? -1.967  -63.797 -38.358  1.00 56.32  ? 1188 HOH   D O   1 
HETATM 15244 O  O   . HOH   BA 7 .   ? 7.214   -55.597 -23.035  1.00 44.40  ? 1189 HOH   D O   1 
HETATM 15245 O  O   . HOH   BA 7 .   ? -0.028  -39.899 -36.699  1.00 47.00  ? 1190 HOH   D O   1 
HETATM 15246 O  O   . HOH   BA 7 .   ? 19.496  -69.851 -29.921  1.00 41.60  ? 1191 HOH   D O   1 
HETATM 15247 O  O   . HOH   BA 7 .   ? 0.795   -41.589 -66.788  1.00 59.34  ? 1192 HOH   D O   1 
HETATM 15248 O  O   . HOH   BA 7 .   ? 21.634  -42.629 -15.432  1.00 41.72  ? 1193 HOH   D O   1 
HETATM 15249 O  O   . HOH   BA 7 .   ? -4.463  -62.690 -39.999  1.00 59.53  ? 1194 HOH   D 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   . PHE A 4   ? 0.9195 0.6301 0.6492 -0.1358 0.0340  0.0159  305 PHE A N   
2     C CA  . PHE A 4   ? 0.8897 0.6449 0.6501 -0.1367 0.0348  0.0136  305 PHE A CA  
3     C C   . PHE A 4   ? 0.8637 0.6296 0.6321 -0.1205 0.0320  0.0162  305 PHE A C   
4     O O   . PHE A 4   ? 0.9395 0.6830 0.6885 -0.1157 0.0327  0.0205  305 PHE A O   
5     C CB  . PHE A 4   ? 1.0587 0.8278 0.8200 -0.1575 0.0427  0.0133  305 PHE A CB  
6     C CG  . PHE A 4   ? 1.2307 0.9927 0.9791 -0.1595 0.0480  0.0180  305 PHE A CG  
7     C CD1 . PHE A 4   ? 1.2060 1.0007 0.9734 -0.1562 0.0501  0.0180  305 PHE A CD1 
8     C CD2 . PHE A 4   ? 1.3303 1.0511 1.0454 -0.1643 0.0510  0.0225  305 PHE A CD2 
9     C CE1 . PHE A 4   ? 1.1837 0.9716 0.9380 -0.1578 0.0552  0.0221  305 PHE A CE1 
10    C CE2 . PHE A 4   ? 1.3024 1.0158 1.0041 -0.1661 0.0560  0.0270  305 PHE A CE2 
11    C CZ  . PHE A 4   ? 1.2553 1.0031 0.9771 -0.1630 0.0581  0.0267  305 PHE A CZ  
12    N N   . LEU A 5   ? 0.6852 0.4843 0.4809 -0.1123 0.0287  0.0134  306 LEU A N   
13    C CA  . LEU A 5   ? 0.6541 0.4662 0.4588 -0.0994 0.0263  0.0149  306 LEU A CA  
14    C C   . LEU A 5   ? 0.5627 0.4119 0.3910 -0.1029 0.0289  0.0122  306 LEU A C   
15    O O   . LEU A 5   ? 0.6269 0.4965 0.4719 -0.1072 0.0286  0.0084  306 LEU A O   
16    C CB  . LEU A 5   ? 0.6098 0.4206 0.4211 -0.0821 0.0182  0.0146  306 LEU A CB  
17    C CG  . LEU A 5   ? 0.6432 0.4212 0.4333 -0.0738 0.0146  0.0172  306 LEU A CG  
18    C CD1 . LEU A 5   ? 0.5733 0.3601 0.3765 -0.0589 0.0074  0.0157  306 LEU A CD1 
19    C CD2 . LEU A 5   ? 0.5820 0.3397 0.3513 -0.0692 0.0152  0.0219  306 LEU A CD2 
20    N N   . LYS A 6   ? 0.4915 0.3489 0.3199 -0.1001 0.0313  0.0139  307 LYS A N   
21    C CA  . LYS A 6   ? 0.4912 0.3818 0.3388 -0.1015 0.0344  0.0115  307 LYS A CA  
22    C C   . LYS A 6   ? 0.4621 0.3650 0.3227 -0.0859 0.0288  0.0104  307 LYS A C   
23    O O   . LYS A 6   ? 0.5614 0.4487 0.4128 -0.0763 0.0246  0.0125  307 LYS A O   
24    C CB  . LYS A 6   ? 0.5608 0.4536 0.3987 -0.1098 0.0423  0.0137  307 LYS A CB  
25    C CG  . LYS A 6   ? 0.7175 0.6058 0.5459 -0.1287 0.0492  0.0143  307 LYS A CG  
26    C CD  . LYS A 6   ? 0.7846 0.6779 0.6041 -0.1369 0.0577  0.0168  307 LYS A CD  
27    C CE  . LYS A 6   ? 0.8631 0.7490 0.6704 -0.1579 0.0650  0.0179  307 LYS A CE  
28    N NZ  . LYS A 6   ? 0.8862 0.7949 0.7110 -0.1682 0.0649  0.0135  307 LYS A NZ  
29    N N   . VAL A 7   ? 0.3705 0.3012 0.2515 -0.0838 0.0287  0.0070  308 VAL A N   
30    C CA  . VAL A 7   ? 0.4112 0.3534 0.3025 -0.0711 0.0248  0.0058  308 VAL A CA  
31    C C   . VAL A 7   ? 0.4828 0.4481 0.3816 -0.0721 0.0304  0.0044  308 VAL A C   
32    O O   . VAL A 7   ? 0.4864 0.4708 0.3938 -0.0804 0.0351  0.0027  308 VAL A O   
33    C CB  . VAL A 7   ? 0.4882 0.4394 0.3947 -0.0641 0.0187  0.0032  308 VAL A CB  
34    C CG1 . VAL A 7   ? 0.5873 0.5171 0.4862 -0.0603 0.0132  0.0047  308 VAL A CG1 
35    C CG2 . VAL A 7   ? 0.4437 0.4148 0.3636 -0.0712 0.0210  0.0003  308 VAL A CG2 
36    N N   . LYS A 8   ? 0.4913 0.4554 0.3861 -0.0636 0.0299  0.0049  309 LYS A N   
37    C CA  . LYS A 8   ? 0.3906 0.3735 0.2892 -0.0620 0.0354  0.0037  309 LYS A CA  
38    C C   . LYS A 8   ? 0.3036 0.2975 0.2130 -0.0498 0.0313  0.0010  309 LYS A C   
39    O O   . LYS A 8   ? 0.3397 0.3203 0.2466 -0.0425 0.0247  0.0011  309 LYS A O   
40    C CB  . LYS A 8   ? 0.3941 0.3637 0.2748 -0.0621 0.0391  0.0064  309 LYS A CB  
41    C CG  . LYS A 8   ? 0.4077 0.3955 0.2902 -0.0587 0.0452  0.0050  309 LYS A CG  
42    C CD  . LYS A 8   ? 0.5432 0.5179 0.4065 -0.0619 0.0504  0.0081  309 LYS A CD  
43    C CE  . LYS A 8   ? 0.5563 0.5468 0.4191 -0.0560 0.0562  0.0065  309 LYS A CE  
44    N NZ  . LYS A 8   ? 0.5874 0.5641 0.4302 -0.0591 0.0613  0.0096  309 LYS A NZ  
45    N N   . ASN A 9   ? 0.3634 0.3815 0.2839 -0.0478 0.0353  -0.0015 310 ASN A N   
46    C CA  . ASN A 9   ? 0.3775 0.4027 0.3026 -0.0354 0.0330  -0.0037 310 ASN A CA  
47    C C   . ASN A 9   ? 0.3436 0.3675 0.2573 -0.0309 0.0377  -0.0035 310 ASN A C   
48    O O   . ASN A 9   ? 0.3938 0.4324 0.3072 -0.0353 0.0454  -0.0033 310 ASN A O   
49    C CB  . ASN A 9   ? 0.3876 0.4387 0.3291 -0.0327 0.0343  -0.0065 310 ASN A CB  
50    C CG  . ASN A 9   ? 0.4450 0.4979 0.3883 -0.0193 0.0314  -0.0085 310 ASN A CG  
51    O OD1 . ASN A 9   ? 0.4827 0.5383 0.4195 -0.0121 0.0348  -0.0093 310 ASN A OD1 
52    N ND2 . ASN A 9   ? 0.4046 0.4531 0.3543 -0.0157 0.0252  -0.0093 310 ASN A ND2 
53    N N   . TRP A 10  ? 0.3007 0.3073 0.2043 -0.0230 0.0334  -0.0036 311 TRP A N   
54    C CA  . TRP A 10  ? 0.4563 0.4567 0.3453 -0.0193 0.0372  -0.0034 311 TRP A CA  
55    C C   . TRP A 10  ? 0.5119 0.5275 0.4031 -0.0094 0.0413  -0.0063 311 TRP A C   
56    O O   . TRP A 10  ? 0.5160 0.5302 0.3955 -0.0058 0.0461  -0.0065 311 TRP A O   
57    C CB  . TRP A 10  ? 0.4011 0.3762 0.2762 -0.0159 0.0305  -0.0025 311 TRP A CB  
58    C CG  . TRP A 10  ? 0.4060 0.3664 0.2742 -0.0238 0.0285  0.0010  311 TRP A CG  
59    C CD1 . TRP A 10  ? 0.4084 0.3615 0.2820 -0.0268 0.0227  0.0022  311 TRP A CD1 
60    C CD2 . TRP A 10  ? 0.5075 0.4577 0.3603 -0.0290 0.0329  0.0039  311 TRP A CD2 
61    N NE1 . TRP A 10  ? 0.3906 0.3284 0.2523 -0.0324 0.0229  0.0056  311 TRP A NE1 
62    C CE2 . TRP A 10  ? 0.4744 0.4094 0.3228 -0.0343 0.0290  0.0069  311 TRP A CE2 
63    C CE3 . TRP A 10  ? 0.5122 0.4639 0.3532 -0.0289 0.0399  0.0044  311 TRP A CE3 
64    C CZ2 . TRP A 10  ? 0.5283 0.4476 0.3597 -0.0395 0.0316  0.0105  311 TRP A CZ2 
65    C CZ3 . TRP A 10  ? 0.5837 0.5210 0.4087 -0.0352 0.0428  0.0081  311 TRP A CZ3 
66    C CH2 . TRP A 10  ? 0.6687 0.5891 0.4884 -0.0404 0.0385  0.0113  311 TRP A CH2 
67    N N   . GLU A 11  ? 0.4170 0.4462 0.3213 -0.0040 0.0395  -0.0085 312 GLU A N   
68    C CA  . GLU A 11  ? 0.4530 0.4987 0.3595 0.0066  0.0438  -0.0112 312 GLU A CA  
69    C C   . GLU A 11  ? 0.5050 0.5815 0.4230 0.0023  0.0518  -0.0112 312 GLU A C   
70    O O   . GLU A 11  ? 0.5357 0.6261 0.4501 0.0078  0.0588  -0.0121 312 GLU A O   
71    C CB  . GLU A 11  ? 0.4620 0.5067 0.3751 0.0153  0.0381  -0.0132 312 GLU A CB  
72    C CG  . GLU A 11  ? 0.6857 0.7418 0.5975 0.0293  0.0415  -0.0159 312 GLU A CG  
73    C CD  . GLU A 11  ? 0.7805 0.8324 0.6966 0.0371  0.0357  -0.0173 312 GLU A CD  
74    O OE1 . GLU A 11  ? 0.5834 0.6226 0.5030 0.0311  0.0292  -0.0162 312 GLU A OE1 
75    O OE2 . GLU A 11  ? 0.9346 0.9957 0.8496 0.0497  0.0380  -0.0193 312 GLU A OE2 
76    N N   . THR A 12  ? 0.4195 0.5077 0.3507 -0.0081 0.0510  -0.0103 313 THR A N   
77    C CA  . THR A 12  ? 0.4234 0.5440 0.3676 -0.0137 0.0576  -0.0109 313 THR A CA  
78    C C   . THR A 12  ? 0.4447 0.5668 0.3849 -0.0294 0.0633  -0.0084 313 THR A C   
79    O O   . THR A 12  ? 0.4345 0.5847 0.3831 -0.0355 0.0702  -0.0087 313 THR A O   
80    C CB  . THR A 12  ? 0.4789 0.6133 0.4396 -0.0160 0.0531  -0.0121 313 THR A CB  
81    O OG1 . THR A 12  ? 0.5458 0.6604 0.5050 -0.0269 0.0481  -0.0104 313 THR A OG1 
82    C CG2 . THR A 12  ? 0.4752 0.6068 0.4381 -0.0006 0.0479  -0.0142 313 THR A CG2 
83    N N   . GLU A 13  ? 0.4305 0.5235 0.3576 -0.0361 0.0605  -0.0057 314 GLU A N   
84    C CA  . GLU A 13  ? 0.5139 0.5998 0.4333 -0.0514 0.0648  -0.0027 314 GLU A CA  
85    C C   . GLU A 13  ? 0.4619 0.5577 0.3924 -0.0647 0.0643  -0.0027 314 GLU A C   
86    O O   . GLU A 13  ? 0.5183 0.6091 0.4421 -0.0792 0.0685  -0.0005 314 GLU A O   
87    C CB  . GLU A 13  ? 0.6507 0.7510 0.5639 -0.0543 0.0749  -0.0018 314 GLU A CB  
88    C CG  . GLU A 13  ? 0.7843 0.8755 0.6853 -0.0402 0.0758  -0.0025 314 GLU A CG  
89    C CD  . GLU A 13  ? 0.9646 1.0469 0.8483 -0.0457 0.0829  0.0003  314 GLU A CD  
90    O OE1 . GLU A 13  ? 1.0679 1.1259 0.9390 -0.0552 0.0814  0.0036  314 GLU A OE1 
91    O OE2 . GLU A 13  ? 0.9930 1.0924 0.8746 -0.0399 0.0903  -0.0007 314 GLU A OE2 
92    N N   . VAL A 14  ? 0.4820 0.5893 0.4273 -0.0607 0.0591  -0.0052 315 VAL A N   
93    C CA  . VAL A 14  ? 0.5016 0.6126 0.4547 -0.0730 0.0572  -0.0055 315 VAL A CA  
94    C C   . VAL A 14  ? 0.4803 0.5562 0.4195 -0.0791 0.0529  -0.0029 315 VAL A C   
95    O O   . VAL A 14  ? 0.4375 0.4914 0.3699 -0.0697 0.0471  -0.0021 315 VAL A O   
96    C CB  . VAL A 14  ? 0.5165 0.6438 0.4859 -0.0654 0.0518  -0.0086 315 VAL A CB  
97    C CG1 . VAL A 14  ? 0.4954 0.6200 0.4699 -0.0771 0.0482  -0.0091 315 VAL A CG1 
98    C CG2 . VAL A 14  ? 0.5340 0.6988 0.5166 -0.0598 0.0564  -0.0109 315 VAL A CG2 
99    N N   . VAL A 15  ? 0.4092 0.4795 0.3427 -0.0949 0.0560  -0.0015 316 VAL A N   
100   C CA  . VAL A 15  ? 0.4232 0.4600 0.3422 -0.1006 0.0524  0.0009  316 VAL A CA  
101   C C   . VAL A 15  ? 0.4150 0.4549 0.3415 -0.1094 0.0495  -0.0010 316 VAL A C   
102   O O   . VAL A 15  ? 0.4590 0.5200 0.3928 -0.1215 0.0539  -0.0025 316 VAL A O   
103   C CB  . VAL A 15  ? 0.4104 0.4290 0.3097 -0.1115 0.0585  0.0046  316 VAL A CB  
104   C CG1 . VAL A 15  ? 0.4180 0.4005 0.3007 -0.1153 0.0542  0.0071  316 VAL A CG1 
105   C CG2 . VAL A 15  ? 0.3888 0.4038 0.2789 -0.1027 0.0613  0.0064  316 VAL A CG2 
106   N N   . LEU A 16  ? 0.4350 0.4550 0.3593 -0.1036 0.0423  -0.0010 317 LEU A N   
107   C CA  . LEU A 16  ? 0.4539 0.4709 0.3817 -0.1105 0.0390  -0.0028 317 LEU A CA  
108   C C   . LEU A 16  ? 0.5313 0.5119 0.4387 -0.1157 0.0377  -0.0002 317 LEU A C   
109   O O   . LEU A 16  ? 0.5997 0.5583 0.4950 -0.1074 0.0356  0.0026  317 LEU A O   
110   C CB  . LEU A 16  ? 0.4143 0.4393 0.3561 -0.0983 0.0321  -0.0053 317 LEU A CB  
111   C CG  . LEU A 16  ? 0.4546 0.5115 0.4135 -0.0902 0.0329  -0.0076 317 LEU A CG  
112   C CD1 . LEU A 16  ? 0.4068 0.4659 0.3754 -0.0781 0.0263  -0.0092 317 LEU A CD1 
113   C CD2 . LEU A 16  ? 0.4195 0.5064 0.3890 -0.1012 0.0377  -0.0098 317 LEU A CD2 
114   N N   . THR A 17  ? 0.4689 0.4426 0.3710 -0.1292 0.0388  -0.0012 318 THR A N   
115   C CA  . THR A 17  ? 0.5382 0.4748 0.4173 -0.1352 0.0385  0.0012  318 THR A CA  
116   C C   . THR A 17  ? 0.4606 0.3856 0.3407 -0.1310 0.0322  -0.0009 318 THR A C   
117   O O   . THR A 17  ? 0.4689 0.4095 0.3594 -0.1380 0.0314  -0.0044 318 THR A O   
118   C CB  . THR A 17  ? 0.5882 0.5200 0.4550 -0.1557 0.0455  0.0019  318 THR A CB  
119   O OG1 . THR A 17  ? 0.6225 0.5748 0.4934 -0.1597 0.0521  0.0032  318 THR A OG1 
120   C CG2 . THR A 17  ? 0.6482 0.5357 0.4858 -0.1598 0.0460  0.0054  318 THR A CG2 
121   N N   . ASP A 18  ? 0.4096 0.3087 0.2785 -0.1196 0.0277  0.0012  319 ASP A N   
122   C CA  . ASP A 18  ? 0.3704 0.2604 0.2411 -0.1122 0.0218  -0.0005 319 ASP A CA  
123   C C   . ASP A 18  ? 0.5729 0.4284 0.4198 -0.1195 0.0223  0.0002  319 ASP A C   
124   O O   . ASP A 18  ? 0.5386 0.3662 0.3646 -0.1179 0.0235  0.0039  319 ASP A O   
125   C CB  . ASP A 18  ? 0.4448 0.3318 0.3195 -0.0942 0.0164  0.0011  319 ASP A CB  
126   C CG  . ASP A 18  ? 0.4418 0.3278 0.3231 -0.0859 0.0109  -0.0010 319 ASP A CG  
127   O OD1 . ASP A 18  ? 0.4843 0.3474 0.3514 -0.0875 0.0099  -0.0011 319 ASP A OD1 
128   O OD2 . ASP A 18  ? 0.4451 0.3522 0.3445 -0.0778 0.0078  -0.0025 319 ASP A OD2 
129   N N   . THR A 19  ? 0.5105 0.3665 0.3589 -0.1270 0.0213  -0.0033 320 THR A N   
130   C CA  . THR A 19  ? 0.4537 0.2748 0.2793 -0.1305 0.0204  -0.0035 320 THR A CA  
131   C C   . THR A 19  ? 0.4885 0.3080 0.3199 -0.1187 0.0146  -0.0060 320 THR A C   
132   O O   . THR A 19  ? 0.5456 0.3340 0.3571 -0.1156 0.0132  -0.0058 320 THR A O   
133   C CB  . THR A 19  ? 0.4861 0.3028 0.3024 -0.1524 0.0247  -0.0060 320 THR A CB  
134   O OG1 . THR A 19  ? 0.5276 0.3811 0.3679 -0.1583 0.0238  -0.0104 320 THR A OG1 
135   C CG2 . THR A 19  ? 0.5741 0.3845 0.3781 -0.1659 0.0314  -0.0029 320 THR A CG2 
136   N N   . LEU A 20  ? 0.4719 0.3228 0.3283 -0.1116 0.0116  -0.0082 321 LEU A N   
137   C CA  . LEU A 20  ? 0.4954 0.3461 0.3573 -0.1009 0.0067  -0.0104 321 LEU A CA  
138   C C   . LEU A 20  ? 0.5727 0.4007 0.4229 -0.0852 0.0038  -0.0074 321 LEU A C   
139   O O   . LEU A 20  ? 0.4508 0.2638 0.2930 -0.0791 0.0013  -0.0087 321 LEU A O   
140   C CB  . LEU A 20  ? 0.3595 0.2462 0.2485 -0.0948 0.0043  -0.0122 321 LEU A CB  
141   C CG  . LEU A 20  ? 0.3974 0.2892 0.2945 -0.0855 -0.0002 -0.0146 321 LEU A CG  
142   C CD1 . LEU A 20  ? 0.4550 0.3380 0.3437 -0.0956 -0.0003 -0.0185 321 LEU A CD1 
143   C CD2 . LEU A 20  ? 0.3041 0.2285 0.2249 -0.0800 -0.0018 -0.0154 321 LEU A CD2 
144   N N   . HIS A 21  ? 0.4333 0.2584 0.2811 -0.0785 0.0041  -0.0034 322 HIS A N   
145   C CA  . HIS A 21  ? 0.4365 0.2463 0.2761 -0.0625 0.0005  -0.0006 322 HIS A CA  
146   C C   . HIS A 21  ? 0.5271 0.2999 0.3394 -0.0609 0.0008  0.0002  322 HIS A C   
147   O O   . HIS A 21  ? 0.5067 0.2681 0.3123 -0.0461 -0.0025 0.0018  322 HIS A O   
148   C CB  . HIS A 21  ? 0.4319 0.2428 0.2700 -0.0577 0.0007  0.0033  322 HIS A CB  
149   C CG  . HIS A 21  ? 0.4848 0.2713 0.3003 -0.0665 0.0050  0.0060  322 HIS A CG  
150   N ND1 . HIS A 21  ? 0.4774 0.2724 0.2943 -0.0815 0.0102  0.0057  322 HIS A ND1 
151   C CD2 . HIS A 21  ? 0.5427 0.2958 0.3319 -0.0626 0.0053  0.0092  322 HIS A CD2 
152   C CE1 . HIS A 21  ? 0.6282 0.3957 0.4208 -0.0878 0.0138  0.0087  322 HIS A CE1 
153   N NE2 . HIS A 21  ? 0.6022 0.3423 0.3767 -0.0762 0.0107  0.0109  322 HIS A NE2 
154   N N   . LEU A 22  ? 0.5154 0.2685 0.3104 -0.0758 0.0047  -0.0008 323 LEU A N   
155   C CA  . LEU A 22  ? 0.6381 0.3514 0.4036 -0.0743 0.0051  -0.0003 323 LEU A CA  
156   C C   . LEU A 22  ? 0.6905 0.4014 0.4576 -0.0659 0.0019  -0.0037 323 LEU A C   
157   O O   . LEU A 22  ? 0.8033 0.4823 0.5468 -0.0582 0.0012  -0.0032 323 LEU A O   
158   C CB  . LEU A 22  ? 0.7434 0.4358 0.4894 -0.0948 0.0102  -0.0012 323 LEU A CB  
159   C CG  . LEU A 22  ? 0.7606 0.4504 0.4998 -0.1054 0.0149  0.0024  323 LEU A CG  
160   C CD1 . LEU A 22  ? 0.8678 0.5385 0.5883 -0.1277 0.0200  0.0009  323 LEU A CD1 
161   C CD2 . LEU A 22  ? 0.7527 0.4172 0.4723 -0.0923 0.0142  0.0078  323 LEU A CD2 
162   N N   . LYS A 23  ? 0.5494 0.2923 0.3420 -0.0663 0.0000  -0.0070 324 LYS A N   
163   C CA  . LYS A 23  ? 0.6074 0.3521 0.4037 -0.0583 -0.0028 -0.0102 324 LYS A CA  
164   C C   . LYS A 23  ? 0.6660 0.4274 0.4772 -0.0393 -0.0065 -0.0085 324 LYS A C   
165   O O   . LYS A 23  ? 0.7308 0.5012 0.5499 -0.0326 -0.0085 -0.0109 324 LYS A O   
166   C CB  . LYS A 23  ? 0.5426 0.3122 0.3566 -0.0700 -0.0028 -0.0148 324 LYS A CB  
167   C CG  . LYS A 23  ? 0.7219 0.4777 0.5218 -0.0896 0.0001  -0.0176 324 LYS A CG  
168   C CD  . LYS A 23  ? 0.8507 0.6053 0.6491 -0.0928 -0.0017 -0.0228 324 LYS A CD  
169   C CE  . LYS A 23  ? 0.9863 0.6971 0.7521 -0.0916 -0.0012 -0.0239 324 LYS A CE  
170   N NZ  . LYS A 23  ? 1.0022 0.7009 0.7549 -0.1110 -0.0001 -0.0288 324 LYS A NZ  
171   N N   . SER A 24  ? 0.5301 0.2978 0.3458 -0.0315 -0.0075 -0.0044 325 SER A N   
172   C CA  . SER A 24  ? 0.5936 0.3801 0.4246 -0.0157 -0.0113 -0.0031 325 SER A CA  
173   C C   . SER A 24  ? 0.6761 0.4425 0.4911 -0.0010 -0.0129 -0.0026 325 SER A C   
174   O O   . SER A 24  ? 0.6980 0.4314 0.4866 0.0001  -0.0115 -0.0017 325 SER A O   
175   C CB  . SER A 24  ? 0.5842 0.3814 0.4219 -0.0118 -0.0124 0.0007  325 SER A CB  
176   O OG  . SER A 24  ? 0.7835 0.5544 0.5989 -0.0045 -0.0127 0.0041  325 SER A OG  
177   N N   . THR A 25  ? 0.7206 0.5067 0.5507 0.0107  -0.0155 -0.0031 326 THR A N   
178   C CA  . THR A 25  ? 0.8077 0.5797 0.6250 0.0256  -0.0166 -0.0032 326 THR A CA  
179   C C   . THR A 25  ? 0.7977 0.5834 0.6220 0.0426  -0.0198 0.0002  326 THR A C   
180   O O   . THR A 25  ? 0.9322 0.6984 0.7379 0.0557  -0.0206 0.0020  326 THR A O   
181   C CB  . THR A 25  ? 0.8995 0.6808 0.7247 0.0249  -0.0162 -0.0073 326 THR A CB  
182   O OG1 . THR A 25  ? 0.8662 0.6787 0.7172 0.0162  -0.0166 -0.0085 326 THR A OG1 
183   C CG2 . THR A 25  ? 0.9522 0.7043 0.7558 0.0149  -0.0136 -0.0108 326 THR A CG2 
184   N N   . LEU A 26  ? 0.6478 0.4661 0.4971 0.0425  -0.0219 0.0011  327 LEU A N   
185   C CA  . LEU A 26  ? 0.6765 0.5125 0.5349 0.0563  -0.0254 0.0039  327 LEU A CA  
186   C C   . LEU A 26  ? 0.6887 0.5260 0.5463 0.0552  -0.0275 0.0072  327 LEU A C   
187   O O   . LEU A 26  ? 0.5433 0.3799 0.4033 0.0425  -0.0261 0.0071  327 LEU A O   
188   C CB  . LEU A 26  ? 0.8025 0.6726 0.6872 0.0564  -0.0266 0.0028  327 LEU A CB  
189   C CG  . LEU A 26  ? 0.8129 0.6879 0.7005 0.0617  -0.0252 0.0002  327 LEU A CG  
190   C CD1 . LEU A 26  ? 0.7613 0.6145 0.6276 0.0763  -0.0248 0.0005  327 LEU A CD1 
191   C CD2 . LEU A 26  ? 0.8175 0.6884 0.7068 0.0486  -0.0225 -0.0034 327 LEU A CD2 
192   N N   . GLU A 27  ? 0.6120 0.4525 0.4659 0.0695  -0.0309 0.0100  328 GLU A N   
193   C CA  . GLU A 27  ? 0.5712 0.4180 0.4265 0.0700  -0.0339 0.0130  328 GLU A CA  
194   C C   . GLU A 27  ? 0.5533 0.4297 0.4334 0.0606  -0.0352 0.0122  328 GLU A C   
195   O O   . GLU A 27  ? 0.5014 0.4005 0.3997 0.0605  -0.0357 0.0106  328 GLU A O   
196   C CB  . GLU A 27  ? 0.5213 0.3728 0.3713 0.0882  -0.0382 0.0158  328 GLU A CB  
197   C CG  . GLU A 27  ? 0.5281 0.3457 0.3489 0.1000  -0.0372 0.0173  328 GLU A CG  
198   C CD  . GLU A 27  ? 0.6659 0.4906 0.4814 0.1201  -0.0418 0.0202  328 GLU A CD  
199   O OE1 . GLU A 27  ? 0.6345 0.4943 0.4718 0.1241  -0.0457 0.0207  328 GLU A OE1 
200   O OE2 . GLU A 27  ? 0.7182 0.5136 0.5070 0.1320  -0.0417 0.0222  328 GLU A OE2 
201   N N   . THR A 28  ? 0.4704 0.3445 0.3492 0.0525  -0.0354 0.0133  329 THR A N   
202   C CA  . THR A 28  ? 0.3532 0.2517 0.2515 0.0453  -0.0371 0.0127  329 THR A CA  
203   C C   . THR A 28  ? 0.3725 0.2910 0.2793 0.0539  -0.0427 0.0145  329 THR A C   
204   O O   . THR A 28  ? 0.4351 0.3752 0.3587 0.0489  -0.0445 0.0136  329 THR A O   
205   C CB  . THR A 28  ? 0.4931 0.3824 0.3856 0.0350  -0.0352 0.0132  329 THR A CB  
206   O OG1 . THR A 28  ? 0.4500 0.3230 0.3245 0.0409  -0.0370 0.0163  329 THR A OG1 
207   C CG2 . THR A 28  ? 0.4608 0.3365 0.3480 0.0242  -0.0297 0.0112  329 THR A CG2 
208   N N   . GLY A 29  ? 0.4045 0.3157 0.2989 0.0666  -0.0455 0.0169  330 GLY A N   
209   C CA  . GLY A 29  ? 0.4855 0.4150 0.3853 0.0741  -0.0515 0.0188  330 GLY A CA  
210   C C   . GLY A 29  ? 0.5073 0.4238 0.3928 0.0740  -0.0538 0.0211  330 GLY A C   
211   O O   . GLY A 29  ? 0.5341 0.4585 0.4163 0.0840  -0.0591 0.0233  330 GLY A O   
212   N N   . CYS A 30  ? 0.5110 0.4093 0.3879 0.0632  -0.0498 0.0208  331 CYS A N   
213   C CA  . CYS A 30  ? 0.4393 0.3231 0.3003 0.0627  -0.0510 0.0232  331 CYS A CA  
214   C C   . CYS A 30  ? 0.4824 0.3381 0.3180 0.0729  -0.0505 0.0262  331 CYS A C   
215   O O   . CYS A 30  ? 0.4891 0.3311 0.3170 0.0776  -0.0478 0.0259  331 CYS A O   
216   C CB  . CYS A 30  ? 0.3821 0.2569 0.2418 0.0480  -0.0460 0.0219  331 CYS A CB  
217   S SG  . CYS A 30  ? 0.4220 0.3237 0.3070 0.0372  -0.0460 0.0184  331 CYS A SG  
218   N N   . THR A 31  ? 0.4580 0.3030 0.2782 0.0766  -0.0531 0.0291  332 THR A N   
219   C CA  . THR A 31  ? 0.5157 0.3275 0.3068 0.0836  -0.0516 0.0325  332 THR A CA  
220   C C   . THR A 31  ? 0.5093 0.3063 0.2874 0.0741  -0.0494 0.0341  332 THR A C   
221   O O   . THR A 31  ? 0.5812 0.3949 0.3730 0.0646  -0.0496 0.0325  332 THR A O   
222   C CB  . THR A 31  ? 0.5529 0.3663 0.3342 0.1032  -0.0580 0.0355  332 THR A CB  
223   O OG1 . THR A 31  ? 0.5398 0.3695 0.3247 0.1051  -0.0641 0.0368  332 THR A OG1 
224   C CG2 . THR A 31  ? 0.5146 0.3515 0.3131 0.1128  -0.0605 0.0337  332 THR A CG2 
225   N N   . GLU A 32  ? 0.5832 0.3470 0.3327 0.0771  -0.0469 0.0375  333 GLU A N   
226   C CA  . GLU A 32  ? 0.6573 0.4080 0.3930 0.0695  -0.0449 0.0396  333 GLU A CA  
227   C C   . GLU A 32  ? 0.5934 0.3619 0.3328 0.0766  -0.0522 0.0409  333 GLU A C   
228   O O   . GLU A 32  ? 0.6127 0.3782 0.3466 0.0691  -0.0509 0.0416  333 GLU A O   
229   C CB  . GLU A 32  ? 0.8165 0.5257 0.5179 0.0711  -0.0407 0.0436  333 GLU A CB  
230   C CG  . GLU A 32  ? 1.0461 0.7383 0.7285 0.0902  -0.0448 0.0465  333 GLU A CG  
231   C CD  . GLU A 32  ? 1.2793 0.9528 0.9546 0.0907  -0.0406 0.0451  333 GLU A CD  
232   O OE1 . GLU A 32  ? 1.1970 0.8927 0.8961 0.0879  -0.0404 0.0411  333 GLU A OE1 
233   O OE2 . GLU A 32  ? 1.4492 1.0835 1.0930 0.0934  -0.0374 0.0481  333 GLU A OE2 
234   N N   . TYR A 33  ? 0.5406 0.3297 0.2900 0.0900  -0.0597 0.0409  334 TYR A N   
235   C CA  . TYR A 33  ? 0.5084 0.3168 0.2617 0.0961  -0.0676 0.0417  334 TYR A CA  
236   C C   . TYR A 33  ? 0.5152 0.3608 0.2988 0.0897  -0.0714 0.0376  334 TYR A C   
237   O O   . TYR A 33  ? 0.5185 0.3790 0.3056 0.0892  -0.0770 0.0373  334 TYR A O   
238   C CB  . TYR A 33  ? 0.5998 0.4070 0.3408 0.1164  -0.0743 0.0450  334 TYR A CB  
239   C CG  . TYR A 33  ? 0.7636 0.5303 0.4695 0.1237  -0.0716 0.0496  334 TYR A CG  
240   C CD1 . TYR A 33  ? 0.9667 0.7149 0.6531 0.1189  -0.0706 0.0522  334 TYR A CD1 
241   C CD2 . TYR A 33  ? 0.8090 0.5538 0.4989 0.1354  -0.0697 0.0515  334 TYR A CD2 
242   C CE1 . TYR A 33  ? 1.0893 0.7983 0.7414 0.1247  -0.0677 0.0570  334 TYR A CE1 
243   C CE2 . TYR A 33  ? 0.9826 0.6858 0.6367 0.1416  -0.0670 0.0559  334 TYR A CE2 
244   C CZ  . TYR A 33  ? 1.1368 0.8224 0.7723 0.1358  -0.0660 0.0589  334 TYR A CZ  
245   O OH  . TYR A 33  ? 1.2886 0.9327 0.8885 0.1402  -0.0625 0.0631  334 TYR A OH  
246   N N   . ILE A 34  ? 0.5001 0.3595 0.3036 0.0844  -0.0685 0.0345  335 ILE A N   
247   C CA  . ILE A 34  ? 0.4853 0.3771 0.3152 0.0781  -0.0717 0.0310  335 ILE A CA  
248   C C   . ILE A 34  ? 0.5243 0.4175 0.3680 0.0652  -0.0649 0.0278  335 ILE A C   
249   O O   . ILE A 34  ? 0.5846 0.4660 0.4261 0.0654  -0.0599 0.0276  335 ILE A O   
250   C CB  . ILE A 34  ? 0.5339 0.4514 0.3769 0.0897  -0.0780 0.0310  335 ILE A CB  
251   C CG1 . ILE A 34  ? 0.4869 0.4366 0.3535 0.0816  -0.0821 0.0280  335 ILE A CG1 
252   C CG2 . ILE A 34  ? 0.6573 0.5713 0.5041 0.0949  -0.0739 0.0306  335 ILE A CG2 
253   C CD1 . ILE A 34  ? 0.4435 0.4202 0.3177 0.0917  -0.0907 0.0288  335 ILE A CD1 
254   N N   . CYS A 35  ? 0.4193 0.3258 0.2757 0.0544  -0.0648 0.0251  336 CYS A N   
255   C CA  . CYS A 35  ? 0.3538 0.2652 0.2244 0.0439  -0.0594 0.0221  336 CYS A CA  
256   C C   . CYS A 35  ? 0.3958 0.3346 0.2881 0.0429  -0.0632 0.0198  336 CYS A C   
257   O O   . CYS A 35  ? 0.3941 0.3480 0.2915 0.0423  -0.0689 0.0193  336 CYS A O   
258   C CB  . CYS A 35  ? 0.3777 0.2817 0.2451 0.0329  -0.0551 0.0207  336 CYS A CB  
259   S SG  . CYS A 35  ? 0.4051 0.3198 0.2914 0.0225  -0.0498 0.0170  336 CYS A SG  
260   N N   . MET A 36  ? 0.3632 0.3078 0.2668 0.0423  -0.0601 0.0186  337 MET A N   
261   C CA  . MET A 36  ? 0.3200 0.2891 0.2431 0.0406  -0.0624 0.0168  337 MET A CA  
262   C C   . MET A 36  ? 0.2866 0.2577 0.2201 0.0297  -0.0578 0.0141  337 MET A C   
263   O O   . MET A 36  ? 0.3265 0.3118 0.2739 0.0280  -0.0573 0.0128  337 MET A O   
264   C CB  . MET A 36  ? 0.4368 0.4136 0.3643 0.0507  -0.0630 0.0177  337 MET A CB  
265   C CG  . MET A 36  ? 0.5533 0.5332 0.4722 0.0636  -0.0685 0.0203  337 MET A CG  
266   S SD  . MET A 36  ? 0.7181 0.7183 0.6481 0.0755  -0.0699 0.0207  337 MET A SD  
267   C CE  . MET A 36  ? 0.7859 0.8160 0.7236 0.0813  -0.0791 0.0219  337 MET A CE  
268   N N   . GLY A 37  ? 0.3870 0.3448 0.3132 0.0228  -0.0543 0.0133  338 GLY A N   
269   C CA  . GLY A 37  ? 0.3225 0.2809 0.2563 0.0146  -0.0495 0.0109  338 GLY A CA  
270   C C   . GLY A 37  ? 0.3250 0.2994 0.2721 0.0098  -0.0517 0.0090  338 GLY A C   
271   O O   . GLY A 37  ? 0.3264 0.3034 0.2812 0.0055  -0.0482 0.0074  338 GLY A O   
272   N N   . SER A 38  ? 0.3225 0.3071 0.2712 0.0098  -0.0575 0.0092  339 SER A N   
273   C CA  . SER A 38  ? 0.3699 0.3675 0.3289 0.0035  -0.0596 0.0075  339 SER A CA  
274   C C   . SER A 38  ? 0.3784 0.3957 0.3496 0.0057  -0.0628 0.0082  339 SER A C   
275   O O   . SER A 38  ? 0.3494 0.3784 0.3285 -0.0007 -0.0649 0.0071  339 SER A O   
276   C CB  . SER A 38  ? 0.3066 0.3021 0.2585 -0.0014 -0.0636 0.0064  339 SER A CB  
277   O OG  . SER A 38  ? 0.3312 0.3344 0.2798 0.0023  -0.0701 0.0076  339 SER A OG  
278   N N   . ILE A 39  ? 0.3618 0.3826 0.3336 0.0147  -0.0631 0.0100  340 ILE A N   
279   C CA  . ILE A 39  ? 0.3101 0.3512 0.2940 0.0184  -0.0649 0.0106  340 ILE A CA  
280   C C   . ILE A 39  ? 0.2887 0.3305 0.2808 0.0154  -0.0595 0.0096  340 ILE A C   
281   O O   . ILE A 39  ? 0.2976 0.3244 0.2847 0.0167  -0.0548 0.0092  340 ILE A O   
282   C CB  . ILE A 39  ? 0.4046 0.4466 0.3834 0.0313  -0.0665 0.0128  340 ILE A CB  
283   C CG1 . ILE A 39  ? 0.4559 0.4949 0.4240 0.0353  -0.0719 0.0141  340 ILE A CG1 
284   C CG2 . ILE A 39  ? 0.4061 0.4723 0.3980 0.0365  -0.0680 0.0134  340 ILE A CG2 
285   C CD1 . ILE A 39  ? 0.4857 0.5488 0.4623 0.0328  -0.0787 0.0139  340 ILE A CD1 
286   N N   . MET A 40  ? 0.2643 0.3240 0.2684 0.0108  -0.0604 0.0093  341 MET A N   
287   C CA  . MET A 40  ? 0.3364 0.3967 0.3473 0.0075  -0.0556 0.0085  341 MET A CA  
288   C C   . MET A 40  ? 0.3593 0.4191 0.3711 0.0166  -0.0524 0.0091  341 MET A C   
289   O O   . MET A 40  ? 0.3187 0.3671 0.3285 0.0160  -0.0479 0.0081  341 MET A O   
290   C CB  . MET A 40  ? 0.4312 0.5103 0.4528 0.0001  -0.0571 0.0085  341 MET A CB  
291   C CG  . MET A 40  ? 0.6484 0.7277 0.6755 -0.0035 -0.0524 0.0081  341 MET A CG  
292   S SD  . MET A 40  ? 0.7084 0.7695 0.7289 -0.0130 -0.0501 0.0065  341 MET A SD  
293   C CE  . MET A 40  ? 0.4160 0.4830 0.4349 -0.0230 -0.0555 0.0062  341 MET A CE  
294   N N   . HIS A 41  ? 0.3622 0.4345 0.3762 0.0256  -0.0548 0.0105  342 HIS A N   
295   C CA  A HIS A 41  ? 0.4297 0.4991 0.4411 0.0363  -0.0521 0.0109  342 HIS A CA  
296   C CA  B HIS A 41  ? 0.4311 0.5004 0.4425 0.0363  -0.0521 0.0109  342 HIS A CA  
297   C C   . HIS A 41  ? 0.3852 0.4465 0.3852 0.0469  -0.0550 0.0124  342 HIS A C   
298   O O   . HIS A 41  ? 0.3357 0.4134 0.3387 0.0560  -0.0583 0.0138  342 HIS A O   
299   C CB  A HIS A 41  ? 0.4354 0.5286 0.4591 0.0398  -0.0515 0.0114  342 HIS A CB  
300   C CB  B HIS A 41  ? 0.4354 0.5281 0.4591 0.0395  -0.0513 0.0114  342 HIS A CB  
301   C CG  A HIS A 41  ? 0.4119 0.5194 0.4471 0.0282  -0.0509 0.0110  342 HIS A CG  
302   C CG  B HIS A 41  ? 0.5068 0.5936 0.5268 0.0493  -0.0473 0.0111  342 HIS A CG  
303   N ND1 A HIS A 41  ? 0.4509 0.5494 0.4870 0.0215  -0.0466 0.0099  342 HIS A ND1 
304   N ND1 B HIS A 41  ? 0.5139 0.6194 0.5396 0.0593  -0.0472 0.0120  342 HIS A ND1 
305   C CD2 A HIS A 41  ? 0.4517 0.5813 0.4968 0.0218  -0.0541 0.0117  342 HIS A CD2 
306   C CD2 B HIS A 41  ? 0.4828 0.5476 0.4934 0.0503  -0.0434 0.0097  342 HIS A CD2 
307   C CE1 A HIS A 41  ? 0.4150 0.5265 0.4593 0.0120  -0.0469 0.0102  342 HIS A CE1 
308   C CE1 B HIS A 41  ? 0.5193 0.6117 0.5375 0.0669  -0.0433 0.0111  342 HIS A CE1 
309   N NE2 A HIS A 41  ? 0.4245 0.5548 0.4744 0.0111  -0.0512 0.0112  342 HIS A NE2 
310   N NE2 B HIS A 41  ? 0.4946 0.5619 0.5034 0.0608  -0.0411 0.0096  342 HIS A NE2 
311   N N   . PRO A 42  ? 0.4930 0.5298 0.4791 0.0464  -0.0538 0.0122  343 PRO A N   
312   C CA  . PRO A 42  ? 0.5087 0.5352 0.4813 0.0557  -0.0567 0.0141  343 PRO A CA  
313   C C   . PRO A 42  ? 0.5382 0.5581 0.5023 0.0697  -0.0556 0.0151  343 PRO A C   
314   O O   . PRO A 42  ? 0.4731 0.4909 0.4278 0.0805  -0.0590 0.0171  343 PRO A O   
315   C CB  . PRO A 42  ? 0.4707 0.4721 0.4304 0.0490  -0.0544 0.0137  343 PRO A CB  
316   C CG  . PRO A 42  ? 0.4934 0.4894 0.4579 0.0407  -0.0492 0.0115  343 PRO A CG  
317   C CD  . PRO A 42  ? 0.4900 0.5090 0.4717 0.0371  -0.0497 0.0106  343 PRO A CD  
318   N N   . SER A 43  ? 0.4416 0.4570 0.4070 0.0707  -0.0511 0.0137  344 SER A N   
319   C CA  . SER A 43  ? 0.5522 0.5524 0.5039 0.0835  -0.0493 0.0142  344 SER A CA  
320   C C   . SER A 43  ? 0.5687 0.5838 0.5301 0.0884  -0.0468 0.0130  344 SER A C   
321   O O   . SER A 43  ? 0.4900 0.5152 0.4639 0.0788  -0.0444 0.0114  344 SER A O   
322   C CB  . SER A 43  ? 0.5130 0.4794 0.4469 0.0788  -0.0453 0.0133  344 SER A CB  
323   O OG  . SER A 43  ? 0.5518 0.4988 0.4695 0.0898  -0.0433 0.0133  344 SER A OG  
324   N N   . GLN A 44  ? 0.5916 0.6084 0.5464 0.1043  -0.0473 0.0140  345 GLN A N   
325   C CA  . GLN A 44  ? 0.6615 0.6876 0.6208 0.1114  -0.0440 0.0128  345 GLN A CA  
326   C C   . GLN A 44  ? 0.7086 0.7023 0.6464 0.1189  -0.0403 0.0115  345 GLN A C   
327   O O   . GLN A 44  ? 0.7211 0.7176 0.6566 0.1296  -0.0380 0.0106  345 GLN A O   
328   C CB  . GLN A 44  ? 0.6548 0.7118 0.6241 0.1247  -0.0468 0.0145  345 GLN A CB  
329   C CG  . GLN A 44  ? 0.7473 0.8353 0.7350 0.1170  -0.0514 0.0158  345 GLN A CG  
330   C CD  . GLN A 44  ? 0.7581 0.8775 0.7540 0.1309  -0.0550 0.0176  345 GLN A CD  
331   O OE1 . GLN A 44  ? 0.7212 0.8636 0.7279 0.1364  -0.0527 0.0173  345 GLN A OE1 
332   N NE2 . GLN A 44  ? 0.7249 0.8467 0.7153 0.1371  -0.0607 0.0195  345 GLN A NE2 
333   N N   . HIS A 45  ? 0.6507 0.6133 0.5718 0.1130  -0.0396 0.0112  346 HIS A N   
334   C CA  . HIS A 45  ? 0.7234 0.6516 0.6215 0.1169  -0.0362 0.0097  346 HIS A CA  
335   C C   . HIS A 45  ? 0.7495 0.6776 0.6535 0.1086  -0.0321 0.0064  346 HIS A C   
336   O O   . HIS A 45  ? 0.7768 0.7060 0.6891 0.0931  -0.0310 0.0050  346 HIS A O   
337   C CB  . HIS A 45  ? 0.7464 0.6442 0.6268 0.1090  -0.0360 0.0105  346 HIS A CB  
338   C CG  . HIS A 45  ? 0.7777 0.6368 0.6299 0.1138  -0.0332 0.0096  346 HIS A CG  
339   N ND1 . HIS A 45  ? 0.7773 0.6066 0.6128 0.1023  -0.0311 0.0093  346 HIS A ND1 
340   C CD2 . HIS A 45  ? 0.7706 0.6147 0.6067 0.1285  -0.0318 0.0089  346 HIS A CD2 
341   C CE1 . HIS A 45  ? 0.8074 0.6034 0.6170 0.1083  -0.0288 0.0084  346 HIS A CE1 
342   N NE2 . HIS A 45  ? 0.7494 0.5523 0.5580 0.1250  -0.0292 0.0081  346 HIS A NE2 
343   N N   . ALA A 46  ? 0.7682 0.6963 0.6676 0.1200  -0.0300 0.0050  347 ALA A N   
344   C CA  . ALA A 46  ? 0.6522 0.5770 0.5529 0.1144  -0.0262 0.0017  347 ALA A CA  
345   C C   . ALA A 46  ? 0.7022 0.5885 0.5751 0.1185  -0.0238 -0.0006 347 ALA A C   
346   O O   . ALA A 46  ? 0.7661 0.6311 0.6188 0.1304  -0.0245 0.0008  347 ALA A O   
347   C CB  . ALA A 46  ? 0.5705 0.5244 0.4861 0.1232  -0.0250 0.0015  347 ALA A CB  
348   N N   . ARG A 47  ? 0.7983 0.6744 0.6685 0.1085  -0.0211 -0.0041 348 ARG A N   
349   C CA  . ARG A 47  ? 0.8715 0.7088 0.7140 0.1087  -0.0190 -0.0068 348 ARG A CA  
350   C C   . ARG A 47  ? 0.8039 0.6314 0.6317 0.1260  -0.0170 -0.0084 348 ARG A C   
351   O O   . ARG A 47  ? 0.9017 0.6928 0.7010 0.1314  -0.0159 -0.0098 348 ARG A O   
352   C CB  . ARG A 47  ? 0.8366 0.6672 0.6810 0.0899  -0.0175 -0.0102 348 ARG A CB  
353   C CG  . ARG A 47  ? 0.8312 0.6718 0.6889 0.0747  -0.0190 -0.0086 348 ARG A CG  
354   C CD  . ARG A 47  ? 0.8959 0.7166 0.7435 0.0585  -0.0175 -0.0116 348 ARG A CD  
355   N NE  . ARG A 47  ? 1.0242 0.8508 0.8763 0.0535  -0.0163 -0.0155 348 ARG A NE  
356   C CZ  . ARG A 47  ? 1.0650 0.8722 0.9039 0.0424  -0.0151 -0.0192 348 ARG A CZ  
357   N NH1 . ARG A 47  ? 1.1734 0.9539 0.9939 0.0344  -0.0145 -0.0193 348 ARG A NH1 
358   N NH2 . ARG A 47  ? 0.8524 0.6669 0.6957 0.0386  -0.0146 -0.0228 348 ARG A NH2 
359   N N   . ARG A 48  ? 0.7752 0.6331 0.6201 0.1349  -0.0164 -0.0082 349 ARG A N   
360   C CA  . ARG A 48  ? 0.8650 0.7194 0.6983 0.1535  -0.0141 -0.0094 349 ARG A CA  
361   C C   . ARG A 48  ? 0.8661 0.7609 0.7207 0.1663  -0.0149 -0.0063 349 ARG A C   
362   O O   . ARG A 48  ? 0.8746 0.8013 0.7551 0.1565  -0.0164 -0.0044 349 ARG A O   
363   C CB  . ARG A 48  ? 0.8396 0.6886 0.6695 0.1486  -0.0108 -0.0139 349 ARG A CB  
364   C CG  . ARG A 48  ? 0.7834 0.6511 0.6345 0.1287  -0.0111 -0.0150 349 ARG A CG  
365   C CD  . ARG A 48  ? 0.7699 0.6802 0.6492 0.1301  -0.0107 -0.0127 349 ARG A CD  
366   N NE  . ARG A 48  ? 0.8993 0.8209 0.7764 0.1484  -0.0081 -0.0127 349 ARG A NE  
367   C CZ  . ARG A 48  ? 0.9479 0.8636 0.8161 0.1531  -0.0047 -0.0159 349 ARG A CZ  
368   N NH1 . ARG A 48  ? 0.9022 0.8008 0.7631 0.1405  -0.0041 -0.0196 349 ARG A NH1 
369   N NH2 . ARG A 48  ? 1.0242 0.9525 0.8907 0.1711  -0.0019 -0.0156 349 ARG A NH2 
370   N N   . PRO A 49  ? 0.9189 0.8133 0.7624 0.1880  -0.0139 -0.0057 350 PRO A N   
371   C CA  . PRO A 49  ? 0.9819 0.9185 0.8463 0.2003  -0.0148 -0.0026 350 PRO A CA  
372   C C   . PRO A 49  ? 1.0644 1.0373 0.9548 0.1921  -0.0124 -0.0031 350 PRO A C   
373   O O   . PRO A 49  ? 1.0804 1.0448 0.9702 0.1809  -0.0098 -0.0060 350 PRO A O   
374   C CB  . PRO A 49  ? 0.9787 0.9035 0.8220 0.2262  -0.0131 -0.0029 350 PRO A CB  
375   C CG  . PRO A 49  ? 1.0136 0.8922 0.8271 0.2256  -0.0101 -0.0070 350 PRO A CG  
376   C CD  . PRO A 49  ? 1.0036 0.8586 0.8134 0.2027  -0.0119 -0.0078 350 PRO A CD  
377   N N   . GLU A 50  ? 1.2135 1.2279 1.1260 0.1977  -0.0135 -0.0002 351 GLU A N   
378   C CA  . GLU A 50  ? 1.3045 1.3549 1.2439 0.1852  -0.0121 0.0005  351 GLU A CA  
379   C C   . GLU A 50  ? 1.3118 1.3629 1.2493 0.1863  -0.0066 -0.0022 351 GLU A C   
380   O O   . GLU A 50  ? 1.2881 1.3456 1.2366 0.1704  -0.0053 -0.0030 351 GLU A O   
381   C CB  . GLU A 50  ? 1.3582 1.4526 1.3188 0.1919  -0.0140 0.0040  351 GLU A CB  
382   C CG  . GLU A 50  ? 1.3698 1.4706 1.3387 0.1841  -0.0200 0.0066  351 GLU A CG  
383   C CD  . GLU A 50  ? 1.3896 1.5159 1.3633 0.2007  -0.0232 0.0094  351 GLU A CD  
384   O OE1 . GLU A 50  ? 1.3807 1.5284 1.3570 0.2170  -0.0205 0.0095  351 GLU A OE1 
385   O OE2 . GLU A 50  ? 1.3990 1.5251 1.3737 0.1981  -0.0286 0.0113  351 GLU A OE2 
386   N N   . ASP A 51  ? 1.3162 1.3598 1.2381 0.2056  -0.0033 -0.0037 352 ASP A N   
387   C CA  . ASP A 51  ? 1.2896 1.3325 1.2076 0.2072  0.0020  -0.0066 352 ASP A CA  
388   C C   . ASP A 51  ? 1.2500 1.2470 1.1357 0.2149  0.0036  -0.0108 352 ASP A C   
389   O O   . ASP A 51  ? 1.2994 1.2625 1.1673 0.2127  0.0006  -0.0116 352 ASP A O   
390   C CB  . ASP A 51  ? 1.3036 1.3856 1.2344 0.2222  0.0058  -0.0050 352 ASP A CB  
391   C CG  . ASP A 51  ? 1.3722 1.4475 1.2858 0.2483  0.0066  -0.0051 352 ASP A CG  
392   O OD1 . ASP A 51  ? 1.3935 1.4482 1.2944 0.2543  0.0024  -0.0042 352 ASP A OD1 
393   O OD2 . ASP A 51  ? 1.3943 1.4837 1.3055 0.2636  0.0116  -0.0061 352 ASP A OD2 
394   N N   . VAL A 52  ? 1.1419 1.1369 1.0186 0.2239  0.0086  -0.0136 353 VAL A N   
395   C CA  . VAL A 52  ? 1.0509 1.0030 0.8985 0.2249  0.0104  -0.0186 353 VAL A CA  
396   C C   . VAL A 52  ? 0.9792 0.8893 0.7976 0.2344  0.0081  -0.0197 353 VAL A C   
397   O O   . VAL A 52  ? 0.8827 0.7877 0.6868 0.2567  0.0093  -0.0192 353 VAL A O   
398   C CB  . VAL A 52  ? 0.9468 0.9056 0.7871 0.2386  0.0163  -0.0211 353 VAL A CB  
399   C CG1 . VAL A 52  ? 0.9950 0.9828 0.8411 0.2619  0.0189  -0.0185 353 VAL A CG1 
400   C CG2 . VAL A 52  ? 0.9355 0.8456 0.7404 0.2427  0.0177  -0.0268 353 VAL A CG2 
401   N N   . ALA A 53  ? 0.9190 0.7992 0.7278 0.2174  0.0049  -0.0211 354 ALA A N   
402   C CA  . ALA A 53  ? 0.7958 0.6333 0.5759 0.2221  0.0029  -0.0218 354 ALA A CA  
403   C C   . ALA A 53  ? 0.8059 0.6045 0.5509 0.2353  0.0061  -0.0264 354 ALA A C   
404   O O   . ALA A 53  ? 0.7866 0.5824 0.5276 0.2322  0.0090  -0.0303 354 ALA A O   
405   C CB  . ALA A 53  ? 0.7707 0.5885 0.5501 0.1982  -0.0004 -0.0224 354 ALA A CB  
406   N N   . THR A 54  ? 0.7754 0.5425 0.4931 0.2511  0.0056  -0.0259 355 THR A N   
407   C CA  . THR A 54  ? 0.7881 0.5114 0.4691 0.2549  0.0073  -0.0294 355 THR A CA  
408   C C   . THR A 54  ? 0.7523 0.4349 0.4157 0.2341  0.0062  -0.0340 355 THR A C   
409   O O   . THR A 54  ? 0.7142 0.4066 0.3955 0.2140  0.0034  -0.0327 355 THR A O   
410   C CB  . THR A 54  ? 0.8217 0.5267 0.4801 0.2685  0.0060  -0.0257 355 THR A CB  
411   O OG1 . THR A 54  ? 0.8266 0.5223 0.4863 0.2612  0.0024  -0.0227 355 THR A OG1 
412   C CG2 . THR A 54  ? 0.7654 0.5104 0.4380 0.2888  0.0073  -0.0221 355 THR A CG2 
413   N N   . LYS A 55  ? 0.7495 0.3952 0.3819 0.2323  0.0074  -0.0374 356 LYS A N   
414   C CA  . LYS A 55  ? 0.8280 0.4376 0.4431 0.2104  0.0063  -0.0422 356 LYS A CA  
415   C C   . LYS A 55  ? 0.7006 0.2875 0.3079 0.1977  0.0034  -0.0399 356 LYS A C   
416   O O   . LYS A 55  ? 0.6883 0.2753 0.3059 0.1763  0.0017  -0.0416 356 LYS A O   
417   C CB  . LYS A 55  ? 0.9055 0.4802 0.4875 0.2118  0.0078  -0.0451 356 LYS A CB  
418   C CG  . LYS A 55  ? 0.9223 0.4647 0.4877 0.1878  0.0064  -0.0502 356 LYS A CG  
419   C CD  . LYS A 55  ? 1.1019 0.6116 0.6352 0.1899  0.0076  -0.0528 356 LYS A CD  
420   C CE  . LYS A 55  ? 1.1790 0.6674 0.7027 0.1645  0.0060  -0.0585 356 LYS A CE  
421   N NZ  . LYS A 55  ? 1.2387 0.7254 0.7723 0.1439  0.0034  -0.0581 356 LYS A NZ  
422   N N   . ASP A 56  ? 0.7503 0.3218 0.3407 0.2087  0.0027  -0.0352 357 ASP A N   
423   C CA  . ASP A 56  ? 0.8160 0.3655 0.3973 0.1970  0.0005  -0.0325 357 ASP A CA  
424   C C   . ASP A 56  ? 0.7925 0.3731 0.4053 0.1934  -0.0016 -0.0297 357 ASP A C   
425   O O   . ASP A 56  ? 0.8437 0.4088 0.4521 0.1811  -0.0034 -0.0277 357 ASP A O   
426   C CB  . ASP A 56  ? 0.9563 0.4823 0.5102 0.2110  0.0004  -0.0281 357 ASP A CB  
427   C CG  . ASP A 56  ? 1.1157 0.6746 0.6824 0.2366  0.0004  -0.0243 357 ASP A CG  
428   O OD1 . ASP A 56  ? 1.2344 0.7856 0.7885 0.2473  -0.0008 -0.0202 357 ASP A OD1 
429   O OD2 . ASP A 56  ? 1.2120 0.8059 0.8010 0.2453  0.0018  -0.0255 357 ASP A OD2 
430   N N   . GLN A 57  ? 0.6788 0.3076 0.3252 0.2006  -0.0016 -0.0285 358 GLN A N   
431   C CA  . GLN A 57  ? 0.7176 0.3876 0.4005 0.1890  -0.0043 -0.0243 358 GLN A CA  
432   C C   . GLN A 57  ? 0.7121 0.4000 0.4166 0.1643  -0.0047 -0.0267 358 GLN A C   
433   O O   . GLN A 57  ? 0.6673 0.3663 0.3877 0.1476  -0.0069 -0.0247 358 GLN A O   
434   C CB  . GLN A 57  ? 0.7155 0.4320 0.4248 0.2067  -0.0044 -0.0207 358 GLN A CB  
435   C CG  . GLN A 57  ? 0.8604 0.5702 0.5564 0.2296  -0.0056 -0.0168 358 GLN A CG  
436   C CD  . GLN A 57  ? 0.8620 0.6147 0.5779 0.2504  -0.0049 -0.0147 358 GLN A CD  
437   O OE1 . GLN A 57  ? 0.8410 0.6273 0.5800 0.2471  -0.0029 -0.0159 358 GLN A OE1 
438   N NE2 . GLN A 57  ? 0.8515 0.6103 0.5610 0.2651  -0.0064 -0.0109 358 GLN A NE2 
439   N N   . LEU A 58  ? 0.7086 0.3993 0.4127 0.1625  -0.0027 -0.0311 359 LEU A N   
440   C CA  . LEU A 58  ? 0.6663 0.3771 0.3915 0.1416  -0.0035 -0.0332 359 LEU A CA  
441   C C   . LEU A 58  ? 0.6280 0.3039 0.3324 0.1223  -0.0041 -0.0376 359 LEU A C   
442   O O   . LEU A 58  ? 0.5831 0.2707 0.3030 0.1025  -0.0059 -0.0375 359 LEU A O   
443   C CB  . LEU A 58  ? 0.6058 0.3414 0.3432 0.1483  -0.0012 -0.0353 359 LEU A CB  
444   C CG  . LEU A 58  ? 0.6559 0.4145 0.4149 0.1295  -0.0021 -0.0370 359 LEU A CG  
445   C CD1 . LEU A 58  ? 0.5900 0.3812 0.3799 0.1189  -0.0044 -0.0324 359 LEU A CD1 
446   C CD2 . LEU A 58  ? 0.5878 0.3665 0.3541 0.1374  0.0007  -0.0389 359 LEU A CD2 
447   N N   . PHE A 59  ? 0.6796 0.3134 0.3487 0.1274  -0.0026 -0.0417 360 PHE A N   
448   C CA  . PHE A 59  ? 0.7233 0.3264 0.3732 0.1066  -0.0034 -0.0466 360 PHE A CA  
449   C C   . PHE A 59  ? 0.6889 0.2839 0.3404 0.0885  -0.0051 -0.0442 360 PHE A C   
450   O O   . PHE A 59  ? 0.7092 0.3122 0.3706 0.0667  -0.0065 -0.0465 360 PHE A O   
451   C CB  . PHE A 59  ? 0.7170 0.2694 0.3235 0.1146  -0.0016 -0.0513 360 PHE A CB  
452   C CG  . PHE A 59  ? 0.8202 0.3429 0.4070 0.0913  -0.0026 -0.0568 360 PHE A CG  
453   C CD1 . PHE A 59  ? 0.8477 0.3838 0.4423 0.0806  -0.0035 -0.0619 360 PHE A CD1 
454   C CD2 . PHE A 59  ? 0.7886 0.2757 0.3523 0.0784  -0.0030 -0.0562 360 PHE A CD2 
455   C CE1 . PHE A 59  ? 0.9168 0.4300 0.4951 0.0581  -0.0051 -0.0673 360 PHE A CE1 
456   C CE2 . PHE A 59  ? 0.8600 0.3304 0.4119 0.0542  -0.0040 -0.0598 360 PHE A CE2 
457   C CZ  . PHE A 59  ? 0.9908 0.4730 0.5492 0.0442  -0.0053 -0.0660 360 PHE A CZ  
458   N N   . PRO A 60  ? 0.7469 0.3273 0.3886 0.0963  -0.0051 -0.0397 361 PRO A N   
459   C CA  . PRO A 60  ? 0.6495 0.2246 0.2937 0.0780  -0.0062 -0.0373 361 PRO A CA  
460   C C   . PRO A 60  ? 0.6386 0.2592 0.3218 0.0638  -0.0079 -0.0357 361 PRO A C   
461   O O   . PRO A 60  ? 0.6718 0.2909 0.3580 0.0429  -0.0084 -0.0366 361 PRO A O   
462   C CB  . PRO A 60  ? 0.7253 0.2870 0.3580 0.0945  -0.0062 -0.0319 361 PRO A CB  
463   C CG  . PRO A 60  ? 0.7888 0.3275 0.3967 0.1182  -0.0046 -0.0333 361 PRO A CG  
464   C CD  . PRO A 60  ? 0.7912 0.3595 0.4181 0.1222  -0.0041 -0.0366 361 PRO A CD  
465   N N   . LEU A 61  ? 0.6178 0.2788 0.3302 0.0745  -0.0086 -0.0333 362 LEU A N   
466   C CA  . LEU A 61  ? 0.6215 0.3226 0.3681 0.0621  -0.0101 -0.0318 362 LEU A CA  
467   C C   . LEU A 61  ? 0.6869 0.3960 0.4398 0.0470  -0.0104 -0.0366 362 LEU A C   
468   O O   . LEU A 61  ? 0.6007 0.3254 0.3688 0.0302  -0.0116 -0.0368 362 LEU A O   
469   C CB  . LEU A 61  ? 0.5382 0.2771 0.3112 0.0763  -0.0105 -0.0281 362 LEU A CB  
470   C CG  . LEU A 61  ? 0.6335 0.3701 0.4028 0.0916  -0.0111 -0.0233 362 LEU A CG  
471   C CD1 . LEU A 61  ? 0.5454 0.3203 0.3394 0.1049  -0.0115 -0.0204 362 LEU A CD1 
472   C CD2 . LEU A 61  ? 0.6440 0.3777 0.4165 0.0801  -0.0125 -0.0202 362 LEU A CD2 
473   N N   . ALA A 62  ? 0.6365 0.3362 0.3774 0.0538  -0.0095 -0.0407 363 ALA A N   
474   C CA  . ALA A 62  ? 0.6601 0.3661 0.4042 0.0405  -0.0104 -0.0456 363 ALA A CA  
475   C C   . ALA A 62  ? 0.6928 0.3727 0.4189 0.0204  -0.0112 -0.0491 363 ALA A C   
476   O O   . ALA A 62  ? 0.5850 0.2831 0.3257 0.0034  -0.0129 -0.0508 363 ALA A O   
477   C CB  . ALA A 62  ? 0.6057 0.3021 0.3358 0.0531  -0.0090 -0.0493 363 ALA A CB  
478   N N   . LYS A 63  ? 0.6664 0.3035 0.3597 0.0222  -0.0100 -0.0503 364 LYS A N   
479   C CA  . LYS A 63  ? 0.7156 0.3244 0.3885 0.0016  -0.0102 -0.0533 364 LYS A CA  
480   C C   . LYS A 63  ? 0.7330 0.3639 0.4272 -0.0139 -0.0109 -0.0501 364 LYS A C   
481   O O   . LYS A 63  ? 0.7432 0.3830 0.4433 -0.0341 -0.0121 -0.0530 364 LYS A O   
482   C CB  . LYS A 63  ? 0.7772 0.3349 0.4109 0.0084  -0.0083 -0.0534 364 LYS A CB  
483   C CG  . LYS A 63  ? 0.9810 0.5027 0.5875 -0.0140 -0.0081 -0.0571 364 LYS A CG  
484   C CD  . LYS A 63  ? 1.0748 0.5473 0.6435 -0.0071 -0.0058 -0.0551 364 LYS A CD  
485   C CE  . LYS A 63  ? 1.0526 0.5047 0.6036 -0.0312 -0.0050 -0.0552 364 LYS A CE  
486   N NZ  . LYS A 63  ? 0.9632 0.4378 0.5347 -0.0535 -0.0055 -0.0550 364 LYS A NZ  
487   N N   . GLU A 64  ? 0.6980 0.3401 0.4041 -0.0041 -0.0103 -0.0441 365 GLU A N   
488   C CA  . GLU A 64  ? 0.7370 0.4000 0.4625 -0.0163 -0.0106 -0.0408 365 GLU A CA  
489   C C   . GLU A 64  ? 0.6353 0.3393 0.3914 -0.0266 -0.0123 -0.0423 365 GLU A C   
490   O O   . GLU A 64  ? 0.6058 0.3189 0.3686 -0.0448 -0.0126 -0.0434 365 GLU A O   
491   C CB  . GLU A 64  ? 0.7617 0.4345 0.4971 -0.0010 -0.0103 -0.0345 365 GLU A CB  
492   C CG  . GLU A 64  ? 0.9640 0.6636 0.7229 -0.0101 -0.0107 -0.0309 365 GLU A CG  
493   C CD  . GLU A 64  ? 1.1817 0.8954 0.9526 0.0058  -0.0113 -0.0254 365 GLU A CD  
494   O OE1 . GLU A 64  ? 1.2248 0.9334 0.9934 0.0027  -0.0109 -0.0218 365 GLU A OE1 
495   O OE2 . GLU A 64  ? 1.2138 0.9446 0.9962 0.0208  -0.0123 -0.0247 365 GLU A OE2 
496   N N   . PHE A 65  ? 0.5211 0.2507 0.2956 -0.0148 -0.0133 -0.0421 366 PHE A N   
497   C CA  . PHE A 65  ? 0.5288 0.2952 0.3301 -0.0225 -0.0150 -0.0430 366 PHE A CA  
498   C C   . PHE A 65  ? 0.5712 0.3333 0.3646 -0.0376 -0.0164 -0.0490 366 PHE A C   
499   O O   . PHE A 65  ? 0.5347 0.3180 0.3426 -0.0516 -0.0177 -0.0501 366 PHE A O   
500   C CB  . PHE A 65  ? 0.5370 0.3282 0.3562 -0.0073 -0.0155 -0.0413 366 PHE A CB  
501   C CG  . PHE A 65  ? 0.5895 0.4115 0.4299 -0.0139 -0.0172 -0.0427 366 PHE A CG  
502   C CD1 . PHE A 65  ? 0.5221 0.3701 0.3844 -0.0205 -0.0180 -0.0401 366 PHE A CD1 
503   C CD2 . PHE A 65  ? 0.5410 0.3645 0.3773 -0.0132 -0.0181 -0.0468 366 PHE A CD2 
504   C CE1 . PHE A 65  ? 0.5377 0.4125 0.4175 -0.0252 -0.0197 -0.0412 366 PHE A CE1 
505   C CE2 . PHE A 65  ? 0.5765 0.4277 0.4307 -0.0185 -0.0200 -0.0478 366 PHE A CE2 
506   C CZ  . PHE A 65  ? 0.4957 0.3723 0.3715 -0.0241 -0.0209 -0.0450 366 PHE A CZ  
507   N N   . ILE A 66  ? 0.5876 0.3239 0.3580 -0.0342 -0.0164 -0.0532 367 ILE A N   
508   C CA  . ILE A 66  ? 0.6850 0.4167 0.4464 -0.0493 -0.0183 -0.0594 367 ILE A CA  
509   C C   . ILE A 66  ? 0.6505 0.3698 0.4023 -0.0704 -0.0182 -0.0608 367 ILE A C   
510   O O   . ILE A 66  ? 0.6050 0.3455 0.3687 -0.0865 -0.0202 -0.0634 367 ILE A O   
511   C CB  . ILE A 66  ? 0.6710 0.3718 0.4048 -0.0416 -0.0180 -0.0639 367 ILE A CB  
512   C CG1 . ILE A 66  ? 0.6585 0.3745 0.4024 -0.0207 -0.0173 -0.0623 367 ILE A CG1 
513   C CG2 . ILE A 66  ? 0.6718 0.3673 0.3949 -0.0587 -0.0207 -0.0708 367 ILE A CG2 
514   C CD1 . ILE A 66  ? 0.6668 0.4224 0.4377 -0.0219 -0.0194 -0.0624 367 ILE A CD1 
515   N N   . ASP A 67  ? 0.6723 0.3584 0.4024 -0.0703 -0.0158 -0.0588 368 ASP A N   
516   C CA  . ASP A 67  ? 0.7326 0.4068 0.4537 -0.0902 -0.0146 -0.0588 368 ASP A CA  
517   C C   . ASP A 67  ? 0.6546 0.3706 0.4073 -0.0995 -0.0151 -0.0563 368 ASP A C   
518   O O   . ASP A 67  ? 0.6396 0.3673 0.3964 -0.1191 -0.0158 -0.0592 368 ASP A O   
519   C CB  . ASP A 67  ? 0.7877 0.4258 0.4859 -0.0837 -0.0116 -0.0548 368 ASP A CB  
520   C CG  . ASP A 67  ? 0.8696 0.4577 0.5283 -0.0803 -0.0107 -0.0581 368 ASP A CG  
521   O OD1 . ASP A 67  ? 0.8626 0.4433 0.5112 -0.0841 -0.0123 -0.0639 368 ASP A OD1 
522   O OD2 . ASP A 67  ? 0.8958 0.4507 0.5320 -0.0732 -0.0083 -0.0549 368 ASP A OD2 
523   N N   . GLN A 68  ? 0.5896 0.3290 0.3645 -0.0853 -0.0147 -0.0511 369 GLN A N   
524   C CA  . GLN A 68  ? 0.5346 0.3112 0.3376 -0.0912 -0.0148 -0.0485 369 GLN A CA  
525   C C   . GLN A 68  ? 0.5947 0.4040 0.4166 -0.0979 -0.0178 -0.0522 369 GLN A C   
526   O O   . GLN A 68  ? 0.6155 0.4460 0.4490 -0.1125 -0.0181 -0.0533 369 GLN A O   
527   C CB  . GLN A 68  ? 0.5471 0.3388 0.3669 -0.0737 -0.0143 -0.0429 369 GLN A CB  
528   C CG  . GLN A 68  ? 0.6518 0.4788 0.4984 -0.0775 -0.0144 -0.0403 369 GLN A CG  
529   C CD  . GLN A 68  ? 0.7753 0.6188 0.6388 -0.0608 -0.0147 -0.0356 369 GLN A CD  
530   O OE1 . GLN A 68  ? 0.7437 0.6173 0.6293 -0.0584 -0.0160 -0.0349 369 GLN A OE1 
531   N NE2 . GLN A 68  ? 0.8229 0.6464 0.6750 -0.0491 -0.0138 -0.0326 369 GLN A NE2 
532   N N   . TYR A 69  ? 0.5449 0.3600 0.3699 -0.0868 -0.0198 -0.0540 370 TYR A N   
533   C CA  . TYR A 69  ? 0.5963 0.4397 0.4361 -0.0918 -0.0230 -0.0575 370 TYR A CA  
534   C C   . TYR A 69  ? 0.5573 0.3942 0.3846 -0.1122 -0.0246 -0.0633 370 TYR A C   
535   O O   . TYR A 69  ? 0.5426 0.4089 0.3857 -0.1234 -0.0265 -0.0649 370 TYR A O   
536   C CB  . TYR A 69  ? 0.6181 0.4622 0.4574 -0.0772 -0.0244 -0.0587 370 TYR A CB  
537   C CG  . TYR A 69  ? 0.5421 0.4098 0.3909 -0.0832 -0.0280 -0.0627 370 TYR A CG  
538   C CD1 . TYR A 69  ? 0.4967 0.4012 0.3710 -0.0824 -0.0296 -0.0606 370 TYR A CD1 
539   C CD2 . TYR A 69  ? 0.5778 0.4301 0.4083 -0.0894 -0.0302 -0.0687 370 TYR A CD2 
540   C CE1 . TYR A 69  ? 0.5183 0.4449 0.4004 -0.0865 -0.0333 -0.0640 370 TYR A CE1 
541   C CE2 . TYR A 69  ? 0.6046 0.4798 0.4434 -0.0946 -0.0342 -0.0724 370 TYR A CE2 
542   C CZ  . TYR A 69  ? 0.5828 0.4958 0.4478 -0.0927 -0.0357 -0.0699 370 TYR A CZ  
543   O OH  . TYR A 69  ? 0.5704 0.5067 0.4428 -0.0964 -0.0400 -0.0733 370 TYR A OH  
544   N N   . TYR A 70  ? 0.5050 0.3035 0.3030 -0.1173 -0.0239 -0.0665 371 TYR A N   
545   C CA  . TYR A 70  ? 0.5884 0.3809 0.3736 -0.1385 -0.0259 -0.0726 371 TYR A CA  
546   C C   . TYR A 70  ? 0.5893 0.3873 0.3771 -0.1573 -0.0240 -0.0715 371 TYR A C   
547   O O   . TYR A 70  ? 0.6617 0.4770 0.4537 -0.1759 -0.0260 -0.0756 371 TYR A O   
548   C CB  . TYR A 70  ? 0.6741 0.4214 0.4244 -0.1395 -0.0259 -0.0770 371 TYR A CB  
549   C CG  . TYR A 70  ? 0.6629 0.4172 0.4133 -0.1313 -0.0293 -0.0812 371 TYR A CG  
550   C CD1 . TYR A 70  ? 0.6069 0.3565 0.3577 -0.1086 -0.0283 -0.0788 371 TYR A CD1 
551   C CD2 . TYR A 70  ? 0.6282 0.3983 0.3803 -0.1461 -0.0336 -0.0871 371 TYR A CD2 
552   C CE1 . TYR A 70  ? 0.6176 0.3745 0.3681 -0.1010 -0.0308 -0.0823 371 TYR A CE1 
553   C CE2 . TYR A 70  ? 0.6093 0.3865 0.3609 -0.1381 -0.0369 -0.0907 371 TYR A CE2 
554   C CZ  . TYR A 70  ? 0.6117 0.3812 0.3620 -0.1156 -0.0351 -0.0882 371 TYR A CZ  
555   O OH  . TYR A 70  ? 0.6224 0.3986 0.3712 -0.1077 -0.0377 -0.0915 371 TYR A OH  
556   N N   . SER A 71  ? 0.6466 0.4326 0.4325 -0.1528 -0.0200 -0.0661 372 SER A N   
557   C CA  . SER A 71  ? 0.7249 0.5226 0.5177 -0.1685 -0.0175 -0.0641 372 SER A CA  
558   C C   . SER A 71  ? 0.6369 0.4862 0.4637 -0.1693 -0.0190 -0.0632 372 SER A C   
559   O O   . SER A 71  ? 0.6466 0.5171 0.4813 -0.1871 -0.0188 -0.0651 372 SER A O   
560   C CB  . SER A 71  ? 0.7814 0.5576 0.5661 -0.1603 -0.0132 -0.0580 372 SER A CB  
561   O OG  . SER A 71  ? 0.8961 0.6225 0.6464 -0.1599 -0.0116 -0.0586 372 SER A OG  
562   N N   . SER A 72  ? 0.5959 0.4659 0.4422 -0.1501 -0.0203 -0.0604 373 SER A N   
563   C CA  . SER A 72  ? 0.5671 0.4819 0.4430 -0.1480 -0.0215 -0.0590 373 SER A CA  
564   C C   . SER A 72  ? 0.6279 0.5695 0.5121 -0.1599 -0.0254 -0.0643 373 SER A C   
565   O O   . SER A 72  ? 0.6035 0.5812 0.5079 -0.1648 -0.0257 -0.0640 373 SER A O   
566   C CB  . SER A 72  ? 0.5278 0.4539 0.4183 -0.1260 -0.0224 -0.0553 373 SER A CB  
567   O OG  . SER A 72  ? 0.6032 0.5335 0.4939 -0.1193 -0.0259 -0.0584 373 SER A OG  
568   N N   . ILE A 73  ? 0.5674 0.4932 0.4360 -0.1641 -0.0284 -0.0694 374 ILE A N   
569   C CA  . ILE A 73  ? 0.5517 0.5028 0.4267 -0.1758 -0.0330 -0.0749 374 ILE A CA  
570   C C   . ILE A 73  ? 0.5412 0.4763 0.3970 -0.2007 -0.0331 -0.0800 374 ILE A C   
571   O O   . ILE A 73  ? 0.6208 0.5659 0.4736 -0.2119 -0.0374 -0.0857 374 ILE A O   
572   C CB  . ILE A 73  ? 0.5971 0.5484 0.4703 -0.1635 -0.0373 -0.0776 374 ILE A CB  
573   C CG1 . ILE A 73  ? 0.5399 0.4455 0.3832 -0.1620 -0.0368 -0.0802 374 ILE A CG1 
574   C CG2 . ILE A 73  ? 0.5943 0.5628 0.4864 -0.1413 -0.0369 -0.0724 374 ILE A CG2 
575   C CD1 . ILE A 73  ? 0.5421 0.4467 0.3800 -0.1533 -0.0408 -0.0840 374 ILE A CD1 
576   N N   . LYS A 74  ? 0.6027 0.5133 0.4448 -0.2103 -0.0283 -0.0778 375 LYS A N   
577   C CA  . LYS A 74  ? 0.7179 0.6168 0.5455 -0.2301 -0.0261 -0.0790 375 LYS A CA  
578   C C   . LYS A 74  ? 0.6990 0.5660 0.5015 -0.2325 -0.0282 -0.0830 375 LYS A C   
579   O O   . LYS A 74  ? 0.7112 0.5838 0.5091 -0.2465 -0.0290 -0.0854 375 LYS A O   
580   C CB  . LYS A 74  ? 0.7188 0.6657 0.5697 -0.2420 -0.0267 -0.0794 375 LYS A CB  
581   C CG  . LYS A 74  ? 0.6685 0.6545 0.5474 -0.2365 -0.0255 -0.0763 375 LYS A CG  
582   C CD  . LYS A 74  ? 0.7784 0.7500 0.6522 -0.2408 -0.0189 -0.0714 375 LYS A CD  
583   C CE  . LYS A 74  ? 0.7143 0.7167 0.6125 -0.2314 -0.0179 -0.0682 375 LYS A CE  
584   N NZ  . LYS A 74  ? 0.5821 0.5552 0.4703 -0.2230 -0.0127 -0.0624 375 LYS A NZ  
585   N N   . ARG A 75  ? 0.6618 0.4951 0.4472 -0.2181 -0.0289 -0.0837 376 ARG A N   
586   C CA  . ARG A 75  ? 0.7017 0.5034 0.4624 -0.2166 -0.0307 -0.0875 376 ARG A CA  
587   C C   . ARG A 75  ? 0.7665 0.5162 0.4977 -0.2075 -0.0268 -0.0852 376 ARG A C   
588   O O   . ARG A 75  ? 0.6718 0.3939 0.3841 -0.1966 -0.0280 -0.0876 376 ARG A O   
589   C CB  . ARG A 75  ? 0.6800 0.4970 0.4488 -0.2046 -0.0361 -0.0917 376 ARG A CB  
590   C CG  . ARG A 75  ? 0.7056 0.5706 0.4989 -0.2121 -0.0407 -0.0942 376 ARG A CG  
591   C CD  . ARG A 75  ? 0.9196 0.7827 0.7028 -0.2285 -0.0420 -0.0974 376 ARG A CD  
592   N NE  . ARG A 75  ? 1.0533 0.9643 0.8603 -0.2342 -0.0467 -0.0997 376 ARG A NE  
593   C CZ  . ARG A 75  ? 1.0982 1.0462 0.9269 -0.2435 -0.0457 -0.0975 376 ARG A CZ  
594   N NH1 . ARG A 75  ? 1.0000 0.9911 0.8491 -0.2458 -0.0501 -0.0994 376 ARG A NH1 
595   N NH2 . ARG A 75  ? 1.1708 1.1127 0.9997 -0.2495 -0.0400 -0.0932 376 ARG A NH2 
596   N N   . PHE A 76  ? 0.7374 0.4737 0.4638 -0.2104 -0.0220 -0.0802 377 PHE A N   
597   C CA  . PHE A 76  ? 0.8499 0.5380 0.5480 -0.1999 -0.0185 -0.0772 377 PHE A CA  
598   C C   . PHE A 76  ? 0.8880 0.5414 0.5558 -0.2074 -0.0176 -0.0791 377 PHE A C   
599   O O   . PHE A 76  ? 0.8777 0.5356 0.5418 -0.2267 -0.0166 -0.0795 377 PHE A O   
600   C CB  . PHE A 76  ? 0.8970 0.5788 0.5951 -0.2022 -0.0137 -0.0712 377 PHE A CB  
601   C CG  . PHE A 76  ? 0.9976 0.6325 0.6677 -0.1884 -0.0106 -0.0676 377 PHE A CG  
602   C CD1 . PHE A 76  ? 1.0363 0.6645 0.7095 -0.1679 -0.0108 -0.0656 377 PHE A CD1 
603   C CD2 . PHE A 76  ? 1.0475 0.6452 0.6869 -0.1950 -0.0077 -0.0663 377 PHE A CD2 
604   C CE1 . PHE A 76  ? 1.0308 0.6190 0.6789 -0.1530 -0.0083 -0.0620 377 PHE A CE1 
605   C CE2 . PHE A 76  ? 1.0734 0.6292 0.6861 -0.1804 -0.0052 -0.0627 377 PHE A CE2 
606   C CZ  . PHE A 76  ? 1.0703 0.6227 0.6882 -0.1587 -0.0056 -0.0605 377 PHE A CZ  
607   N N   . GLY A 77  ? 0.8949 0.5140 0.5404 -0.1918 -0.0179 -0.0802 378 GLY A N   
608   C CA  . GLY A 77  ? 0.8980 0.4810 0.5124 -0.1961 -0.0172 -0.0820 378 GLY A CA  
609   C C   . GLY A 77  ? 0.8791 0.4764 0.4961 -0.2052 -0.0216 -0.0882 378 GLY A C   
610   O O   . GLY A 77  ? 0.9090 0.4765 0.4996 -0.2096 -0.0214 -0.0902 378 GLY A O   
611   N N   . SER A 78  ? 0.7858 0.4276 0.4328 -0.2075 -0.0256 -0.0910 379 SER A N   
612   C CA  . SER A 78  ? 0.7116 0.3714 0.3633 -0.2149 -0.0304 -0.0968 379 SER A CA  
613   C C   . SER A 78  ? 0.8736 0.5042 0.5038 -0.1997 -0.0318 -0.1002 379 SER A C   
614   O O   . SER A 78  ? 0.8543 0.4589 0.4719 -0.1808 -0.0293 -0.0981 379 SER A O   
615   C CB  . SER A 78  ? 0.7378 0.4500 0.4250 -0.2147 -0.0345 -0.0984 379 SER A CB  
616   O OG  . SER A 78  ? 0.6991 0.4141 0.3942 -0.1942 -0.0351 -0.0977 379 SER A OG  
617   N N   . LYS A 79  ? 0.7430 0.3802 0.3697 -0.2074 -0.0357 -0.1055 380 LYS A N   
618   C CA  . LYS A 79  ? 0.8820 0.4969 0.4905 -0.1932 -0.0373 -0.1093 380 LYS A CA  
619   C C   . LYS A 79  ? 0.8085 0.4357 0.4302 -0.1710 -0.0378 -0.1089 380 LYS A C   
620   O O   . LYS A 79  ? 0.8794 0.4773 0.4837 -0.1523 -0.0349 -0.1077 380 LYS A O   
621   C CB  . LYS A 79  ? 0.9108 0.5410 0.5199 -0.2057 -0.0425 -0.1153 380 LYS A CB  
622   C CG  . LYS A 79  ? 0.9581 0.5599 0.5428 -0.1945 -0.0436 -0.1195 380 LYS A CG  
623   C CD  . LYS A 79  ? 1.0380 0.6535 0.6218 -0.2092 -0.0489 -0.1254 380 LYS A CD  
624   C CE  . LYS A 79  ? 1.0613 0.6719 0.6376 -0.2338 -0.0483 -0.1251 380 LYS A CE  
625   N NZ  . LYS A 79  ? 1.0445 0.6014 0.5836 -0.2349 -0.0438 -0.1235 380 LYS A NZ  
626   N N   . ALA A 80  ? 0.7820 0.4533 0.4342 -0.1722 -0.0410 -0.1093 381 ALA A N   
627   C CA  . ALA A 80  ? 0.7757 0.4601 0.4396 -0.1527 -0.0415 -0.1089 381 ALA A CA  
628   C C   . ALA A 80  ? 0.8020 0.4661 0.4612 -0.1384 -0.0366 -0.1038 381 ALA A C   
629   O O   . ALA A 80  ? 0.7797 0.4328 0.4328 -0.1180 -0.0351 -0.1034 381 ALA A O   
630   C CB  . ALA A 80  ? 0.7247 0.4596 0.4209 -0.1582 -0.0458 -0.1093 381 ALA A CB  
631   N N   . HIS A 81  ? 0.8126 0.4736 0.4751 -0.1481 -0.0339 -0.0996 382 HIS A N   
632   C CA  . HIS A 81  ? 0.7823 0.4238 0.4397 -0.1350 -0.0296 -0.0946 382 HIS A CA  
633   C C   . HIS A 81  ? 0.8203 0.4170 0.4468 -0.1196 -0.0264 -0.0939 382 HIS A C   
634   O O   . HIS A 81  ? 0.7626 0.3498 0.3859 -0.0983 -0.0245 -0.0921 382 HIS A O   
635   C CB  . HIS A 81  ? 0.7803 0.4246 0.4435 -0.1502 -0.0271 -0.0903 382 HIS A CB  
636   C CG  . HIS A 81  ? 0.8390 0.4660 0.4982 -0.1381 -0.0233 -0.0848 382 HIS A CG  
637   N ND1 . HIS A 81  ? 0.8873 0.5104 0.5469 -0.1487 -0.0202 -0.0803 382 HIS A ND1 
638   C CD2 . HIS A 81  ? 0.8620 0.4816 0.5214 -0.1140 -0.0214 -0.0814 382 HIS A CD2 
639   C CE1 . HIS A 81  ? 0.8630 0.4705 0.5183 -0.1334 -0.0176 -0.0760 382 HIS A CE1 
640   N NE2 . HIS A 81  ? 0.8633 0.4728 0.5217 -0.1111 -0.0182 -0.0756 382 HIS A NE2 
641   N N   . MET A 82  ? 0.7667 0.3365 0.3698 -0.1294 -0.0257 -0.0951 383 MET A N   
642   C CA  . MET A 82  ? 0.7803 0.3065 0.3519 -0.1149 -0.0226 -0.0939 383 MET A CA  
643   C C   . MET A 82  ? 0.8599 0.3845 0.4265 -0.0964 -0.0236 -0.0975 383 MET A C   
644   O O   . MET A 82  ? 0.9443 0.4477 0.4971 -0.0747 -0.0206 -0.0953 383 MET A O   
645   C CB  . MET A 82  ? 0.9201 0.4175 0.4660 -0.1314 -0.0218 -0.0945 383 MET A CB  
646   C CG  . MET A 82  ? 0.9380 0.4355 0.4857 -0.1496 -0.0198 -0.0906 383 MET A CG  
647   S SD  . MET A 82  ? 1.0481 0.5368 0.5986 -0.1338 -0.0158 -0.0833 383 MET A SD  
648   C CE  . MET A 82  ? 1.1577 0.5939 0.6683 -0.1127 -0.0127 -0.0811 383 MET A CE  
649   N N   . GLU A 83  ? 0.8365 0.3849 0.4141 -0.1040 -0.0277 -0.1028 384 GLU A N   
650   C CA  . GLU A 83  ? 0.8537 0.4044 0.4281 -0.0867 -0.0284 -0.1061 384 GLU A CA  
651   C C   . GLU A 83  ? 0.7927 0.3596 0.3828 -0.0664 -0.0266 -0.1033 384 GLU A C   
652   O O   . GLU A 83  ? 0.8238 0.3770 0.4031 -0.0444 -0.0236 -0.1025 384 GLU A O   
653   C CB  . GLU A 83  ? 0.9335 0.5110 0.5189 -0.0993 -0.0336 -0.1118 384 GLU A CB  
654   C CG  . GLU A 83  ? 1.0794 0.6390 0.6460 -0.1165 -0.0355 -0.1153 384 GLU A CG  
655   C CD  . GLU A 83  ? 1.1851 0.7729 0.7628 -0.1270 -0.0412 -0.1210 384 GLU A CD  
656   O OE1 . GLU A 83  ? 1.2043 0.8206 0.7997 -0.1176 -0.0434 -0.1221 384 GLU A OE1 
657   O OE2 . GLU A 83  ? 1.2522 0.8337 0.8200 -0.1444 -0.0437 -0.1241 384 GLU A OE2 
658   N N   . ARG A 84  ? 0.7917 0.3904 0.4090 -0.0729 -0.0280 -0.1010 385 ARG A N   
659   C CA  . ARG A 84  ? 0.7827 0.4119 0.4286 -0.0532 -0.0254 -0.0937 385 ARG A CA  
660   C C   . ARG A 84  ? 0.7700 0.3718 0.4013 -0.0353 -0.0208 -0.0895 385 ARG A C   
661   O O   . ARG A 84  ? 0.8125 0.4221 0.4494 -0.0136 -0.0183 -0.0866 385 ARG A O   
662   C CB  . ARG A 84  ? 0.7474 0.4174 0.4283 -0.0634 -0.0269 -0.0892 385 ARG A CB  
663   C CG  . ARG A 84  ? 0.6723 0.3764 0.3834 -0.0460 -0.0251 -0.0824 385 ARG A CG  
664   C CD  . ARG A 84  ? 0.6576 0.3889 0.3828 -0.0384 -0.0267 -0.0835 385 ARG A CD  
665   N NE  . ARG A 84  ? 0.6343 0.3937 0.3854 -0.0232 -0.0244 -0.0767 385 ARG A NE  
666   C CZ  . ARG A 84  ? 0.7158 0.4762 0.4664 -0.0043 -0.0214 -0.0747 385 ARG A CZ  
667   N NH1 . ARG A 84  ? 0.8098 0.5452 0.5354 0.0040  -0.0201 -0.0789 385 ARG A NH1 
668   N NH2 . ARG A 84  ? 0.5777 0.3649 0.3525 0.0060  -0.0195 -0.0685 385 ARG A NH2 
669   N N   . LEU A 85  ? 0.7726 0.3427 0.3841 -0.0441 -0.0197 -0.0891 386 LEU A N   
670   C CA  . LEU A 85  ? 0.7626 0.3020 0.3550 -0.0265 -0.0158 -0.0855 386 LEU A CA  
671   C C   . LEU A 85  ? 0.8009 0.3173 0.3704 -0.0075 -0.0138 -0.0874 386 LEU A C   
672   O O   . LEU A 85  ? 0.7969 0.3147 0.3673 0.0161  -0.0111 -0.0848 386 LEU A O   
673   C CB  . LEU A 85  ? 0.8402 0.3517 0.4153 -0.0404 -0.0147 -0.0828 386 LEU A CB  
674   C CG  . LEU A 85  ? 0.8245 0.3563 0.4206 -0.0541 -0.0154 -0.0801 386 LEU A CG  
675   C CD1 . LEU A 85  ? 0.9001 0.4058 0.4792 -0.0646 -0.0130 -0.0757 386 LEU A CD1 
676   C CD2 . LEU A 85  ? 0.7121 0.2777 0.3385 -0.0351 -0.0141 -0.0731 386 LEU A CD2 
677   N N   . GLU A 86  ? 0.8514 0.3511 0.4029 -0.0172 -0.0150 -0.0913 387 GLU A N   
678   C CA  . GLU A 86  ? 0.8956 0.3758 0.4263 -0.0003 -0.0131 -0.0927 387 GLU A CA  
679   C C   . GLU A 86  ? 0.8710 0.3782 0.4173 0.0172  -0.0125 -0.0945 387 GLU A C   
680   O O   . GLU A 86  ? 0.9369 0.4374 0.4748 0.0401  -0.0091 -0.0927 387 GLU A O   
681   C CB  . GLU A 86  ? 1.0561 0.5180 0.5676 -0.0168 -0.0153 -0.0973 387 GLU A CB  
682   C CG  . GLU A 86  ? 1.2951 0.7172 0.7775 -0.0248 -0.0139 -0.0950 387 GLU A CG  
683   C CD  . GLU A 86  ? 1.4543 0.8476 0.9141 -0.0005 -0.0099 -0.0906 387 GLU A CD  
684   O OE1 . GLU A 86  ? 1.4483 0.8211 0.8961 -0.0002 -0.0081 -0.0857 387 GLU A OE1 
685   O OE2 . GLU A 86  ? 1.5520 0.9451 1.0065 0.0189  -0.0085 -0.0919 387 GLU A OE2 
686   N N   . GLU A 87  ? 0.7552 0.2945 0.3240 0.0068  -0.0156 -0.0976 388 GLU A N   
687   C CA  . GLU A 87  ? 0.7218 0.2954 0.3119 0.0215  -0.0147 -0.0964 388 GLU A CA  
688   C C   . GLU A 87  ? 0.7427 0.3385 0.3547 0.0408  -0.0110 -0.0884 388 GLU A C   
689   O O   . GLU A 87  ? 0.7401 0.3416 0.3516 0.0617  -0.0075 -0.0871 388 GLU A O   
690   C CB  . GLU A 87  ? 0.7397 0.3528 0.3581 0.0049  -0.0190 -0.0970 388 GLU A CB  
691   C CG  . GLU A 87  ? 0.8229 0.4707 0.4618 0.0165  -0.0184 -0.0956 388 GLU A CG  
692   C CD  . GLU A 87  ? 0.9278 0.6097 0.5899 0.0003  -0.0232 -0.0964 388 GLU A CD  
693   O OE1 . GLU A 87  ? 0.8074 0.4996 0.4826 -0.0160 -0.0260 -0.0953 388 GLU A OE1 
694   O OE2 . GLU A 87  ? 0.9621 0.6604 0.6285 0.0044  -0.0242 -0.0982 388 GLU A OE2 
695   N N   . VAL A 88  ? 0.7517 0.3609 0.3825 0.0336  -0.0117 -0.0833 389 VAL A N   
696   C CA  . VAL A 88  ? 0.7401 0.3705 0.3912 0.0501  -0.0089 -0.0760 389 VAL A CA  
697   C C   . VAL A 88  ? 0.7092 0.3074 0.3334 0.0710  -0.0053 -0.0755 389 VAL A C   
698   O O   . VAL A 88  ? 0.6802 0.2959 0.3143 0.0915  -0.0023 -0.0720 389 VAL A O   
699   C CB  . VAL A 88  ? 0.7159 0.3615 0.3875 0.0376  -0.0105 -0.0712 389 VAL A CB  
700   C CG1 . VAL A 88  ? 0.6343 0.2959 0.3217 0.0544  -0.0082 -0.0642 389 VAL A CG1 
701   C CG2 . VAL A 88  ? 0.6332 0.3163 0.3337 0.0219  -0.0137 -0.0713 389 VAL A CG2 
702   N N   . ASN A 89  ? 0.7414 0.2919 0.3296 0.0664  -0.0053 -0.0793 390 ASN A N   
703   C CA  . ASN A 89  ? 0.8309 0.3506 0.3924 0.0872  -0.0020 -0.0779 390 ASN A CA  
704   C C   . ASN A 89  ? 0.9281 0.4544 0.4848 0.1058  0.0006  -0.0795 390 ASN A C   
705   O O   . ASN A 89  ? 0.8456 0.3775 0.4024 0.1288  0.0038  -0.0754 390 ASN A O   
706   C CB  . ASN A 89  ? 0.9073 0.3867 0.4396 0.0747  -0.0029 -0.0775 390 ASN A CB  
707   C CG  . ASN A 89  ? 1.0974 0.5503 0.6039 0.0949  -0.0001 -0.0742 390 ASN A CG  
708   O OD1 . ASN A 89  ? 1.0069 0.4565 0.5116 0.1091  0.0013  -0.0688 390 ASN A OD1 
709   N ND2 . ASN A 89  ? 1.1703 0.6051 0.6561 0.0969  0.0004  -0.0775 390 ASN A ND2 
710   N N   . LYS A 90  ? 0.8857 0.4133 0.4385 0.0961  -0.0007 -0.0850 391 LYS A N   
711   C CA  . LYS A 90  ? 0.8369 0.3705 0.3843 0.1128  0.0021  -0.0864 391 LYS A CA  
712   C C   . LYS A 90  ? 0.7769 0.3516 0.3516 0.1283  0.0049  -0.0845 391 LYS A C   
713   O O   . LYS A 90  ? 0.8467 0.4312 0.4217 0.1499  0.0091  -0.0818 391 LYS A O   
714   C CB  . LYS A 90  ? 0.9919 0.5184 0.5291 0.0977  -0.0005 -0.0928 391 LYS A CB  
715   C CG  . LYS A 90  ? 1.2480 0.7364 0.7584 0.0808  -0.0032 -0.0950 391 LYS A CG  
716   C CD  . LYS A 90  ? 1.3242 0.7782 0.8062 0.0960  -0.0002 -0.0917 391 LYS A CD  
717   C CE  . LYS A 90  ? 1.2869 0.7018 0.7408 0.0779  -0.0025 -0.0935 391 LYS A CE  
718   N NZ  . LYS A 90  ? 1.2931 0.6750 0.7219 0.0898  -0.0002 -0.0884 391 LYS A NZ  
719   N N   . GLU A 91  ? 0.7362 0.3482 0.3447 0.1138  0.0023  -0.0817 392 GLU A N   
720   C CA  . GLU A 91  ? 0.7569 0.4173 0.4006 0.1230  0.0044  -0.0760 392 GLU A CA  
721   C C   . GLU A 91  ? 0.7755 0.4444 0.4261 0.1422  0.0076  -0.0702 392 GLU A C   
722   O O   . GLU A 91  ? 0.7562 0.4468 0.4155 0.1603  0.0117  -0.0679 392 GLU A O   
723   C CB  . GLU A 91  ? 0.7155 0.4091 0.3918 0.1035  0.0006  -0.0730 392 GLU A CB  
724   C CG  . GLU A 91  ? 0.8014 0.4988 0.4774 0.0871  -0.0028 -0.0779 392 GLU A CG  
725   C CD  . GLU A 91  ? 0.9254 0.6611 0.6356 0.0737  -0.0056 -0.0740 392 GLU A CD  
726   O OE1 . GLU A 91  ? 1.0121 0.7805 0.7469 0.0820  -0.0034 -0.0687 392 GLU A OE1 
727   O OE2 . GLU A 91  ? 1.0253 0.7585 0.7370 0.0548  -0.0100 -0.0764 392 GLU A OE2 
728   N N   . ILE A 92  ? 0.7210 0.3746 0.3681 0.1383  0.0058  -0.0677 393 ILE A N   
729   C CA  . ILE A 92  ? 0.7948 0.4553 0.4467 0.1567  0.0079  -0.0623 393 ILE A CA  
730   C C   . ILE A 92  ? 0.7758 0.4105 0.3976 0.1809  0.0120  -0.0647 393 ILE A C   
731   O O   . ILE A 92  ? 0.7842 0.4430 0.4167 0.2013  0.0154  -0.0613 393 ILE A O   
732   C CB  . ILE A 92  ? 0.7665 0.4101 0.4154 0.1469  0.0050  -0.0596 393 ILE A CB  
733   C CG1 . ILE A 92  ? 0.6887 0.3663 0.3719 0.1271  0.0018  -0.0564 393 ILE A CG1 
734   C CG2 . ILE A 92  ? 0.8012 0.4432 0.4464 0.1680  0.0067  -0.0549 393 ILE A CG2 
735   C CD1 . ILE A 92  ? 0.7196 0.3817 0.4003 0.1135  -0.0009 -0.0544 393 ILE A CD1 
736   N N   . ASP A 93  ? 0.8356 0.4282 0.4242 0.1762  0.0112  -0.0688 394 ASP A N   
737   C CA  . ASP A 93  ? 0.9742 0.5505 0.5407 0.1934  0.0137  -0.0674 394 ASP A CA  
738   C C   . ASP A 93  ? 0.9776 0.5846 0.5563 0.2084  0.0177  -0.0676 394 ASP A C   
739   O O   . ASP A 93  ? 1.0873 0.7016 0.6620 0.2288  0.0206  -0.0640 394 ASP A O   
740   C CB  . ASP A 93  ? 1.0902 0.6225 0.6237 0.1808  0.0118  -0.0714 394 ASP A CB  
741   C CG  . ASP A 93  ? 1.2421 0.7388 0.7541 0.1743  0.0097  -0.0689 394 ASP A CG  
742   O OD1 . ASP A 93  ? 1.2972 0.7680 0.7952 0.1528  0.0070  -0.0722 394 ASP A OD1 
743   O OD2 . ASP A 93  ? 1.3315 0.8281 0.8409 0.1904  0.0108  -0.0635 394 ASP A OD2 
744   N N   . THR A 94  ? 0.8057 0.4317 0.3983 0.1983  0.0178  -0.0717 395 THR A N   
745   C CA  . THR A 94  ? 0.8877 0.5377 0.4871 0.2099  0.0219  -0.0722 395 THR A CA  
746   C C   . THR A 94  ? 0.9196 0.6194 0.5538 0.2163  0.0250  -0.0690 395 THR A C   
747   O O   . THR A 94  ? 0.9074 0.6321 0.5496 0.2287  0.0294  -0.0674 395 THR A O   
748   C CB  . THR A 94  ? 0.9017 0.5377 0.4885 0.1954  0.0203  -0.0787 395 THR A CB  
749   O OG1 . THR A 94  ? 0.9705 0.6160 0.5716 0.1757  0.0168  -0.0817 395 THR A OG1 
750   C CG2 . THR A 94  ? 0.9583 0.5472 0.5108 0.1892  0.0178  -0.0817 395 THR A CG2 
751   N N   . THR A 95  ? 0.8329 0.5537 0.4932 0.2035  0.0219  -0.0652 396 THR A N   
752   C CA  . THR A 95  ? 0.7742 0.5468 0.4733 0.2025  0.0232  -0.0591 396 THR A CA  
753   C C   . THR A 95  ? 0.7087 0.5003 0.4286 0.2041  0.0215  -0.0529 396 THR A C   
754   O O   . THR A 95  ? 0.7640 0.5974 0.5152 0.2023  0.0223  -0.0478 396 THR A O   
755   C CB  . THR A 95  ? 0.6966 0.4870 0.4148 0.1801  0.0201  -0.0593 396 THR A CB  
756   O OG1 . THR A 95  ? 0.6928 0.4747 0.4177 0.1617  0.0146  -0.0586 396 THR A OG1 
757   C CG2 . THR A 95  ? 0.6458 0.4151 0.3418 0.1759  0.0203  -0.0660 396 THR A CG2 
758   N N   . SER A 96  ? 0.6215 0.3824 0.3236 0.2067  0.0192  -0.0531 397 SER A N   
759   C CA  . SER A 96  ? 0.7058 0.4798 0.4240 0.2070  0.0168  -0.0475 397 SER A CA  
760   C C   . SER A 96  ? 0.7063 0.4994 0.4508 0.1837  0.0126  -0.0449 397 SER A C   
761   O O   . SER A 96  ? 0.7015 0.5108 0.4633 0.1820  0.0105  -0.0402 397 SER A O   
762   C CB  . SER A 96  ? 0.7402 0.5520 0.4774 0.2264  0.0199  -0.0426 397 SER A CB  
763   O OG  . SER A 96  ? 0.7795 0.5712 0.4913 0.2510  0.0228  -0.0438 397 SER A OG  
764   N N   . THR A 97  ? 0.6603 0.4524 0.4078 0.1664  0.0111  -0.0480 398 THR A N   
765   C CA  . THR A 97  ? 0.5994 0.4077 0.3693 0.1454  0.0073  -0.0460 398 THR A CA  
766   C C   . THR A 97  ? 0.5932 0.3783 0.3487 0.1286  0.0047  -0.0515 398 THR A C   
767   O O   . THR A 97  ? 0.6148 0.3680 0.3415 0.1322  0.0055  -0.0568 398 THR A O   
768   C CB  . THR A 97  ? 0.5051 0.3590 0.3075 0.1441  0.0086  -0.0416 398 THR A CB  
769   O OG1 . THR A 97  ? 0.5243 0.3928 0.3475 0.1271  0.0049  -0.0388 398 THR A OG1 
770   C CG2 . THR A 97  ? 0.4893 0.3515 0.2905 0.1436  0.0110  -0.0444 398 THR A CG2 
771   N N   . TYR A 98  ? 0.5787 0.3795 0.3531 0.1103  0.0014  -0.0505 399 TYR A N   
772   C CA  . TYR A 98  ? 0.5521 0.3410 0.3179 0.0943  -0.0013 -0.0556 399 TYR A CA  
773   C C   . TYR A 98  ? 0.5049 0.3280 0.2994 0.0825  -0.0033 -0.0530 399 TYR A C   
774   O O   . TYR A 98  ? 0.4865 0.3365 0.3045 0.0845  -0.0027 -0.0475 399 TYR A O   
775   C CB  . TYR A 98  ? 0.5792 0.3348 0.3257 0.0817  -0.0042 -0.0587 399 TYR A CB  
776   C CG  . TYR A 98  ? 0.5771 0.3437 0.3412 0.0704  -0.0066 -0.0547 399 TYR A CG  
777   C CD1 . TYR A 98  ? 0.5626 0.3375 0.3368 0.0510  -0.0100 -0.0560 399 TYR A CD1 
778   C CD2 . TYR A 98  ? 0.5283 0.2977 0.2981 0.0799  -0.0055 -0.0497 399 TYR A CD2 
779   C CE1 . TYR A 98  ? 0.5324 0.3170 0.3213 0.0417  -0.0115 -0.0525 399 TYR A CE1 
780   C CE2 . TYR A 98  ? 0.5585 0.3367 0.3425 0.0700  -0.0075 -0.0463 399 TYR A CE2 
781   C CZ  . TYR A 98  ? 0.5641 0.3491 0.3572 0.0510  -0.0102 -0.0477 399 TYR A CZ  
782   O OH  . TYR A 98  ? 0.5609 0.3548 0.3674 0.0419  -0.0117 -0.0443 399 TYR A OH  
783   N N   . GLN A 99  ? 0.5538 0.3749 0.3446 0.0704  -0.0058 -0.0571 400 GLN A N   
784   C CA  . GLN A 99  ? 0.4943 0.3450 0.3080 0.0610  -0.0078 -0.0552 400 GLN A CA  
785   C C   . GLN A 99  ? 0.5004 0.3480 0.3168 0.0428  -0.0124 -0.0571 400 GLN A C   
786   O O   . GLN A 99  ? 0.5274 0.3509 0.3239 0.0345  -0.0145 -0.0625 400 GLN A O   
787   C CB  . GLN A 99  ? 0.4904 0.3478 0.2994 0.0641  -0.0069 -0.0578 400 GLN A CB  
788   C CG  . GLN A 99  ? 0.5244 0.3879 0.3309 0.0819  -0.0015 -0.0559 400 GLN A CG  
789   C CD  . GLN A 99  ? 0.5841 0.4762 0.4153 0.0879  0.0011  -0.0489 400 GLN A CD  
790   O OE1 . GLN A 99  ? 0.6053 0.5199 0.4571 0.0798  -0.0004 -0.0453 400 GLN A OE1 
791   N NE2 . GLN A 99  ? 0.5786 0.4696 0.4069 0.1023  0.0048  -0.0469 400 GLN A NE2 
792   N N   . LEU A 100 ? 0.4662 0.3381 0.3062 0.0365  -0.0139 -0.0530 401 LEU A N   
793   C CA  . LEU A 100 ? 0.5110 0.3861 0.3568 0.0204  -0.0178 -0.0543 401 LEU A CA  
794   C C   . LEU A 100 ? 0.4863 0.3709 0.3320 0.0126  -0.0209 -0.0581 401 LEU A C   
795   O O   . LEU A 100 ? 0.5103 0.4114 0.3634 0.0188  -0.0202 -0.0567 401 LEU A O   
796   C CB  . LEU A 100 ? 0.4073 0.3052 0.2771 0.0183  -0.0180 -0.0487 401 LEU A CB  
797   C CG  . LEU A 100 ? 0.3917 0.2812 0.2618 0.0238  -0.0160 -0.0452 401 LEU A CG  
798   C CD1 . LEU A 100 ? 0.3827 0.2943 0.2752 0.0207  -0.0167 -0.0402 401 LEU A CD1 
799   C CD2 . LEU A 100 ? 0.3731 0.2345 0.2241 0.0161  -0.0169 -0.0485 401 LEU A CD2 
800   N N   . LYS A 101 ? 0.4365 0.3112 0.2731 -0.0013 -0.0244 -0.0628 402 LYS A N   
801   C CA  . LYS A 101 ? 0.4449 0.3366 0.2874 -0.0106 -0.0285 -0.0656 402 LYS A CA  
802   C C   . LYS A 101 ? 0.4024 0.3251 0.2709 -0.0111 -0.0294 -0.0606 402 LYS A C   
803   O O   . LYS A 101 ? 0.3948 0.3227 0.2752 -0.0103 -0.0277 -0.0562 402 LYS A O   
804   C CB  . LYS A 101 ? 0.4631 0.3427 0.2938 -0.0275 -0.0321 -0.0712 402 LYS A CB  
805   C CG  . LYS A 101 ? 0.5585 0.4027 0.3598 -0.0287 -0.0315 -0.0766 402 LYS A CG  
806   C CD  . LYS A 101 ? 0.6287 0.4698 0.4182 -0.0213 -0.0321 -0.0801 402 LYS A CD  
807   C CE  . LYS A 101 ? 0.7688 0.5789 0.5349 -0.0087 -0.0280 -0.0815 402 LYS A CE  
808   N NZ  . LYS A 101 ? 0.7545 0.5477 0.4972 -0.0084 -0.0294 -0.0881 402 LYS A NZ  
809   N N   . ASP A 102 ? 0.4047 0.3463 0.2799 -0.0119 -0.0321 -0.0613 403 ASP A N   
810   C CA  . ASP A 102 ? 0.3906 0.3589 0.2869 -0.0117 -0.0333 -0.0569 403 ASP A CA  
811   C C   . ASP A 102 ? 0.3846 0.3600 0.2909 -0.0220 -0.0348 -0.0565 403 ASP A C   
812   O O   . ASP A 102 ? 0.3901 0.3774 0.3114 -0.0192 -0.0334 -0.0517 403 ASP A O   
813   C CB  . ASP A 102 ? 0.4068 0.3910 0.3042 -0.0121 -0.0370 -0.0588 403 ASP A CB  
814   C CG  . ASP A 102 ? 0.7032 0.6820 0.5907 -0.0018 -0.0350 -0.0587 403 ASP A CG  
815   O OD1 . ASP A 102 ? 0.7984 0.7619 0.6782 0.0055  -0.0307 -0.0578 403 ASP A OD1 
816   O OD2 . ASP A 102 ? 0.7305 0.7211 0.6174 -0.0004 -0.0377 -0.0595 403 ASP A OD2 
817   N N   . THR A 103 ? 0.4113 0.3801 0.3087 -0.0346 -0.0376 -0.0617 404 THR A N   
818   C CA  . THR A 103 ? 0.4273 0.4033 0.3329 -0.0457 -0.0384 -0.0615 404 THR A CA  
819   C C   . THR A 103 ? 0.4496 0.4108 0.3552 -0.0430 -0.0343 -0.0578 404 THR A C   
820   O O   . THR A 103 ? 0.3774 0.3511 0.2969 -0.0444 -0.0334 -0.0543 404 THR A O   
821   C CB  . THR A 103 ? 0.4875 0.4562 0.3806 -0.0615 -0.0415 -0.0680 404 THR A CB  
822   O OG1 . THR A 103 ? 0.5708 0.5061 0.4409 -0.0623 -0.0399 -0.0711 404 THR A OG1 
823   C CG2 . THR A 103 ? 0.4816 0.4691 0.3762 -0.0647 -0.0466 -0.0719 404 THR A CG2 
824   N N   . GLU A 104 ? 0.4491 0.3838 0.3383 -0.0380 -0.0318 -0.0585 405 GLU A N   
825   C CA  . GLU A 104 ? 0.3999 0.3204 0.2875 -0.0340 -0.0284 -0.0548 405 GLU A CA  
826   C C   . GLU A 104 ? 0.4194 0.3564 0.3245 -0.0224 -0.0264 -0.0488 405 GLU A C   
827   O O   . GLU A 104 ? 0.4053 0.3446 0.3184 -0.0223 -0.0251 -0.0451 405 GLU A O   
828   C CB  . GLU A 104 ? 0.4035 0.2925 0.2681 -0.0284 -0.0263 -0.0569 405 GLU A CB  
829   C CG  . GLU A 104 ? 0.5077 0.3739 0.3504 -0.0406 -0.0280 -0.0632 405 GLU A CG  
830   C CD  . GLU A 104 ? 0.5647 0.4005 0.3827 -0.0320 -0.0264 -0.0661 405 GLU A CD  
831   O OE1 . GLU A 104 ? 0.5224 0.3321 0.3177 -0.0414 -0.0273 -0.0711 405 GLU A OE1 
832   O OE2 . GLU A 104 ? 0.5835 0.4215 0.4038 -0.0160 -0.0239 -0.0633 405 GLU A OE2 
833   N N   . LEU A 105 ? 0.4206 0.3677 0.3299 -0.0130 -0.0261 -0.0476 406 LEU A N   
834   C CA  . LEU A 105 ? 0.3576 0.3207 0.2826 -0.0042 -0.0244 -0.0421 406 LEU A CA  
835   C C   . LEU A 105 ? 0.3754 0.3574 0.3164 -0.0097 -0.0260 -0.0398 406 LEU A C   
836   O O   . LEU A 105 ? 0.4037 0.3905 0.3543 -0.0071 -0.0246 -0.0357 406 LEU A O   
837   C CB  . LEU A 105 ? 0.3826 0.3541 0.3081 0.0038  -0.0238 -0.0416 406 LEU A CB  
838   C CG  . LEU A 105 ? 0.3851 0.3711 0.3242 0.0117  -0.0215 -0.0358 406 LEU A CG  
839   C CD1 . LEU A 105 ? 0.4370 0.4148 0.3749 0.0186  -0.0184 -0.0333 406 LEU A CD1 
840   C CD2 . LEU A 105 ? 0.3614 0.3560 0.2997 0.0173  -0.0208 -0.0352 406 LEU A CD2 
841   N N   . ILE A 106 ? 0.3424 0.3358 0.2857 -0.0167 -0.0290 -0.0427 407 ILE A N   
842   C CA  . ILE A 106 ? 0.3090 0.3221 0.2668 -0.0197 -0.0304 -0.0407 407 ILE A CA  
843   C C   . ILE A 106 ? 0.4012 0.4104 0.3613 -0.0270 -0.0294 -0.0403 407 ILE A C   
844   O O   . ILE A 106 ? 0.4019 0.4187 0.3721 -0.0247 -0.0283 -0.0366 407 ILE A O   
845   C CB  . ILE A 106 ? 0.2783 0.3068 0.2376 -0.0244 -0.0342 -0.0441 407 ILE A CB  
846   C CG1 . ILE A 106 ? 0.2880 0.3222 0.2462 -0.0156 -0.0349 -0.0431 407 ILE A CG1 
847   C CG2 . ILE A 106 ? 0.2844 0.3327 0.2569 -0.0281 -0.0354 -0.0429 407 ILE A CG2 
848   C CD1 . ILE A 106 ? 0.3590 0.4040 0.3136 -0.0194 -0.0392 -0.0474 407 ILE A CD1 
849   N N   . TYR A 107 ? 0.4038 0.3994 0.3524 -0.0363 -0.0298 -0.0441 408 TYR A N   
850   C CA  . TYR A 107 ? 0.4159 0.4038 0.3630 -0.0439 -0.0282 -0.0436 408 TYR A CA  
851   C C   . TYR A 107 ? 0.3899 0.3674 0.3379 -0.0357 -0.0254 -0.0390 408 TYR A C   
852   O O   . TYR A 107 ? 0.3321 0.3151 0.2878 -0.0372 -0.0243 -0.0362 408 TYR A O   
853   C CB  . TYR A 107 ? 0.4012 0.3683 0.3303 -0.0545 -0.0285 -0.0481 408 TYR A CB  
854   C CG  . TYR A 107 ? 0.4197 0.3722 0.3426 -0.0618 -0.0261 -0.0470 408 TYR A CG  
855   C CD1 . TYR A 107 ? 0.3491 0.3147 0.2787 -0.0737 -0.0261 -0.0475 408 TYR A CD1 
856   C CD2 . TYR A 107 ? 0.4471 0.3732 0.3564 -0.0560 -0.0238 -0.0452 408 TYR A CD2 
857   C CE1 . TYR A 107 ? 0.3796 0.3309 0.3020 -0.0809 -0.0234 -0.0462 408 TYR A CE1 
858   C CE2 . TYR A 107 ? 0.5056 0.4164 0.4070 -0.0620 -0.0217 -0.0438 408 TYR A CE2 
859   C CZ  . TYR A 107 ? 0.5050 0.4276 0.4125 -0.0750 -0.0213 -0.0442 408 TYR A CZ  
860   O OH  . TYR A 107 ? 0.6201 0.5264 0.5182 -0.0814 -0.0187 -0.0425 408 TYR A OH  
861   N N   . GLY A 108 ? 0.3500 0.3138 0.2900 -0.0266 -0.0243 -0.0382 409 GLY A N   
862   C CA  . GLY A 108 ? 0.3341 0.2898 0.2745 -0.0187 -0.0222 -0.0342 409 GLY A CA  
863   C C   . GLY A 108 ? 0.4110 0.3854 0.3681 -0.0134 -0.0220 -0.0299 409 GLY A C   
864   O O   . GLY A 108 ? 0.3224 0.2958 0.2834 -0.0125 -0.0212 -0.0269 409 GLY A O   
865   N N   . ALA A 109 ? 0.2829 0.2726 0.2482 -0.0101 -0.0229 -0.0294 410 ALA A N   
866   C CA  . ALA A 109 ? 0.2957 0.2997 0.2739 -0.0058 -0.0226 -0.0255 410 ALA A CA  
867   C C   . ALA A 109 ? 0.2784 0.2913 0.2640 -0.0115 -0.0233 -0.0249 410 ALA A C   
868   O O   . ALA A 109 ? 0.3486 0.3632 0.3397 -0.0097 -0.0225 -0.0218 410 ALA A O   
869   C CB  . ALA A 109 ? 0.2572 0.2722 0.2389 -0.0015 -0.0232 -0.0251 410 ALA A CB  
870   N N   . LYS A 110 ? 0.2709 0.2906 0.2565 -0.0183 -0.0247 -0.0280 411 LYS A N   
871   C CA  . LYS A 110 ? 0.3101 0.3407 0.3029 -0.0231 -0.0247 -0.0277 411 LYS A CA  
872   C C   . LYS A 110 ? 0.3498 0.3689 0.3389 -0.0272 -0.0229 -0.0266 411 LYS A C   
873   O O   . LYS A 110 ? 0.2999 0.3244 0.2948 -0.0268 -0.0220 -0.0244 411 LYS A O   
874   C CB  . LYS A 110 ? 0.2547 0.2976 0.2484 -0.0304 -0.0266 -0.0316 411 LYS A CB  
875   C CG  . LYS A 110 ? 0.2713 0.3286 0.2693 -0.0251 -0.0289 -0.0321 411 LYS A CG  
876   C CD  . LYS A 110 ? 0.2553 0.3287 0.2553 -0.0320 -0.0315 -0.0360 411 LYS A CD  
877   C CE  . LYS A 110 ? 0.2567 0.3431 0.2588 -0.0252 -0.0343 -0.0364 411 LYS A CE  
878   N NZ  . LYS A 110 ? 0.3196 0.4274 0.3265 -0.0310 -0.0372 -0.0399 411 LYS A NZ  
879   N N   . HIS A 111 ? 0.3434 0.3446 0.3207 -0.0303 -0.0222 -0.0281 412 HIS A N   
880   C CA  . HIS A 111 ? 0.2889 0.2767 0.2600 -0.0340 -0.0205 -0.0268 412 HIS A CA  
881   C C   . HIS A 111 ? 0.3906 0.3726 0.3630 -0.0252 -0.0199 -0.0229 412 HIS A C   
882   O O   . HIS A 111 ? 0.3173 0.2964 0.2898 -0.0267 -0.0189 -0.0208 412 HIS A O   
883   C CB  . HIS A 111 ? 0.3331 0.3006 0.2880 -0.0404 -0.0200 -0.0297 412 HIS A CB  
884   C CG  . HIS A 111 ? 0.4011 0.3753 0.3553 -0.0535 -0.0201 -0.0330 412 HIS A CG  
885   N ND1 . HIS A 111 ? 0.4457 0.4143 0.3953 -0.0631 -0.0181 -0.0328 412 HIS A ND1 
886   C CD2 . HIS A 111 ? 0.3758 0.3668 0.3357 -0.0585 -0.0220 -0.0363 412 HIS A CD2 
887   C CE1 . HIS A 111 ? 0.3995 0.3815 0.3520 -0.0746 -0.0185 -0.0360 412 HIS A CE1 
888   N NE2 . HIS A 111 ? 0.4143 0.4106 0.3734 -0.0717 -0.0213 -0.0382 412 HIS A NE2 
889   N N   . ALA A 112 ? 0.2902 0.2731 0.2644 -0.0166 -0.0204 -0.0217 413 ALA A N   
890   C CA  . ALA A 112 ? 0.2902 0.2737 0.2685 -0.0093 -0.0203 -0.0180 413 ALA A CA  
891   C C   . ALA A 112 ? 0.3106 0.3073 0.2997 -0.0102 -0.0206 -0.0159 413 ALA A C   
892   O O   . ALA A 112 ? 0.2888 0.2834 0.2788 -0.0090 -0.0206 -0.0135 413 ALA A O   
893   C CB  . ALA A 112 ? 0.2616 0.2481 0.2414 -0.0013 -0.0204 -0.0172 413 ALA A CB  
894   N N   . TRP A 113 ? 0.2486 0.2582 0.2443 -0.0116 -0.0211 -0.0169 414 TRP A N   
895   C CA  . TRP A 113 ? 0.2403 0.2599 0.2434 -0.0116 -0.0211 -0.0153 414 TRP A CA  
896   C C   . TRP A 113 ? 0.2487 0.2672 0.2503 -0.0173 -0.0201 -0.0159 414 TRP A C   
897   O O   . TRP A 113 ? 0.2873 0.3052 0.2902 -0.0164 -0.0196 -0.0139 414 TRP A O   
898   C CB  . TRP A 113 ? 0.1866 0.2188 0.1946 -0.0102 -0.0219 -0.0163 414 TRP A CB  
899   C CG  . TRP A 113 ? 0.2473 0.2872 0.2602 -0.0079 -0.0219 -0.0147 414 TRP A CG  
900   C CD1 . TRP A 113 ? 0.2600 0.2962 0.2733 -0.0073 -0.0213 -0.0127 414 TRP A CD1 
901   C CD2 . TRP A 113 ? 0.2709 0.3219 0.2869 -0.0050 -0.0225 -0.0151 414 TRP A CD2 
902   N NE1 . TRP A 113 ? 0.2513 0.2940 0.2667 -0.0044 -0.0212 -0.0121 414 TRP A NE1 
903   C CE2 . TRP A 113 ? 0.2793 0.3312 0.2964 -0.0022 -0.0220 -0.0134 414 TRP A CE2 
904   C CE3 . TRP A 113 ? 0.2587 0.3185 0.2753 -0.0037 -0.0238 -0.0169 414 TRP A CE3 
905   C CZ2 . TRP A 113 ? 0.2289 0.2888 0.2468 0.0029  -0.0223 -0.0132 414 TRP A CZ2 
906   C CZ3 . TRP A 113 ? 0.3045 0.3743 0.3231 0.0012  -0.0246 -0.0165 414 TRP A CZ3 
907   C CH2 . TRP A 113 ? 0.3016 0.3707 0.3204 0.0050  -0.0237 -0.0146 414 TRP A CH2 
908   N N   . ARG A 114 ? 0.2757 0.2945 0.2740 -0.0241 -0.0195 -0.0188 415 ARG A N   
909   C CA  . ARG A 114 ? 0.2808 0.2997 0.2772 -0.0312 -0.0177 -0.0192 415 ARG A CA  
910   C C   . ARG A 114 ? 0.3244 0.3275 0.3133 -0.0310 -0.0167 -0.0169 415 ARG A C   
911   O O   . ARG A 114 ? 0.3331 0.3372 0.3220 -0.0336 -0.0151 -0.0158 415 ARG A O   
912   C CB  . ARG A 114 ? 0.3031 0.3224 0.2951 -0.0405 -0.0174 -0.0227 415 ARG A CB  
913   C CG  . ARG A 114 ? 0.2847 0.3095 0.2765 -0.0497 -0.0151 -0.0235 415 ARG A CG  
914   C CD  . ARG A 114 ? 0.2912 0.3128 0.2761 -0.0611 -0.0149 -0.0270 415 ARG A CD  
915   N NE  . ARG A 114 ? 0.2669 0.3027 0.2554 -0.0710 -0.0126 -0.0281 415 ARG A NE  
916   C CZ  . ARG A 114 ? 0.3319 0.3703 0.3162 -0.0839 -0.0120 -0.0312 415 ARG A CZ  
917   N NH1 . ARG A 114 ? 0.3089 0.3643 0.2983 -0.0929 -0.0095 -0.0318 415 ARG A NH1 
918   N NH2 . ARG A 114 ? 0.3297 0.3545 0.3043 -0.0881 -0.0140 -0.0339 415 ARG A NH2 
919   N N   . ASN A 115 ? 0.2387 0.2277 0.2207 -0.0270 -0.0175 -0.0162 416 ASN A N   
920   C CA  . ASN A 115 ? 0.3230 0.2966 0.2963 -0.0252 -0.0171 -0.0139 416 ASN A CA  
921   C C   . ASN A 115 ? 0.3628 0.3405 0.3417 -0.0179 -0.0185 -0.0109 416 ASN A C   
922   O O   . ASN A 115 ? 0.3118 0.2792 0.2843 -0.0150 -0.0189 -0.0089 416 ASN A O   
923   C CB  . ASN A 115 ? 0.3006 0.2569 0.2621 -0.0226 -0.0174 -0.0146 416 ASN A CB  
924   C CG  . ASN A 115 ? 0.3588 0.3049 0.3102 -0.0317 -0.0161 -0.0177 416 ASN A CG  
925   O OD1 . ASN A 115 ? 0.3102 0.2617 0.2627 -0.0411 -0.0146 -0.0189 416 ASN A OD1 
926   N ND2 . ASN A 115 ? 0.3422 0.2737 0.2827 -0.0292 -0.0165 -0.0194 416 ASN A ND2 
927   N N   . ALA A 116 ? 0.2512 0.2429 0.2405 -0.0150 -0.0194 -0.0106 417 ALA A N   
928   C CA  . ALA A 116 ? 0.2651 0.2599 0.2585 -0.0097 -0.0210 -0.0080 417 ALA A CA  
929   C C   . ALA A 116 ? 0.2457 0.2401 0.2383 -0.0117 -0.0207 -0.0069 417 ALA A C   
930   O O   . ALA A 116 ? 0.2336 0.2360 0.2305 -0.0130 -0.0199 -0.0075 417 ALA A O   
931   C CB  . ALA A 116 ? 0.2021 0.2079 0.2036 -0.0070 -0.0218 -0.0079 417 ALA A CB  
932   N N   . SER A 117 ? 0.2442 0.2289 0.2300 -0.0109 -0.0212 -0.0054 418 SER A N   
933   C CA  A SER A 117 ? 0.2564 0.2386 0.2387 -0.0132 -0.0205 -0.0045 418 SER A CA  
934   C CA  B SER A 117 ? 0.2575 0.2395 0.2397 -0.0131 -0.0205 -0.0045 418 SER A CA  
935   C C   . SER A 117 ? 0.3070 0.2963 0.2944 -0.0111 -0.0219 -0.0037 418 SER A C   
936   O O   . SER A 117 ? 0.3095 0.2988 0.2947 -0.0128 -0.0207 -0.0038 418 SER A O   
937   C CB  A SER A 117 ? 0.2535 0.2225 0.2256 -0.0116 -0.0213 -0.0026 418 SER A CB  
938   C CB  B SER A 117 ? 0.2587 0.2277 0.2308 -0.0114 -0.0214 -0.0026 418 SER A CB  
939   O OG  A SER A 117 ? 0.3072 0.2786 0.2817 -0.0056 -0.0246 -0.0010 418 SER A OG  
940   O OG  B SER A 117 ? 0.2424 0.1999 0.2062 -0.0125 -0.0201 -0.0031 418 SER A OG  
941   N N   . ARG A 118 ? 0.2775 0.2718 0.2702 -0.0079 -0.0242 -0.0031 419 ARG A N   
942   C CA  . ARG A 118 ? 0.2711 0.2688 0.2660 -0.0074 -0.0258 -0.0024 419 ARG A CA  
943   C C   . ARG A 118 ? 0.3393 0.3423 0.3377 -0.0075 -0.0243 -0.0036 419 ARG A C   
944   O O   . ARG A 118 ? 0.2639 0.2660 0.2611 -0.0072 -0.0253 -0.0032 419 ARG A O   
945   C CB  . ARG A 118 ? 0.2442 0.2455 0.2425 -0.0055 -0.0287 -0.0009 419 ARG A CB  
946   C CG  . ARG A 118 ? 0.2513 0.2491 0.2455 -0.0034 -0.0310 0.0005  419 ARG A CG  
947   C CD  . ARG A 118 ? 0.2434 0.2501 0.2430 -0.0011 -0.0338 0.0018  419 ARG A CD  
948   N NE  . ARG A 118 ? 0.2910 0.2971 0.2868 0.0015  -0.0369 0.0032  419 ARG A NE  
949   C CZ  . ARG A 118 ? 0.3878 0.4043 0.3881 0.0044  -0.0398 0.0045  419 ARG A CZ  
950   N NH1 . ARG A 118 ? 0.3042 0.3319 0.3129 0.0044  -0.0392 0.0047  419 ARG A NH1 
951   N NH2 . ARG A 118 ? 0.4139 0.4311 0.4103 0.0077  -0.0432 0.0058  419 ARG A NH2 
952   N N   . CYS A 119 ? 0.2940 0.3015 0.2951 -0.0079 -0.0224 -0.0051 420 CYS A N   
953   C CA  . CYS A 119 ? 0.1949 0.2087 0.1990 -0.0062 -0.0217 -0.0059 420 CYS A CA  
954   C C   . CYS A 119 ? 0.2039 0.2216 0.2068 -0.0062 -0.0195 -0.0073 420 CYS A C   
955   O O   . CYS A 119 ? 0.2154 0.2370 0.2189 -0.0093 -0.0177 -0.0086 420 CYS A O   
956   C CB  . CYS A 119 ? 0.2532 0.2724 0.2612 -0.0058 -0.0215 -0.0068 420 CYS A CB  
957   S SG  . CYS A 119 ? 0.2782 0.3058 0.2886 -0.0024 -0.0210 -0.0077 420 CYS A SG  
958   N N   . VAL A 120 ? 0.2355 0.2519 0.2355 -0.0030 -0.0193 -0.0071 421 VAL A N   
959   C CA  . VAL A 120 ? 0.2872 0.3091 0.2858 -0.0008 -0.0169 -0.0084 421 VAL A CA  
960   C C   . VAL A 120 ? 0.3076 0.3419 0.3110 0.0023  -0.0161 -0.0097 421 VAL A C   
961   O O   . VAL A 120 ? 0.2933 0.3378 0.2978 0.0042  -0.0138 -0.0111 421 VAL A O   
962   C CB  . VAL A 120 ? 0.2871 0.3000 0.2779 0.0030  -0.0172 -0.0079 421 VAL A CB  
963   C CG1 . VAL A 120 ? 0.2590 0.2678 0.2473 0.0072  -0.0185 -0.0073 421 VAL A CG1 
964   C CG2 . VAL A 120 ? 0.2896 0.3069 0.2771 0.0059  -0.0140 -0.0092 421 VAL A CG2 
965   N N   . GLY A 121 ? 0.3145 0.3498 0.3207 0.0031  -0.0178 -0.0094 422 GLY A N   
966   C CA  . GLY A 121 ? 0.2896 0.3362 0.2991 0.0069  -0.0178 -0.0105 422 GLY A CA  
967   C C   . GLY A 121 ? 0.3533 0.4119 0.3688 0.0023  -0.0176 -0.0126 422 GLY A C   
968   O O   . GLY A 121 ? 0.3087 0.3781 0.3272 0.0049  -0.0184 -0.0137 422 GLY A O   
969   N N   . ARG A 122 ? 0.3180 0.3740 0.3337 -0.0047 -0.0166 -0.0131 423 ARG A N   
970   C CA  . ARG A 122 ? 0.2881 0.3494 0.3063 -0.0109 -0.0167 -0.0150 423 ARG A CA  
971   C C   . ARG A 122 ? 0.2726 0.3523 0.2956 -0.0133 -0.0156 -0.0175 423 ARG A C   
972   O O   . ARG A 122 ? 0.2525 0.3369 0.2768 -0.0198 -0.0161 -0.0196 423 ARG A O   
973   C CB  . ARG A 122 ? 0.2420 0.2913 0.2557 -0.0174 -0.0158 -0.0147 423 ARG A CB  
974   C CG  . ARG A 122 ? 0.2396 0.2751 0.2500 -0.0154 -0.0175 -0.0129 423 ARG A CG  
975   C CD  . ARG A 122 ? 0.2544 0.2778 0.2584 -0.0198 -0.0167 -0.0124 423 ARG A CD  
976   N NE  . ARG A 122 ? 0.2594 0.2779 0.2604 -0.0192 -0.0159 -0.0107 423 ARG A NE  
977   C CZ  . ARG A 122 ? 0.2384 0.2474 0.2325 -0.0231 -0.0147 -0.0100 423 ARG A CZ  
978   N NH1 . ARG A 122 ? 0.2358 0.2376 0.2246 -0.0280 -0.0139 -0.0109 423 ARG A NH1 
979   N NH2 . ARG A 122 ? 0.2442 0.2486 0.2345 -0.0220 -0.0142 -0.0084 423 ARG A NH2 
980   N N   . ILE A 123 ? 0.2110 0.3022 0.2363 -0.0085 -0.0142 -0.0176 424 ILE A N   
981   C CA  . ILE A 123 ? 0.2563 0.3703 0.2880 -0.0102 -0.0134 -0.0201 424 ILE A CA  
982   C C   . ILE A 123 ? 0.3216 0.4447 0.3565 -0.0077 -0.0167 -0.0214 424 ILE A C   
983   O O   . ILE A 123 ? 0.2131 0.3544 0.2532 -0.0123 -0.0173 -0.0240 424 ILE A O   
984   C CB  . ILE A 123 ? 0.2747 0.4008 0.3078 -0.0024 -0.0112 -0.0198 424 ILE A CB  
985   C CG1 . ILE A 123 ? 0.2979 0.4508 0.3388 -0.0068 -0.0094 -0.0223 424 ILE A CG1 
986   C CG2 . ILE A 123 ? 0.2505 0.3751 0.2811 0.0103  -0.0133 -0.0188 424 ILE A CG2 
987   C CD1 . ILE A 123 ? 0.3300 0.4955 0.3720 -0.0001 -0.0059 -0.0222 424 ILE A CD1 
988   N N   . GLN A 124 ? 0.2955 0.4059 0.3265 -0.0016 -0.0188 -0.0197 425 GLN A N   
989   C CA  . GLN A 124 ? 0.3641 0.4794 0.3956 0.0020  -0.0217 -0.0204 425 GLN A CA  
990   C C   . GLN A 124 ? 0.2867 0.3946 0.3167 -0.0054 -0.0231 -0.0217 425 GLN A C   
991   O O   . GLN A 124 ? 0.3002 0.4105 0.3293 -0.0026 -0.0254 -0.0223 425 GLN A O   
992   C CB  . GLN A 124 ? 0.3556 0.4586 0.3816 0.0117  -0.0224 -0.0174 425 GLN A CB  
993   C CG  . GLN A 124 ? 0.3836 0.4909 0.4075 0.0212  -0.0215 -0.0164 425 GLN A CG  
994   C CD  . GLN A 124 ? 0.5091 0.6358 0.5355 0.0284  -0.0232 -0.0178 425 GLN A CD  
995   O OE1 . GLN A 124 ? 0.4912 0.6220 0.5181 0.0284  -0.0258 -0.0184 425 GLN A OE1 
996   N NE2 . GLN A 124 ? 0.5291 0.6691 0.5569 0.0353  -0.0219 -0.0183 425 GLN A NE2 
997   N N   . TRP A 125 ? 0.2877 0.3854 0.3155 -0.0138 -0.0216 -0.0221 426 TRP A N   
998   C CA  . TRP A 125 ? 0.1994 0.2825 0.2221 -0.0176 -0.0224 -0.0225 426 TRP A CA  
999   C C   . TRP A 125 ? 0.2253 0.3159 0.2476 -0.0208 -0.0247 -0.0256 426 TRP A C   
1000  O O   . TRP A 125 ? 0.3086 0.3896 0.3264 -0.0191 -0.0258 -0.0257 426 TRP A O   
1001  C CB  . TRP A 125 ? 0.2347 0.3049 0.2528 -0.0251 -0.0205 -0.0225 426 TRP A CB  
1002  C CG  . TRP A 125 ? 0.2272 0.3056 0.2454 -0.0354 -0.0195 -0.0254 426 TRP A CG  
1003  C CD1 . TRP A 125 ? 0.2576 0.3483 0.2798 -0.0392 -0.0173 -0.0256 426 TRP A CD1 
1004  C CD2 . TRP A 125 ? 0.1945 0.2694 0.2076 -0.0443 -0.0204 -0.0286 426 TRP A CD2 
1005  N NE1 . TRP A 125 ? 0.3447 0.4415 0.3657 -0.0509 -0.0166 -0.0285 426 TRP A NE1 
1006  C CE2 . TRP A 125 ? 0.3109 0.3969 0.3256 -0.0546 -0.0188 -0.0305 426 TRP A CE2 
1007  C CE3 . TRP A 125 ? 0.2389 0.3020 0.2451 -0.0447 -0.0222 -0.0301 426 TRP A CE3 
1008  C CZ2 . TRP A 125 ? 0.2998 0.3841 0.3089 -0.0667 -0.0192 -0.0340 426 TRP A CZ2 
1009  C CZ3 . TRP A 125 ? 0.3223 0.3820 0.3218 -0.0554 -0.0228 -0.0338 426 TRP A CZ3 
1010  C CH2 . TRP A 125 ? 0.2986 0.3684 0.2993 -0.0670 -0.0215 -0.0358 426 TRP A CH2 
1011  N N   . SER A 126 ? 0.2782 0.3864 0.3046 -0.0261 -0.0253 -0.0285 427 SER A N   
1012  C CA  . SER A 126 ? 0.3642 0.4789 0.3891 -0.0307 -0.0281 -0.0320 427 SER A CA  
1013  C C   . SER A 126 ? 0.3011 0.4270 0.3282 -0.0212 -0.0310 -0.0317 427 SER A C   
1014  O O   . SER A 126 ? 0.3913 0.5206 0.4156 -0.0231 -0.0337 -0.0343 427 SER A O   
1015  C CB  . SER A 126 ? 0.4144 0.5452 0.4425 -0.0421 -0.0281 -0.0355 427 SER A CB  
1016  O OG  . SER A 126 ? 0.4453 0.6017 0.4832 -0.0378 -0.0284 -0.0355 427 SER A OG  
1017  N N   . LYS A 127 ? 0.3058 0.4355 0.3358 -0.0109 -0.0304 -0.0286 428 LYS A N   
1018  C CA  . LYS A 127 ? 0.3764 0.5111 0.4052 -0.0005 -0.0327 -0.0273 428 LYS A CA  
1019  C C   . LYS A 127 ? 0.5067 0.6204 0.5291 0.0042  -0.0316 -0.0240 428 LYS A C   
1020  O O   . LYS A 127 ? 0.6090 0.7149 0.6297 0.0106  -0.0302 -0.0206 428 LYS A O   
1021  C CB  . LYS A 127 ? 0.3741 0.5224 0.4066 0.0085  -0.0325 -0.0259 428 LYS A CB  
1022  C CG  . LYS A 127 ? 0.6272 0.8036 0.6669 0.0078  -0.0344 -0.0289 428 LYS A CG  
1023  C CD  . LYS A 127 ? 0.8316 1.0182 0.8715 0.0222  -0.0348 -0.0268 428 LYS A CD  
1024  C CE  . LYS A 127 ? 0.8578 1.0296 0.8883 0.0325  -0.0364 -0.0238 428 LYS A CE  
1025  N NZ  . LYS A 127 ? 0.8226 1.0036 0.8499 0.0474  -0.0376 -0.0222 428 LYS A NZ  
1026  N N   . LEU A 128 ? 0.3549 0.4593 0.3728 0.0002  -0.0322 -0.0253 429 LEU A N   
1027  C CA  . LEU A 128 ? 0.2089 0.2965 0.2217 0.0034  -0.0307 -0.0225 429 LEU A CA  
1028  C C   . LEU A 128 ? 0.2698 0.3579 0.2773 0.0054  -0.0325 -0.0238 429 LEU A C   
1029  O O   . LEU A 128 ? 0.2885 0.3785 0.2937 -0.0003 -0.0340 -0.0276 429 LEU A O   
1030  C CB  . LEU A 128 ? 0.1928 0.2668 0.2040 -0.0022 -0.0286 -0.0226 429 LEU A CB  
1031  C CG  . LEU A 128 ? 0.2274 0.2893 0.2346 0.0017  -0.0272 -0.0201 429 LEU A CG  
1032  C CD1 . LEU A 128 ? 0.2268 0.2873 0.2358 0.0070  -0.0261 -0.0159 429 LEU A CD1 
1033  C CD2 . LEU A 128 ? 0.2334 0.2831 0.2380 -0.0016 -0.0256 -0.0204 429 LEU A CD2 
1034  N N   . GLN A 129 ? 0.2494 0.3346 0.2534 0.0128  -0.0323 -0.0208 430 GLN A N   
1035  C CA  . GLN A 129 ? 0.2288 0.3133 0.2264 0.0152  -0.0335 -0.0216 430 GLN A CA  
1036  C C   . GLN A 129 ? 0.2755 0.3463 0.2692 0.0137  -0.0308 -0.0208 430 GLN A C   
1037  O O   . GLN A 129 ? 0.2996 0.3629 0.2944 0.0154  -0.0281 -0.0172 430 GLN A O   
1038  C CB  . GLN A 129 ? 0.2600 0.3464 0.2534 0.0239  -0.0342 -0.0183 430 GLN A CB  
1039  C CG  . GLN A 129 ? 0.3601 0.4451 0.3453 0.0270  -0.0352 -0.0186 430 GLN A CG  
1040  C CD  . GLN A 129 ? 0.4151 0.5123 0.3997 0.0243  -0.0393 -0.0236 430 GLN A CD  
1041  O OE1 . GLN A 129 ? 0.4328 0.5441 0.4234 0.0223  -0.0419 -0.0260 430 GLN A OE1 
1042  N NE2 . GLN A 129 ? 0.5834 0.6762 0.5605 0.0237  -0.0398 -0.0254 430 GLN A NE2 
1043  N N   . VAL A 130 ? 0.2699 0.3378 0.2587 0.0105  -0.0316 -0.0244 431 VAL A N   
1044  C CA  . VAL A 130 ? 0.2629 0.3184 0.2471 0.0106  -0.0288 -0.0242 431 VAL A CA  
1045  C C   . VAL A 130 ? 0.3140 0.3683 0.2905 0.0154  -0.0284 -0.0239 431 VAL A C   
1046  O O   . VAL A 130 ? 0.3315 0.3889 0.3022 0.0146  -0.0311 -0.0274 431 VAL A O   
1047  C CB  . VAL A 130 ? 0.2808 0.3287 0.2613 0.0043  -0.0291 -0.0284 431 VAL A CB  
1048  C CG1 . VAL A 130 ? 0.3202 0.3550 0.2944 0.0074  -0.0261 -0.0279 431 VAL A CG1 
1049  C CG2 . VAL A 130 ? 0.2089 0.2579 0.1959 -0.0009 -0.0291 -0.0282 431 VAL A CG2 
1050  N N   . PHE A 131 ? 0.3353 0.3856 0.3113 0.0197  -0.0249 -0.0198 432 PHE A N   
1051  C CA  . PHE A 131 ? 0.3223 0.3710 0.2907 0.0242  -0.0233 -0.0189 432 PHE A CA  
1052  C C   . PHE A 131 ? 0.3440 0.3852 0.3084 0.0251  -0.0203 -0.0204 432 PHE A C   
1053  O O   . PHE A 131 ? 0.3164 0.3558 0.2857 0.0257  -0.0174 -0.0179 432 PHE A O   
1054  C CB  . PHE A 131 ? 0.2733 0.3231 0.2425 0.0275  -0.0207 -0.0133 432 PHE A CB  
1055  C CG  . PHE A 131 ? 0.3896 0.4436 0.3588 0.0291  -0.0235 -0.0118 432 PHE A CG  
1056  C CD1 . PHE A 131 ? 0.3923 0.4511 0.3552 0.0320  -0.0268 -0.0138 432 PHE A CD1 
1057  C CD2 . PHE A 131 ? 0.3214 0.3744 0.2956 0.0286  -0.0229 -0.0086 432 PHE A CD2 
1058  C CE1 . PHE A 131 ? 0.4317 0.4955 0.3939 0.0356  -0.0295 -0.0123 432 PHE A CE1 
1059  C CE2 . PHE A 131 ? 0.3773 0.4326 0.3494 0.0320  -0.0252 -0.0072 432 PHE A CE2 
1060  C CZ  . PHE A 131 ? 0.3705 0.4318 0.3369 0.0362  -0.0285 -0.0090 432 PHE A CZ  
1061  N N   . ASP A 132 ? 0.3612 0.3982 0.3158 0.0258  -0.0213 -0.0245 433 ASP A N   
1062  C CA  . ASP A 132 ? 0.3602 0.3880 0.3077 0.0285  -0.0185 -0.0265 433 ASP A CA  
1063  C C   . ASP A 132 ? 0.4312 0.4620 0.3759 0.0349  -0.0141 -0.0231 433 ASP A C   
1064  O O   . ASP A 132 ? 0.3558 0.3878 0.2926 0.0372  -0.0143 -0.0236 433 ASP A O   
1065  C CB  . ASP A 132 ? 0.3298 0.3494 0.2654 0.0259  -0.0215 -0.0328 433 ASP A CB  
1066  C CG  . ASP A 132 ? 0.3376 0.3434 0.2623 0.0296  -0.0187 -0.0355 433 ASP A CG  
1067  O OD1 . ASP A 132 ? 0.4505 0.4454 0.3630 0.0264  -0.0211 -0.0410 433 ASP A OD1 
1068  O OD2 . ASP A 132 ? 0.3349 0.3407 0.2622 0.0357  -0.0144 -0.0323 433 ASP A OD2 
1069  N N   . ALA A 133 ? 0.4159 0.4491 0.3667 0.0374  -0.0101 -0.0196 434 ALA A N   
1070  C CA  . ALA A 133 ? 0.3248 0.3637 0.2743 0.0423  -0.0051 -0.0161 434 ALA A CA  
1071  C C   . ALA A 133 ? 0.3434 0.3792 0.2883 0.0485  -0.0015 -0.0178 434 ALA A C   
1072  O O   . ALA A 133 ? 0.3036 0.3483 0.2525 0.0524  0.0033  -0.0144 434 ALA A O   
1073  C CB  . ALA A 133 ? 0.2509 0.2988 0.2114 0.0397  -0.0030 -0.0102 434 ALA A CB  
1074  N N   . ARG A 134 ? 0.2974 0.3206 0.2329 0.0495  -0.0036 -0.0232 435 ARG A N   
1075  C CA  . ARG A 134 ? 0.3312 0.3478 0.2593 0.0572  -0.0004 -0.0251 435 ARG A CA  
1076  C C   . ARG A 134 ? 0.3358 0.3532 0.2530 0.0645  0.0037  -0.0259 435 ARG A C   
1077  O O   . ARG A 134 ? 0.3779 0.3922 0.2889 0.0731  0.0074  -0.0270 435 ARG A O   
1078  C CB  . ARG A 134 ? 0.3664 0.3648 0.2845 0.0553  -0.0038 -0.0305 435 ARG A CB  
1079  C CG  . ARG A 134 ? 0.3086 0.3065 0.2368 0.0501  -0.0061 -0.0290 435 ARG A CG  
1080  C CD  . ARG A 134 ? 0.3776 0.3562 0.2943 0.0460  -0.0092 -0.0339 435 ARG A CD  
1081  N NE  . ARG A 134 ? 0.3695 0.3446 0.2803 0.0381  -0.0131 -0.0379 435 ARG A NE  
1082  C CZ  . ARG A 134 ? 0.3989 0.3569 0.2959 0.0329  -0.0157 -0.0433 435 ARG A CZ  
1083  N NH1 . ARG A 134 ? 0.4464 0.3855 0.3321 0.0358  -0.0144 -0.0451 435 ARG A NH1 
1084  N NH2 . ARG A 134 ? 0.3805 0.3397 0.2738 0.0249  -0.0197 -0.0469 435 ARG A NH2 
1085  N N   . ASP A 135 ? 0.3435 0.3650 0.2575 0.0624  0.0033  -0.0253 436 ASP A N   
1086  C CA  . ASP A 135 ? 0.3662 0.3893 0.2695 0.0692  0.0077  -0.0254 436 ASP A CA  
1087  C C   . ASP A 135 ? 0.4257 0.4663 0.3388 0.0711  0.0136  -0.0190 436 ASP A C   
1088  O O   . ASP A 135 ? 0.4311 0.4760 0.3368 0.0767  0.0186  -0.0181 436 ASP A O   
1089  C CB  . ASP A 135 ? 0.3334 0.3512 0.2258 0.0662  0.0041  -0.0281 436 ASP A CB  
1090  C CG  . ASP A 135 ? 0.5281 0.5555 0.4291 0.0605  0.0020  -0.0236 436 ASP A CG  
1091  O OD1 . ASP A 135 ? 0.4950 0.5216 0.3872 0.0602  0.0001  -0.0243 436 ASP A OD1 
1092  O OD2 . ASP A 135 ? 0.5201 0.5549 0.4352 0.0568  0.0023  -0.0195 436 ASP A OD2 
1093  N N   . CYS A 136 ? 0.3534 0.4037 0.2819 0.0660  0.0134  -0.0145 437 CYS A N   
1094  C CA  . CYS A 136 ? 0.3492 0.4157 0.2869 0.0646  0.0185  -0.0083 437 CYS A CA  
1095  C C   . CYS A 136 ? 0.3877 0.4656 0.3277 0.0726  0.0246  -0.0076 437 CYS A C   
1096  O O   . CYS A 136 ? 0.4329 0.5069 0.3725 0.0785  0.0239  -0.0106 437 CYS A O   
1097  C CB  . CYS A 136 ? 0.3104 0.3818 0.2621 0.0565  0.0159  -0.0047 437 CYS A CB  
1098  S SG  . CYS A 136 ? 0.3779 0.4658 0.3389 0.0510  0.0212  0.0027  437 CYS A SG  
1099  N N   . THR A 137 ? 0.3566 0.4487 0.2979 0.0732  0.0308  -0.0034 438 THR A N   
1100  C CA  . THR A 137 ? 0.2780 0.3856 0.2221 0.0815  0.0373  -0.0025 438 THR A CA  
1101  C C   . THR A 137 ? 0.3024 0.4337 0.2605 0.0760  0.0425  0.0039  438 THR A C   
1102  O O   . THR A 137 ? 0.3475 0.4969 0.3116 0.0825  0.0475  0.0048  438 THR A O   
1103  C CB  . THR A 137 ? 0.3858 0.4897 0.3138 0.0905  0.0419  -0.0051 438 THR A CB  
1104  O OG1 . THR A 137 ? 0.3945 0.5050 0.3196 0.0854  0.0459  -0.0008 438 THR A OG1 
1105  C CG2 . THR A 137 ? 0.3934 0.4726 0.3048 0.0937  0.0366  -0.0117 438 THR A CG2 
1106  N N   . THR A 138 ? 0.2767 0.4085 0.2388 0.0646  0.0416  0.0081  439 THR A N   
1107  C CA  . THR A 138 ? 0.2602 0.4122 0.2326 0.0570  0.0468  0.0142  439 THR A CA  
1108  C C   . THR A 138 ? 0.2694 0.4165 0.2494 0.0448  0.0423  0.0170  439 THR A C   
1109  O O   . THR A 138 ? 0.2863 0.4147 0.2614 0.0427  0.0362  0.0151  439 THR A O   
1110  C CB  . THR A 138 ? 0.3448 0.5000 0.3074 0.0550  0.0534  0.0176  439 THR A CB  
1111  O OG1 . THR A 138 ? 0.3425 0.4771 0.2938 0.0499  0.0495  0.0181  439 THR A OG1 
1112  C CG2 . THR A 138 ? 0.3273 0.4854 0.2796 0.0676  0.0582  0.0145  439 THR A CG2 
1113  N N   . ALA A 139 ? 0.3522 0.5171 0.3439 0.0366  0.0452  0.0215  440 ALA A N   
1114  C CA  . ALA A 139 ? 0.3100 0.4684 0.3061 0.0244  0.0415  0.0242  440 ALA A CA  
1115  C C   . ALA A 139 ? 0.2711 0.4097 0.2534 0.0189  0.0409  0.0264  440 ALA A C   
1116  O O   . ALA A 139 ? 0.2539 0.3770 0.2342 0.0142  0.0356  0.0264  440 ALA A O   
1117  C CB  . ALA A 139 ? 0.2509 0.4319 0.2596 0.0149  0.0452  0.0286  440 ALA A CB  
1118  N N   . HIS A 140 ? 0.2787 0.4173 0.2501 0.0207  0.0463  0.0283  441 HIS A N   
1119  C CA  . HIS A 140 ? 0.3370 0.4556 0.2925 0.0180  0.0455  0.0303  441 HIS A CA  
1120  C C   . HIS A 140 ? 0.2886 0.3891 0.2376 0.0249  0.0380  0.0255  441 HIS A C   
1121  O O   . HIS A 140 ? 0.3685 0.4536 0.3116 0.0216  0.0337  0.0264  441 HIS A O   
1122  C CB  . HIS A 140 ? 0.2864 0.4087 0.2302 0.0203  0.0526  0.0328  441 HIS A CB  
1123  C CG  . HIS A 140 ? 0.3244 0.4564 0.2681 0.0090  0.0598  0.0394  441 HIS A CG  
1124  N ND1 . HIS A 140 ? 0.3490 0.5077 0.3055 0.0057  0.0659  0.0412  441 HIS A ND1 
1125  C CD2 . HIS A 140 ? 0.3871 0.5056 0.3182 -0.0002 0.0620  0.0448  441 HIS A CD2 
1126  C CE1 . HIS A 140 ? 0.3785 0.5409 0.3312 -0.0068 0.0717  0.0472  441 HIS A CE1 
1127  N NE2 . HIS A 140 ? 0.3864 0.5223 0.3224 -0.0107 0.0696  0.0496  441 HIS A NE2 
1128  N N   . GLY A 141 ? 0.2792 0.3814 0.2282 0.0346  0.0365  0.0201  442 GLY A N   
1129  C CA  . GLY A 141 ? 0.2630 0.3505 0.2074 0.0391  0.0293  0.0151  442 GLY A CA  
1130  C C   . GLY A 141 ? 0.3061 0.3898 0.2607 0.0348  0.0236  0.0141  442 GLY A C   
1131  O O   . GLY A 141 ? 0.3329 0.4048 0.2837 0.0344  0.0181  0.0124  442 GLY A O   
1132  N N   . MET A 142 ? 0.2959 0.3911 0.2635 0.0318  0.0248  0.0152  443 MET A N   
1133  C CA  . MET A 142 ? 0.2757 0.3670 0.2520 0.0274  0.0198  0.0145  443 MET A CA  
1134  C C   . MET A 142 ? 0.2744 0.3566 0.2471 0.0195  0.0185  0.0184  443 MET A C   
1135  O O   . MET A 142 ? 0.2777 0.3496 0.2504 0.0185  0.0134  0.0170  443 MET A O   
1136  C CB  . MET A 142 ? 0.2714 0.3781 0.2611 0.0260  0.0213  0.0153  443 MET A CB  
1137  C CG  . MET A 142 ? 0.3239 0.4367 0.3161 0.0354  0.0217  0.0114  443 MET A CG  
1138  S SD  . MET A 142 ? 0.3533 0.4875 0.3612 0.0349  0.0232  0.0131  443 MET A SD  
1139  C CE  . MET A 142 ? 0.2998 0.4246 0.3141 0.0283  0.0164  0.0126  443 MET A CE  
1140  N N   . PHE A 143 ? 0.3322 0.4173 0.3006 0.0140  0.0235  0.0233  444 PHE A N   
1141  C CA  . PHE A 143 ? 0.2746 0.3464 0.2350 0.0070  0.0229  0.0273  444 PHE A CA  
1142  C C   . PHE A 143 ? 0.3387 0.3940 0.2863 0.0126  0.0191  0.0260  444 PHE A C   
1143  O O   . PHE A 143 ? 0.3300 0.3732 0.2745 0.0115  0.0150  0.0262  444 PHE A O   
1144  C CB  . PHE A 143 ? 0.2632 0.3398 0.2184 -0.0004 0.0299  0.0328  444 PHE A CB  
1145  C CG  . PHE A 143 ? 0.4161 0.4741 0.3578 -0.0072 0.0300  0.0373  444 PHE A CG  
1146  C CD1 . PHE A 143 ? 0.3415 0.3879 0.2662 -0.0053 0.0328  0.0402  444 PHE A CD1 
1147  C CD2 . PHE A 143 ? 0.4050 0.4548 0.3488 -0.0147 0.0272  0.0384  444 PHE A CD2 
1148  C CE1 . PHE A 143 ? 0.4135 0.4391 0.3225 -0.0104 0.0329  0.0446  444 PHE A CE1 
1149  C CE2 . PHE A 143 ? 0.4165 0.4454 0.3447 -0.0202 0.0275  0.0423  444 PHE A CE2 
1150  C CZ  . PHE A 143 ? 0.4705 0.4865 0.3808 -0.0178 0.0304  0.0456  444 PHE A CZ  
1151  N N   . ASN A 144 ? 0.2669 0.3224 0.2062 0.0192  0.0204  0.0247  445 ASN A N   
1152  C CA  . ASN A 144 ? 0.2893 0.3331 0.2172 0.0254  0.0160  0.0228  445 ASN A CA  
1153  C C   . ASN A 144 ? 0.2576 0.2996 0.1926 0.0282  0.0091  0.0179  445 ASN A C   
1154  O O   . ASN A 144 ? 0.3365 0.3695 0.2667 0.0295  0.0049  0.0181  445 ASN A O   
1155  C CB  . ASN A 144 ? 0.3893 0.4365 0.3090 0.0320  0.0180  0.0208  445 ASN A CB  
1156  C CG  . ASN A 144 ? 0.5092 0.5462 0.4152 0.0377  0.0138  0.0197  445 ASN A CG  
1157  O OD1 . ASN A 144 ? 0.5755 0.6018 0.4724 0.0371  0.0127  0.0234  445 ASN A OD1 
1158  N ND2 . ASN A 144 ? 0.4890 0.5286 0.3920 0.0437  0.0111  0.0145  445 ASN A ND2 
1159  N N   . TYR A 145 ? 0.2580 0.3084 0.2033 0.0296  0.0081  0.0136  446 TYR A N   
1160  C CA  . TYR A 145 ? 0.3566 0.4055 0.3083 0.0306  0.0024  0.0092  446 TYR A CA  
1161  C C   . TYR A 145 ? 0.3508 0.3959 0.3084 0.0259  0.0004  0.0112  446 TYR A C   
1162  O O   . TYR A 145 ? 0.2739 0.3146 0.2313 0.0272  -0.0041 0.0093  446 TYR A O   
1163  C CB  . TYR A 145 ? 0.3223 0.3775 0.2816 0.0323  0.0026  0.0051  446 TYR A CB  
1164  C CG  . TYR A 145 ? 0.3178 0.3710 0.2696 0.0376  0.0012  0.0003  446 TYR A CG  
1165  C CD1 . TYR A 145 ? 0.3070 0.3637 0.2547 0.0417  0.0054  -0.0006 446 TYR A CD1 
1166  C CD2 . TYR A 145 ? 0.3423 0.3908 0.2905 0.0383  -0.0043 -0.0036 446 TYR A CD2 
1167  C CE1 . TYR A 145 ? 0.2991 0.3509 0.2372 0.0463  0.0039  -0.0056 446 TYR A CE1 
1168  C CE2 . TYR A 145 ? 0.3280 0.3740 0.2681 0.0414  -0.0061 -0.0085 446 TYR A CE2 
1169  C CZ  . TYR A 145 ? 0.3282 0.3740 0.2623 0.0453  -0.0021 -0.0096 446 TYR A CZ  
1170  O OH  . TYR A 145 ? 0.4100 0.4505 0.3335 0.0482  -0.0041 -0.0149 446 TYR A OH  
1171  N N   . ILE A 146 ? 0.3158 0.3637 0.2783 0.0202  0.0038  0.0148  447 ILE A N   
1172  C CA  . ILE A 146 ? 0.3535 0.3964 0.3201 0.0153  0.0018  0.0163  447 ILE A CA  
1173  C C   . ILE A 146 ? 0.3602 0.3893 0.3145 0.0154  0.0009  0.0192  447 ILE A C   
1174  O O   . ILE A 146 ? 0.3152 0.3375 0.2690 0.0164  -0.0028 0.0183  447 ILE A O   
1175  C CB  . ILE A 146 ? 0.3447 0.3955 0.3191 0.0082  0.0052  0.0190  447 ILE A CB  
1176  C CG1 . ILE A 146 ? 0.2947 0.3573 0.2811 0.0105  0.0044  0.0156  447 ILE A CG1 
1177  C CG2 . ILE A 146 ? 0.3440 0.3857 0.3174 0.0016  0.0038  0.0213  447 ILE A CG2 
1178  C CD1 . ILE A 146 ? 0.2674 0.3438 0.2625 0.0061  0.0078  0.0178  447 ILE A CD1 
1179  N N   . CYS A 147 ? 0.3203 0.3445 0.2631 0.0155  0.0042  0.0228  448 CYS A N   
1180  C CA  . CYS A 147 ? 0.3242 0.3324 0.2519 0.0174  0.0033  0.0258  448 CYS A CA  
1181  C C   . CYS A 147 ? 0.3644 0.3711 0.2893 0.0264  -0.0022 0.0223  448 CYS A C   
1182  O O   . CYS A 147 ? 0.3739 0.3708 0.2929 0.0293  -0.0050 0.0230  448 CYS A O   
1183  C CB  . CYS A 147 ? 0.3737 0.3763 0.2877 0.0166  0.0081  0.0303  448 CYS A CB  
1184  S SG  . CYS A 147 ? 0.4554 0.4576 0.3694 0.0038  0.0146  0.0355  448 CYS A SG  
1185  N N   . ASN A 148 ? 0.3021 0.3189 0.2303 0.0309  -0.0037 0.0185  449 ASN A N   
1186  C CA  . ASN A 148 ? 0.3040 0.3234 0.2312 0.0377  -0.0093 0.0146  449 ASN A CA  
1187  C C   . ASN A 148 ? 0.2445 0.2676 0.1828 0.0365  -0.0127 0.0116  449 ASN A C   
1188  O O   . ASN A 148 ? 0.3060 0.3280 0.2419 0.0413  -0.0165 0.0107  449 ASN A O   
1189  C CB  . ASN A 148 ? 0.2546 0.2832 0.1825 0.0404  -0.0101 0.0105  449 ASN A CB  
1190  C CG  . ASN A 148 ? 0.3813 0.4058 0.2955 0.0432  -0.0070 0.0134  449 ASN A CG  
1191  O OD1 . ASN A 148 ? 0.3391 0.3533 0.2418 0.0441  -0.0052 0.0184  449 ASN A OD1 
1192  N ND2 . ASN A 148 ? 0.3590 0.3898 0.2726 0.0446  -0.0062 0.0103  449 ASN A ND2 
1193  N N   . HIS A 149 ? 0.2589 0.2871 0.2090 0.0310  -0.0114 0.0101  450 HIS A N   
1194  C CA  . HIS A 149 ? 0.3171 0.3474 0.2767 0.0291  -0.0140 0.0078  450 HIS A CA  
1195  C C   . HIS A 149 ? 0.2867 0.3067 0.2411 0.0292  -0.0143 0.0109  450 HIS A C   
1196  O O   . HIS A 149 ? 0.2927 0.3126 0.2466 0.0334  -0.0175 0.0094  450 HIS A O   
1197  C CB  . HIS A 149 ? 0.2759 0.3111 0.2460 0.0238  -0.0120 0.0069  450 HIS A CB  
1198  C CG  . HIS A 149 ? 0.3241 0.3603 0.3028 0.0214  -0.0142 0.0049  450 HIS A CG  
1199  N ND1 . HIS A 149 ? 0.2763 0.3180 0.2629 0.0199  -0.0149 0.0016  450 HIS A ND1 
1200  C CD2 . HIS A 149 ? 0.2899 0.3209 0.2687 0.0204  -0.0155 0.0059  450 HIS A CD2 
1201  C CE1 . HIS A 149 ? 0.3329 0.3736 0.3246 0.0177  -0.0165 0.0009  450 HIS A CE1 
1202  N NE2 . HIS A 149 ? 0.2897 0.3247 0.2773 0.0181  -0.0169 0.0033  450 HIS A NE2 
1203  N N   . VAL A 150 ? 0.2516 0.2625 0.2007 0.0246  -0.0108 0.0153  451 VAL A N   
1204  C CA  . VAL A 150 ? 0.2691 0.2658 0.2101 0.0236  -0.0108 0.0181  451 VAL A CA  
1205  C C   . VAL A 150 ? 0.3706 0.3586 0.2983 0.0327  -0.0130 0.0190  451 VAL A C   
1206  O O   . VAL A 150 ? 0.2693 0.2507 0.1934 0.0367  -0.0151 0.0187  451 VAL A O   
1207  C CB  . VAL A 150 ? 0.3196 0.3076 0.2547 0.0153  -0.0065 0.0227  451 VAL A CB  
1208  C CG1 . VAL A 150 ? 0.2753 0.2425 0.1957 0.0144  -0.0064 0.0259  451 VAL A CG1 
1209  C CG2 . VAL A 150 ? 0.2895 0.2889 0.2390 0.0075  -0.0053 0.0216  451 VAL A CG2 
1210  N N   . LYS A 151 ? 0.3785 0.3667 0.2979 0.0372  -0.0126 0.0202  452 LYS A N   
1211  C CA  . LYS A 151 ? 0.3625 0.3432 0.2680 0.0473  -0.0151 0.0213  452 LYS A CA  
1212  C C   . LYS A 151 ? 0.3082 0.3036 0.2224 0.0543  -0.0201 0.0165  452 LYS A C   
1213  O O   . LYS A 151 ? 0.2980 0.2892 0.2060 0.0621  -0.0225 0.0168  452 LYS A O   
1214  C CB  . LYS A 151 ? 0.4361 0.4144 0.3300 0.0505  -0.0138 0.0237  452 LYS A CB  
1215  C CG  . LYS A 151 ? 0.3901 0.3582 0.2665 0.0618  -0.0162 0.0259  452 LYS A CG  
1216  C CD  . LYS A 151 ? 0.4455 0.4099 0.3089 0.0639  -0.0144 0.0287  452 LYS A CD  
1217  C CE  . LYS A 151 ? 0.5060 0.4539 0.3472 0.0747  -0.0159 0.0326  452 LYS A CE  
1218  N NZ  . LYS A 151 ? 0.5039 0.4438 0.3292 0.0759  -0.0132 0.0364  452 LYS A NZ  
1219  N N   . TYR A 152 ? 0.2689 0.2814 0.1964 0.0517  -0.0216 0.0121  453 TYR A N   
1220  C CA  . TYR A 152 ? 0.3507 0.3787 0.2875 0.0552  -0.0260 0.0074  453 TYR A CA  
1221  C C   . TYR A 152 ? 0.2402 0.2676 0.1839 0.0538  -0.0262 0.0066  453 TYR A C   
1222  O O   . TYR A 152 ? 0.3300 0.3626 0.2732 0.0606  -0.0289 0.0054  453 TYR A O   
1223  C CB  . TYR A 152 ? 0.2471 0.2886 0.1948 0.0499  -0.0269 0.0028  453 TYR A CB  
1224  C CG  . TYR A 152 ? 0.3404 0.3976 0.2976 0.0505  -0.0310 -0.0021 453 TYR A CG  
1225  C CD1 . TYR A 152 ? 0.3696 0.4389 0.3243 0.0560  -0.0352 -0.0045 453 TYR A CD1 
1226  C CD2 . TYR A 152 ? 0.2839 0.3447 0.2521 0.0452  -0.0306 -0.0041 453 TYR A CD2 
1227  C CE1 . TYR A 152 ? 0.3961 0.4824 0.3601 0.0551  -0.0387 -0.0089 453 TYR A CE1 
1228  C CE2 . TYR A 152 ? 0.3166 0.3921 0.2928 0.0445  -0.0336 -0.0082 453 TYR A CE2 
1229  C CZ  . TYR A 152 ? 0.3885 0.4776 0.3631 0.0489  -0.0376 -0.0107 453 TYR A CZ  
1230  O OH  . TYR A 152 ? 0.5189 0.6255 0.5024 0.0466  -0.0404 -0.0148 453 TYR A OH  
1231  N N   . ALA A 153 ? 0.2793 0.3020 0.2295 0.0455  -0.0235 0.0070  454 ALA A N   
1232  C CA  . ALA A 153 ? 0.2909 0.3130 0.2475 0.0433  -0.0237 0.0059  454 ALA A CA  
1233  C C   . ALA A 153 ? 0.3007 0.3086 0.2452 0.0492  -0.0235 0.0088  454 ALA A C   
1234  O O   . ALA A 153 ? 0.3903 0.4010 0.3369 0.0530  -0.0248 0.0072  454 ALA A O   
1235  C CB  . ALA A 153 ? 0.2188 0.2378 0.1825 0.0339  -0.0211 0.0064  454 ALA A CB  
1236  N N   . THR A 154 ? 0.3795 0.3705 0.3096 0.0498  -0.0215 0.0131  455 THR A N   
1237  C CA  . THR A 154 ? 0.3846 0.3563 0.2991 0.0550  -0.0210 0.0160  455 THR A CA  
1238  C C   . THR A 154 ? 0.4240 0.3995 0.3312 0.0690  -0.0239 0.0153  455 THR A C   
1239  O O   . THR A 154 ? 0.3425 0.3162 0.2474 0.0755  -0.0249 0.0143  455 THR A O   
1240  C CB  . THR A 154 ? 0.4158 0.3666 0.3149 0.0504  -0.0177 0.0209  455 THR A CB  
1241  O OG1 . THR A 154 ? 0.3481 0.2993 0.2558 0.0375  -0.0152 0.0213  455 THR A OG1 
1242  C CG2 . THR A 154 ? 0.3603 0.2859 0.2383 0.0563  -0.0172 0.0240  455 THR A CG2 
1243  N N   . ASN A 155 ? 0.3951 0.3770 0.2982 0.0744  -0.0254 0.0158  456 ASN A N   
1244  C CA  . ASN A 155 ? 0.3978 0.3905 0.2973 0.0879  -0.0292 0.0145  456 ASN A CA  
1245  C C   . ASN A 155 ? 0.4231 0.3964 0.3043 0.0990  -0.0290 0.0174  456 ASN A C   
1246  O O   . ASN A 155 ? 0.4065 0.3897 0.2896 0.1089  -0.0312 0.0153  456 ASN A O   
1247  C CB  . ASN A 155 ? 0.4039 0.4240 0.3231 0.0872  -0.0320 0.0090  456 ASN A CB  
1248  C CG  . ASN A 155 ? 0.4700 0.5089 0.3890 0.0995  -0.0364 0.0071  456 ASN A CG  
1249  O OD1 . ASN A 155 ? 0.4561 0.4939 0.3648 0.1064  -0.0383 0.0088  456 ASN A OD1 
1250  N ND2 . ASN A 155 ? 0.3373 0.3952 0.2679 0.1021  -0.0381 0.0036  456 ASN A ND2 
1251  N N   . LYS A 156 ? 0.3738 0.3186 0.2365 0.0966  -0.0259 0.0221  457 LYS A N   
1252  C CA  . LYS A 156 ? 0.4146 0.3328 0.2539 0.1064  -0.0251 0.0255  457 LYS A CA  
1253  C C   . LYS A 156 ? 0.4408 0.3574 0.2831 0.1090  -0.0252 0.0231  457 LYS A C   
1254  O O   . LYS A 156 ? 0.5154 0.4216 0.3430 0.1231  -0.0261 0.0237  457 LYS A O   
1255  C CB  . LYS A 156 ? 0.4128 0.3316 0.2377 0.1237  -0.0281 0.0270  457 LYS A CB  
1256  C CG  . LYS A 156 ? 0.5040 0.4224 0.3229 0.1221  -0.0281 0.0296  457 LYS A CG  
1257  C CD  . LYS A 156 ? 0.5982 0.5189 0.4028 0.1404  -0.0320 0.0310  457 LYS A CD  
1258  C CE  . LYS A 156 ? 0.7219 0.6361 0.5150 0.1395  -0.0315 0.0344  457 LYS A CE  
1259  N NZ  . LYS A 156 ? 0.7475 0.6301 0.5246 0.1280  -0.0257 0.0395  457 LYS A NZ  
1260  N N   . GLY A 157 ? 0.4488 0.3753 0.3088 0.0966  -0.0241 0.0203  458 GLY A N   
1261  C CA  . GLY A 157 ? 0.4044 0.3277 0.2666 0.0970  -0.0236 0.0181  458 GLY A CA  
1262  C C   . GLY A 157 ? 0.4248 0.3786 0.3071 0.1008  -0.0257 0.0134  458 GLY A C   
1263  O O   . GLY A 157 ? 0.4384 0.3935 0.3263 0.0986  -0.0248 0.0113  458 GLY A O   
1264  N N   . ASN A 158 ? 0.3817 0.3600 0.2742 0.1059  -0.0284 0.0117  459 ASN A N   
1265  C CA  . ASN A 158 ? 0.3917 0.4014 0.3046 0.1059  -0.0302 0.0071  459 ASN A CA  
1266  C C   . ASN A 158 ? 0.4114 0.4323 0.3417 0.0901  -0.0297 0.0051  459 ASN A C   
1267  O O   . ASN A 158 ? 0.4126 0.4502 0.3517 0.0874  -0.0317 0.0034  459 ASN A O   
1268  C CB  . ASN A 158 ? 0.3711 0.4020 0.2850 0.1185  -0.0338 0.0059  459 ASN A CB  
1269  C CG  . ASN A 158 ? 0.5125 0.5765 0.4458 0.1185  -0.0355 0.0012  459 ASN A CG  
1270  O OD1 . ASN A 158 ? 0.4659 0.5329 0.4074 0.1132  -0.0334 -0.0006 459 ASN A OD1 
1271  N ND2 . ASN A 158 ? 0.5646 0.6540 0.5045 0.1238  -0.0392 -0.0007 459 ASN A ND2 
1272  N N   . LEU A 159 ? 0.3201 0.3305 0.2538 0.0800  -0.0273 0.0051  460 LEU A N   
1273  C CA  . LEU A 159 ? 0.3454 0.3601 0.2910 0.0664  -0.0265 0.0043  460 LEU A CA  
1274  C C   . LEU A 159 ? 0.2973 0.3376 0.2599 0.0630  -0.0282 0.0001  460 LEU A C   
1275  O O   . LEU A 159 ? 0.3378 0.3932 0.3069 0.0667  -0.0292 -0.0025 460 LEU A O   
1276  C CB  . LEU A 159 ? 0.3021 0.3041 0.2488 0.0576  -0.0243 0.0048  460 LEU A CB  
1277  C CG  . LEU A 159 ? 0.5374 0.5126 0.4670 0.0576  -0.0226 0.0083  460 LEU A CG  
1278  C CD1 . LEU A 159 ? 0.5605 0.5281 0.4941 0.0454  -0.0212 0.0086  460 LEU A CD1 
1279  C CD2 . LEU A 159 ? 0.4393 0.4026 0.3561 0.0597  -0.0221 0.0118  460 LEU A CD2 
1280  N N   . ARG A 160 ? 0.2616 0.3060 0.2302 0.0554  -0.0283 -0.0006 461 ARG A N   
1281  C CA  . ARG A 160 ? 0.2305 0.2941 0.2117 0.0505  -0.0299 -0.0045 461 ARG A CA  
1282  C C   . ARG A 160 ? 0.3055 0.3638 0.2926 0.0400  -0.0281 -0.0049 461 ARG A C   
1283  O O   . ARG A 160 ? 0.2801 0.3269 0.2624 0.0376  -0.0265 -0.0023 461 ARG A O   
1284  C CB  . ARG A 160 ? 0.2811 0.3546 0.2600 0.0543  -0.0325 -0.0055 461 ARG A CB  
1285  C CG  . ARG A 160 ? 0.3712 0.4541 0.3449 0.0662  -0.0352 -0.0054 461 ARG A CG  
1286  C CD  . ARG A 160 ? 0.3507 0.4450 0.3225 0.0690  -0.0385 -0.0068 461 ARG A CD  
1287  N NE  . ARG A 160 ? 0.3323 0.4093 0.2910 0.0718  -0.0374 -0.0030 461 ARG A NE  
1288  C CZ  . ARG A 160 ? 0.3974 0.4788 0.3487 0.0779  -0.0401 -0.0027 461 ARG A CZ  
1289  N NH1 . ARG A 160 ? 0.3754 0.4795 0.3322 0.0815  -0.0446 -0.0063 461 ARG A NH1 
1290  N NH2 . ARG A 160 ? 0.2848 0.3492 0.2229 0.0798  -0.0384 0.0013  461 ARG A NH2 
1291  N N   . SER A 161 ? 0.2673 0.3341 0.2639 0.0340  -0.0281 -0.0079 462 SER A N   
1292  C CA  A SER A 161 ? 0.2940 0.3549 0.2947 0.0259  -0.0266 -0.0081 462 SER A CA  
1293  C CA  B SER A 161 ? 0.2944 0.3554 0.2951 0.0259  -0.0266 -0.0081 462 SER A CA  
1294  C C   . SER A 161 ? 0.3111 0.3738 0.3113 0.0238  -0.0271 -0.0093 462 SER A C   
1295  O O   . SER A 161 ? 0.2541 0.3269 0.2547 0.0247  -0.0292 -0.0119 462 SER A O   
1296  C CB  A SER A 161 ? 0.2481 0.3151 0.2561 0.0206  -0.0265 -0.0108 462 SER A CB  
1297  C CB  B SER A 161 ? 0.2480 0.3150 0.2560 0.0206  -0.0264 -0.0107 462 SER A CB  
1298  O OG  A SER A 161 ? 0.1978 0.2792 0.2098 0.0189  -0.0282 -0.0143 462 SER A OG  
1299  O OG  B SER A 161 ? 0.1926 0.2594 0.2003 0.0235  -0.0258 -0.0100 462 SER A OG  
1300  N N   . ALA A 162 ? 0.2406 0.2945 0.2397 0.0210  -0.0252 -0.0075 463 ALA A N   
1301  C CA  . ALA A 162 ? 0.2206 0.2753 0.2179 0.0202  -0.0249 -0.0085 463 ALA A CA  
1302  C C   . ALA A 162 ? 0.2920 0.3410 0.2915 0.0166  -0.0227 -0.0078 463 ALA A C   
1303  O O   . ALA A 162 ? 0.2182 0.2628 0.2199 0.0149  -0.0215 -0.0054 463 ALA A O   
1304  C CB  . ALA A 162 ? 0.2330 0.2851 0.2224 0.0251  -0.0246 -0.0060 463 ALA A CB  
1305  N N   . ILE A 163 ? 0.2193 0.2687 0.2173 0.0160  -0.0224 -0.0100 464 ILE A N   
1306  C CA  . ILE A 163 ? 0.2241 0.2696 0.2229 0.0152  -0.0201 -0.0092 464 ILE A CA  
1307  C C   . ILE A 163 ? 0.3041 0.3497 0.2971 0.0182  -0.0190 -0.0099 464 ILE A C   
1308  O O   . ILE A 163 ? 0.2511 0.2981 0.2396 0.0188  -0.0208 -0.0129 464 ILE A O   
1309  C CB  . ILE A 163 ? 0.1931 0.2352 0.1938 0.0123  -0.0207 -0.0118 464 ILE A CB  
1310  C CG1 . ILE A 163 ? 0.1828 0.2216 0.1835 0.0140  -0.0185 -0.0107 464 ILE A CG1 
1311  C CG2 . ILE A 163 ? 0.1866 0.2282 0.1830 0.0102  -0.0225 -0.0164 464 ILE A CG2 
1312  C CD1 . ILE A 163 ? 0.2042 0.2370 0.2054 0.0123  -0.0189 -0.0119 464 ILE A CD1 
1313  N N   . THR A 164 ? 0.2444 0.2902 0.2375 0.0197  -0.0159 -0.0071 465 THR A N   
1314  C CA  . THR A 164 ? 0.2799 0.3264 0.2674 0.0231  -0.0137 -0.0076 465 THR A CA  
1315  C C   . THR A 164 ? 0.3095 0.3551 0.2983 0.0249  -0.0117 -0.0084 465 THR A C   
1316  O O   . THR A 164 ? 0.2870 0.3360 0.2821 0.0241  -0.0104 -0.0059 465 THR A O   
1317  C CB  . THR A 164 ? 0.2665 0.3154 0.2517 0.0240  -0.0110 -0.0032 465 THR A CB  
1318  O OG1 . THR A 164 ? 0.2728 0.3198 0.2540 0.0242  -0.0132 -0.0024 465 THR A OG1 
1319  C CG2 . THR A 164 ? 0.2789 0.3296 0.2579 0.0278  -0.0080 -0.0035 465 THR A CG2 
1320  N N   . ILE A 165 ? 0.2300 0.2708 0.2116 0.0276  -0.0118 -0.0122 466 ILE A N   
1321  C CA  . ILE A 165 ? 0.2805 0.3169 0.2602 0.0309  -0.0104 -0.0138 466 ILE A CA  
1322  C C   . ILE A 165 ? 0.2524 0.2907 0.2260 0.0374  -0.0068 -0.0138 466 ILE A C   
1323  O O   . ILE A 165 ? 0.3265 0.3596 0.2904 0.0391  -0.0070 -0.0169 466 ILE A O   
1324  C CB  . ILE A 165 ? 0.3782 0.4028 0.3515 0.0285  -0.0132 -0.0184 466 ILE A CB  
1325  C CG1 . ILE A 165 ? 0.2956 0.3209 0.2758 0.0223  -0.0159 -0.0179 466 ILE A CG1 
1326  C CG2 . ILE A 165 ? 0.3790 0.3950 0.3469 0.0334  -0.0117 -0.0196 466 ILE A CG2 
1327  C CD1 . ILE A 165 ? 0.2665 0.2823 0.2407 0.0174  -0.0184 -0.0222 466 ILE A CD1 
1328  N N   . PHE A 166 ? 0.3181 0.3653 0.2974 0.0408  -0.0034 -0.0106 467 PHE A N   
1329  C CA  . PHE A 166 ? 0.2808 0.3337 0.2562 0.0477  0.0010  -0.0101 467 PHE A CA  
1330  C C   . PHE A 166 ? 0.3239 0.3683 0.2915 0.0554  0.0017  -0.0135 467 PHE A C   
1331  O O   . PHE A 166 ? 0.3460 0.3793 0.3111 0.0543  -0.0012 -0.0157 467 PHE A O   
1332  C CB  . PHE A 166 ? 0.3216 0.3912 0.3077 0.0467  0.0043  -0.0049 467 PHE A CB  
1333  C CG  . PHE A 166 ? 0.3522 0.4254 0.3407 0.0398  0.0045  -0.0016 467 PHE A CG  
1334  C CD1 . PHE A 166 ? 0.3116 0.3851 0.2927 0.0409  0.0070  -0.0009 467 PHE A CD1 
1335  C CD2 . PHE A 166 ? 0.3313 0.4052 0.3271 0.0329  0.0022  0.0009  467 PHE A CD2 
1336  C CE1 . PHE A 166 ? 0.3565 0.4300 0.3367 0.0355  0.0072  0.0025  467 PHE A CE1 
1337  C CE2 . PHE A 166 ? 0.3526 0.4259 0.3473 0.0276  0.0024  0.0039  467 PHE A CE2 
1338  C CZ  . PHE A 166 ? 0.2893 0.3619 0.2759 0.0290  0.0050  0.0050  467 PHE A CZ  
1339  N N   . PRO A 167 ? 0.3528 0.4003 0.3140 0.0637  0.0058  -0.0141 468 PRO A N   
1340  C CA  . PRO A 167 ? 0.3650 0.4001 0.3145 0.0728  0.0066  -0.0178 468 PRO A CA  
1341  C C   . PRO A 167 ? 0.3248 0.3600 0.2793 0.0761  0.0056  -0.0167 468 PRO A C   
1342  O O   . PRO A 167 ? 0.3146 0.3675 0.2829 0.0759  0.0065  -0.0125 468 PRO A O   
1343  C CB  . PRO A 167 ? 0.3831 0.4279 0.3284 0.0821  0.0122  -0.0172 468 PRO A CB  
1344  C CG  . PRO A 167 ? 0.3328 0.3848 0.2799 0.0760  0.0132  -0.0155 468 PRO A CG  
1345  C CD  . PRO A 167 ? 0.3274 0.3856 0.2876 0.0654  0.0100  -0.0121 468 PRO A CD  
1346  N N   . GLN A 168 ? 0.3654 0.3796 0.3071 0.0789  0.0035  -0.0204 469 GLN A N   
1347  C CA  . GLN A 168 ? 0.3755 0.3854 0.3180 0.0831  0.0022  -0.0195 469 GLN A CA  
1348  C C   . GLN A 168 ? 0.4469 0.4711 0.3921 0.0964  0.0060  -0.0174 469 GLN A C   
1349  O O   . GLN A 168 ? 0.3428 0.3750 0.2848 0.1037  0.0101  -0.0177 469 GLN A O   
1350  C CB  . GLN A 168 ? 0.3374 0.3182 0.2611 0.0838  0.0001  -0.0240 469 GLN A CB  
1351  C CG  . GLN A 168 ? 0.3770 0.3430 0.2816 0.0934  0.0027  -0.0280 469 GLN A CG  
1352  C CD  . GLN A 168 ? 0.4017 0.3387 0.2873 0.0870  0.0000  -0.0333 469 GLN A CD  
1353  O OE1 . GLN A 168 ? 0.4594 0.3959 0.3488 0.0740  -0.0030 -0.0345 469 GLN A OE1 
1354  N NE2 . GLN A 168 ? 0.4271 0.3397 0.2913 0.0958  0.0011  -0.0365 469 GLN A NE2 
1355  N N   . ARG A 169 ? 0.4320 0.4606 0.3828 0.1001  0.0046  -0.0152 470 ARG A N   
1356  C CA  . ARG A 169 ? 0.4153 0.4588 0.3684 0.1143  0.0074  -0.0133 470 ARG A CA  
1357  C C   . ARG A 169 ? 0.4279 0.4505 0.3592 0.1284  0.0096  -0.0172 470 ARG A C   
1358  O O   . ARG A 169 ? 0.4576 0.4498 0.3711 0.1267  0.0075  -0.0209 470 ARG A O   
1359  C CB  . ARG A 169 ? 0.5608 0.6113 0.5225 0.1153  0.0042  -0.0105 470 ARG A CB  
1360  C CG  . ARG A 169 ? 0.6782 0.7391 0.6380 0.1326  0.0058  -0.0093 470 ARG A CG  
1361  C CD  . ARG A 169 ? 0.6963 0.7698 0.6672 0.1326  0.0021  -0.0061 470 ARG A CD  
1362  N NE  . ARG A 169 ? 0.6181 0.7198 0.6109 0.1206  0.0014  -0.0027 470 ARG A NE  
1363  C CZ  . ARG A 169 ? 0.6959 0.7970 0.6967 0.1087  -0.0027 -0.0012 470 ARG A CZ  
1364  N NH1 . ARG A 169 ? 0.7156 0.7917 0.7056 0.1072  -0.0062 -0.0025 470 ARG A NH1 
1365  N NH2 . ARG A 169 ? 0.7638 0.8880 0.7817 0.0980  -0.0030 0.0017  470 ARG A NH2 
1366  N N   . THR A 170 ? 0.4616 0.5004 0.3931 0.1419  0.0142  -0.0165 471 THR A N   
1367  C CA  . THR A 170 ? 0.5111 0.5302 0.4202 0.1578  0.0170  -0.0202 471 THR A CA  
1368  C C   . THR A 170 ? 0.5945 0.6212 0.5023 0.1751  0.0176  -0.0184 471 THR A C   
1369  O O   . THR A 170 ? 0.6686 0.6710 0.5625 0.1799  0.0146  -0.0195 471 THR A O   
1370  C CB  . THR A 170 ? 0.5446 0.5734 0.4506 0.1625  0.0224  -0.0215 471 THR A CB  
1371  O OG1 . THR A 170 ? 0.5634 0.6316 0.4914 0.1631  0.0258  -0.0169 471 THR A OG1 
1372  C CG2 . THR A 170 ? 0.5089 0.5240 0.4102 0.1478  0.0209  -0.0241 471 THR A CG2 
1373  N N   . ASP A 171 ? 0.6718 0.7328 0.5935 0.1846  0.0216  -0.0156 472 ASP A N   
1374  C CA  . ASP A 171 ? 0.7138 0.7900 0.6379 0.2017  0.0219  -0.0134 472 ASP A CA  
1375  C C   . ASP A 171 ? 0.7526 0.8616 0.7026 0.1940  0.0188  -0.0085 472 ASP A C   
1376  O O   . ASP A 171 ? 0.8221 0.9440 0.7752 0.2064  0.0174  -0.0066 472 ASP A O   
1377  C CB  . ASP A 171 ? 0.7471 0.8430 0.6688 0.2199  0.0285  -0.0137 472 ASP A CB  
1378  C CG  . ASP A 171 ? 0.7610 0.8947 0.7043 0.2113  0.0329  -0.0110 472 ASP A CG  
1379  O OD1 . ASP A 171 ? 0.7080 0.8502 0.6667 0.1916  0.0306  -0.0089 472 ASP A OD1 
1380  O OD2 . ASP A 171 ? 0.7627 0.9168 0.7062 0.2245  0.0390  -0.0109 472 ASP A OD2 
1381  N N   . GLY A 172 ? 0.5925 0.7142 0.5595 0.1744  0.0176  -0.0066 473 GLY A N   
1382  C CA  . GLY A 172 ? 0.5294 0.6806 0.5193 0.1653  0.0148  -0.0024 473 GLY A CA  
1383  C C   . GLY A 172 ? 0.4942 0.6869 0.5035 0.1634  0.0193  0.0006  473 GLY A C   
1384  O O   . GLY A 172 ? 0.5454 0.7619 0.5734 0.1514  0.0172  0.0039  473 GLY A O   
1385  N N   . LYS A 173 ? 0.5564 0.7581 0.5607 0.1743  0.0255  -0.0004 474 LYS A N   
1386  C CA  . LYS A 173 ? 0.6639 0.9043 0.6853 0.1708  0.0309  0.0026  474 LYS A CA  
1387  C C   . LYS A 173 ? 0.6610 0.8941 0.6814 0.1560  0.0340  0.0025  474 LYS A C   
1388  O O   . LYS A 173 ? 0.6204 0.8821 0.6539 0.1491  0.0385  0.0055  474 LYS A O   
1389  C CB  . LYS A 173 ? 0.7665 1.0254 0.7836 0.1924  0.0369  0.0020  474 LYS A CB  
1390  C CG  . LYS A 173 ? 0.8831 1.1644 0.9070 0.2081  0.0348  0.0035  474 LYS A CG  
1391  C CD  . LYS A 173 ? 0.9784 1.2972 1.0102 0.2190  0.0409  0.0052  474 LYS A CD  
1392  C CE  . LYS A 173 ? 1.0239 1.3484 1.0505 0.2340  0.0375  0.0059  474 LYS A CE  
1393  N NZ  . LYS A 173 ? 1.0487 1.3322 1.0461 0.2523  0.0369  0.0022  474 LYS A NZ  
1394  N N   . HIS A 174 ? 0.5960 0.7923 0.6009 0.1506  0.0315  -0.0006 475 HIS A N   
1395  C CA  . HIS A 174 ? 0.5455 0.7328 0.5468 0.1388  0.0336  -0.0010 475 HIS A CA  
1396  C C   . HIS A 174 ? 0.4694 0.6396 0.4734 0.1215  0.0279  -0.0007 475 HIS A C   
1397  O O   . HIS A 174 ? 0.5129 0.6614 0.5067 0.1151  0.0271  -0.0028 475 HIS A O   
1398  C CB  . HIS A 174 ? 0.6297 0.7917 0.6088 0.1491  0.0363  -0.0056 475 HIS A CB  
1399  C CG  . HIS A 174 ? 0.7592 0.9374 0.7337 0.1669  0.0429  -0.0061 475 HIS A CG  
1400  N ND1 . HIS A 174 ? 0.7750 0.9636 0.7497 0.1837  0.0433  -0.0061 475 HIS A ND1 
1401  C CD2 . HIS A 174 ? 0.7417 0.9277 0.7105 0.1717  0.0496  -0.0066 475 HIS A CD2 
1402  C CE1 . HIS A 174 ? 0.7360 0.9393 0.7058 0.1985  0.0501  -0.0067 475 HIS A CE1 
1403  N NE2 . HIS A 174 ? 0.7643 0.9663 0.7305 0.1912  0.0543  -0.0071 475 HIS A NE2 
1404  N N   . ASP A 175 ? 0.3808 0.5617 0.3983 0.1144  0.0239  0.0019  476 ASP A N   
1405  C CA  . ASP A 175 ? 0.3208 0.4845 0.3395 0.1001  0.0185  0.0019  476 ASP A CA  
1406  C C   . ASP A 175 ? 0.3389 0.5047 0.3613 0.0862  0.0201  0.0038  476 ASP A C   
1407  O O   . ASP A 175 ? 0.3866 0.5753 0.4177 0.0825  0.0245  0.0070  476 ASP A O   
1408  C CB  . ASP A 175 ? 0.3630 0.5388 0.3944 0.0957  0.0141  0.0043  476 ASP A CB  
1409  C CG  . ASP A 175 ? 0.3819 0.5449 0.4057 0.1072  0.0106  0.0024  476 ASP A CG  
1410  O OD1 . ASP A 175 ? 0.4230 0.5681 0.4311 0.1192  0.0120  -0.0007 476 ASP A OD1 
1411  O OD2 . ASP A 175 ? 0.4640 0.6332 0.4957 0.1040  0.0064  0.0041  476 ASP A OD2 
1412  N N   . PHE A 176 ? 0.2653 0.4073 0.2801 0.0786  0.0167  0.0019  477 PHE A N   
1413  C CA  . PHE A 176 ? 0.2711 0.4121 0.2894 0.0652  0.0163  0.0041  477 PHE A CA  
1414  C C   . PHE A 176 ? 0.3027 0.4465 0.3311 0.0556  0.0119  0.0062  477 PHE A C   
1415  O O   . PHE A 176 ? 0.3128 0.4440 0.3392 0.0568  0.0075  0.0043  477 PHE A O   
1416  C CB  . PHE A 176 ? 0.2287 0.3456 0.2340 0.0633  0.0144  0.0009  477 PHE A CB  
1417  C CG  . PHE A 176 ? 0.2383 0.3531 0.2330 0.0695  0.0187  -0.0007 477 PHE A CG  
1418  C CD1 . PHE A 176 ? 0.3038 0.4150 0.2896 0.0823  0.0209  -0.0038 477 PHE A CD1 
1419  C CD2 . PHE A 176 ? 0.2654 0.3811 0.2575 0.0635  0.0209  0.0011  477 PHE A CD2 
1420  C CE1 . PHE A 176 ? 0.3711 0.4797 0.3457 0.0885  0.0250  -0.0055 477 PHE A CE1 
1421  C CE2 . PHE A 176 ? 0.3731 0.4872 0.3544 0.0695  0.0249  -0.0003 477 PHE A CE2 
1422  C CZ  . PHE A 176 ? 0.4036 0.5145 0.3765 0.0818  0.0270  -0.0038 477 PHE A CZ  
1423  N N   . ARG A 177 ? 0.2415 0.4002 0.2790 0.0457  0.0134  0.0101  478 ARG A N   
1424  C CA  . ARG A 177 ? 0.3650 0.5243 0.4099 0.0360  0.0092  0.0117  478 ARG A CA  
1425  C C   . ARG A 177 ? 0.3127 0.4690 0.3570 0.0233  0.0102  0.0146  478 ARG A C   
1426  O O   . ARG A 177 ? 0.3516 0.5189 0.3964 0.0200  0.0149  0.0172  478 ARG A O   
1427  C CB  . ARG A 177 ? 0.2825 0.4661 0.3398 0.0367  0.0089  0.0137  478 ARG A CB  
1428  C CG  . ARG A 177 ? 0.2923 0.4777 0.3490 0.0502  0.0071  0.0114  478 ARG A CG  
1429  C CD  . ARG A 177 ? 0.3416 0.5030 0.3916 0.0504  0.0018  0.0090  478 ARG A CD  
1430  N NE  . ARG A 177 ? 0.3027 0.4642 0.3588 0.0395  -0.0023 0.0105  478 ARG A NE  
1431  C CZ  . ARG A 177 ? 0.3793 0.5537 0.4431 0.0396  -0.0054 0.0116  478 ARG A CZ  
1432  N NH1 . ARG A 177 ? 0.3197 0.5098 0.3869 0.0510  -0.0051 0.0117  478 ARG A NH1 
1433  N NH2 . ARG A 177 ? 0.2858 0.4573 0.3527 0.0291  -0.0091 0.0126  478 ARG A NH2 
1434  N N   . VAL A 178 ? 0.2439 0.3847 0.2859 0.0167  0.0060  0.0142  479 VAL A N   
1435  C CA  . VAL A 178 ? 0.2849 0.4224 0.3263 0.0048  0.0060  0.0172  479 VAL A CA  
1436  C C   . VAL A 178 ? 0.3331 0.4846 0.3843 -0.0018 0.0040  0.0188  479 VAL A C   
1437  O O   . VAL A 178 ? 0.3095 0.4566 0.3631 -0.0004 -0.0005 0.0171  479 VAL A O   
1438  C CB  . VAL A 178 ? 0.2363 0.3506 0.2690 0.0026  0.0026  0.0158  479 VAL A CB  
1439  C CG1 . VAL A 178 ? 0.2149 0.3228 0.2440 -0.0083 0.0028  0.0189  479 VAL A CG1 
1440  C CG2 . VAL A 178 ? 0.2495 0.3532 0.2732 0.0092  0.0038  0.0138  479 VAL A CG2 
1441  N N   . TRP A 179 ? 0.2942 0.4641 0.3512 -0.0092 0.0074  0.0220  480 TRP A N   
1442  C CA  . TRP A 179 ? 0.2558 0.4422 0.3226 -0.0163 0.0050  0.0232  480 TRP A CA  
1443  C C   . TRP A 179 ? 0.3041 0.4733 0.3659 -0.0273 0.0010  0.0235  480 TRP A C   
1444  O O   . TRP A 179 ? 0.2989 0.4752 0.3666 -0.0315 -0.0030 0.0232  480 TRP A O   
1445  C CB  . TRP A 179 ? 0.2647 0.4781 0.3395 -0.0232 0.0098  0.0264  480 TRP A CB  
1446  C CG  . TRP A 179 ? 0.2570 0.4942 0.3398 -0.0110 0.0129  0.0259  480 TRP A CG  
1447  C CD1 . TRP A 179 ? 0.1832 0.4131 0.2609 0.0039  0.0144  0.0234  480 TRP A CD1 
1448  C CD2 . TRP A 179 ? 0.2251 0.4976 0.3216 -0.0120 0.0150  0.0276  480 TRP A CD2 
1449  N NE1 . TRP A 179 ? 0.3166 0.5728 0.4024 0.0134  0.0176  0.0235  480 TRP A NE1 
1450  C CE2 . TRP A 179 ? 0.1989 0.4835 0.2973 0.0045  0.0180  0.0261  480 TRP A CE2 
1451  C CE3 . TRP A 179 ? 0.3139 0.6097 0.4206 -0.0254 0.0145  0.0300  480 TRP A CE3 
1452  C CZ2 . TRP A 179 ? 0.2091 0.5300 0.3202 0.0098  0.0208  0.0272  480 TRP A CZ2 
1453  C CZ3 . TRP A 179 ? 0.2666 0.6009 0.3875 -0.0218 0.0169  0.0310  480 TRP A CZ3 
1454  C CH2 . TRP A 179 ? 0.2735 0.6208 0.3969 -0.0035 0.0201  0.0298  480 TRP A CH2 
1455  N N   . ASN A 180 ? 0.2946 0.4409 0.3445 -0.0308 0.0017  0.0240  481 ASN A N   
1456  C CA  . ASN A 180 ? 0.3025 0.4289 0.3449 -0.0383 -0.0019 0.0239  481 ASN A CA  
1457  C C   . ASN A 180 ? 0.3538 0.4718 0.3974 -0.0312 -0.0069 0.0206  481 ASN A C   
1458  O O   . ASN A 180 ? 0.3123 0.4274 0.3560 -0.0205 -0.0071 0.0183  481 ASN A O   
1459  C CB  . ASN A 180 ? 0.3122 0.4160 0.3403 -0.0396 0.0000  0.0250  481 ASN A CB  
1460  C CG  . ASN A 180 ? 0.2765 0.3858 0.3008 -0.0459 0.0056  0.0286  481 ASN A CG  
1461  O OD1 . ASN A 180 ? 0.3663 0.4888 0.3944 -0.0399 0.0094  0.0289  481 ASN A OD1 
1462  N ND2 . ASN A 180 ? 0.3154 0.4129 0.3302 -0.0580 0.0065  0.0314  481 ASN A ND2 
1463  N N   . SER A 181 ? 0.2010 0.3134 0.2438 -0.0378 -0.0107 0.0202  482 SER A N   
1464  C CA  . SER A 181 ? 0.2627 0.3654 0.3048 -0.0317 -0.0149 0.0174  482 SER A CA  
1465  C C   . SER A 181 ? 0.2179 0.2980 0.2496 -0.0281 -0.0150 0.0161  482 SER A C   
1466  O O   . SER A 181 ? 0.2309 0.3056 0.2625 -0.0204 -0.0164 0.0137  482 SER A O   
1467  C CB  . SER A 181 ? 0.2224 0.3263 0.2659 -0.0394 -0.0191 0.0173  482 SER A CB  
1468  O OG  . SER A 181 ? 0.2957 0.3879 0.3305 -0.0509 -0.0186 0.0188  482 SER A OG  
1469  N N   . GLN A 182 ? 0.2086 0.2758 0.2306 -0.0337 -0.0133 0.0178  483 GLN A N   
1470  C CA  . GLN A 182 ? 0.2680 0.3174 0.2799 -0.0287 -0.0129 0.0171  483 GLN A CA  
1471  C C   . GLN A 182 ? 0.3271 0.3732 0.3320 -0.0308 -0.0089 0.0199  483 GLN A C   
1472  O O   . GLN A 182 ? 0.3157 0.3670 0.3200 -0.0396 -0.0067 0.0227  483 GLN A O   
1473  C CB  . GLN A 182 ? 0.2228 0.2538 0.2254 -0.0310 -0.0155 0.0164  483 GLN A CB  
1474  C CG  . GLN A 182 ? 0.3117 0.3443 0.3195 -0.0283 -0.0190 0.0136  483 GLN A CG  
1475  C CD  . GLN A 182 ? 0.4595 0.4857 0.4633 -0.0363 -0.0216 0.0138  483 GLN A CD  
1476  O OE1 . GLN A 182 ? 0.5508 0.5875 0.5619 -0.0383 -0.0240 0.0130  483 GLN A OE1 
1477  N NE2 . GLN A 182 ? 0.4328 0.4405 0.4234 -0.0401 -0.0213 0.0146  483 GLN A NE2 
1478  N N   . LEU A 183 ? 0.2909 0.3288 0.2897 -0.0234 -0.0081 0.0192  484 LEU A N   
1479  C CA  . LEU A 183 ? 0.2940 0.3284 0.2847 -0.0237 -0.0045 0.0218  484 LEU A CA  
1480  C C   . LEU A 183 ? 0.3547 0.3739 0.3329 -0.0326 -0.0032 0.0252  484 LEU A C   
1481  O O   . LEU A 183 ? 0.3254 0.3464 0.2994 -0.0389 0.0006  0.0285  484 LEU A O   
1482  C CB  . LEU A 183 ? 0.2649 0.2919 0.2497 -0.0140 -0.0052 0.0202  484 LEU A CB  
1483  C CG  . LEU A 183 ? 0.2590 0.2979 0.2530 -0.0066 -0.0061 0.0167  484 LEU A CG  
1484  C CD1 . LEU A 183 ? 0.3007 0.3335 0.2879 0.0008  -0.0070 0.0151  484 LEU A CD1 
1485  C CD2 . LEU A 183 ? 0.2288 0.2833 0.2295 -0.0070 -0.0028 0.0175  484 LEU A CD2 
1486  N N   . ILE A 184 ? 0.3378 0.3408 0.3084 -0.0336 -0.0060 0.0244  485 ILE A N   
1487  C CA  . ILE A 184 ? 0.3276 0.3100 0.2820 -0.0414 -0.0052 0.0271  485 ILE A CA  
1488  C C   . ILE A 184 ? 0.4225 0.4033 0.3791 -0.0497 -0.0079 0.0260  485 ILE A C   
1489  O O   . ILE A 184 ? 0.3256 0.3039 0.2848 -0.0446 -0.0113 0.0230  485 ILE A O   
1490  C CB  . ILE A 184 ? 0.3433 0.3033 0.2813 -0.0328 -0.0059 0.0272  485 ILE A CB  
1491  C CG1 . ILE A 184 ? 0.4256 0.3882 0.3604 -0.0255 -0.0035 0.0286  485 ILE A CG1 
1492  C CG2 . ILE A 184 ? 0.3240 0.2579 0.2417 -0.0401 -0.0050 0.0300  485 ILE A CG2 
1493  C CD1 . ILE A 184 ? 0.3964 0.3479 0.3221 -0.0133 -0.0055 0.0274  485 ILE A CD1 
1494  N N   . ARG A 185 ? 0.3628 0.3472 0.3188 -0.0629 -0.0064 0.0283  486 ARG A N   
1495  C CA  . ARG A 185 ? 0.4119 0.3934 0.3671 -0.0733 -0.0093 0.0274  486 ARG A CA  
1496  C C   . ARG A 185 ? 0.4136 0.3845 0.3561 -0.0886 -0.0066 0.0308  486 ARG A C   
1497  O O   . ARG A 185 ? 0.3807 0.3530 0.3195 -0.0911 -0.0021 0.0340  486 ARG A O   
1498  C CB  . ARG A 185 ? 0.3377 0.3476 0.3134 -0.0747 -0.0116 0.0255  486 ARG A CB  
1499  C CG  . ARG A 185 ? 0.3111 0.3294 0.2975 -0.0613 -0.0141 0.0222  486 ARG A CG  
1500  C CD  . ARG A 185 ? 0.3368 0.3747 0.3374 -0.0630 -0.0174 0.0205  486 ARG A CD  
1501  N NE  . ARG A 185 ? 0.3855 0.4123 0.3791 -0.0708 -0.0210 0.0194  486 ARG A NE  
1502  C CZ  . ARG A 185 ? 0.4115 0.4504 0.4134 -0.0727 -0.0249 0.0177  486 ARG A CZ  
1503  N NH1 . ARG A 185 ? 0.3063 0.3683 0.3236 -0.0664 -0.0257 0.0171  486 ARG A NH1 
1504  N NH2 . ARG A 185 ? 0.3589 0.3853 0.3520 -0.0802 -0.0282 0.0166  486 ARG A NH2 
1505  N N   . TYR A 186 ? 0.3224 0.2816 0.2568 -0.0995 -0.0091 0.0301  487 TYR A N   
1506  C CA  . TYR A 186 ? 0.3505 0.2968 0.2705 -0.1166 -0.0069 0.0330  487 TYR A CA  
1507  C C   . TYR A 186 ? 0.3375 0.3139 0.2741 -0.1308 -0.0074 0.0333  487 TYR A C   
1508  O O   . TYR A 186 ? 0.4531 0.4502 0.4059 -0.1287 -0.0114 0.0304  487 TYR A O   
1509  C CB  . TYR A 186 ? 0.3685 0.2791 0.2649 -0.1213 -0.0093 0.0319  487 TYR A CB  
1510  C CG  . TYR A 186 ? 0.4826 0.3637 0.3607 -0.1068 -0.0086 0.0320  487 TYR A CG  
1511  C CD1 . TYR A 186 ? 0.4165 0.2862 0.2910 -0.0953 -0.0121 0.0285  487 TYR A CD1 
1512  C CD2 . TYR A 186 ? 0.4567 0.3231 0.3209 -0.1039 -0.0042 0.0357  487 TYR A CD2 
1513  C CE1 . TYR A 186 ? 0.4948 0.3412 0.3535 -0.0810 -0.0114 0.0285  487 TYR A CE1 
1514  C CE2 . TYR A 186 ? 0.4736 0.3151 0.3209 -0.0894 -0.0040 0.0359  487 TYR A CE2 
1515  C CZ  . TYR A 186 ? 0.5139 0.3467 0.3591 -0.0777 -0.0077 0.0322  487 TYR A CZ  
1516  O OH  . TYR A 186 ? 0.4933 0.3051 0.3226 -0.0622 -0.0075 0.0324  487 TYR A OH  
1517  N N   . ALA A 187 ? 0.4416 0.4209 0.3734 -0.1453 -0.0032 0.0369  488 ALA A N   
1518  C CA  . ALA A 187 ? 0.3729 0.3846 0.3208 -0.1599 -0.0031 0.0374  488 ALA A CA  
1519  C C   . ALA A 187 ? 0.4820 0.4883 0.4256 -0.1733 -0.0085 0.0349  488 ALA A C   
1520  O O   . ALA A 187 ? 0.4486 0.4205 0.3717 -0.1745 -0.0110 0.0335  488 ALA A O   
1521  C CB  . ALA A 187 ? 0.3783 0.3930 0.3199 -0.1743 0.0033  0.0421  488 ALA A CB  
1522  N N   . GLY A 188 ? 0.4607 0.5025 0.4233 -0.1828 -0.0104 0.0343  489 GLY A N   
1523  C CA  . GLY A 188 ? 0.3991 0.4415 0.3589 -0.1983 -0.0157 0.0321  489 GLY A CA  
1524  C C   . GLY A 188 ? 0.3848 0.4585 0.3554 -0.2182 -0.0138 0.0343  489 GLY A C   
1525  O O   . GLY A 188 ? 0.4495 0.5602 0.4410 -0.2138 -0.0107 0.0360  489 GLY A O   
1526  N N   . TYR A 189 ? 0.3927 0.4524 0.3484 -0.2402 -0.0155 0.0342  490 TYR A N   
1527  C CA  . TYR A 189 ? 0.5475 0.6347 0.5106 -0.2627 -0.0130 0.0365  490 TYR A CA  
1528  C C   . TYR A 189 ? 0.5568 0.6535 0.5212 -0.2717 -0.0200 0.0324  490 TYR A C   
1529  O O   . TYR A 189 ? 0.6431 0.7051 0.5871 -0.2750 -0.0243 0.0296  490 TYR A O   
1530  C CB  . TYR A 189 ? 0.5689 0.6233 0.5062 -0.2745 -0.0065 0.0399  490 TYR A CB  
1531  C CG  . TYR A 189 ? 0.5964 0.6307 0.5248 -0.2623 0.0000  0.0437  490 TYR A CG  
1532  C CD1 . TYR A 189 ? 0.5855 0.5706 0.4880 -0.2518 -0.0003 0.0433  490 TYR A CD1 
1533  C CD2 . TYR A 189 ? 0.5825 0.6472 0.5274 -0.2570 0.0063  0.0470  490 TYR A CD2 
1534  C CE1 . TYR A 189 ? 0.6140 0.5822 0.5080 -0.2370 0.0049  0.0462  490 TYR A CE1 
1535  C CE2 . TYR A 189 ? 0.5920 0.6377 0.5274 -0.2426 0.0117  0.0497  490 TYR A CE2 
1536  C CZ  . TYR A 189 ? 0.6419 0.6401 0.5523 -0.2330 0.0106  0.0493  490 TYR A CZ  
1537  O OH  . TYR A 189 ? 0.5946 0.5763 0.4958 -0.2184 0.0153  0.0519  490 TYR A OH  
1538  N N   . LYS A 190 ? 0.5942 0.7373 0.5812 -0.2744 -0.0209 0.0320  491 LYS A N   
1539  C CA  . LYS A 190 ? 0.7071 0.8618 0.6944 -0.2852 -0.0266 0.0289  491 LYS A CA  
1540  C C   . LYS A 190 ? 0.7109 0.8442 0.6762 -0.3051 -0.0233 0.0301  491 LYS A C   
1541  O O   . LYS A 190 ? 0.7003 0.8461 0.6680 -0.3118 -0.0169 0.0334  491 LYS A O   
1542  C CB  . LYS A 190 ? 0.7531 0.9645 0.7707 -0.2800 -0.0284 0.0285  491 LYS A CB  
1543  C CG  . LYS A 190 ? 0.8132 1.0453 0.8508 -0.2595 -0.0323 0.0271  491 LYS A CG  
1544  C CD  . LYS A 190 ? 0.8831 1.1450 0.9349 -0.2566 -0.0398 0.0239  491 LYS A CD  
1545  C CE  . LYS A 190 ? 0.8931 1.2074 0.9700 -0.2512 -0.0378 0.0253  491 LYS A CE  
1546  N NZ  . LYS A 190 ? 0.8455 1.1779 0.9389 -0.2313 -0.0343 0.0271  491 LYS A NZ  
1547  N N   . GLN A 191 ? 0.7758 0.8760 0.7185 -0.3142 -0.0276 0.0273  492 GLN A N   
1548  C CA  . GLN A 191 ? 0.8730 0.9483 0.7912 -0.3333 -0.0254 0.0278  492 GLN A CA  
1549  C C   . GLN A 191 ? 0.9062 1.0182 0.8362 -0.3476 -0.0281 0.0266  492 GLN A C   
1550  O O   . GLN A 191 ? 0.7708 0.9154 0.7209 -0.3423 -0.0338 0.0241  492 GLN A O   
1551  C CB  . GLN A 191 ? 0.8493 0.8701 0.7350 -0.3355 -0.0286 0.0252  492 GLN A CB  
1552  C CG  . GLN A 191 ? 0.8489 0.8279 0.7173 -0.3225 -0.0256 0.0266  492 GLN A CG  
1553  C CD  . GLN A 191 ? 0.8835 0.8435 0.7377 -0.3266 -0.0174 0.0311  492 GLN A CD  
1554  O OE1 . GLN A 191 ? 0.8734 0.8642 0.7466 -0.3253 -0.0125 0.0344  492 GLN A OE1 
1555  N NE2 . GLN A 191 ? 0.9464 0.8547 0.7656 -0.3305 -0.0158 0.0312  492 GLN A NE2 
1556  N N   . PRO A 192 ? 1.0076 1.1148 0.9247 -0.3657 -0.0240 0.0283  493 PRO A N   
1557  C CA  . PRO A 192 ? 0.9861 1.1293 0.9140 -0.3809 -0.0265 0.0271  493 PRO A CA  
1558  C C   . PRO A 192 ? 1.0021 1.1430 0.9264 -0.3843 -0.0351 0.0227  493 PRO A C   
1559  O O   . PRO A 192 ? 0.9838 1.1682 0.9307 -0.3841 -0.0393 0.0212  493 PRO A O   
1560  C CB  . PRO A 192 ? 0.9865 1.1066 0.8905 -0.4011 -0.0211 0.0293  493 PRO A CB  
1561  C CG  . PRO A 192 ? 0.9714 1.0613 0.8632 -0.3930 -0.0142 0.0327  493 PRO A CG  
1562  C CD  . PRO A 192 ? 1.0007 1.0680 0.8911 -0.3735 -0.0174 0.0312  493 PRO A CD  
1563  N N   . ASP A 193 ? 0.9977 1.0883 0.8934 -0.3858 -0.0377 0.0205  494 ASP A N   
1564  C CA  . ASP A 193 ? 0.9107 0.9953 0.7999 -0.3893 -0.0456 0.0162  494 ASP A CA  
1565  C C   . ASP A 193 ? 0.8347 0.9455 0.7481 -0.3708 -0.0512 0.0141  494 ASP A C   
1566  O O   . ASP A 193 ? 0.9081 1.0337 0.8268 -0.3731 -0.0580 0.0109  494 ASP A O   
1567  C CB  . ASP A 193 ? 0.9847 1.0069 0.8356 -0.3930 -0.0463 0.0145  494 ASP A CB  
1568  C CG  . ASP A 193 ? 1.0989 1.0851 0.9378 -0.3777 -0.0420 0.0163  494 ASP A CG  
1569  O OD1 . ASP A 193 ? 1.0913 1.0593 0.9270 -0.3630 -0.0455 0.0140  494 ASP A OD1 
1570  O OD2 . ASP A 193 ? 1.1892 1.1659 1.0217 -0.3803 -0.0351 0.0199  494 ASP A OD2 
1571  N N   . GLY A 194 ? 0.7453 0.8620 0.6728 -0.3526 -0.0487 0.0158  495 GLY A N   
1572  C CA  . GLY A 194 ? 0.6608 0.8014 0.6103 -0.3344 -0.0537 0.0140  495 GLY A CA  
1573  C C   . GLY A 194 ? 0.6830 0.7881 0.6218 -0.3191 -0.0546 0.0130  495 GLY A C   
1574  O O   . GLY A 194 ? 0.6667 0.7906 0.6236 -0.3030 -0.0579 0.0120  495 GLY A O   
1575  N N   . SER A 195 ? 0.6749 0.7292 0.5840 -0.3228 -0.0519 0.0131  496 SER A N   
1576  C CA  . SER A 195 ? 0.7466 0.7668 0.6445 -0.3078 -0.0521 0.0123  496 SER A CA  
1577  C C   . SER A 195 ? 0.6929 0.7248 0.6056 -0.2964 -0.0464 0.0160  496 SER A C   
1578  O O   . SER A 195 ? 0.5888 0.6574 0.5219 -0.2983 -0.0429 0.0188  496 SER A O   
1579  C CB  . SER A 195 ? 0.8253 0.7879 0.6852 -0.3140 -0.0507 0.0114  496 SER A CB  
1580  O OG  . SER A 195 ? 0.9181 0.8659 0.7639 -0.3249 -0.0441 0.0148  496 SER A OG  
1581  N N   . THR A 196 ? 0.6060 0.6067 0.5079 -0.2840 -0.0453 0.0160  497 THR A N   
1582  C CA  . THR A 196 ? 0.5659 0.5743 0.4798 -0.2729 -0.0403 0.0194  497 THR A CA  
1583  C C   . THR A 196 ? 0.5932 0.5511 0.4786 -0.2706 -0.0356 0.0212  497 THR A C   
1584  O O   . THR A 196 ? 0.6489 0.5677 0.5119 -0.2663 -0.0381 0.0186  497 THR A O   
1585  C CB  . THR A 196 ? 0.5882 0.6170 0.5229 -0.2561 -0.0445 0.0178  497 THR A CB  
1586  O OG1 . THR A 196 ? 0.6390 0.7165 0.6002 -0.2552 -0.0483 0.0168  497 THR A OG1 
1587  C CG2 . THR A 196 ? 0.5276 0.5582 0.4705 -0.2374 -0.0380 0.0210  497 THR A CG2 
1588  N N   . LEU A 197 ? 0.5758 0.5346 0.4614 -0.2720 -0.0285 0.0257  498 LEU A N   
1589  C CA  . LEU A 197 ? 0.6477 0.5618 0.5078 -0.2671 -0.0235 0.0283  498 LEU A CA  
1590  C C   . LEU A 197 ? 0.6467 0.5709 0.5217 -0.2420 -0.0210 0.0295  498 LEU A C   
1591  O O   . LEU A 197 ? 0.5858 0.5509 0.4879 -0.2359 -0.0193 0.0308  498 LEU A O   
1592  C CB  . LEU A 197 ? 0.6300 0.5370 0.4778 -0.2792 -0.0168 0.0322  498 LEU A CB  
1593  C CG  . LEU A 197 ? 0.7310 0.5962 0.5537 -0.2725 -0.0109 0.0360  498 LEU A CG  
1594  C CD1 . LEU A 197 ? 0.7870 0.5988 0.5758 -0.2677 -0.0133 0.0335  498 LEU A CD1 
1595  C CD2 . LEU A 197 ? 0.6738 0.5404 0.4891 -0.2844 -0.0042 0.0401  498 LEU A CD2 
1596  N N   . GLY A 198 ? 0.6208 0.5090 0.4779 -0.2255 -0.0209 0.0285  499 GLY A N   
1597  C CA  . GLY A 198 ? 0.5066 0.4041 0.3770 -0.2009 -0.0193 0.0287  499 GLY A CA  
1598  C C   . GLY A 198 ? 0.5534 0.4737 0.4442 -0.1874 -0.0246 0.0248  499 GLY A C   
1599  O O   . GLY A 198 ? 0.5864 0.4979 0.4711 -0.1912 -0.0298 0.0213  499 GLY A O   
1600  N N   . ASP A 199 ? 0.5286 0.4766 0.4418 -0.1718 -0.0232 0.0253  500 ASP A N   
1601  C CA  . ASP A 199 ? 0.3839 0.3499 0.3140 -0.1576 -0.0274 0.0221  500 ASP A CA  
1602  C C   . ASP A 199 ? 0.4251 0.4320 0.3785 -0.1649 -0.0305 0.0215  500 ASP A C   
1603  O O   . ASP A 199 ? 0.3779 0.4141 0.3485 -0.1641 -0.0274 0.0238  500 ASP A O   
1604  C CB  . ASP A 199 ? 0.4100 0.3814 0.3494 -0.1375 -0.0245 0.0227  500 ASP A CB  
1605  C CG  . ASP A 199 ? 0.4370 0.4159 0.3868 -0.1229 -0.0283 0.0194  500 ASP A CG  
1606  O OD1 . ASP A 199 ? 0.4613 0.4533 0.4186 -0.1272 -0.0330 0.0172  500 ASP A OD1 
1607  O OD2 . ASP A 199 ? 0.4325 0.4048 0.3825 -0.1076 -0.0267 0.0190  500 ASP A OD2 
1608  N N   . PRO A 200 ? 0.4641 0.4753 0.4185 -0.1707 -0.0366 0.0184  501 PRO A N   
1609  C CA  . PRO A 200 ? 0.3625 0.4152 0.3390 -0.1767 -0.0401 0.0180  501 PRO A CA  
1610  C C   . PRO A 200 ? 0.3551 0.4372 0.3542 -0.1586 -0.0397 0.0182  501 PRO A C   
1611  O O   . PRO A 200 ? 0.3846 0.5038 0.4028 -0.1607 -0.0400 0.0193  501 PRO A O   
1612  C CB  . PRO A 200 ? 0.3575 0.4018 0.3261 -0.1836 -0.0473 0.0143  501 PRO A CB  
1613  C CG  . PRO A 200 ? 0.5012 0.4987 0.4402 -0.1899 -0.0463 0.0135  501 PRO A CG  
1614  C CD  . PRO A 200 ? 0.4114 0.3896 0.3446 -0.1740 -0.0405 0.0154  501 PRO A CD  
1615  N N   . ALA A 201 ? 0.3414 0.4082 0.3381 -0.1408 -0.0390 0.0172  502 ALA A N   
1616  C CA  . ALA A 201 ? 0.3710 0.4609 0.3857 -0.1245 -0.0383 0.0173  502 ALA A CA  
1617  C C   . ALA A 201 ? 0.4675 0.5785 0.4935 -0.1236 -0.0328 0.0203  502 ALA A C   
1618  O O   . ALA A 201 ? 0.4114 0.5514 0.4546 -0.1152 -0.0327 0.0206  502 ALA A O   
1619  C CB  . ALA A 201 ? 0.4003 0.4677 0.4082 -0.1084 -0.0375 0.0158  502 ALA A CB  
1620  N N   . ASN A 202 ? 0.4148 0.5109 0.4298 -0.1317 -0.0280 0.0226  503 ASN A N   
1621  C CA  . ASN A 202 ? 0.3498 0.4619 0.3726 -0.1296 -0.0220 0.0256  503 ASN A CA  
1622  C C   . ASN A 202 ? 0.4076 0.5431 0.4365 -0.1469 -0.0200 0.0280  503 ASN A C   
1623  O O   . ASN A 202 ? 0.4229 0.5661 0.4533 -0.1491 -0.0139 0.0310  503 ASN A O   
1624  C CB  . ASN A 202 ? 0.2846 0.3663 0.2912 -0.1247 -0.0175 0.0270  503 ASN A CB  
1625  C CG  . ASN A 202 ? 0.3203 0.3872 0.3249 -0.1072 -0.0190 0.0247  503 ASN A CG  
1626  O OD1 . ASN A 202 ? 0.3712 0.4557 0.3896 -0.0961 -0.0208 0.0230  503 ASN A OD1 
1627  N ND2 . ASN A 202 ? 0.2846 0.3193 0.2712 -0.1045 -0.0183 0.0245  503 ASN A ND2 
1628  N N   . VAL A 203 ? 0.3852 0.5343 0.4181 -0.1597 -0.0248 0.0268  504 VAL A N   
1629  C CA  . VAL A 203 ? 0.4301 0.6052 0.4701 -0.1781 -0.0230 0.0289  504 VAL A CA  
1630  C C   . VAL A 203 ? 0.4281 0.6453 0.4905 -0.1696 -0.0194 0.0306  504 VAL A C   
1631  O O   . VAL A 203 ? 0.4415 0.6719 0.5064 -0.1774 -0.0132 0.0338  504 VAL A O   
1632  C CB  . VAL A 203 ? 0.4061 0.5909 0.4470 -0.1932 -0.0299 0.0267  504 VAL A CB  
1633  C CG1 . VAL A 203 ? 0.3136 0.5391 0.3693 -0.2098 -0.0286 0.0286  504 VAL A CG1 
1634  C CG2 . VAL A 203 ? 0.4346 0.5754 0.4491 -0.2059 -0.0316 0.0256  504 VAL A CG2 
1635  N N   . GLN A 204 ? 0.3015 0.5385 0.3785 -0.1527 -0.0229 0.0287  505 GLN A N   
1636  C CA  . GLN A 204 ? 0.3211 0.5967 0.4176 -0.1423 -0.0196 0.0300  505 GLN A CA  
1637  C C   . GLN A 204 ? 0.3581 0.6234 0.4504 -0.1327 -0.0120 0.0320  505 GLN A C   
1638  O O   . GLN A 204 ? 0.3125 0.6021 0.4130 -0.1355 -0.0062 0.0345  505 GLN A O   
1639  C CB  . GLN A 204 ? 0.3028 0.5938 0.4108 -0.1243 -0.0249 0.0275  505 GLN A CB  
1640  C CG  . GLN A 204 ? 0.4617 0.7935 0.5884 -0.1129 -0.0219 0.0287  505 GLN A CG  
1641  C CD  . GLN A 204 ? 0.5103 0.8509 0.6442 -0.0924 -0.0263 0.0266  505 GLN A CD  
1642  O OE1 . GLN A 204 ? 0.5493 0.8608 0.6732 -0.0836 -0.0295 0.0246  505 GLN A OE1 
1643  N NE2 . GLN A 204 ? 0.4839 0.8651 0.6343 -0.0843 -0.0263 0.0272  505 GLN A NE2 
1644  N N   . PHE A 205 ? 0.3435 0.5750 0.4235 -0.1212 -0.0120 0.0308  506 PHE A N   
1645  C CA  . PHE A 205 ? 0.3357 0.5567 0.4106 -0.1123 -0.0056 0.0324  506 PHE A CA  
1646  C C   . PHE A 205 ? 0.3862 0.5994 0.4509 -0.1281 0.0002  0.0359  506 PHE A C   
1647  O O   . PHE A 205 ? 0.3069 0.5344 0.3753 -0.1263 0.0065  0.0383  506 PHE A O   
1648  C CB  . PHE A 205 ? 0.3652 0.5520 0.4280 -0.0996 -0.0073 0.0303  506 PHE A CB  
1649  C CG  . PHE A 205 ? 0.3701 0.5482 0.4281 -0.0894 -0.0019 0.0313  506 PHE A CG  
1650  C CD1 . PHE A 205 ? 0.3447 0.5415 0.4134 -0.0746 0.0000  0.0304  506 PHE A CD1 
1651  C CD2 . PHE A 205 ? 0.3300 0.4809 0.3714 -0.0942 0.0013  0.0331  506 PHE A CD2 
1652  C CE1 . PHE A 205 ? 0.3592 0.5478 0.4224 -0.0658 0.0047  0.0310  506 PHE A CE1 
1653  C CE2 . PHE A 205 ? 0.4123 0.5564 0.4489 -0.0846 0.0058  0.0340  506 PHE A CE2 
1654  C CZ  . PHE A 205 ? 0.3810 0.5444 0.4288 -0.0710 0.0074  0.0327  506 PHE A CZ  
1655  N N   . THR A 206 ? 0.2606 0.4499 0.3106 -0.1437 -0.0017 0.0363  507 THR A N   
1656  C CA  . THR A 206 ? 0.4105 0.5889 0.4476 -0.1607 0.0036  0.0400  507 THR A CA  
1657  C C   . THR A 206 ? 0.4443 0.6636 0.4967 -0.1723 0.0078  0.0425  507 THR A C   
1658  O O   . THR A 206 ? 0.4290 0.6513 0.4775 -0.1774 0.0150  0.0460  507 THR A O   
1659  C CB  . THR A 206 ? 0.3839 0.5304 0.4018 -0.1762 0.0001  0.0394  507 THR A CB  
1660  O OG1 . THR A 206 ? 0.3956 0.5065 0.3997 -0.1635 -0.0030 0.0372  507 THR A OG1 
1661  C CG2 . THR A 206 ? 0.3313 0.4610 0.3319 -0.1944 0.0059  0.0435  507 THR A CG2 
1662  N N   . GLU A 207 ? 0.3847 0.6377 0.4547 -0.1760 0.0034  0.0408  508 GLU A N   
1663  C CA  . GLU A 207 ? 0.3364 0.6336 0.4228 -0.1869 0.0072  0.0431  508 GLU A CA  
1664  C C   . GLU A 207 ? 0.2913 0.6132 0.3901 -0.1704 0.0135  0.0445  508 GLU A C   
1665  O O   . GLU A 207 ? 0.2743 0.6179 0.3774 -0.1790 0.0206  0.0478  508 GLU A O   
1666  C CB  . GLU A 207 ? 0.4415 0.7720 0.5446 -0.1921 0.0002  0.0407  508 GLU A CB  
1667  C CG  . GLU A 207 ? 0.6751 0.9859 0.7651 -0.2136 -0.0049 0.0395  508 GLU A CG  
1668  C CD  . GLU A 207 ? 0.7763 1.1102 0.8772 -0.2130 -0.0129 0.0360  508 GLU A CD  
1669  O OE1 . GLU A 207 ? 0.7560 1.1164 0.8741 -0.1958 -0.0161 0.0345  508 GLU A OE1 
1670  O OE2 . GLU A 207 ? 0.7999 1.1235 0.8901 -0.2295 -0.0158 0.0348  508 GLU A OE2 
1671  N N   . ILE A 208 ? 0.3713 0.6890 0.4743 -0.1472 0.0113  0.0419  509 ILE A N   
1672  C CA  . ILE A 208 ? 0.3374 0.6718 0.4479 -0.1304 0.0171  0.0427  509 ILE A CA  
1673  C C   . ILE A 208 ? 0.3566 0.6680 0.4515 -0.1340 0.0245  0.0458  509 ILE A C   
1674  O O   . ILE A 208 ? 0.3494 0.6827 0.4492 -0.1347 0.0319  0.0484  509 ILE A O   
1675  C CB  . ILE A 208 ? 0.3494 0.6740 0.4620 -0.1068 0.0129  0.0391  509 ILE A CB  
1676  C CG1 . ILE A 208 ? 0.3679 0.7193 0.4960 -0.1011 0.0064  0.0367  509 ILE A CG1 
1677  C CG2 . ILE A 208 ? 0.3047 0.6368 0.4192 -0.0903 0.0190  0.0395  509 ILE A CG2 
1678  C CD1 . ILE A 208 ? 0.4041 0.7345 0.5284 -0.0834 0.0007  0.0333  509 ILE A CD1 
1679  N N   . CYS A 209 ? 0.3677 0.6352 0.4427 -0.1360 0.0228  0.0455  510 CYS A N   
1680  C CA  . CYS A 209 ? 0.3787 0.6210 0.4362 -0.1388 0.0290  0.0486  510 CYS A CA  
1681  C C   . CYS A 209 ? 0.3698 0.6240 0.4240 -0.1601 0.0353  0.0531  510 CYS A C   
1682  O O   . CYS A 209 ? 0.3879 0.6505 0.4402 -0.1597 0.0430  0.0562  510 CYS A O   
1683  C CB  . CYS A 209 ? 0.3843 0.5795 0.4207 -0.1383 0.0252  0.0477  510 CYS A CB  
1684  S SG  . CYS A 209 ? 0.3875 0.5680 0.4255 -0.1138 0.0199  0.0431  510 CYS A SG  
1685  N N   . ILE A 210 ? 0.3298 0.5834 0.3820 -0.1799 0.0322  0.0534  511 ILE A N   
1686  C CA  . ILE A 210 ? 0.3519 0.6154 0.3996 -0.2035 0.0380  0.0576  511 ILE A CA  
1687  C C   . ILE A 210 ? 0.3724 0.6880 0.4422 -0.2028 0.0439  0.0593  511 ILE A C   
1688  O O   . ILE A 210 ? 0.4274 0.7508 0.4929 -0.2112 0.0525  0.0634  511 ILE A O   
1689  C CB  . ILE A 210 ? 0.4180 0.6759 0.4616 -0.2249 0.0325  0.0567  511 ILE A CB  
1690  C CG1 . ILE A 210 ? 0.4976 0.7006 0.5156 -0.2249 0.0280  0.0554  511 ILE A CG1 
1691  C CG2 . ILE A 210 ? 0.3596 0.6267 0.3982 -0.2461 0.0373  0.0593  511 ILE A CG2 
1692  C CD1 . ILE A 210 ? 0.5579 0.7504 0.5693 -0.2434 0.0218  0.0535  511 ILE A CD1 
1693  N N   . GLN A 211 ? 0.3210 0.6724 0.4136 -0.1913 0.0395  0.0561  512 GLN A N   
1694  C CA  . GLN A 211 ? 0.3685 0.7676 0.4811 -0.1847 0.0439  0.0565  512 GLN A CA  
1695  C C   . GLN A 211 ? 0.4046 0.8068 0.5164 -0.1686 0.0518  0.0583  512 GLN A C   
1696  O O   . GLN A 211 ? 0.4513 0.8822 0.5711 -0.1666 0.0581  0.0598  512 GLN A O   
1697  C CB  . GLN A 211 ? 0.4957 0.9234 0.6279 -0.1719 0.0362  0.0523  512 GLN A CB  
1698  C CG  . GLN A 211 ? 0.6431 1.1141 0.7929 -0.1598 0.0388  0.0517  512 GLN A CG  
1699  C CD  . GLN A 211 ? 0.8094 1.2918 0.9686 -0.1333 0.0391  0.0499  512 GLN A CD  
1700  O OE1 . GLN A 211 ? 0.8136 1.3092 0.9752 -0.1214 0.0461  0.0510  512 GLN A OE1 
1701  N NE2 . GLN A 211 ? 0.8335 1.3087 0.9965 -0.1235 0.0313  0.0470  512 GLN A NE2 
1702  N N   . GLN A 212 ? 0.3705 0.7337 0.4678 -0.1533 0.0499  0.0567  513 GLN A N   
1703  C CA  . GLN A 212 ? 0.3898 0.7468 0.4812 -0.1372 0.0560  0.0574  513 GLN A CA  
1704  C C   . GLN A 212 ? 0.5128 0.8455 0.5840 -0.1493 0.0632  0.0619  513 GLN A C   
1705  O O   . GLN A 212 ? 0.5538 0.8756 0.6162 -0.1371 0.0679  0.0626  513 GLN A O   
1706  C CB  . GLN A 212 ? 0.4778 0.8064 0.5631 -0.1159 0.0503  0.0532  513 GLN A CB  
1707  C CG  . GLN A 212 ? 0.5078 0.8620 0.6108 -0.0978 0.0462  0.0493  513 GLN A CG  
1708  C CD  . GLN A 212 ? 0.5351 0.9330 0.6531 -0.0910 0.0530  0.0504  513 GLN A CD  
1709  O OE1 . GLN A 212 ? 0.5519 0.9883 0.6872 -0.0963 0.0525  0.0508  513 GLN A OE1 
1710  N NE2 . GLN A 212 ? 0.5303 0.9237 0.6413 -0.0789 0.0592  0.0509  513 GLN A NE2 
1711  N N   . GLY A 213 ? 0.5091 0.8315 0.5710 -0.1730 0.0640  0.0650  514 GLY A N   
1712  C CA  . GLY A 213 ? 0.4760 0.7736 0.5162 -0.1859 0.0711  0.0699  514 GLY A CA  
1713  C C   . GLY A 213 ? 0.4815 0.7244 0.4955 -0.1897 0.0671  0.0703  514 GLY A C   
1714  O O   . GLY A 213 ? 0.5307 0.7478 0.5230 -0.1996 0.0726  0.0747  514 GLY A O   
1715  N N   . TRP A 214 ? 0.4560 0.6800 0.4699 -0.1812 0.0581  0.0660  515 TRP A N   
1716  C CA  . TRP A 214 ? 0.4716 0.6453 0.4606 -0.1833 0.0544  0.0661  515 TRP A CA  
1717  C C   . TRP A 214 ? 0.5553 0.7134 0.5295 -0.2096 0.0555  0.0692  515 TRP A C   
1718  O O   . TRP A 214 ? 0.5553 0.7381 0.5425 -0.2245 0.0535  0.0684  515 TRP A O   
1719  C CB  . TRP A 214 ? 0.3817 0.5428 0.3752 -0.1696 0.0450  0.0608  515 TRP A CB  
1720  C CG  . TRP A 214 ? 0.4998 0.6115 0.4683 -0.1675 0.0416  0.0607  515 TRP A CG  
1721  C CD1 . TRP A 214 ? 0.5214 0.6031 0.4701 -0.1591 0.0443  0.0627  515 TRP A CD1 
1722  C CD2 . TRP A 214 ? 0.4877 0.5755 0.4480 -0.1724 0.0347  0.0582  515 TRP A CD2 
1723  N NE1 . TRP A 214 ? 0.4556 0.4976 0.3848 -0.1576 0.0396  0.0618  515 TRP A NE1 
1724  C CE2 . TRP A 214 ? 0.4442 0.4884 0.3797 -0.1657 0.0340  0.0590  515 TRP A CE2 
1725  C CE3 . TRP A 214 ? 0.4561 0.5555 0.4267 -0.1809 0.0289  0.0553  515 TRP A CE3 
1726  C CZ2 . TRP A 214 ? 0.4857 0.4981 0.4067 -0.1666 0.0284  0.0569  515 TRP A CZ2 
1727  C CZ3 . TRP A 214 ? 0.5152 0.5810 0.4704 -0.1830 0.0232  0.0531  515 TRP A CZ3 
1728  C CH2 . TRP A 214 ? 0.4704 0.4932 0.4010 -0.1756 0.0233  0.0539  515 TRP A CH2 
1729  N N   . LYS A 215 ? 0.4983 0.6147 0.4439 -0.2152 0.0586  0.0728  516 LYS A N   
1730  C CA  . LYS A 215 ? 0.5264 0.6163 0.4505 -0.2394 0.0599  0.0759  516 LYS A CA  
1731  C C   . LYS A 215 ? 0.6389 0.6888 0.5473 -0.2358 0.0518  0.0726  516 LYS A C   
1732  O O   . LYS A 215 ? 0.8131 0.8249 0.7011 -0.2228 0.0508  0.0730  516 LYS A O   
1733  C CB  . LYS A 215 ? 0.7092 0.7732 0.6075 -0.2467 0.0684  0.0821  516 LYS A CB  
1734  C CG  . LYS A 215 ? 0.7840 0.8868 0.6960 -0.2494 0.0775  0.0855  516 LYS A CG  
1735  C CD  . LYS A 215 ? 0.8554 0.9919 0.7845 -0.2654 0.0775  0.0837  516 LYS A CD  
1736  C CE  . LYS A 215 ? 0.8339 1.0057 0.7752 -0.2651 0.0860  0.0862  516 LYS A CE  
1737  N NZ  . LYS A 215 ? 0.7360 0.9605 0.7105 -0.2523 0.0854  0.0832  516 LYS A NZ  
1738  N N   . PRO A 216 ? 0.5846 0.6437 0.5021 -0.2458 0.0458  0.0693  517 PRO A N   
1739  C CA  . PRO A 216 ? 0.5652 0.5891 0.4689 -0.2410 0.0382  0.0657  517 PRO A CA  
1740  C C   . PRO A 216 ? 0.6440 0.6179 0.5117 -0.2563 0.0399  0.0688  517 PRO A C   
1741  O O   . PRO A 216 ? 0.6717 0.6462 0.5318 -0.2762 0.0430  0.0705  517 PRO A O   
1742  C CB  . PRO A 216 ? 0.6503 0.7047 0.5754 -0.2494 0.0320  0.0616  517 PRO A CB  
1743  C CG  . PRO A 216 ? 0.6952 0.7857 0.6325 -0.2690 0.0370  0.0643  517 PRO A CG  
1744  C CD  . PRO A 216 ? 0.5656 0.6701 0.5064 -0.2620 0.0456  0.0686  517 PRO A CD  
1745  N N   . PRO A 217 ? 0.6776 0.6077 0.5226 -0.2425 0.0372  0.0680  518 PRO A N   
1746  C CA  . PRO A 217 ? 0.6735 0.5519 0.4818 -0.2555 0.0375  0.0700  518 PRO A CA  
1747  C C   . PRO A 217 ? 0.7266 0.5997 0.5336 -0.2682 0.0309  0.0653  518 PRO A C   
1748  O O   . PRO A 217 ? 0.7747 0.6137 0.5558 -0.2773 0.0301  0.0643  518 PRO A O   
1749  C CB  . PRO A 217 ? 0.6387 0.4796 0.4280 -0.2316 0.0355  0.0696  518 PRO A CB  
1750  C CG  . PRO A 217 ? 0.6334 0.5073 0.4520 -0.2087 0.0323  0.0659  518 PRO A CG  
1751  C CD  . PRO A 217 ? 0.6076 0.5338 0.4575 -0.2146 0.0349  0.0660  518 PRO A CD  
1752  N N   . ARG A 218 ? 0.5970 0.5045 0.4316 -0.2658 0.0256  0.0613  519 ARG A N   
1753  C CA  . ARG A 218 ? 0.7282 0.6379 0.5651 -0.2762 0.0187  0.0563  519 ARG A CA  
1754  C C   . ARG A 218 ? 0.7509 0.6065 0.5557 -0.2729 0.0148  0.0540  519 ARG A C   
1755  O O   . ARG A 218 ? 0.7858 0.6229 0.5739 -0.2848 0.0122  0.0513  519 ARG A O   
1756  C CB  . ARG A 218 ? 0.8012 0.7332 0.6430 -0.2953 0.0200  0.0557  519 ARG A CB  
1757  C CG  . ARG A 218 ? 0.8577 0.8443 0.7307 -0.2962 0.0242  0.0578  519 ARG A CG  
1758  C CD  . ARG A 218 ? 0.9075 0.9248 0.7912 -0.3134 0.0236  0.0562  519 ARG A CD  
1759  N NE  . ARG A 218 ? 0.9378 0.9877 0.8442 -0.3131 0.0163  0.0517  519 ARG A NE  
1760  C CZ  . ARG A 218 ? 0.9161 1.0190 0.8550 -0.3079 0.0159  0.0511  519 ARG A CZ  
1761  N NH1 . ARG A 218 ? 0.9444 1.0721 0.9001 -0.3064 0.0086  0.0470  519 ARG A NH1 
1762  N NH2 . ARG A 218 ? 0.8063 0.9369 0.7596 -0.3029 0.0227  0.0545  519 ARG A NH2 
1763  N N   . GLY A 219 ? 0.7173 0.5496 0.5138 -0.2531 0.0140  0.0543  520 GLY A N   
1764  C CA  . GLY A 219 ? 0.7253 0.5138 0.4970 -0.2449 0.0097  0.0514  520 GLY A CA  
1765  C C   . GLY A 219 ? 0.7196 0.5279 0.5126 -0.2297 0.0028  0.0457  520 GLY A C   
1766  O O   . GLY A 219 ? 0.6152 0.4687 0.4406 -0.2264 0.0010  0.0440  520 GLY A O   
1767  N N   . ARG A 220 ? 0.7776 0.5494 0.5499 -0.2196 -0.0008 0.0428  521 ARG A N   
1768  C CA  . ARG A 220 ? 0.7132 0.4982 0.5010 -0.2067 -0.0070 0.0375  521 ARG A CA  
1769  C C   . ARG A 220 ? 0.6432 0.4452 0.4490 -0.1806 -0.0069 0.0368  521 ARG A C   
1770  O O   . ARG A 220 ? 0.5279 0.3519 0.3537 -0.1707 -0.0112 0.0330  521 ARG A O   
1771  C CB  . ARG A 220 ? 0.7469 0.4870 0.5046 -0.2067 -0.0104 0.0344  521 ARG A CB  
1772  C CG  . ARG A 220 ? 0.7949 0.5496 0.5667 -0.2013 -0.0169 0.0289  521 ARG A CG  
1773  C CD  . ARG A 220 ? 0.8921 0.6022 0.6328 -0.2008 -0.0199 0.0256  521 ARG A CD  
1774  N NE  . ARG A 220 ? 0.8950 0.6222 0.6493 -0.2008 -0.0260 0.0206  521 ARG A NE  
1775  C CZ  . ARG A 220 ? 0.9818 0.6822 0.7186 -0.1931 -0.0293 0.0166  521 ARG A CZ  
1776  N NH1 . ARG A 220 ? 0.9687 0.6236 0.6736 -0.1834 -0.0270 0.0169  521 ARG A NH1 
1777  N NH2 . ARG A 220 ? 0.9834 0.7028 0.7340 -0.1938 -0.0347 0.0124  521 ARG A NH2 
1778  N N   . PHE A 221 ? 0.5615 0.3535 0.3597 -0.1701 -0.0023 0.0403  522 PHE A N   
1779  C CA  . PHE A 221 ? 0.5477 0.3533 0.3600 -0.1466 -0.0024 0.0396  522 PHE A CA  
1780  C C   . PHE A 221 ? 0.6081 0.4291 0.4275 -0.1446 0.0029  0.0438  522 PHE A C   
1781  O O   . PHE A 221 ? 0.7378 0.5413 0.5439 -0.1322 0.0054  0.0461  522 PHE A O   
1782  C CB  . PHE A 221 ? 0.5911 0.3608 0.3806 -0.1297 -0.0036 0.0385  522 PHE A CB  
1783  C CG  . PHE A 221 ? 0.6655 0.4181 0.4459 -0.1295 -0.0082 0.0341  522 PHE A CG  
1784  C CD1 . PHE A 221 ? 0.6783 0.3880 0.4255 -0.1378 -0.0082 0.0343  522 PHE A CD1 
1785  C CD2 . PHE A 221 ? 0.5678 0.3450 0.3703 -0.1208 -0.0123 0.0299  522 PHE A CD2 
1786  C CE1 . PHE A 221 ? 0.7362 0.4288 0.4730 -0.1371 -0.0123 0.0300  522 PHE A CE1 
1787  C CE2 . PHE A 221 ? 0.6036 0.3648 0.3964 -0.1204 -0.0162 0.0259  522 PHE A CE2 
1788  C CZ  . PHE A 221 ? 0.6314 0.3509 0.3916 -0.1284 -0.0163 0.0259  522 PHE A CZ  
1789  N N   . ASP A 222 ? 0.5979 0.4537 0.4384 -0.1562 0.0047  0.0449  523 ASP A N   
1790  C CA  . ASP A 222 ? 0.5910 0.4658 0.4403 -0.1546 0.0101  0.0486  523 ASP A CA  
1791  C C   . ASP A 222 ? 0.5588 0.4631 0.4331 -0.1358 0.0086  0.0460  523 ASP A C   
1792  O O   . ASP A 222 ? 0.4990 0.4347 0.3972 -0.1359 0.0059  0.0433  523 ASP A O   
1793  C CB  . ASP A 222 ? 0.6023 0.5023 0.4620 -0.1755 0.0134  0.0509  523 ASP A CB  
1794  C CG  . ASP A 222 ? 0.6412 0.5113 0.4748 -0.1970 0.0153  0.0535  523 ASP A CG  
1795  O OD1 . ASP A 222 ? 0.6524 0.4784 0.4559 -0.1937 0.0160  0.0550  523 ASP A OD1 
1796  O OD2 . ASP A 222 ? 0.6425 0.5331 0.4848 -0.2172 0.0161  0.0541  523 ASP A OD2 
1797  N N   . VAL A 223 ? 0.4644 0.3580 0.3320 -0.1196 0.0099  0.0469  524 VAL A N   
1798  C CA  . VAL A 223 ? 0.4360 0.3559 0.3252 -0.1034 0.0086  0.0443  524 VAL A CA  
1799  C C   . VAL A 223 ? 0.4043 0.3596 0.3138 -0.1093 0.0120  0.0456  524 VAL A C   
1800  O O   . VAL A 223 ? 0.4318 0.3881 0.3348 -0.1172 0.0174  0.0496  524 VAL A O   
1801  C CB  . VAL A 223 ? 0.4943 0.3986 0.3719 -0.0871 0.0095  0.0452  524 VAL A CB  
1802  C CG1 . VAL A 223 ? 0.4078 0.3400 0.3070 -0.0735 0.0085  0.0425  524 VAL A CG1 
1803  C CG2 . VAL A 223 ? 0.4636 0.3377 0.3235 -0.0782 0.0060  0.0436  524 VAL A CG2 
1804  N N   . LEU A 224 ? 0.3289 0.3131 0.2617 -0.1054 0.0091  0.0422  525 LEU A N   
1805  C CA  . LEU A 224 ? 0.3526 0.3722 0.3050 -0.1091 0.0120  0.0430  525 LEU A CA  
1806  C C   . LEU A 224 ? 0.3639 0.3916 0.3189 -0.0972 0.0160  0.0440  525 LEU A C   
1807  O O   . LEU A 224 ? 0.3142 0.3279 0.2630 -0.0835 0.0144  0.0426  525 LEU A O   
1808  C CB  . LEU A 224 ? 0.3032 0.3483 0.2772 -0.1049 0.0074  0.0391  525 LEU A CB  
1809  C CG  . LEU A 224 ? 0.3857 0.4347 0.3620 -0.1194 0.0040  0.0383  525 LEU A CG  
1810  C CD1 . LEU A 224 ? 0.3293 0.3899 0.3193 -0.1111 -0.0020 0.0340  525 LEU A CD1 
1811  C CD2 . LEU A 224 ? 0.4247 0.5017 0.4110 -0.1338 0.0078  0.0410  525 LEU A CD2 
1812  N N   . PRO A 225 ? 0.3042 0.3560 0.2683 -0.1022 0.0210  0.0463  526 PRO A N   
1813  C CA  . PRO A 225 ? 0.2958 0.3577 0.2632 -0.0900 0.0245  0.0466  526 PRO A CA  
1814  C C   . PRO A 225 ? 0.3851 0.4648 0.3698 -0.0757 0.0208  0.0420  526 PRO A C   
1815  O O   . PRO A 225 ? 0.3625 0.4536 0.3593 -0.0765 0.0167  0.0394  526 PRO A O   
1816  C CB  . PRO A 225 ? 0.3015 0.3871 0.2747 -0.1007 0.0312  0.0502  526 PRO A CB  
1817  C CG  . PRO A 225 ? 0.3463 0.4507 0.3324 -0.1132 0.0290  0.0496  526 PRO A CG  
1818  C CD  . PRO A 225 ? 0.3420 0.4169 0.3153 -0.1186 0.0236  0.0483  526 PRO A CD  
1819  N N   . LEU A 226 ? 0.2871 0.3668 0.2707 -0.0627 0.0222  0.0409  527 LEU A N   
1820  C CA  . LEU A 226 ? 0.3106 0.4075 0.3086 -0.0502 0.0200  0.0369  527 LEU A CA  
1821  C C   . LEU A 226 ? 0.2921 0.4200 0.3037 -0.0514 0.0244  0.0378  527 LEU A C   
1822  O O   . LEU A 226 ? 0.3636 0.4988 0.3715 -0.0566 0.0304  0.0412  527 LEU A O   
1823  C CB  . LEU A 226 ? 0.3274 0.4129 0.3180 -0.0371 0.0196  0.0349  527 LEU A CB  
1824  C CG  . LEU A 226 ? 0.3801 0.4406 0.3600 -0.0330 0.0148  0.0333  527 LEU A CG  
1825  C CD1 . LEU A 226 ? 0.3380 0.3908 0.3094 -0.0224 0.0151  0.0323  527 LEU A CD1 
1826  C CD2 . LEU A 226 ? 0.2961 0.3584 0.2859 -0.0296 0.0093  0.0294  527 LEU A CD2 
1827  N N   . LEU A 227 ? 0.2798 0.4262 0.3064 -0.0463 0.0215  0.0349  528 LEU A N   
1828  C CA  . LEU A 227 ? 0.2533 0.4315 0.2939 -0.0435 0.0250  0.0351  528 LEU A CA  
1829  C C   . LEU A 227 ? 0.2746 0.4536 0.3178 -0.0264 0.0235  0.0312  528 LEU A C   
1830  O O   . LEU A 227 ? 0.2534 0.4308 0.3019 -0.0206 0.0184  0.0281  528 LEU A O   
1831  C CB  . LEU A 227 ? 0.3118 0.5108 0.3660 -0.0512 0.0223  0.0353  528 LEU A CB  
1832  C CG  . LEU A 227 ? 0.3936 0.6236 0.4579 -0.0618 0.0270  0.0385  528 LEU A CG  
1833  C CD1 . LEU A 227 ? 0.2965 0.5524 0.3773 -0.0618 0.0227  0.0369  528 LEU A CD1 
1834  C CD2 . LEU A 227 ? 0.3134 0.5609 0.3791 -0.0558 0.0346  0.0401  528 LEU A CD2 
1835  N N   . LEU A 228 ? 0.3486 0.5284 0.3863 -0.0189 0.0281  0.0312  529 LEU A N   
1836  C CA  . LEU A 228 ? 0.3536 0.5256 0.3877 -0.0042 0.0267  0.0272  529 LEU A CA  
1837  C C   . LEU A 228 ? 0.3556 0.5507 0.3967 0.0057  0.0308  0.0263  529 LEU A C   
1838  O O   . LEU A 228 ? 0.2743 0.4849 0.3159 0.0037  0.0372  0.0290  529 LEU A O   
1839  C CB  . LEU A 228 ? 0.2622 0.4133 0.2813 -0.0020 0.0278  0.0271  529 LEU A CB  
1840  C CG  . LEU A 228 ? 0.2319 0.3602 0.2423 -0.0096 0.0240  0.0282  529 LEU A CG  
1841  C CD1 . LEU A 228 ? 0.2414 0.3519 0.2372 -0.0048 0.0244  0.0279  529 LEU A CD1 
1842  C CD2 . LEU A 228 ? 0.2318 0.3522 0.2472 -0.0081 0.0174  0.0251  529 LEU A CD2 
1843  N N   . GLN A 229 ? 0.2610 0.4568 0.3057 0.0169  0.0275  0.0225  530 GLN A N   
1844  C CA  . GLN A 229 ? 0.2844 0.4978 0.3329 0.0296  0.0308  0.0210  530 GLN A CA  
1845  C C   . GLN A 229 ? 0.3302 0.5236 0.3664 0.0420  0.0298  0.0166  530 GLN A C   
1846  O O   . GLN A 229 ? 0.2871 0.4616 0.3193 0.0443  0.0243  0.0135  530 GLN A O   
1847  C CB  . GLN A 229 ? 0.2735 0.5044 0.3344 0.0334  0.0278  0.0204  530 GLN A CB  
1848  C CG  . GLN A 229 ? 0.2825 0.5247 0.3436 0.0504  0.0300  0.0181  530 GLN A CG  
1849  C CD  . GLN A 229 ? 0.3334 0.5916 0.4052 0.0556  0.0263  0.0178  530 GLN A CD  
1850  O OE1 . GLN A 229 ? 0.3167 0.5703 0.3932 0.0475  0.0210  0.0182  530 GLN A OE1 
1851  N NE2 . GLN A 229 ? 0.5031 0.7807 0.5780 0.0698  0.0292  0.0171  530 GLN A NE2 
1852  N N   . ALA A 230 ? 0.2980 0.4961 0.3276 0.0495  0.0353  0.0161  531 ALA A N   
1853  C CA  . ALA A 230 ? 0.3232 0.5033 0.3391 0.0609  0.0351  0.0116  531 ALA A CA  
1854  C C   . ALA A 230 ? 0.3508 0.5448 0.3668 0.0756  0.0389  0.0099  531 ALA A C   
1855  O O   . ALA A 230 ? 0.2944 0.5143 0.3177 0.0773  0.0448  0.0127  531 ALA A O   
1856  C CB  . ALA A 230 ? 0.4183 0.5881 0.4221 0.0584  0.0381  0.0121  531 ALA A CB  
1857  N N   . ASN A 231 ? 0.3750 0.5513 0.3817 0.0861  0.0357  0.0052  532 ASN A N   
1858  C CA  . ASN A 231 ? 0.4201 0.6012 0.4206 0.1027  0.0391  0.0027  532 ASN A CA  
1859  C C   . ASN A 231 ? 0.4172 0.6312 0.4329 0.1080  0.0421  0.0057  532 ASN A C   
1860  O O   . ASN A 231 ? 0.4322 0.6639 0.4473 0.1192  0.0481  0.0059  532 ASN A O   
1861  C CB  . ASN A 231 ? 0.4464 0.6234 0.4337 0.1084  0.0447  0.0012  532 ASN A CB  
1862  C CG  . ASN A 231 ? 0.6598 0.8259 0.6325 0.1260  0.0463  -0.0034 532 ASN A CG  
1863  O OD1 . ASN A 231 ? 0.6668 0.8160 0.6337 0.1318  0.0418  -0.0065 532 ASN A OD1 
1864  N ND2 . ASN A 231 ? 0.6622 0.8360 0.6269 0.1347  0.0530  -0.0040 532 ASN A ND2 
1865  N N   . GLY A 232 ? 0.3637 0.5873 0.3930 0.0999  0.0378  0.0080  533 GLY A N   
1866  C CA  . GLY A 232 ? 0.3617 0.6174 0.4063 0.1039  0.0389  0.0106  533 GLY A CA  
1867  C C   . GLY A 232 ? 0.3992 0.6892 0.4572 0.0962  0.0449  0.0150  533 GLY A C   
1868  O O   . GLY A 232 ? 0.3835 0.7052 0.4561 0.0981  0.0457  0.0171  533 GLY A O   
1869  N N   . ASN A 233 ? 0.3080 0.5936 0.3611 0.0871  0.0492  0.0165  534 ASN A N   
1870  C CA  . ASN A 233 ? 0.3274 0.6437 0.3909 0.0783  0.0558  0.0210  534 ASN A CA  
1871  C C   . ASN A 233 ? 0.2868 0.6135 0.3634 0.0593  0.0526  0.0247  534 ASN A C   
1872  O O   . ASN A 233 ? 0.2608 0.5680 0.3368 0.0529  0.0455  0.0238  534 ASN A O   
1873  C CB  . ASN A 233 ? 0.4270 0.7312 0.4776 0.0752  0.0614  0.0217  534 ASN A CB  
1874  C CG  . ASN A 233 ? 0.4781 0.7716 0.5141 0.0934  0.0646  0.0177  534 ASN A CG  
1875  O OD1 . ASN A 233 ? 0.5516 0.8657 0.5907 0.1077  0.0686  0.0168  534 ASN A OD1 
1876  N ND2 . ASN A 233 ? 0.4590 0.7202 0.4781 0.0936  0.0626  0.0149  534 ASN A ND2 
1877  N N   . ASP A 234 ? 0.2838 0.6417 0.3715 0.0498  0.0581  0.0289  535 ASP A N   
1878  C CA  . ASP A 234 ? 0.3017 0.6678 0.3990 0.0295  0.0558  0.0324  535 ASP A CA  
1879  C C   . ASP A 234 ? 0.2517 0.5801 0.3358 0.0177  0.0524  0.0326  535 ASP A C   
1880  O O   . ASP A 234 ? 0.2684 0.5759 0.3384 0.0205  0.0551  0.0321  535 ASP A O   
1881  C CB  . ASP A 234 ? 0.3537 0.7542 0.4603 0.0186  0.0637  0.0369  535 ASP A CB  
1882  C CG  . ASP A 234 ? 0.3786 0.8241 0.5030 0.0267  0.0659  0.0372  535 ASP A CG  
1883  O OD1 . ASP A 234 ? 0.3890 0.8680 0.5225 0.0195  0.0731  0.0406  535 ASP A OD1 
1884  O OD2 . ASP A 234 ? 0.4448 0.8929 0.5736 0.0405  0.0605  0.0342  535 ASP A OD2 
1885  N N   . PRO A 235 ? 0.2520 0.5709 0.3394 0.0057  0.0462  0.0332  536 PRO A N   
1886  C CA  . PRO A 235 ? 0.2824 0.5660 0.3566 -0.0033 0.0430  0.0333  536 PRO A CA  
1887  C C   . PRO A 235 ? 0.3137 0.5960 0.3816 -0.0182 0.0486  0.0379  536 PRO A C   
1888  O O   . PRO A 235 ? 0.3369 0.6466 0.4130 -0.0265 0.0541  0.0412  536 PRO A O   
1889  C CB  . PRO A 235 ? 0.2380 0.5158 0.3182 -0.0104 0.0354  0.0325  536 PRO A CB  
1890  C CG  . PRO A 235 ? 0.2225 0.5376 0.3196 -0.0140 0.0361  0.0340  536 PRO A CG  
1891  C CD  . PRO A 235 ? 0.2490 0.5881 0.3511 0.0016  0.0414  0.0333  536 PRO A CD  
1892  N N   . GLU A 236 ? 0.2611 0.5112 0.3133 -0.0212 0.0475  0.0381  537 GLU A N   
1893  C CA  . GLU A 236 ? 0.2404 0.4818 0.2813 -0.0330 0.0528  0.0425  537 GLU A CA  
1894  C C   . GLU A 236 ? 0.3090 0.5204 0.3390 -0.0438 0.0481  0.0436  537 GLU A C   
1895  O O   . GLU A 236 ? 0.3273 0.5173 0.3530 -0.0372 0.0418  0.0404  537 GLU A O   
1896  C CB  . GLU A 236 ? 0.2520 0.4836 0.2801 -0.0224 0.0573  0.0421  537 GLU A CB  
1897  C CG  . GLU A 236 ? 0.2886 0.5474 0.3248 -0.0098 0.0624  0.0406  537 GLU A CG  
1898  C CD  . GLU A 236 ? 0.4461 0.6927 0.4681 0.0023  0.0659  0.0389  537 GLU A CD  
1899  O OE1 . GLU A 236 ? 0.4745 0.6990 0.4811 -0.0019 0.0668  0.0407  537 GLU A OE1 
1900  O OE2 . GLU A 236 ? 0.4336 0.6926 0.4589 0.0167  0.0675  0.0357  537 GLU A OE2 
1901  N N   . LEU A 237 ? 0.3696 0.5786 0.3939 -0.0604 0.0515  0.0482  538 LEU A N   
1902  C CA  . LEU A 237 ? 0.2953 0.4739 0.3063 -0.0707 0.0477  0.0496  538 LEU A CA  
1903  C C   . LEU A 237 ? 0.3252 0.4733 0.3155 -0.0661 0.0488  0.0509  538 LEU A C   
1904  O O   . LEU A 237 ? 0.3373 0.4878 0.3198 -0.0652 0.0551  0.0535  538 LEU A O   
1905  C CB  . LEU A 237 ? 0.2828 0.4683 0.2931 -0.0915 0.0509  0.0540  538 LEU A CB  
1906  C CG  . LEU A 237 ? 0.3665 0.5787 0.3952 -0.0997 0.0480  0.0528  538 LEU A CG  
1907  C CD1 . LEU A 237 ? 0.2901 0.5137 0.3177 -0.1217 0.0527  0.0573  538 LEU A CD1 
1908  C CD2 . LEU A 237 ? 0.3612 0.5540 0.3892 -0.0981 0.0392  0.0494  538 LEU A CD2 
1909  N N   . PHE A 238 ? 0.3173 0.4376 0.2981 -0.0632 0.0427  0.0491  539 PHE A N   
1910  C CA  . PHE A 238 ? 0.3346 0.4256 0.2949 -0.0590 0.0427  0.0505  539 PHE A CA  
1911  C C   . PHE A 238 ? 0.4021 0.4656 0.3506 -0.0656 0.0382  0.0513  539 PHE A C   
1912  O O   . PHE A 238 ? 0.4375 0.5004 0.3943 -0.0649 0.0326  0.0481  539 PHE A O   
1913  C CB  . PHE A 238 ? 0.3409 0.4273 0.3009 -0.0418 0.0391  0.0461  539 PHE A CB  
1914  C CG  . PHE A 238 ? 0.2996 0.4081 0.2680 -0.0332 0.0429  0.0445  539 PHE A CG  
1915  C CD1 . PHE A 238 ? 0.2787 0.4095 0.2650 -0.0282 0.0415  0.0410  539 PHE A CD1 
1916  C CD2 . PHE A 238 ? 0.2884 0.3941 0.2450 -0.0291 0.0480  0.0464  539 PHE A CD2 
1917  C CE1 . PHE A 238 ? 0.2790 0.4281 0.2706 -0.0187 0.0453  0.0393  539 PHE A CE1 
1918  C CE2 . PHE A 238 ? 0.3437 0.4685 0.3062 -0.0204 0.0517  0.0445  539 PHE A CE2 
1919  C CZ  . PHE A 238 ? 0.3047 0.4508 0.2845 -0.0148 0.0505  0.0408  539 PHE A CZ  
1920  N N   . GLN A 239 ? 0.4613 0.5004 0.3886 -0.0710 0.0409  0.0555  540 GLN A N   
1921  C CA  . GLN A 239 ? 0.5149 0.5234 0.4266 -0.0748 0.0370  0.0563  540 GLN A CA  
1922  C C   . GLN A 239 ? 0.4437 0.4342 0.3468 -0.0586 0.0321  0.0537  540 GLN A C   
1923  O O   . GLN A 239 ? 0.3804 0.3633 0.2719 -0.0508 0.0340  0.0551  540 GLN A O   
1924  C CB  . GLN A 239 ? 0.4963 0.4837 0.3861 -0.0882 0.0422  0.0623  540 GLN A CB  
1925  C CG  . GLN A 239 ? 0.5939 0.5455 0.4633 -0.0910 0.0386  0.0632  540 GLN A CG  
1926  C CD  . GLN A 239 ? 0.7581 0.6816 0.5997 -0.1003 0.0439  0.0694  540 GLN A CD  
1927  O OE1 . GLN A 239 ? 0.6836 0.5912 0.5088 -0.0907 0.0454  0.0718  540 GLN A OE1 
1928  N NE2 . GLN A 239 ? 0.9299 0.8468 0.7650 -0.1198 0.0466  0.0723  540 GLN A NE2 
1929  N N   . ILE A 240 ? 0.3979 0.3835 0.3068 -0.0537 0.0259  0.0497  541 ILE A N   
1930  C CA  . ILE A 240 ? 0.4640 0.4341 0.3646 -0.0395 0.0213  0.0474  541 ILE A CA  
1931  C C   . ILE A 240 ? 0.4951 0.4347 0.3691 -0.0396 0.0227  0.0518  541 ILE A C   
1932  O O   . ILE A 240 ? 0.5005 0.4221 0.3620 -0.0507 0.0242  0.0549  541 ILE A O   
1933  C CB  . ILE A 240 ? 0.3969 0.3658 0.3065 -0.0361 0.0152  0.0431  541 ILE A CB  
1934  C CG1 . ILE A 240 ? 0.3566 0.3529 0.2899 -0.0373 0.0141  0.0396  541 ILE A CG1 
1935  C CG2 . ILE A 240 ? 0.4079 0.3675 0.3123 -0.0216 0.0108  0.0404  541 ILE A CG2 
1936  C CD1 . ILE A 240 ? 0.4422 0.4374 0.3835 -0.0374 0.0090  0.0362  541 ILE A CD1 
1937  N N   . PRO A 241 ? 0.5161 0.4478 0.3788 -0.0280 0.0224  0.0524  542 PRO A N   
1938  C CA  . PRO A 241 ? 0.5644 0.4649 0.3995 -0.0256 0.0231  0.0567  542 PRO A CA  
1939  C C   . PRO A 241 ? 0.5349 0.4142 0.3613 -0.0239 0.0188  0.0556  542 PRO A C   
1940  O O   . PRO A 241 ? 0.4720 0.3590 0.3097 -0.0145 0.0135  0.0509  542 PRO A O   
1941  C CB  . PRO A 241 ? 0.5557 0.4584 0.3860 -0.0101 0.0210  0.0556  542 PRO A CB  
1942  C CG  . PRO A 241 ? 0.4774 0.4094 0.3272 -0.0102 0.0228  0.0530  542 PRO A CG  
1943  C CD  . PRO A 241 ? 0.4855 0.4356 0.3578 -0.0173 0.0216  0.0495  542 PRO A CD  
1944  N N   . PRO A 242 ? 0.4862 0.3386 0.2921 -0.0337 0.0212  0.0597  543 PRO A N   
1945  C CA  . PRO A 242 ? 0.5292 0.3606 0.3262 -0.0332 0.0176  0.0583  543 PRO A CA  
1946  C C   . PRO A 242 ? 0.5872 0.4059 0.3741 -0.0142 0.0129  0.0565  543 PRO A C   
1947  O O   . PRO A 242 ? 0.5923 0.4071 0.3821 -0.0094 0.0089  0.0531  543 PRO A O   
1948  C CB  . PRO A 242 ? 0.5536 0.3542 0.3249 -0.0475 0.0220  0.0637  543 PRO A CB  
1949  C CG  . PRO A 242 ? 0.6336 0.4522 0.4124 -0.0609 0.0280  0.0668  543 PRO A CG  
1950  C CD  . PRO A 242 ? 0.5672 0.4081 0.3579 -0.0477 0.0279  0.0656  543 PRO A CD  
1951  N N   . GLU A 243 ? 0.5297 0.3446 0.3055 -0.0028 0.0131  0.0586  544 GLU A N   
1952  C CA  . GLU A 243 ? 0.5470 0.3565 0.3161 0.0161  0.0081  0.0566  544 GLU A CA  
1953  C C   . GLU A 243 ? 0.4929 0.3337 0.2899 0.0232  0.0034  0.0501  544 GLU A C   
1954  O O   . GLU A 243 ? 0.5256 0.3663 0.3216 0.0366  -0.0010 0.0475  544 GLU A O   
1955  C CB  . GLU A 243 ? 0.6146 0.4161 0.3663 0.0266  0.0089  0.0601  544 GLU A CB  
1956  C CG  . GLU A 243 ? 0.5584 0.3884 0.3268 0.0266  0.0099  0.0588  544 GLU A CG  
1957  C CD  . GLU A 243 ? 0.6275 0.4564 0.3923 0.0117  0.0168  0.0631  544 GLU A CD  
1958  O OE1 . GLU A 243 ? 0.5820 0.3928 0.3364 -0.0014 0.0204  0.0663  544 GLU A OE1 
1959  O OE2 . GLU A 243 ? 0.7915 0.6373 0.5625 0.0128  0.0188  0.0632  544 GLU A OE2 
1960  N N   . LEU A 244 ? 0.4460 0.3133 0.2667 0.0149  0.0045  0.0476  545 LEU A N   
1961  C CA  . LEU A 244 ? 0.4227 0.3152 0.2672 0.0198  0.0004  0.0417  545 LEU A CA  
1962  C C   . LEU A 244 ? 0.4275 0.3196 0.2811 0.0140  -0.0012 0.0392  545 LEU A C   
1963  O O   . LEU A 244 ? 0.3917 0.3002 0.2615 0.0189  -0.0047 0.0346  545 LEU A O   
1964  C CB  . LEU A 244 ? 0.3937 0.3126 0.2576 0.0155  0.0019  0.0397  545 LEU A CB  
1965  C CG  . LEU A 244 ? 0.4776 0.4026 0.3365 0.0223  0.0026  0.0406  545 LEU A CG  
1966  C CD1 . LEU A 244 ? 0.4320 0.3827 0.3109 0.0196  0.0034  0.0371  545 LEU A CD1 
1967  C CD2 . LEU A 244 ? 0.4933 0.4153 0.3440 0.0372  -0.0022 0.0390  545 LEU A CD2 
1968  N N   . VAL A 245 ? 0.4466 0.3207 0.2898 0.0029  0.0013  0.0419  546 VAL A N   
1969  C CA  . VAL A 245 ? 0.4541 0.3282 0.3053 -0.0042 -0.0003 0.0395  546 VAL A CA  
1970  C C   . VAL A 245 ? 0.4533 0.3010 0.2852 0.0033  -0.0024 0.0395  546 VAL A C   
1971  O O   . VAL A 245 ? 0.5069 0.3260 0.3161 -0.0018 -0.0004 0.0429  546 VAL A O   
1972  C CB  . VAL A 245 ? 0.4952 0.3684 0.3478 -0.0220 0.0031  0.0417  546 VAL A CB  
1973  C CG1 . VAL A 245 ? 0.4358 0.3112 0.2973 -0.0285 0.0005  0.0387  546 VAL A CG1 
1974  C CG2 . VAL A 245 ? 0.4691 0.3687 0.3388 -0.0273 0.0058  0.0421  546 VAL A CG2 
1975  N N   . LEU A 246 ? 0.4147 0.2715 0.2544 0.0155  -0.0061 0.0356  547 LEU A N   
1976  C CA  . LEU A 246 ? 0.4302 0.2657 0.2532 0.0250  -0.0079 0.0351  547 LEU A CA  
1977  C C   . LEU A 246 ? 0.5038 0.3285 0.3257 0.0148  -0.0080 0.0337  547 LEU A C   
1978  O O   . LEU A 246 ? 0.5387 0.3835 0.3812 0.0078  -0.0091 0.0308  547 LEU A O   
1979  C CB  . LEU A 246 ? 0.4928 0.3470 0.3272 0.0401  -0.0115 0.0312  547 LEU A CB  
1980  C CG  . LEU A 246 ? 0.5973 0.4363 0.4176 0.0531  -0.0133 0.0300  547 LEU A CG  
1981  C CD1 . LEU A 246 ? 0.6376 0.4430 0.4266 0.0597  -0.0119 0.0344  547 LEU A CD1 
1982  C CD2 . LEU A 246 ? 0.5819 0.4464 0.4160 0.0669  -0.0164 0.0267  547 LEU A CD2 
1983  N N   . GLU A 247 ? 0.4960 0.2871 0.2916 0.0140  -0.0071 0.0359  548 GLU A N   
1984  C CA  . GLU A 247 ? 0.5733 0.3489 0.3626 0.0035  -0.0073 0.0347  548 GLU A CA  
1985  C C   . GLU A 247 ? 0.5944 0.3423 0.3608 0.0160  -0.0085 0.0337  548 GLU A C   
1986  O O   . GLU A 247 ? 0.6024 0.3335 0.3498 0.0295  -0.0081 0.0359  548 GLU A O   
1987  C CB  . GLU A 247 ? 0.5641 0.3221 0.3405 -0.0152 -0.0042 0.0384  548 GLU A CB  
1988  C CG  . GLU A 247 ? 0.5036 0.2924 0.3051 -0.0292 -0.0030 0.0386  548 GLU A CG  
1989  C CD  . GLU A 247 ? 0.5888 0.3645 0.3788 -0.0482 0.0005  0.0424  548 GLU A CD  
1990  O OE1 . GLU A 247 ? 0.7029 0.4585 0.4726 -0.0489 0.0037  0.0468  548 GLU A OE1 
1991  O OE2 . GLU A 247 ? 0.6085 0.3950 0.4094 -0.0630 0.0000  0.0411  548 GLU A OE2 
1992  N N   . VAL A 248 ? 0.6035 0.3472 0.3710 0.0126  -0.0100 0.0304  549 VAL A N   
1993  C CA  . VAL A 248 ? 0.6064 0.3252 0.3528 0.0253  -0.0109 0.0289  549 VAL A CA  
1994  C C   . VAL A 248 ? 0.6417 0.3258 0.3646 0.0124  -0.0102 0.0292  549 VAL A C   
1995  O O   . VAL A 248 ? 0.7200 0.4134 0.4550 -0.0016 -0.0114 0.0269  549 VAL A O   
1996  C CB  . VAL A 248 ? 0.5692 0.3128 0.3353 0.0352  -0.0132 0.0240  549 VAL A CB  
1997  C CG1 . VAL A 248 ? 0.5744 0.2939 0.3178 0.0507  -0.0134 0.0225  549 VAL A CG1 
1998  C CG2 . VAL A 248 ? 0.5360 0.3159 0.3269 0.0440  -0.0141 0.0233  549 VAL A CG2 
1999  N N   . PRO A 249 ? 0.6456 0.2887 0.3337 0.0162  -0.0086 0.0319  550 PRO A N   
2000  C CA  . PRO A 249 ? 0.6940 0.3002 0.3562 0.0048  -0.0084 0.0313  550 PRO A CA  
2001  C C   . PRO A 249 ? 0.6907 0.2963 0.3533 0.0143  -0.0106 0.0263  550 PRO A C   
2002  O O   . PRO A 249 ? 0.6898 0.3015 0.3527 0.0353  -0.0110 0.0248  550 PRO A O   
2003  C CB  . PRO A 249 ? 0.6976 0.2582 0.3197 0.0119  -0.0060 0.0354  550 PRO A CB  
2004  C CG  . PRO A 249 ? 0.7270 0.3045 0.3568 0.0256  -0.0052 0.0387  550 PRO A CG  
2005  C CD  . PRO A 249 ? 0.6436 0.2702 0.3118 0.0339  -0.0075 0.0351  550 PRO A CD  
2006  N N   . ILE A 250 ? 0.6723 0.2731 0.3356 -0.0011 -0.0120 0.0235  551 ILE A N   
2007  C CA  . ILE A 250 ? 0.6417 0.2447 0.3072 0.0065  -0.0139 0.0186  551 ILE A CA  
2008  C C   . ILE A 250 ? 0.7170 0.2698 0.3412 0.0118  -0.0133 0.0178  551 ILE A C   
2009  O O   . ILE A 250 ? 0.7392 0.2594 0.3399 -0.0045 -0.0130 0.0188  551 ILE A O   
2010  C CB  . ILE A 250 ? 0.6823 0.3094 0.3712 -0.0108 -0.0164 0.0157  551 ILE A CB  
2011  C CG1 . ILE A 250 ? 0.6384 0.3107 0.3643 -0.0162 -0.0167 0.0169  551 ILE A CG1 
2012  C CG2 . ILE A 250 ? 0.6237 0.2553 0.3155 -0.0012 -0.0180 0.0109  551 ILE A CG2 
2013  C CD1 . ILE A 250 ? 0.4877 0.1909 0.2358 0.0016  -0.0168 0.0156  551 ILE A CD1 
2014  N N   . ARG A 251 ? 0.7372 0.2834 0.3514 0.0345  -0.0128 0.0159  552 ARG A N   
2015  C CA  . ARG A 251 ? 0.7906 0.2903 0.3657 0.0429  -0.0121 0.0143  552 ARG A CA  
2016  C C   . ARG A 251 ? 0.7334 0.2474 0.3163 0.0583  -0.0127 0.0094  552 ARG A C   
2017  O O   . ARG A 251 ? 0.6694 0.2276 0.2860 0.0642  -0.0133 0.0080  552 ARG A O   
2018  C CB  . ARG A 251 ? 0.8808 0.3466 0.4237 0.0591  -0.0098 0.0181  552 ARG A CB  
2019  C CG  . ARG A 251 ? 0.8744 0.3680 0.4319 0.0834  -0.0094 0.0193  552 ARG A CG  
2020  C CD  . ARG A 251 ? 0.8374 0.3647 0.4227 0.0759  -0.0096 0.0227  552 ARG A CD  
2021  N NE  . ARG A 251 ? 0.8674 0.4095 0.4558 0.0989  -0.0094 0.0245  552 ARG A NE  
2022  C CZ  . ARG A 251 ? 0.7730 0.3508 0.3877 0.0995  -0.0100 0.0264  552 ARG A CZ  
2023  N NH1 . ARG A 251 ? 0.7162 0.3053 0.3302 0.1212  -0.0104 0.0275  552 ARG A NH1 
2024  N NH2 . ARG A 251 ? 0.6258 0.2290 0.2670 0.0795  -0.0103 0.0269  552 ARG A NH2 
2025  N N   . HIS A 252 ? 0.7761 0.2511 0.3262 0.0640  -0.0123 0.0067  553 HIS A N   
2026  C CA  . HIS A 252 ? 0.7556 0.2391 0.3084 0.0769  -0.0123 0.0019  553 HIS A CA  
2027  C C   . HIS A 252 ? 0.8031 0.2712 0.3326 0.1043  -0.0098 0.0015  553 HIS A C   
2028  O O   . HIS A 252 ? 0.8314 0.2718 0.3324 0.1064  -0.0083 0.0031  553 HIS A O   
2029  C CB  . HIS A 252 ? 0.7801 0.2374 0.3158 0.0608  -0.0140 -0.0019 553 HIS A CB  
2030  C CG  . HIS A 252 ? 0.8042 0.2788 0.3502 0.0688  -0.0143 -0.0068 553 HIS A CG  
2031  N ND1 . HIS A 252 ? 0.8867 0.3468 0.4121 0.0901  -0.0120 -0.0094 553 HIS A ND1 
2032  C CD2 . HIS A 252 ? 0.8173 0.3260 0.3927 0.0580  -0.0163 -0.0093 553 HIS A CD2 
2033  C CE1 . HIS A 252 ? 0.8526 0.3299 0.3909 0.0925  -0.0123 -0.0136 553 HIS A CE1 
2034  N NE2 . HIS A 252 ? 0.8386 0.3473 0.4080 0.0726  -0.0150 -0.0134 553 HIS A NE2 
2035  N N   . PRO A 253 ? 0.7433 0.2370 0.2874 0.1244  -0.0088 -0.0009 554 PRO A N   
2036  C CA  . PRO A 253 ? 0.8296 0.3225 0.3579 0.1496  -0.0063 -0.0011 554 PRO A CA  
2037  C C   . PRO A 253 ? 0.9534 0.4119 0.4462 0.1523  -0.0049 -0.0032 554 PRO A C   
2038  O O   . PRO A 253 ? 1.0149 0.4658 0.4881 0.1718  -0.0029 -0.0027 554 PRO A O   
2039  C CB  . PRO A 253 ? 0.7858 0.3203 0.3428 0.1659  -0.0055 -0.0035 554 PRO A CB  
2040  C CG  . PRO A 253 ? 0.7822 0.3385 0.3654 0.1453  -0.0072 -0.0059 554 PRO A CG  
2041  C CD  . PRO A 253 ? 0.6974 0.2432 0.2834 0.1206  -0.0096 -0.0030 554 PRO A CD  
2042  N N   . LYS A 254 ? 0.9373 0.3751 0.4203 0.1334  -0.0063 -0.0054 555 LYS A N   
2043  C CA  . LYS A 254 ? 0.9716 0.3771 0.4212 0.1346  -0.0056 -0.0075 555 LYS A CA  
2044  C C   . LYS A 254 ? 0.9997 0.3697 0.4262 0.1104  -0.0072 -0.0068 555 LYS A C   
2045  O O   . LYS A 254 ? 1.1483 0.4840 0.5392 0.1131  -0.0062 -0.0065 555 LYS A O   
2046  C CB  . LYS A 254 ? 1.0556 0.4753 0.5161 0.1369  -0.0057 -0.0118 555 LYS A CB  
2047  C CG  . LYS A 254 ? 1.2147 0.6158 0.6473 0.1527  -0.0036 -0.0134 555 LYS A CG  
2048  C CD  . LYS A 254 ? 1.2892 0.6890 0.7234 0.1433  -0.0047 -0.0174 555 LYS A CD  
2049  C CE  . LYS A 254 ? 1.3095 0.7484 0.7828 0.1392  -0.0054 -0.0199 555 LYS A CE  
2050  N NZ  . LYS A 254 ? 1.3241 0.7585 0.8002 0.1201  -0.0081 -0.0235 555 LYS A NZ  
2051  N N   . PHE A 255 ? 0.9584 0.3370 0.4040 0.0866  -0.0099 -0.0065 556 PHE A N   
2052  C CA  . PHE A 255 ? 0.9673 0.3196 0.3956 0.0610  -0.0117 -0.0061 556 PHE A CA  
2053  C C   . PHE A 255 ? 0.9620 0.3055 0.3848 0.0545  -0.0106 -0.0017 556 PHE A C   
2054  O O   . PHE A 255 ? 0.9416 0.3075 0.3906 0.0444  -0.0115 0.0006  556 PHE A O   
2055  C CB  . PHE A 255 ? 0.9597 0.3304 0.4125 0.0385  -0.0153 -0.0082 556 PHE A CB  
2056  C CG  . PHE A 255 ? 0.9648 0.3437 0.4223 0.0438  -0.0164 -0.0128 556 PHE A CG  
2057  C CD1 . PHE A 255 ? 0.9193 0.3266 0.4071 0.0337  -0.0190 -0.0152 556 PHE A CD1 
2058  C CD2 . PHE A 255 ? 0.9949 0.3528 0.4254 0.0591  -0.0146 -0.0146 556 PHE A CD2 
2059  C CE1 . PHE A 255 ? 0.8934 0.3082 0.3845 0.0385  -0.0198 -0.0196 556 PHE A CE1 
2060  C CE2 . PHE A 255 ? 1.0225 0.3884 0.4570 0.0641  -0.0151 -0.0186 556 PHE A CE2 
2061  C CZ  . PHE A 255 ? 0.8997 0.2941 0.3646 0.0537  -0.0177 -0.0212 556 PHE A CZ  
2062  N N   . GLU A 256 ? 1.0096 0.3195 0.3966 0.0605  -0.0085 -0.0005 557 GLU A N   
2063  C CA  . GLU A 256 ? 1.1234 0.4224 0.5018 0.0556  -0.0070 0.0034  557 GLU A CA  
2064  C C   . GLU A 256 ? 1.0695 0.3660 0.4538 0.0244  -0.0086 0.0047  557 GLU A C   
2065  O O   . GLU A 256 ? 1.0276 0.3281 0.4181 0.0169  -0.0075 0.0084  557 GLU A O   
2066  C CB  . GLU A 256 ? 1.2657 0.5264 0.6011 0.0689  -0.0044 0.0038  557 GLU A CB  
2067  C CG  . GLU A 256 ? 1.4142 0.6822 0.7450 0.1009  -0.0027 0.0031  557 GLU A CG  
2068  C CD  . GLU A 256 ? 1.6502 0.8823 0.9390 0.1158  -0.0001 0.0040  557 GLU A CD  
2069  O OE1 . GLU A 256 ? 1.7296 0.9675 1.0119 0.1424  0.0014  0.0036  557 GLU A OE1 
2070  O OE2 . GLU A 256 ? 1.7654 0.9644 1.0273 0.1008  0.0005  0.0051  557 GLU A OE2 
2071  N N   . TRP A 257 ? 1.0591 0.3525 0.4434 0.0061  -0.0112 0.0019  558 TRP A N   
2072  C CA  . TRP A 257 ? 1.0324 0.3301 0.4256 -0.0239 -0.0130 0.0029  558 TRP A CA  
2073  C C   . TRP A 257 ? 0.9805 0.3196 0.4167 -0.0327 -0.0146 0.0044  558 TRP A C   
2074  O O   . TRP A 257 ? 0.9709 0.3197 0.4183 -0.0555 -0.0154 0.0063  558 TRP A O   
2075  C CB  . TRP A 257 ? 1.0171 0.3016 0.3974 -0.0400 -0.0159 -0.0006 558 TRP A CB  
2076  C CG  . TRP A 257 ? 1.0500 0.3516 0.4456 -0.0311 -0.0182 -0.0044 558 TRP A CG  
2077  C CD1 . TRP A 257 ? 1.1035 0.3877 0.4785 -0.0140 -0.0176 -0.0072 558 TRP A CD1 
2078  C CD2 . TRP A 257 ? 0.9712 0.3102 0.4046 -0.0389 -0.0211 -0.0059 558 TRP A CD2 
2079  N NE1 . TRP A 257 ? 1.0460 0.3548 0.4441 -0.0109 -0.0198 -0.0104 558 TRP A NE1 
2080  C CE2 . TRP A 257 ? 0.9410 0.2825 0.3742 -0.0261 -0.0222 -0.0098 558 TRP A CE2 
2081  C CE3 . TRP A 257 ? 0.8485 0.2188 0.3146 -0.0554 -0.0229 -0.0043 558 TRP A CE3 
2082  C CZ2 . TRP A 257 ? 0.9083 0.2811 0.3721 -0.0291 -0.0249 -0.0125 558 TRP A CZ2 
2083  C CZ3 . TRP A 257 ? 0.9123 0.3138 0.4086 -0.0580 -0.0260 -0.0068 558 TRP A CZ3 
2084  C CH2 . TRP A 257 ? 0.9078 0.3095 0.4022 -0.0451 -0.0270 -0.0110 558 TRP A CH2 
2085  N N   . PHE A 258 ? 0.8569 0.2212 0.3168 -0.0154 -0.0150 0.0035  559 PHE A N   
2086  C CA  . PHE A 258 ? 0.8462 0.2476 0.3448 -0.0243 -0.0169 0.0045  559 PHE A CA  
2087  C C   . PHE A 258 ? 0.8704 0.2813 0.3796 -0.0323 -0.0152 0.0098  559 PHE A C   
2088  O O   . PHE A 258 ? 0.7951 0.2286 0.3277 -0.0515 -0.0166 0.0113  559 PHE A O   
2089  C CB  . PHE A 258 ? 0.8503 0.2739 0.3686 -0.0023 -0.0170 0.0028  559 PHE A CB  
2090  C CG  . PHE A 258 ? 0.8567 0.3205 0.4137 -0.0124 -0.0197 0.0018  559 PHE A CG  
2091  C CD1 . PHE A 258 ? 0.7898 0.2648 0.3557 -0.0179 -0.0225 -0.0029 559 PHE A CD1 
2092  C CD2 . PHE A 258 ? 0.7492 0.2508 0.3378 -0.0162 -0.0192 0.0055  559 PHE A CD2 
2093  C CE1 . PHE A 258 ? 0.7545 0.2765 0.3594 -0.0262 -0.0248 -0.0036 559 PHE A CE1 
2094  C CE2 . PHE A 258 ? 0.7713 0.3196 0.3989 -0.0244 -0.0214 0.0045  559 PHE A CE2 
2095  C CZ  . PHE A 258 ? 0.7008 0.2590 0.3364 -0.0291 -0.0242 0.0000  559 PHE A CZ  
2096  N N   . LYS A 259 ? 0.8761 0.2713 0.3681 -0.0174 -0.0120 0.0128  560 LYS A N   
2097  C CA  . LYS A 259 ? 0.9467 0.3503 0.4472 -0.0234 -0.0101 0.0181  560 LYS A CA  
2098  C C   . LYS A 259 ? 1.0302 0.4254 0.5239 -0.0516 -0.0097 0.0194  560 LYS A C   
2099  O O   . LYS A 259 ? 0.9821 0.3964 0.4940 -0.0646 -0.0088 0.0233  560 LYS A O   
2100  C CB  . LYS A 259 ? 0.9851 0.3714 0.4649 -0.0015 -0.0071 0.0204  560 LYS A CB  
2101  C CG  . LYS A 259 ? 1.0921 0.4370 0.5304 0.0004  -0.0054 0.0187  560 LYS A CG  
2102  C CD  . LYS A 259 ? 1.0249 0.3547 0.4435 0.0212  -0.0026 0.0212  560 LYS A CD  
2103  C CE  . LYS A 259 ? 1.1158 0.4025 0.4905 0.0257  -0.0010 0.0192  560 LYS A CE  
2104  N NZ  . LYS A 259 ? 1.1525 0.4312 0.5170 0.0354  -0.0024 0.0146  560 LYS A NZ  
2105  N N   . ASP A 260 ? 0.9409 0.3093 0.4084 -0.0615 -0.0103 0.0164  561 ASP A N   
2106  C CA  . ASP A 260 ? 1.0577 0.4197 0.5181 -0.0889 -0.0102 0.0173  561 ASP A CA  
2107  C C   . ASP A 260 ? 1.0214 0.4197 0.5154 -0.1104 -0.0131 0.0168  561 ASP A C   
2108  O O   . ASP A 260 ? 1.0447 0.4491 0.5412 -0.1332 -0.0127 0.0184  561 ASP A O   
2109  C CB  . ASP A 260 ? 1.2438 0.5691 0.6676 -0.0939 -0.0107 0.0140  561 ASP A CB  
2110  C CG  . ASP A 260 ? 1.4009 0.6891 0.7886 -0.0733 -0.0077 0.0144  561 ASP A CG  
2111  O OD1 . ASP A 260 ? 1.4451 0.7320 0.8314 -0.0638 -0.0047 0.0181  561 ASP A OD1 
2112  O OD2 . ASP A 260 ? 1.4672 0.7281 0.8273 -0.0662 -0.0083 0.0112  561 ASP A OD2 
2113  N N   . LEU A 261 ? 0.9250 0.3484 0.4444 -0.1034 -0.0160 0.0146  562 LEU A N   
2114  C CA  . LEU A 261 ? 0.9140 0.3750 0.4671 -0.1216 -0.0189 0.0143  562 LEU A CA  
2115  C C   . LEU A 261 ? 0.8931 0.3792 0.4686 -0.1280 -0.0164 0.0196  562 LEU A C   
2116  O O   . LEU A 261 ? 0.8278 0.3461 0.4295 -0.1455 -0.0180 0.0201  562 LEU A O   
2117  C CB  . LEU A 261 ? 0.9043 0.3845 0.4778 -0.1108 -0.0223 0.0107  562 LEU A CB  
2118  C CG  . LEU A 261 ? 0.9386 0.4010 0.4949 -0.1051 -0.0249 0.0052  562 LEU A CG  
2119  C CD1 . LEU A 261 ? 0.8576 0.3339 0.4296 -0.0866 -0.0264 0.0024  562 LEU A CD1 
2120  C CD2 . LEU A 261 ? 0.9975 0.4687 0.5571 -0.1291 -0.0287 0.0027  562 LEU A CD2 
2121  N N   . GLY A 262 ? 0.8654 0.3392 0.4312 -0.1133 -0.0126 0.0236  563 GLY A N   
2122  C CA  . GLY A 262 ? 0.8175 0.3121 0.4007 -0.1180 -0.0097 0.0292  563 GLY A CA  
2123  C C   . GLY A 262 ? 0.7850 0.3328 0.4120 -0.1113 -0.0113 0.0284  563 GLY A C   
2124  O O   . GLY A 262 ? 0.7972 0.3766 0.4475 -0.1208 -0.0098 0.0311  563 GLY A O   
2125  N N   . LEU A 263 ? 0.7471 0.3085 0.3867 -0.0944 -0.0140 0.0242  564 LEU A N   
2126  C CA  . LEU A 263 ? 0.7061 0.3184 0.3865 -0.0873 -0.0155 0.0229  564 LEU A CA  
2127  C C   . LEU A 263 ? 0.6931 0.3189 0.3830 -0.0678 -0.0131 0.0255  564 LEU A C   
2128  O O   . LEU A 263 ? 0.6817 0.2803 0.3485 -0.0521 -0.0115 0.0267  564 LEU A O   
2129  C CB  . LEU A 263 ? 0.6320 0.2542 0.3218 -0.0792 -0.0191 0.0176  564 LEU A CB  
2130  C CG  . LEU A 263 ? 0.7214 0.3308 0.4013 -0.0973 -0.0224 0.0144  564 LEU A CG  
2131  C CD1 . LEU A 263 ? 0.7170 0.3246 0.3961 -0.0848 -0.0251 0.0095  564 LEU A CD1 
2132  C CD2 . LEU A 263 ? 0.7008 0.3467 0.4083 -0.1171 -0.0244 0.0147  564 LEU A CD2 
2133  N N   . LYS A 264 ? 0.6210 0.2891 0.3441 -0.0686 -0.0130 0.0262  565 LYS A N   
2134  C CA  . LYS A 264 ? 0.6825 0.3705 0.4198 -0.0505 -0.0118 0.0273  565 LYS A CA  
2135  C C   . LYS A 264 ? 0.6058 0.3395 0.3805 -0.0510 -0.0136 0.0251  565 LYS A C   
2136  O O   . LYS A 264 ? 0.5661 0.3159 0.3547 -0.0653 -0.0153 0.0238  565 LYS A O   
2137  C CB  . LYS A 264 ? 0.7049 0.3843 0.4321 -0.0513 -0.0082 0.0325  565 LYS A CB  
2138  C CG  . LYS A 264 ? 0.7711 0.4645 0.5082 -0.0723 -0.0062 0.0353  565 LYS A CG  
2139  C CD  . LYS A 264 ? 0.7951 0.4806 0.5216 -0.0710 -0.0020 0.0406  565 LYS A CD  
2140  C CE  . LYS A 264 ? 0.8862 0.5687 0.6078 -0.0944 0.0012  0.0441  565 LYS A CE  
2141  N NZ  . LYS A 264 ? 0.9296 0.6040 0.6397 -0.0935 0.0059  0.0496  565 LYS A NZ  
2142  N N   . TRP A 265 ? 0.5229 0.2769 0.3125 -0.0352 -0.0134 0.0247  566 TRP A N   
2143  C CA  . TRP A 265 ? 0.5304 0.3243 0.3523 -0.0357 -0.0144 0.0234  566 TRP A CA  
2144  C C   . TRP A 265 ? 0.5238 0.3312 0.3532 -0.0239 -0.0128 0.0251  566 TRP A C   
2145  O O   . TRP A 265 ? 0.5572 0.3460 0.3688 -0.0131 -0.0117 0.0268  566 TRP A O   
2146  C CB  . TRP A 265 ? 0.3902 0.1985 0.2258 -0.0297 -0.0173 0.0190  566 TRP A CB  
2147  C CG  . TRP A 265 ? 0.3722 0.2136 0.2353 -0.0363 -0.0187 0.0177  566 TRP A CG  
2148  C CD1 . TRP A 265 ? 0.3403 0.2085 0.2248 -0.0280 -0.0192 0.0162  566 TRP A CD1 
2149  C CD2 . TRP A 265 ? 0.3902 0.2411 0.2613 -0.0524 -0.0198 0.0179  566 TRP A CD2 
2150  N NE1 . TRP A 265 ? 0.3440 0.2351 0.2475 -0.0367 -0.0204 0.0156  566 TRP A NE1 
2151  C CE2 . TRP A 265 ? 0.3872 0.2703 0.2840 -0.0511 -0.0210 0.0166  566 TRP A CE2 
2152  C CE3 . TRP A 265 ? 0.4269 0.2626 0.2851 -0.0682 -0.0202 0.0189  566 TRP A CE3 
2153  C CZ2 . TRP A 265 ? 0.3884 0.2902 0.2989 -0.0627 -0.0225 0.0165  566 TRP A CZ2 
2154  C CZ3 . TRP A 265 ? 0.3667 0.2238 0.2403 -0.0815 -0.0219 0.0186  566 TRP A CZ3 
2155  C CH2 . TRP A 265 ? 0.3354 0.2260 0.2352 -0.0776 -0.0231 0.0175  566 TRP A CH2 
2156  N N   . TYR A 266 ? 0.4242 0.2636 0.2789 -0.0257 -0.0130 0.0245  567 TYR A N   
2157  C CA  . TYR A 266 ? 0.5030 0.3574 0.3661 -0.0157 -0.0119 0.0254  567 TYR A CA  
2158  C C   . TYR A 266 ? 0.4772 0.3464 0.3518 -0.0020 -0.0141 0.0218  567 TYR A C   
2159  O O   . TYR A 266 ? 0.4539 0.3304 0.3375 -0.0026 -0.0160 0.0188  567 TYR A O   
2160  C CB  . TYR A 266 ? 0.3875 0.2667 0.2692 -0.0241 -0.0105 0.0265  567 TYR A CB  
2161  C CG  . TYR A 266 ? 0.4097 0.3099 0.3113 -0.0315 -0.0123 0.0240  567 TYR A CG  
2162  C CD1 . TYR A 266 ? 0.3799 0.3021 0.3002 -0.0243 -0.0141 0.0209  567 TYR A CD1 
2163  C CD2 . TYR A 266 ? 0.4245 0.3221 0.3249 -0.0460 -0.0125 0.0247  567 TYR A CD2 
2164  C CE1 . TYR A 266 ? 0.4115 0.3505 0.3474 -0.0296 -0.0158 0.0189  567 TYR A CE1 
2165  C CE2 . TYR A 266 ? 0.4373 0.3553 0.3553 -0.0513 -0.0147 0.0225  567 TYR A CE2 
2166  C CZ  . TYR A 266 ? 0.4246 0.3622 0.3597 -0.0423 -0.0163 0.0198  567 TYR A CZ  
2167  O OH  . TYR A 266 ? 0.4612 0.4168 0.4114 -0.0461 -0.0185 0.0179  567 TYR A OH  
2168  N N   . GLY A 267 ? 0.4412 0.3157 0.3154 0.0097  -0.0139 0.0223  568 GLY A N   
2169  C CA  . GLY A 267 ? 0.3755 0.2646 0.2591 0.0220  -0.0159 0.0190  568 GLY A CA  
2170  C C   . GLY A 267 ? 0.3524 0.2708 0.2606 0.0198  -0.0169 0.0163  568 GLY A C   
2171  O O   . GLY A 267 ? 0.3905 0.3208 0.3081 0.0250  -0.0184 0.0131  568 GLY A O   
2172  N N   . LEU A 268 ? 0.3282 0.2576 0.2459 0.0121  -0.0158 0.0175  569 LEU A N   
2173  C CA  . LEU A 268 ? 0.2616 0.2152 0.1984 0.0124  -0.0165 0.0152  569 LEU A CA  
2174  C C   . LEU A 268 ? 0.3432 0.3068 0.2930 0.0030  -0.0167 0.0142  569 LEU A C   
2175  O O   . LEU A 268 ? 0.3171 0.2826 0.2688 -0.0052 -0.0152 0.0163  569 LEU A O   
2176  C CB  . LEU A 268 ? 0.2605 0.2201 0.1973 0.0134  -0.0150 0.0170  569 LEU A CB  
2177  C CG  . LEU A 268 ? 0.3575 0.3386 0.3100 0.0155  -0.0159 0.0141  569 LEU A CG  
2178  C CD1 . LEU A 268 ? 0.3560 0.3439 0.3105 0.0245  -0.0184 0.0111  569 LEU A CD1 
2179  C CD2 . LEU A 268 ? 0.3242 0.3110 0.2766 0.0149  -0.0140 0.0156  569 LEU A CD2 
2180  N N   . PRO A 269 ? 0.3146 0.2858 0.2732 0.0042  -0.0184 0.0112  570 PRO A N   
2181  C CA  . PRO A 269 ? 0.2697 0.2518 0.2406 -0.0026 -0.0190 0.0102  570 PRO A CA  
2182  C C   . PRO A 269 ? 0.3086 0.3073 0.2912 -0.0010 -0.0186 0.0091  570 PRO A C   
2183  O O   . PRO A 269 ? 0.2955 0.3009 0.2823 0.0044  -0.0194 0.0067  570 PRO A O   
2184  C CB  . PRO A 269 ? 0.2166 0.1975 0.1889 -0.0006 -0.0208 0.0077  570 PRO A CB  
2185  C CG  . PRO A 269 ? 0.2434 0.2246 0.2124 0.0088  -0.0208 0.0062  570 PRO A CG  
2186  C CD  . PRO A 269 ? 0.2626 0.2341 0.2201 0.0124  -0.0197 0.0087  570 PRO A CD  
2187  N N   . ALA A 270 ? 0.2892 0.2949 0.2767 -0.0059 -0.0174 0.0107  571 ALA A N   
2188  C CA  . ALA A 270 ? 0.2171 0.2351 0.2117 -0.0030 -0.0164 0.0099  571 ALA A CA  
2189  C C   . ALA A 270 ? 0.2887 0.3180 0.2929 -0.0069 -0.0161 0.0100  571 ALA A C   
2190  O O   . ALA A 270 ? 0.3267 0.3605 0.3317 -0.0115 -0.0142 0.0125  571 ALA A O   
2191  C CB  . ALA A 270 ? 0.2411 0.2566 0.2288 -0.0017 -0.0141 0.0121  571 ALA A CB  
2192  N N   . VAL A 271 ? 0.2819 0.3158 0.2923 -0.0049 -0.0178 0.0076  572 VAL A N   
2193  C CA  . VAL A 271 ? 0.2223 0.2662 0.2404 -0.0065 -0.0181 0.0078  572 VAL A CA  
2194  C C   . VAL A 271 ? 0.2267 0.2801 0.2483 -0.0027 -0.0160 0.0077  572 VAL A C   
2195  O O   . VAL A 271 ? 0.2585 0.3099 0.2782 0.0022  -0.0157 0.0055  572 VAL A O   
2196  C CB  . VAL A 271 ? 0.2493 0.2917 0.2698 -0.0047 -0.0205 0.0056  572 VAL A CB  
2197  C CG1 . VAL A 271 ? 0.2461 0.2987 0.2730 -0.0030 -0.0209 0.0057  572 VAL A CG1 
2198  C CG2 . VAL A 271 ? 0.2351 0.2698 0.2523 -0.0086 -0.0224 0.0058  572 VAL A CG2 
2199  N N   . SER A 272 ? 0.2281 0.2929 0.2545 -0.0049 -0.0145 0.0097  573 SER A N   
2200  C CA  . SER A 272 ? 0.2938 0.3681 0.3221 -0.0006 -0.0115 0.0099  573 SER A CA  
2201  C C   . SER A 272 ? 0.3075 0.3967 0.3436 0.0022  -0.0113 0.0101  573 SER A C   
2202  O O   . SER A 272 ? 0.3447 0.4440 0.3826 0.0063  -0.0083 0.0105  573 SER A O   
2203  C CB  . SER A 272 ? 0.2045 0.2803 0.2292 -0.0045 -0.0082 0.0127  573 SER A CB  
2204  O OG  . SER A 272 ? 0.2184 0.2968 0.2441 -0.0134 -0.0081 0.0155  573 SER A OG  
2205  N N   . ASN A 273 ? 0.2526 0.3438 0.2926 0.0011  -0.0143 0.0098  574 ASN A N   
2206  C CA  . ASN A 273 ? 0.2459 0.3526 0.2928 0.0054  -0.0147 0.0102  574 ASN A CA  
2207  C C   . ASN A 273 ? 0.2540 0.3535 0.2982 0.0134  -0.0168 0.0079  574 ASN A C   
2208  O O   . ASN A 273 ? 0.3032 0.4129 0.3511 0.0186  -0.0178 0.0082  574 ASN A O   
2209  C CB  . ASN A 273 ? 0.2983 0.4168 0.3516 -0.0021 -0.0167 0.0123  574 ASN A CB  
2210  C CG  . ASN A 273 ? 0.2658 0.3713 0.3155 -0.0068 -0.0207 0.0115  574 ASN A CG  
2211  O OD1 . ASN A 273 ? 0.2940 0.3829 0.3373 -0.0048 -0.0215 0.0097  574 ASN A OD1 
2212  N ND2 . ASN A 273 ? 0.3310 0.4454 0.3847 -0.0135 -0.0232 0.0127  574 ASN A ND2 
2213  N N   . MET A 274 ? 0.2569 0.3395 0.2939 0.0146  -0.0173 0.0056  575 MET A N   
2214  C CA  . MET A 274 ? 0.2425 0.3153 0.2746 0.0202  -0.0190 0.0035  575 MET A CA  
2215  C C   . MET A 274 ? 0.2988 0.3670 0.3251 0.0277  -0.0167 0.0015  575 MET A C   
2216  O O   . MET A 274 ? 0.2625 0.3343 0.2882 0.0285  -0.0141 0.0014  575 MET A O   
2217  C CB  . MET A 274 ? 0.2488 0.3071 0.2764 0.0156  -0.0208 0.0021  575 MET A CB  
2218  C CG  . MET A 274 ? 0.2537 0.3135 0.2843 0.0103  -0.0234 0.0035  575 MET A CG  
2219  S SD  . MET A 274 ? 0.3201 0.3647 0.3448 0.0068  -0.0247 0.0018  575 MET A SD  
2220  C CE  . MET A 274 ? 0.2591 0.2971 0.2792 0.0116  -0.0263 0.0012  575 MET A CE  
2221  N N   . LEU A 275 ? 0.2407 0.2993 0.2605 0.0334  -0.0178 0.0000  576 LEU A N   
2222  C CA  . LEU A 275 ? 0.3309 0.3806 0.3415 0.0411  -0.0160 -0.0022 576 LEU A CA  
2223  C C   . LEU A 275 ? 0.3418 0.3715 0.3426 0.0375  -0.0169 -0.0051 576 LEU A C   
2224  O O   . LEU A 275 ? 0.3530 0.3749 0.3519 0.0341  -0.0189 -0.0050 576 LEU A O   
2225  C CB  . LEU A 275 ? 0.4051 0.4578 0.4132 0.0515  -0.0162 -0.0015 576 LEU A CB  
2226  C CG  . LEU A 275 ? 0.5786 0.6204 0.5745 0.0621  -0.0141 -0.0037 576 LEU A CG  
2227  C CD1 . LEU A 275 ? 0.5976 0.6551 0.5967 0.0739  -0.0131 -0.0019 576 LEU A CD1 
2228  C CD2 . LEU A 275 ? 0.5682 0.5845 0.5494 0.0626  -0.0156 -0.0059 576 LEU A CD2 
2229  N N   . LEU A 276 ? 0.2814 0.3042 0.2758 0.0373  -0.0154 -0.0077 577 LEU A N   
2230  C CA  . LEU A 276 ? 0.3420 0.3482 0.3270 0.0326  -0.0163 -0.0110 577 LEU A CA  
2231  C C   . LEU A 276 ? 0.3304 0.3199 0.3008 0.0392  -0.0155 -0.0132 577 LEU A C   
2232  O O   . LEU A 276 ? 0.3465 0.3362 0.3121 0.0463  -0.0136 -0.0143 577 LEU A O   
2233  C CB  . LEU A 276 ? 0.2779 0.2868 0.2638 0.0276  -0.0160 -0.0128 577 LEU A CB  
2234  C CG  . LEU A 276 ? 0.2898 0.2851 0.2654 0.0230  -0.0168 -0.0169 577 LEU A CG  
2235  C CD1 . LEU A 276 ? 0.2673 0.2561 0.2424 0.0159  -0.0184 -0.0173 577 LEU A CD1 
2236  C CD2 . LEU A 276 ? 0.3236 0.3264 0.3014 0.0199  -0.0171 -0.0183 577 LEU A CD2 
2237  N N   . GLU A 277 ? 0.2951 0.2688 0.2569 0.0372  -0.0167 -0.0139 578 GLU A N   
2238  C CA  . GLU A 277 ? 0.3181 0.2710 0.2625 0.0436  -0.0160 -0.0157 578 GLU A CA  
2239  C C   . GLU A 277 ? 0.4115 0.3452 0.3433 0.0344  -0.0163 -0.0195 578 GLU A C   
2240  O O   . GLU A 277 ? 0.3815 0.3121 0.3146 0.0251  -0.0173 -0.0195 578 GLU A O   
2241  C CB  . GLU A 277 ? 0.4901 0.4379 0.4315 0.0491  -0.0171 -0.0130 578 GLU A CB  
2242  C CG  . GLU A 277 ? 0.6978 0.6265 0.6210 0.0607  -0.0162 -0.0137 578 GLU A CG  
2243  C CD  . GLU A 277 ? 0.8889 0.7869 0.7916 0.0553  -0.0161 -0.0163 578 GLU A CD  
2244  O OE1 . GLU A 277 ? 0.9741 0.8510 0.8578 0.0628  -0.0148 -0.0184 578 GLU A OE1 
2245  O OE2 . GLU A 277 ? 0.9069 0.8012 0.8113 0.0433  -0.0169 -0.0164 578 GLU A OE2 
2246  N N   . ILE A 278 ? 0.3832 0.3054 0.3028 0.0365  -0.0152 -0.0230 579 ILE A N   
2247  C CA  . ILE A 278 ? 0.4318 0.3359 0.3379 0.0267  -0.0157 -0.0272 579 ILE A CA  
2248  C C   . ILE A 278 ? 0.4595 0.3367 0.3423 0.0338  -0.0144 -0.0299 579 ILE A C   
2249  O O   . ILE A 278 ? 0.4339 0.3121 0.3127 0.0436  -0.0130 -0.0309 579 ILE A O   
2250  C CB  . ILE A 278 ? 0.4504 0.3672 0.3633 0.0200  -0.0165 -0.0299 579 ILE A CB  
2251  C CG1 . ILE A 278 ? 0.3348 0.2765 0.2685 0.0155  -0.0175 -0.0271 579 ILE A CG1 
2252  C CG2 . ILE A 278 ? 0.4617 0.3622 0.3611 0.0086  -0.0176 -0.0345 579 ILE A CG2 
2253  C CD1 . ILE A 278 ? 0.3253 0.2806 0.2652 0.0125  -0.0183 -0.0288 579 ILE A CD1 
2254  N N   . GLY A 279 ? 0.4518 0.3038 0.3177 0.0292  -0.0146 -0.0308 580 GLY A N   
2255  C CA  . GLY A 279 ? 0.5212 0.3412 0.3602 0.0346  -0.0134 -0.0337 580 GLY A CA  
2256  C C   . GLY A 279 ? 0.5343 0.3515 0.3672 0.0540  -0.0118 -0.0320 580 GLY A C   
2257  O O   . GLY A 279 ? 0.5286 0.3266 0.3425 0.0617  -0.0104 -0.0351 580 GLY A O   
2258  N N   . GLY A 280 ? 0.4429 0.2793 0.2910 0.0623  -0.0120 -0.0273 581 GLY A N   
2259  C CA  . GLY A 280 ? 0.5790 0.4201 0.4250 0.0810  -0.0107 -0.0254 581 GLY A CA  
2260  C C   . GLY A 280 ? 0.5238 0.3934 0.3866 0.0867  -0.0092 -0.0251 581 GLY A C   
2261  O O   . GLY A 280 ? 0.5243 0.4065 0.3907 0.1015  -0.0078 -0.0229 581 GLY A O   
2262  N N   . LEU A 281 ? 0.4402 0.3213 0.3130 0.0757  -0.0095 -0.0270 582 LEU A N   
2263  C CA  . LEU A 281 ? 0.4354 0.3432 0.3237 0.0793  -0.0079 -0.0260 582 LEU A CA  
2264  C C   . LEU A 281 ? 0.4165 0.3528 0.3294 0.0748  -0.0090 -0.0216 582 LEU A C   
2265  O O   . LEU A 281 ? 0.4474 0.3839 0.3668 0.0642  -0.0113 -0.0206 582 LEU A O   
2266  C CB  . LEU A 281 ? 0.4527 0.3582 0.3381 0.0705  -0.0079 -0.0299 582 LEU A CB  
2267  C CG  . LEU A 281 ? 0.4218 0.2956 0.2808 0.0708  -0.0077 -0.0352 582 LEU A CG  
2268  C CD1 . LEU A 281 ? 0.4430 0.3182 0.3008 0.0607  -0.0087 -0.0391 582 LEU A CD1 
2269  C CD2 . LEU A 281 ? 0.4753 0.3406 0.3206 0.0887  -0.0045 -0.0356 582 LEU A CD2 
2270  N N   . GLU A 282 ? 0.3956 0.3556 0.3211 0.0825  -0.0072 -0.0189 583 GLU A N   
2271  C CA  . GLU A 282 ? 0.3935 0.3793 0.3402 0.0786  -0.0082 -0.0147 583 GLU A CA  
2272  C C   . GLU A 282 ? 0.4526 0.4575 0.4110 0.0741  -0.0064 -0.0141 583 GLU A C   
2273  O O   . GLU A 282 ? 0.4070 0.4220 0.3654 0.0820  -0.0032 -0.0139 583 GLU A O   
2274  C CB  . GLU A 282 ? 0.4528 0.4518 0.4042 0.0905  -0.0078 -0.0116 583 GLU A CB  
2275  C CG  . GLU A 282 ? 0.5583 0.5368 0.4957 0.0968  -0.0096 -0.0118 583 GLU A CG  
2276  C CD  . GLU A 282 ? 0.6811 0.6769 0.6253 0.1085  -0.0102 -0.0084 583 GLU A CD  
2277  O OE1 . GLU A 282 ? 0.6414 0.6560 0.5909 0.1187  -0.0076 -0.0077 583 GLU A OE1 
2278  O OE2 . GLU A 282 ? 0.7652 0.7577 0.7099 0.1074  -0.0133 -0.0065 583 GLU A OE2 
2279  N N   . PHE A 283 ? 0.3482 0.3572 0.3150 0.0622  -0.0082 -0.0136 584 PHE A N   
2280  C CA  . PHE A 283 ? 0.2814 0.3055 0.2574 0.0574  -0.0069 -0.0124 584 PHE A CA  
2281  C C   . PHE A 283 ? 0.3601 0.4045 0.3521 0.0545  -0.0071 -0.0080 584 PHE A C   
2282  O O   . PHE A 283 ? 0.3498 0.3945 0.3479 0.0465  -0.0096 -0.0068 584 PHE A O   
2283  C CB  . PHE A 283 ? 0.3069 0.3222 0.2802 0.0477  -0.0089 -0.0147 584 PHE A CB  
2284  C CG  . PHE A 283 ? 0.3478 0.3448 0.3052 0.0486  -0.0091 -0.0195 584 PHE A CG  
2285  C CD1 . PHE A 283 ? 0.3125 0.2906 0.2597 0.0453  -0.0111 -0.0221 584 PHE A CD1 
2286  C CD2 . PHE A 283 ? 0.3762 0.3737 0.3272 0.0521  -0.0071 -0.0213 584 PHE A CD2 
2287  C CE1 . PHE A 283 ? 0.3894 0.3489 0.3202 0.0442  -0.0114 -0.0268 584 PHE A CE1 
2288  C CE2 . PHE A 283 ? 0.4163 0.3959 0.3511 0.0520  -0.0077 -0.0262 584 PHE A CE2 
2289  C CZ  . PHE A 283 ? 0.4252 0.3854 0.3498 0.0476  -0.0100 -0.0291 584 PHE A CZ  
2290  N N   . SER A 284 ? 0.3302 0.3918 0.3281 0.0608  -0.0043 -0.0057 585 SER A N   
2291  C CA  . SER A 284 ? 0.3002 0.3823 0.3122 0.0578  -0.0045 -0.0018 585 SER A CA  
2292  C C   . SER A 284 ? 0.3443 0.4348 0.3638 0.0474  -0.0039 0.0004  585 SER A C   
2293  O O   . SER A 284 ? 0.2974 0.4004 0.3266 0.0417  -0.0047 0.0034  585 SER A O   
2294  C CB  . SER A 284 ? 0.3469 0.4479 0.3631 0.0677  -0.0014 -0.0003 585 SER A CB  
2295  O OG  . SER A 284 ? 0.3698 0.4720 0.3802 0.0727  0.0029  -0.0015 585 SER A OG  
2296  N N   . ALA A 285 ? 0.3753 0.4582 0.3888 0.0451  -0.0026 -0.0009 586 ALA A N   
2297  C CA  . ALA A 285 ? 0.3194 0.4052 0.3360 0.0366  -0.0022 0.0011  586 ALA A CA  
2298  C C   . ALA A 285 ? 0.2627 0.3321 0.2721 0.0334  -0.0049 -0.0016 586 ALA A C   
2299  O O   . ALA A 285 ? 0.3070 0.3687 0.3078 0.0367  -0.0043 -0.0045 586 ALA A O   
2300  C CB  . ALA A 285 ? 0.3437 0.4399 0.3596 0.0380  0.0024  0.0028  586 ALA A CB  
2301  N N   . CYS A 286 ? 0.2619 0.3273 0.2746 0.0272  -0.0078 -0.0010 587 CYS A N   
2302  C CA  . CYS A 286 ? 0.2300 0.2838 0.2376 0.0244  -0.0104 -0.0036 587 CYS A CA  
2303  C C   . CYS A 286 ? 0.2804 0.3343 0.2917 0.0184  -0.0120 -0.0016 587 CYS A C   
2304  O O   . CYS A 286 ? 0.2900 0.3387 0.3023 0.0158  -0.0144 -0.0026 587 CYS A O   
2305  C CB  . CYS A 286 ? 0.3143 0.3585 0.3185 0.0258  -0.0124 -0.0065 587 CYS A CB  
2306  S SG  . CYS A 286 ? 0.3024 0.3488 0.3131 0.0246  -0.0140 -0.0044 587 CYS A SG  
2307  N N   . PRO A 287 ? 0.3045 0.3627 0.3163 0.0161  -0.0103 0.0014  588 PRO A N   
2308  C CA  . PRO A 287 ? 0.2722 0.3269 0.2845 0.0111  -0.0117 0.0034  588 PRO A CA  
2309  C C   . PRO A 287 ? 0.2495 0.2969 0.2583 0.0116  -0.0143 0.0009  588 PRO A C   
2310  O O   . PRO A 287 ? 0.3091 0.3555 0.3138 0.0142  -0.0147 -0.0013 588 PRO A O   
2311  C CB  . PRO A 287 ? 0.2994 0.3559 0.3082 0.0093  -0.0090 0.0067  588 PRO A CB  
2312  C CG  . PRO A 287 ? 0.3379 0.3976 0.3431 0.0142  -0.0068 0.0054  588 PRO A CG  
2313  C CD  . PRO A 287 ? 0.2984 0.3618 0.3072 0.0181  -0.0069 0.0029  588 PRO A CD  
2314  N N   . PHE A 288 ? 0.3023 0.3462 0.3131 0.0090  -0.0162 0.0009  589 PHE A N   
2315  C CA  . PHE A 288 ? 0.1733 0.2137 0.1822 0.0094  -0.0183 -0.0012 589 PHE A CA  
2316  C C   . PHE A 288 ? 0.2589 0.2945 0.2657 0.0080  -0.0188 0.0009  589 PHE A C   
2317  O O   . PHE A 288 ? 0.3098 0.3431 0.3172 0.0047  -0.0183 0.0032  589 PHE A O   
2318  C CB  . PHE A 288 ? 0.2326 0.2722 0.2440 0.0086  -0.0196 -0.0040 589 PHE A CB  
2319  C CG  . PHE A 288 ? 0.2686 0.3066 0.2833 0.0064  -0.0199 -0.0028 589 PHE A CG  
2320  C CD1 . PHE A 288 ? 0.2821 0.3170 0.2970 0.0043  -0.0209 -0.0022 589 PHE A CD1 
2321  C CD2 . PHE A 288 ? 0.2217 0.2613 0.2382 0.0077  -0.0193 -0.0026 589 PHE A CD2 
2322  C CE1 . PHE A 288 ? 0.2604 0.2938 0.2773 0.0023  -0.0217 -0.0013 589 PHE A CE1 
2323  C CE2 . PHE A 288 ? 0.2482 0.2877 0.2673 0.0065  -0.0203 -0.0015 589 PHE A CE2 
2324  C CZ  . PHE A 288 ? 0.2207 0.2569 0.2399 0.0033  -0.0216 -0.0009 589 PHE A CZ  
2325  N N   . SER A 289 ? 0.2563 0.2904 0.2595 0.0107  -0.0199 -0.0001 590 SER A N   
2326  C CA  . SER A 289 ? 0.2051 0.2319 0.2027 0.0115  -0.0201 0.0019  590 SER A CA  
2327  C C   . SER A 289 ? 0.1888 0.2181 0.1862 0.0151  -0.0216 -0.0004 590 SER A C   
2328  O O   . SER A 289 ? 0.2365 0.2743 0.2370 0.0167  -0.0226 -0.0030 590 SER A O   
2329  C CB  . SER A 289 ? 0.2930 0.3142 0.2822 0.0134  -0.0188 0.0048  590 SER A CB  
2330  O OG  . SER A 289 ? 0.3161 0.3419 0.3027 0.0186  -0.0196 0.0035  590 SER A OG  
2331  N N   . GLY A 290 ? 0.2576 0.2801 0.2511 0.0160  -0.0217 0.0004  591 GLY A N   
2332  C CA  . GLY A 290 ? 0.2801 0.3066 0.2726 0.0211  -0.0226 -0.0014 591 GLY A CA  
2333  C C   . GLY A 290 ? 0.3267 0.3411 0.3080 0.0262  -0.0223 0.0007  591 GLY A C   
2334  O O   . GLY A 290 ? 0.3057 0.3127 0.2785 0.0292  -0.0220 0.0029  591 GLY A O   
2335  N N   . TRP A 291 ? 0.3071 0.3170 0.2861 0.0272  -0.0221 0.0000  592 TRP A N   
2336  C CA  . TRP A 291 ? 0.3289 0.3226 0.2943 0.0317  -0.0217 0.0018  592 TRP A CA  
2337  C C   . TRP A 291 ? 0.2789 0.2643 0.2426 0.0275  -0.0213 0.0013  592 TRP A C   
2338  O O   . TRP A 291 ? 0.2733 0.2680 0.2464 0.0237  -0.0215 -0.0005 592 TRP A O   
2339  C CB  . TRP A 291 ? 0.2610 0.2587 0.2210 0.0432  -0.0220 0.0010  592 TRP A CB  
2340  C CG  . TRP A 291 ? 0.3148 0.3305 0.2849 0.0453  -0.0221 -0.0022 592 TRP A CG  
2341  C CD1 . TRP A 291 ? 0.3941 0.4093 0.3643 0.0456  -0.0210 -0.0036 592 TRP A CD1 
2342  C CD2 . TRP A 291 ? 0.2766 0.3139 0.2574 0.0463  -0.0231 -0.0045 592 TRP A CD2 
2343  N NE1 . TRP A 291 ? 0.3338 0.3699 0.3146 0.0466  -0.0208 -0.0062 592 TRP A NE1 
2344  C CE2 . TRP A 291 ? 0.3016 0.3516 0.2893 0.0464  -0.0223 -0.0069 592 TRP A CE2 
2345  C CE3 . TRP A 291 ? 0.3210 0.3681 0.3055 0.0465  -0.0247 -0.0048 592 TRP A CE3 
2346  C CZ2 . TRP A 291 ? 0.3707 0.4434 0.3692 0.0452  -0.0229 -0.0097 592 TRP A CZ2 
2347  C CZ3 . TRP A 291 ? 0.3609 0.4294 0.3554 0.0459  -0.0258 -0.0079 592 TRP A CZ3 
2348  C CH2 . TRP A 291 ? 0.4210 0.5025 0.4226 0.0447  -0.0250 -0.0102 592 TRP A CH2 
2349  N N   . TYR A 292 ? 0.3115 0.2776 0.2613 0.0278  -0.0210 0.0029  593 TYR A N   
2350  C CA  . TYR A 292 ? 0.3192 0.2749 0.2652 0.0219  -0.0212 0.0026  593 TYR A CA  
2351  C C   . TYR A 292 ? 0.3663 0.3233 0.3105 0.0278  -0.0208 0.0002  593 TYR A C   
2352  O O   . TYR A 292 ? 0.3629 0.3212 0.3020 0.0380  -0.0199 -0.0005 593 TYR A O   
2353  C CB  . TYR A 292 ? 0.2767 0.2087 0.2055 0.0191  -0.0211 0.0048  593 TYR A CB  
2354  C CG  . TYR A 292 ? 0.2755 0.2061 0.2072 0.0076  -0.0214 0.0068  593 TYR A CG  
2355  C CD1 . TYR A 292 ? 0.3806 0.3025 0.3044 0.0053  -0.0203 0.0097  593 TYR A CD1 
2356  C CD2 . TYR A 292 ? 0.2658 0.2050 0.2077 -0.0007 -0.0227 0.0060  593 TYR A CD2 
2357  C CE1 . TYR A 292 ? 0.3200 0.2438 0.2474 -0.0059 -0.0201 0.0117  593 TYR A CE1 
2358  C CE2 . TYR A 292 ? 0.3325 0.2745 0.2783 -0.0106 -0.0230 0.0078  593 TYR A CE2 
2359  C CZ  . TYR A 292 ? 0.2934 0.2288 0.2326 -0.0136 -0.0215 0.0106  593 TYR A CZ  
2360  O OH  . TYR A 292 ? 0.3689 0.3110 0.3136 -0.0241 -0.0214 0.0123  593 TYR A OH  
2361  N N   . MET A 293 ? 0.3395 0.2970 0.2875 0.0218  -0.0212 -0.0009 594 MET A N   
2362  C CA  . MET A 293 ? 0.2906 0.2404 0.2304 0.0255  -0.0205 -0.0026 594 MET A CA  
2363  C C   . MET A 293 ? 0.3174 0.2425 0.2401 0.0221  -0.0214 -0.0017 594 MET A C   
2364  O O   . MET A 293 ? 0.3613 0.2818 0.2849 0.0122  -0.0229 -0.0003 594 MET A O   
2365  C CB  . MET A 293 ? 0.2850 0.2459 0.2350 0.0206  -0.0207 -0.0041 594 MET A CB  
2366  C CG  . MET A 293 ? 0.3078 0.2632 0.2498 0.0248  -0.0193 -0.0059 594 MET A CG  
2367  S SD  . MET A 293 ? 0.3505 0.3206 0.3043 0.0197  -0.0187 -0.0072 594 MET A SD  
2368  C CE  . MET A 293 ? 0.3135 0.2745 0.2670 0.0091  -0.0222 -0.0059 594 MET A CE  
2369  N N   . GLY A 294 ? 0.3857 0.2952 0.2922 0.0303  -0.0203 -0.0025 595 GLY A N   
2370  C CA  . GLY A 294 ? 0.3843 0.2655 0.2701 0.0275  -0.0209 -0.0017 595 GLY A CA  
2371  C C   . GLY A 294 ? 0.3919 0.2660 0.2767 0.0144  -0.0231 -0.0021 595 GLY A C   
2372  O O   . GLY A 294 ? 0.4099 0.2680 0.2846 0.0057  -0.0244 -0.0007 595 GLY A O   
2373  N N   . THR A 295 ? 0.3869 0.2733 0.2814 0.0125  -0.0237 -0.0039 596 THR A N   
2374  C CA  . THR A 295 ? 0.4001 0.2811 0.2929 0.0015  -0.0265 -0.0045 596 THR A CA  
2375  C C   . THR A 295 ? 0.3793 0.2703 0.2836 -0.0097 -0.0286 -0.0025 596 THR A C   
2376  O O   . THR A 295 ? 0.3508 0.2350 0.2506 -0.0199 -0.0313 -0.0025 596 THR A O   
2377  C CB  . THR A 295 ? 0.3826 0.2756 0.2832 0.0026  -0.0266 -0.0064 596 THR A CB  
2378  O OG1 . THR A 295 ? 0.3079 0.2246 0.2278 0.0043  -0.0256 -0.0057 596 THR A OG1 
2379  C CG2 . THR A 295 ? 0.3989 0.2814 0.2860 0.0126  -0.0242 -0.0086 596 THR A CG2 
2380  N N   . GLU A 296 ? 0.3509 0.2596 0.2703 -0.0079 -0.0276 -0.0010 597 GLU A N   
2381  C CA  . GLU A 296 ? 0.4210 0.3403 0.3509 -0.0168 -0.0289 0.0010  597 GLU A CA  
2382  C C   . GLU A 296 ? 0.4187 0.3215 0.3357 -0.0248 -0.0294 0.0026  597 GLU A C   
2383  O O   . GLU A 296 ? 0.4133 0.3204 0.3338 -0.0358 -0.0314 0.0034  597 GLU A O   
2384  C CB  . GLU A 296 ? 0.4819 0.4178 0.4251 -0.0122 -0.0272 0.0021  597 GLU A CB  
2385  C CG  . GLU A 296 ? 0.3919 0.3436 0.3472 -0.0065 -0.0265 0.0005  597 GLU A CG  
2386  C CD  . GLU A 296 ? 0.3335 0.2989 0.2993 -0.0035 -0.0252 0.0012  597 GLU A CD  
2387  O OE1 . GLU A 296 ? 0.2420 0.2165 0.2164 -0.0082 -0.0258 0.0024  597 GLU A OE1 
2388  O OE2 . GLU A 296 ? 0.2769 0.2445 0.2418 0.0039  -0.0237 0.0005  597 GLU A OE2 
2389  N N   . ILE A 297 ? 0.3259 0.2098 0.2271 -0.0194 -0.0274 0.0032  598 ILE A N   
2390  C CA  . ILE A 297 ? 0.3623 0.2245 0.2463 -0.0270 -0.0273 0.0049  598 ILE A CA  
2391  C C   . ILE A 297 ? 0.4166 0.2556 0.2818 -0.0319 -0.0291 0.0029  598 ILE A C   
2392  O O   . ILE A 297 ? 0.4117 0.2438 0.2714 -0.0456 -0.0312 0.0032  598 ILE A O   
2393  C CB  . ILE A 297 ? 0.3575 0.2061 0.2293 -0.0178 -0.0245 0.0067  598 ILE A CB  
2394  C CG1 . ILE A 297 ? 0.3666 0.2386 0.2562 -0.0124 -0.0231 0.0081  598 ILE A CG1 
2395  C CG2 . ILE A 297 ? 0.3875 0.2109 0.2393 -0.0270 -0.0240 0.0090  598 ILE A CG2 
2396  C CD1 . ILE A 297 ? 0.3280 0.1904 0.2068 -0.0005 -0.0211 0.0095  598 ILE A CD1 
2397  N N   . GLY A 298 ? 0.3970 0.2234 0.2507 -0.0207 -0.0282 0.0007  599 GLY A N   
2398  C CA  . GLY A 298 ? 0.4653 0.2643 0.2961 -0.0232 -0.0294 -0.0014 599 GLY A CA  
2399  C C   . GLY A 298 ? 0.4129 0.2185 0.2488 -0.0333 -0.0330 -0.0036 599 GLY A C   
2400  O O   . GLY A 298 ? 0.5098 0.2943 0.3281 -0.0425 -0.0352 -0.0050 599 GLY A O   
2401  N N   . VAL A 299 ? 0.4539 0.2873 0.3120 -0.0320 -0.0339 -0.0040 600 VAL A N   
2402  C CA  . VAL A 299 ? 0.4353 0.2756 0.2975 -0.0399 -0.0377 -0.0058 600 VAL A CA  
2403  C C   . VAL A 299 ? 0.4803 0.3399 0.3579 -0.0526 -0.0405 -0.0040 600 VAL A C   
2404  O O   . VAL A 299 ? 0.4811 0.3353 0.3523 -0.0650 -0.0441 -0.0047 600 VAL A O   
2405  C CB  . VAL A 299 ? 0.4459 0.3018 0.3192 -0.0307 -0.0370 -0.0072 600 VAL A CB  
2406  C CG1 . VAL A 299 ? 0.4489 0.3082 0.3224 -0.0379 -0.0411 -0.0088 600 VAL A CG1 
2407  C CG2 . VAL A 299 ? 0.4829 0.3251 0.3431 -0.0174 -0.0334 -0.0089 600 VAL A CG2 
2408  N N   . ARG A 300 ? 0.4461 0.3293 0.3440 -0.0495 -0.0392 -0.0019 601 ARG A N   
2409  C CA  . ARG A 300 ? 0.3689 0.2741 0.2828 -0.0587 -0.0416 -0.0004 601 ARG A CA  
2410  C C   . ARG A 300 ? 0.3968 0.2983 0.3071 -0.0692 -0.0410 0.0018  601 ARG A C   
2411  O O   . ARG A 300 ? 0.4991 0.4038 0.4085 -0.0823 -0.0440 0.0018  601 ARG A O   
2412  C CB  . ARG A 300 ? 0.2762 0.2057 0.2106 -0.0509 -0.0402 0.0006  601 ARG A CB  
2413  C CG  . ARG A 300 ? 0.3339 0.2668 0.2713 -0.0418 -0.0401 -0.0011 601 ARG A CG  
2414  C CD  . ARG A 300 ? 0.3360 0.2691 0.2702 -0.0467 -0.0443 -0.0027 601 ARG A CD  
2415  N NE  . ARG A 300 ? 0.3823 0.3325 0.3271 -0.0551 -0.0478 -0.0015 601 ARG A NE  
2416  C CZ  . ARG A 300 ? 0.3588 0.3303 0.3197 -0.0520 -0.0483 -0.0002 601 ARG A CZ  
2417  N NH1 . ARG A 300 ? 0.2630 0.2387 0.2299 -0.0423 -0.0456 -0.0001 601 ARG A NH1 
2418  N NH2 . ARG A 300 ? 0.3667 0.3553 0.3366 -0.0585 -0.0514 0.0009  601 ARG A NH2 
2419  N N   . ASP A 301 ? 0.4243 0.3204 0.3325 -0.0642 -0.0371 0.0037  602 ASP A N   
2420  C CA  . ASP A 301 ? 0.4397 0.3333 0.3447 -0.0740 -0.0356 0.0064  602 ASP A CA  
2421  C C   . ASP A 301 ? 0.4490 0.3159 0.3315 -0.0858 -0.0369 0.0059  602 ASP A C   
2422  O O   . ASP A 301 ? 0.4500 0.3214 0.3327 -0.1009 -0.0382 0.0070  602 ASP A O   
2423  C CB  . ASP A 301 ? 0.4107 0.2997 0.3139 -0.0648 -0.0313 0.0086  602 ASP A CB  
2424  C CG  . ASP A 301 ? 0.4350 0.3505 0.3597 -0.0560 -0.0301 0.0090  602 ASP A CG  
2425  O OD1 . ASP A 301 ? 0.4268 0.3653 0.3681 -0.0601 -0.0316 0.0092  602 ASP A OD1 
2426  O OD2 . ASP A 301 ? 0.4558 0.3688 0.3798 -0.0447 -0.0278 0.0092  602 ASP A OD2 
2427  N N   . TYR A 302 ? 0.3888 0.2277 0.2508 -0.0792 -0.0366 0.0040  603 TYR A N   
2428  C CA  . TYR A 302 ? 0.4477 0.2546 0.2833 -0.0893 -0.0375 0.0032  603 TYR A CA  
2429  C C   . TYR A 302 ? 0.5375 0.3432 0.3693 -0.0995 -0.0424 0.0000  603 TYR A C   
2430  O O   . TYR A 302 ? 0.5241 0.3151 0.3416 -0.1154 -0.0444 -0.0004 603 TYR A O   
2431  C CB  . TYR A 302 ? 0.5477 0.3231 0.3602 -0.0759 -0.0348 0.0024  603 TYR A CB  
2432  C CG  . TYR A 302 ? 0.5849 0.3500 0.3902 -0.0712 -0.0307 0.0059  603 TYR A CG  
2433  C CD1 . TYR A 302 ? 0.5831 0.3266 0.3715 -0.0554 -0.0281 0.0059  603 TYR A CD1 
2434  C CD2 . TYR A 302 ? 0.6127 0.3906 0.4274 -0.0819 -0.0294 0.0093  603 TYR A CD2 
2435  C CE1 . TYR A 302 ? 0.5359 0.2693 0.3161 -0.0502 -0.0248 0.0094  603 TYR A CE1 
2436  C CE2 . TYR A 302 ? 0.6196 0.3869 0.4260 -0.0776 -0.0256 0.0128  603 TYR A CE2 
2437  C CZ  . TYR A 302 ? 0.6022 0.3466 0.3908 -0.0617 -0.0236 0.0128  603 TYR A CZ  
2438  O OH  . TYR A 302 ? 0.5780 0.3116 0.3570 -0.0565 -0.0203 0.0164  603 TYR A OH  
2439  N N   . CYS A 303 ? 0.4700 0.2907 0.3131 -0.0920 -0.0446 -0.0023 604 CYS A N   
2440  C CA  . CYS A 303 ? 0.5297 0.3428 0.3633 -0.0995 -0.0493 -0.0056 604 CYS A CA  
2441  C C   . CYS A 303 ? 0.5235 0.3685 0.3781 -0.1061 -0.0540 -0.0061 604 CYS A C   
2442  O O   . CYS A 303 ? 0.5204 0.3602 0.3664 -0.1146 -0.0587 -0.0088 604 CYS A O   
2443  C CB  . CYS A 303 ? 0.5461 0.3406 0.3658 -0.0857 -0.0485 -0.0086 604 CYS A CB  
2444  S SG  . CYS A 303 ? 0.5945 0.3461 0.3823 -0.0781 -0.0442 -0.0089 604 CYS A SG  
2445  N N   . ASP A 304 ? 0.4006 0.2771 0.2804 -0.1021 -0.0531 -0.0037 605 ASP A N   
2446  C CA  . ASP A 304 ? 0.4238 0.3298 0.3212 -0.1090 -0.0578 -0.0037 605 ASP A CA  
2447  C C   . ASP A 304 ? 0.5373 0.4431 0.4286 -0.1286 -0.0612 -0.0039 605 ASP A C   
2448  O O   . ASP A 304 ? 0.5406 0.4342 0.4233 -0.1370 -0.0584 -0.0022 605 ASP A O   
2449  C CB  . ASP A 304 ? 0.3951 0.3322 0.3176 -0.1026 -0.0558 -0.0009 605 ASP A CB  
2450  C CG  . ASP A 304 ? 0.4817 0.4260 0.4134 -0.0864 -0.0543 -0.0012 605 ASP A CG  
2451  O OD1 . ASP A 304 ? 0.4836 0.4103 0.4036 -0.0793 -0.0538 -0.0033 605 ASP A OD1 
2452  O OD2 . ASP A 304 ? 0.4769 0.4445 0.4268 -0.0811 -0.0533 0.0006  605 ASP A OD2 
2453  N N   . ASN A 305 ? 0.4460 0.3656 0.3410 -0.1364 -0.0673 -0.0058 606 ASN A N   
2454  C CA  . ASN A 305 ? 0.4454 0.3705 0.3369 -0.1567 -0.0713 -0.0063 606 ASN A CA  
2455  C C   . ASN A 305 ? 0.4696 0.4235 0.3804 -0.1635 -0.0692 -0.0028 606 ASN A C   
2456  O O   . ASN A 305 ? 0.4647 0.4157 0.3691 -0.1806 -0.0690 -0.0021 606 ASN A O   
2457  C CB  . ASN A 305 ? 0.4647 0.4053 0.3597 -0.1617 -0.0790 -0.0091 606 ASN A CB  
2458  C CG  . ASN A 305 ? 0.6135 0.5239 0.4861 -0.1577 -0.0812 -0.0129 606 ASN A CG  
2459  O OD1 . ASN A 305 ? 0.7561 0.6317 0.6040 -0.1636 -0.0799 -0.0147 606 ASN A OD1 
2460  N ND2 . ASN A 305 ? 0.6140 0.5355 0.4933 -0.1467 -0.0840 -0.0140 606 ASN A ND2 
2461  N N   . SER A 306 ? 0.5522 0.5335 0.4853 -0.1509 -0.0673 -0.0006 607 SER A N   
2462  C CA  . SER A 306 ? 0.5192 0.5293 0.4707 -0.1553 -0.0648 0.0026  607 SER A CA  
2463  C C   . SER A 306 ? 0.4773 0.4747 0.4264 -0.1491 -0.0574 0.0054  607 SER A C   
2464  O O   . SER A 306 ? 0.4943 0.5153 0.4592 -0.1480 -0.0542 0.0081  607 SER A O   
2465  C CB  . SER A 306 ? 0.4083 0.4554 0.3838 -0.1449 -0.0670 0.0033  607 SER A CB  
2466  O OG  . SER A 306 ? 0.5096 0.5487 0.4870 -0.1262 -0.0645 0.0033  607 SER A OG  
2467  N N   . ARG A 307 ? 0.4262 0.3879 0.3553 -0.1439 -0.0546 0.0046  608 ARG A N   
2468  C CA  . ARG A 307 ? 0.4442 0.3923 0.3682 -0.1387 -0.0483 0.0073  608 ARG A CA  
2469  C C   . ARG A 307 ? 0.4660 0.3802 0.3641 -0.1513 -0.0468 0.0075  608 ARG A C   
2470  O O   . ARG A 307 ? 0.4313 0.3473 0.3244 -0.1697 -0.0491 0.0074  608 ARG A O   
2471  C CB  . ARG A 307 ? 0.4137 0.3522 0.3378 -0.1189 -0.0458 0.0067  608 ARG A CB  
2472  C CG  . ARG A 307 ? 0.4377 0.4055 0.3845 -0.1072 -0.0468 0.0066  608 ARG A CG  
2473  C CD  . ARG A 307 ? 0.5055 0.5005 0.4707 -0.1067 -0.0440 0.0095  608 ARG A CD  
2474  N NE  . ARG A 307 ? 0.4331 0.4158 0.3923 -0.1036 -0.0385 0.0117  608 ARG A NE  
2475  C CZ  . ARG A 307 ? 0.4330 0.4055 0.3900 -0.0898 -0.0358 0.0116  608 ARG A CZ  
2476  N NH1 . ARG A 307 ? 0.3834 0.3564 0.3440 -0.0789 -0.0374 0.0094  608 ARG A NH1 
2477  N NH2 . ARG A 307 ? 0.4144 0.3766 0.3650 -0.0875 -0.0315 0.0137  608 ARG A NH2 
2478  N N   . TYR A 308 ? 0.4205 0.3036 0.3007 -0.1419 -0.0431 0.0079  609 TYR A N   
2479  C CA  . TYR A 308 ? 0.4593 0.3066 0.3116 -0.1530 -0.0415 0.0085  609 TYR A CA  
2480  C C   . TYR A 308 ? 0.5649 0.3877 0.3965 -0.1617 -0.0461 0.0047  609 TYR A C   
2481  O O   . TYR A 308 ? 0.5543 0.3504 0.3631 -0.1766 -0.0459 0.0048  609 TYR A O   
2482  C CB  . TYR A 308 ? 0.4846 0.3053 0.3218 -0.1390 -0.0366 0.0102  609 TYR A CB  
2483  C CG  . TYR A 308 ? 0.5915 0.4256 0.4384 -0.1392 -0.0319 0.0145  609 TYR A CG  
2484  C CD1 . TYR A 308 ? 0.4453 0.3111 0.3177 -0.1277 -0.0305 0.0155  609 TYR A CD1 
2485  C CD2 . TYR A 308 ? 0.6322 0.4457 0.4608 -0.1517 -0.0287 0.0175  609 TYR A CD2 
2486  C CE1 . TYR A 308 ? 0.4577 0.3352 0.3376 -0.1276 -0.0262 0.0192  609 TYR A CE1 
2487  C CE2 . TYR A 308 ? 0.6306 0.4564 0.4672 -0.1518 -0.0240 0.0216  609 TYR A CE2 
2488  C CZ  . TYR A 308 ? 0.4109 0.2692 0.2732 -0.1394 -0.0229 0.0223  609 TYR A CZ  
2489  O OH  . TYR A 308 ? 0.5082 0.3780 0.3770 -0.1392 -0.0182 0.0261  609 TYR A OH  
2490  N N   . ASN A 309 ? 0.5316 0.3614 0.3689 -0.1534 -0.0500 0.0014  610 ASN A N   
2491  C CA  . ASN A 309 ? 0.5036 0.3184 0.3254 -0.1631 -0.0553 -0.0026 610 ASN A CA  
2492  C C   . ASN A 309 ? 0.5418 0.3074 0.3271 -0.1672 -0.0540 -0.0041 610 ASN A C   
2493  O O   . ASN A 309 ? 0.5804 0.3289 0.3480 -0.1856 -0.0569 -0.0057 610 ASN A O   
2494  C CB  . ASN A 309 ? 0.5577 0.3994 0.3919 -0.1834 -0.0599 -0.0027 610 ASN A CB  
2495  C CG  . ASN A 309 ? 0.6136 0.4470 0.4357 -0.1934 -0.0668 -0.0072 610 ASN A CG  
2496  O OD1 . ASN A 309 ? 0.5623 0.3824 0.3761 -0.1820 -0.0685 -0.0102 610 ASN A OD1 
2497  N ND2 . ASN A 309 ? 0.5979 0.4402 0.4187 -0.2156 -0.0705 -0.0078 610 ASN A ND2 
2498  N N   . ILE A 310 ? 0.5203 0.2620 0.2926 -0.1495 -0.0497 -0.0037 611 ILE A N   
2499  C CA  . ILE A 310 ? 0.6003 0.2938 0.3362 -0.1514 -0.0476 -0.0042 611 ILE A CA  
2500  C C   . ILE A 310 ? 0.6849 0.3486 0.3968 -0.1455 -0.0500 -0.0090 611 ILE A C   
2501  O O   . ILE A 310 ? 0.7466 0.3668 0.4253 -0.1441 -0.0481 -0.0098 611 ILE A O   
2502  C CB  . ILE A 310 ? 0.6904 0.3699 0.4199 -0.1358 -0.0415 -0.0008 611 ILE A CB  
2503  C CG1 . ILE A 310 ? 0.6216 0.3061 0.3577 -0.1114 -0.0400 -0.0022 611 ILE A CG1 
2504  C CG2 . ILE A 310 ? 0.6318 0.3398 0.3837 -0.1405 -0.0389 0.0038  611 ILE A CG2 
2505  C CD1 . ILE A 310 ? 0.6398 0.3056 0.3636 -0.0950 -0.0350 0.0003  611 ILE A CD1 
2506  N N   . LEU A 311 ? 0.6414 0.3254 0.3670 -0.1418 -0.0539 -0.0120 612 LEU A N   
2507  C CA  . LEU A 311 ? 0.6424 0.2990 0.3450 -0.1346 -0.0555 -0.0165 612 LEU A CA  
2508  C C   . LEU A 311 ? 0.6666 0.2835 0.3348 -0.1516 -0.0582 -0.0193 612 LEU A C   
2509  O O   . LEU A 311 ? 0.7492 0.3263 0.3863 -0.1432 -0.0561 -0.0213 612 LEU A O   
2510  C CB  . LEU A 311 ? 0.5955 0.2811 0.3176 -0.1312 -0.0597 -0.0190 612 LEU A CB  
2511  C CG  . LEU A 311 ? 0.5836 0.2974 0.3307 -0.1116 -0.0568 -0.0175 612 LEU A CG  
2512  C CD1 . LEU A 311 ? 0.5835 0.3236 0.3472 -0.1118 -0.0613 -0.0194 612 LEU A CD1 
2513  C CD2 . LEU A 311 ? 0.6328 0.3220 0.3628 -0.0923 -0.0519 -0.0185 612 LEU A CD2 
2514  N N   . GLU A 312 ? 0.8140 0.4463 0.4892 -0.1735 -0.0620 -0.0189 613 GLU A N   
2515  C CA  . GLU A 312 ? 0.9036 0.5145 0.5553 -0.1865 -0.0625 -0.0191 613 GLU A CA  
2516  C C   . GLU A 312 ? 0.9474 0.5179 0.5693 -0.1818 -0.0567 -0.0167 613 GLU A C   
2517  O O   . GLU A 312 ? 0.9078 0.4431 0.4993 -0.1762 -0.0557 -0.0185 613 GLU A O   
2518  C CB  . GLU A 312 ? 1.1173 0.7606 0.7880 -0.2083 -0.0653 -0.0172 613 GLU A CB  
2519  C CG  . GLU A 312 ? 1.3197 0.9534 0.9738 -0.2239 -0.0684 -0.0188 613 GLU A CG  
2520  C CD  . GLU A 312 ? 1.4542 1.1161 1.1246 -0.2280 -0.0752 -0.0221 613 GLU A CD  
2521  O OE1 . GLU A 312 ? 1.4986 1.1516 1.1639 -0.2148 -0.0770 -0.0253 613 GLU A OE1 
2522  O OE2 . GLU A 312 ? 1.4958 1.1899 1.1843 -0.2435 -0.0785 -0.0213 613 GLU A OE2 
2523  N N   . GLU A 313 ? 0.8327 0.4082 0.4621 -0.1835 -0.0528 -0.0125 614 GLU A N   
2524  C CA  . GLU A 313 ? 0.9433 0.4826 0.5449 -0.1786 -0.0473 -0.0098 614 GLU A CA  
2525  C C   . GLU A 313 ? 0.9165 0.4236 0.4958 -0.1547 -0.0447 -0.0115 614 GLU A C   
2526  O O   . GLU A 313 ? 0.9485 0.4188 0.4948 -0.1503 -0.0425 -0.0117 614 GLU A O   
2527  C CB  . GLU A 313 ? 1.1104 0.6643 0.7275 -0.1802 -0.0436 -0.0049 614 GLU A CB  
2528  C CG  . GLU A 313 ? 1.3615 0.9270 0.9819 -0.2023 -0.0428 -0.0019 614 GLU A CG  
2529  C CD  . GLU A 313 ? 1.5621 1.0875 1.1473 -0.2046 -0.0385 0.0002  614 GLU A CD  
2530  O OE1 . GLU A 313 ? 1.6162 1.1254 1.1812 -0.2181 -0.0400 -0.0013 614 GLU A OE1 
2531  O OE2 . GLU A 313 ? 1.5957 1.1052 1.1723 -0.1927 -0.0339 0.0032  614 GLU A OE2 
2532  N N   . VAL A 314 ? 0.8999 0.4218 0.4966 -0.1386 -0.0448 -0.0129 615 VAL A N   
2533  C CA  . VAL A 314 ? 0.8114 0.3089 0.3906 -0.1140 -0.0416 -0.0141 615 VAL A CA  
2534  C C   . VAL A 314 ? 0.7876 0.2647 0.3449 -0.1094 -0.0432 -0.0184 615 VAL A C   
2535  O O   . VAL A 314 ? 0.7851 0.2295 0.3130 -0.0964 -0.0401 -0.0186 615 VAL A O   
2536  C CB  . VAL A 314 ? 0.7423 0.2707 0.3509 -0.0978 -0.0406 -0.0139 615 VAL A CB  
2537  C CG1 . VAL A 314 ? 0.7163 0.2282 0.3108 -0.0717 -0.0373 -0.0157 615 VAL A CG1 
2538  C CG2 . VAL A 314 ? 0.6982 0.2504 0.3285 -0.0986 -0.0377 -0.0085 615 VAL A CG2 
2539  N N   . ALA A 315 ? 0.7919 0.2887 0.3626 -0.1192 -0.0482 -0.0216 616 ALA A N   
2540  C CA  . ALA A 315 ? 0.8316 0.3106 0.3824 -0.1153 -0.0499 -0.0255 616 ALA A CA  
2541  C C   . ALA A 315 ? 0.8434 0.2884 0.3610 -0.1248 -0.0494 -0.0247 616 ALA A C   
2542  O O   . ALA A 315 ? 0.9324 0.3474 0.4220 -0.1133 -0.0478 -0.0264 616 ALA A O   
2543  C CB  . ALA A 315 ? 0.7784 0.2868 0.3502 -0.1261 -0.0559 -0.0285 616 ALA A CB  
2544  N N   . LYS A 316 ? 0.9520 0.4014 0.4714 -0.1456 -0.0504 -0.0221 617 LYS A N   
2545  C CA  . LYS A 316 ? 1.0339 0.4497 0.5202 -0.1561 -0.0496 -0.0213 617 LYS A CA  
2546  C C   . LYS A 316 ? 1.0986 0.4759 0.5539 -0.1377 -0.0441 -0.0198 617 LYS A C   
2547  O O   . LYS A 316 ? 1.0904 0.4341 0.5134 -0.1312 -0.0434 -0.0213 617 LYS A O   
2548  C CB  . LYS A 316 ? 1.0744 0.5044 0.5701 -0.1796 -0.0503 -0.0183 617 LYS A CB  
2549  C CG  . LYS A 316 ? 1.1513 0.6130 0.6678 -0.2009 -0.0560 -0.0197 617 LYS A CG  
2550  C CD  . LYS A 316 ? 1.3183 0.7926 0.8415 -0.2219 -0.0552 -0.0163 617 LYS A CD  
2551  C CE  . LYS A 316 ? 1.4000 0.8976 0.9336 -0.2445 -0.0604 -0.0177 617 LYS A CE  
2552  N NZ  . LYS A 316 ? 1.3263 0.8694 0.8971 -0.2442 -0.0651 -0.0194 617 LYS A NZ  
2553  N N   . LYS A 317 ? 1.0826 0.4651 0.5470 -0.1285 -0.0403 -0.0166 618 LYS A N   
2554  C CA  . LYS A 317 ? 1.0522 0.4026 0.4895 -0.1090 -0.0353 -0.0148 618 LYS A CA  
2555  C C   . LYS A 317 ? 1.0406 0.3794 0.4669 -0.0845 -0.0341 -0.0177 618 LYS A C   
2556  O O   . LYS A 317 ? 1.0159 0.3226 0.4111 -0.0693 -0.0309 -0.0173 618 LYS A O   
2557  C CB  . LYS A 317 ? 1.0443 0.4095 0.4993 -0.1021 -0.0321 -0.0110 618 LYS A CB  
2558  C CG  . LYS A 317 ? 1.0951 0.4742 0.5623 -0.1249 -0.0323 -0.0077 618 LYS A CG  
2559  C CD  . LYS A 317 ? 1.2467 0.5923 0.6824 -0.1272 -0.0286 -0.0048 618 LYS A CD  
2560  C CE  . LYS A 317 ? 1.3687 0.7201 0.8057 -0.1557 -0.0296 -0.0031 618 LYS A CE  
2561  N NZ  . LYS A 317 ? 1.4122 0.7657 0.8523 -0.1587 -0.0257 0.0015  618 LYS A NZ  
2562  N N   . MET A 318 ? 0.9430 0.3085 0.3937 -0.0798 -0.0364 -0.0206 619 MET A N   
2563  C CA  . MET A 318 ? 0.9676 0.3256 0.4093 -0.0577 -0.0350 -0.0235 619 MET A CA  
2564  C C   . MET A 318 ? 0.9951 0.3315 0.4126 -0.0630 -0.0373 -0.0265 619 MET A C   
2565  O O   . MET A 318 ? 0.9872 0.3143 0.3933 -0.0449 -0.0356 -0.0287 619 MET A O   
2566  C CB  . MET A 318 ? 0.8268 0.2210 0.3027 -0.0497 -0.0360 -0.0256 619 MET A CB  
2567  C CG  . MET A 318 ? 0.8000 0.2100 0.2937 -0.0351 -0.0326 -0.0232 619 MET A CG  
2568  S SD  . MET A 318 ? 0.8448 0.2960 0.3768 -0.0289 -0.0340 -0.0261 619 MET A SD  
2569  C CE  . MET A 318 ? 0.8478 0.2903 0.3648 -0.0095 -0.0323 -0.0306 619 MET A CE  
2570  N N   . ASN A 319 ? 0.9839 0.3137 0.3940 -0.0871 -0.0408 -0.0264 620 ASN A N   
2571  C CA  . ASN A 319 ? 1.1009 0.4086 0.4866 -0.0944 -0.0434 -0.0291 620 ASN A CA  
2572  C C   . ASN A 319 ? 1.0603 0.3872 0.4611 -0.0885 -0.0461 -0.0330 620 ASN A C   
2573  O O   . ASN A 319 ? 1.0077 0.3140 0.3865 -0.0791 -0.0458 -0.0354 620 ASN A O   
2574  C CB  . ASN A 319 ? 1.2820 0.5447 0.6249 -0.0805 -0.0396 -0.0284 620 ASN A CB  
2575  C CG  . ASN A 319 ? 1.4211 0.6597 0.7426 -0.0920 -0.0380 -0.0251 620 ASN A CG  
2576  O OD1 . ASN A 319 ? 1.4935 0.7353 0.8169 -0.1168 -0.0410 -0.0246 620 ASN A OD1 
2577  N ND2 . ASN A 319 ? 1.5007 0.7175 0.8026 -0.0739 -0.0332 -0.0227 620 ASN A ND2 
2578  N N   . LEU A 320 ? 0.9814 0.3476 0.4188 -0.0940 -0.0487 -0.0337 621 LEU A N   
2579  C CA  . LEU A 320 ? 0.9209 0.3073 0.3734 -0.0909 -0.0517 -0.0375 621 LEU A CA  
2580  C C   . LEU A 320 ? 1.0116 0.4041 0.4647 -0.1137 -0.0580 -0.0393 621 LEU A C   
2581  O O   . LEU A 320 ? 0.9946 0.3889 0.4485 -0.1339 -0.0603 -0.0374 621 LEU A O   
2582  C CB  . LEU A 320 ? 0.8570 0.2819 0.3463 -0.0856 -0.0519 -0.0376 621 LEU A CB  
2583  C CG  . LEU A 320 ? 0.8744 0.2983 0.3672 -0.0648 -0.0461 -0.0357 621 LEU A CG  
2584  C CD1 . LEU A 320 ? 0.8229 0.2838 0.3518 -0.0663 -0.0470 -0.0352 621 LEU A CD1 
2585  C CD2 . LEU A 320 ? 0.9124 0.3230 0.3899 -0.0398 -0.0418 -0.0378 621 LEU A CD2 
2586  N N   . ASP A 321 ? 1.0037 0.4006 0.4563 -0.1098 -0.0606 -0.0429 622 ASP A N   
2587  C CA  . ASP A 321 ? 1.0787 0.4861 0.5347 -0.1292 -0.0671 -0.0450 622 ASP A CA  
2588  C C   . ASP A 321 ? 1.0291 0.4821 0.5242 -0.1398 -0.0714 -0.0447 622 ASP A C   
2589  O O   . ASP A 321 ? 1.0222 0.4982 0.5364 -0.1299 -0.0722 -0.0465 622 ASP A O   
2590  C CB  . ASP A 321 ? 1.1115 0.5076 0.5528 -0.1197 -0.0682 -0.0489 622 ASP A CB  
2591  C CG  . ASP A 321 ? 1.2836 0.6911 0.7281 -0.1387 -0.0754 -0.0513 622 ASP A CG  
2592  O OD1 . ASP A 321 ? 1.2436 0.6584 0.6928 -0.1596 -0.0789 -0.0499 622 ASP A OD1 
2593  O OD2 . ASP A 321 ? 1.3754 0.7860 0.8179 -0.1325 -0.0774 -0.0545 622 ASP A OD2 
2594  N N   . MET A 322 ? 0.9813 0.4486 0.4877 -0.1601 -0.0742 -0.0425 623 MET A N   
2595  C CA  . MET A 322 ? 0.9408 0.4529 0.4842 -0.1697 -0.0780 -0.0415 623 MET A CA  
2596  C C   . MET A 322 ? 0.9859 0.5204 0.5394 -0.1866 -0.0852 -0.0435 623 MET A C   
2597  O O   . MET A 322 ? 1.0247 0.5965 0.6067 -0.1978 -0.0889 -0.0422 623 MET A O   
2598  C CB  . MET A 322 ? 0.8423 0.3628 0.3966 -0.1792 -0.0756 -0.0374 623 MET A CB  
2599  C CG  . MET A 322 ? 0.9733 0.4732 0.5182 -0.1627 -0.0688 -0.0352 623 MET A CG  
2600  S SD  . MET A 322 ? 1.0453 0.5414 0.5894 -0.1761 -0.0657 -0.0303 623 MET A SD  
2601  C CE  . MET A 322 ? 0.8412 0.3928 0.4305 -0.1893 -0.0695 -0.0286 623 MET A CE  
2602  N N   . ARG A 323 ? 0.9846 0.4982 0.5155 -0.1874 -0.0875 -0.0466 624 ARG A N   
2603  C CA  . ARG A 323 ? 0.9782 0.5115 0.5163 -0.2032 -0.0948 -0.0488 624 ARG A CA  
2604  C C   . ARG A 323 ? 0.9360 0.5052 0.5005 -0.1968 -0.0991 -0.0505 624 ARG A C   
2605  O O   . ARG A 323 ? 0.9364 0.5397 0.5223 -0.2093 -0.1051 -0.0506 624 ARG A O   
2606  C CB  . ARG A 323 ? 1.0806 0.5777 0.5841 -0.2059 -0.0959 -0.0516 624 ARG A CB  
2607  C CG  . ARG A 323 ? 1.1202 0.6345 0.6281 -0.2191 -0.1036 -0.0547 624 ARG A CG  
2608  C CD  . ARG A 323 ? 1.1343 0.6084 0.6048 -0.2228 -0.1041 -0.0573 624 ARG A CD  
2609  N NE  . ARG A 323 ? 1.3229 0.8052 0.7925 -0.2226 -0.1098 -0.0614 624 ARG A NE  
2610  C CZ  . ARG A 323 ? 1.4846 0.9568 0.9462 -0.2043 -0.1083 -0.0636 624 ARG A CZ  
2611  N NH1 . ARG A 323 ? 1.5066 0.9619 0.9616 -0.1847 -0.1012 -0.0624 624 ARG A NH1 
2612  N NH2 . ARG A 323 ? 1.5299 1.0098 0.9898 -0.2054 -0.1137 -0.0672 624 ARG A NH2 
2613  N N   . LYS A 324 ? 0.9011 0.4639 0.4636 -0.1769 -0.0961 -0.0518 625 LYS A N   
2614  C CA  . LYS A 324 ? 0.9709 0.5626 0.5530 -0.1695 -0.0998 -0.0534 625 LYS A CA  
2615  C C   . LYS A 324 ? 0.8815 0.4839 0.4789 -0.1533 -0.0952 -0.0520 625 LYS A C   
2616  O O   . LYS A 324 ? 0.8903 0.4694 0.4756 -0.1421 -0.0887 -0.0511 625 LYS A O   
2617  C CB  . LYS A 324 ? 1.0708 0.6439 0.6315 -0.1620 -0.1011 -0.0573 625 LYS A CB  
2618  C CG  . LYS A 324 ? 1.2035 0.7352 0.7344 -0.1465 -0.0940 -0.0583 625 LYS A CG  
2619  C CD  . LYS A 324 ? 1.3119 0.8186 0.8154 -0.1462 -0.0958 -0.0617 625 LYS A CD  
2620  C CE  . LYS A 324 ? 1.3735 0.8382 0.8456 -0.1316 -0.0887 -0.0620 625 LYS A CE  
2621  N NZ  . LYS A 324 ? 1.3548 0.8226 0.8325 -0.1090 -0.0823 -0.0619 625 LYS A NZ  
2622  N N   . THR A 325 ? 0.7371 0.3751 0.3605 -0.1516 -0.0989 -0.0516 626 THR A N   
2623  C CA  . THR A 325 ? 0.8224 0.4717 0.4605 -0.1375 -0.0951 -0.0503 626 THR A CA  
2624  C C   . THR A 325 ? 0.7519 0.3770 0.3712 -0.1179 -0.0893 -0.0527 626 THR A C   
2625  O O   . THR A 325 ? 0.7212 0.3427 0.3434 -0.1052 -0.0837 -0.0519 626 THR A O   
2626  C CB  . THR A 325 ? 0.8249 0.5150 0.4911 -0.1388 -0.1006 -0.0492 626 THR A CB  
2627  O OG1 . THR A 325 ? 0.8812 0.5749 0.5409 -0.1364 -0.1049 -0.0517 626 THR A OG1 
2628  C CG2 . THR A 325 ? 0.8544 0.5731 0.5420 -0.1558 -0.1053 -0.0466 626 THR A CG2 
2629  N N   . SER A 326 ? 0.7624 0.3719 0.3623 -0.1148 -0.0904 -0.0555 627 SER A N   
2630  C CA  . SER A 326 ? 0.7145 0.3080 0.2996 -0.0956 -0.0847 -0.0576 627 SER A CA  
2631  C C   . SER A 326 ? 0.8116 0.3719 0.3751 -0.0843 -0.0770 -0.0577 627 SER A C   
2632  O O   . SER A 326 ? 0.8542 0.4054 0.4086 -0.0662 -0.0710 -0.0590 627 SER A O   
2633  C CB  . SER A 326 ? 0.7695 0.3571 0.3403 -0.0956 -0.0880 -0.0604 627 SER A CB  
2634  O OG  . SER A 326 ? 0.8836 0.4548 0.4391 -0.1094 -0.0918 -0.0614 627 SER A OG  
2635  N N   . SER A 327 ? 0.7545 0.2977 0.3092 -0.0934 -0.0766 -0.0560 628 SER A N   
2636  C CA  . SER A 327 ? 0.7770 0.2918 0.3134 -0.0799 -0.0692 -0.0551 628 SER A CA  
2637  C C   . SER A 327 ? 0.7720 0.3013 0.3261 -0.0680 -0.0646 -0.0535 628 SER A C   
2638  O O   . SER A 327 ? 0.8010 0.3119 0.3426 -0.0528 -0.0581 -0.0529 628 SER A O   
2639  C CB  . SER A 327 ? 0.7716 0.2627 0.2916 -0.0923 -0.0697 -0.0531 628 SER A CB  
2640  O OG  . SER A 327 ? 0.7984 0.3100 0.3398 -0.1066 -0.0722 -0.0503 628 SER A OG  
2641  N N   . LEU A 328 ? 0.6900 0.2525 0.2724 -0.0742 -0.0680 -0.0528 629 LEU A N   
2642  C CA  . LEU A 328 ? 0.7000 0.2893 0.3103 -0.0635 -0.0628 -0.0481 629 LEU A CA  
2643  C C   . LEU A 328 ? 0.7210 0.2930 0.3247 -0.0647 -0.0599 -0.0459 629 LEU A C   
2644  O O   . LEU A 328 ? 0.6953 0.2729 0.3074 -0.0499 -0.0536 -0.0431 629 LEU A O   
2645  C CB  . LEU A 328 ? 0.6711 0.2688 0.2855 -0.0415 -0.0559 -0.0479 629 LEU A CB  
2646  C CG  . LEU A 328 ? 0.7051 0.3172 0.3231 -0.0393 -0.0577 -0.0497 629 LEU A CG  
2647  C CD1 . LEU A 328 ? 0.6406 0.2718 0.2722 -0.0204 -0.0501 -0.0478 629 LEU A CD1 
2648  C CD2 . LEU A 328 ? 0.6259 0.2680 0.2677 -0.0541 -0.0647 -0.0478 629 LEU A CD2 
2649  N N   . TRP A 329 ? 0.6993 0.2523 0.2885 -0.0832 -0.0644 -0.0467 630 TRP A N   
2650  C CA  . TRP A 329 ? 0.7352 0.2732 0.3184 -0.0861 -0.0613 -0.0434 630 TRP A CA  
2651  C C   . TRP A 329 ? 0.7232 0.2947 0.3393 -0.0865 -0.0600 -0.0389 630 TRP A C   
2652  O O   . TRP A 329 ? 0.7222 0.2866 0.3376 -0.0776 -0.0549 -0.0360 630 TRP A O   
2653  C CB  . TRP A 329 ? 0.7714 0.2964 0.3418 -0.1059 -0.0646 -0.0420 630 TRP A CB  
2654  C CG  . TRP A 329 ? 0.7851 0.3413 0.3783 -0.1263 -0.0712 -0.0414 630 TRP A CG  
2655  C CD1 . TRP A 329 ? 0.8662 0.4357 0.4629 -0.1357 -0.0771 -0.0437 630 TRP A CD1 
2656  C CD2 . TRP A 329 ? 0.8102 0.3899 0.4256 -0.1392 -0.0724 -0.0380 630 TRP A CD2 
2657  N NE1 . TRP A 329 ? 0.8279 0.4297 0.4487 -0.1527 -0.0820 -0.0420 630 TRP A NE1 
2658  C CE2 . TRP A 329 ? 0.7869 0.3959 0.4197 -0.1552 -0.0790 -0.0384 630 TRP A CE2 
2659  C CE3 . TRP A 329 ? 0.7609 0.3408 0.3832 -0.1379 -0.0684 -0.0345 630 TRP A CE3 
2660  C CZ2 . TRP A 329 ? 0.7454 0.3855 0.4030 -0.1693 -0.0813 -0.0355 630 TRP A CZ2 
2661  C CZ3 . TRP A 329 ? 0.7303 0.3388 0.3761 -0.1530 -0.0706 -0.0316 630 TRP A CZ3 
2662  C CH2 . TRP A 329 ? 0.7286 0.3679 0.3923 -0.1683 -0.0768 -0.0321 630 TRP A CH2 
2663  N N   . LYS A 330 ? 0.6140 0.2256 0.2611 -0.0944 -0.0638 -0.0374 631 LYS A N   
2664  C CA  . LYS A 330 ? 0.5755 0.2225 0.2559 -0.0921 -0.0616 -0.0324 631 LYS A CA  
2665  C C   . LYS A 330 ? 0.6870 0.3437 0.3777 -0.0699 -0.0550 -0.0306 631 LYS A C   
2666  O O   . LYS A 330 ? 0.5757 0.2386 0.2762 -0.0636 -0.0510 -0.0273 631 LYS A O   
2667  C CB  . LYS A 330 ? 0.5592 0.2455 0.2681 -0.1020 -0.0669 -0.0313 631 LYS A CB  
2668  C CG  . LYS A 330 ? 0.6132 0.3021 0.3210 -0.1250 -0.0731 -0.0317 631 LYS A CG  
2669  C CD  . LYS A 330 ? 0.6607 0.3931 0.3992 -0.1315 -0.0778 -0.0300 631 LYS A CD  
2670  C CE  . LYS A 330 ? 0.7096 0.4503 0.4498 -0.1543 -0.0835 -0.0302 631 LYS A CE  
2671  N NZ  . LYS A 330 ? 0.7402 0.5254 0.5103 -0.1584 -0.0882 -0.0284 631 LYS A NZ  
2672  N N   . ASP A 331 ? 0.5924 0.2511 0.2805 -0.0583 -0.0539 -0.0330 632 ASP A N   
2673  C CA  . ASP A 331 ? 0.5519 0.2241 0.2512 -0.0387 -0.0476 -0.0316 632 ASP A CA  
2674  C C   . ASP A 331 ? 0.6135 0.2588 0.2924 -0.0259 -0.0424 -0.0316 632 ASP A C   
2675  O O   . ASP A 331 ? 0.6001 0.2598 0.2925 -0.0137 -0.0378 -0.0290 632 ASP A O   
2676  C CB  . ASP A 331 ? 0.5760 0.2528 0.2724 -0.0305 -0.0471 -0.0342 632 ASP A CB  
2677  C CG  . ASP A 331 ? 0.5899 0.2855 0.2985 -0.0429 -0.0532 -0.0347 632 ASP A CG  
2678  O OD1 . ASP A 331 ? 0.6062 0.2860 0.2994 -0.0566 -0.0590 -0.0372 632 ASP A OD1 
2679  O OD2 . ASP A 331 ? 0.5575 0.2833 0.2901 -0.0392 -0.0526 -0.0324 632 ASP A OD2 
2680  N N   . GLN A 332 ? 0.6405 0.2457 0.2850 -0.0280 -0.0432 -0.0348 633 GLN A N   
2681  C CA  . GLN A 332 ? 0.6955 0.2702 0.3155 -0.0142 -0.0385 -0.0350 633 GLN A CA  
2682  C C   . GLN A 332 ? 0.6799 0.2536 0.3054 -0.0184 -0.0376 -0.0309 633 GLN A C   
2683  O O   . GLN A 332 ? 0.6306 0.2079 0.2594 -0.0029 -0.0329 -0.0286 633 GLN A O   
2684  C CB  . GLN A 332 ? 0.7524 0.2804 0.3314 -0.0174 -0.0401 -0.0396 633 GLN A CB  
2685  C CG  . GLN A 332 ? 0.9696 0.4704 0.5219 0.0048  -0.0344 -0.0415 633 GLN A CG  
2686  C CD  . GLN A 332 ? 1.0945 0.5655 0.6164 0.0039  -0.0355 -0.0448 633 GLN A CD  
2687  O OE1 . GLN A 332 ? 0.9769 0.4412 0.4934 -0.0153 -0.0408 -0.0452 633 GLN A OE1 
2688  N NE2 . GLN A 332 ? 1.2650 0.7253 0.7713 0.0250  -0.0303 -0.0457 633 GLN A NE2 
2689  N N   . ALA A 333 ? 0.6779 0.2491 0.3049 -0.0394 -0.0420 -0.0298 634 ALA A N   
2690  C CA  . ALA A 333 ? 0.6969 0.2698 0.3304 -0.0447 -0.0407 -0.0255 634 ALA A CA  
2691  C C   . ALA A 333 ? 0.6521 0.2679 0.3223 -0.0367 -0.0385 -0.0218 634 ALA A C   
2692  O O   . ALA A 333 ? 0.6022 0.2187 0.2752 -0.0286 -0.0350 -0.0187 634 ALA A O   
2693  C CB  . ALA A 333 ? 0.6921 0.2613 0.3242 -0.0703 -0.0456 -0.0251 634 ALA A CB  
2694  N N   . LEU A 334 ? 0.6536 0.3035 0.3500 -0.0388 -0.0405 -0.0223 635 LEU A N   
2695  C CA  . LEU A 334 ? 0.5993 0.2880 0.3289 -0.0328 -0.0386 -0.0192 635 LEU A CA  
2696  C C   . LEU A 334 ? 0.6321 0.3223 0.3616 -0.0121 -0.0332 -0.0184 635 LEU A C   
2697  O O   . LEU A 334 ? 0.5523 0.2576 0.2963 -0.0076 -0.0311 -0.0153 635 LEU A O   
2698  C CB  . LEU A 334 ? 0.5273 0.2454 0.2785 -0.0359 -0.0413 -0.0201 635 LEU A CB  
2699  C CG  . LEU A 334 ? 0.5234 0.2782 0.3062 -0.0302 -0.0394 -0.0172 635 LEU A CG  
2700  C CD1 . LEU A 334 ? 0.5622 0.3308 0.3600 -0.0412 -0.0408 -0.0139 635 LEU A CD1 
2701  C CD2 . LEU A 334 ? 0.4922 0.2696 0.2904 -0.0301 -0.0411 -0.0182 635 LEU A CD2 
2702  N N   . VAL A 335 ? 0.5997 0.2745 0.3119 0.0009  -0.0309 -0.0214 636 VAL A N   
2703  C CA  . VAL A 335 ? 0.6037 0.2843 0.3169 0.0212  -0.0258 -0.0209 636 VAL A CA  
2704  C C   . VAL A 335 ? 0.6386 0.2962 0.3346 0.0274  -0.0239 -0.0188 636 VAL A C   
2705  O O   . VAL A 335 ? 0.5863 0.2610 0.2954 0.0375  -0.0214 -0.0162 636 VAL A O   
2706  C CB  . VAL A 335 ? 0.6003 0.2704 0.2976 0.0342  -0.0233 -0.0245 636 VAL A CB  
2707  C CG1 . VAL A 335 ? 0.5519 0.2281 0.2483 0.0556  -0.0180 -0.0240 636 VAL A CG1 
2708  C CG2 . VAL A 335 ? 0.5898 0.2862 0.3062 0.0296  -0.0244 -0.0258 636 VAL A CG2 
2709  N N   . GLU A 336 ? 0.5740 0.1918 0.2393 0.0207  -0.0253 -0.0197 637 GLU A N   
2710  C CA  . GLU A 336 ? 0.6014 0.1912 0.2449 0.0269  -0.0234 -0.0175 637 GLU A CA  
2711  C C   . GLU A 336 ? 0.6886 0.2973 0.3522 0.0186  -0.0238 -0.0130 637 GLU A C   
2712  O O   . GLU A 336 ? 0.6909 0.2991 0.3529 0.0305  -0.0212 -0.0103 637 GLU A O   
2713  C CB  . GLU A 336 ? 0.6835 0.2244 0.2887 0.0175  -0.0250 -0.0194 637 GLU A CB  
2714  C CG  . GLU A 336 ? 0.8301 0.3457 0.4092 0.0283  -0.0241 -0.0241 637 GLU A CG  
2715  C CD  . GLU A 336 ? 0.9791 0.4910 0.5482 0.0561  -0.0190 -0.0244 637 GLU A CD  
2716  O OE1 . GLU A 336 ? 0.8964 0.4136 0.4692 0.0672  -0.0167 -0.0210 637 GLU A OE1 
2717  O OE2 . GLU A 336 ? 1.0263 0.5314 0.5835 0.0673  -0.0174 -0.0282 637 GLU A OE2 
2718  N N   . ILE A 337 ? 0.6326 0.2598 0.3154 -0.0008 -0.0271 -0.0122 638 ILE A N   
2719  C CA  . ILE A 337 ? 0.6377 0.2854 0.3406 -0.0090 -0.0272 -0.0081 638 ILE A CA  
2720  C C   . ILE A 337 ? 0.6193 0.3012 0.3483 0.0054  -0.0249 -0.0066 638 ILE A C   
2721  O O   . ILE A 337 ? 0.5919 0.2772 0.3237 0.0110  -0.0230 -0.0036 638 ILE A O   
2722  C CB  . ILE A 337 ? 0.6266 0.2923 0.3467 -0.0305 -0.0312 -0.0081 638 ILE A CB  
2723  C CG1 . ILE A 337 ? 0.6501 0.2815 0.3431 -0.0474 -0.0336 -0.0091 638 ILE A CG1 
2724  C CG2 . ILE A 337 ? 0.5432 0.2388 0.2898 -0.0361 -0.0308 -0.0043 638 ILE A CG2 
2725  C CD1 . ILE A 337 ? 0.6738 0.3230 0.3808 -0.0671 -0.0383 -0.0103 638 ILE A CD1 
2726  N N   . ASN A 338 ? 0.5288 0.2347 0.2747 0.0117  -0.0248 -0.0089 639 ASN A N   
2727  C CA  . ASN A 338 ? 0.5045 0.2435 0.2750 0.0229  -0.0228 -0.0078 639 ASN A CA  
2728  C C   . ASN A 338 ? 0.5396 0.2710 0.2980 0.0431  -0.0194 -0.0078 639 ASN A C   
2729  O O   . ASN A 338 ? 0.5373 0.2900 0.3109 0.0509  -0.0181 -0.0060 639 ASN A O   
2730  C CB  . ASN A 338 ? 0.4512 0.2162 0.2414 0.0216  -0.0235 -0.0099 639 ASN A CB  
2731  C CG  . ASN A 338 ? 0.5301 0.3140 0.3402 0.0055  -0.0266 -0.0088 639 ASN A CG  
2732  O OD1 . ASN A 338 ? 0.5307 0.3411 0.3636 0.0050  -0.0263 -0.0070 639 ASN A OD1 
2733  N ND2 . ASN A 338 ? 0.4984 0.2683 0.2988 -0.0078 -0.0299 -0.0099 639 ASN A ND2 
2734  N N   . ILE A 339 ? 0.5053 0.2069 0.2358 0.0523  -0.0181 -0.0099 640 ILE A N   
2735  C CA  . ILE A 339 ? 0.5769 0.2676 0.2918 0.0727  -0.0151 -0.0095 640 ILE A CA  
2736  C C   . ILE A 339 ? 0.6694 0.3463 0.3754 0.0724  -0.0152 -0.0057 640 ILE A C   
2737  O O   . ILE A 339 ? 0.5631 0.2545 0.2761 0.0855  -0.0138 -0.0038 640 ILE A O   
2738  C CB  . ILE A 339 ? 0.5801 0.2356 0.2621 0.0824  -0.0137 -0.0125 640 ILE A CB  
2739  C CG1 . ILE A 339 ? 0.5722 0.2460 0.2639 0.0871  -0.0125 -0.0161 640 ILE A CG1 
2740  C CG2 . ILE A 339 ? 0.6018 0.2373 0.2609 0.1033  -0.0111 -0.0114 640 ILE A CG2 
2741  C CD1 . ILE A 339 ? 0.5779 0.2191 0.2377 0.0977  -0.0108 -0.0195 640 ILE A CD1 
2742  N N   . ALA A 340 ? 0.6323 0.2817 0.3226 0.0565  -0.0169 -0.0044 641 ALA A N   
2743  C CA  . ALA A 340 ? 0.6667 0.2986 0.3447 0.0542  -0.0165 -0.0004 641 ALA A CA  
2744  C C   . ALA A 340 ? 0.6470 0.3154 0.3555 0.0514  -0.0167 0.0025  641 ALA A C   
2745  O O   . ALA A 340 ? 0.5973 0.2650 0.3020 0.0617  -0.0154 0.0053  641 ALA A O   
2746  C CB  . ALA A 340 ? 0.6308 0.2306 0.2889 0.0338  -0.0181 0.0003  641 ALA A CB  
2747  N N   . VAL A 341 ? 0.5383 0.2376 0.2755 0.0384  -0.0184 0.0019  642 VAL A N   
2748  C CA  . VAL A 341 ? 0.5309 0.2621 0.2949 0.0351  -0.0185 0.0042  642 VAL A CA  
2749  C C   . VAL A 341 ? 0.5654 0.3183 0.3403 0.0537  -0.0172 0.0041  642 VAL A C   
2750  O O   . VAL A 341 ? 0.5189 0.2774 0.2959 0.0591  -0.0166 0.0067  642 VAL A O   
2751  C CB  . VAL A 341 ? 0.5086 0.2676 0.2992 0.0207  -0.0205 0.0031  642 VAL A CB  
2752  C CG1 . VAL A 341 ? 0.4574 0.2516 0.2760 0.0225  -0.0203 0.0043  642 VAL A CG1 
2753  C CG2 . VAL A 341 ? 0.5202 0.2653 0.3043 0.0011  -0.0222 0.0042  642 VAL A CG2 
2754  N N   . LEU A 342 ? 0.5243 0.2906 0.3058 0.0633  -0.0166 0.0009  643 LEU A N   
2755  C CA  . LEU A 342 ? 0.5385 0.3289 0.3311 0.0800  -0.0153 0.0003  643 LEU A CA  
2756  C C   . LEU A 342 ? 0.5674 0.3375 0.3368 0.0967  -0.0141 0.0020  643 LEU A C   
2757  O O   . LEU A 342 ? 0.5453 0.3318 0.3225 0.1056  -0.0142 0.0036  643 LEU A O   
2758  C CB  . LEU A 342 ? 0.4965 0.3009 0.2957 0.0865  -0.0141 -0.0033 643 LEU A CB  
2759  C CG  . LEU A 342 ? 0.4697 0.2987 0.2934 0.0731  -0.0151 -0.0046 643 LEU A CG  
2760  C CD1 . LEU A 342 ? 0.3885 0.2208 0.2104 0.0781  -0.0135 -0.0079 643 LEU A CD1 
2761  C CD2 . LEU A 342 ? 0.3852 0.2489 0.2358 0.0718  -0.0154 -0.0038 643 LEU A CD2 
2762  N N   . TYR A 343 ? 0.6446 0.3781 0.3838 0.1021  -0.0132 0.0014  644 TYR A N   
2763  C CA  . TYR A 343 ? 0.6386 0.3474 0.3511 0.1196  -0.0121 0.0032  644 TYR A CA  
2764  C C   . TYR A 343 ? 0.6360 0.3361 0.3437 0.1153  -0.0128 0.0076  644 TYR A C   
2765  O O   . TYR A 343 ? 0.6138 0.3150 0.3145 0.1311  -0.0125 0.0095  644 TYR A O   
2766  C CB  . TYR A 343 ? 0.5829 0.2467 0.2601 0.1222  -0.0111 0.0018  644 TYR A CB  
2767  C CG  . TYR A 343 ? 0.6272 0.2551 0.2702 0.1378  -0.0100 0.0042  644 TYR A CG  
2768  C CD1 . TYR A 343 ? 0.7000 0.3343 0.3357 0.1636  -0.0085 0.0037  644 TYR A CD1 
2769  C CD2 . TYR A 343 ? 0.6933 0.2805 0.3099 0.1270  -0.0102 0.0072  644 TYR A CD2 
2770  C CE1 . TYR A 343 ? 0.7303 0.3300 0.3324 0.1800  -0.0077 0.0061  644 TYR A CE1 
2771  C CE2 . TYR A 343 ? 0.7769 0.3267 0.3585 0.1415  -0.0090 0.0097  644 TYR A CE2 
2772  C CZ  . TYR A 343 ? 0.7957 0.3510 0.3696 0.1689  -0.0079 0.0092  644 TYR A CZ  
2773  O OH  . TYR A 343 ? 0.8459 0.3787 0.3913 0.1792  -0.0063 0.0105  644 TYR A OH  
2774  N N   . SER A 344 ? 0.6452 0.3381 0.3566 0.0942  -0.0137 0.0092  645 SER A N   
2775  C CA  . SER A 344 ? 0.6613 0.3421 0.3647 0.0885  -0.0136 0.0136  645 SER A CA  
2776  C C   . SER A 344 ? 0.6614 0.3806 0.3922 0.0918  -0.0143 0.0148  645 SER A C   
2777  O O   . SER A 344 ? 0.5855 0.3007 0.3075 0.1016  -0.0141 0.0178  645 SER A O   
2778  C CB  . SER A 344 ? 0.5909 0.2563 0.2912 0.0643  -0.0139 0.0148  645 SER A CB  
2779  O OG  . SER A 344 ? 0.6555 0.2788 0.3241 0.0609  -0.0135 0.0139  645 SER A OG  
2780  N N   . PHE A 345 ? 0.5622 0.3171 0.3244 0.0836  -0.0153 0.0125  646 PHE A N   
2781  C CA  . PHE A 345 ? 0.5124 0.3028 0.2996 0.0862  -0.0161 0.0129  646 PHE A CA  
2782  C C   . PHE A 345 ? 0.5411 0.3439 0.3267 0.1077  -0.0163 0.0122  646 PHE A C   
2783  O O   . PHE A 345 ? 0.4926 0.3042 0.2793 0.1149  -0.0171 0.0142  646 PHE A O   
2784  C CB  . PHE A 345 ? 0.4272 0.2491 0.2443 0.0750  -0.0170 0.0102  646 PHE A CB  
2785  C CG  . PHE A 345 ? 0.4450 0.2703 0.2727 0.0566  -0.0173 0.0117  646 PHE A CG  
2786  C CD1 . PHE A 345 ? 0.4620 0.2633 0.2766 0.0433  -0.0171 0.0127  646 PHE A CD1 
2787  C CD2 . PHE A 345 ? 0.4022 0.2555 0.2524 0.0525  -0.0179 0.0120  646 PHE A CD2 
2788  C CE1 . PHE A 345 ? 0.4144 0.2237 0.2406 0.0267  -0.0173 0.0142  646 PHE A CE1 
2789  C CE2 . PHE A 345 ? 0.3816 0.2402 0.2417 0.0375  -0.0179 0.0134  646 PHE A CE2 
2790  C CZ  . PHE A 345 ? 0.3602 0.1989 0.2095 0.0248  -0.0175 0.0146  646 PHE A CZ  
2791  N N   . GLN A 346 ? 0.5550 0.3589 0.3368 0.1186  -0.0157 0.0093  647 GLN A N   
2792  C CA  . GLN A 346 ? 0.5476 0.3685 0.3298 0.1396  -0.0157 0.0083  647 GLN A CA  
2793  C C   . GLN A 346 ? 0.5721 0.3656 0.3255 0.1549  -0.0157 0.0115  647 GLN A C   
2794  O O   . GLN A 346 ? 0.6238 0.4352 0.3804 0.1694  -0.0170 0.0123  647 GLN A O   
2795  C CB  . GLN A 346 ? 0.5083 0.3345 0.2902 0.1479  -0.0142 0.0047  647 GLN A CB  
2796  C CG  . GLN A 346 ? 0.5590 0.4190 0.3711 0.1365  -0.0141 0.0017  647 GLN A CG  
2797  C CD  . GLN A 346 ? 0.5553 0.4138 0.3638 0.1406  -0.0120 -0.0015 647 GLN A CD  
2798  O OE1 . GLN A 346 ? 0.6786 0.5080 0.4614 0.1505  -0.0106 -0.0018 647 GLN A OE1 
2799  N NE2 . GLN A 346 ? 0.5395 0.4274 0.3719 0.1331  -0.0115 -0.0039 647 GLN A NE2 
2800  N N   . SER A 347 ? 0.5562 0.3053 0.2798 0.1518  -0.0145 0.0134  648 SER A N   
2801  C CA  . SER A 347 ? 0.5506 0.2675 0.2422 0.1664  -0.0142 0.0169  648 SER A CA  
2802  C C   . SER A 347 ? 0.6322 0.3545 0.3275 0.1622  -0.0154 0.0208  648 SER A C   
2803  O O   . SER A 347 ? 0.6811 0.3962 0.3607 0.1790  -0.0160 0.0234  648 SER A O   
2804  C CB  . SER A 347 ? 0.7053 0.3700 0.3621 0.1607  -0.0125 0.0179  648 SER A CB  
2805  O OG  . SER A 347 ? 0.7675 0.4241 0.4163 0.1676  -0.0113 0.0140  648 SER A OG  
2806  N N   . ASP A 348 ? 0.6002 0.3360 0.3157 0.1412  -0.0156 0.0213  649 ASP A N   
2807  C CA  . ASP A 348 ? 0.5448 0.2878 0.2655 0.1357  -0.0162 0.0247  649 ASP A CA  
2808  C C   . ASP A 348 ? 0.5717 0.3613 0.3233 0.1396  -0.0185 0.0227  649 ASP A C   
2809  O O   . ASP A 348 ? 0.5783 0.3784 0.3377 0.1341  -0.0191 0.0248  649 ASP A O   
2810  C CB  . ASP A 348 ? 0.6153 0.3474 0.3392 0.1114  -0.0148 0.0263  649 ASP A CB  
2811  C CG  . ASP A 348 ? 0.6797 0.3633 0.3687 0.1059  -0.0127 0.0296  649 ASP A CG  
2812  O OD1 . ASP A 348 ? 0.6755 0.3304 0.3358 0.1220  -0.0123 0.0305  649 ASP A OD1 
2813  O OD2 . ASP A 348 ? 0.7031 0.3772 0.3924 0.0857  -0.0114 0.0312  649 ASP A OD2 
2814  N N   . LYS A 349 ? 0.4850 0.3022 0.2532 0.1483  -0.0194 0.0187  650 LYS A N   
2815  C CA  . LYS A 349 ? 0.5064 0.3677 0.3027 0.1511  -0.0216 0.0164  650 LYS A CA  
2816  C C   . LYS A 349 ? 0.4984 0.3765 0.3174 0.1311  -0.0219 0.0160  650 LYS A C   
2817  O O   . LYS A 349 ? 0.5079 0.4058 0.3385 0.1302  -0.0236 0.0164  650 LYS A O   
2818  C CB  . LYS A 349 ? 0.5748 0.4426 0.3623 0.1684  -0.0239 0.0184  650 LYS A CB  
2819  C CG  . LYS A 349 ? 0.7337 0.5928 0.5021 0.1917  -0.0240 0.0183  650 LYS A CG  
2820  C CD  . LYS A 349 ? 0.8685 0.7494 0.6375 0.2095  -0.0273 0.0191  650 LYS A CD  
2821  C CE  . LYS A 349 ? 1.0089 0.8989 0.7700 0.2333  -0.0277 0.0175  650 LYS A CE  
2822  N NZ  . LYS A 349 ? 1.1227 0.9653 0.8462 0.2463  -0.0255 0.0203  650 LYS A NZ  
2823  N N   . VAL A 350 ? 0.4614 0.3307 0.2851 0.1156  -0.0203 0.0151  651 VAL A N   
2824  C CA  . VAL A 350 ? 0.4360 0.3221 0.2814 0.0982  -0.0204 0.0144  651 VAL A CA  
2825  C C   . VAL A 350 ? 0.4993 0.4092 0.3656 0.0946  -0.0206 0.0102  651 VAL A C   
2826  O O   . VAL A 350 ? 0.4737 0.3732 0.3339 0.0957  -0.0196 0.0087  651 VAL A O   
2827  C CB  . VAL A 350 ? 0.4297 0.2902 0.2650 0.0829  -0.0186 0.0170  651 VAL A CB  
2828  C CG1 . VAL A 350 ? 0.4032 0.2841 0.2615 0.0673  -0.0187 0.0161  651 VAL A CG1 
2829  C CG2 . VAL A 350 ? 0.4166 0.2516 0.2287 0.0857  -0.0177 0.0215  651 VAL A CG2 
2830  N N   . THR A 351 ? 0.4348 0.3746 0.3237 0.0902  -0.0218 0.0082  652 THR A N   
2831  C CA  . THR A 351 ? 0.3695 0.3315 0.2768 0.0867  -0.0218 0.0045  652 THR A CA  
2832  C C   . THR A 351 ? 0.4001 0.3493 0.3078 0.0750  -0.0205 0.0042  652 THR A C   
2833  O O   . THR A 351 ? 0.3923 0.3321 0.3005 0.0633  -0.0204 0.0058  652 THR A O   
2834  C CB  . THR A 351 ? 0.3519 0.3419 0.2800 0.0806  -0.0232 0.0028  652 THR A CB  
2835  O OG1 . THR A 351 ? 0.4170 0.4186 0.3436 0.0907  -0.0251 0.0030  652 THR A OG1 
2836  C CG2 . THR A 351 ? 0.2865 0.2982 0.2310 0.0774  -0.0229 -0.0009 652 THR A CG2 
2837  N N   . ILE A 352 ? 0.3625 0.3123 0.2693 0.0787  -0.0196 0.0020  653 ILE A N   
2838  C CA  . ILE A 352 ? 0.3023 0.2438 0.2105 0.0686  -0.0189 0.0011  653 ILE A CA  
2839  C C   . ILE A 352 ? 0.3417 0.2992 0.2576 0.0736  -0.0177 -0.0020 653 ILE A C   
2840  O O   . ILE A 352 ? 0.4072 0.3748 0.3210 0.0865  -0.0171 -0.0030 653 ILE A O   
2841  C CB  . ILE A 352 ? 0.3438 0.2513 0.2293 0.0672  -0.0183 0.0028  653 ILE A CB  
2842  C CG1 . ILE A 352 ? 0.4497 0.3501 0.3381 0.0533  -0.0187 0.0022  653 ILE A CG1 
2843  C CG2 . ILE A 352 ? 0.3640 0.2588 0.2324 0.0815  -0.0172 0.0018  653 ILE A CG2 
2844  C CD1 . ILE A 352 ? 0.4134 0.2824 0.2813 0.0469  -0.0188 0.0040  653 ILE A CD1 
2845  N N   . VAL A 353 ? 0.3564 0.3178 0.2810 0.0638  -0.0174 -0.0033 654 VAL A N   
2846  C CA  . VAL A 353 ? 0.3792 0.3543 0.3097 0.0670  -0.0157 -0.0059 654 VAL A CA  
2847  C C   . VAL A 353 ? 0.3516 0.3071 0.2715 0.0626  -0.0151 -0.0064 654 VAL A C   
2848  O O   . VAL A 353 ? 0.3729 0.3162 0.2916 0.0517  -0.0166 -0.0053 654 VAL A O   
2849  C CB  . VAL A 353 ? 0.3189 0.3205 0.2704 0.0595  -0.0157 -0.0073 654 VAL A CB  
2850  C CG1 . VAL A 353 ? 0.2610 0.2575 0.2188 0.0459  -0.0170 -0.0065 654 VAL A CG1 
2851  C CG2 . VAL A 353 ? 0.4541 0.4709 0.4108 0.0623  -0.0132 -0.0096 654 VAL A CG2 
2852  N N   . ASP A 354 ? 0.3518 0.3047 0.2632 0.0716  -0.0130 -0.0081 655 ASP A N   
2853  C CA  . ASP A 354 ? 0.3964 0.3313 0.2974 0.0668  -0.0127 -0.0090 655 ASP A CA  
2854  C C   . ASP A 354 ? 0.3766 0.3286 0.2929 0.0578  -0.0121 -0.0101 655 ASP A C   
2855  O O   . ASP A 354 ? 0.4213 0.3980 0.3534 0.0576  -0.0110 -0.0107 655 ASP A O   
2856  C CB  . ASP A 354 ? 0.4598 0.3809 0.3421 0.0801  -0.0103 -0.0105 655 ASP A CB  
2857  C CG  . ASP A 354 ? 0.5535 0.5007 0.4450 0.0902  -0.0070 -0.0123 655 ASP A CG  
2858  O OD1 . ASP A 354 ? 0.6952 0.6489 0.5824 0.1044  -0.0059 -0.0124 655 ASP A OD1 
2859  O OD2 . ASP A 354 ? 0.5707 0.5328 0.4734 0.0840  -0.0056 -0.0136 655 ASP A OD2 
2860  N N   . HIS A 355 ? 0.3804 0.3179 0.2904 0.0500  -0.0132 -0.0104 656 HIS A N   
2861  C CA  . HIS A 355 ? 0.3750 0.3249 0.2966 0.0417  -0.0130 -0.0110 656 HIS A CA  
2862  C C   . HIS A 355 ? 0.3932 0.3587 0.3183 0.0477  -0.0091 -0.0128 656 HIS A C   
2863  O O   . HIS A 355 ? 0.3928 0.3742 0.3303 0.0417  -0.0082 -0.0128 656 HIS A O   
2864  C CB  . HIS A 355 ? 0.3652 0.2967 0.2775 0.0335  -0.0154 -0.0111 656 HIS A CB  
2865  C CG  . HIS A 355 ? 0.4075 0.3160 0.2984 0.0389  -0.0150 -0.0125 656 HIS A CG  
2866  N ND1 . HIS A 355 ? 0.4436 0.3310 0.3189 0.0419  -0.0159 -0.0120 656 HIS A ND1 
2867  C CD2 . HIS A 355 ? 0.3461 0.2468 0.2263 0.0413  -0.0135 -0.0144 656 HIS A CD2 
2868  C CE1 . HIS A 355 ? 0.4885 0.3548 0.3437 0.0464  -0.0152 -0.0139 656 HIS A CE1 
2869  N NE2 . HIS A 355 ? 0.4389 0.3137 0.2971 0.0464  -0.0138 -0.0155 656 HIS A NE2 
2870  N N   . HIS A 356 ? 0.3115 0.2729 0.2251 0.0598  -0.0065 -0.0141 657 HIS A N   
2871  C CA  . HIS A 356 ? 0.3408 0.3221 0.2596 0.0658  -0.0021 -0.0156 657 HIS A CA  
2872  C C   . HIS A 356 ? 0.3621 0.3730 0.2995 0.0660  -0.0011 -0.0154 657 HIS A C   
2873  O O   . HIS A 356 ? 0.3660 0.3962 0.3156 0.0598  0.0010  -0.0159 657 HIS A O   
2874  C CB  . HIS A 356 ? 0.3405 0.3123 0.2424 0.0807  0.0007  -0.0171 657 HIS A CB  
2875  C CG  . HIS A 356 ? 0.4515 0.3917 0.3323 0.0800  -0.0005 -0.0179 657 HIS A CG  
2876  N ND1 . HIS A 356 ? 0.4314 0.3662 0.3083 0.0738  0.0003  -0.0188 657 HIS A ND1 
2877  C CD2 . HIS A 356 ? 0.5309 0.4420 0.3922 0.0834  -0.0027 -0.0178 657 HIS A CD2 
2878  C CE1 . HIS A 356 ? 0.4937 0.3988 0.3502 0.0736  -0.0018 -0.0197 657 HIS A CE1 
2879  N NE2 . HIS A 356 ? 0.4894 0.3789 0.3358 0.0788  -0.0034 -0.0191 657 HIS A NE2 
2880  N N   . SER A 357 ? 0.3413 0.3550 0.2794 0.0725  -0.0027 -0.0148 658 SER A N   
2881  C CA  A SER A 357 ? 0.3679 0.4097 0.3227 0.0725  -0.0027 -0.0150 658 SER A CA  
2882  C CA  B SER A 357 ? 0.3698 0.4117 0.3246 0.0724  -0.0026 -0.0150 658 SER A CA  
2883  C C   . SER A 357 ? 0.3321 0.3802 0.3004 0.0576  -0.0046 -0.0143 658 SER A C   
2884  O O   . SER A 357 ? 0.2986 0.3691 0.2801 0.0524  -0.0033 -0.0152 658 SER A O   
2885  C CB  A SER A 357 ? 0.3259 0.3658 0.2760 0.0828  -0.0047 -0.0142 658 SER A CB  
2886  C CB  B SER A 357 ? 0.3245 0.3653 0.2749 0.0830  -0.0046 -0.0142 658 SER A CB  
2887  O OG  A SER A 357 ? 0.3247 0.3918 0.2902 0.0824  -0.0055 -0.0146 658 SER A OG  
2888  O OG  B SER A 357 ? 0.3658 0.3994 0.3016 0.0985  -0.0026 -0.0149 658 SER A OG  
2889  N N   . ALA A 358 ? 0.2856 0.3141 0.2500 0.0507  -0.0077 -0.0128 659 ALA A N   
2890  C CA  . ALA A 358 ? 0.2676 0.3009 0.2431 0.0389  -0.0095 -0.0121 659 ALA A CA  
2891  C C   . ALA A 358 ? 0.3393 0.3781 0.3194 0.0310  -0.0075 -0.0127 659 ALA A C   
2892  O O   . ALA A 358 ? 0.2743 0.3271 0.2647 0.0243  -0.0070 -0.0131 659 ALA A O   
2893  C CB  . ALA A 358 ? 0.2532 0.2666 0.2233 0.0342  -0.0128 -0.0103 659 ALA A CB  
2894  N N   . THR A 359 ? 0.3367 0.3627 0.3072 0.0314  -0.0065 -0.0127 660 THR A N   
2895  C CA  . THR A 359 ? 0.2933 0.3221 0.2658 0.0240  -0.0046 -0.0128 660 THR A CA  
2896  C C   . THR A 359 ? 0.2834 0.3344 0.2630 0.0248  -0.0002 -0.0141 660 THR A C   
2897  O O   . THR A 359 ? 0.2848 0.3440 0.2707 0.0160  0.0012  -0.0140 660 THR A O   
2898  C CB  . THR A 359 ? 0.2777 0.2884 0.2372 0.0246  -0.0047 -0.0127 660 THR A CB  
2899  O OG1 . THR A 359 ? 0.3488 0.3552 0.2981 0.0350  -0.0027 -0.0139 660 THR A OG1 
2900  C CG2 . THR A 359 ? 0.2565 0.2494 0.2117 0.0200  -0.0095 -0.0114 660 THR A CG2 
2901  N N   . GLU A 360 ? 0.2403 0.3018 0.2184 0.0352  0.0021  -0.0153 661 GLU A N   
2902  C CA  . GLU A 360 ? 0.2845 0.3728 0.2714 0.0358  0.0062  -0.0166 661 GLU A CA  
2903  C C   . GLU A 360 ? 0.3384 0.4440 0.3391 0.0281  0.0048  -0.0170 661 GLU A C   
2904  O O   . GLU A 360 ? 0.3549 0.4753 0.3629 0.0189  0.0073  -0.0175 661 GLU A O   
2905  C CB  . GLU A 360 ? 0.4245 0.5228 0.4076 0.0507  0.0084  -0.0179 661 GLU A CB  
2906  C CG  . GLU A 360 ? 0.5556 0.6869 0.5492 0.0523  0.0129  -0.0194 661 GLU A CG  
2907  C CD  . GLU A 360 ? 0.8130 0.9576 0.8038 0.0697  0.0144  -0.0205 661 GLU A CD  
2908  O OE1 . GLU A 360 ? 0.8523 0.9818 0.8347 0.0795  0.0111  -0.0200 661 GLU A OE1 
2909  O OE2 . GLU A 360 ? 0.9355 1.1059 0.9317 0.0739  0.0192  -0.0218 661 GLU A OE2 
2910  N N   . SER A 361 ? 0.3076 0.4101 0.3103 0.0309  0.0008  -0.0166 662 SER A N   
2911  C CA  . SER A 361 ? 0.3206 0.4368 0.3342 0.0237  -0.0011 -0.0173 662 SER A CA  
2912  C C   . SER A 361 ? 0.2840 0.3912 0.2990 0.0102  -0.0013 -0.0167 662 SER A C   
2913  O O   . SER A 361 ? 0.2939 0.4144 0.3160 0.0013  -0.0005 -0.0178 662 SER A O   
2914  C CB  . SER A 361 ? 0.3565 0.4661 0.3693 0.0290  -0.0053 -0.0166 662 SER A CB  
2915  O OG  . SER A 361 ? 0.5404 0.6581 0.5503 0.0424  -0.0052 -0.0170 662 SER A OG  
2916  N N   . PHE A 362 ? 0.3202 0.4045 0.3272 0.0084  -0.0026 -0.0150 663 PHE A N   
2917  C CA  . PHE A 362 ? 0.3490 0.4235 0.3557 -0.0020 -0.0032 -0.0142 663 PHE A CA  
2918  C C   . PHE A 362 ? 0.3508 0.4317 0.3569 -0.0094 0.0011  -0.0145 663 PHE A C   
2919  O O   . PHE A 362 ? 0.3838 0.4653 0.3916 -0.0190 0.0015  -0.0147 663 PHE A O   
2920  C CB  . PHE A 362 ? 0.2341 0.2862 0.2330 -0.0014 -0.0059 -0.0123 663 PHE A CB  
2921  C CG  . PHE A 362 ? 0.2998 0.3420 0.2976 -0.0094 -0.0070 -0.0113 663 PHE A CG  
2922  C CD1 . PHE A 362 ? 0.3089 0.3512 0.3110 -0.0124 -0.0092 -0.0115 663 PHE A CD1 
2923  C CD2 . PHE A 362 ? 0.3037 0.3365 0.2946 -0.0131 -0.0056 -0.0102 663 PHE A CD2 
2924  C CE1 . PHE A 362 ? 0.3559 0.3877 0.3549 -0.0180 -0.0100 -0.0106 663 PHE A CE1 
2925  C CE2 . PHE A 362 ? 0.3386 0.3609 0.3264 -0.0188 -0.0066 -0.0090 663 PHE A CE2 
2926  C CZ  . PHE A 362 ? 0.3849 0.4063 0.3765 -0.0208 -0.0088 -0.0093 663 PHE A CZ  
2927  N N   . ILE A 363 ? 0.3067 0.3909 0.3086 -0.0052 0.0045  -0.0145 664 ILE A N   
2928  C CA  . ILE A 363 ? 0.3102 0.4032 0.3115 -0.0123 0.0095  -0.0146 664 ILE A CA  
2929  C C   . ILE A 363 ? 0.3416 0.4593 0.3536 -0.0186 0.0114  -0.0164 664 ILE A C   
2930  O O   . ILE A 363 ? 0.3043 0.4243 0.3164 -0.0306 0.0138  -0.0164 664 ILE A O   
2931  C CB  . ILE A 363 ? 0.3213 0.4174 0.3168 -0.0047 0.0133  -0.0148 664 ILE A CB  
2932  C CG1 . ILE A 363 ? 0.3046 0.3753 0.2878 -0.0009 0.0113  -0.0134 664 ILE A CG1 
2933  C CG2 . ILE A 363 ? 0.2876 0.3980 0.2840 -0.0121 0.0195  -0.0149 664 ILE A CG2 
2934  C CD1 . ILE A 363 ? 0.3242 0.3790 0.3010 -0.0103 0.0109  -0.0115 664 ILE A CD1 
2935  N N   . LYS A 364 ? 0.2250 0.3613 0.2448 -0.0109 0.0104  -0.0180 665 LYS A N   
2936  C CA  . LYS A 364 ? 0.3304 0.4929 0.3613 -0.0168 0.0109  -0.0200 665 LYS A CA  
2937  C C   . LYS A 364 ? 0.3171 0.4701 0.3488 -0.0278 0.0077  -0.0203 665 LYS A C   
2938  O O   . LYS A 364 ? 0.2962 0.4594 0.3309 -0.0403 0.0095  -0.0215 665 LYS A O   
2939  C CB  . LYS A 364 ? 0.2910 0.4722 0.3283 -0.0041 0.0090  -0.0214 665 LYS A CB  
2940  C CG  . LYS A 364 ? 0.5404 0.7517 0.5899 -0.0091 0.0085  -0.0238 665 LYS A CG  
2941  C CD  . LYS A 364 ? 0.6931 0.9369 0.7499 -0.0060 0.0132  -0.0251 665 LYS A CD  
2942  C CE  . LYS A 364 ? 0.7521 1.0217 0.8189 -0.0219 0.0149  -0.0271 665 LYS A CE  
2943  N NZ  . LYS A 364 ? 0.8202 1.1270 0.8961 -0.0190 0.0197  -0.0283 665 LYS A NZ  
2944  N N   . HIS A 365 ? 0.2562 0.3891 0.2839 -0.0237 0.0033  -0.0193 666 HIS A N   
2945  C CA  . HIS A 365 ? 0.2594 0.3809 0.2859 -0.0319 0.0004  -0.0197 666 HIS A CA  
2946  C C   . HIS A 365 ? 0.3533 0.4590 0.3718 -0.0430 0.0027  -0.0186 666 HIS A C   
2947  O O   . HIS A 365 ? 0.3255 0.4306 0.3429 -0.0539 0.0029  -0.0198 666 HIS A O   
2948  C CB  . HIS A 365 ? 0.2582 0.3623 0.2816 -0.0243 -0.0039 -0.0184 666 HIS A CB  
2949  C CG  . HIS A 365 ? 0.2440 0.3348 0.2647 -0.0307 -0.0063 -0.0186 666 HIS A CG  
2950  N ND1 . HIS A 365 ? 0.2430 0.3434 0.2674 -0.0366 -0.0076 -0.0209 666 HIS A ND1 
2951  C CD2 . HIS A 365 ? 0.2529 0.3219 0.2665 -0.0315 -0.0077 -0.0169 666 HIS A CD2 
2952  C CE1 . HIS A 365 ? 0.3422 0.4250 0.3608 -0.0403 -0.0094 -0.0208 666 HIS A CE1 
2953  N NE2 . HIS A 365 ? 0.2679 0.3325 0.2803 -0.0368 -0.0094 -0.0182 666 HIS A NE2 
2954  N N   . MET A 366 ? 0.3289 0.4203 0.3397 -0.0405 0.0045  -0.0164 667 MET A N   
2955  C CA  . MET A 366 ? 0.3337 0.4087 0.3347 -0.0497 0.0067  -0.0149 667 MET A CA  
2956  C C   . MET A 366 ? 0.2189 0.3084 0.2213 -0.0619 0.0113  -0.0162 667 MET A C   
2957  O O   . MET A 366 ? 0.2660 0.3446 0.2618 -0.0731 0.0119  -0.0163 667 MET A O   
2958  C CB  . MET A 366 ? 0.3293 0.3912 0.3221 -0.0446 0.0080  -0.0126 667 MET A CB  
2959  C CG  . MET A 366 ? 0.3768 0.4175 0.3639 -0.0389 0.0036  -0.0108 667 MET A CG  
2960  S SD  . MET A 366 ? 0.4316 0.4570 0.4072 -0.0355 0.0046  -0.0084 667 MET A SD  
2961  C CE  . MET A 366 ? 0.4191 0.4297 0.3827 -0.0462 0.0076  -0.0066 667 MET A CE  
2962  N N   . GLU A 367 ? 0.2305 0.3445 0.2404 -0.0599 0.0148  -0.0171 668 GLU A N   
2963  C CA  . GLU A 367 ? 0.3402 0.4725 0.3528 -0.0725 0.0197  -0.0182 668 GLU A CA  
2964  C C   . GLU A 367 ? 0.2870 0.4298 0.3053 -0.0825 0.0175  -0.0209 668 GLU A C   
2965  O O   . GLU A 367 ? 0.3586 0.4985 0.3717 -0.0979 0.0200  -0.0214 668 GLU A O   
2966  C CB  . GLU A 367 ? 0.4303 0.5912 0.4515 -0.0661 0.0237  -0.0190 668 GLU A CB  
2967  C CG  . GLU A 367 ? 0.6282 0.7771 0.6411 -0.0575 0.0264  -0.0168 668 GLU A CG  
2968  C CD  . GLU A 367 ? 0.8108 0.9865 0.8305 -0.0484 0.0304  -0.0178 668 GLU A CD  
2969  O OE1 . GLU A 367 ? 0.8843 1.0899 0.9165 -0.0480 0.0307  -0.0200 668 GLU A OE1 
2970  O OE2 . GLU A 367 ? 0.8443 1.0113 0.8562 -0.0410 0.0330  -0.0165 668 GLU A OE2 
2971  N N   . ASN A 368 ? 0.2981 0.4520 0.3253 -0.0745 0.0129  -0.0227 669 ASN A N   
2972  C CA  . ASN A 368 ? 0.3013 0.4633 0.3325 -0.0831 0.0099  -0.0256 669 ASN A CA  
2973  C C   . ASN A 368 ? 0.3119 0.4429 0.3298 -0.0927 0.0086  -0.0252 669 ASN A C   
2974  O O   . ASN A 368 ? 0.3078 0.4388 0.3218 -0.1077 0.0095  -0.0270 669 ASN A O   
2975  C CB  . ASN A 368 ? 0.2543 0.4255 0.2935 -0.0707 0.0047  -0.0268 669 ASN A CB  
2976  C CG  . ASN A 368 ? 0.3509 0.5538 0.4018 -0.0606 0.0055  -0.0277 669 ASN A CG  
2977  O OD1 . ASN A 368 ? 0.3836 0.6095 0.4400 -0.0650 0.0098  -0.0283 669 ASN A OD1 
2978  N ND2 . ASN A 368 ? 0.3520 0.5561 0.4058 -0.0465 0.0015  -0.0276 669 ASN A ND2 
2979  N N   . GLU A 369 ? 0.2972 0.4016 0.3071 -0.0841 0.0064  -0.0228 670 GLU A N   
2980  C CA  . GLU A 369 ? 0.2734 0.3480 0.2698 -0.0895 0.0050  -0.0222 670 GLU A CA  
2981  C C   . GLU A 369 ? 0.3233 0.3827 0.3067 -0.1020 0.0095  -0.0209 670 GLU A C   
2982  O O   . GLU A 369 ? 0.3987 0.4419 0.3711 -0.1129 0.0095  -0.0219 670 GLU A O   
2983  C CB  . GLU A 369 ? 0.2747 0.3296 0.2673 -0.0763 0.0018  -0.0198 670 GLU A CB  
2984  C CG  . GLU A 369 ? 0.2829 0.3480 0.2851 -0.0661 -0.0024 -0.0210 670 GLU A CG  
2985  C CD  . GLU A 369 ? 0.3547 0.4155 0.3550 -0.0704 -0.0054 -0.0235 670 GLU A CD  
2986  O OE1 . GLU A 369 ? 0.2916 0.3336 0.2856 -0.0654 -0.0078 -0.0227 670 GLU A OE1 
2987  O OE2 . GLU A 369 ? 0.3394 0.4164 0.3439 -0.0788 -0.0053 -0.0265 670 GLU A OE2 
2988  N N   . TYR A 370 ? 0.3044 0.3663 0.2864 -0.1007 0.0135  -0.0185 671 TYR A N   
2989  C CA  . TYR A 370 ? 0.3283 0.3755 0.2965 -0.1134 0.0183  -0.0168 671 TYR A CA  
2990  C C   . TYR A 370 ? 0.3927 0.4575 0.3636 -0.1306 0.0214  -0.0195 671 TYR A C   
2991  O O   . TYR A 370 ? 0.3793 0.4249 0.3356 -0.1447 0.0235  -0.0194 671 TYR A O   
2992  C CB  . TYR A 370 ? 0.2760 0.3242 0.2419 -0.1087 0.0223  -0.0138 671 TYR A CB  
2993  C CG  . TYR A 370 ? 0.3784 0.3976 0.3325 -0.0987 0.0198  -0.0107 671 TYR A CG  
2994  C CD1 . TYR A 370 ? 0.3325 0.3526 0.2936 -0.0838 0.0152  -0.0105 671 TYR A CD1 
2995  C CD2 . TYR A 370 ? 0.4308 0.4216 0.3659 -0.1046 0.0216  -0.0080 671 TYR A CD2 
2996  C CE1 . TYR A 370 ? 0.3532 0.3507 0.3049 -0.0756 0.0123  -0.0079 671 TYR A CE1 
2997  C CE2 . TYR A 370 ? 0.4169 0.3842 0.3418 -0.0946 0.0186  -0.0053 671 TYR A CE2 
2998  C CZ  . TYR A 370 ? 0.4241 0.3966 0.3584 -0.0805 0.0138  -0.0054 671 TYR A CZ  
2999  O OH  . TYR A 370 ? 0.4881 0.4410 0.4136 -0.0715 0.0105  -0.0029 671 TYR A OH  
3000  N N   . ARG A 371 ? 0.3743 0.4753 0.3629 -0.1298 0.0215  -0.0221 672 ARG A N   
3001  C CA  . ARG A 371 ? 0.4160 0.5399 0.4095 -0.1468 0.0241  -0.0249 672 ARG A CA  
3002  C C   . ARG A 371 ? 0.4498 0.5624 0.4377 -0.1566 0.0199  -0.0280 672 ARG A C   
3003  O O   . ARG A 371 ? 0.4434 0.5469 0.4205 -0.1750 0.0223  -0.0291 672 ARG A O   
3004  C CB  . ARG A 371 ? 0.4598 0.6281 0.4741 -0.1411 0.0246  -0.0268 672 ARG A CB  
3005  C CG  . ARG A 371 ? 0.6701 0.8685 0.6922 -0.1587 0.0265  -0.0302 672 ARG A CG  
3006  C CD  . ARG A 371 ? 0.8431 1.0879 0.8864 -0.1502 0.0260  -0.0323 672 ARG A CD  
3007  N NE  . ARG A 371 ? 0.9763 1.2286 1.0243 -0.1328 0.0286  -0.0297 672 ARG A NE  
3008  C CZ  . ARG A 371 ? 0.9986 1.2592 1.0547 -0.1131 0.0249  -0.0299 672 ARG A CZ  
3009  N NH1 . ARG A 371 ? 0.9600 1.2244 1.0215 -0.1081 0.0184  -0.0321 672 ARG A NH1 
3010  N NH2 . ARG A 371 ? 0.9557 1.2191 1.0127 -0.0986 0.0276  -0.0278 672 ARG A NH2 
3011  N N   . CYS A 372 ? 0.3729 0.4840 0.3660 -0.1451 0.0139  -0.0295 673 CYS A N   
3012  C CA  A CYS A 372 ? 0.4325 0.5347 0.4199 -0.1539 0.0100  -0.0330 673 CYS A CA  
3013  C CA  B CYS A 372 ? 0.4329 0.5352 0.4204 -0.1538 0.0100  -0.0330 673 CYS A CA  
3014  C C   . CYS A 372 ? 0.4853 0.5434 0.4522 -0.1532 0.0086  -0.0317 673 CYS A C   
3015  O O   . CYS A 372 ? 0.5904 0.6317 0.5443 -0.1658 0.0079  -0.0341 673 CYS A O   
3016  C CB  A CYS A 372 ? 0.4233 0.5472 0.4254 -0.1429 0.0044  -0.0356 673 CYS A CB  
3017  C CB  B CYS A 372 ? 0.4248 0.5496 0.4273 -0.1427 0.0045  -0.0356 673 CYS A CB  
3018  S SG  A CYS A 372 ? 0.3830 0.4846 0.3829 -0.1216 0.0002  -0.0332 673 CYS A SG  
3019  S SG  B CYS A 372 ? 0.4942 0.6734 0.5196 -0.1431 0.0051  -0.0379 673 CYS A SG  
3020  N N   . ARG A 373 ? 0.3966 0.4356 0.3592 -0.1386 0.0082  -0.0281 674 ARG A N   
3021  C CA  . ARG A 373 ? 0.3963 0.3982 0.3418 -0.1339 0.0061  -0.0269 674 ARG A CA  
3022  C C   . ARG A 373 ? 0.4627 0.4356 0.3902 -0.1360 0.0097  -0.0231 674 ARG A C   
3023  O O   . ARG A 373 ? 0.4217 0.3620 0.3315 -0.1339 0.0085  -0.0222 674 ARG A O   
3024  C CB  . ARG A 373 ? 0.4213 0.4240 0.3752 -0.1148 0.0018  -0.0259 674 ARG A CB  
3025  C CG  . ARG A 373 ? 0.4561 0.4341 0.3989 -0.1096 -0.0017 -0.0267 674 ARG A CG  
3026  C CD  . ARG A 373 ? 0.3606 0.3404 0.3116 -0.0917 -0.0048 -0.0248 674 ARG A CD  
3027  N NE  . ARG A 373 ? 0.3761 0.3352 0.3170 -0.0862 -0.0075 -0.0256 674 ARG A NE  
3028  C CZ  . ARG A 373 ? 0.4781 0.4330 0.4218 -0.0723 -0.0097 -0.0237 674 ARG A CZ  
3029  N NH1 . ARG A 373 ? 0.3491 0.3170 0.3044 -0.0636 -0.0101 -0.0211 674 ARG A NH1 
3030  N NH2 . ARG A 373 ? 0.4526 0.3903 0.3866 -0.0674 -0.0114 -0.0246 674 ARG A NH2 
3031  N N   . GLY A 374 ? 0.4268 0.4103 0.3573 -0.1390 0.0141  -0.0207 675 GLY A N   
3032  C CA  . GLY A 374 ? 0.4018 0.3579 0.3144 -0.1399 0.0173  -0.0168 675 GLY A CA  
3033  C C   . GLY A 374 ? 0.4664 0.4117 0.3787 -0.1219 0.0149  -0.0134 675 GLY A C   
3034  O O   . GLY A 374 ? 0.4477 0.3656 0.3426 -0.1201 0.0160  -0.0102 675 GLY A O   
3035  N N   . GLY A 375 ? 0.3683 0.3335 0.2980 -0.1091 0.0115  -0.0141 676 GLY A N   
3036  C CA  . GLY A 375 ? 0.3893 0.3462 0.3192 -0.0940 0.0089  -0.0112 676 GLY A CA  
3037  C C   . GLY A 375 ? 0.4776 0.4503 0.4232 -0.0822 0.0044  -0.0126 676 GLY A C   
3038  O O   . GLY A 375 ? 0.4288 0.4142 0.3828 -0.0840 0.0027  -0.0156 676 GLY A O   
3039  N N   . CYS A 376 ? 0.4072 0.3779 0.3551 -0.0707 0.0025  -0.0104 677 CYS A N   
3040  C CA  . CYS A 376 ? 0.3941 0.3761 0.3544 -0.0598 -0.0015 -0.0110 677 CYS A CA  
3041  C C   . CYS A 376 ? 0.4066 0.3750 0.3618 -0.0503 -0.0040 -0.0081 677 CYS A C   
3042  O O   . CYS A 376 ? 0.3769 0.3462 0.3309 -0.0478 -0.0031 -0.0063 677 CYS A O   
3043  C CB  . CYS A 376 ? 0.3343 0.3417 0.3084 -0.0576 -0.0004 -0.0121 677 CYS A CB  
3044  S SG  . CYS A 376 ? 0.3650 0.3817 0.3503 -0.0452 -0.0048 -0.0124 677 CYS A SG  
3045  N N   . PRO A 377 ? 0.3143 0.2702 0.2653 -0.0449 -0.0071 -0.0075 678 PRO A N   
3046  C CA  . PRO A 377 ? 0.3397 0.2876 0.2879 -0.0356 -0.0101 -0.0049 678 PRO A CA  
3047  C C   . PRO A 377 ? 0.3493 0.3134 0.3100 -0.0301 -0.0119 -0.0049 678 PRO A C   
3048  O O   . PRO A 377 ? 0.2894 0.2668 0.2605 -0.0290 -0.0125 -0.0067 678 PRO A O   
3049  C CB  . PRO A 377 ? 0.3903 0.3283 0.3348 -0.0307 -0.0127 -0.0051 678 PRO A CB  
3050  C CG  . PRO A 377 ? 0.3185 0.2665 0.2703 -0.0349 -0.0121 -0.0083 678 PRO A CG  
3051  C CD  . PRO A 377 ? 0.2887 0.2435 0.2409 -0.0456 -0.0086 -0.0098 678 PRO A CD  
3052  N N   . ALA A 378 ? 0.3599 0.3212 0.3176 -0.0268 -0.0127 -0.0030 679 ALA A N   
3053  C CA  . ALA A 378 ? 0.3026 0.2751 0.2685 -0.0227 -0.0142 -0.0032 679 ALA A CA  
3054  C C   . ALA A 378 ? 0.2767 0.2421 0.2375 -0.0181 -0.0174 -0.0011 679 ALA A C   
3055  O O   . ALA A 378 ? 0.2961 0.2509 0.2464 -0.0189 -0.0168 0.0005  679 ALA A O   
3056  C CB  . ALA A 378 ? 0.3160 0.2983 0.2843 -0.0258 -0.0106 -0.0044 679 ALA A CB  
3057  N N   . ASP A 379 ? 0.2909 0.2625 0.2584 -0.0140 -0.0207 -0.0011 680 ASP A N   
3058  C CA  . ASP A 379 ? 0.3014 0.2701 0.2662 -0.0104 -0.0247 0.0004  680 ASP A CA  
3059  C C   . ASP A 379 ? 0.3046 0.2758 0.2690 -0.0109 -0.0249 -0.0003 680 ASP A C   
3060  O O   . ASP A 379 ? 0.2627 0.2398 0.2328 -0.0103 -0.0260 -0.0012 680 ASP A O   
3061  C CB  . ASP A 379 ? 0.3102 0.2850 0.2823 -0.0071 -0.0280 0.0008  680 ASP A CB  
3062  C CG  . ASP A 379 ? 0.3876 0.3637 0.3587 -0.0043 -0.0326 0.0023  680 ASP A CG  
3063  O OD1 . ASP A 379 ? 0.3614 0.3430 0.3369 -0.0009 -0.0350 0.0032  680 ASP A OD1 
3064  O OD2 . ASP A 379 ? 0.3815 0.3543 0.3471 -0.0054 -0.0338 0.0025  680 ASP A OD2 
3065  N N   . TRP A 380 ? 0.3153 0.2798 0.2704 -0.0119 -0.0237 0.0002  681 TRP A N   
3066  C CA  . TRP A 380 ? 0.3181 0.2824 0.2696 -0.0117 -0.0232 -0.0008 681 TRP A CA  
3067  C C   . TRP A 380 ? 0.2794 0.2446 0.2327 -0.0104 -0.0278 -0.0012 681 TRP A C   
3068  O O   . TRP A 380 ? 0.2649 0.2307 0.2182 -0.0100 -0.0273 -0.0026 681 TRP A O   
3069  C CB  . TRP A 380 ? 0.2988 0.2541 0.2382 -0.0124 -0.0221 0.0002  681 TRP A CB  
3070  C CG  . TRP A 380 ? 0.3272 0.2810 0.2603 -0.0120 -0.0197 -0.0011 681 TRP A CG  
3071  C CD1 . TRP A 380 ? 0.3381 0.2949 0.2689 -0.0132 -0.0138 -0.0019 681 TRP A CD1 
3072  C CD2 . TRP A 380 ? 0.2800 0.2290 0.2068 -0.0103 -0.0230 -0.0020 681 TRP A CD2 
3073  N NE1 . TRP A 380 ? 0.3310 0.2849 0.2543 -0.0107 -0.0129 -0.0031 681 TRP A NE1 
3074  C CE2 . TRP A 380 ? 0.3403 0.2876 0.2601 -0.0092 -0.0186 -0.0034 681 TRP A CE2 
3075  C CE3 . TRP A 380 ? 0.2748 0.2216 0.2011 -0.0101 -0.0291 -0.0020 681 TRP A CE3 
3076  C CZ2 . TRP A 380 ? 0.3330 0.2728 0.2431 -0.0072 -0.0203 -0.0049 681 TRP A CZ2 
3077  C CZ3 . TRP A 380 ? 0.3325 0.2725 0.2496 -0.0100 -0.0311 -0.0035 681 TRP A CZ3 
3078  C CH2 . TRP A 380 ? 0.3047 0.2397 0.2130 -0.0082 -0.0268 -0.0050 681 TRP A CH2 
3079  N N   . VAL A 381 ? 0.2282 0.1935 0.1821 -0.0097 -0.0324 0.0003  682 VAL A N   
3080  C CA  . VAL A 381 ? 0.3036 0.2718 0.2593 -0.0106 -0.0371 0.0000  682 VAL A CA  
3081  C C   . VAL A 381 ? 0.3638 0.3375 0.3275 -0.0117 -0.0363 -0.0009 682 VAL A C   
3082  O O   . VAL A 381 ? 0.3178 0.2895 0.2793 -0.0139 -0.0381 -0.0018 682 VAL A O   
3083  C CB  . VAL A 381 ? 0.2505 0.2233 0.2082 -0.0089 -0.0417 0.0018  682 VAL A CB  
3084  C CG1 . VAL A 381 ? 0.2516 0.2320 0.2137 -0.0116 -0.0464 0.0016  682 VAL A CG1 
3085  C CG2 . VAL A 381 ? 0.2403 0.2053 0.1868 -0.0070 -0.0432 0.0030  682 VAL A CG2 
3086  N N   . TRP A 382 ? 0.2880 0.2671 0.2593 -0.0105 -0.0336 -0.0008 683 TRP A N   
3087  C CA  . TRP A 382 ? 0.2933 0.2772 0.2711 -0.0108 -0.0327 -0.0014 683 TRP A CA  
3088  C C   . TRP A 382 ? 0.2823 0.2644 0.2583 -0.0095 -0.0289 -0.0029 683 TRP A C   
3089  O O   . TRP A 382 ? 0.2910 0.2726 0.2672 -0.0090 -0.0287 -0.0034 683 TRP A O   
3090  C CB  . TRP A 382 ? 0.2692 0.2604 0.2552 -0.0095 -0.0323 -0.0006 683 TRP A CB  
3091  C CG  . TRP A 382 ? 0.2385 0.2360 0.2289 -0.0098 -0.0359 0.0007  683 TRP A CG  
3092  C CD1 . TRP A 382 ? 0.3023 0.3014 0.2908 -0.0090 -0.0394 0.0019  683 TRP A CD1 
3093  C CD2 . TRP A 382 ? 0.2769 0.2821 0.2741 -0.0108 -0.0363 0.0013  683 TRP A CD2 
3094  N NE1 . TRP A 382 ? 0.2646 0.2747 0.2600 -0.0094 -0.0420 0.0029  683 TRP A NE1 
3095  C CE2 . TRP A 382 ? 0.3089 0.3225 0.3096 -0.0111 -0.0398 0.0026  683 TRP A CE2 
3096  C CE3 . TRP A 382 ? 0.3440 0.3507 0.3444 -0.0112 -0.0340 0.0009  683 TRP A CE3 
3097  C CZ2 . TRP A 382 ? 0.2898 0.3143 0.2978 -0.0127 -0.0404 0.0035  683 TRP A CZ2 
3098  C CZ3 . TRP A 382 ? 0.3052 0.3197 0.3111 -0.0128 -0.0346 0.0020  683 TRP A CZ3 
3099  C CH2 . TRP A 382 ? 0.3198 0.3437 0.3299 -0.0140 -0.0375 0.0033  683 TRP A CH2 
3100  N N   . ILE A 383 ? 0.2366 0.2185 0.2103 -0.0088 -0.0257 -0.0035 684 ILE A N   
3101  C CA  . ILE A 383 ? 0.2268 0.2124 0.2010 -0.0068 -0.0219 -0.0050 684 ILE A CA  
3102  C C   . ILE A 383 ? 0.3210 0.2998 0.2865 -0.0044 -0.0215 -0.0060 684 ILE A C   
3103  O O   . ILE A 383 ? 0.3102 0.2900 0.2749 -0.0006 -0.0199 -0.0070 684 ILE A O   
3104  C CB  . ILE A 383 ? 0.2655 0.2552 0.2403 -0.0084 -0.0183 -0.0053 684 ILE A CB  
3105  C CG1 . ILE A 383 ? 0.3069 0.3005 0.2880 -0.0107 -0.0185 -0.0049 684 ILE A CG1 
3106  C CG2 . ILE A 383 ? 0.2167 0.2144 0.1925 -0.0062 -0.0144 -0.0070 684 ILE A CG2 
3107  C CD1 . ILE A 383 ? 0.3100 0.3116 0.2986 -0.0092 -0.0186 -0.0058 684 ILE A CD1 
3108  N N   . VAL A 384 ? 0.2586 0.2293 0.2159 -0.0056 -0.0229 -0.0058 685 VAL A N   
3109  C CA  . VAL A 384 ? 0.2651 0.2267 0.2113 -0.0032 -0.0224 -0.0072 685 VAL A CA  
3110  C C   . VAL A 384 ? 0.3043 0.2586 0.2474 -0.0035 -0.0254 -0.0075 685 VAL A C   
3111  O O   . VAL A 384 ? 0.3637 0.3173 0.3093 -0.0081 -0.0294 -0.0064 685 VAL A O   
3112  C CB  . VAL A 384 ? 0.3047 0.2584 0.2414 -0.0050 -0.0240 -0.0070 685 VAL A CB  
3113  C CG1 . VAL A 384 ? 0.2702 0.2118 0.1932 -0.0027 -0.0240 -0.0089 685 VAL A CG1 
3114  C CG2 . VAL A 384 ? 0.2857 0.2439 0.2225 -0.0052 -0.0201 -0.0064 685 VAL A CG2 
3115  N N   . PRO A 385 ? 0.2985 0.2472 0.2352 0.0012  -0.0234 -0.0087 686 PRO A N   
3116  C CA  . PRO A 385 ? 0.2860 0.2248 0.2175 0.0002  -0.0256 -0.0087 686 PRO A CA  
3117  C C   . PRO A 385 ? 0.3370 0.2627 0.2580 -0.0056 -0.0298 -0.0091 686 PRO A C   
3118  O O   . PRO A 385 ? 0.3449 0.2658 0.2585 -0.0059 -0.0302 -0.0101 686 PRO A O   
3119  C CB  . PRO A 385 ? 0.3866 0.3194 0.3095 0.0086  -0.0222 -0.0100 686 PRO A CB  
3120  C CG  . PRO A 385 ? 0.3708 0.3202 0.3031 0.0131  -0.0183 -0.0103 686 PRO A CG  
3121  C CD  . PRO A 385 ? 0.3060 0.2602 0.2418 0.0081  -0.0185 -0.0100 686 PRO A CD  
3122  N N   . PRO A 386 ? 0.3997 0.3200 0.3194 -0.0111 -0.0328 -0.0084 687 PRO A N   
3123  C CA  . PRO A 386 ? 0.3266 0.2373 0.2375 -0.0189 -0.0374 -0.0090 687 PRO A CA  
3124  C C   . PRO A 386 ? 0.3766 0.2649 0.2667 -0.0180 -0.0373 -0.0113 687 PRO A C   
3125  O O   . PRO A 386 ? 0.4180 0.2962 0.2985 -0.0258 -0.0415 -0.0123 687 PRO A O   
3126  C CB  . PRO A 386 ? 0.3696 0.2849 0.2874 -0.0258 -0.0396 -0.0073 687 PRO A CB  
3127  C CG  . PRO A 386 ? 0.3327 0.2457 0.2509 -0.0200 -0.0356 -0.0066 687 PRO A CG  
3128  C CD  . PRO A 386 ? 0.3163 0.2399 0.2420 -0.0114 -0.0321 -0.0069 687 PRO A CD  
3129  N N   . MET A 387 ? 0.3593 0.2397 0.2413 -0.0086 -0.0330 -0.0125 688 MET A N   
3130  C CA  . MET A 387 ? 0.4029 0.2616 0.2633 -0.0049 -0.0323 -0.0151 688 MET A CA  
3131  C C   . MET A 387 ? 0.4912 0.3558 0.3511 0.0061  -0.0272 -0.0161 688 MET A C   
3132  O O   . MET A 387 ? 0.4111 0.2940 0.2858 0.0110  -0.0240 -0.0149 688 MET A O   
3133  C CB  . MET A 387 ? 0.4547 0.2918 0.2992 -0.0035 -0.0317 -0.0155 688 MET A CB  
3134  C CG  . MET A 387 ? 0.5430 0.3838 0.3898 0.0083  -0.0271 -0.0147 688 MET A CG  
3135  S SD  . MET A 387 ? 0.5904 0.4022 0.4148 0.0118  -0.0264 -0.0146 688 MET A SD  
3136  C CE  . MET A 387 ? 0.5431 0.3282 0.3397 0.0202  -0.0248 -0.0183 688 MET A CE  
3137  N N   . SER A 388 ? 0.4654 0.3154 0.3082 0.0093  -0.0265 -0.0186 689 SER A N   
3138  C CA  . SER A 388 ? 0.4462 0.3006 0.2854 0.0204  -0.0210 -0.0199 689 SER A CA  
3139  C C   . SER A 388 ? 0.4084 0.2882 0.2667 0.0202  -0.0185 -0.0183 689 SER A C   
3140  O O   . SER A 388 ? 0.4474 0.3403 0.3115 0.0280  -0.0134 -0.0183 689 SER A O   
3141  C CB  . SER A 388 ? 0.5491 0.3994 0.3828 0.0319  -0.0171 -0.0203 689 SER A CB  
3142  O OG  . SER A 388 ? 0.6141 0.4369 0.4276 0.0312  -0.0194 -0.0215 689 SER A OG  
3143  N N   . GLY A 389 ? 0.3859 0.2725 0.2530 0.0111  -0.0222 -0.0168 690 GLY A N   
3144  C CA  . GLY A 389 ? 0.3619 0.2682 0.2448 0.0097  -0.0203 -0.0150 690 GLY A CA  
3145  C C   . GLY A 389 ? 0.3946 0.3090 0.2762 0.0159  -0.0142 -0.0156 690 GLY A C   
3146  O O   . GLY A 389 ? 0.3748 0.3055 0.2681 0.0188  -0.0102 -0.0149 690 GLY A O   
3147  N N   . SER A 390 ? 0.3586 0.2624 0.2253 0.0177  -0.0133 -0.0171 691 SER A N   
3148  C CA  . SER A 390 ? 0.3435 0.2574 0.2098 0.0218  -0.0071 -0.0172 691 SER A CA  
3149  C C   . SER A 390 ? 0.3458 0.2658 0.2101 0.0324  -0.0011 -0.0188 691 SER A C   
3150  O O   . SER A 390 ? 0.3850 0.3182 0.2512 0.0359  0.0048  -0.0189 691 SER A O   
3151  C CB  . SER A 390 ? 0.4263 0.3277 0.2767 0.0206  -0.0076 -0.0180 691 SER A CB  
3152  O OG  . SER A 390 ? 0.4399 0.3231 0.2716 0.0261  -0.0079 -0.0210 691 SER A OG  
3153  N N   . ILE A 391 ? 0.4075 0.3195 0.2676 0.0381  -0.0023 -0.0200 692 ILE A N   
3154  C CA  . ILE A 391 ? 0.4425 0.3645 0.3026 0.0499  0.0033  -0.0211 692 ILE A CA  
3155  C C   . ILE A 391 ? 0.4481 0.3921 0.3282 0.0495  0.0040  -0.0195 692 ILE A C   
3156  O O   . ILE A 391 ? 0.5017 0.4595 0.3852 0.0591  0.0080  -0.0202 692 ILE A O   
3157  C CB  . ILE A 391 ? 0.4871 0.3865 0.3268 0.0598  0.0029  -0.0234 692 ILE A CB  
3158  C CG1 . ILE A 391 ? 0.5388 0.4229 0.3766 0.0552  -0.0028 -0.0227 692 ILE A CG1 
3159  C CG2 . ILE A 391 ? 0.5267 0.4054 0.3445 0.0610  0.0032  -0.0257 692 ILE A CG2 
3160  C CD1 . ILE A 391 ? 0.6364 0.4999 0.4554 0.0660  -0.0023 -0.0243 692 ILE A CD1 
3161  N N   . THR A 392 ? 0.4281 0.3772 0.3214 0.0390  0.0002  -0.0175 693 THR A N   
3162  C CA  . THR A 392 ? 0.4313 0.4022 0.3431 0.0372  0.0013  -0.0162 693 THR A CA  
3163  C C   . THR A 392 ? 0.4154 0.4022 0.3366 0.0304  0.0044  -0.0153 693 THR A C   
3164  O O   . THR A 392 ? 0.3498 0.3278 0.2651 0.0248  0.0038  -0.0146 693 THR A O   
3165  C CB  . THR A 392 ? 0.4105 0.3771 0.3298 0.0307  -0.0040 -0.0147 693 THR A CB  
3166  O OG1 . THR A 392 ? 0.4307 0.3916 0.3513 0.0211  -0.0072 -0.0134 693 THR A OG1 
3167  C CG2 . THR A 392 ? 0.3612 0.3092 0.2690 0.0349  -0.0070 -0.0152 693 THR A CG2 
3168  N N   . PRO A 393 ? 0.3932 0.4025 0.3277 0.0302  0.0077  -0.0152 694 PRO A N   
3169  C CA  . PRO A 393 ? 0.3308 0.3533 0.2713 0.0227  0.0116  -0.0144 694 PRO A CA  
3170  C C   . PRO A 393 ? 0.2904 0.3046 0.2337 0.0119  0.0082  -0.0124 694 PRO A C   
3171  O O   . PRO A 393 ? 0.3823 0.3964 0.3229 0.0058  0.0107  -0.0113 694 PRO A O   
3172  C CB  . PRO A 393 ? 0.3737 0.4229 0.3281 0.0240  0.0149  -0.0151 694 PRO A CB  
3173  C CG  . PRO A 393 ? 0.3206 0.3688 0.2788 0.0301  0.0109  -0.0156 694 PRO A CG  
3174  C CD  . PRO A 393 ? 0.3415 0.3655 0.2841 0.0372  0.0084  -0.0160 694 PRO A CD  
3175  N N   . VAL A 394 ? 0.3197 0.3264 0.2670 0.0100  0.0028  -0.0117 695 VAL A N   
3176  C CA  . VAL A 394 ? 0.3288 0.3301 0.2793 0.0016  -0.0001 -0.0099 695 VAL A CA  
3177  C C   . VAL A 394 ? 0.2910 0.2760 0.2300 -0.0004 -0.0023 -0.0088 695 VAL A C   
3178  O O   . VAL A 394 ? 0.2605 0.2413 0.1988 -0.0060 -0.0033 -0.0071 695 VAL A O   
3179  C CB  . VAL A 394 ? 0.2563 0.2559 0.2142 0.0008  -0.0049 -0.0094 695 VAL A CB  
3180  C CG1 . VAL A 394 ? 0.2585 0.2750 0.2279 0.0014  -0.0032 -0.0103 695 VAL A CG1 
3181  C CG2 . VAL A 394 ? 0.2663 0.2539 0.2179 0.0056  -0.0085 -0.0098 695 VAL A CG2 
3182  N N   . PHE A 395 ? 0.3274 0.3021 0.2556 0.0045  -0.0032 -0.0099 696 PHE A N   
3183  C CA  . PHE A 395 ? 0.4135 0.3736 0.3300 0.0024  -0.0059 -0.0093 696 PHE A CA  
3184  C C   . PHE A 395 ? 0.3437 0.3054 0.2553 -0.0006 -0.0016 -0.0081 696 PHE A C   
3185  O O   . PHE A 395 ? 0.3014 0.2543 0.2073 -0.0044 -0.0042 -0.0063 696 PHE A O   
3186  C CB  . PHE A 395 ? 0.3698 0.3175 0.2735 0.0077  -0.0071 -0.0113 696 PHE A CB  
3187  C CG  . PHE A 395 ? 0.3523 0.2855 0.2422 0.0055  -0.0103 -0.0112 696 PHE A CG  
3188  C CD1 . PHE A 395 ? 0.3926 0.3158 0.2796 0.0022  -0.0172 -0.0112 696 PHE A CD1 
3189  C CD2 . PHE A 395 ? 0.3638 0.2948 0.2435 0.0066  -0.0063 -0.0113 696 PHE A CD2 
3190  C CE1 . PHE A 395 ? 0.3858 0.2976 0.2602 0.0001  -0.0209 -0.0114 696 PHE A CE1 
3191  C CE2 . PHE A 395 ? 0.4154 0.3329 0.2813 0.0051  -0.0096 -0.0113 696 PHE A CE2 
3192  C CZ  . PHE A 395 ? 0.4125 0.3206 0.2757 0.0019  -0.0173 -0.0115 696 PHE A CZ  
3193  N N   . HIS A 396 ? 0.2922 0.2663 0.2059 0.0009  0.0049  -0.0088 697 HIS A N   
3194  C CA  . HIS A 396 ? 0.3195 0.2965 0.2276 -0.0026 0.0104  -0.0077 697 HIS A CA  
3195  C C   . HIS A 396 ? 0.3293 0.3150 0.2460 -0.0108 0.0126  -0.0059 697 HIS A C   
3196  O O   . HIS A 396 ? 0.3821 0.3703 0.2941 -0.0159 0.0179  -0.0047 697 HIS A O   
3197  C CB  . HIS A 396 ? 0.3624 0.3507 0.2679 0.0034  0.0170  -0.0096 697 HIS A CB  
3198  C CG  . HIS A 396 ? 0.4474 0.4242 0.3419 0.0124  0.0150  -0.0119 697 HIS A CG  
3199  N ND1 . HIS A 396 ? 0.4621 0.4234 0.3399 0.0140  0.0147  -0.0122 697 HIS A ND1 
3200  C CD2 . HIS A 396 ? 0.5085 0.4838 0.4039 0.0199  0.0130  -0.0139 697 HIS A CD2 
3201  C CE1 . HIS A 396 ? 0.5207 0.4713 0.3894 0.0216  0.0126  -0.0147 697 HIS A CE1 
3202  N NE2 . HIS A 396 ? 0.4747 0.4325 0.3532 0.0253  0.0117  -0.0155 697 HIS A NE2 
3203  N N   . GLN A 397 ? 0.2781 0.2669 0.2055 -0.0128 0.0090  -0.0059 698 GLN A N   
3204  C CA  . GLN A 397 ? 0.3062 0.3010 0.2405 -0.0205 0.0105  -0.0049 698 GLN A CA  
3205  C C   . GLN A 397 ? 0.3268 0.3045 0.2548 -0.0240 0.0063  -0.0025 698 GLN A C   
3206  O O   . GLN A 397 ? 0.3971 0.3684 0.3274 -0.0208 0.0005  -0.0024 698 GLN A O   
3207  C CB  . GLN A 397 ? 0.2789 0.2869 0.2273 -0.0192 0.0089  -0.0065 698 GLN A CB  
3208  C CG  . GLN A 397 ? 0.2419 0.2547 0.1963 -0.0276 0.0098  -0.0061 698 GLN A CG  
3209  C CD  . GLN A 397 ? 0.2989 0.3242 0.2534 -0.0346 0.0166  -0.0062 698 GLN A CD  
3210  O OE1 . GLN A 397 ? 0.2604 0.3049 0.2212 -0.0318 0.0202  -0.0080 698 GLN A OE1 
3211  N NE2 . GLN A 397 ? 0.2757 0.2901 0.2220 -0.0435 0.0185  -0.0043 698 GLN A NE2 
3212  N N   . GLU A 398 ? 0.2891 0.2597 0.2085 -0.0304 0.0095  -0.0005 699 GLU A N   
3213  C CA  . GLU A 398 ? 0.2803 0.2345 0.1929 -0.0325 0.0058  0.0019  699 GLU A CA  
3214  C C   . GLU A 398 ? 0.3436 0.3017 0.2660 -0.0352 0.0042  0.0012  699 GLU A C   
3215  O O   . GLU A 398 ? 0.3152 0.2868 0.2459 -0.0398 0.0077  -0.0004 699 GLU A O   
3216  C CB  . GLU A 398 ? 0.3381 0.2804 0.2361 -0.0385 0.0101  0.0045  699 GLU A CB  
3217  C CG  . GLU A 398 ? 0.3214 0.2571 0.2070 -0.0353 0.0112  0.0055  699 GLU A CG  
3218  C CD  . GLU A 398 ? 0.4004 0.3224 0.2697 -0.0414 0.0155  0.0087  699 GLU A CD  
3219  O OE1 . GLU A 398 ? 0.4286 0.3398 0.2842 -0.0383 0.0151  0.0103  699 GLU A OE1 
3220  O OE2 . GLU A 398 ? 0.4694 0.3900 0.3382 -0.0496 0.0192  0.0095  699 GLU A OE2 
3221  N N   . MET A 399 ? 0.3344 0.2824 0.2557 -0.0319 -0.0012 0.0022  700 MET A N   
3222  C CA  . MET A 399 ? 0.3725 0.3224 0.3013 -0.0330 -0.0030 0.0014  700 MET A CA  
3223  C C   . MET A 399 ? 0.3948 0.3263 0.3124 -0.0328 -0.0052 0.0037  700 MET A C   
3224  O O   . MET A 399 ? 0.4618 0.3819 0.3693 -0.0288 -0.0076 0.0060  700 MET A O   
3225  C CB  . MET A 399 ? 0.3524 0.3116 0.2931 -0.0268 -0.0075 -0.0001 700 MET A CB  
3226  C CG  . MET A 399 ? 0.2554 0.2301 0.2050 -0.0257 -0.0054 -0.0023 700 MET A CG  
3227  S SD  . MET A 399 ? 0.3524 0.3319 0.3105 -0.0188 -0.0104 -0.0034 700 MET A SD  
3228  C CE  . MET A 399 ? 0.3334 0.3252 0.2947 -0.0159 -0.0068 -0.0055 700 MET A CE  
3229  N N   . LEU A 400 ? 0.2947 0.2227 0.2126 -0.0368 -0.0042 0.0031  701 LEU A N   
3230  C CA  . LEU A 400 ? 0.3042 0.2136 0.2109 -0.0347 -0.0064 0.0049  701 LEU A CA  
3231  C C   . LEU A 400 ? 0.3962 0.3119 0.3133 -0.0290 -0.0105 0.0035  701 LEU A C   
3232  O O   . LEU A 400 ? 0.4134 0.3417 0.3417 -0.0320 -0.0095 0.0010  701 LEU A O   
3233  C CB  . LEU A 400 ? 0.3509 0.2468 0.2457 -0.0441 -0.0019 0.0051  701 LEU A CB  
3234  C CG  . LEU A 400 ? 0.4433 0.3279 0.3233 -0.0504 0.0026  0.0074  701 LEU A CG  
3235  C CD1 . LEU A 400 ? 0.4591 0.3316 0.3286 -0.0622 0.0072  0.0072  701 LEU A CD1 
3236  C CD2 . LEU A 400 ? 0.4460 0.3122 0.3113 -0.0423 -0.0006 0.0109  701 LEU A CD2 
3237  N N   . ASN A 401 ? 0.4053 0.3144 0.3190 -0.0206 -0.0149 0.0052  702 ASN A N   
3238  C CA  . ASN A 401 ? 0.3285 0.2447 0.2516 -0.0148 -0.0183 0.0042  702 ASN A CA  
3239  C C   . ASN A 401 ? 0.3735 0.2724 0.2845 -0.0113 -0.0187 0.0050  702 ASN A C   
3240  O O   . ASN A 401 ? 0.3983 0.2817 0.2950 -0.0069 -0.0198 0.0076  702 ASN A O   
3241  C CB  . ASN A 401 ? 0.3836 0.3102 0.3144 -0.0076 -0.0231 0.0050  702 ASN A CB  
3242  C CG  . ASN A 401 ? 0.4045 0.3435 0.3479 -0.0040 -0.0253 0.0038  702 ASN A CG  
3243  O OD1 . ASN A 401 ? 0.3743 0.3162 0.3224 -0.0070 -0.0231 0.0019  702 ASN A OD1 
3244  N ND2 . ASN A 401 ? 0.3687 0.3159 0.3173 0.0018  -0.0295 0.0048  702 ASN A ND2 
3245  N N   . TYR A 402 ? 0.3979 0.2982 0.3129 -0.0127 -0.0179 0.0029  703 TYR A N   
3246  C CA  . TYR A 402 ? 0.3036 0.1862 0.2058 -0.0085 -0.0182 0.0031  703 TYR A CA  
3247  C C   . TYR A 402 ? 0.3515 0.2446 0.2644 -0.0068 -0.0188 0.0004  703 TYR A C   
3248  O O   . TYR A 402 ? 0.3444 0.2555 0.2721 -0.0109 -0.0184 -0.0015 703 TYR A O   
3249  C CB  . TYR A 402 ? 0.3442 0.2041 0.2280 -0.0170 -0.0142 0.0031  703 TYR A CB  
3250  C CG  . TYR A 402 ? 0.4192 0.2881 0.3092 -0.0306 -0.0103 0.0007  703 TYR A CG  
3251  C CD1 . TYR A 402 ? 0.4140 0.2855 0.3071 -0.0368 -0.0091 -0.0026 703 TYR A CD1 
3252  C CD2 . TYR A 402 ? 0.4141 0.2900 0.3061 -0.0370 -0.0078 0.0016  703 TYR A CD2 
3253  C CE1 . TYR A 402 ? 0.3319 0.2155 0.2316 -0.0491 -0.0060 -0.0049 703 TYR A CE1 
3254  C CE2 . TYR A 402 ? 0.3518 0.2395 0.2502 -0.0485 -0.0040 -0.0006 703 TYR A CE2 
3255  C CZ  . TYR A 402 ? 0.3843 0.2769 0.2872 -0.0546 -0.0033 -0.0038 703 TYR A CZ  
3256  O OH  . TYR A 402 ? 0.4153 0.3236 0.3256 -0.0657 0.0000  -0.0059 703 TYR A OH  
3257  N N   . ARG A 403 ? 0.3915 0.2727 0.2955 0.0006  -0.0198 0.0005  704 ARG A N   
3258  C CA  . ARG A 403 ? 0.3944 0.2860 0.3076 0.0052  -0.0207 -0.0015 704 ARG A CA  
3259  C C   . ARG A 403 ? 0.4490 0.3252 0.3512 -0.0002 -0.0183 -0.0044 704 ARG A C   
3260  O O   . ARG A 403 ? 0.5036 0.3556 0.3865 0.0029  -0.0176 -0.0041 704 ARG A O   
3261  C CB  . ARG A 403 ? 0.3910 0.2849 0.3037 0.0190  -0.0237 0.0004  704 ARG A CB  
3262  C CG  . ARG A 403 ? 0.4562 0.3671 0.3800 0.0224  -0.0267 0.0028  704 ARG A CG  
3263  C CD  . ARG A 403 ? 0.6355 0.5535 0.5606 0.0355  -0.0299 0.0046  704 ARG A CD  
3264  N NE  . ARG A 403 ? 0.7429 0.6788 0.6817 0.0381  -0.0298 0.0032  704 ARG A NE  
3265  C CZ  . ARG A 403 ? 0.7974 0.7424 0.7386 0.0491  -0.0313 0.0040  704 ARG A CZ  
3266  N NH1 . ARG A 403 ? 0.8297 0.7682 0.7608 0.0599  -0.0334 0.0062  704 ARG A NH1 
3267  N NH2 . ARG A 403 ? 0.7671 0.7284 0.7204 0.0500  -0.0305 0.0029  704 ARG A NH2 
3268  N N   . LEU A 404 ? 0.4144 0.3036 0.3274 -0.0083 -0.0172 -0.0073 705 LEU A N   
3269  C CA  . LEU A 404 ? 0.3934 0.2722 0.2981 -0.0148 -0.0156 -0.0107 705 LEU A CA  
3270  C C   . LEU A 404 ? 0.3551 0.2427 0.2665 -0.0076 -0.0169 -0.0125 705 LEU A C   
3271  O O   . LEU A 404 ? 0.3800 0.2878 0.3070 -0.0020 -0.0184 -0.0114 705 LEU A O   
3272  C CB  . LEU A 404 ? 0.3818 0.2719 0.2938 -0.0285 -0.0139 -0.0129 705 LEU A CB  
3273  C CG  . LEU A 404 ? 0.4125 0.2972 0.3189 -0.0371 -0.0116 -0.0113 705 LEU A CG  
3274  C CD1 . LEU A 404 ? 0.3831 0.2854 0.2997 -0.0492 -0.0098 -0.0138 705 LEU A CD1 
3275  C CD2 . LEU A 404 ? 0.3773 0.2302 0.2591 -0.0404 -0.0098 -0.0107 705 LEU A CD2 
3276  N N   . THR A 405 ? 0.4330 0.3039 0.3307 -0.0086 -0.0161 -0.0152 706 THR A N   
3277  C CA  . THR A 405 ? 0.4340 0.3124 0.3362 -0.0027 -0.0168 -0.0174 706 THR A CA  
3278  C C   . THR A 405 ? 0.4642 0.3456 0.3670 -0.0139 -0.0164 -0.0215 706 THR A C   
3279  O O   . THR A 405 ? 0.4108 0.2799 0.3034 -0.0254 -0.0153 -0.0233 706 THR A O   
3280  C CB  . THR A 405 ? 0.5380 0.3947 0.4223 0.0085  -0.0166 -0.0175 706 THR A CB  
3281  O OG1 . THR A 405 ? 0.5768 0.4437 0.4667 0.0157  -0.0168 -0.0192 706 THR A OG1 
3282  C CG2 . THR A 405 ? 0.5315 0.3569 0.3915 0.0010  -0.0151 -0.0201 706 THR A CG2 
3283  N N   . PRO A 406 ? 0.4515 0.3500 0.3658 -0.0115 -0.0173 -0.0232 707 PRO A N   
3284  C CA  . PRO A 406 ? 0.3739 0.2898 0.3011 -0.0009 -0.0181 -0.0213 707 PRO A CA  
3285  C C   . PRO A 406 ? 0.3665 0.3005 0.3096 0.0008  -0.0188 -0.0177 707 PRO A C   
3286  O O   . PRO A 406 ? 0.4044 0.3426 0.3519 -0.0065 -0.0188 -0.0170 707 PRO A O   
3287  C CB  . PRO A 406 ? 0.4260 0.3540 0.3594 -0.0044 -0.0186 -0.0243 707 PRO A CB  
3288  C CG  . PRO A 406 ? 0.4896 0.4009 0.4081 -0.0134 -0.0185 -0.0284 707 PRO A CG  
3289  C CD  . PRO A 406 ? 0.4732 0.3736 0.3856 -0.0214 -0.0176 -0.0275 707 PRO A CD  
3290  N N   . SER A 407 ? 0.3188 0.2641 0.2701 0.0100  -0.0193 -0.0154 708 SER A N   
3291  C CA  . SER A 407 ? 0.3505 0.3101 0.3143 0.0108  -0.0203 -0.0122 708 SER A CA  
3292  C C   . SER A 407 ? 0.3448 0.3215 0.3199 0.0167  -0.0206 -0.0106 708 SER A C   
3293  O O   . SER A 407 ? 0.3552 0.3325 0.3280 0.0225  -0.0197 -0.0114 708 SER A O   
3294  C CB  . SER A 407 ? 0.4444 0.3942 0.4015 0.0147  -0.0210 -0.0097 708 SER A CB  
3295  O OG  . SER A 407 ? 0.5382 0.4829 0.4889 0.0255  -0.0211 -0.0090 708 SER A OG  
3296  N N   . PHE A 408 ? 0.3135 0.3032 0.2996 0.0146  -0.0216 -0.0084 709 PHE A N   
3297  C CA  . PHE A 408 ? 0.2971 0.3019 0.2930 0.0182  -0.0219 -0.0062 709 PHE A CA  
3298  C C   . PHE A 408 ? 0.3753 0.3824 0.3719 0.0230  -0.0234 -0.0037 709 PHE A C   
3299  O O   . PHE A 408 ? 0.3771 0.3784 0.3711 0.0206  -0.0248 -0.0030 709 PHE A O   
3300  C CB  . PHE A 408 ? 0.2864 0.3011 0.2911 0.0125  -0.0222 -0.0054 709 PHE A CB  
3301  C CG  . PHE A 408 ? 0.3288 0.3449 0.3336 0.0098  -0.0213 -0.0074 709 PHE A CG  
3302  C CD1 . PHE A 408 ? 0.3170 0.3310 0.3210 0.0045  -0.0215 -0.0090 709 PHE A CD1 
3303  C CD2 . PHE A 408 ? 0.3371 0.3582 0.3425 0.0130  -0.0201 -0.0077 709 PHE A CD2 
3304  C CE1 . PHE A 408 ? 0.2785 0.2964 0.2829 0.0028  -0.0213 -0.0109 709 PHE A CE1 
3305  C CE2 . PHE A 408 ? 0.2878 0.3102 0.2922 0.0111  -0.0197 -0.0095 709 PHE A CE2 
3306  C CZ  . PHE A 408 ? 0.2666 0.2880 0.2708 0.0061  -0.0207 -0.0111 709 PHE A CZ  
3307  N N   . GLU A 409 ? 0.3202 0.3369 0.3200 0.0300  -0.0232 -0.0025 710 GLU A N   
3308  C CA  . GLU A 409 ? 0.3610 0.3837 0.3619 0.0361  -0.0250 -0.0003 710 GLU A CA  
3309  C C   . GLU A 409 ? 0.3688 0.4136 0.3827 0.0354  -0.0254 0.0018  710 GLU A C   
3310  O O   . GLU A 409 ? 0.3376 0.3907 0.3567 0.0332  -0.0234 0.0017  710 GLU A O   
3311  C CB  . GLU A 409 ? 0.3535 0.3681 0.3444 0.0471  -0.0242 -0.0008 710 GLU A CB  
3312  C CG  . GLU A 409 ? 0.4961 0.4854 0.4712 0.0465  -0.0234 -0.0030 710 GLU A CG  
3313  C CD  . GLU A 409 ? 0.6183 0.5962 0.5872 0.0434  -0.0253 -0.0019 710 GLU A CD  
3314  O OE1 . GLU A 409 ? 0.6101 0.5991 0.5856 0.0448  -0.0278 0.0005  710 GLU A OE1 
3315  O OE2 . GLU A 409 ? 0.6441 0.6022 0.6010 0.0390  -0.0243 -0.0034 710 GLU A OE2 
3316  N N   . TYR A 410 ? 0.2722 0.3267 0.2904 0.0365  -0.0282 0.0038  711 TYR A N   
3317  C CA  . TYR A 410 ? 0.2728 0.3501 0.3026 0.0354  -0.0288 0.0057  711 TYR A CA  
3318  C C   . TYR A 410 ? 0.2686 0.3584 0.3003 0.0458  -0.0270 0.0062  711 TYR A C   
3319  O O   . TYR A 410 ? 0.3571 0.4365 0.3794 0.0559  -0.0265 0.0053  711 TYR A O   
3320  C CB  . TYR A 410 ? 0.3869 0.4724 0.4203 0.0333  -0.0330 0.0073  711 TYR A CB  
3321  C CG  . TYR A 410 ? 0.4591 0.5348 0.4909 0.0234  -0.0346 0.0070  711 TYR A CG  
3322  C CD1 . TYR A 410 ? 0.7483 0.8115 0.7726 0.0239  -0.0370 0.0068  711 TYR A CD1 
3323  C CD2 . TYR A 410 ? 0.5600 0.6379 0.5961 0.0143  -0.0334 0.0069  711 TYR A CD2 
3324  C CE1 . TYR A 410 ? 0.7893 0.8443 0.8114 0.0158  -0.0380 0.0063  711 TYR A CE1 
3325  C CE2 . TYR A 410 ? 0.7229 0.7909 0.7558 0.0071  -0.0346 0.0065  711 TYR A CE2 
3326  C CZ  . TYR A 410 ? 0.6948 0.7523 0.7213 0.0079  -0.0368 0.0060  711 TYR A CZ  
3327  O OH  . TYR A 410 ? 0.6965 0.7448 0.7192 0.0015  -0.0375 0.0054  711 TYR A OH  
3328  N N   . GLN A 411 ? 0.2225 0.3343 0.2651 0.0435  -0.0257 0.0076  712 GLN A N   
3329  C CA  . GLN A 411 ? 0.2476 0.3765 0.2938 0.0535  -0.0235 0.0082  712 GLN A CA  
3330  C C   . GLN A 411 ? 0.3371 0.4955 0.3976 0.0484  -0.0243 0.0106  712 GLN A C   
3331  O O   . GLN A 411 ? 0.3001 0.4608 0.3654 0.0357  -0.0256 0.0115  712 GLN A O   
3332  C CB  . GLN A 411 ? 0.3140 0.4371 0.3560 0.0559  -0.0187 0.0068  712 GLN A CB  
3333  C CG  . GLN A 411 ? 0.2581 0.3828 0.3048 0.0439  -0.0167 0.0073  712 GLN A CG  
3334  C CD  . GLN A 411 ? 0.1886 0.3069 0.2297 0.0468  -0.0124 0.0058  712 GLN A CD  
3335  O OE1 . GLN A 411 ? 0.3402 0.4588 0.3762 0.0575  -0.0102 0.0047  712 GLN A OE1 
3336  N NE2 . GLN A 411 ? 0.2866 0.3978 0.3268 0.0379  -0.0115 0.0057  712 GLN A NE2 
3337  N N   . PRO A 412 ? 0.3831 0.5643 0.4496 0.0580  -0.0236 0.0117  713 PRO A N   
3338  C CA  . PRO A 412 ? 0.4116 0.6248 0.4928 0.0516  -0.0244 0.0139  713 PRO A CA  
3339  C C   . PRO A 412 ? 0.4026 0.6217 0.4891 0.0391  -0.0203 0.0148  713 PRO A C   
3340  O O   . PRO A 412 ? 0.3464 0.5543 0.4274 0.0410  -0.0159 0.0140  713 PRO A O   
3341  C CB  . PRO A 412 ? 0.4341 0.6710 0.5198 0.0671  -0.0232 0.0146  713 PRO A CB  
3342  C CG  . PRO A 412 ? 0.4394 0.6512 0.5097 0.0823  -0.0234 0.0128  713 PRO A CG  
3343  C CD  . PRO A 412 ? 0.3931 0.5726 0.4526 0.0751  -0.0217 0.0109  713 PRO A CD  
3344  N N   . ASP A 413 ? 0.3940 0.6287 0.4894 0.0258  -0.0220 0.0164  714 ASP A N   
3345  C CA  . ASP A 413 ? 0.3908 0.6341 0.4905 0.0139  -0.0179 0.0180  714 ASP A CA  
3346  C C   . ASP A 413 ? 0.4119 0.6787 0.5179 0.0222  -0.0125 0.0190  714 ASP A C   
3347  O O   . ASP A 413 ? 0.4281 0.7202 0.5421 0.0314  -0.0133 0.0195  714 ASP A O   
3348  C CB  . ASP A 413 ? 0.4135 0.6717 0.5207 -0.0018 -0.0208 0.0195  714 ASP A CB  
3349  C CG  . ASP A 413 ? 0.5739 0.8066 0.6727 -0.0106 -0.0252 0.0184  714 ASP A CG  
3350  O OD1 . ASP A 413 ? 0.5706 0.7756 0.6591 -0.0101 -0.0238 0.0173  714 ASP A OD1 
3351  O OD2 . ASP A 413 ? 0.6648 0.9063 0.7672 -0.0176 -0.0301 0.0186  714 ASP A OD2 
3352  N N   . PRO A 414 ? 0.3702 0.6302 0.4721 0.0201  -0.0069 0.0193  715 PRO A N   
3353  C CA  . PRO A 414 ? 0.3173 0.5968 0.4228 0.0300  -0.0012 0.0199  715 PRO A CA  
3354  C C   . PRO A 414 ? 0.3302 0.6496 0.4508 0.0249  0.0007  0.0225  715 PRO A C   
3355  O O   . PRO A 414 ? 0.4034 0.7466 0.5297 0.0373  0.0039  0.0228  715 PRO A O   
3356  C CB  . PRO A 414 ? 0.3052 0.5659 0.4014 0.0260  0.0036  0.0198  715 PRO A CB  
3357  C CG  . PRO A 414 ? 0.3337 0.5772 0.4265 0.0101  0.0012  0.0206  715 PRO A CG  
3358  C CD  . PRO A 414 ? 0.3709 0.6062 0.4641 0.0094  -0.0056 0.0193  715 PRO A CD  
3359  N N   . TRP A 415 ? 0.2836 0.6119 0.4103 0.0071  -0.0011 0.0244  716 TRP A N   
3360  C CA  . TRP A 415 ? 0.3316 0.7008 0.4734 0.0002  0.0007  0.0267  716 TRP A CA  
3361  C C   . TRP A 415 ? 0.4052 0.8016 0.5577 0.0101  -0.0043 0.0262  716 TRP A C   
3362  O O   . TRP A 415 ? 0.4068 0.8435 0.5734 0.0094  -0.0026 0.0278  716 TRP A O   
3363  C CB  . TRP A 415 ? 0.2902 0.6594 0.4332 -0.0232 0.0000  0.0287  716 TRP A CB  
3364  C CG  . TRP A 415 ? 0.3712 0.7185 0.5087 -0.0308 -0.0073 0.0273  716 TRP A CG  
3365  C CD1 . TRP A 415 ? 0.3517 0.7146 0.4966 -0.0340 -0.0138 0.0267  716 TRP A CD1 
3366  C CD2 . TRP A 415 ? 0.4234 0.7302 0.5461 -0.0357 -0.0088 0.0262  716 TRP A CD2 
3367  N NE1 . TRP A 415 ? 0.3624 0.6952 0.4970 -0.0407 -0.0189 0.0252  716 TRP A NE1 
3368  C CE2 . TRP A 415 ? 0.4328 0.7316 0.5541 -0.0416 -0.0157 0.0249  716 TRP A CE2 
3369  C CE3 . TRP A 415 ? 0.4252 0.7031 0.5354 -0.0349 -0.0050 0.0261  716 TRP A CE3 
3370  C CZ2 . TRP A 415 ? 0.5040 0.7675 0.6123 -0.0461 -0.0184 0.0236  716 TRP A CZ2 
3371  C CZ3 . TRP A 415 ? 0.4556 0.7001 0.5537 -0.0393 -0.0081 0.0248  716 TRP A CZ3 
3372  C CH2 . TRP A 415 ? 0.5393 0.7770 0.6366 -0.0446 -0.0144 0.0236  716 TRP A CH2 
3373  N N   . ASN A 416 ? 0.4439 0.8207 0.5898 0.0195  -0.0103 0.0241  717 ASN A N   
3374  C CA  . ASN A 416 ? 0.5029 0.9024 0.6559 0.0326  -0.0150 0.0237  717 ASN A CA  
3375  C C   . ASN A 416 ? 0.5459 0.9538 0.6971 0.0556  -0.0113 0.0231  717 ASN A C   
3376  O O   . ASN A 416 ? 0.5798 1.0160 0.7389 0.0681  -0.0136 0.0235  717 ASN A O   
3377  C CB  . ASN A 416 ? 0.3997 0.7730 0.5438 0.0348  -0.0224 0.0221  717 ASN A CB  
3378  C CG  . ASN A 416 ? 0.4946 0.8618 0.6397 0.0144  -0.0269 0.0223  717 ASN A CG  
3379  O OD1 . ASN A 416 ? 0.5909 0.9835 0.7465 -0.0002 -0.0267 0.0238  717 ASN A OD1 
3380  N ND2 . ASN A 416 ? 0.4059 0.7390 0.5390 0.0129  -0.0306 0.0208  717 ASN A ND2 
3381  N N   . THR A 417 ? 0.5152 0.8989 0.6550 0.0620  -0.0060 0.0221  718 THR A N   
3382  C CA  . THR A 417 ? 0.4773 0.8595 0.6102 0.0843  -0.0027 0.0208  718 THR A CA  
3383  C C   . THR A 417 ? 0.5389 0.9347 0.6734 0.0873  0.0058  0.0214  718 THR A C   
3384  O O   . THR A 417 ? 0.5246 0.9287 0.6556 0.1066  0.0091  0.0205  718 THR A O   
3385  C CB  . THR A 417 ? 0.4964 0.8324 0.6098 0.0921  -0.0047 0.0180  718 THR A CB  
3386  O OG1 . THR A 417 ? 0.5350 0.8442 0.6418 0.0775  -0.0032 0.0175  718 THR A OG1 
3387  C CG2 . THR A 417 ? 0.4614 0.7863 0.5716 0.0943  -0.0124 0.0176  718 THR A CG2 
3388  N N   . HIS A 418 ? 0.5122 0.9100 0.6502 0.0697  0.0096  0.0229  719 HIS A N   
3389  C CA  . HIS A 418 ? 0.5494 0.9550 0.6859 0.0719  0.0180  0.0236  719 HIS A CA  
3390  C C   . HIS A 418 ? 0.5564 1.0122 0.7096 0.0751  0.0223  0.0259  719 HIS A C   
3391  O O   . HIS A 418 ? 0.5059 0.9901 0.6737 0.0602  0.0209  0.0282  719 HIS A O   
3392  C CB  . HIS A 418 ? 0.5249 0.9130 0.6572 0.0522  0.0206  0.0249  719 HIS A CB  
3393  C CG  . HIS A 418 ? 0.4684 0.8606 0.5967 0.0537  0.0291  0.0258  719 HIS A CG  
3394  N ND1 . HIS A 418 ? 0.4527 0.8206 0.5661 0.0671  0.0319  0.0232  719 HIS A ND1 
3395  C CD2 . HIS A 418 ? 0.4460 0.8628 0.5818 0.0426  0.0354  0.0290  719 HIS A CD2 
3396  C CE1 . HIS A 418 ? 0.4674 0.8452 0.5794 0.0654  0.0395  0.0247  719 HIS A CE1 
3397  N NE2 . HIS A 418 ? 0.4704 0.8778 0.5958 0.0507  0.0421  0.0284  719 HIS A NE2 
3398  N N   . VAL A 419 ? 0.6228 1.0899 0.7731 0.0943  0.0278  0.0250  720 VAL A N   
3399  C CA  . VAL A 419 ? 0.6867 1.1900 0.8459 0.0955  0.0329  0.0268  720 VAL A CA  
3400  C C   . VAL A 419 ? 0.6345 1.1411 0.7933 0.0843  0.0414  0.0287  720 VAL A C   
3401  O O   . VAL A 419 ? 0.6016 1.0895 0.7487 0.0940  0.0465  0.0272  720 VAL A O   
3402  C CB  . VAL A 419 ? 0.7521 1.2567 0.9022 0.1206  0.0340  0.0249  720 VAL A CB  
3403  C CG1 . VAL A 419 ? 0.7343 1.2558 0.8900 0.1262  0.0274  0.0250  720 VAL A CG1 
3404  C CG2 . VAL A 419 ? 0.7887 1.2556 0.9206 0.1379  0.0340  0.0216  720 VAL A CG2 
3405  N N   . TRP A 420 ? 0.5950 1.1232 0.7646 0.0634  0.0430  0.0318  721 TRP A N   
3406  C CA  . TRP A 420 ? 0.6071 1.1359 0.7747 0.0499  0.0509  0.0343  721 TRP A CA  
3407  C C   . TRP A 420 ? 0.6474 1.1899 0.8110 0.0626  0.0586  0.0343  721 TRP A C   
3408  O O   . TRP A 420 ? 0.6971 1.2546 0.8618 0.0789  0.0577  0.0330  721 TRP A O   
3409  C CB  . TRP A 420 ? 0.5556 1.1004 0.7329 0.0235  0.0502  0.0375  721 TRP A CB  
3410  C CG  . TRP A 420 ? 0.5471 1.0715 0.7240 0.0082  0.0445  0.0378  721 TRP A CG  
3411  C CD1 . TRP A 420 ? 0.4837 1.0029 0.6643 0.0082  0.0354  0.0361  721 TRP A CD1 
3412  C CD2 . TRP A 420 ? 0.4533 0.9433 0.6170 -0.0086 0.0458  0.0392  721 TRP A CD2 
3413  N NE1 . TRP A 420 ? 0.4429 0.9264 0.6135 -0.0077 0.0311  0.0361  721 TRP A NE1 
3414  C CE2 . TRP A 420 ? 0.4551 0.9202 0.6151 -0.0176 0.0372  0.0379  721 TRP A CE2 
3415  C CE3 . TRP A 420 ? 0.4566 0.9337 0.6097 -0.0158 0.0532  0.0414  721 TRP A CE3 
3416  C CZ2 . TRP A 420 ? 0.4422 0.8706 0.5886 -0.0326 0.0360  0.0387  721 TRP A CZ2 
3417  C CZ3 . TRP A 420 ? 0.4840 0.9241 0.6233 -0.0308 0.0516  0.0424  721 TRP A CZ3 
3418  C CH2 . TRP A 420 ? 0.5115 0.9279 0.6476 -0.0385 0.0431  0.0410  721 TRP A CH2 
3419  N N   . LYS A 421 ? 0.6899 1.2257 0.8469 0.0554  0.0663  0.0360  722 LYS A N   
3420  C CA  . LYS A 421 ? 0.7503 1.2982 0.9026 0.0653  0.0742  0.0364  722 LYS A CA  
3421  C C   . LYS A 421 ? 0.7906 1.3612 0.9499 0.0450  0.0798  0.0405  722 LYS A C   
3422  O O   . LYS A 421 ? 0.8029 1.4001 0.9672 0.0493  0.0835  0.0413  722 LYS A O   
3423  C CB  . LYS A 421 ? 0.7568 1.2758 0.8917 0.0769  0.0792  0.0344  722 LYS A CB  
3424  C CG  . LYS A 421 ? 0.7914 1.2826 0.9164 0.0953  0.0739  0.0299  722 LYS A CG  
3425  C CD  . LYS A 421 ? 0.8153 1.2741 0.9193 0.1058  0.0780  0.0272  722 LYS A CD  
3426  C CE  . LYS A 421 ? 0.8129 1.2259 0.9014 0.1128  0.0699  0.0227  722 LYS A CE  
3427  N NZ  . LYS A 421 ? 0.7961 1.2093 0.8825 0.1341  0.0665  0.0194  722 LYS A NZ  
3428  N N   . ARG B 3   ? 0.8620 0.8992 0.8127 0.1347  0.0311  -0.0356 304 ARG B N   
3429  C CA  . ARG B 3   ? 0.8666 0.8913 0.8102 0.1243  0.0307  -0.0380 304 ARG B CA  
3430  C C   . ARG B 3   ? 0.8757 0.9137 0.8306 0.1101  0.0281  -0.0358 304 ARG B C   
3431  O O   . ARG B 3   ? 0.8579 0.9044 0.8227 0.1060  0.0244  -0.0331 304 ARG B O   
3432  C CB  . ARG B 3   ? 0.9129 0.9060 0.8417 0.1230  0.0268  -0.0408 304 ARG B CB  
3433  C CG  . ARG B 3   ? 0.9636 0.9445 0.8854 0.1122  0.0252  -0.0434 304 ARG B CG  
3434  C CD  . ARG B 3   ? 1.0237 0.9750 0.9297 0.1126  0.0224  -0.0471 304 ARG B CD  
3435  N NE  . ARG B 3   ? 1.0528 0.9926 0.9593 0.1115  0.0177  -0.0458 304 ARG B NE  
3436  C CZ  . ARG B 3   ? 1.0215 0.9554 0.9309 0.1006  0.0125  -0.0451 304 ARG B CZ  
3437  N NH1 . ARG B 3   ? 0.9029 0.8410 0.8147 0.0906  0.0110  -0.0456 304 ARG B NH1 
3438  N NH2 . ARG B 3   ? 0.9981 0.9217 0.9072 0.1002  0.0090  -0.0437 304 ARG B NH2 
3439  N N   . PHE B 4   ? 0.7701 0.8088 0.7222 0.1030  0.0304  -0.0370 305 PHE B N   
3440  C CA  . PHE B 4   ? 0.6935 0.7431 0.6541 0.0902  0.0290  -0.0350 305 PHE B CA  
3441  C C   . PHE B 4   ? 0.6246 0.6552 0.5741 0.0827  0.0271  -0.0372 305 PHE B C   
3442  O O   . PHE B 4   ? 0.5003 0.5158 0.4370 0.0874  0.0286  -0.0403 305 PHE B O   
3443  C CB  . PHE B 4   ? 0.8293 0.9047 0.7992 0.0891  0.0349  -0.0333 305 PHE B CB  
3444  C CG  . PHE B 4   ? 0.9801 1.0782 0.9617 0.0973  0.0370  -0.0314 305 PHE B CG  
3445  C CD1 . PHE B 4   ? 1.0893 1.1878 1.0666 0.1116  0.0406  -0.0327 305 PHE B CD1 
3446  C CD2 . PHE B 4   ? 0.9862 1.1061 0.9829 0.0910  0.0355  -0.0285 305 PHE B CD2 
3447  C CE1 . PHE B 4   ? 1.1049 1.2259 1.0933 0.1202  0.0424  -0.0308 305 PHE B CE1 
3448  C CE2 . PHE B 4   ? 0.9711 1.1143 0.9793 0.0986  0.0370  -0.0269 305 PHE B CE2 
3449  C CZ  . PHE B 4   ? 1.0425 1.1869 1.0468 0.1135  0.0403  -0.0278 305 PHE B CZ  
3450  N N   . LEU B 5   ? 0.4694 0.5005 0.4234 0.0716  0.0236  -0.0357 306 LEU B N   
3451  C CA  . LEU B 5   ? 0.4176 0.4350 0.3626 0.0645  0.0221  -0.0371 306 LEU B CA  
3452  C C   . LEU B 5   ? 0.4373 0.4680 0.3888 0.0554  0.0238  -0.0346 306 LEU B C   
3453  O O   . LEU B 5   ? 0.4618 0.5050 0.4247 0.0507  0.0224  -0.0321 306 LEU B O   
3454  C CB  . LEU B 5   ? 0.3810 0.3808 0.3221 0.0603  0.0154  -0.0382 306 LEU B CB  
3455  C CG  . LEU B 5   ? 0.4649 0.4469 0.3963 0.0674  0.0138  -0.0412 306 LEU B CG  
3456  C CD1 . LEU B 5   ? 0.4820 0.4499 0.4119 0.0618  0.0076  -0.0418 306 LEU B CD1 
3457  C CD2 . LEU B 5   ? 0.4740 0.4453 0.3919 0.0709  0.0166  -0.0447 306 LEU B CD2 
3458  N N   . LYS B 6   ? 0.4680 0.4952 0.4115 0.0530  0.0268  -0.0352 307 LYS B N   
3459  C CA  . LYS B 6   ? 0.5017 0.5388 0.4490 0.0443  0.0291  -0.0326 307 LYS B CA  
3460  C C   . LYS B 6   ? 0.4213 0.4438 0.3626 0.0367  0.0244  -0.0325 307 LYS B C   
3461  O O   . LYS B 6   ? 0.4188 0.4249 0.3496 0.0387  0.0214  -0.0350 307 LYS B O   
3462  C CB  . LYS B 6   ? 0.5225 0.5667 0.4647 0.0463  0.0364  -0.0324 307 LYS B CB  
3463  C CG  . LYS B 6   ? 0.5881 0.6531 0.5397 0.0523  0.0419  -0.0316 307 LYS B CG  
3464  C CD  . LYS B 6   ? 0.7621 0.8376 0.7108 0.0514  0.0497  -0.0307 307 LYS B CD  
3465  C CE  . LYS B 6   ? 0.8090 0.9054 0.7660 0.0595  0.0555  -0.0305 307 LYS B CE  
3466  N NZ  . LYS B 6   ? 0.7627 0.8737 0.7349 0.0602  0.0524  -0.0292 307 LYS B NZ  
3467  N N   . VAL B 7   ? 0.3910 0.4196 0.3390 0.0283  0.0234  -0.0299 308 VAL B N   
3468  C CA  . VAL B 7   ? 0.3808 0.3975 0.3229 0.0215  0.0201  -0.0293 308 VAL B CA  
3469  C C   . VAL B 7   ? 0.4254 0.4488 0.3668 0.0150  0.0248  -0.0266 308 VAL B C   
3470  O O   . VAL B 7   ? 0.4886 0.5281 0.4392 0.0121  0.0285  -0.0248 308 VAL B O   
3471  C CB  . VAL B 7   ? 0.4094 0.4225 0.3577 0.0174  0.0139  -0.0289 308 VAL B CB  
3472  C CG1 . VAL B 7   ? 0.4006 0.4040 0.3473 0.0228  0.0094  -0.0314 308 VAL B CG1 
3473  C CG2 . VAL B 7   ? 0.3710 0.4001 0.3324 0.0136  0.0148  -0.0267 308 VAL B CG2 
3474  N N   . LYS B 8   ? 0.3632 0.3742 0.2934 0.0123  0.0244  -0.0263 309 LYS B N   
3475  C CA  . LYS B 8   ? 0.3514 0.3643 0.2770 0.0065  0.0293  -0.0235 309 LYS B CA  
3476  C C   . LYS B 8   ? 0.3614 0.3633 0.2833 -0.0001 0.0255  -0.0219 309 LYS B C   
3477  O O   . LYS B 8   ? 0.4048 0.3946 0.3222 0.0018  0.0198  -0.0233 309 LYS B O   
3478  C CB  . LYS B 8   ? 0.4098 0.4163 0.3220 0.0109  0.0333  -0.0242 309 LYS B CB  
3479  C CG  . LYS B 8   ? 0.4828 0.4864 0.3863 0.0052  0.0379  -0.0211 309 LYS B CG  
3480  C CD  . LYS B 8   ? 0.4798 0.4782 0.3699 0.0106  0.0419  -0.0221 309 LYS B CD  
3481  C CE  . LYS B 8   ? 0.6157 0.6138 0.4977 0.0051  0.0483  -0.0184 309 LYS B CE  
3482  N NZ  . LYS B 8   ? 0.6435 0.6359 0.5109 0.0107  0.0521  -0.0193 309 LYS B NZ  
3483  N N   . ASN B 9   ? 0.3548 0.3611 0.2786 -0.0078 0.0289  -0.0189 310 ASN B N   
3484  C CA  . ASN B 9   ? 0.4389 0.4323 0.3554 -0.0133 0.0268  -0.0170 310 ASN B CA  
3485  C C   . ASN B 9   ? 0.4535 0.4383 0.3555 -0.0136 0.0312  -0.0151 310 ASN B C   
3486  O O   . ASN B 9   ? 0.3944 0.3875 0.2959 -0.0163 0.0381  -0.0134 310 ASN B O   
3487  C CB  . ASN B 9   ? 0.4770 0.4768 0.4017 -0.0221 0.0278  -0.0150 310 ASN B CB  
3488  C CG  . ASN B 9   ? 0.4640 0.4482 0.3804 -0.0267 0.0253  -0.0133 310 ASN B CG  
3489  O OD1 . ASN B 9   ? 0.4548 0.4282 0.3586 -0.0282 0.0280  -0.0112 310 ASN B OD1 
3490  N ND2 . ASN B 9   ? 0.4184 0.4007 0.3408 -0.0283 0.0202  -0.0142 310 ASN B ND2 
3491  N N   . TRP B 10  ? 0.4106 0.3799 0.3008 -0.0106 0.0273  -0.0154 311 TRP B N   
3492  C CA  . TRP B 10  ? 0.4673 0.4276 0.3420 -0.0093 0.0309  -0.0138 311 TRP B CA  
3493  C C   . TRP B 10  ? 0.5039 0.4569 0.3714 -0.0166 0.0344  -0.0095 311 TRP B C   
3494  O O   . TRP B 10  ? 0.4836 0.4292 0.3376 -0.0166 0.0385  -0.0073 311 TRP B O   
3495  C CB  . TRP B 10  ? 0.4150 0.3629 0.2795 -0.0027 0.0250  -0.0159 311 TRP B CB  
3496  C CG  . TRP B 10  ? 0.4755 0.4285 0.3433 0.0038  0.0236  -0.0200 311 TRP B CG  
3497  C CD1 . TRP B 10  ? 0.3970 0.3537 0.2751 0.0063  0.0187  -0.0230 311 TRP B CD1 
3498  C CD2 . TRP B 10  ? 0.5395 0.4936 0.3994 0.0088  0.0276  -0.0214 311 TRP B CD2 
3499  N NE1 . TRP B 10  ? 0.4197 0.3784 0.2962 0.0125  0.0193  -0.0263 311 TRP B NE1 
3500  C CE2 . TRP B 10  ? 0.4629 0.4202 0.3282 0.0144  0.0247  -0.0256 311 TRP B CE2 
3501  C CE3 . TRP B 10  ? 0.5962 0.5479 0.4436 0.0093  0.0337  -0.0196 311 TRP B CE3 
3502  C CZ2 . TRP B 10  ? 0.5133 0.4709 0.3720 0.0206  0.0275  -0.0284 311 TRP B CZ2 
3503  C CZ3 . TRP B 10  ? 0.6284 0.5818 0.4697 0.0155  0.0365  -0.0223 311 TRP B CZ3 
3504  C CH2 . TRP B 10  ? 0.6070 0.5630 0.4538 0.0213  0.0334  -0.0268 311 TRP B CH2 
3505  N N   . GLU B 11  ? 0.4413 0.3952 0.3163 -0.0230 0.0331  -0.0084 312 GLU B N   
3506  C CA  . GLU B 11  ? 0.5434 0.4892 0.4118 -0.0310 0.0367  -0.0046 312 GLU B CA  
3507  C C   . GLU B 11  ? 0.5329 0.4930 0.4089 -0.0389 0.0441  -0.0031 312 GLU B C   
3508  O O   . GLU B 11  ? 0.4610 0.4171 0.3278 -0.0440 0.0505  0.0001  312 GLU B O   
3509  C CB  . GLU B 11  ? 0.5299 0.4680 0.4015 -0.0337 0.0312  -0.0048 312 GLU B CB  
3510  C CG  . GLU B 11  ? 0.5887 0.5118 0.4490 -0.0400 0.0335  -0.0012 312 GLU B CG  
3511  C CD  . GLU B 11  ? 0.6591 0.5789 0.5255 -0.0447 0.0301  -0.0017 312 GLU B CD  
3512  O OE1 . GLU B 11  ? 0.6203 0.5429 0.4946 -0.0403 0.0239  -0.0044 312 GLU B OE1 
3513  O OE2 . GLU B 11  ? 0.7439 0.6578 0.6063 -0.0533 0.0340  0.0007  312 GLU B OE2 
3514  N N   . THR B 12  ? 0.5001 0.4777 0.3926 -0.0400 0.0435  -0.0053 313 THR B N   
3515  C CA  . THR B 12  ? 0.5166 0.5115 0.4188 -0.0474 0.0497  -0.0042 313 THR B CA  
3516  C C   . THR B 12  ? 0.5450 0.5566 0.4524 -0.0422 0.0543  -0.0053 313 THR B C   
3517  O O   . THR B 12  ? 0.5768 0.6041 0.4908 -0.0478 0.0607  -0.0041 313 THR B O   
3518  C CB  . THR B 12  ? 0.4787 0.4845 0.3962 -0.0517 0.0461  -0.0058 313 THR B CB  
3519  O OG1 . THR B 12  ? 0.4255 0.4393 0.3523 -0.0430 0.0412  -0.0090 313 THR B OG1 
3520  C CG2 . THR B 12  ? 0.5127 0.5018 0.4249 -0.0563 0.0417  -0.0052 313 THR B CG2 
3521  N N   . GLU B 13  ? 0.4662 0.4751 0.3708 -0.0317 0.0513  -0.0078 314 GLU B N   
3522  C CA  . GLU B 13  ? 0.4951 0.5179 0.4040 -0.0247 0.0548  -0.0097 314 GLU B CA  
3523  C C   . GLU B 13  ? 0.4380 0.4822 0.3653 -0.0243 0.0547  -0.0112 314 GLU B C   
3524  O O   . GLU B 13  ? 0.4908 0.5491 0.4230 -0.0187 0.0586  -0.0124 314 GLU B O   
3525  C CB  . GLU B 13  ? 0.5134 0.5393 0.4137 -0.0264 0.0636  -0.0073 314 GLU B CB  
3526  C CG  . GLU B 13  ? 0.6932 0.7011 0.5751 -0.0204 0.0631  -0.0073 314 GLU B CG  
3527  C CD  . GLU B 13  ? 0.9121 0.9183 0.7823 -0.0239 0.0715  -0.0040 314 GLU B CD  
3528  O OE1 . GLU B 13  ? 0.9762 0.9701 0.8308 -0.0182 0.0718  -0.0041 314 GLU B OE1 
3529  O OE2 . GLU B 13  ? 0.9552 0.9722 0.8310 -0.0328 0.0778  -0.0012 314 GLU B OE2 
3530  N N   . VAL B 14  ? 0.4866 0.5332 0.4234 -0.0292 0.0501  -0.0114 315 VAL B N   
3531  C CA  . VAL B 14  ? 0.4927 0.5578 0.4457 -0.0272 0.0483  -0.0131 315 VAL B CA  
3532  C C   . VAL B 14  ? 0.4883 0.5505 0.4415 -0.0154 0.0442  -0.0160 315 VAL B C   
3533  O O   . VAL B 14  ? 0.4598 0.5046 0.4047 -0.0119 0.0391  -0.0173 315 VAL B O   
3534  C CB  . VAL B 14  ? 0.5042 0.5695 0.4648 -0.0345 0.0435  -0.0129 315 VAL B CB  
3535  C CG1 . VAL B 14  ? 0.4203 0.5013 0.3955 -0.0302 0.0399  -0.0148 315 VAL B CG1 
3536  C CG2 . VAL B 14  ? 0.5051 0.5758 0.4670 -0.0470 0.0481  -0.0105 315 VAL B CG2 
3537  N N   . VAL B 15  ? 0.4641 0.5432 0.4261 -0.0093 0.0466  -0.0172 316 VAL B N   
3538  C CA  . VAL B 15  ? 0.4521 0.5282 0.4140 0.0019  0.0434  -0.0200 316 VAL B CA  
3539  C C   . VAL B 15  ? 0.4499 0.5404 0.4264 0.0037  0.0403  -0.0205 316 VAL B C   
3540  O O   . VAL B 15  ? 0.4317 0.5430 0.4193 0.0012  0.0436  -0.0194 316 VAL B O   
3541  C CB  . VAL B 15  ? 0.4788 0.5589 0.4351 0.0101  0.0492  -0.0210 316 VAL B CB  
3542  C CG1 . VAL B 15  ? 0.4559 0.5312 0.4113 0.0214  0.0459  -0.0241 316 VAL B CG1 
3543  C CG2 . VAL B 15  ? 0.3666 0.4313 0.3068 0.0085  0.0519  -0.0205 316 VAL B CG2 
3544  N N   . LEU B 16  ? 0.4702 0.5500 0.4464 0.0077  0.0338  -0.0221 317 LEU B N   
3545  C CA  . LEU B 16  ? 0.4321 0.5219 0.4196 0.0106  0.0301  -0.0224 317 LEU B CA  
3546  C C   . LEU B 16  ? 0.4920 0.5771 0.4769 0.0224  0.0289  -0.0246 317 LEU B C   
3547  O O   . LEU B 16  ? 0.5478 0.6167 0.5212 0.0267  0.0286  -0.0263 317 LEU B O   
3548  C CB  . LEU B 16  ? 0.3490 0.4292 0.3378 0.0049  0.0237  -0.0222 317 LEU B CB  
3549  C CG  . LEU B 16  ? 0.3848 0.4637 0.3729 -0.0066 0.0244  -0.0205 317 LEU B CG  
3550  C CD1 . LEU B 16  ? 0.3206 0.3861 0.3069 -0.0100 0.0182  -0.0208 317 LEU B CD1 
3551  C CD2 . LEU B 16  ? 0.3606 0.4614 0.3603 -0.0125 0.0275  -0.0192 317 LEU B CD2 
3552  N N   . THR B 17  ? 0.3670 0.4657 0.3617 0.0277  0.0282  -0.0244 318 THR B N   
3553  C CA  . THR B 17  ? 0.3810 0.4767 0.3731 0.0398  0.0282  -0.0261 318 THR B CA  
3554  C C   . THR B 17  ? 0.3778 0.4679 0.3732 0.0422  0.0221  -0.0261 318 THR B C   
3555  O O   . THR B 17  ? 0.3248 0.4294 0.3310 0.0405  0.0203  -0.0246 318 THR B O   
3556  C CB  . THR B 17  ? 0.4406 0.5584 0.4403 0.0463  0.0338  -0.0255 318 THR B CB  
3557  O OG1 . THR B 17  ? 0.5573 0.6820 0.5546 0.0425  0.0401  -0.0251 318 THR B OG1 
3558  C CG2 . THR B 17  ? 0.4660 0.5771 0.4601 0.0597  0.0344  -0.0274 318 THR B CG2 
3559  N N   . ASP B 18  ? 0.3693 0.4387 0.3551 0.0460  0.0188  -0.0279 319 ASP B N   
3560  C CA  . ASP B 18  ? 0.3862 0.4474 0.3735 0.0468  0.0132  -0.0278 319 ASP B CA  
3561  C C   . ASP B 18  ? 0.4225 0.4827 0.4086 0.0585  0.0136  -0.0283 319 ASP B C   
3562  O O   . ASP B 18  ? 0.4507 0.4978 0.4268 0.0650  0.0152  -0.0305 319 ASP B O   
3563  C CB  . ASP B 18  ? 0.3306 0.3703 0.3089 0.0425  0.0092  -0.0292 319 ASP B CB  
3564  C CG  . ASP B 18  ? 0.3980 0.4303 0.3783 0.0417  0.0039  -0.0287 319 ASP B CG  
3565  O OD1 . ASP B 18  ? 0.4126 0.4413 0.3920 0.0492  0.0031  -0.0289 319 ASP B OD1 
3566  O OD2 . ASP B 18  ? 0.4135 0.4428 0.3956 0.0339  0.0007  -0.0281 319 ASP B OD2 
3567  N N   . THR B 19  ? 0.4096 0.4830 0.4051 0.0614  0.0122  -0.0264 320 THR B N   
3568  C CA  . THR B 19  ? 0.5051 0.5748 0.4987 0.0725  0.0114  -0.0263 320 THR B CA  
3569  C C   . THR B 19  ? 0.4671 0.5244 0.4594 0.0708  0.0058  -0.0254 320 THR B C   
3570  O O   . THR B 19  ? 0.4020 0.4482 0.3887 0.0791  0.0049  -0.0254 320 THR B O   
3571  C CB  . THR B 19  ? 0.4821 0.5768 0.4865 0.0790  0.0137  -0.0244 320 THR B CB  
3572  O OG1 . THR B 19  ? 0.4303 0.5412 0.4461 0.0706  0.0110  -0.0224 320 THR B OG1 
3573  C CG2 . THR B 19  ? 0.4104 0.5181 0.4159 0.0818  0.0201  -0.0253 320 THR B CG2 
3574  N N   . LEU B 20  ? 0.3748 0.4331 0.3715 0.0605  0.0025  -0.0245 321 LEU B N   
3575  C CA  . LEU B 20  ? 0.3133 0.3632 0.3099 0.0587  -0.0023 -0.0233 321 LEU B CA  
3576  C C   . LEU B 20  ? 0.3703 0.3954 0.3557 0.0598  -0.0040 -0.0250 321 LEU B C   
3577  O O   . LEU B 20  ? 0.3384 0.3543 0.3214 0.0618  -0.0068 -0.0239 321 LEU B O   
3578  C CB  . LEU B 20  ? 0.3328 0.3888 0.3356 0.0475  -0.0049 -0.0224 321 LEU B CB  
3579  C CG  . LEU B 20  ? 0.3799 0.4294 0.3833 0.0443  -0.0096 -0.0211 321 LEU B CG  
3580  C CD1 . LEU B 20  ? 0.3453 0.4036 0.3527 0.0516  -0.0109 -0.0189 321 LEU B CD1 
3581  C CD2 . LEU B 20  ? 0.3716 0.4266 0.3798 0.0336  -0.0113 -0.0209 321 LEU B CD2 
3582  N N   . HIS B 21  ? 0.3242 0.3383 0.3019 0.0582  -0.0024 -0.0276 322 HIS B N   
3583  C CA  . HIS B 21  ? 0.3209 0.3126 0.2881 0.0580  -0.0043 -0.0297 322 HIS B CA  
3584  C C   . HIS B 21  ? 0.4175 0.3981 0.3780 0.0677  -0.0038 -0.0299 322 HIS B C   
3585  O O   . HIS B 21  ? 0.4045 0.3664 0.3572 0.0667  -0.0060 -0.0310 322 HIS B O   
3586  C CB  . HIS B 21  ? 0.3913 0.3752 0.3509 0.0559  -0.0026 -0.0327 322 HIS B CB  
3587  C CG  . HIS B 21  ? 0.4226 0.4087 0.3775 0.0643  0.0020  -0.0341 322 HIS B CG  
3588  N ND1 . HIS B 21  ? 0.4871 0.4916 0.4482 0.0656  0.0061  -0.0331 322 HIS B ND1 
3589  C CD2 . HIS B 21  ? 0.4707 0.4428 0.4151 0.0720  0.0036  -0.0366 322 HIS B CD2 
3590  C CE1 . HIS B 21  ? 0.4645 0.4673 0.4194 0.0742  0.0101  -0.0348 322 HIS B CE1 
3591  N NE2 . HIS B 21  ? 0.4895 0.4720 0.4337 0.0785  0.0087  -0.0371 322 HIS B NE2 
3592  N N   . LEU B 22  ? 0.4316 0.4230 0.3945 0.0771  -0.0007 -0.0288 323 LEU B N   
3593  C CA  . LEU B 22  ? 0.4844 0.4646 0.4401 0.0879  0.0000  -0.0286 323 LEU B CA  
3594  C C   . LEU B 22  ? 0.4888 0.4645 0.4460 0.0878  -0.0035 -0.0257 323 LEU B C   
3595  O O   . LEU B 22  ? 0.5149 0.4738 0.4630 0.0942  -0.0037 -0.0255 323 LEU B O   
3596  C CB  . LEU B 22  ? 0.4608 0.4569 0.4200 0.0989  0.0042  -0.0279 323 LEU B CB  
3597  C CG  . LEU B 22  ? 0.5679 0.5703 0.5257 0.0994  0.0086  -0.0304 323 LEU B CG  
3598  C CD1 . LEU B 22  ? 0.5761 0.6010 0.5413 0.1087  0.0128  -0.0291 323 LEU B CD1 
3599  C CD2 . LEU B 22  ? 0.6045 0.5825 0.5467 0.1025  0.0098  -0.0343 323 LEU B CD2 
3600  N N   . LYS B 23  ? 0.4305 0.4195 0.3976 0.0806  -0.0062 -0.0235 324 LYS B N   
3601  C CA  . LYS B 23  ? 0.4918 0.4769 0.4598 0.0795  -0.0095 -0.0207 324 LYS B CA  
3602  C C   . LYS B 23  ? 0.5872 0.5541 0.5497 0.0708  -0.0121 -0.0217 324 LYS B C   
3603  O O   . LYS B 23  ? 0.6425 0.6053 0.6053 0.0687  -0.0146 -0.0194 324 LYS B O   
3604  C CB  . LYS B 23  ? 0.4233 0.4309 0.4038 0.0758  -0.0113 -0.0182 324 LYS B CB  
3605  C CG  . LYS B 23  ? 0.6191 0.6432 0.6049 0.0858  -0.0106 -0.0157 324 LYS B CG  
3606  C CD  . LYS B 23  ? 0.7463 0.7846 0.7356 0.0912  -0.0065 -0.0171 324 LYS B CD  
3607  C CE  . LYS B 23  ? 0.8482 0.8906 0.8357 0.1058  -0.0049 -0.0155 324 LYS B CE  
3608  N NZ  . LYS B 23  ? 0.7917 0.8393 0.7820 0.1092  -0.0085 -0.0119 324 LYS B NZ  
3609  N N   . SER B 24  ? 0.4780 0.4350 0.4356 0.0657  -0.0117 -0.0250 325 SER B N   
3610  C CA  . SER B 24  ? 0.5407 0.4851 0.4955 0.0568  -0.0145 -0.0259 325 SER B CA  
3611  C C   . SER B 24  ? 0.5964 0.5190 0.5405 0.0595  -0.0149 -0.0261 325 SER B C   
3612  O O   . SER B 24  ? 0.6402 0.5537 0.5766 0.0683  -0.0127 -0.0266 325 SER B O   
3613  C CB  . SER B 24  ? 0.4760 0.4186 0.4295 0.0500  -0.0147 -0.0292 325 SER B CB  
3614  O OG  . SER B 24  ? 0.6976 0.6303 0.6422 0.0549  -0.0124 -0.0322 325 SER B OG  
3615  N N   . THR B 25  ? 0.7624 0.6767 0.7059 0.0519  -0.0174 -0.0257 326 THR B N   
3616  C CA  . THR B 25  ? 0.9804 0.8769 0.9158 0.0530  -0.0178 -0.0243 326 THR B CA  
3617  C C   . THR B 25  ? 0.9700 0.8503 0.8992 0.0446  -0.0192 -0.0273 326 THR B C   
3618  O O   . THR B 25  ? 0.9922 0.8536 0.9104 0.0464  -0.0183 -0.0294 326 THR B O   
3619  C CB  . THR B 25  ? 1.0333 0.9371 0.9744 0.0516  -0.0194 -0.0200 326 THR B CB  
3620  O OG1 . THR B 25  ? 1.0493 0.9688 1.0006 0.0439  -0.0211 -0.0200 326 THR B OG1 
3621  C CG2 . THR B 25  ? 0.9843 0.8973 0.9271 0.0620  -0.0184 -0.0167 326 THR B CG2 
3622  N N   . LEU B 26  ? 0.9473 0.8357 0.8835 0.0355  -0.0214 -0.0277 327 LEU B N   
3623  C CA  . LEU B 26  ? 0.9528 0.8310 0.8863 0.0264  -0.0232 -0.0299 327 LEU B CA  
3624  C C   . LEU B 26  ? 0.8732 0.7523 0.8055 0.0234  -0.0240 -0.0343 327 LEU B C   
3625  O O   . LEU B 26  ? 0.8863 0.7748 0.8206 0.0274  -0.0229 -0.0351 327 LEU B O   
3626  C CB  . LEU B 26  ? 0.9648 0.8533 0.9071 0.0197  -0.0250 -0.0274 327 LEU B CB  
3627  C CG  . LEU B 26  ? 0.8886 0.7806 0.8326 0.0245  -0.0242 -0.0227 327 LEU B CG  
3628  C CD1 . LEU B 26  ? 0.8691 0.7765 0.8228 0.0202  -0.0256 -0.0203 327 LEU B CD1 
3629  C CD2 . LEU B 26  ? 0.8256 0.6986 0.7601 0.0251  -0.0234 -0.0211 327 LEU B CD2 
3630  N N   . GLU B 27  ? 0.8066 0.6770 0.7359 0.0157  -0.0260 -0.0370 328 GLU B N   
3631  C CA  . GLU B 27  ? 0.7023 0.5700 0.6275 0.0133  -0.0272 -0.0415 328 GLU B CA  
3632  C C   . GLU B 27  ? 0.6330 0.5168 0.5668 0.0091  -0.0291 -0.0417 328 GLU B C   
3633  O O   . GLU B 27  ? 0.6295 0.5228 0.5716 0.0049  -0.0303 -0.0394 328 GLU B O   
3634  C CB  . GLU B 27  ? 0.7718 0.6232 0.6893 0.0068  -0.0289 -0.0447 328 GLU B CB  
3635  C CG  . GLU B 27  ? 0.9968 0.8280 0.9024 0.0114  -0.0267 -0.0452 328 GLU B CG  
3636  C CD  . GLU B 27  ? 1.2249 1.0385 1.1220 0.0036  -0.0283 -0.0487 328 GLU B CD  
3637  O OE1 . GLU B 27  ? 1.3449 1.1456 1.2315 0.0048  -0.0283 -0.0532 328 GLU B OE1 
3638  O OE2 . GLU B 27  ? 1.2824 1.0953 1.1832 -0.0041 -0.0294 -0.0471 328 GLU B OE2 
3639  N N   . THR B 28  ? 0.5734 0.4594 0.5042 0.0107  -0.0291 -0.0445 329 THR B N   
3640  C CA  . THR B 28  ? 0.5051 0.4028 0.4412 0.0070  -0.0310 -0.0451 329 THR B CA  
3641  C C   . THR B 28  ? 0.4550 0.3491 0.3895 -0.0002 -0.0348 -0.0481 329 THR B C   
3642  O O   . THR B 28  ? 0.5614 0.4656 0.5016 -0.0037 -0.0369 -0.0478 329 THR B O   
3643  C CB  . THR B 28  ? 0.6057 0.5070 0.5380 0.0118  -0.0292 -0.0464 329 THR B CB  
3644  O OG1 . THR B 28  ? 0.4743 0.3627 0.3955 0.0131  -0.0294 -0.0506 329 THR B OG1 
3645  C CG2 . THR B 28  ? 0.5767 0.4849 0.5120 0.0185  -0.0254 -0.0435 329 THR B CG2 
3646  N N   . GLY B 29  ? 0.4265 0.3065 0.3532 -0.0024 -0.0356 -0.0512 330 GLY B N   
3647  C CA  . GLY B 29  ? 0.5222 0.3993 0.4462 -0.0090 -0.0394 -0.0551 330 GLY B CA  
3648  C C   . GLY B 29  ? 0.5224 0.3934 0.4365 -0.0067 -0.0401 -0.0594 330 GLY B C   
3649  O O   . GLY B 29  ? 0.5991 0.4628 0.5074 -0.0117 -0.0431 -0.0636 330 GLY B O   
3650  N N   . CYS B 30  ? 0.4333 0.3074 0.3450 0.0004  -0.0373 -0.0586 331 CYS B N   
3651  C CA  . CYS B 30  ? 0.4140 0.2816 0.3150 0.0030  -0.0375 -0.0627 331 CYS B CA  
3652  C C   . CYS B 30  ? 0.4991 0.3486 0.3887 0.0060  -0.0356 -0.0656 331 CYS B C   
3653  O O   . CYS B 30  ? 0.5559 0.3988 0.4458 0.0083  -0.0332 -0.0636 331 CYS B O   
3654  C CB  . CYS B 30  ? 0.4067 0.2838 0.3083 0.0093  -0.0345 -0.0608 331 CYS B CB  
3655  S SG  . CYS B 30  ? 0.4103 0.3057 0.3229 0.0067  -0.0358 -0.0571 331 CYS B SG  
3656  N N   . THR B 31  ? 0.4848 0.3251 0.3631 0.0061  -0.0369 -0.0706 332 THR B N   
3657  C CA  . THR B 31  ? 0.5584 0.3806 0.4234 0.0106  -0.0345 -0.0739 332 THR B CA  
3658  C C   . THR B 31  ? 0.5583 0.3827 0.4164 0.0184  -0.0315 -0.0751 332 THR B C   
3659  O O   . THR B 31  ? 0.5201 0.3590 0.3835 0.0192  -0.0315 -0.0733 332 THR B O   
3660  C CB  . THR B 31  ? 0.6099 0.4167 0.4653 0.0032  -0.0383 -0.0795 332 THR B CB  
3661  O OG1 . THR B 31  ? 0.6647 0.4727 0.5130 0.0020  -0.0412 -0.0839 332 THR B OG1 
3662  C CG2 . THR B 31  ? 0.5996 0.4111 0.4643 -0.0069 -0.0421 -0.0784 332 THR B CG2 
3663  N N   . GLU B 32  ? 0.5410 0.3498 0.3863 0.0243  -0.0287 -0.0783 333 GLU B N   
3664  C CA  . GLU B 32  ? 0.6388 0.4491 0.4764 0.0321  -0.0253 -0.0798 333 GLU B CA  
3665  C C   . GLU B 32  ? 0.6470 0.4588 0.4781 0.0281  -0.0288 -0.0837 333 GLU B C   
3666  O O   . GLU B 32  ? 0.6037 0.4221 0.4314 0.0330  -0.0263 -0.0835 333 GLU B O   
3667  C CB  . GLU B 32  ? 0.7788 0.5707 0.6029 0.0399  -0.0215 -0.0827 333 GLU B CB  
3668  C CG  . GLU B 32  ? 1.0103 0.8023 0.8399 0.0465  -0.0174 -0.0784 333 GLU B CG  
3669  C CD  . GLU B 32  ? 1.2354 1.0036 1.0509 0.0515  -0.0155 -0.0814 333 GLU B CD  
3670  O OE1 . GLU B 32  ? 1.3069 1.0585 1.1154 0.0442  -0.0189 -0.0846 333 GLU B OE1 
3671  O OE2 . GLU B 32  ? 1.3223 1.0885 1.1335 0.0628  -0.0104 -0.0806 333 GLU B OE2 
3672  N N   . TYR B 33  ? 0.4819 0.2887 0.3113 0.0191  -0.0346 -0.0869 334 TYR B N   
3673  C CA  . TYR B 33  ? 0.4698 0.2780 0.2922 0.0156  -0.0388 -0.0910 334 TYR B CA  
3674  C C   . TYR B 33  ? 0.5152 0.3389 0.3491 0.0083  -0.0439 -0.0889 334 TYR B C   
3675  O O   . TYR B 33  ? 0.5222 0.3498 0.3514 0.0060  -0.0478 -0.0914 334 TYR B O   
3676  C CB  . TYR B 33  ? 0.5773 0.3659 0.3847 0.0119  -0.0417 -0.0981 334 TYR B CB  
3677  C CG  . TYR B 33  ? 0.6924 0.4648 0.4852 0.0207  -0.0365 -0.1009 334 TYR B CG  
3678  C CD1 . TYR B 33  ? 0.7728 0.5456 0.5552 0.0271  -0.0343 -0.1031 334 TYR B CD1 
3679  C CD2 . TYR B 33  ? 0.7459 0.5028 0.5349 0.0234  -0.0335 -0.1011 334 TYR B CD2 
3680  C CE1 . TYR B 33  ? 0.8922 0.6512 0.6613 0.0361  -0.0291 -0.1057 334 TYR B CE1 
3681  C CE2 . TYR B 33  ? 0.7751 0.5171 0.5503 0.0328  -0.0285 -0.1036 334 TYR B CE2 
3682  C CZ  . TYR B 33  ? 0.9147 0.6585 0.6804 0.0392  -0.0263 -0.1061 334 TYR B CZ  
3683  O OH  . TYR B 33  ? 1.0347 0.7645 0.7866 0.0494  -0.0209 -0.1087 334 TYR B OH  
3684  N N   . ILE B 34  ? 0.4358 0.2686 0.2839 0.0052  -0.0441 -0.0843 335 ILE B N   
3685  C CA  . ILE B 34  ? 0.4183 0.2660 0.2772 -0.0006 -0.0485 -0.0823 335 ILE B CA  
3686  C C   . ILE B 34  ? 0.4991 0.3600 0.3711 0.0022  -0.0452 -0.0758 335 ILE B C   
3687  O O   . ILE B 34  ? 0.5129 0.3715 0.3896 0.0041  -0.0418 -0.0731 335 ILE B O   
3688  C CB  . ILE B 34  ? 0.5272 0.3722 0.3899 -0.0100 -0.0533 -0.0846 335 ILE B CB  
3689  C CG1 . ILE B 34  ? 0.5931 0.4234 0.4422 -0.0138 -0.0564 -0.0916 335 ILE B CG1 
3690  C CG2 . ILE B 34  ? 0.5467 0.4083 0.4194 -0.0148 -0.0580 -0.0832 335 ILE B CG2 
3691  C CD1 . ILE B 34  ? 0.7708 0.5848 0.6161 -0.0182 -0.0557 -0.0937 335 ILE B CD1 
3692  N N   . CYS B 35  ? 0.4239 0.2978 0.3007 0.0027  -0.0463 -0.0732 336 CYS B N   
3693  C CA  . CYS B 35  ? 0.3593 0.2453 0.2481 0.0038  -0.0440 -0.0676 336 CYS B CA  
3694  C C   . CYS B 35  ? 0.4243 0.3190 0.3228 -0.0023 -0.0484 -0.0665 336 CYS B C   
3695  O O   . CYS B 35  ? 0.4406 0.3392 0.3373 -0.0050 -0.0529 -0.0685 336 CYS B O   
3696  C CB  . CYS B 35  ? 0.3686 0.2618 0.2556 0.0084  -0.0412 -0.0650 336 CYS B CB  
3697  S SG  . CYS B 35  ? 0.4250 0.3315 0.3258 0.0087  -0.0384 -0.0586 336 CYS B SG  
3698  N N   . MET B 36  ? 0.4079 0.3066 0.3166 -0.0040 -0.0470 -0.0632 337 MET B N   
3699  C CA  . MET B 36  ? 0.4090 0.3166 0.3277 -0.0092 -0.0502 -0.0617 337 MET B CA  
3700  C C   . MET B 36  ? 0.4085 0.3267 0.3359 -0.0070 -0.0479 -0.0568 337 MET B C   
3701  O O   . MET B 36  ? 0.3565 0.2810 0.2930 -0.0099 -0.0486 -0.0546 337 MET B O   
3702  C CB  . MET B 36  ? 0.5088 0.4107 0.4307 -0.0141 -0.0507 -0.0625 337 MET B CB  
3703  C CG  . MET B 36  ? 0.5959 0.4852 0.5080 -0.0173 -0.0528 -0.0678 337 MET B CG  
3704  S SD  . MET B 36  ? 0.7128 0.5981 0.6289 -0.0268 -0.0554 -0.0695 337 MET B SD  
3705  C CE  . MET B 36  ? 0.6877 0.5783 0.6147 -0.0256 -0.0515 -0.0634 337 MET B CE  
3706  N N   . GLY B 37  ? 0.3568 0.2767 0.2808 -0.0022 -0.0451 -0.0551 338 GLY B N   
3707  C CA  . GLY B 37  ? 0.3526 0.2807 0.2832 -0.0006 -0.0425 -0.0508 338 GLY B CA  
3708  C C   . GLY B 37  ? 0.3960 0.3322 0.3323 -0.0029 -0.0454 -0.0492 338 GLY B C   
3709  O O   . GLY B 37  ? 0.4593 0.4011 0.4019 -0.0028 -0.0436 -0.0460 338 GLY B O   
3710  N N   . SER B 38  ? 0.3428 0.2801 0.2765 -0.0046 -0.0499 -0.0517 339 SER B N   
3711  C CA  . SER B 38  ? 0.3972 0.3431 0.3365 -0.0056 -0.0527 -0.0503 339 SER B CA  
3712  C C   . SER B 38  ? 0.4543 0.4047 0.4015 -0.0103 -0.0556 -0.0514 339 SER B C   
3713  O O   . SER B 38  ? 0.4123 0.3710 0.3645 -0.0109 -0.0581 -0.0507 339 SER B O   
3714  C CB  . SER B 38  ? 0.3206 0.2678 0.2527 -0.0034 -0.0560 -0.0514 339 SER B CB  
3715  O OG  . SER B 38  ? 0.3957 0.3417 0.3243 -0.0058 -0.0604 -0.0557 339 SER B OG  
3716  N N   . ILE B 39  ? 0.4030 0.3477 0.3507 -0.0135 -0.0550 -0.0532 340 ILE B N   
3717  C CA  . ILE B 39  ? 0.4090 0.3574 0.3642 -0.0189 -0.0567 -0.0537 340 ILE B CA  
3718  C C   . ILE B 39  ? 0.3111 0.2642 0.2744 -0.0186 -0.0538 -0.0497 340 ILE B C   
3719  O O   . ILE B 39  ? 0.3604 0.3094 0.3230 -0.0161 -0.0501 -0.0475 340 ILE B O   
3720  C CB  . ILE B 39  ? 0.4795 0.4174 0.4307 -0.0226 -0.0565 -0.0565 340 ILE B CB  
3721  C CG1 . ILE B 39  ? 0.4966 0.4286 0.4381 -0.0228 -0.0594 -0.0610 340 ILE B CG1 
3722  C CG2 . ILE B 39  ? 0.4338 0.3749 0.3924 -0.0291 -0.0575 -0.0566 340 ILE B CG2 
3723  C CD1 . ILE B 39  ? 0.5100 0.4514 0.4535 -0.0259 -0.0648 -0.0634 340 ILE B CD1 
3724  N N   . MET B 40  ? 0.3311 0.2939 0.3021 -0.0209 -0.0555 -0.0489 341 MET B N   
3725  C CA  . MET B 40  ? 0.3829 0.3504 0.3606 -0.0202 -0.0529 -0.0454 341 MET B CA  
3726  C C   . MET B 40  ? 0.3759 0.3382 0.3557 -0.0230 -0.0502 -0.0443 341 MET B C   
3727  O O   . MET B 40  ? 0.3975 0.3580 0.3779 -0.0206 -0.0471 -0.0416 341 MET B O   
3728  C CB  . MET B 40  ? 0.4198 0.3989 0.4045 -0.0213 -0.0552 -0.0451 341 MET B CB  
3729  C CG  . MET B 40  ? 0.6543 0.6380 0.6446 -0.0202 -0.0525 -0.0419 341 MET B CG  
3730  S SD  . MET B 40  ? 0.7768 0.7638 0.7651 -0.0142 -0.0524 -0.0401 341 MET B SD  
3731  C CE  . MET B 40  ? 0.5046 0.5003 0.4936 -0.0132 -0.0574 -0.0424 341 MET B CE  
3732  N N   . HIS B 41  ? 0.4320 0.3919 0.4126 -0.0283 -0.0515 -0.0462 342 HIS B N   
3733  C CA  . HIS B 41  ? 0.5442 0.4966 0.5247 -0.0311 -0.0490 -0.0450 342 HIS B CA  
3734  C C   . HIS B 41  ? 0.5990 0.5390 0.5716 -0.0332 -0.0497 -0.0482 342 HIS B C   
3735  O O   . HIS B 41  ? 0.5706 0.5092 0.5434 -0.0394 -0.0517 -0.0507 342 HIS B O   
3736  C CB  . HIS B 41  ? 0.6287 0.5878 0.6166 -0.0366 -0.0490 -0.0441 342 HIS B CB  
3737  C CG  . HIS B 41  ? 0.9040 0.8763 0.8993 -0.0349 -0.0492 -0.0422 342 HIS B CG  
3738  N ND1 . HIS B 41  ? 0.9894 0.9634 0.9864 -0.0311 -0.0465 -0.0389 342 HIS B ND1 
3739  C CD2 . HIS B 41  ? 0.9616 0.9461 0.9627 -0.0363 -0.0517 -0.0433 342 HIS B CD2 
3740  C CE1 . HIS B 41  ? 0.9613 0.9461 0.9637 -0.0302 -0.0471 -0.0382 342 HIS B CE1 
3741  N NE2 . HIS B 41  ? 0.9252 0.9169 0.9304 -0.0328 -0.0501 -0.0407 342 HIS B NE2 
3742  N N   . PRO B 42  ? 0.6474 0.5784 0.6128 -0.0283 -0.0480 -0.0484 343 PRO B N   
3743  C CA  . PRO B 42  ? 0.7197 0.6370 0.6759 -0.0293 -0.0482 -0.0517 343 PRO B CA  
3744  C C   . PRO B 42  ? 0.8972 0.8035 0.8514 -0.0316 -0.0458 -0.0504 343 PRO B C   
3745  O O   . PRO B 42  ? 0.9403 0.8505 0.9003 -0.0322 -0.0440 -0.0468 343 PRO B O   
3746  C CB  . PRO B 42  ? 0.6321 0.5459 0.5821 -0.0221 -0.0465 -0.0518 343 PRO B CB  
3747  C CG  . PRO B 42  ? 0.6438 0.5662 0.5999 -0.0180 -0.0441 -0.0476 343 PRO B CG  
3748  C CD  . PRO B 42  ? 0.6720 0.6057 0.6371 -0.0217 -0.0457 -0.0460 343 PRO B CD  
3749  N N   . SER B 43  ? 1.0059 0.8971 0.9504 -0.0323 -0.0456 -0.0533 344 SER B N   
3750  C CA  . SER B 43  ? 1.1118 0.9877 1.0508 -0.0353 -0.0437 -0.0530 344 SER B CA  
3751  C C   . SER B 43  ? 1.1515 1.0263 1.0918 -0.0458 -0.0463 -0.0557 344 SER B C   
3752  O O   . SER B 43  ? 1.2040 1.0659 1.1397 -0.0506 -0.0449 -0.0555 344 SER B O   
3753  C CB  . SER B 43  ? 1.1290 1.0052 1.0716 -0.0324 -0.0403 -0.0477 344 SER B CB  
3754  O OG  . SER B 43  ? 1.1149 1.0028 1.0672 -0.0378 -0.0409 -0.0455 344 SER B OG  
3755  N N   . ASP B 51  ? 1.0924 0.8686 0.9925 -0.0657 -0.0076 -0.0005 352 ASP B N   
3756  C CA  . ASP B 51  ? 1.1247 0.9283 1.0398 -0.0659 -0.0088 -0.0004 352 ASP B CA  
3757  C C   . ASP B 51  ? 1.1073 0.9202 1.0241 -0.0528 -0.0101 0.0022  352 ASP B C   
3758  O O   . ASP B 51  ? 1.0775 0.9101 1.0053 -0.0494 -0.0128 -0.0001 352 ASP B O   
3759  C CB  . ASP B 51  ? 1.1808 0.9893 1.0986 -0.0754 -0.0054 0.0030  352 ASP B CB  
3760  C CG  . ASP B 51  ? 1.2306 1.0673 1.1642 -0.0771 -0.0065 0.0018  352 ASP B CG  
3761  O OD1 . ASP B 51  ? 1.1373 0.9815 1.0722 -0.0766 -0.0040 0.0060  352 ASP B OD1 
3762  O OD2 . ASP B 51  ? 1.2776 1.1282 1.2210 -0.0785 -0.0098 -0.0033 352 ASP B OD2 
3763  N N   . VAL B 52  ? 1.0108 0.8093 0.9162 -0.0457 -0.0082 0.0072  353 VAL B N   
3764  C CA  . VAL B 52  ? 0.9156 0.7219 0.8214 -0.0333 -0.0096 0.0098  353 VAL B CA  
3765  C C   . VAL B 52  ? 0.8584 0.6445 0.7510 -0.0238 -0.0092 0.0115  353 VAL B C   
3766  O O   . VAL B 52  ? 0.9075 0.6703 0.7877 -0.0267 -0.0069 0.0126  353 VAL B O   
3767  C CB  . VAL B 52  ? 0.9344 0.7487 0.8406 -0.0322 -0.0079 0.0152  353 VAL B CB  
3768  C CG1 . VAL B 52  ? 0.9382 0.7722 0.8568 -0.0406 -0.0077 0.0135  353 VAL B CG1 
3769  C CG2 . VAL B 52  ? 0.8405 0.6328 0.7321 -0.0340 -0.0040 0.0207  353 VAL B CG2 
3770  N N   . ALA B 53  ? 0.7889 0.5843 0.6839 -0.0124 -0.0115 0.0117  354 ALA B N   
3771  C CA  . ALA B 53  ? 0.8056 0.5862 0.6904 -0.0017 -0.0115 0.0123  354 ALA B CA  
3772  C C   . ALA B 53  ? 0.8194 0.5785 0.6887 0.0025  -0.0088 0.0183  354 ALA B C   
3773  O O   . ALA B 53  ? 0.7952 0.5584 0.6632 0.0032  -0.0079 0.0232  354 ALA B O   
3774  C CB  . ALA B 53  ? 0.7663 0.5654 0.6586 0.0091  -0.0142 0.0118  354 ALA B CB  
3775  N N   . THR B 54  ? 0.8994 0.6342 0.7554 0.0056  -0.0073 0.0178  355 THR B N   
3776  C CA  . THR B 54  ? 0.9978 0.7092 0.8369 0.0116  -0.0046 0.0237  355 THR B CA  
3777  C C   . THR B 54  ? 0.9665 0.6863 0.8044 0.0275  -0.0063 0.0274  355 THR B C   
3778  O O   . THR B 54  ? 0.8805 0.6225 0.7302 0.0333  -0.0092 0.0248  355 THR B O   
3779  C CB  . THR B 54  ? 1.0291 0.7105 0.8532 0.0110  -0.0026 0.0217  355 THR B CB  
3780  O OG1 . THR B 54  ? 1.0278 0.7115 0.8528 0.0211  -0.0045 0.0177  355 THR B OG1 
3781  C CG2 . THR B 54  ? 1.0943 0.7700 0.9208 -0.0056 -0.0016 0.0173  355 THR B CG2 
3782  N N   . LYS B 55  ? 0.9558 0.6575 0.7788 0.0345  -0.0043 0.0336  356 LYS B N   
3783  C CA  . LYS B 55  ? 0.8795 0.5878 0.6997 0.0507  -0.0061 0.0373  356 LYS B CA  
3784  C C   . LYS B 55  ? 0.8939 0.6036 0.7153 0.0611  -0.0075 0.0334  356 LYS B C   
3785  O O   . LYS B 55  ? 0.8669 0.5991 0.6981 0.0701  -0.0103 0.0329  356 LYS B O   
3786  C CB  . LYS B 55  ? 0.8399 0.5236 0.6409 0.0572  -0.0036 0.0446  356 LYS B CB  
3787  C CG  . LYS B 55  ? 0.7469 0.4392 0.5478 0.0556  -0.0035 0.0504  356 LYS B CG  
3788  C CD  . LYS B 55  ? 0.7694 0.4349 0.5490 0.0637  -0.0010 0.0579  356 LYS B CD  
3789  C CE  . LYS B 55  ? 0.8871 0.5550 0.6634 0.0586  0.0004  0.0637  356 LYS B CE  
3790  N NZ  . LYS B 55  ? 0.9984 0.6390 0.7524 0.0667  0.0030  0.0715  356 LYS B NZ  
3791  N N   . ASP B 56  ? 0.8897 0.5753 0.7006 0.0597  -0.0054 0.0304  357 ASP B N   
3792  C CA  . ASP B 56  ? 0.9460 0.6294 0.7550 0.0707  -0.0060 0.0269  357 ASP B CA  
3793  C C   . ASP B 56  ? 0.8688 0.5794 0.6961 0.0676  -0.0086 0.0208  357 ASP B C   
3794  O O   . ASP B 56  ? 0.8619 0.5854 0.6940 0.0786  -0.0098 0.0194  357 ASP B O   
3795  C CB  . ASP B 56  ? 1.0173 0.6667 0.8095 0.0685  -0.0030 0.0246  357 ASP B CB  
3796  C CG  . ASP B 56  ? 1.1209 0.7414 0.8922 0.0785  -0.0003 0.0306  357 ASP B CG  
3797  O OD1 . ASP B 56  ? 1.1114 0.7383 0.8813 0.0855  -0.0009 0.0369  357 ASP B OD1 
3798  O OD2 . ASP B 56  ? 1.2185 0.8092 0.9738 0.0798  0.0022  0.0288  357 ASP B OD2 
3799  N N   . GLN B 57  ? 0.7460 0.4656 0.5834 0.0530  -0.0092 0.0173  358 GLN B N   
3800  C CA  . GLN B 57  ? 0.7074 0.4520 0.5611 0.0500  -0.0116 0.0122  358 GLN B CA  
3801  C C   . GLN B 57  ? 0.6720 0.4453 0.5387 0.0550  -0.0141 0.0144  358 GLN B C   
3802  O O   . GLN B 57  ? 0.5614 0.3540 0.4388 0.0583  -0.0158 0.0112  358 GLN B O   
3803  C CB  . GLN B 57  ? 0.7722 0.5193 0.6327 0.0339  -0.0119 0.0083  358 GLN B CB  
3804  C CG  . GLN B 57  ? 0.8638 0.5853 0.7130 0.0268  -0.0101 0.0050  358 GLN B CG  
3805  C CD  . GLN B 57  ? 0.9045 0.6307 0.7610 0.0107  -0.0106 0.0020  358 GLN B CD  
3806  O OE1 . GLN B 57  ? 0.9069 0.6434 0.7698 0.0040  -0.0104 0.0048  358 GLN B OE1 
3807  N NE2 . GLN B 57  ? 0.9472 0.6673 0.8030 0.0046  -0.0112 -0.0040 358 GLN B NE2 
3808  N N   . LEU B 58  ? 0.5624 0.3385 0.4277 0.0553  -0.0142 0.0197  359 LEU B N   
3809  C CA  . LEU B 58  ? 0.5861 0.3897 0.4640 0.0572  -0.0169 0.0210  359 LEU B CA  
3810  C C   . LEU B 58  ? 0.5478 0.3623 0.4264 0.0720  -0.0185 0.0228  359 LEU B C   
3811  O O   . LEU B 58  ? 0.5890 0.4282 0.4804 0.0735  -0.0208 0.0210  359 LEU B O   
3812  C CB  . LEU B 58  ? 0.5890 0.3927 0.4648 0.0520  -0.0166 0.0257  359 LEU B CB  
3813  C CG  . LEU B 58  ? 0.5417 0.3725 0.4302 0.0507  -0.0193 0.0260  359 LEU B CG  
3814  C CD1 . LEU B 58  ? 0.6562 0.5046 0.5592 0.0430  -0.0207 0.0201  359 LEU B CD1 
3815  C CD2 . LEU B 58  ? 0.6061 0.4345 0.4908 0.0449  -0.0183 0.0302  359 LEU B CD2 
3816  N N   . PHE B 59  ? 0.5850 0.3815 0.4498 0.0829  -0.0171 0.0263  360 PHE B N   
3817  C CA  . PHE B 59  ? 0.7068 0.5143 0.5719 0.0983  -0.0186 0.0285  360 PHE B CA  
3818  C C   . PHE B 59  ? 0.6527 0.4799 0.5300 0.1012  -0.0196 0.0234  360 PHE B C   
3819  O O   . PHE B 59  ? 0.6663 0.5201 0.5557 0.1041  -0.0222 0.0235  360 PHE B O   
3820  C CB  . PHE B 59  ? 0.8211 0.6025 0.6681 0.1103  -0.0163 0.0320  360 PHE B CB  
3821  C CG  . PHE B 59  ? 0.9767 0.7396 0.8099 0.1110  -0.0153 0.0384  360 PHE B CG  
3822  C CD1 . PHE B 59  ? 0.9766 0.7542 0.8117 0.1159  -0.0178 0.0433  360 PHE B CD1 
3823  C CD2 . PHE B 59  ? 1.0262 0.7558 0.8430 0.1071  -0.0118 0.0395  360 PHE B CD2 
3824  C CE1 . PHE B 59  ? 0.9425 0.7020 0.7632 0.1171  -0.0165 0.0497  360 PHE B CE1 
3825  C CE2 . PHE B 59  ? 1.0293 0.7402 0.8319 0.1075  -0.0103 0.0459  360 PHE B CE2 
3826  C CZ  . PHE B 59  ? 0.9647 0.6907 0.7692 0.1128  -0.0126 0.0511  360 PHE B CZ  
3827  N N   . PRO B 60  ? 0.6663 0.4819 0.5407 0.1003  -0.0176 0.0190  361 PRO B N   
3828  C CA  . PRO B 60  ? 0.5567 0.3911 0.4417 0.1041  -0.0181 0.0147  361 PRO B CA  
3829  C C   . PRO B 60  ? 0.5155 0.3744 0.4169 0.0937  -0.0201 0.0117  361 PRO B C   
3830  O O   . PRO B 60  ? 0.4902 0.3717 0.4023 0.0976  -0.0212 0.0103  361 PRO B O   
3831  C CB  . PRO B 60  ? 0.6389 0.4515 0.5148 0.1033  -0.0154 0.0105  361 PRO B CB  
3832  C CG  . PRO B 60  ? 0.6786 0.4694 0.5463 0.0919  -0.0145 0.0107  361 PRO B CG  
3833  C CD  . PRO B 60  ? 0.6763 0.4624 0.5383 0.0943  -0.0149 0.0171  361 PRO B CD  
3834  N N   . LEU B 61  ? 0.4838 0.3389 0.3874 0.0805  -0.0205 0.0107  362 LEU B N   
3835  C CA  . LEU B 61  ? 0.4607 0.3376 0.3785 0.0715  -0.0223 0.0082  362 LEU B CA  
3836  C C   . LEU B 61  ? 0.4812 0.3793 0.4065 0.0748  -0.0248 0.0112  362 LEU B C   
3837  O O   . LEU B 61  ? 0.4518 0.3718 0.3885 0.0743  -0.0263 0.0093  362 LEU B O   
3838  C CB  . LEU B 61  ? 0.5043 0.3728 0.4221 0.0581  -0.0221 0.0069  362 LEU B CB  
3839  C CG  . LEU B 61  ? 0.5834 0.4334 0.4951 0.0528  -0.0204 0.0031  362 LEU B CG  
3840  C CD1 . LEU B 61  ? 0.5718 0.4156 0.4840 0.0400  -0.0203 0.0026  362 LEU B CD1 
3841  C CD2 . LEU B 61  ? 0.5081 0.3690 0.4270 0.0527  -0.0208 -0.0018 362 LEU B CD2 
3842  N N   . ALA B 62  ? 0.4576 0.3489 0.3757 0.0778  -0.0252 0.0161  363 ALA B N   
3843  C CA  . ALA B 62  ? 0.4373 0.3477 0.3607 0.0817  -0.0280 0.0191  363 ALA B CA  
3844  C C   . ALA B 62  ? 0.4919 0.4183 0.4199 0.0934  -0.0291 0.0192  363 ALA B C   
3845  O O   . ALA B 62  ? 0.3969 0.3476 0.3364 0.0926  -0.0314 0.0180  363 ALA B O   
3846  C CB  . ALA B 62  ? 0.3974 0.2944 0.3094 0.0845  -0.0279 0.0247  363 ALA B CB  
3847  N N   . LYS B 63  ? 0.5460 0.4590 0.4651 0.1041  -0.0273 0.0202  364 LYS B N   
3848  C CA  . LYS B 63  ? 0.5432 0.4725 0.4667 0.1164  -0.0280 0.0205  364 LYS B CA  
3849  C C   . LYS B 63  ? 0.4896 0.4397 0.4271 0.1119  -0.0279 0.0156  364 LYS B C   
3850  O O   . LYS B 63  ? 0.5051 0.4808 0.4532 0.1148  -0.0299 0.0155  364 LYS B O   
3851  C CB  . LYS B 63  ? 0.5454 0.4543 0.4560 0.1286  -0.0253 0.0217  364 LYS B CB  
3852  C CG  . LYS B 63  ? 0.5286 0.4560 0.4441 0.1428  -0.0257 0.0221  364 LYS B CG  
3853  C CD  . LYS B 63  ? 0.6510 0.5572 0.5530 0.1558  -0.0226 0.0229  364 LYS B CD  
3854  C CE  . LYS B 63  ? 0.7829 0.7075 0.6879 0.1725  -0.0235 0.0252  364 LYS B CE  
3855  N NZ  . LYS B 63  ? 0.8011 0.7572 0.7234 0.1715  -0.0239 0.0215  364 LYS B NZ  
3856  N N   . GLU B 64  ? 0.4170 0.3568 0.3543 0.1043  -0.0257 0.0114  365 GLU B N   
3857  C CA  . GLU B 64  ? 0.4247 0.3820 0.3733 0.1007  -0.0252 0.0071  365 GLU B CA  
3858  C C   . GLU B 64  ? 0.4047 0.3839 0.3655 0.0917  -0.0279 0.0066  365 GLU B C   
3859  O O   . GLU B 64  ? 0.3557 0.3573 0.3269 0.0926  -0.0285 0.0053  365 GLU B O   
3860  C CB  . GLU B 64  ? 0.5339 0.4754 0.4789 0.0938  -0.0228 0.0029  365 GLU B CB  
3861  C CG  . GLU B 64  ? 0.8588 0.8020 0.8035 0.1009  -0.0202 0.0000  365 GLU B CG  
3862  C CD  . GLU B 64  ? 1.0884 1.0589 1.0469 0.0994  -0.0203 -0.0020 365 GLU B CD  
3863  O OE1 . GLU B 64  ? 1.1438 1.1356 1.1107 0.1020  -0.0222 0.0001  365 GLU B OE1 
3864  O OE2 . GLU B 64  ? 1.1754 1.1459 1.1357 0.0951  -0.0184 -0.0058 365 GLU B OE2 
3865  N N   . PHE B 65  ? 0.3830 0.3560 0.3423 0.0830  -0.0293 0.0075  366 PHE B N   
3866  C CA  . PHE B 65  ? 0.3847 0.3763 0.3539 0.0750  -0.0317 0.0068  366 PHE B CA  
3867  C C   . PHE B 65  ? 0.3563 0.3677 0.3301 0.0815  -0.0345 0.0094  366 PHE B C   
3868  O O   . PHE B 65  ? 0.3308 0.3638 0.3150 0.0786  -0.0359 0.0076  366 PHE B O   
3869  C CB  . PHE B 65  ? 0.3665 0.3474 0.3324 0.0656  -0.0323 0.0074  366 PHE B CB  
3870  C CG  . PHE B 65  ? 0.3813 0.3788 0.3546 0.0592  -0.0349 0.0071  366 PHE B CG  
3871  C CD1 . PHE B 65  ? 0.4000 0.4090 0.3820 0.0515  -0.0350 0.0033  366 PHE B CD1 
3872  C CD2 . PHE B 65  ? 0.3326 0.3337 0.3031 0.0610  -0.0371 0.0105  366 PHE B CD2 
3873  C CE1 . PHE B 65  ? 0.3713 0.3937 0.3589 0.0455  -0.0372 0.0027  366 PHE B CE1 
3874  C CE2 . PHE B 65  ? 0.4125 0.4282 0.3888 0.0550  -0.0395 0.0096  366 PHE B CE2 
3875  C CZ  . PHE B 65  ? 0.3906 0.4166 0.3754 0.0471  -0.0395 0.0056  366 PHE B CZ  
3876  N N   . ILE B 66  ? 0.3652 0.3695 0.3308 0.0900  -0.0355 0.0137  367 ILE B N   
3877  C CA  . ILE B 66  ? 0.3919 0.4160 0.3615 0.0966  -0.0388 0.0163  367 ILE B CA  
3878  C C   . ILE B 66  ? 0.4200 0.4632 0.3976 0.1045  -0.0386 0.0150  367 ILE B C   
3879  O O   . ILE B 66  ? 0.3884 0.4569 0.3761 0.1042  -0.0412 0.0145  367 ILE B O   
3880  C CB  . ILE B 66  ? 0.4107 0.4213 0.3680 0.1053  -0.0397 0.0217  367 ILE B CB  
3881  C CG1 . ILE B 66  ? 0.4223 0.4176 0.3729 0.0962  -0.0396 0.0230  367 ILE B CG1 
3882  C CG2 . ILE B 66  ? 0.3843 0.4166 0.3452 0.1139  -0.0436 0.0245  367 ILE B CG2 
3883  C CD1 . ILE B 66  ? 0.4543 0.4672 0.4122 0.0879  -0.0428 0.0220  367 ILE B CD1 
3884  N N   . ASP B 67  ? 0.3712 0.4033 0.3447 0.1111  -0.0352 0.0141  368 ASP B N   
3885  C CA  . ASP B 67  ? 0.3953 0.4459 0.3769 0.1182  -0.0340 0.0125  368 ASP B CA  
3886  C C   . ASP B 67  ? 0.3395 0.4092 0.3341 0.1073  -0.0339 0.0085  368 ASP B C   
3887  O O   . ASP B 67  ? 0.3428 0.4381 0.3480 0.1093  -0.0349 0.0079  368 ASP B O   
3888  C CB  . ASP B 67  ? 0.4033 0.4355 0.3766 0.1260  -0.0299 0.0116  368 ASP B CB  
3889  C CG  . ASP B 67  ? 0.4496 0.4666 0.4104 0.1400  -0.0296 0.0157  368 ASP B CG  
3890  O OD1 . ASP B 67  ? 0.4703 0.4936 0.4295 0.1454  -0.0328 0.0197  368 ASP B OD1 
3891  O OD2 . ASP B 67  ? 0.4441 0.4414 0.3954 0.1460  -0.0262 0.0149  368 ASP B OD2 
3892  N N   . GLN B 68  ? 0.3021 0.3598 0.2958 0.0956  -0.0327 0.0058  369 GLN B N   
3893  C CA  . GLN B 68  ? 0.3828 0.4566 0.3872 0.0863  -0.0322 0.0023  369 GLN B CA  
3894  C C   . GLN B 68  ? 0.3895 0.4806 0.4013 0.0787  -0.0358 0.0024  369 GLN B C   
3895  O O   . GLN B 68  ? 0.3983 0.5102 0.4202 0.0744  -0.0362 0.0005  369 GLN B O   
3896  C CB  . GLN B 68  ? 0.4899 0.5466 0.4909 0.0776  -0.0297 -0.0008 369 GLN B CB  
3897  C CG  . GLN B 68  ? 0.6426 0.6874 0.6404 0.0677  -0.0312 -0.0009 369 GLN B CG  
3898  C CD  . GLN B 68  ? 0.6776 0.7127 0.6750 0.0591  -0.0293 -0.0043 369 GLN B CD  
3899  O OE1 . GLN B 68  ? 0.5515 0.5937 0.5542 0.0500  -0.0300 -0.0061 369 GLN B OE1 
3900  N NE2 . GLN B 68  ? 0.7454 0.7635 0.7357 0.0622  -0.0269 -0.0053 369 GLN B NE2 
3901  N N   . TYR B 69  ? 0.3380 0.4209 0.3442 0.0771  -0.0385 0.0046  370 TYR B N   
3902  C CA  . TYR B 69  ? 0.3687 0.4682 0.3805 0.0713  -0.0423 0.0047  370 TYR B CA  
3903  C C   . TYR B 69  ? 0.3562 0.4809 0.3754 0.0787  -0.0447 0.0059  370 TYR B C   
3904  O O   . TYR B 69  ? 0.3874 0.5331 0.4159 0.0724  -0.0466 0.0039  370 TYR B O   
3905  C CB  . TYR B 69  ? 0.3299 0.4161 0.3331 0.0700  -0.0443 0.0073  370 TYR B CB  
3906  C CG  . TYR B 69  ? 0.4040 0.5078 0.4115 0.0662  -0.0486 0.0074  370 TYR B CG  
3907  C CD1 . TYR B 69  ? 0.4942 0.6045 0.5068 0.0543  -0.0493 0.0041  370 TYR B CD1 
3908  C CD2 . TYR B 69  ? 0.2942 0.4082 0.2999 0.0748  -0.0519 0.0107  370 TYR B CD2 
3909  C CE1 . TYR B 69  ? 0.4073 0.5327 0.4228 0.0502  -0.0533 0.0036  370 TYR B CE1 
3910  C CE2 . TYR B 69  ? 0.3743 0.5052 0.3835 0.0710  -0.0563 0.0104  370 TYR B CE2 
3911  C CZ  . TYR B 69  ? 0.4026 0.5388 0.4166 0.0582  -0.0569 0.0066  370 TYR B CZ  
3912  O OH  . TYR B 69  ? 0.4968 0.6483 0.5131 0.0537  -0.0612 0.0057  370 TYR B OH  
3913  N N   . TYR B 70  ? 0.3080 0.4311 0.3227 0.0921  -0.0447 0.0091  371 TYR B N   
3914  C CA  . TYR B 70  ? 0.3108 0.4599 0.3328 0.1002  -0.0475 0.0105  371 TYR B CA  
3915  C C   . TYR B 70  ? 0.3224 0.4910 0.3555 0.1011  -0.0450 0.0079  371 TYR B C   
3916  O O   . TYR B 70  ? 0.3918 0.5883 0.4356 0.1012  -0.0474 0.0073  371 TYR B O   
3917  C CB  . TYR B 70  ? 0.3167 0.4575 0.3294 0.1154  -0.0484 0.0151  371 TYR B CB  
3918  C CG  . TYR B 70  ? 0.3067 0.4439 0.3130 0.1144  -0.0525 0.0180  371 TYR B CG  
3919  C CD1 . TYR B 70  ? 0.3212 0.4313 0.3156 0.1107  -0.0515 0.0195  371 TYR B CD1 
3920  C CD2 . TYR B 70  ? 0.3045 0.4666 0.3170 0.1159  -0.0575 0.0188  371 TYR B CD2 
3921  C CE1 . TYR B 70  ? 0.4506 0.5575 0.4386 0.1095  -0.0547 0.0222  371 TYR B CE1 
3922  C CE2 . TYR B 70  ? 0.3736 0.5324 0.3792 0.1149  -0.0614 0.0213  371 TYR B CE2 
3923  C CZ  . TYR B 70  ? 0.4568 0.5877 0.4499 0.1119  -0.0598 0.0231  371 TYR B CZ  
3924  O OH  . TYR B 70  ? 0.4319 0.5592 0.4175 0.1109  -0.0630 0.0258  371 TYR B OH  
3925  N N   . SER B 71  ? 0.2811 0.4361 0.3118 0.1012  -0.0402 0.0061  372 SER B N   
3926  C CA  . SER B 71  ? 0.4636 0.6356 0.5042 0.0999  -0.0371 0.0034  372 SER B CA  
3927  C C   . SER B 71  ? 0.4938 0.6797 0.5436 0.0847  -0.0379 0.0003  372 SER B C   
3928  O O   . SER B 71  ? 0.5265 0.7381 0.5876 0.0827  -0.0378 -0.0010 372 SER B O   
3929  C CB  . SER B 71  ? 0.3738 0.5252 0.4075 0.1025  -0.0320 0.0020  372 SER B CB  
3930  O OG  . SER B 71  ? 0.6160 0.7841 0.6571 0.1071  -0.0286 0.0006  372 SER B OG  
3931  N N   . SER B 72  ? 0.4534 0.6227 0.4983 0.0738  -0.0386 -0.0009 373 SER B N   
3932  C CA  . SER B 72  ? 0.4523 0.6306 0.5037 0.0597  -0.0391 -0.0038 373 SER B CA  
3933  C C   . SER B 72  ? 0.4975 0.7011 0.5572 0.0565  -0.0434 -0.0039 373 SER B C   
3934  O O   . SER B 72  ? 0.5197 0.7389 0.5876 0.0469  -0.0432 -0.0064 373 SER B O   
3935  C CB  . SER B 72  ? 0.4243 0.5803 0.4679 0.0509  -0.0396 -0.0047 373 SER B CB  
3936  O OG  . SER B 72  ? 0.4295 0.5854 0.4699 0.0506  -0.0439 -0.0030 373 SER B OG  
3937  N N   . ILE B 73  ? 0.4978 0.7051 0.5547 0.0638  -0.0475 -0.0012 374 ILE B N   
3938  C CA  . ILE B 73  ? 0.4670 0.6981 0.5307 0.0612  -0.0524 -0.0013 374 ILE B CA  
3939  C C   . ILE B 73  ? 0.4623 0.7193 0.5343 0.0724  -0.0535 0.0003  374 ILE B C   
3940  O O   . ILE B 73  ? 0.4986 0.7753 0.5748 0.0743  -0.0585 0.0011  374 ILE B O   
3941  C CB  . ILE B 73  ? 0.4712 0.6917 0.5261 0.0612  -0.0568 0.0005  374 ILE B CB  
3942  C CG1 . ILE B 73  ? 0.4289 0.6383 0.4751 0.0760  -0.0573 0.0050  374 ILE B CG1 
3943  C CG2 . ILE B 73  ? 0.4168 0.6141 0.4646 0.0504  -0.0553 -0.0013 374 ILE B CG2 
3944  C CD1 . ILE B 73  ? 0.4146 0.6209 0.4533 0.0778  -0.0622 0.0076  374 ILE B CD1 
3945  N N   . LYS B 74  ? 0.5265 0.7846 0.6009 0.0801  -0.0490 0.0006  375 LYS B N   
3946  C CA  . LYS B 74  ? 0.5229 0.8067 0.6060 0.0917  -0.0491 0.0019  375 LYS B CA  
3947  C C   . LYS B 74  ? 0.4567 0.7443 0.5352 0.1050  -0.0537 0.0058  375 LYS B C   
3948  O O   . LYS B 74  ? 0.4650 0.7812 0.5523 0.1100  -0.0574 0.0066  375 LYS B O   
3949  C CB  . LYS B 74  ? 0.5838 0.9006 0.6822 0.0824  -0.0499 -0.0009 375 LYS B CB  
3950  C CG  . LYS B 74  ? 0.6135 0.9260 0.7152 0.0679  -0.0456 -0.0044 375 LYS B CG  
3951  C CD  . LYS B 74  ? 0.7262 1.0222 0.8235 0.0731  -0.0391 -0.0045 375 LYS B CD  
3952  C CE  . LYS B 74  ? 0.7369 1.0286 0.8365 0.0590  -0.0348 -0.0076 375 LYS B CE  
3953  N NZ  . LYS B 74  ? 0.7622 1.0251 0.8515 0.0609  -0.0303 -0.0078 375 LYS B NZ  
3954  N N   . ARG B 75  ? 0.4496 0.7081 0.5138 0.1105  -0.0538 0.0084  376 ARG B N   
3955  C CA  . ARG B 75  ? 0.4339 0.6899 0.4905 0.1239  -0.0574 0.0128  376 ARG B CA  
3956  C C   . ARG B 75  ? 0.3852 0.6149 0.4295 0.1369  -0.0536 0.0156  376 ARG B C   
3957  O O   . ARG B 75  ? 0.3972 0.6115 0.4298 0.1458  -0.0555 0.0195  376 ARG B O   
3958  C CB  . ARG B 75  ? 0.4677 0.7136 0.5168 0.1172  -0.0619 0.0139  376 ARG B CB  
3959  C CG  . ARG B 75  ? 0.4681 0.7392 0.5270 0.1059  -0.0667 0.0112  376 ARG B CG  
3960  C CD  . ARG B 75  ? 0.5739 0.8788 0.6425 0.1148  -0.0710 0.0124  376 ARG B CD  
3961  N NE  . ARG B 75  ? 0.5831 0.9088 0.6578 0.1043  -0.0768 0.0102  376 ARG B NE  
3962  C CZ  . ARG B 75  ? 0.5273 0.8735 0.6145 0.0912  -0.0768 0.0058  376 ARG B CZ  
3963  N NH1 . ARG B 75  ? 0.4156 0.7783 0.5066 0.0816  -0.0823 0.0035  376 ARG B NH1 
3964  N NH2 . ARG B 75  ? 0.4323 0.7818 0.5272 0.0876  -0.0713 0.0035  376 ARG B NH2 
3965  N N   . PHE B 76  ? 0.3634 0.5861 0.4088 0.1377  -0.0480 0.0135  377 PHE B N   
3966  C CA  . PHE B 76  ? 0.4060 0.6023 0.4388 0.1492  -0.0443 0.0155  377 PHE B CA  
3967  C C   . PHE B 76  ? 0.4425 0.6485 0.4730 0.1682  -0.0458 0.0194  377 PHE B C   
3968  O O   . PHE B 76  ? 0.4927 0.7300 0.5353 0.1740  -0.0470 0.0192  377 PHE B O   
3969  C CB  . PHE B 76  ? 0.3962 0.5869 0.4312 0.1470  -0.0383 0.0121  377 PHE B CB  
3970  C CG  . PHE B 76  ? 0.3733 0.5318 0.3935 0.1551  -0.0345 0.0129  377 PHE B CG  
3971  C CD1 . PHE B 76  ? 0.4462 0.5754 0.4566 0.1459  -0.0333 0.0119  377 PHE B CD1 
3972  C CD2 . PHE B 76  ? 0.4581 0.6158 0.4741 0.1720  -0.0322 0.0146  377 PHE B CD2 
3973  C CE1 . PHE B 76  ? 0.4760 0.5757 0.4726 0.1521  -0.0300 0.0123  377 PHE B CE1 
3974  C CE2 . PHE B 76  ? 0.4976 0.6239 0.4987 0.1789  -0.0286 0.0149  377 PHE B CE2 
3975  C CZ  . PHE B 76  ? 0.4714 0.5685 0.4627 0.1683  -0.0276 0.0137  377 PHE B CZ  
3976  N N   . GLY B 77  ? 0.4064 0.5858 0.4212 0.1778  -0.0458 0.0231  378 GLY B N   
3977  C CA  . GLY B 77  ? 0.4427 0.6270 0.4525 0.1969  -0.0474 0.0274  378 GLY B CA  
3978  C C   . GLY B 77  ? 0.4733 0.6794 0.4869 0.1999  -0.0541 0.0304  378 GLY B C   
3979  O O   . GLY B 77  ? 0.5535 0.7639 0.5619 0.2166  -0.0561 0.0346  378 GLY B O   
3980  N N   . SER B 78  ? 0.4754 0.6947 0.4967 0.1848  -0.0577 0.0284  379 SER B N   
3981  C CA  . SER B 78  ? 0.5117 0.7514 0.5357 0.1866  -0.0645 0.0308  379 SER B CA  
3982  C C   . SER B 78  ? 0.5609 0.7750 0.5667 0.1952  -0.0663 0.0362  379 SER B C   
3983  O O   . SER B 78  ? 0.4640 0.6434 0.4557 0.1956  -0.0624 0.0376  379 SER B O   
3984  C CB  . SER B 78  ? 0.4413 0.6943 0.4744 0.1676  -0.0674 0.0270  379 SER B CB  
3985  O OG  . SER B 78  ? 0.4176 0.6407 0.4409 0.1561  -0.0654 0.0262  379 SER B OG  
3986  N N   . LYS B 79  ? 0.5461 0.7779 0.5519 0.2019  -0.0725 0.0393  380 LYS B N   
3987  C CA  . LYS B 79  ? 0.4924 0.7013 0.4803 0.2089  -0.0746 0.0448  380 LYS B CA  
3988  C C   . LYS B 79  ? 0.4495 0.6338 0.4296 0.1929  -0.0734 0.0438  380 LYS B C   
3989  O O   . LYS B 79  ? 0.4854 0.6367 0.4493 0.1951  -0.0706 0.0470  380 LYS B O   
3990  C CB  . LYS B 79  ? 0.6076 0.8432 0.5977 0.2174  -0.0820 0.0479  380 LYS B CB  
3991  C CG  . LYS B 79  ? 0.7781 0.9954 0.7500 0.2353  -0.0835 0.0551  380 LYS B CG  
3992  C CD  . LYS B 79  ? 0.8929 1.1157 0.8580 0.2339  -0.0900 0.0582  380 LYS B CD  
3993  C CE  . LYS B 79  ? 0.9105 1.1782 0.8915 0.2340  -0.0973 0.0562  380 LYS B CE  
3994  N NZ  . LYS B 79  ? 0.9488 1.2281 0.9261 0.2518  -0.1000 0.0604  380 LYS B NZ  
3995  N N   . ALA B 80  ? 0.4002 0.5998 0.3914 0.1764  -0.0752 0.0391  381 ALA B N   
3996  C CA  . ALA B 80  ? 0.4805 0.6589 0.4654 0.1614  -0.0738 0.0377  381 ALA B CA  
3997  C C   . ALA B 80  ? 0.4981 0.6473 0.4777 0.1570  -0.0670 0.0363  381 ALA B C   
3998  O O   . ALA B 80  ? 0.5455 0.6677 0.5134 0.1519  -0.0649 0.0377  381 ALA B O   
3999  C CB  . ALA B 80  ? 0.4394 0.6398 0.4372 0.1456  -0.0766 0.0324  381 ALA B CB  
4000  N N   . HIS B 81  ? 0.4200 0.5753 0.4081 0.1584  -0.0636 0.0333  382 HIS B N   
4001  C CA  . HIS B 81  ? 0.3717 0.4999 0.3540 0.1555  -0.0576 0.0319  382 HIS B CA  
4002  C C   . HIS B 81  ? 0.3904 0.4887 0.3550 0.1671  -0.0554 0.0368  382 HIS B C   
4003  O O   . HIS B 81  ? 0.4358 0.5057 0.3899 0.1607  -0.0525 0.0371  382 HIS B O   
4004  C CB  . HIS B 81  ? 0.3826 0.5243 0.3759 0.1576  -0.0544 0.0283  382 HIS B CB  
4005  C CG  . HIS B 81  ? 0.3669 0.4826 0.3541 0.1551  -0.0486 0.0263  382 HIS B CG  
4006  N ND1 . HIS B 81  ? 0.3980 0.5191 0.3906 0.1595  -0.0449 0.0237  382 HIS B ND1 
4007  C CD2 . HIS B 81  ? 0.3639 0.4491 0.3401 0.1484  -0.0460 0.0263  382 HIS B CD2 
4008  C CE1 . HIS B 81  ? 0.3680 0.4622 0.3524 0.1558  -0.0406 0.0221  382 HIS B CE1 
4009  N NE2 . HIS B 81  ? 0.4287 0.5014 0.4037 0.1487  -0.0413 0.0236  382 HIS B NE2 
4010  N N   . MET B 82  ? 0.4280 0.5323 0.3885 0.1841  -0.0569 0.0406  383 MET B N   
4011  C CA  . MET B 82  ? 0.5124 0.5866 0.4546 0.1962  -0.0545 0.0455  383 MET B CA  
4012  C C   . MET B 82  ? 0.4763 0.5319 0.4049 0.1930  -0.0563 0.0498  383 MET B C   
4013  O O   . MET B 82  ? 0.5347 0.5572 0.4483 0.1926  -0.0527 0.0521  383 MET B O   
4014  C CB  . MET B 82  ? 0.4902 0.5770 0.4314 0.2164  -0.0558 0.0487  383 MET B CB  
4015  C CG  . MET B 82  ? 0.6262 0.7266 0.5781 0.2211  -0.0526 0.0448  383 MET B CG  
4016  S SD  . MET B 82  ? 0.7556 0.8179 0.6962 0.2191  -0.0450 0.0423  383 MET B SD  
4017  C CE  . MET B 82  ? 0.7275 0.8119 0.6875 0.2053  -0.0429 0.0349  383 MET B CE  
4018  N N   . GLU B 83  ? 0.4772 0.5531 0.4104 0.1899  -0.0616 0.0509  384 GLU B N   
4019  C CA  . GLU B 83  ? 0.4918 0.5507 0.4116 0.1866  -0.0629 0.0549  384 GLU B CA  
4020  C C   . GLU B 83  ? 0.4433 0.4836 0.3617 0.1693  -0.0595 0.0520  384 GLU B C   
4021  O O   . GLU B 83  ? 0.4998 0.5136 0.4038 0.1671  -0.0573 0.0555  384 GLU B O   
4022  C CB  . GLU B 83  ? 0.5704 0.6564 0.4952 0.1872  -0.0696 0.0561  384 GLU B CB  
4023  C CG  . GLU B 83  ? 0.7293 0.8188 0.6444 0.2056  -0.0731 0.0624  384 GLU B CG  
4024  C CD  . GLU B 83  ? 0.8285 0.9552 0.7544 0.2084  -0.0803 0.0618  384 GLU B CD  
4025  O OE1 . GLU B 83  ? 0.8816 1.0257 0.8183 0.1941  -0.0828 0.0573  384 GLU B OE1 
4026  O OE2 . GLU B 83  ? 0.8820 1.0206 0.8052 0.2251  -0.0836 0.0658  384 GLU B OE2 
4027  N N   . ARG B 84  ? 0.4213 0.4753 0.3542 0.1570  -0.0588 0.0459  385 ARG B N   
4028  C CA  . ARG B 84  ? 0.4537 0.4913 0.3861 0.1417  -0.0555 0.0430  385 ARG B CA  
4029  C C   . ARG B 84  ? 0.4676 0.4741 0.3896 0.1428  -0.0500 0.0437  385 ARG B C   
4030  O O   . ARG B 84  ? 0.4790 0.4632 0.3919 0.1354  -0.0475 0.0448  385 ARG B O   
4031  C CB  . ARG B 84  ? 0.3739 0.4319 0.3229 0.1300  -0.0559 0.0366  385 ARG B CB  
4032  C CG  . ARG B 84  ? 0.3865 0.4311 0.3361 0.1147  -0.0531 0.0333  385 ARG B CG  
4033  C CD  . ARG B 84  ? 0.3986 0.4357 0.3403 0.1090  -0.0545 0.0357  385 ARG B CD  
4034  N NE  . ARG B 84  ? 0.4090 0.4337 0.3513 0.0956  -0.0515 0.0328  385 ARG B NE  
4035  C CZ  . ARG B 84  ? 0.4517 0.4596 0.3845 0.0907  -0.0499 0.0350  385 ARG B CZ  
4036  N NH1 . ARG B 84  ? 0.4534 0.4530 0.3741 0.0975  -0.0508 0.0405  385 ARG B NH1 
4037  N NH2 . ARG B 84  ? 0.3439 0.3437 0.2792 0.0791  -0.0472 0.0319  385 ARG B NH2 
4038  N N   . LEU B 85  ? 0.4715 0.4765 0.3945 0.1519  -0.0480 0.0428  386 LEU B N   
4039  C CA  . LEU B 85  ? 0.5265 0.5008 0.4381 0.1537  -0.0431 0.0432  386 LEU B CA  
4040  C C   . LEU B 85  ? 0.6100 0.5583 0.5027 0.1606  -0.0422 0.0495  386 LEU B C   
4041  O O   . LEU B 85  ? 0.5927 0.5141 0.4751 0.1535  -0.0388 0.0501  386 LEU B O   
4042  C CB  . LEU B 85  ? 0.5582 0.5363 0.4728 0.1644  -0.0412 0.0413  386 LEU B CB  
4043  C CG  . LEU B 85  ? 0.5482 0.5393 0.4767 0.1561  -0.0396 0.0350  386 LEU B CG  
4044  C CD1 . LEU B 85  ? 0.5303 0.5261 0.4600 0.1691  -0.0376 0.0340  386 LEU B CD1 
4045  C CD2 . LEU B 85  ? 0.5200 0.4884 0.4445 0.1429  -0.0362 0.0320  386 LEU B CD2 
4046  N N   . GLU B 86  ? 0.5952 0.5515 0.4828 0.1745  -0.0453 0.0543  387 GLU B N   
4047  C CA  . GLU B 86  ? 0.6939 0.6270 0.5626 0.1818  -0.0449 0.0611  387 GLU B CA  
4048  C C   . GLU B 86  ? 0.6276 0.5504 0.4918 0.1679  -0.0444 0.0622  387 GLU B C   
4049  O O   . GLU B 86  ? 0.5833 0.4762 0.4334 0.1642  -0.0406 0.0648  387 GLU B O   
4050  C CB  . GLU B 86  ? 0.8037 0.7559 0.6713 0.1971  -0.0498 0.0655  387 GLU B CB  
4051  C CG  . GLU B 86  ? 1.0256 0.9541 0.8729 0.2122  -0.0490 0.0727  387 GLU B CG  
4052  C CD  . GLU B 86  ? 1.2057 1.1581 1.0547 0.2291  -0.0543 0.0763  387 GLU B CD  
4053  O OE1 . GLU B 86  ? 1.2592 1.2314 1.1120 0.2270  -0.0592 0.0778  387 GLU B OE1 
4054  O OE2 . GLU B 86  ? 1.2968 1.2493 1.1436 0.2445  -0.0537 0.0773  387 GLU B OE2 
4055  N N   . GLU B 87  ? 0.5887 0.5362 0.4648 0.1595  -0.0480 0.0599  388 GLU B N   
4056  C CA  . GLU B 87  ? 0.5697 0.5110 0.4421 0.1473  -0.0477 0.0608  388 GLU B CA  
4057  C C   . GLU B 87  ? 0.6068 0.5292 0.4794 0.1334  -0.0428 0.0574  388 GLU B C   
4058  O O   . GLU B 87  ? 0.5299 0.4314 0.3914 0.1276  -0.0399 0.0604  388 GLU B O   
4059  C CB  . GLU B 87  ? 0.5776 0.5497 0.4634 0.1413  -0.0525 0.0578  388 GLU B CB  
4060  C CG  . GLU B 87  ? 0.6000 0.5681 0.4826 0.1293  -0.0522 0.0581  388 GLU B CG  
4061  C CD  . GLU B 87  ? 0.7261 0.7229 0.6208 0.1232  -0.0568 0.0544  388 GLU B CD  
4062  O OE1 . GLU B 87  ? 0.6948 0.7098 0.6044 0.1193  -0.0580 0.0489  388 GLU B OE1 
4063  O OE2 . GLU B 87  ? 0.8186 0.8187 0.7070 0.1222  -0.0592 0.0569  388 GLU B OE2 
4064  N N   . VAL B 88  ? 0.4598 0.3906 0.3452 0.1277  -0.0417 0.0514  389 VAL B N   
4065  C CA  . VAL B 88  ? 0.5057 0.4209 0.3922 0.1151  -0.0377 0.0478  389 VAL B CA  
4066  C C   . VAL B 88  ? 0.6163 0.4989 0.4868 0.1180  -0.0334 0.0509  389 VAL B C   
4067  O O   . VAL B 88  ? 0.6229 0.4874 0.4870 0.1082  -0.0304 0.0516  389 VAL B O   
4068  C CB  . VAL B 88  ? 0.4946 0.4236 0.3957 0.1109  -0.0375 0.0413  389 VAL B CB  
4069  C CG1 . VAL B 88  ? 0.4168 0.3256 0.3156 0.1018  -0.0334 0.0383  389 VAL B CG1 
4070  C CG2 . VAL B 88  ? 0.4541 0.4098 0.3698 0.1027  -0.0406 0.0376  389 VAL B CG2 
4071  N N   . ASN B 89  ? 0.6337 0.5082 0.4973 0.1314  -0.0330 0.0528  390 ASN B N   
4072  C CA  . ASN B 89  ? 0.6066 0.4477 0.4532 0.1352  -0.0290 0.0556  390 ASN B CA  
4073  C C   . ASN B 89  ? 0.6065 0.4284 0.4374 0.1343  -0.0277 0.0621  390 ASN B C   
4074  O O   . ASN B 89  ? 0.6397 0.4347 0.4596 0.1273  -0.0236 0.0632  390 ASN B O   
4075  C CB  . ASN B 89  ? 0.7366 0.5748 0.5779 0.1521  -0.0292 0.0568  390 ASN B CB  
4076  C CG  . ASN B 89  ? 0.9269 0.7580 0.7715 0.1510  -0.0265 0.0514  390 ASN B CG  
4077  O OD1 . ASN B 89  ? 1.0455 0.8511 0.8763 0.1582  -0.0235 0.0525  390 ASN B OD1 
4078  N ND2 . ASN B 89  ? 0.8976 0.7493 0.7591 0.1418  -0.0274 0.0454  390 ASN B ND2 
4079  N N   . LYS B 90  ? 0.5859 0.4216 0.4152 0.1410  -0.0312 0.0665  391 LYS B N   
4080  C CA  . LYS B 90  ? 0.7527 0.5718 0.5668 0.1401  -0.0300 0.0729  391 LYS B CA  
4081  C C   . LYS B 90  ? 0.6958 0.5088 0.5121 0.1223  -0.0271 0.0712  391 LYS B C   
4082  O O   . LYS B 90  ? 0.7050 0.4919 0.5074 0.1175  -0.0229 0.0748  391 LYS B O   
4083  C CB  . LYS B 90  ? 0.8640 0.7043 0.6786 0.1481  -0.0350 0.0767  391 LYS B CB  
4084  C CG  . LYS B 90  ? 0.9975 0.8472 0.8094 0.1667  -0.0386 0.0796  391 LYS B CG  
4085  C CD  . LYS B 90  ? 1.0771 0.9500 0.8905 0.1717  -0.0441 0.0827  391 LYS B CD  
4086  C CE  . LYS B 90  ? 1.1063 1.0031 0.9264 0.1873  -0.0491 0.0829  391 LYS B CE  
4087  N NZ  . LYS B 90  ? 1.1278 1.0042 0.9350 0.2030  -0.0470 0.0866  391 LYS B NZ  
4088  N N   . GLU B 91  ? 0.5737 0.4109 0.4070 0.1126  -0.0291 0.0659  392 GLU B N   
4089  C CA  . GLU B 91  ? 0.5921 0.4267 0.4286 0.0969  -0.0265 0.0641  392 GLU B CA  
4090  C C   . GLU B 91  ? 0.6041 0.4180 0.4388 0.0880  -0.0219 0.0613  392 GLU B C   
4091  O O   . GLU B 91  ? 0.6734 0.4723 0.5019 0.0781  -0.0182 0.0629  392 GLU B O   
4092  C CB  . GLU B 91  ? 0.5472 0.4109 0.4016 0.0896  -0.0296 0.0586  392 GLU B CB  
4093  C CG  . GLU B 91  ? 0.5695 0.4563 0.4277 0.0965  -0.0346 0.0599  392 GLU B CG  
4094  C CD  . GLU B 91  ? 0.6727 0.5823 0.5450 0.0866  -0.0367 0.0549  392 GLU B CD  
4095  O OE1 . GLU B 91  ? 0.6991 0.6039 0.5749 0.0748  -0.0338 0.0522  392 GLU B OE1 
4096  O OE2 . GLU B 91  ? 0.7783 0.7104 0.6579 0.0907  -0.0414 0.0535  392 GLU B OE2 
4097  N N   . ILE B 92  ? 0.5993 0.4133 0.4398 0.0908  -0.0221 0.0569  393 ILE B N   
4098  C CA  . ILE B 92  ? 0.6217 0.4152 0.4591 0.0828  -0.0183 0.0540  393 ILE B CA  
4099  C C   . ILE B 92  ? 0.7031 0.4638 0.5202 0.0856  -0.0145 0.0594  393 ILE B C   
4100  O O   . ILE B 92  ? 0.8599 0.6027 0.6712 0.0744  -0.0107 0.0595  393 ILE B O   
4101  C CB  . ILE B 92  ? 0.5777 0.3769 0.4232 0.0869  -0.0192 0.0485  393 ILE B CB  
4102  C CG1 . ILE B 92  ? 0.5802 0.4101 0.4451 0.0823  -0.0224 0.0433  393 ILE B CG1 
4103  C CG2 . ILE B 92  ? 0.5902 0.3660 0.4302 0.0792  -0.0156 0.0454  393 ILE B CG2 
4104  C CD1 . ILE B 92  ? 0.5574 0.3957 0.4306 0.0864  -0.0232 0.0382  393 ILE B CD1 
4105  N N   . ASP B 93  ? 0.7135 0.4660 0.5190 0.1007  -0.0154 0.0642  394 ASP B N   
4106  C CA  . ASP B 93  ? 0.7994 0.5185 0.5832 0.1049  -0.0118 0.0700  394 ASP B CA  
4107  C C   . ASP B 93  ? 0.7327 0.4423 0.5081 0.0958  -0.0092 0.0750  394 ASP B C   
4108  O O   . ASP B 93  ? 0.8290 0.5120 0.5925 0.0876  -0.0046 0.0767  394 ASP B O   
4109  C CB  . ASP B 93  ? 0.9391 0.6550 0.7125 0.1244  -0.0138 0.0748  394 ASP B CB  
4110  C CG  . ASP B 93  ? 1.1557 0.8504 0.9199 0.1332  -0.0119 0.0734  394 ASP B CG  
4111  O OD1 . ASP B 93  ? 1.2337 0.9395 1.0100 0.1320  -0.0127 0.0669  394 ASP B OD1 
4112  O OD2 . ASP B 93  ? 1.2416 0.9076 0.9854 0.1416  -0.0095 0.0789  394 ASP B OD2 
4113  N N   . THR B 94  ? 0.7301 0.4612 0.5111 0.0967  -0.0120 0.0772  395 THR B N   
4114  C CA  . THR B 94  ? 0.8129 0.5357 0.5841 0.0907  -0.0095 0.0828  395 THR B CA  
4115  C C   . THR B 94  ? 0.8304 0.5624 0.6125 0.0731  -0.0073 0.0792  395 THR B C   
4116  O O   . THR B 94  ? 0.9603 0.6785 0.7329 0.0651  -0.0032 0.0832  395 THR B O   
4117  C CB  . THR B 94  ? 0.9232 0.6634 0.6926 0.1012  -0.0136 0.0872  395 THR B CB  
4118  O OG1 . THR B 94  ? 0.9158 0.6898 0.7051 0.0999  -0.0183 0.0816  395 THR B OG1 
4119  C CG2 . THR B 94  ? 0.9851 0.7150 0.7416 0.1196  -0.0156 0.0920  395 THR B CG2 
4120  N N   . THR B 95  ? 0.7612 0.5163 0.5626 0.0672  -0.0097 0.0721  396 THR B N   
4121  C CA  . THR B 95  ? 0.7114 0.4786 0.5240 0.0525  -0.0081 0.0687  396 THR B CA  
4122  C C   . THR B 95  ? 0.7290 0.4955 0.5522 0.0423  -0.0068 0.0620  396 THR B C   
4123  O O   . THR B 95  ? 0.8175 0.5929 0.6497 0.0302  -0.0053 0.0591  396 THR B O   
4124  C CB  . THR B 95  ? 0.7042 0.5022 0.5300 0.0536  -0.0124 0.0664  396 THR B CB  
4125  O OG1 . THR B 95  ? 0.6860 0.5014 0.5265 0.0559  -0.0160 0.0601  396 THR B OG1 
4126  C CG2 . THR B 95  ? 0.6550 0.4572 0.4714 0.0655  -0.0152 0.0722  396 THR B CG2 
4127  N N   . SER B 96  ? 0.7021 0.4586 0.5239 0.0475  -0.0074 0.0594  397 SER B N   
4128  C CA  . SER B 96  ? 0.7321 0.4880 0.5628 0.0397  -0.0069 0.0528  397 SER B CA  
4129  C C   . SER B 96  ? 0.6920 0.4770 0.5421 0.0370  -0.0104 0.0468  397 SER B C   
4130  O O   . SER B 96  ? 0.6221 0.4098 0.4808 0.0291  -0.0102 0.0413  397 SER B O   
4131  C CB  . SER B 96  ? 0.8690 0.6092 0.6961 0.0251  -0.0025 0.0523  397 SER B CB  
4132  O OG  . SER B 96  ? 0.9551 0.6640 0.7639 0.0269  0.0008  0.0561  397 SER B OG  
4133  N N   . THR B 97  ? 0.6811 0.4870 0.5374 0.0431  -0.0137 0.0477  398 THR B N   
4134  C CA  . THR B 97  ? 0.5645 0.3964 0.4377 0.0412  -0.0170 0.0423  398 THR B CA  
4135  C C   . THR B 97  ? 0.5402 0.3891 0.4153 0.0517  -0.0209 0.0443  398 THR B C   
4136  O O   . THR B 97  ? 0.6045 0.4451 0.4684 0.0613  -0.0213 0.0495  398 THR B O   
4137  C CB  . THR B 97  ? 0.5352 0.3775 0.4172 0.0287  -0.0159 0.0399  398 THR B CB  
4138  O OG1 . THR B 97  ? 0.5738 0.4378 0.4706 0.0271  -0.0188 0.0345  398 THR B OG1 
4139  C CG2 . THR B 97  ? 0.4517 0.2970 0.3280 0.0281  -0.0151 0.0447  398 THR B CG2 
4140  N N   . TYR B 98  ? 0.4772 0.3498 0.3660 0.0500  -0.0240 0.0402  399 TYR B N   
4141  C CA  . TYR B 98  ? 0.5155 0.4064 0.4071 0.0580  -0.0280 0.0415  399 TYR B CA  
4142  C C   . TYR B 98  ? 0.4827 0.3949 0.3869 0.0507  -0.0300 0.0373  399 TYR B C   
4143  O O   . TYR B 98  ? 0.4734 0.3868 0.3847 0.0413  -0.0284 0.0333  399 TYR B O   
4144  C CB  . TYR B 98  ? 0.5307 0.4270 0.4245 0.0691  -0.0302 0.0407  399 TYR B CB  
4145  C CG  . TYR B 98  ? 0.5256 0.4330 0.4322 0.0662  -0.0309 0.0345  399 TYR B CG  
4146  C CD1 . TYR B 98  ? 0.4489 0.3806 0.3671 0.0679  -0.0343 0.0317  399 TYR B CD1 
4147  C CD2 . TYR B 98  ? 0.3841 0.2774 0.2903 0.0617  -0.0281 0.0317  399 TYR B CD2 
4148  C CE1 . TYR B 98  ? 0.4511 0.3920 0.3798 0.0653  -0.0344 0.0266  399 TYR B CE1 
4149  C CE2 . TYR B 98  ? 0.3883 0.2913 0.3049 0.0596  -0.0286 0.0263  399 TYR B CE2 
4150  C CZ  . TYR B 98  ? 0.4214 0.3479 0.3490 0.0616  -0.0316 0.0241  399 TYR B CZ  
4151  O OH  . TYR B 98  ? 0.4522 0.3879 0.3892 0.0594  -0.0317 0.0192  399 TYR B OH  
4152  N N   . GLN B 99  ? 0.3845 0.3134 0.2907 0.0552  -0.0336 0.0382  400 GLN B N   
4153  C CA  . GLN B 99  ? 0.3655 0.3135 0.2817 0.0489  -0.0357 0.0342  400 GLN B CA  
4154  C C   . GLN B 99  ? 0.4355 0.4025 0.3617 0.0531  -0.0395 0.0310  400 GLN B C   
4155  O O   . GLN B 99  ? 0.4238 0.3960 0.3476 0.0628  -0.0420 0.0334  400 GLN B O   
4156  C CB  . GLN B 99  ? 0.4404 0.3926 0.3502 0.0486  -0.0368 0.0373  400 GLN B CB  
4157  C CG  . GLN B 99  ? 0.5167 0.4516 0.4167 0.0439  -0.0325 0.0408  400 GLN B CG  
4158  C CD  . GLN B 99  ? 0.5188 0.4521 0.4260 0.0330  -0.0294 0.0367  400 GLN B CD  
4159  O OE1 . GLN B 99  ? 0.5746 0.5220 0.4914 0.0284  -0.0309 0.0321  400 GLN B OE1 
4160  N NE2 . GLN B 99  ? 0.4949 0.4109 0.3971 0.0288  -0.0252 0.0384  400 GLN B NE2 
4161  N N   . LEU B 100 ? 0.3673 0.3447 0.3044 0.0460  -0.0398 0.0256  401 LEU B N   
4162  C CA  . LEU B 100 ? 0.3491 0.3454 0.2961 0.0479  -0.0429 0.0223  401 LEU B CA  
4163  C C   . LEU B 100 ? 0.4011 0.4140 0.3490 0.0484  -0.0469 0.0225  401 LEU B C   
4164  O O   . LEU B 100 ? 0.3460 0.3581 0.2905 0.0431  -0.0468 0.0225  401 LEU B O   
4165  C CB  . LEU B 100 ? 0.3038 0.3040 0.2603 0.0396  -0.0418 0.0170  401 LEU B CB  
4166  C CG  . LEU B 100 ? 0.3066 0.2934 0.2635 0.0387  -0.0386 0.0157  401 LEU B CG  
4167  C CD1 . LEU B 100 ? 0.2851 0.2754 0.2500 0.0304  -0.0377 0.0109  401 LEU B CD1 
4168  C CD2 . LEU B 100 ? 0.3041 0.2924 0.2614 0.0476  -0.0391 0.0164  401 LEU B CD2 
4169  N N   . LYS B 101 ? 0.3792 0.4077 0.3315 0.0546  -0.0503 0.0224  402 LYS B N   
4170  C CA  . LYS B 101 ? 0.3408 0.3886 0.2971 0.0526  -0.0545 0.0206  402 LYS B CA  
4171  C C   . LYS B 101 ? 0.3664 0.4203 0.3309 0.0418  -0.0540 0.0150  402 LYS B C   
4172  O O   . LYS B 101 ? 0.3311 0.3792 0.3004 0.0380  -0.0512 0.0126  402 LYS B O   
4173  C CB  . LYS B 101 ? 0.3284 0.3945 0.2901 0.0604  -0.0582 0.0210  402 LYS B CB  
4174  C CG  . LYS B 101 ? 0.4375 0.4981 0.3910 0.0730  -0.0589 0.0265  402 LYS B CG  
4175  C CD  . LYS B 101 ? 0.4816 0.5367 0.4234 0.0752  -0.0605 0.0307  402 LYS B CD  
4176  C CE  . LYS B 101 ? 0.6173 0.6799 0.5540 0.0883  -0.0641 0.0353  402 LYS B CE  
4177  N NZ  . LYS B 101 ? 0.7211 0.7616 0.6424 0.0950  -0.0619 0.0416  402 LYS B NZ  
4178  N N   . ASP B 102 ? 0.3405 0.4057 0.3055 0.0373  -0.0570 0.0130  403 ASP B N   
4179  C CA  . ASP B 102 ? 0.3504 0.4197 0.3211 0.0274  -0.0566 0.0078  403 ASP B CA  
4180  C C   . ASP B 102 ? 0.3227 0.4027 0.3040 0.0257  -0.0568 0.0046  403 ASP B C   
4181  O O   . ASP B 102 ? 0.3434 0.4189 0.3288 0.0194  -0.0544 0.0014  403 ASP B O   
4182  C CB  . ASP B 102 ? 0.3990 0.4782 0.3669 0.0236  -0.0601 0.0061  403 ASP B CB  
4183  C CG  . ASP B 102 ? 0.6355 0.7042 0.5923 0.0245  -0.0593 0.0090  403 ASP B CG  
4184  O OD1 . ASP B 102 ? 0.6692 0.7227 0.6211 0.0271  -0.0557 0.0124  403 ASP B OD1 
4185  O OD2 . ASP B 102 ? 0.6558 0.7311 0.6083 0.0222  -0.0621 0.0078  403 ASP B OD2 
4186  N N   . THR B 103 ? 0.2973 0.3926 0.2830 0.0312  -0.0597 0.0054  404 THR B N   
4187  C CA  . THR B 103 ? 0.3249 0.4316 0.3208 0.0302  -0.0593 0.0028  404 THR B CA  
4188  C C   . THR B 103 ? 0.3802 0.4730 0.3768 0.0319  -0.0548 0.0031  404 THR B C   
4189  O O   . THR B 103 ? 0.3254 0.4190 0.3278 0.0265  -0.0529 -0.0001 404 THR B O   
4190  C CB  . THR B 103 ? 0.3347 0.4602 0.3348 0.0381  -0.0627 0.0045  404 THR B CB  
4191  O OG1 . THR B 103 ? 0.4089 0.5255 0.4013 0.0488  -0.0626 0.0096  404 THR B OG1 
4192  C CG2 . THR B 103 ? 0.3444 0.4875 0.3459 0.0344  -0.0677 0.0029  404 THR B CG2 
4193  N N   . GLU B 104 ? 0.3718 0.4508 0.3615 0.0391  -0.0532 0.0069  405 GLU B N   
4194  C CA  . GLU B 104 ? 0.4242 0.4893 0.4134 0.0409  -0.0494 0.0070  405 GLU B CA  
4195  C C   . GLU B 104 ? 0.3537 0.4058 0.3419 0.0321  -0.0467 0.0045  405 GLU B C   
4196  O O   . GLU B 104 ? 0.3438 0.3912 0.3353 0.0298  -0.0443 0.0023  405 GLU B O   
4197  C CB  . GLU B 104 ? 0.3555 0.4072 0.3359 0.0502  -0.0484 0.0116  405 GLU B CB  
4198  C CG  . GLU B 104 ? 0.4006 0.4639 0.3807 0.0610  -0.0510 0.0145  405 GLU B CG  
4199  C CD  . GLU B 104 ? 0.4122 0.4594 0.3804 0.0696  -0.0504 0.0197  405 GLU B CD  
4200  O OE1 . GLU B 104 ? 0.3748 0.4274 0.3412 0.0806  -0.0518 0.0226  405 GLU B OE1 
4201  O OE2 . GLU B 104 ? 0.3940 0.4233 0.3546 0.0655  -0.0482 0.0210  405 GLU B OE2 
4202  N N   . LEU B 105 ? 0.3458 0.3929 0.3293 0.0277  -0.0471 0.0049  406 LEU B N   
4203  C CA  . LEU B 105 ? 0.3389 0.3765 0.3221 0.0200  -0.0448 0.0026  406 LEU B CA  
4204  C C   . LEU B 105 ? 0.3119 0.3582 0.3023 0.0137  -0.0451 -0.0018 406 LEU B C   
4205  O O   . LEU B 105 ? 0.3126 0.3521 0.3050 0.0101  -0.0428 -0.0039 406 LEU B O   
4206  C CB  . LEU B 105 ? 0.3033 0.3368 0.2804 0.0172  -0.0451 0.0038  406 LEU B CB  
4207  C CG  . LEU B 105 ? 0.3623 0.3865 0.3387 0.0104  -0.0425 0.0018  406 LEU B CG  
4208  C CD1 . LEU B 105 ? 0.3273 0.3374 0.3013 0.0116  -0.0394 0.0036  406 LEU B CD1 
4209  C CD2 . LEU B 105 ? 0.3924 0.4165 0.3633 0.0079  -0.0428 0.0023  406 LEU B CD2 
4210  N N   . ILE B 106 ? 0.2952 0.3560 0.2888 0.0119  -0.0479 -0.0033 407 ILE B N   
4211  C CA  . ILE B 106 ? 0.2594 0.3271 0.2585 0.0051  -0.0479 -0.0073 407 ILE B CA  
4212  C C   . ILE B 106 ? 0.2335 0.3037 0.2384 0.0066  -0.0461 -0.0081 407 ILE B C   
4213  O O   . ILE B 106 ? 0.2372 0.3029 0.2440 0.0019  -0.0441 -0.0105 407 ILE B O   
4214  C CB  . ILE B 106 ? 0.2657 0.3491 0.2668 0.0025  -0.0515 -0.0087 407 ILE B CB  
4215  C CG1 . ILE B 106 ? 0.3754 0.4548 0.3694 0.0001  -0.0530 -0.0087 407 ILE B CG1 
4216  C CG2 . ILE B 106 ? 0.2321 0.3224 0.2388 -0.0046 -0.0512 -0.0125 407 ILE B CG2 
4217  C CD1 . ILE B 106 ? 0.3328 0.4270 0.3267 -0.0006 -0.0573 -0.0094 407 ILE B CD1 
4218  N N   . TYR B 107 ? 0.3342 0.4123 0.3415 0.0137  -0.0468 -0.0061 408 TYR B N   
4219  C CA  . TYR B 107 ? 0.2668 0.3474 0.2787 0.0165  -0.0447 -0.0066 408 TYR B CA  
4220  C C   . TYR B 107 ? 0.3422 0.4052 0.3504 0.0166  -0.0416 -0.0067 408 TYR B C   
4221  O O   . TYR B 107 ? 0.3146 0.3760 0.3255 0.0141  -0.0395 -0.0088 408 TYR B O   
4222  C CB  . TYR B 107 ? 0.2524 0.3422 0.2656 0.0261  -0.0458 -0.0039 408 TYR B CB  
4223  C CG  . TYR B 107 ? 0.3115 0.4010 0.3275 0.0311  -0.0430 -0.0041 408 TYR B CG  
4224  C CD1 . TYR B 107 ? 0.3120 0.4180 0.3361 0.0302  -0.0425 -0.0058 408 TYR B CD1 
4225  C CD2 . TYR B 107 ? 0.3485 0.4210 0.3584 0.0366  -0.0407 -0.0026 408 TYR B CD2 
4226  C CE1 . TYR B 107 ? 0.2966 0.4025 0.3225 0.0352  -0.0395 -0.0061 408 TYR B CE1 
4227  C CE2 . TYR B 107 ? 0.2963 0.3674 0.3073 0.0414  -0.0381 -0.0032 408 TYR B CE2 
4228  C CZ  . TYR B 107 ? 0.3875 0.4757 0.4066 0.0411  -0.0374 -0.0049 408 TYR B CZ  
4229  O OH  . TYR B 107 ? 0.3953 0.4830 0.4152 0.0463  -0.0343 -0.0056 408 TYR B OH  
4230  N N   . GLY B 108 ? 0.3043 0.3541 0.3060 0.0195  -0.0412 -0.0044 409 GLY B N   
4231  C CA  . GLY B 108 ? 0.2753 0.3091 0.2735 0.0193  -0.0386 -0.0047 409 GLY B CA  
4232  C C   . GLY B 108 ? 0.3580 0.3872 0.3573 0.0114  -0.0377 -0.0075 409 GLY B C   
4233  O O   . GLY B 108 ? 0.3070 0.3306 0.3070 0.0102  -0.0359 -0.0093 409 GLY B O   
4234  N N   . ALA B 109 ? 0.2536 0.2851 0.2524 0.0066  -0.0388 -0.0081 410 ALA B N   
4235  C CA  . ALA B 109 ? 0.2542 0.2811 0.2533 0.0002  -0.0379 -0.0107 410 ALA B CA  
4236  C C   . ALA B 109 ? 0.2647 0.2974 0.2681 -0.0027 -0.0374 -0.0133 410 ALA B C   
4237  O O   . ALA B 109 ? 0.2723 0.2985 0.2755 -0.0049 -0.0359 -0.0149 410 ALA B O   
4238  C CB  . ALA B 109 ? 0.2596 0.2880 0.2564 -0.0035 -0.0390 -0.0111 410 ALA B CB  
4239  N N   . LYS B 110 ? 0.2667 0.3121 0.2736 -0.0028 -0.0386 -0.0137 411 LYS B N   
4240  C CA  . LYS B 110 ? 0.2602 0.3117 0.2709 -0.0064 -0.0377 -0.0158 411 LYS B CA  
4241  C C   . LYS B 110 ? 0.3388 0.3871 0.3506 -0.0030 -0.0354 -0.0158 411 LYS B C   
4242  O O   . LYS B 110 ? 0.2784 0.3232 0.2901 -0.0062 -0.0338 -0.0174 411 LYS B O   
4243  C CB  . LYS B 110 ? 0.2636 0.3315 0.2787 -0.0075 -0.0394 -0.0160 411 LYS B CB  
4244  C CG  . LYS B 110 ? 0.2618 0.3325 0.2751 -0.0132 -0.0416 -0.0174 411 LYS B CG  
4245  C CD  . LYS B 110 ? 0.2776 0.3658 0.2956 -0.0153 -0.0439 -0.0181 411 LYS B CD  
4246  C CE  . LYS B 110 ? 0.3319 0.4213 0.3465 -0.0213 -0.0463 -0.0199 411 LYS B CE  
4247  N NZ  . LYS B 110 ? 0.3152 0.4218 0.3343 -0.0255 -0.0488 -0.0215 411 LYS B NZ  
4248  N N   . HIS B 111 ? 0.3219 0.3699 0.3333 0.0040  -0.0353 -0.0138 412 HIS B N   
4249  C CA  . HIS B 111 ? 0.3331 0.3778 0.3446 0.0078  -0.0330 -0.0141 412 HIS B CA  
4250  C C   . HIS B 111 ? 0.2738 0.3027 0.2805 0.0067  -0.0319 -0.0150 412 HIS B C   
4251  O O   . HIS B 111 ? 0.2982 0.3237 0.3044 0.0066  -0.0302 -0.0164 412 HIS B O   
4252  C CB  . HIS B 111 ? 0.2596 0.3088 0.2714 0.0163  -0.0331 -0.0120 412 HIS B CB  
4253  C CG  . HIS B 111 ? 0.2970 0.3648 0.3153 0.0177  -0.0334 -0.0120 412 HIS B CG  
4254  N ND1 . HIS B 111 ? 0.3324 0.4133 0.3545 0.0146  -0.0359 -0.0118 412 HIS B ND1 
4255  C CD2 . HIS B 111 ? 0.2837 0.3606 0.3059 0.0208  -0.0313 -0.0126 412 HIS B CD2 
4256  C CE1 . HIS B 111 ? 0.2883 0.3863 0.3169 0.0155  -0.0356 -0.0122 412 HIS B CE1 
4257  N NE2 . HIS B 111 ? 0.2991 0.3954 0.3282 0.0195  -0.0325 -0.0125 412 HIS B NE2 
4258  N N   . ALA B 112 ? 0.3255 0.3458 0.3289 0.0055  -0.0329 -0.0142 413 ALA B N   
4259  C CA  . ALA B 112 ? 0.3544 0.3627 0.3547 0.0031  -0.0321 -0.0154 413 ALA B CA  
4260  C C   . ALA B 112 ? 0.3436 0.3532 0.3452 -0.0019 -0.0317 -0.0177 413 ALA B C   
4261  O O   . ALA B 112 ? 0.3164 0.3199 0.3163 -0.0023 -0.0309 -0.0192 413 ALA B O   
4262  C CB  . ALA B 112 ? 0.2305 0.2320 0.2281 0.0016  -0.0329 -0.0142 413 ALA B CB  
4263  N N   . TRP B 113 ? 0.3048 0.3214 0.3084 -0.0055 -0.0324 -0.0181 414 TRP B N   
4264  C CA  . TRP B 113 ? 0.3240 0.3402 0.3273 -0.0099 -0.0317 -0.0200 414 TRP B CA  
4265  C C   . TRP B 113 ? 0.2628 0.2830 0.2674 -0.0091 -0.0300 -0.0206 414 TRP B C   
4266  O O   . TRP B 113 ? 0.3396 0.3543 0.3419 -0.0100 -0.0289 -0.0217 414 TRP B O   
4267  C CB  . TRP B 113 ? 0.2486 0.2696 0.2523 -0.0143 -0.0327 -0.0205 414 TRP B CB  
4268  C CG  . TRP B 113 ? 0.2565 0.2740 0.2581 -0.0188 -0.0318 -0.0222 414 TRP B CG  
4269  C CD1 . TRP B 113 ? 0.3192 0.3297 0.3183 -0.0189 -0.0306 -0.0230 414 TRP B CD1 
4270  C CD2 . TRP B 113 ? 0.3525 0.3720 0.3529 -0.0237 -0.0322 -0.0233 414 TRP B CD2 
4271  N NE1 . TRP B 113 ? 0.3647 0.3722 0.3608 -0.0230 -0.0300 -0.0241 414 TRP B NE1 
4272  C CE2 . TRP B 113 ? 0.4067 0.4189 0.4033 -0.0263 -0.0308 -0.0245 414 TRP B CE2 
4273  C CE3 . TRP B 113 ? 0.2742 0.3003 0.2753 -0.0261 -0.0336 -0.0236 414 TRP B CE3 
4274  C CZ2 . TRP B 113 ? 0.3784 0.3881 0.3715 -0.0314 -0.0305 -0.0258 414 TRP B CZ2 
4275  C CZ3 . TRP B 113 ? 0.3288 0.3532 0.3268 -0.0317 -0.0336 -0.0253 414 TRP B CZ3 
4276  C CH2 . TRP B 113 ? 0.3361 0.3516 0.3300 -0.0343 -0.0319 -0.0264 414 TRP B CH2 
4277  N N   . ARG B 114 ? 0.2799 0.3109 0.2883 -0.0072 -0.0298 -0.0198 415 ARG B N   
4278  C CA  . ARG B 114 ? 0.2788 0.3159 0.2891 -0.0060 -0.0276 -0.0201 415 ARG B CA  
4279  C C   . ARG B 114 ? 0.3139 0.3424 0.3208 -0.0016 -0.0261 -0.0205 415 ARG B C   
4280  O O   . ARG B 114 ? 0.2721 0.3007 0.2780 -0.0018 -0.0240 -0.0214 415 ARG B O   
4281  C CB  . ARG B 114 ? 0.2928 0.3444 0.3084 -0.0030 -0.0279 -0.0190 415 ARG B CB  
4282  C CG  . ARG B 114 ? 0.2593 0.3215 0.2785 -0.0023 -0.0253 -0.0193 415 ARG B CG  
4283  C CD  . ARG B 114 ? 0.2591 0.3369 0.2842 0.0026  -0.0259 -0.0180 415 ARG B CD  
4284  N NE  . ARG B 114 ? 0.2417 0.3340 0.2721 0.0011  -0.0234 -0.0184 415 ARG B NE  
4285  C CZ  . ARG B 114 ? 0.2800 0.3899 0.3170 0.0048  -0.0235 -0.0176 415 ARG B CZ  
4286  N NH1 . ARG B 114 ? 0.2218 0.3460 0.2643 0.0026  -0.0207 -0.0181 415 ARG B NH1 
4287  N NH2 . ARG B 114 ? 0.2706 0.3846 0.3087 0.0109  -0.0262 -0.0160 415 ARG B NH2 
4288  N N   . ASN B 115 ? 0.2895 0.3097 0.2938 0.0020  -0.0272 -0.0199 416 ASN B N   
4289  C CA  . ASN B 115 ? 0.3147 0.3253 0.3147 0.0057  -0.0262 -0.0207 416 ASN B CA  
4290  C C   . ASN B 115 ? 0.3368 0.3369 0.3330 0.0023  -0.0268 -0.0223 416 ASN B C   
4291  O O   . ASN B 115 ? 0.3163 0.3080 0.3084 0.0044  -0.0265 -0.0235 416 ASN B O   
4292  C CB  . ASN B 115 ? 0.3046 0.3102 0.3027 0.0111  -0.0268 -0.0194 416 ASN B CB  
4293  C CG  . ASN B 115 ? 0.3206 0.3367 0.3218 0.0167  -0.0262 -0.0177 416 ASN B CG  
4294  O OD1 . ASN B 115 ? 0.2703 0.2976 0.2753 0.0170  -0.0248 -0.0181 416 ASN B OD1 
4295  N ND2 . ASN B 115 ? 0.2628 0.2755 0.2621 0.0212  -0.0272 -0.0158 416 ASN B ND2 
4296  N N   . ALA B 116 ? 0.2579 0.2582 0.2549 -0.0026 -0.0279 -0.0226 417 ALA B N   
4297  C CA  . ALA B 116 ? 0.2734 0.2654 0.2672 -0.0050 -0.0289 -0.0239 417 ALA B CA  
4298  C C   . ALA B 116 ? 0.3168 0.3069 0.3075 -0.0052 -0.0277 -0.0252 417 ALA B C   
4299  O O   . ALA B 116 ? 0.3078 0.3004 0.2982 -0.0080 -0.0269 -0.0252 417 ALA B O   
4300  C CB  . ALA B 116 ? 0.2230 0.2160 0.2180 -0.0088 -0.0301 -0.0237 417 ALA B CB  
4301  N N   . SER B 117 ? 0.2701 0.2545 0.2573 -0.0025 -0.0273 -0.0264 418 SER B N   
4302  C CA  A SER B 117 ? 0.2649 0.2476 0.2480 -0.0020 -0.0259 -0.0275 418 SER B CA  
4303  C CA  B SER B 117 ? 0.2742 0.2566 0.2572 -0.0020 -0.0260 -0.0275 418 SER B CA  
4304  C C   . SER B 117 ? 0.3240 0.3033 0.3045 -0.0051 -0.0271 -0.0281 418 SER B C   
4305  O O   . SER B 117 ? 0.3530 0.3318 0.3299 -0.0056 -0.0257 -0.0282 418 SER B O   
4306  C CB  A SER B 117 ? 0.3094 0.2854 0.2880 0.0016  -0.0257 -0.0291 418 SER B CB  
4307  C CB  B SER B 117 ? 0.3020 0.2771 0.2804 0.0014  -0.0260 -0.0292 418 SER B CB  
4308  O OG  A SER B 117 ? 0.2786 0.2472 0.2555 0.0004  -0.0283 -0.0303 418 SER B OG  
4309  O OG  B SER B 117 ? 0.3142 0.2903 0.2936 0.0054  -0.0248 -0.0287 418 SER B OG  
4310  N N   . ARG B 118 ? 0.2450 0.2220 0.2267 -0.0068 -0.0295 -0.0282 419 ARG B N   
4311  C CA  . ARG B 118 ? 0.2514 0.2256 0.2304 -0.0083 -0.0308 -0.0287 419 ARG B CA  
4312  C C   . ARG B 118 ? 0.3078 0.2843 0.2876 -0.0107 -0.0301 -0.0275 419 ARG B C   
4313  O O   . ARG B 118 ? 0.3396 0.3126 0.3161 -0.0111 -0.0309 -0.0277 419 ARG B O   
4314  C CB  . ARG B 118 ? 0.2917 0.2637 0.2719 -0.0087 -0.0336 -0.0297 419 ARG B CB  
4315  C CG  . ARG B 118 ? 0.3171 0.2847 0.2944 -0.0074 -0.0348 -0.0316 419 ARG B CG  
4316  C CD  . ARG B 118 ? 0.2793 0.2464 0.2590 -0.0091 -0.0373 -0.0326 419 ARG B CD  
4317  N NE  . ARG B 118 ? 0.3620 0.3245 0.3379 -0.0090 -0.0390 -0.0350 419 ARG B NE  
4318  C CZ  . ARG B 118 ? 0.3713 0.3335 0.3487 -0.0114 -0.0414 -0.0365 419 ARG B CZ  
4319  N NH1 . ARG B 118 ? 0.3930 0.3596 0.3760 -0.0136 -0.0419 -0.0355 419 ARG B NH1 
4320  N NH2 . ARG B 118 ? 0.3420 0.2999 0.3153 -0.0120 -0.0432 -0.0392 419 ARG B NH2 
4321  N N   . CYS B 119 ? 0.2534 0.2352 0.2366 -0.0121 -0.0287 -0.0265 420 CYS B N   
4322  C CA  . CYS B 119 ? 0.2291 0.2121 0.2125 -0.0152 -0.0284 -0.0259 420 CYS B CA  
4323  C C   . CYS B 119 ? 0.2330 0.2167 0.2136 -0.0175 -0.0259 -0.0254 420 CYS B C   
4324  O O   . CYS B 119 ? 0.2324 0.2227 0.2159 -0.0178 -0.0241 -0.0250 420 CYS B O   
4325  C CB  . CYS B 119 ? 0.2249 0.2135 0.2131 -0.0162 -0.0289 -0.0253 420 CYS B CB  
4326  S SG  . CYS B 119 ? 0.2968 0.2864 0.2840 -0.0206 -0.0286 -0.0252 420 CYS B SG  
4327  N N   . VAL B 120 ? 0.2379 0.2150 0.2128 -0.0190 -0.0255 -0.0253 421 VAL B N   
4328  C CA  . VAL B 120 ? 0.2990 0.2748 0.2700 -0.0224 -0.0227 -0.0246 421 VAL B CA  
4329  C C   . VAL B 120 ? 0.3298 0.3098 0.3033 -0.0275 -0.0218 -0.0245 421 VAL B C   
4330  O O   . VAL B 120 ? 0.3247 0.3060 0.2965 -0.0317 -0.0193 -0.0240 421 VAL B O   
4331  C CB  . VAL B 120 ? 0.3575 0.3224 0.3197 -0.0218 -0.0225 -0.0243 421 VAL B CB  
4332  C CG1 . VAL B 120 ? 0.3408 0.3000 0.3007 -0.0225 -0.0239 -0.0246 421 VAL B CG1 
4333  C CG2 . VAL B 120 ? 0.3568 0.3184 0.3130 -0.0248 -0.0190 -0.0231 421 VAL B CG2 
4334  N N   . GLY B 121 ? 0.3341 0.3165 0.3111 -0.0276 -0.0239 -0.0250 422 GLY B N   
4335  C CA  . GLY B 121 ? 0.2796 0.2648 0.2574 -0.0325 -0.0237 -0.0254 422 GLY B CA  
4336  C C   . GLY B 121 ? 0.3071 0.3053 0.2924 -0.0338 -0.0239 -0.0253 422 GLY B C   
4337  O O   . GLY B 121 ? 0.3649 0.3672 0.3517 -0.0374 -0.0248 -0.0259 422 GLY B O   
4338  N N   . ARG B 122 ? 0.2681 0.2733 0.2576 -0.0307 -0.0231 -0.0246 423 ARG B N   
4339  C CA  . ARG B 122 ? 0.2415 0.2592 0.2381 -0.0294 -0.0237 -0.0242 423 ARG B CA  
4340  C C   . ARG B 122 ? 0.3145 0.3434 0.3147 -0.0345 -0.0224 -0.0243 423 ARG B C   
4341  O O   . ARG B 122 ? 0.3259 0.3669 0.3323 -0.0334 -0.0236 -0.0240 423 ARG B O   
4342  C CB  . ARG B 122 ? 0.2256 0.2456 0.2243 -0.0234 -0.0231 -0.0236 423 ARG B CB  
4343  C CG  . ARG B 122 ? 0.2905 0.3038 0.2882 -0.0189 -0.0252 -0.0236 423 ARG B CG  
4344  C CD  . ARG B 122 ? 0.2242 0.2378 0.2224 -0.0136 -0.0244 -0.0234 423 ARG B CD  
4345  N NE  . ARG B 122 ? 0.2557 0.2624 0.2490 -0.0131 -0.0230 -0.0241 423 ARG B NE  
4346  C CZ  . ARG B 122 ? 0.3154 0.3212 0.3073 -0.0090 -0.0217 -0.0245 423 ARG B CZ  
4347  N NH1 . ARG B 122 ? 0.2306 0.2416 0.2258 -0.0047 -0.0214 -0.0240 423 ARG B NH1 
4348  N NH2 . ARG B 122 ? 0.2717 0.2709 0.2581 -0.0086 -0.0207 -0.0252 423 ARG B NH2 
4349  N N   . ILE B 123 ? 0.2644 0.2900 0.2609 -0.0403 -0.0201 -0.0246 424 ILE B N   
4350  C CA  . ILE B 123 ? 0.2521 0.2892 0.2525 -0.0468 -0.0190 -0.0249 424 ILE B CA  
4351  C C   . ILE B 123 ? 0.2850 0.3274 0.2880 -0.0495 -0.0222 -0.0260 424 ILE B C   
4352  O O   . ILE B 123 ? 0.2712 0.3279 0.2801 -0.0530 -0.0227 -0.0264 424 ILE B O   
4353  C CB  . ILE B 123 ? 0.3088 0.3382 0.3028 -0.0540 -0.0159 -0.0250 424 ILE B CB  
4354  C CG1 . ILE B 123 ? 0.3044 0.3482 0.3037 -0.0615 -0.0140 -0.0253 424 ILE B CG1 
4355  C CG2 . ILE B 123 ? 0.2588 0.2725 0.2443 -0.0573 -0.0171 -0.0260 424 ILE B CG2 
4356  C CD1 . ILE B 123 ? 0.3693 0.4059 0.3623 -0.0688 -0.0099 -0.0248 424 ILE B CD1 
4357  N N   . GLN B 124 ? 0.2548 0.2868 0.2534 -0.0474 -0.0245 -0.0265 425 GLN B N   
4358  C CA  . GLN B 124 ? 0.3382 0.3723 0.3370 -0.0493 -0.0274 -0.0276 425 GLN B CA  
4359  C C   . GLN B 124 ? 0.3620 0.4047 0.3662 -0.0430 -0.0299 -0.0266 425 GLN B C   
4360  O O   . GLN B 124 ? 0.3538 0.3982 0.3573 -0.0438 -0.0324 -0.0272 425 GLN B O   
4361  C CB  . GLN B 124 ? 0.3533 0.3711 0.3437 -0.0496 -0.0278 -0.0286 425 GLN B CB  
4362  C CG  . GLN B 124 ? 0.4343 0.4409 0.4170 -0.0559 -0.0257 -0.0296 425 GLN B CG  
4363  C CD  . GLN B 124 ? 0.5071 0.5168 0.4883 -0.0640 -0.0265 -0.0316 425 GLN B CD  
4364  O OE1 . GLN B 124 ? 0.5179 0.5352 0.5021 -0.0640 -0.0292 -0.0325 425 GLN B OE1 
4365  N NE2 . GLN B 124 ? 0.5708 0.5741 0.5468 -0.0712 -0.0241 -0.0323 425 GLN B NE2 
4366  N N   . TRP B 125 ? 0.2941 0.3409 0.3022 -0.0369 -0.0292 -0.0250 426 TRP B N   
4367  C CA  . TRP B 125 ? 0.2949 0.3441 0.3053 -0.0302 -0.0311 -0.0237 426 TRP B CA  
4368  C C   . TRP B 125 ? 0.3518 0.4132 0.3658 -0.0306 -0.0337 -0.0235 426 TRP B C   
4369  O O   . TRP B 125 ? 0.3430 0.4022 0.3555 -0.0276 -0.0358 -0.0228 426 TRP B O   
4370  C CB  . TRP B 125 ? 0.2693 0.3206 0.2823 -0.0239 -0.0296 -0.0224 426 TRP B CB  
4371  C CG  . TRP B 125 ? 0.2583 0.3253 0.2776 -0.0229 -0.0287 -0.0218 426 TRP B CG  
4372  C CD1 . TRP B 125 ? 0.3244 0.3974 0.3458 -0.0258 -0.0259 -0.0223 426 TRP B CD1 
4373  C CD2 . TRP B 125 ? 0.2168 0.2963 0.2411 -0.0182 -0.0305 -0.0206 426 TRP B CD2 
4374  N NE1 . TRP B 125 ? 0.2614 0.3516 0.2899 -0.0234 -0.0257 -0.0216 426 TRP B NE1 
4375  C CE2 . TRP B 125 ? 0.2692 0.3636 0.2995 -0.0182 -0.0287 -0.0205 426 TRP B CE2 
4376  C CE3 . TRP B 125 ? 0.2166 0.2963 0.2405 -0.0136 -0.0332 -0.0193 426 TRP B CE3 
4377  C CZ2 . TRP B 125 ? 0.2366 0.3469 0.2730 -0.0131 -0.0299 -0.0194 426 TRP B CZ2 
4378  C CZ3 . TRP B 125 ? 0.2977 0.3914 0.3264 -0.0086 -0.0345 -0.0179 426 TRP B CZ3 
4379  C CH2 . TRP B 125 ? 0.3175 0.4269 0.3527 -0.0080 -0.0330 -0.0180 426 TRP B CH2 
4380  N N   . SER B 126 ? 0.3005 0.3755 0.3192 -0.0345 -0.0338 -0.0241 427 SER B N   
4381  C CA  . SER B 126 ? 0.2917 0.3805 0.3143 -0.0337 -0.0368 -0.0238 427 SER B CA  
4382  C C   . SER B 126 ? 0.3656 0.4514 0.3839 -0.0393 -0.0393 -0.0256 427 SER B C   
4383  O O   . SER B 126 ? 0.3378 0.4332 0.3576 -0.0383 -0.0424 -0.0255 427 SER B O   
4384  C CB  . SER B 126 ? 0.2519 0.3594 0.2823 -0.0359 -0.0363 -0.0240 427 SER B CB  
4385  O OG  . SER B 126 ? 0.4149 0.5229 0.4443 -0.0459 -0.0353 -0.0263 427 SER B OG  
4386  N N   . LYS B 127 ? 0.3689 0.4415 0.3810 -0.0447 -0.0380 -0.0274 428 LYS B N   
4387  C CA  . LYS B 127 ? 0.4753 0.5425 0.4816 -0.0494 -0.0400 -0.0295 428 LYS B CA  
4388  C C   . LYS B 127 ? 0.6045 0.6572 0.6049 -0.0448 -0.0398 -0.0289 428 LYS B C   
4389  O O   . LYS B 127 ? 0.8346 0.8737 0.8293 -0.0463 -0.0381 -0.0299 428 LYS B O   
4390  C CB  . LYS B 127 ? 0.4901 0.5521 0.4926 -0.0587 -0.0385 -0.0321 428 LYS B CB  
4391  C CG  . LYS B 127 ? 0.6437 0.7220 0.6530 -0.0644 -0.0383 -0.0327 428 LYS B CG  
4392  C CD  . LYS B 127 ? 0.7949 0.8663 0.7994 -0.0747 -0.0364 -0.0350 428 LYS B CD  
4393  C CE  . LYS B 127 ? 0.8529 0.9410 0.8652 -0.0804 -0.0350 -0.0350 428 LYS B CE  
4394  N NZ  . LYS B 127 ? 0.8347 0.9122 0.8427 -0.0860 -0.0306 -0.0350 428 LYS B NZ  
4395  N N   . LEU B 128 ? 0.4585 0.5150 0.4606 -0.0387 -0.0413 -0.0269 429 LEU B N   
4396  C CA  . LEU B 128 ? 0.3155 0.3612 0.3134 -0.0342 -0.0409 -0.0258 429 LEU B CA  
4397  C C   . LEU B 128 ? 0.3134 0.3628 0.3085 -0.0334 -0.0435 -0.0257 429 LEU B C   
4398  O O   . LEU B 128 ? 0.3405 0.4016 0.3389 -0.0314 -0.0457 -0.0244 429 LEU B O   
4399  C CB  . LEU B 128 ? 0.2294 0.2736 0.2305 -0.0277 -0.0397 -0.0232 429 LEU B CB  
4400  C CG  . LEU B 128 ? 0.2793 0.3137 0.2769 -0.0241 -0.0392 -0.0220 429 LEU B CG  
4401  C CD1 . LEU B 128 ? 0.2471 0.2704 0.2409 -0.0263 -0.0375 -0.0237 429 LEU B CD1 
4402  C CD2 . LEU B 128 ? 0.2287 0.2621 0.2289 -0.0185 -0.0385 -0.0195 429 LEU B CD2 
4403  N N   . GLN B 129 ? 0.2751 0.3152 0.2639 -0.0346 -0.0432 -0.0269 430 GLN B N   
4404  C CA  . GLN B 129 ? 0.2997 0.3420 0.2843 -0.0337 -0.0452 -0.0268 430 GLN B CA  
4405  C C   . GLN B 129 ? 0.3177 0.3561 0.3021 -0.0274 -0.0441 -0.0236 430 GLN B C   
4406  O O   . GLN B 129 ? 0.3742 0.4034 0.3576 -0.0262 -0.0417 -0.0233 430 GLN B O   
4407  C CB  . GLN B 129 ? 0.3612 0.3952 0.3381 -0.0379 -0.0449 -0.0300 430 GLN B CB  
4408  C CG  . GLN B 129 ? 0.3713 0.4075 0.3427 -0.0371 -0.0469 -0.0302 430 GLN B CG  
4409  C CD  . GLN B 129 ? 0.5157 0.5659 0.4893 -0.0386 -0.0507 -0.0303 430 GLN B CD  
4410  O OE1 . GLN B 129 ? 0.5157 0.5725 0.4921 -0.0440 -0.0520 -0.0324 430 GLN B OE1 
4411  N NE2 . GLN B 129 ? 0.5612 0.6168 0.5336 -0.0340 -0.0524 -0.0277 430 GLN B NE2 
4412  N N   . VAL B 130 ? 0.3297 0.3753 0.3150 -0.0236 -0.0459 -0.0210 431 VAL B N   
4413  C CA  . VAL B 130 ? 0.2965 0.3377 0.2810 -0.0181 -0.0447 -0.0175 431 VAL B CA  
4414  C C   . VAL B 130 ? 0.3404 0.3802 0.3181 -0.0174 -0.0454 -0.0168 431 VAL B C   
4415  O O   . VAL B 130 ? 0.3684 0.4161 0.3439 -0.0172 -0.0483 -0.0166 431 VAL B O   
4416  C CB  . VAL B 130 ? 0.2752 0.3232 0.2639 -0.0132 -0.0457 -0.0146 431 VAL B CB  
4417  C CG1 . VAL B 130 ? 0.2948 0.3355 0.2808 -0.0080 -0.0444 -0.0109 431 VAL B CG1 
4418  C CG2 . VAL B 130 ? 0.3918 0.4414 0.3866 -0.0140 -0.0446 -0.0157 431 VAL B CG2 
4419  N N   . PHE B 131 ? 0.2971 0.3280 0.2716 -0.0172 -0.0428 -0.0164 432 PHE B N   
4420  C CA  . PHE B 131 ? 0.2737 0.3025 0.2413 -0.0161 -0.0425 -0.0152 432 PHE B CA  
4421  C C   . PHE B 131 ? 0.3342 0.3600 0.3014 -0.0117 -0.0411 -0.0106 432 PHE B C   
4422  O O   . PHE B 131 ? 0.3601 0.3797 0.3299 -0.0113 -0.0385 -0.0096 432 PHE B O   
4423  C CB  . PHE B 131 ? 0.2486 0.2706 0.2127 -0.0184 -0.0400 -0.0177 432 PHE B CB  
4424  C CG  . PHE B 131 ? 0.3138 0.3359 0.2759 -0.0225 -0.0412 -0.0221 432 PHE B CG  
4425  C CD1 . PHE B 131 ? 0.3764 0.4034 0.3337 -0.0245 -0.0441 -0.0238 432 PHE B CD1 
4426  C CD2 . PHE B 131 ? 0.3452 0.3619 0.3095 -0.0245 -0.0396 -0.0244 432 PHE B CD2 
4427  C CE1 . PHE B 131 ? 0.3491 0.3746 0.3035 -0.0294 -0.0451 -0.0282 432 PHE B CE1 
4428  C CE2 . PHE B 131 ? 0.3557 0.3700 0.3165 -0.0286 -0.0404 -0.0283 432 PHE B CE2 
4429  C CZ  . PHE B 131 ? 0.4193 0.4375 0.3752 -0.0314 -0.0430 -0.0303 432 PHE B CZ  
4430  N N   . ASP B 132 ? 0.3366 0.3667 0.3000 -0.0086 -0.0431 -0.0080 433 ASP B N   
4431  C CA  . ASP B 132 ? 0.2783 0.3037 0.2389 -0.0042 -0.0419 -0.0032 433 ASP B CA  
4432  C C   . ASP B 132 ? 0.3297 0.3487 0.2840 -0.0052 -0.0389 -0.0019 433 ASP B C   
4433  O O   . ASP B 132 ? 0.3466 0.3681 0.2943 -0.0052 -0.0399 -0.0020 433 ASP B O   
4434  C CB  . ASP B 132 ? 0.3622 0.3948 0.3202 0.0004  -0.0454 -0.0006 433 ASP B CB  
4435  C CG  . ASP B 132 ? 0.4123 0.4380 0.3660 0.0057  -0.0441 0.0047  433 ASP B CG  
4436  O OD1 . ASP B 132 ? 0.3974 0.4282 0.3494 0.0110  -0.0468 0.0072  433 ASP B OD1 
4437  O OD2 . ASP B 132 ? 0.4200 0.4352 0.3718 0.0047  -0.0403 0.0064  433 ASP B OD2 
4438  N N   . ALA B 133 ? 0.3800 0.3916 0.3361 -0.0064 -0.0353 -0.0010 434 ALA B N   
4439  C CA  . ALA B 133 ? 0.3317 0.3386 0.2830 -0.0076 -0.0318 0.0006  434 ALA B CA  
4440  C C   . ALA B 133 ? 0.3337 0.3334 0.2816 -0.0057 -0.0296 0.0057  434 ALA B C   
4441  O O   . ALA B 133 ? 0.3267 0.3216 0.2736 -0.0080 -0.0257 0.0071  434 ALA B O   
4442  C CB  . ALA B 133 ? 0.3333 0.3388 0.2894 -0.0111 -0.0291 -0.0025 434 ALA B CB  
4443  N N   . ARG B 134 ? 0.2808 0.2796 0.2267 -0.0015 -0.0318 0.0086  435 ARG B N   
4444  C CA  . ARG B 134 ? 0.3852 0.3740 0.3264 0.0004  -0.0295 0.0135  435 ARG B CA  
4445  C C   . ARG B 134 ? 0.3320 0.3173 0.2631 0.0012  -0.0276 0.0175  435 ARG B C   
4446  O O   . ARG B 134 ? 0.3803 0.3555 0.3063 0.0016  -0.0247 0.0218  435 ARG B O   
4447  C CB  . ARG B 134 ? 0.3172 0.3049 0.2583 0.0060  -0.0322 0.0154  435 ARG B CB  
4448  C CG  . ARG B 134 ? 0.3453 0.3335 0.2951 0.0052  -0.0328 0.0124  435 ARG B CG  
4449  C CD  . ARG B 134 ? 0.3181 0.3074 0.2675 0.0118  -0.0353 0.0141  435 ARG B CD  
4450  N NE  . ARG B 134 ? 0.3250 0.3271 0.2745 0.0147  -0.0393 0.0135  435 ARG B NE  
4451  C CZ  . ARG B 134 ? 0.3930 0.4003 0.3419 0.0213  -0.0421 0.0153  435 ARG B CZ  
4452  N NH1 . ARG B 134 ? 0.4148 0.4135 0.3617 0.0265  -0.0411 0.0181  435 ARG B NH1 
4453  N NH2 . ARG B 134 ? 0.3023 0.3234 0.2522 0.0228  -0.0460 0.0142  435 ARG B NH2 
4454  N N   . ASP B 135 ? 0.3028 0.2949 0.2300 0.0010  -0.0287 0.0161  436 ASP B N   
4455  C CA  . ASP B 135 ? 0.4002 0.3888 0.3171 0.0014  -0.0262 0.0197  436 ASP B CA  
4456  C C   . ASP B 135 ? 0.3988 0.3858 0.3168 -0.0037 -0.0210 0.0187  436 ASP B C   
4457  O O   . ASP B 135 ? 0.3722 0.3566 0.2820 -0.0041 -0.0179 0.0216  436 ASP B O   
4458  C CB  . ASP B 135 ? 0.3812 0.3778 0.2918 0.0040  -0.0299 0.0186  436 ASP B CB  
4459  C CG  . ASP B 135 ? 0.4082 0.4126 0.3231 0.0004  -0.0309 0.0125  436 ASP B CG  
4460  O OD1 . ASP B 135 ? 0.4466 0.4560 0.3551 0.0011  -0.0332 0.0109  436 ASP B OD1 
4461  O OD2 . ASP B 135 ? 0.4870 0.4914 0.4107 -0.0029 -0.0296 0.0091  436 ASP B OD2 
4462  N N   . CYS B 136 ? 0.3835 0.3727 0.3111 -0.0073 -0.0200 0.0148  437 CYS B N   
4463  C CA  . CYS B 136 ? 0.3457 0.3360 0.2759 -0.0115 -0.0155 0.0134  437 CYS B CA  
4464  C C   . CYS B 136 ? 0.3522 0.3351 0.2805 -0.0143 -0.0108 0.0178  437 CYS B C   
4465  O O   . CYS B 136 ? 0.3862 0.3618 0.3154 -0.0143 -0.0110 0.0202  437 CYS B O   
4466  C CB  . CYS B 136 ? 0.4377 0.4321 0.3785 -0.0137 -0.0163 0.0084  437 CYS B CB  
4467  S SG  . CYS B 136 ? 0.3847 0.3842 0.3294 -0.0167 -0.0121 0.0054  437 CYS B SG  
4468  N N   . THR B 137 ? 0.3301 0.3149 0.2557 -0.0169 -0.0060 0.0188  438 THR B N   
4469  C CA  . THR B 137 ? 0.3247 0.3032 0.2483 -0.0209 -0.0009 0.0232  438 THR B CA  
4470  C C   . THR B 137 ? 0.3662 0.3513 0.2972 -0.0260 0.0037  0.0212  438 THR B C   
4471  O O   . THR B 137 ? 0.3954 0.3768 0.3272 -0.0309 0.0079  0.0242  438 THR B O   
4472  C CB  . THR B 137 ? 0.3625 0.3358 0.2728 -0.0193 0.0016  0.0285  438 THR B CB  
4473  O OG1 . THR B 137 ? 0.4006 0.3818 0.3077 -0.0189 0.0037  0.0268  438 THR B OG1 
4474  C CG2 . THR B 137 ? 0.4663 0.4344 0.3684 -0.0132 -0.0032 0.0309  438 THR B CG2 
4475  N N   . THR B 138 ? 0.3092 0.3040 0.2452 -0.0250 0.0033  0.0165  439 THR B N   
4476  C CA  . THR B 138 ? 0.3621 0.3653 0.3047 -0.0283 0.0078  0.0148  439 THR B CA  
4477  C C   . THR B 138 ? 0.3355 0.3457 0.2874 -0.0268 0.0051  0.0090  439 THR B C   
4478  O O   . THR B 138 ? 0.3116 0.3206 0.2627 -0.0234 0.0004  0.0062  439 THR B O   
4479  C CB  . THR B 138 ? 0.3496 0.3572 0.2846 -0.0271 0.0121  0.0158  439 THR B CB  
4480  O OG1 . THR B 138 ? 0.3216 0.3313 0.2521 -0.0221 0.0087  0.0121  439 THR B OG1 
4481  C CG2 . THR B 138 ? 0.3293 0.3289 0.2529 -0.0281 0.0150  0.0220  439 THR B CG2 
4482  N N   . ALA B 139 ? 0.3772 0.3954 0.3376 -0.0295 0.0082  0.0074  440 ALA B N   
4483  C CA  . ALA B 139 ? 0.3460 0.3707 0.3144 -0.0274 0.0059  0.0023  440 ALA B CA  
4484  C C   . ALA B 139 ? 0.3134 0.3400 0.2762 -0.0223 0.0051  -0.0008 440 ALA B C   
4485  O O   . ALA B 139 ? 0.2838 0.3098 0.2486 -0.0196 0.0015  -0.0047 440 ALA B O   
4486  C CB  . ALA B 139 ? 0.2758 0.3106 0.2540 -0.0305 0.0094  0.0014  440 ALA B CB  
4487  N N   . HIS B 140 ? 0.3418 0.3694 0.2963 -0.0211 0.0086  0.0006  441 HIS B N   
4488  C CA  . HIS B 140 ? 0.3004 0.3278 0.2475 -0.0165 0.0076  -0.0027 441 HIS B CA  
4489  C C   . HIS B 140 ? 0.3036 0.3238 0.2456 -0.0150 0.0017  -0.0039 441 HIS B C   
4490  O O   . HIS B 140 ? 0.3065 0.3257 0.2472 -0.0126 -0.0011 -0.0081 441 HIS B O   
4491  C CB  . HIS B 140 ? 0.3015 0.3304 0.2390 -0.0156 0.0122  -0.0007 441 HIS B CB  
4492  C CG  . HIS B 140 ? 0.3402 0.3787 0.2817 -0.0150 0.0181  -0.0016 441 HIS B CG  
4493  N ND1 . HIS B 140 ? 0.3930 0.4381 0.3419 -0.0194 0.0226  0.0016  441 HIS B ND1 
4494  C CD2 . HIS B 140 ? 0.3868 0.4300 0.3261 -0.0106 0.0203  -0.0054 441 HIS B CD2 
4495  C CE1 . HIS B 140 ? 0.4168 0.4723 0.3690 -0.0175 0.0274  -0.0001 441 HIS B CE1 
4496  N NE2 . HIS B 140 ? 0.4424 0.4965 0.3886 -0.0116 0.0262  -0.0043 441 HIS B NE2 
4497  N N   . GLY B 141 ? 0.3348 0.3499 0.2734 -0.0164 -0.0001 0.0000  442 GLY B N   
4498  C CA  . GLY B 141 ? 0.3111 0.3220 0.2467 -0.0149 -0.0058 -0.0009 442 GLY B CA  
4499  C C   . GLY B 141 ? 0.3569 0.3678 0.3014 -0.0153 -0.0092 -0.0040 442 GLY B C   
4500  O O   . GLY B 141 ? 0.2934 0.3035 0.2365 -0.0141 -0.0130 -0.0071 442 GLY B O   
4501  N N   . MET B 142 ? 0.3043 0.3160 0.2575 -0.0175 -0.0078 -0.0031 443 MET B N   
4502  C CA  . MET B 142 ? 0.3244 0.3359 0.2853 -0.0177 -0.0109 -0.0060 443 MET B CA  
4503  C C   . MET B 142 ? 0.2620 0.2760 0.2236 -0.0158 -0.0112 -0.0106 443 MET B C   
4504  O O   . MET B 142 ? 0.2675 0.2793 0.2297 -0.0150 -0.0146 -0.0133 443 MET B O   
4505  C CB  . MET B 142 ? 0.3576 0.3701 0.3269 -0.0206 -0.0093 -0.0047 443 MET B CB  
4506  C CG  . MET B 142 ? 0.3263 0.3333 0.2940 -0.0229 -0.0088 -0.0003 443 MET B CG  
4507  S SD  . MET B 142 ? 0.3378 0.3454 0.3146 -0.0277 -0.0069 0.0003  443 MET B SD  
4508  C CE  . MET B 142 ? 0.2534 0.2607 0.2368 -0.0263 -0.0116 -0.0037 443 MET B CE  
4509  N N   . PHE B 143 ? 0.3177 0.3360 0.2785 -0.0147 -0.0073 -0.0115 444 PHE B N   
4510  C CA  . PHE B 143 ? 0.3073 0.3265 0.2671 -0.0117 -0.0071 -0.0158 444 PHE B CA  
4511  C C   . PHE B 143 ? 0.3520 0.3656 0.3028 -0.0104 -0.0100 -0.0183 444 PHE B C   
4512  O O   . PHE B 143 ? 0.3572 0.3671 0.3077 -0.0096 -0.0124 -0.0217 444 PHE B O   
4513  C CB  . PHE B 143 ? 0.3135 0.3389 0.2727 -0.0098 -0.0020 -0.0159 444 PHE B CB  
4514  C CG  . PHE B 143 ? 0.3544 0.3790 0.3100 -0.0053 -0.0013 -0.0203 444 PHE B CG  
4515  C CD1 . PHE B 143 ? 0.4031 0.4254 0.3483 -0.0027 0.0006  -0.0219 444 PHE B CD1 
4516  C CD2 . PHE B 143 ? 0.3619 0.3866 0.3231 -0.0034 -0.0028 -0.0228 444 PHE B CD2 
4517  C CE1 . PHE B 143 ? 0.4410 0.4603 0.3814 0.0018  0.0014  -0.0261 444 PHE B CE1 
4518  C CE2 . PHE B 143 ? 0.3752 0.3971 0.3317 0.0015  -0.0020 -0.0265 444 PHE B CE2 
4519  C CZ  . PHE B 143 ? 0.4612 0.4798 0.4071 0.0041  0.0002  -0.0283 444 PHE B CZ  
4520  N N   . ASN B 144 ? 0.3309 0.3435 0.2738 -0.0107 -0.0098 -0.0167 445 ASN B N   
4521  C CA  . ASN B 144 ? 0.3158 0.3243 0.2498 -0.0103 -0.0130 -0.0192 445 ASN B CA  
4522  C C   . ASN B 144 ? 0.2923 0.2988 0.2299 -0.0122 -0.0180 -0.0199 445 ASN B C   
4523  O O   . ASN B 144 ? 0.2936 0.2968 0.2288 -0.0128 -0.0204 -0.0237 445 ASN B O   
4524  C CB  . ASN B 144 ? 0.3459 0.3551 0.2710 -0.0101 -0.0123 -0.0167 445 ASN B CB  
4525  C CG  . ASN B 144 ? 0.4188 0.4252 0.3342 -0.0101 -0.0159 -0.0196 445 ASN B CG  
4526  O OD1 . ASN B 144 ? 0.5289 0.5362 0.4413 -0.0109 -0.0192 -0.0177 445 ASN B OD1 
4527  N ND2 . ASN B 144 ? 0.4227 0.4256 0.3325 -0.0091 -0.0154 -0.0244 445 ASN B ND2 
4528  N N   . TYR B 145 ? 0.3204 0.3285 0.2635 -0.0134 -0.0192 -0.0163 446 TYR B N   
4529  C CA  . TYR B 145 ? 0.3132 0.3206 0.2604 -0.0146 -0.0233 -0.0167 446 TYR B CA  
4530  C C   . TYR B 145 ? 0.3494 0.3549 0.3022 -0.0152 -0.0237 -0.0198 446 TYR B C   
4531  O O   . TYR B 145 ? 0.2858 0.2900 0.2387 -0.0165 -0.0266 -0.0220 446 TYR B O   
4532  C CB  . TYR B 145 ? 0.2789 0.2870 0.2306 -0.0148 -0.0236 -0.0123 446 TYR B CB  
4533  C CG  . TYR B 145 ? 0.3351 0.3442 0.2813 -0.0137 -0.0259 -0.0096 446 TYR B CG  
4534  C CD1 . TYR B 145 ? 0.2854 0.2932 0.2273 -0.0127 -0.0237 -0.0052 446 TYR B CD1 
4535  C CD2 . TYR B 145 ? 0.3389 0.3506 0.2839 -0.0137 -0.0302 -0.0112 446 TYR B CD2 
4536  C CE1 . TYR B 145 ? 0.2989 0.3071 0.2347 -0.0107 -0.0260 -0.0023 446 TYR B CE1 
4537  C CE2 . TYR B 145 ? 0.3032 0.3176 0.2436 -0.0120 -0.0328 -0.0086 446 TYR B CE2 
4538  C CZ  . TYR B 145 ? 0.3416 0.3538 0.2770 -0.0099 -0.0308 -0.0041 446 TYR B CZ  
4539  O OH  . TYR B 145 ? 0.3902 0.4049 0.3201 -0.0072 -0.0337 -0.0013 446 TYR B OH  
4540  N N   . ILE B 146 ? 0.2828 0.2889 0.2401 -0.0143 -0.0208 -0.0199 447 ILE B N   
4541  C CA  . ILE B 146 ? 0.2845 0.2888 0.2466 -0.0140 -0.0214 -0.0223 447 ILE B CA  
4542  C C   . ILE B 146 ? 0.3457 0.3454 0.3013 -0.0128 -0.0215 -0.0263 447 ILE B C   
4543  O O   . ILE B 146 ? 0.3119 0.3073 0.2674 -0.0136 -0.0234 -0.0285 447 ILE B O   
4544  C CB  . ILE B 146 ? 0.2716 0.2794 0.2408 -0.0132 -0.0189 -0.0211 447 ILE B CB  
4545  C CG1 . ILE B 146 ? 0.3232 0.3323 0.2981 -0.0153 -0.0196 -0.0179 447 ILE B CG1 
4546  C CG2 . ILE B 146 ? 0.2957 0.3017 0.2676 -0.0115 -0.0194 -0.0239 447 ILE B CG2 
4547  C CD1 . ILE B 146 ? 0.3223 0.3356 0.3031 -0.0162 -0.0169 -0.0163 447 ILE B CD1 
4548  N N   . CYS B 147 ? 0.3109 0.3103 0.2600 -0.0109 -0.0191 -0.0274 448 CYS B N   
4549  C CA  . CYS B 147 ? 0.2734 0.2661 0.2140 -0.0097 -0.0190 -0.0315 448 CYS B CA  
4550  C C   . CYS B 147 ? 0.3403 0.3288 0.2760 -0.0134 -0.0228 -0.0333 448 CYS B C   
4551  O O   . CYS B 147 ? 0.3598 0.3413 0.2922 -0.0144 -0.0239 -0.0364 448 CYS B O   
4552  C CB  . CYS B 147 ? 0.3086 0.3017 0.2416 -0.0070 -0.0158 -0.0324 448 CYS B CB  
4553  S SG  . CYS B 147 ? 0.4261 0.4257 0.3649 -0.0026 -0.0109 -0.0311 448 CYS B SG  
4554  N N   . ASN B 148 ? 0.2762 0.2691 0.2110 -0.0154 -0.0248 -0.0314 449 ASN B N   
4555  C CA  . ASN B 148 ? 0.3659 0.3581 0.2975 -0.0192 -0.0287 -0.0331 449 ASN B CA  
4556  C C   . ASN B 148 ? 0.2714 0.2634 0.2101 -0.0214 -0.0306 -0.0331 449 ASN B C   
4557  O O   . ASN B 148 ? 0.3206 0.3089 0.2565 -0.0248 -0.0326 -0.0360 449 ASN B O   
4558  C CB  . ASN B 148 ? 0.2791 0.2781 0.2097 -0.0197 -0.0307 -0.0303 449 ASN B CB  
4559  C CG  . ASN B 148 ? 0.4144 0.4129 0.3354 -0.0179 -0.0291 -0.0307 449 ASN B CG  
4560  O OD1 . ASN B 148 ? 0.3392 0.3323 0.2538 -0.0166 -0.0267 -0.0337 449 ASN B OD1 
4561  N ND2 . ASN B 148 ? 0.2905 0.2942 0.2096 -0.0174 -0.0303 -0.0275 449 ASN B ND2 
4562  N N   . HIS B 149 ? 0.2837 0.2794 0.2312 -0.0201 -0.0299 -0.0299 450 HIS B N   
4563  C CA  . HIS B 149 ? 0.2945 0.2896 0.2482 -0.0215 -0.0311 -0.0299 450 HIS B CA  
4564  C C   . HIS B 149 ? 0.2594 0.2466 0.2104 -0.0214 -0.0301 -0.0329 450 HIS B C   
4565  O O   . HIS B 149 ? 0.2796 0.2632 0.2292 -0.0245 -0.0315 -0.0347 450 HIS B O   
4566  C CB  . HIS B 149 ? 0.2478 0.2465 0.2097 -0.0196 -0.0301 -0.0265 450 HIS B CB  
4567  C CG  . HIS B 149 ? 0.3332 0.3313 0.3009 -0.0204 -0.0312 -0.0264 450 HIS B CG  
4568  N ND1 . HIS B 149 ? 0.3042 0.3060 0.2777 -0.0202 -0.0320 -0.0238 450 HIS B ND1 
4569  C CD2 . HIS B 149 ? 0.3015 0.2949 0.2691 -0.0211 -0.0312 -0.0284 450 HIS B CD2 
4570  C CE1 . HIS B 149 ? 0.2999 0.3002 0.2768 -0.0208 -0.0325 -0.0244 450 HIS B CE1 
4571  N NE2 . HIS B 149 ? 0.2748 0.2701 0.2483 -0.0215 -0.0320 -0.0271 450 HIS B NE2 
4572  N N   . VAL B 150 ? 0.2613 0.2457 0.2111 -0.0178 -0.0274 -0.0333 451 VAL B N   
4573  C CA  . VAL B 150 ? 0.2660 0.2423 0.2124 -0.0162 -0.0263 -0.0358 451 VAL B CA  
4574  C C   . VAL B 150 ? 0.3130 0.2804 0.2492 -0.0189 -0.0271 -0.0393 451 VAL B C   
4575  O O   . VAL B 150 ? 0.3016 0.2616 0.2351 -0.0210 -0.0278 -0.0409 451 VAL B O   
4576  C CB  . VAL B 150 ? 0.3329 0.3097 0.2794 -0.0108 -0.0233 -0.0357 451 VAL B CB  
4577  C CG1 . VAL B 150 ? 0.2766 0.2432 0.2162 -0.0079 -0.0223 -0.0386 451 VAL B CG1 
4578  C CG2 . VAL B 150 ? 0.3131 0.2976 0.2700 -0.0094 -0.0229 -0.0328 451 VAL B CG2 
4579  N N   . LYS B 151 ? 0.3492 0.3168 0.2788 -0.0194 -0.0271 -0.0407 452 LYS B N   
4580  C CA  . LYS B 151 ? 0.3020 0.2602 0.2207 -0.0224 -0.0279 -0.0447 452 LYS B CA  
4581  C C   . LYS B 151 ? 0.3026 0.2620 0.2226 -0.0292 -0.0311 -0.0454 452 LYS B C   
4582  O O   . LYS B 151 ? 0.3370 0.2868 0.2507 -0.0329 -0.0315 -0.0482 452 LYS B O   
4583  C CB  . LYS B 151 ? 0.3044 0.2638 0.2155 -0.0215 -0.0274 -0.0461 452 LYS B CB  
4584  C CG  . LYS B 151 ? 0.3203 0.2684 0.2182 -0.0246 -0.0281 -0.0510 452 LYS B CG  
4585  C CD  . LYS B 151 ? 0.3662 0.3152 0.2560 -0.0222 -0.0271 -0.0523 452 LYS B CD  
4586  C CE  . LYS B 151 ? 0.4677 0.4027 0.3423 -0.0236 -0.0268 -0.0578 452 LYS B CE  
4587  N NZ  . LYS B 151 ? 0.5058 0.4415 0.3718 -0.0200 -0.0250 -0.0590 452 LYS B NZ  
4588  N N   . TYR B 152 ? 0.2961 0.2672 0.2238 -0.0309 -0.0333 -0.0427 453 TYR B N   
4589  C CA  . TYR B 152 ? 0.3195 0.2948 0.2499 -0.0369 -0.0362 -0.0432 453 TYR B CA  
4590  C C   . TYR B 152 ? 0.3021 0.2739 0.2371 -0.0381 -0.0355 -0.0426 453 TYR B C   
4591  O O   . TYR B 152 ? 0.3240 0.2920 0.2564 -0.0436 -0.0364 -0.0446 453 TYR B O   
4592  C CB  . TYR B 152 ? 0.3001 0.2891 0.2378 -0.0365 -0.0385 -0.0400 453 TYR B CB  
4593  C CG  . TYR B 152 ? 0.3171 0.3133 0.2602 -0.0414 -0.0411 -0.0400 453 TYR B CG  
4594  C CD1 . TYR B 152 ? 0.4154 0.4164 0.3550 -0.0466 -0.0442 -0.0424 453 TYR B CD1 
4595  C CD2 . TYR B 152 ? 0.3372 0.3363 0.2887 -0.0409 -0.0405 -0.0378 453 TYR B CD2 
4596  C CE1 . TYR B 152 ? 0.4292 0.4393 0.3747 -0.0512 -0.0465 -0.0425 453 TYR B CE1 
4597  C CE2 . TYR B 152 ? 0.3742 0.3811 0.3307 -0.0450 -0.0424 -0.0378 453 TYR B CE2 
4598  C CZ  . TYR B 152 ? 0.4224 0.4356 0.3764 -0.0502 -0.0453 -0.0401 453 TYR B CZ  
4599  O OH  . TYR B 152 ? 0.5177 0.5412 0.4778 -0.0545 -0.0470 -0.0401 453 TYR B OH  
4600  N N   . ALA B 153 ? 0.3012 0.2746 0.2428 -0.0335 -0.0339 -0.0398 454 ALA B N   
4601  C CA  . ALA B 153 ? 0.2882 0.2591 0.2339 -0.0342 -0.0334 -0.0389 454 ALA B CA  
4602  C C   . ALA B 153 ? 0.3769 0.3337 0.3140 -0.0347 -0.0318 -0.0414 454 ALA B C   
4603  O O   . ALA B 153 ? 0.4094 0.3616 0.3452 -0.0388 -0.0318 -0.0420 454 ALA B O   
4604  C CB  . ALA B 153 ? 0.2590 0.2344 0.2125 -0.0291 -0.0324 -0.0358 454 ALA B CB  
4605  N N   . THR B 154 ? 0.4262 0.3757 0.3567 -0.0305 -0.0301 -0.0428 455 THR B N   
4606  C CA  . THR B 154 ? 0.3656 0.3001 0.2867 -0.0291 -0.0283 -0.0449 455 THR B CA  
4607  C C   . THR B 154 ? 0.4132 0.3376 0.3242 -0.0358 -0.0290 -0.0483 455 THR B C   
4608  O O   . THR B 154 ? 0.4824 0.3954 0.3879 -0.0384 -0.0281 -0.0492 455 THR B O   
4609  C CB  . THR B 154 ? 0.4315 0.3625 0.3486 -0.0218 -0.0262 -0.0456 455 THR B CB  
4610  O OG1 . THR B 154 ? 0.3840 0.3249 0.3111 -0.0168 -0.0256 -0.0425 455 THR B OG1 
4611  C CG2 . THR B 154 ? 0.3960 0.3105 0.3022 -0.0189 -0.0244 -0.0477 455 THR B CG2 
4612  N N   . ASN B 155 ? 0.3857 0.3138 0.2937 -0.0392 -0.0304 -0.0504 456 ASN B N   
4613  C CA  . ASN B 155 ? 0.3749 0.2969 0.2751 -0.0476 -0.0319 -0.0538 456 ASN B CA  
4614  C C   . ASN B 155 ? 0.4334 0.3346 0.3204 -0.0484 -0.0298 -0.0566 456 ASN B C   
4615  O O   . ASN B 155 ? 0.4105 0.3043 0.2934 -0.0557 -0.0300 -0.0579 456 ASN B O   
4616  C CB  . ASN B 155 ? 0.3202 0.2533 0.2295 -0.0543 -0.0340 -0.0523 456 ASN B CB  
4617  C CG  . ASN B 155 ? 0.4253 0.3579 0.3294 -0.0640 -0.0361 -0.0557 456 ASN B CG  
4618  O OD1 . ASN B 155 ? 0.4243 0.3541 0.3206 -0.0658 -0.0374 -0.0589 456 ASN B OD1 
4619  N ND2 . ASN B 155 ? 0.3696 0.3057 0.2780 -0.0707 -0.0365 -0.0553 456 ASN B ND2 
4620  N N   . LYS B 156 ? 0.3885 0.2799 0.2686 -0.0405 -0.0274 -0.0573 457 LYS B N   
4621  C CA  . LYS B 156 ? 0.3724 0.2421 0.2381 -0.0390 -0.0250 -0.0598 457 LYS B CA  
4622  C C   . LYS B 156 ? 0.3908 0.2522 0.2564 -0.0404 -0.0240 -0.0579 457 LYS B C   
4623  O O   . LYS B 156 ? 0.4946 0.3371 0.3475 -0.0438 -0.0227 -0.0600 457 LYS B O   
4624  C CB  . LYS B 156 ? 0.4648 0.3222 0.3168 -0.0463 -0.0257 -0.0648 457 LYS B CB  
4625  C CG  . LYS B 156 ? 0.5142 0.3752 0.3619 -0.0437 -0.0262 -0.0673 457 LYS B CG  
4626  C CD  . LYS B 156 ? 0.6399 0.4872 0.4727 -0.0514 -0.0272 -0.0728 457 LYS B CD  
4627  C CE  . LYS B 156 ? 0.7500 0.6015 0.5777 -0.0488 -0.0278 -0.0755 457 LYS B CE  
4628  N NZ  . LYS B 156 ? 0.7591 0.6101 0.5799 -0.0593 -0.0312 -0.0798 457 LYS B NZ  
4629  N N   . GLY B 157 ? 0.3950 0.2690 0.2734 -0.0382 -0.0245 -0.0539 458 GLY B N   
4630  C CA  . GLY B 157 ? 0.4342 0.3020 0.3128 -0.0387 -0.0235 -0.0517 458 GLY B CA  
4631  C C   . GLY B 157 ? 0.4526 0.3290 0.3384 -0.0476 -0.0247 -0.0505 458 GLY B C   
4632  O O   . GLY B 157 ? 0.3867 0.2629 0.2758 -0.0473 -0.0239 -0.0478 458 GLY B O   
4633  N N   . ASN B 158 ? 0.3859 0.2708 0.2742 -0.0552 -0.0267 -0.0523 459 ASN B N   
4634  C CA  . ASN B 158 ? 0.4266 0.3230 0.3232 -0.0633 -0.0279 -0.0513 459 ASN B CA  
4635  C C   . ASN B 158 ? 0.4297 0.3470 0.3412 -0.0594 -0.0297 -0.0484 459 ASN B C   
4636  O O   . ASN B 158 ? 0.3959 0.3262 0.3127 -0.0618 -0.0320 -0.0490 459 ASN B O   
4637  C CB  . ASN B 158 ? 0.4879 0.3838 0.3795 -0.0737 -0.0294 -0.0549 459 ASN B CB  
4638  C CG  . ASN B 158 ? 0.5558 0.4645 0.4560 -0.0824 -0.0303 -0.0540 459 ASN B CG  
4639  O OD1 . ASN B 158 ? 0.5504 0.4629 0.4569 -0.0814 -0.0289 -0.0509 459 ASN B OD1 
4640  N ND2 . ASN B 158 ? 0.5141 0.4305 0.4147 -0.0908 -0.0328 -0.0568 459 ASN B ND2 
4641  N N   . LEU B 159 ? 0.3830 0.3026 0.3003 -0.0531 -0.0286 -0.0453 460 LEU B N   
4642  C CA  . LEU B 159 ? 0.3481 0.2832 0.2770 -0.0478 -0.0299 -0.0428 460 LEU B CA  
4643  C C   . LEU B 159 ? 0.3654 0.3164 0.3041 -0.0522 -0.0317 -0.0416 460 LEU B C   
4644  O O   . LEU B 159 ? 0.3667 0.3194 0.3068 -0.0580 -0.0313 -0.0416 460 LEU B O   
4645  C CB  . LEU B 159 ? 0.3379 0.2718 0.2704 -0.0411 -0.0287 -0.0401 460 LEU B CB  
4646  C CG  . LEU B 159 ? 0.5558 0.4763 0.4802 -0.0349 -0.0270 -0.0406 460 LEU B CG  
4647  C CD1 . LEU B 159 ? 0.5322 0.4581 0.4634 -0.0281 -0.0270 -0.0380 460 LEU B CD1 
4648  C CD2 . LEU B 159 ? 0.4866 0.4036 0.4054 -0.0323 -0.0268 -0.0428 460 LEU B CD2 
4649  N N   . ARG B 160 ? 0.3245 0.2874 0.2699 -0.0491 -0.0333 -0.0405 461 ARG B N   
4650  C CA  . ARG B 160 ? 0.2904 0.2689 0.2448 -0.0511 -0.0352 -0.0391 461 ARG B CA  
4651  C C   . ARG B 160 ? 0.3535 0.3390 0.3156 -0.0444 -0.0352 -0.0360 461 ARG B C   
4652  O O   . ARG B 160 ? 0.3027 0.2858 0.2637 -0.0396 -0.0348 -0.0355 461 ARG B O   
4653  C CB  . ARG B 160 ? 0.3877 0.3729 0.3404 -0.0543 -0.0377 -0.0409 461 ARG B CB  
4654  C CG  . ARG B 160 ? 0.3281 0.3051 0.2717 -0.0617 -0.0380 -0.0448 461 ARG B CG  
4655  C CD  . ARG B 160 ? 0.3609 0.3460 0.3029 -0.0645 -0.0411 -0.0467 461 ARG B CD  
4656  N NE  . ARG B 160 ? 0.4085 0.3871 0.3436 -0.0597 -0.0409 -0.0476 461 ARG B NE  
4657  C CZ  . ARG B 160 ? 0.4072 0.3855 0.3353 -0.0625 -0.0428 -0.0505 461 ARG B CZ  
4658  N NH1 . ARG B 160 ? 0.3719 0.3568 0.2996 -0.0704 -0.0456 -0.0529 461 ARG B NH1 
4659  N NH2 . ARG B 160 ? 0.3581 0.3307 0.2796 -0.0577 -0.0420 -0.0512 461 ARG B NH2 
4660  N N   . SER B 161 ? 0.3130 0.3070 0.2826 -0.0443 -0.0353 -0.0341 462 SER B N   
4661  C CA  . SER B 161 ? 0.3511 0.3502 0.3270 -0.0386 -0.0353 -0.0314 462 SER B CA  
4662  C C   . SER B 161 ? 0.3237 0.3301 0.3015 -0.0363 -0.0370 -0.0304 462 SER B C   
4663  O O   . SER B 161 ? 0.2570 0.2706 0.2349 -0.0389 -0.0389 -0.0310 462 SER B O   
4664  C CB  . SER B 161 ? 0.2900 0.2961 0.2722 -0.0388 -0.0350 -0.0299 462 SER B CB  
4665  O OG  . SER B 161 ? 0.5535 0.5525 0.5328 -0.0415 -0.0332 -0.0307 462 SER B OG  
4666  N N   . ALA B 162 ? 0.2636 0.2684 0.2427 -0.0315 -0.0364 -0.0286 463 ALA B N   
4667  C CA  . ALA B 162 ? 0.2571 0.2671 0.2366 -0.0292 -0.0375 -0.0271 463 ALA B CA  
4668  C C   . ALA B 162 ? 0.3219 0.3307 0.3047 -0.0249 -0.0363 -0.0246 463 ALA B C   
4669  O O   . ALA B 162 ? 0.2853 0.2890 0.2690 -0.0238 -0.0349 -0.0248 463 ALA B O   
4670  C CB  . ALA B 162 ? 0.2450 0.2514 0.2177 -0.0302 -0.0375 -0.0289 463 ALA B CB  
4671  N N   . ILE B 163 ? 0.3433 0.3567 0.3273 -0.0226 -0.0371 -0.0222 464 ILE B N   
4672  C CA  . ILE B 163 ? 0.3004 0.3115 0.2860 -0.0194 -0.0359 -0.0197 464 ILE B CA  
4673  C C   . ILE B 163 ? 0.3135 0.3261 0.2955 -0.0182 -0.0361 -0.0180 464 ILE B C   
4674  O O   . ILE B 163 ? 0.2926 0.3104 0.2724 -0.0184 -0.0380 -0.0178 464 ILE B O   
4675  C CB  . ILE B 163 ? 0.2290 0.2417 0.2188 -0.0172 -0.0362 -0.0179 464 ILE B CB  
4676  C CG1 . ILE B 163 ? 0.2248 0.2329 0.2150 -0.0149 -0.0349 -0.0156 464 ILE B CG1 
4677  C CG2 . ILE B 163 ? 0.2254 0.2459 0.2159 -0.0159 -0.0381 -0.0168 464 ILE B CG2 
4678  C CD1 . ILE B 163 ? 0.2466 0.2526 0.2396 -0.0130 -0.0347 -0.0149 464 ILE B CD1 
4679  N N   . THR B 164 ? 0.3170 0.3259 0.2982 -0.0172 -0.0341 -0.0166 465 THR B N   
4680  C CA  . THR B 164 ? 0.3329 0.3423 0.3101 -0.0159 -0.0336 -0.0142 465 THR B CA  
4681  C C   . THR B 164 ? 0.3436 0.3496 0.3223 -0.0142 -0.0323 -0.0109 465 THR B C   
4682  O O   . THR B 164 ? 0.2896 0.2922 0.2714 -0.0151 -0.0307 -0.0111 465 THR B O   
4683  C CB  . THR B 164 ? 0.3255 0.3332 0.2990 -0.0168 -0.0316 -0.0155 465 THR B CB  
4684  O OG1 . THR B 164 ? 0.3215 0.3299 0.2915 -0.0183 -0.0329 -0.0187 465 THR B OG1 
4685  C CG2 . THR B 164 ? 0.3330 0.3409 0.3018 -0.0156 -0.0303 -0.0125 465 THR B CG2 
4686  N N   . ILE B 165 ? 0.2865 0.2932 0.2625 -0.0118 -0.0333 -0.0079 466 ILE B N   
4687  C CA  . ILE B 165 ? 0.2915 0.2928 0.2675 -0.0099 -0.0322 -0.0047 466 ILE B CA  
4688  C C   . ILE B 165 ? 0.2930 0.2906 0.2630 -0.0095 -0.0303 -0.0014 466 ILE B C   
4689  O O   . ILE B 165 ? 0.3398 0.3398 0.3046 -0.0073 -0.0314 0.0005  466 ILE B O   
4690  C CB  . ILE B 165 ? 0.3640 0.3672 0.3407 -0.0061 -0.0344 -0.0035 466 ILE B CB  
4691  C CG1 . ILE B 165 ? 0.3446 0.3515 0.3271 -0.0071 -0.0354 -0.0068 466 ILE B CG1 
4692  C CG2 . ILE B 165 ? 0.2527 0.2474 0.2274 -0.0037 -0.0330 -0.0004 466 ILE B CG2 
4693  C CD1 . ILE B 165 ? 0.2531 0.2657 0.2373 -0.0034 -0.0375 -0.0061 466 ILE B CD1 
4694  N N   . PHE B 166 ? 0.3354 0.3279 0.3063 -0.0120 -0.0273 -0.0006 467 PHE B N   
4695  C CA  . PHE B 166 ? 0.3291 0.3174 0.2948 -0.0129 -0.0245 0.0028  467 PHE B CA  
4696  C C   . PHE B 166 ? 0.3802 0.3596 0.3419 -0.0110 -0.0240 0.0068  467 PHE B C   
4697  O O   . PHE B 166 ? 0.3279 0.3049 0.2915 -0.0087 -0.0257 0.0064  467 PHE B O   
4698  C CB  . PHE B 166 ? 0.2605 0.2495 0.2301 -0.0171 -0.0215 0.0014  467 PHE B CB  
4699  C CG  . PHE B 166 ? 0.3171 0.3130 0.2878 -0.0176 -0.0213 -0.0018 467 PHE B CG  
4700  C CD1 . PHE B 166 ? 0.2926 0.2908 0.2572 -0.0168 -0.0203 -0.0009 467 PHE B CD1 
4701  C CD2 . PHE B 166 ? 0.3276 0.3267 0.3041 -0.0184 -0.0223 -0.0056 467 PHE B CD2 
4702  C CE1 . PHE B 166 ? 0.3056 0.3084 0.2698 -0.0168 -0.0200 -0.0041 467 PHE B CE1 
4703  C CE2 . PHE B 166 ? 0.3945 0.3977 0.3705 -0.0181 -0.0220 -0.0085 467 PHE B CE2 
4704  C CZ  . PHE B 166 ? 0.2922 0.2970 0.2619 -0.0173 -0.0208 -0.0079 467 PHE B CZ  
4705  N N   . PRO B 167 ? 0.3589 0.3326 0.3140 -0.0115 -0.0214 0.0108  468 PRO B N   
4706  C CA  . PRO B 167 ? 0.4315 0.3945 0.3803 -0.0088 -0.0209 0.0150  468 PRO B CA  
4707  C C   . PRO B 167 ? 0.4091 0.3640 0.3611 -0.0106 -0.0203 0.0140  468 PRO B C   
4708  O O   . PRO B 167 ? 0.3417 0.2976 0.2995 -0.0159 -0.0188 0.0115  468 PRO B O   
4709  C CB  . PRO B 167 ? 0.3501 0.3076 0.2912 -0.0109 -0.0172 0.0191  468 PRO B CB  
4710  C CG  . PRO B 167 ? 0.3004 0.2684 0.2417 -0.0114 -0.0173 0.0175  468 PRO B CG  
4711  C CD  . PRO B 167 ? 0.3694 0.3459 0.3205 -0.0135 -0.0188 0.0120  468 PRO B CD  
4712  N N   . GLN B 168 ? 0.3688 0.3162 0.3167 -0.0057 -0.0215 0.0160  469 GLN B N   
4713  C CA  . GLN B 168 ? 0.3728 0.3109 0.3218 -0.0065 -0.0211 0.0149  469 GLN B CA  
4714  C C   . GLN B 168 ? 0.4054 0.3310 0.3500 -0.0122 -0.0174 0.0170  469 GLN B C   
4715  O O   . GLN B 168 ? 0.4336 0.3554 0.3722 -0.0140 -0.0148 0.0207  469 GLN B O   
4716  C CB  . GLN B 168 ? 0.3319 0.2644 0.2761 0.0013  -0.0229 0.0167  469 GLN B CB  
4717  C CG  . GLN B 168 ? 0.3736 0.2957 0.3065 0.0055  -0.0217 0.0224  469 GLN B CG  
4718  C CD  . GLN B 168 ? 0.4191 0.3437 0.3487 0.0152  -0.0246 0.0242  469 GLN B CD  
4719  O OE1 . GLN B 168 ? 0.4584 0.3981 0.3939 0.0178  -0.0277 0.0222  469 GLN B OE1 
4720  N NE2 . GLN B 168 ? 0.4411 0.3511 0.3614 0.0206  -0.0237 0.0280  469 GLN B NE2 
4721  N N   . ARG B 169 ? 0.3857 0.3048 0.3328 -0.0154 -0.0170 0.0146  470 ARG B N   
4722  C CA  . ARG B 169 ? 0.3781 0.2844 0.3210 -0.0218 -0.0138 0.0160  470 ARG B CA  
4723  C C   . ARG B 169 ? 0.3962 0.2861 0.3263 -0.0182 -0.0120 0.0213  470 ARG B C   
4724  O O   . ARG B 169 ? 0.4024 0.2882 0.3278 -0.0098 -0.0140 0.0227  470 ARG B O   
4725  C CB  . ARG B 169 ? 0.4634 0.3656 0.4104 -0.0250 -0.0147 0.0118  470 ARG B CB  
4726  C CG  . ARG B 169 ? 0.5949 0.4830 0.5374 -0.0325 -0.0119 0.0124  470 ARG B CG  
4727  C CD  . ARG B 169 ? 0.5579 0.4469 0.5064 -0.0367 -0.0135 0.0072  470 ARG B CD  
4728  N NE  . ARG B 169 ? 0.4940 0.4010 0.4540 -0.0405 -0.0146 0.0038  470 ARG B NE  
4729  C CZ  . ARG B 169 ? 0.7140 0.6269 0.6808 -0.0425 -0.0168 -0.0009 470 ARG B CZ  
4730  N NH1 . ARG B 169 ? 0.7803 0.6826 0.7434 -0.0417 -0.0182 -0.0031 470 ARG B NH1 
4731  N NH2 . ARG B 169 ? 0.6646 0.5935 0.6408 -0.0448 -0.0177 -0.0033 470 ARG B NH2 
4732  N N   . THR B 170 ? 0.3905 0.2711 0.3148 -0.0242 -0.0082 0.0246  471 THR B N   
4733  C CA  . THR B 170 ? 0.4056 0.2676 0.3159 -0.0214 -0.0060 0.0301  471 THR B CA  
4734  C C   . THR B 170 ? 0.4868 0.3314 0.3927 -0.0284 -0.0035 0.0296  471 THR B C   
4735  O O   . THR B 170 ? 0.5365 0.3703 0.4392 -0.0249 -0.0049 0.0279  471 THR B O   
4736  C CB  . THR B 170 ? 0.4699 0.3336 0.3743 -0.0222 -0.0033 0.0351  471 THR B CB  
4737  O OG1 . THR B 170 ? 0.5422 0.4127 0.4525 -0.0324 0.0000  0.0340  471 THR B OG1 
4738  C CG2 . THR B 170 ? 0.4386 0.3181 0.3458 -0.0148 -0.0065 0.0351  471 THR B CG2 
4739  N N   . ASP B 171 ? 0.5780 0.4192 0.4833 -0.0385 0.0004  0.0307  472 ASP B N   
4740  C CA  . ASP B 171 ? 0.6216 0.4466 0.5228 -0.0470 0.0028  0.0298  472 ASP B CA  
4741  C C   . ASP B 171 ? 0.6513 0.4887 0.5657 -0.0552 0.0014  0.0236  472 ASP B C   
4742  O O   . ASP B 171 ? 0.7534 0.5807 0.6662 -0.0641 0.0031  0.0220  472 ASP B O   
4743  C CB  . ASP B 171 ? 0.7197 0.5328 0.6116 -0.0543 0.0081  0.0351  472 ASP B CB  
4744  C CG  . ASP B 171 ? 0.8078 0.6399 0.7077 -0.0592 0.0103  0.0360  472 ASP B CG  
4745  O OD1 . ASP B 171 ? 0.7992 0.6524 0.7120 -0.0577 0.0076  0.0318  472 ASP B OD1 
4746  O OD2 . ASP B 171 ? 0.8248 0.6500 0.7173 -0.0642 0.0151  0.0408  472 ASP B OD2 
4747  N N   . GLY B 172 ? 0.5701 0.4287 0.4968 -0.0524 -0.0016 0.0200  473 GLY B N   
4748  C CA  . GLY B 172 ? 0.5344 0.4067 0.4736 -0.0591 -0.0030 0.0146  473 GLY B CA  
4749  C C   . GLY B 172 ? 0.5826 0.4664 0.5283 -0.0683 0.0002  0.0150  473 GLY B C   
4750  O O   . GLY B 172 ? 0.5655 0.4635 0.5223 -0.0731 -0.0010 0.0107  473 GLY B O   
4751  N N   . LYS B 173 ? 0.6228 0.5014 0.5615 -0.0704 0.0045  0.0202  474 LYS B N   
4752  C CA  . LYS B 173 ? 0.5937 0.4838 0.5378 -0.0786 0.0085  0.0214  474 LYS B CA  
4753  C C   . LYS B 173 ? 0.5094 0.4150 0.4566 -0.0730 0.0090  0.0228  474 LYS B C   
4754  O O   . LYS B 173 ? 0.5758 0.4929 0.5276 -0.0783 0.0125  0.0237  474 LYS B O   
4755  C CB  . LYS B 173 ? 0.6316 0.5042 0.5645 -0.0861 0.0138  0.0264  474 LYS B CB  
4756  C CG  . LYS B 173 ? 0.8130 0.6660 0.7397 -0.0926 0.0139  0.0252  474 LYS B CG  
4757  C CD  . LYS B 173 ? 0.9144 0.7796 0.8539 -0.1001 0.0115  0.0187  474 LYS B CD  
4758  C CE  . LYS B 173 ? 1.0344 0.8853 0.9695 -0.1130 0.0140  0.0182  474 LYS B CE  
4759  N NZ  . LYS B 173 ? 1.1179 0.9389 1.0366 -0.1108 0.0143  0.0201  474 LYS B NZ  
4760  N N   . HIS B 174 ? 0.4900 0.3964 0.4345 -0.0627 0.0057  0.0230  475 HIS B N   
4761  C CA  . HIS B 174 ? 0.4211 0.3400 0.3665 -0.0574 0.0058  0.0242  475 HIS B CA  
4762  C C   . HIS B 174 ? 0.4202 0.3512 0.3733 -0.0507 0.0009  0.0197  475 HIS B C   
4763  O O   . HIS B 174 ? 0.3940 0.3287 0.3442 -0.0436 -0.0009 0.0205  475 HIS B O   
4764  C CB  . HIS B 174 ? 0.5175 0.4247 0.4493 -0.0519 0.0071  0.0300  475 HIS B CB  
4765  C CG  . HIS B 174 ? 0.5367 0.4315 0.4595 -0.0586 0.0126  0.0351  475 HIS B CG  
4766  N ND1 . HIS B 174 ? 0.5955 0.4710 0.5110 -0.0628 0.0141  0.0369  475 HIS B ND1 
4767  C CD2 . HIS B 174 ? 0.5635 0.4619 0.4829 -0.0623 0.0175  0.0387  475 HIS B CD2 
4768  C CE1 . HIS B 174 ? 0.6168 0.4838 0.5244 -0.0692 0.0196  0.0417  475 HIS B CE1 
4769  N NE2 . HIS B 174 ? 0.6062 0.4874 0.5163 -0.0690 0.0219  0.0430  475 HIS B NE2 
4770  N N   . ASP B 175 ? 0.4418 0.3787 0.4042 -0.0532 -0.0014 0.0149  476 ASP B N   
4771  C CA  . ASP B 175 ? 0.3680 0.3137 0.3365 -0.0474 -0.0058 0.0108  476 ASP B CA  
4772  C C   . ASP B 175 ? 0.2961 0.2571 0.2693 -0.0450 -0.0057 0.0096  476 ASP B C   
4773  O O   . ASP B 175 ? 0.3748 0.3445 0.3520 -0.0492 -0.0026 0.0096  476 ASP B O   
4774  C CB  . ASP B 175 ? 0.4586 0.4073 0.4351 -0.0508 -0.0080 0.0062  476 ASP B CB  
4775  C CG  . ASP B 175 ? 0.4722 0.4053 0.4433 -0.0512 -0.0092 0.0060  476 ASP B CG  
4776  O OD1 . ASP B 175 ? 0.4768 0.3962 0.4380 -0.0484 -0.0082 0.0098  476 ASP B OD1 
4777  O OD2 . ASP B 175 ? 0.4672 0.4017 0.4434 -0.0538 -0.0113 0.0021  476 ASP B OD2 
4778  N N   . PHE B 176 ? 0.2968 0.2609 0.2693 -0.0383 -0.0088 0.0084  477 PHE B N   
4779  C CA  . PHE B 176 ? 0.3571 0.3341 0.3346 -0.0359 -0.0098 0.0056  477 PHE B CA  
4780  C C   . PHE B 176 ? 0.3836 0.3660 0.3695 -0.0363 -0.0124 0.0010  477 PHE B C   
4781  O O   . PHE B 176 ? 0.3611 0.3378 0.3471 -0.0349 -0.0150 -0.0001 477 PHE B O   
4782  C CB  . PHE B 176 ? 0.2754 0.2528 0.2478 -0.0296 -0.0121 0.0062  477 PHE B CB  
4783  C CG  . PHE B 176 ? 0.3251 0.3002 0.2891 -0.0285 -0.0098 0.0103  477 PHE B CG  
4784  C CD1 . PHE B 176 ? 0.3571 0.3208 0.3130 -0.0284 -0.0085 0.0148  477 PHE B CD1 
4785  C CD2 . PHE B 176 ? 0.2825 0.2657 0.2451 -0.0272 -0.0089 0.0096  477 PHE B CD2 
4786  C CE1 . PHE B 176 ? 0.4163 0.3772 0.3632 -0.0269 -0.0065 0.0190  477 PHE B CE1 
4787  C CE2 . PHE B 176 ? 0.4009 0.3818 0.3545 -0.0260 -0.0068 0.0133  477 PHE B CE2 
4788  C CZ  . PHE B 176 ? 0.3848 0.3550 0.3307 -0.0259 -0.0057 0.0182  477 PHE B CZ  
4789  N N   . ARG B 177 ? 0.3364 0.3297 0.3287 -0.0377 -0.0116 -0.0014 478 ARG B N   
4790  C CA  . ARG B 177 ? 0.3355 0.3345 0.3349 -0.0374 -0.0141 -0.0055 478 ARG B CA  
4791  C C   . ARG B 177 ? 0.3552 0.3645 0.3575 -0.0345 -0.0138 -0.0076 478 ARG B C   
4792  O O   . ARG B 177 ? 0.2952 0.3105 0.2977 -0.0354 -0.0106 -0.0066 478 ARG B O   
4793  C CB  . ARG B 177 ? 0.3309 0.3321 0.3362 -0.0433 -0.0134 -0.0065 478 ARG B CB  
4794  C CG  . ARG B 177 ? 0.3483 0.3375 0.3502 -0.0468 -0.0138 -0.0054 478 ARG B CG  
4795  C CD  . ARG B 177 ? 0.3048 0.2875 0.3049 -0.0428 -0.0175 -0.0072 478 ARG B CD  
4796  N NE  . ARG B 177 ? 0.3902 0.3801 0.3966 -0.0419 -0.0202 -0.0112 478 ARG B NE  
4797  C CZ  . ARG B 177 ? 0.4287 0.4183 0.4383 -0.0457 -0.0217 -0.0136 478 ARG B CZ  
4798  N NH1 . ARG B 177 ? 0.3337 0.3158 0.3413 -0.0514 -0.0204 -0.0126 478 ARG B NH1 
4799  N NH2 . ARG B 177 ? 0.4441 0.4402 0.4582 -0.0439 -0.0244 -0.0169 478 ARG B NH2 
4800  N N   . VAL B 178 ? 0.3234 0.3340 0.3272 -0.0309 -0.0168 -0.0105 479 VAL B N   
4801  C CA  . VAL B 178 ? 0.3601 0.3790 0.3672 -0.0283 -0.0167 -0.0132 479 VAL B CA  
4802  C C   . VAL B 178 ? 0.3344 0.3590 0.3490 -0.0305 -0.0176 -0.0151 479 VAL B C   
4803  O O   . VAL B 178 ? 0.3318 0.3523 0.3474 -0.0310 -0.0203 -0.0163 479 VAL B O   
4804  C CB  . VAL B 178 ? 0.4003 0.4162 0.4041 -0.0239 -0.0193 -0.0152 479 VAL B CB  
4805  C CG1 . VAL B 178 ? 0.3741 0.3959 0.3794 -0.0207 -0.0189 -0.0178 479 VAL B CG1 
4806  C CG2 . VAL B 178 ? 0.3164 0.3275 0.3131 -0.0226 -0.0193 -0.0135 479 VAL B CG2 
4807  N N   . TRP B 179 ? 0.2989 0.3338 0.3185 -0.0317 -0.0152 -0.0155 480 TRP B N   
4808  C CA  . TRP B 179 ? 0.3306 0.3732 0.3580 -0.0341 -0.0165 -0.0173 480 TRP B CA  
4809  C C   . TRP B 179 ? 0.3082 0.3535 0.3371 -0.0288 -0.0196 -0.0203 480 TRP B C   
4810  O O   . TRP B 179 ? 0.3353 0.3830 0.3683 -0.0299 -0.0223 -0.0221 480 TRP B O   
4811  C CB  . TRP B 179 ? 0.2851 0.3403 0.3186 -0.0373 -0.0130 -0.0167 480 TRP B CB  
4812  C CG  . TRP B 179 ? 0.2504 0.3019 0.2833 -0.0448 -0.0103 -0.0138 480 TRP B CG  
4813  C CD1 . TRP B 179 ? 0.2435 0.2818 0.2684 -0.0462 -0.0095 -0.0110 480 TRP B CD1 
4814  C CD2 . TRP B 179 ? 0.2417 0.3021 0.2815 -0.0520 -0.0083 -0.0135 480 TRP B CD2 
4815  N NE1 . TRP B 179 ? 0.2914 0.3279 0.3167 -0.0535 -0.0067 -0.0087 480 TRP B NE1 
4816  C CE2 . TRP B 179 ? 0.2505 0.3003 0.2850 -0.0579 -0.0058 -0.0103 480 TRP B CE2 
4817  C CE3 . TRP B 179 ? 0.2394 0.3160 0.2892 -0.0540 -0.0083 -0.0156 480 TRP B CE3 
4818  C CZ2 . TRP B 179 ? 0.3260 0.3795 0.3644 -0.0667 -0.0031 -0.0092 480 TRP B CZ2 
4819  C CZ3 . TRP B 179 ? 0.2973 0.3803 0.3525 -0.0630 -0.0059 -0.0148 480 TRP B CZ3 
4820  C CH2 . TRP B 179 ? 0.3198 0.3904 0.3689 -0.0698 -0.0031 -0.0116 480 TRP B CH2 
4821  N N   . ASN B 180 ? 0.3029 0.3466 0.3275 -0.0233 -0.0194 -0.0210 481 ASN B N   
4822  C CA  . ASN B 180 ? 0.2908 0.3332 0.3143 -0.0182 -0.0221 -0.0233 481 ASN B CA  
4823  C C   . ASN B 180 ? 0.3094 0.3427 0.3304 -0.0192 -0.0253 -0.0237 481 ASN B C   
4824  O O   . ASN B 180 ? 0.2563 0.2819 0.2738 -0.0215 -0.0253 -0.0223 481 ASN B O   
4825  C CB  . ASN B 180 ? 0.2487 0.2870 0.2655 -0.0133 -0.0210 -0.0238 481 ASN B CB  
4826  C CG  . ASN B 180 ? 0.3115 0.3571 0.3288 -0.0120 -0.0172 -0.0234 481 ASN B CG  
4827  O OD1 . ASN B 180 ? 0.2996 0.3461 0.3165 -0.0155 -0.0148 -0.0213 481 ASN B OD1 
4828  N ND2 . ASN B 180 ? 0.2819 0.3321 0.2990 -0.0063 -0.0165 -0.0251 481 ASN B ND2 
4829  N N   . SER B 181 ? 0.2738 0.3082 0.2962 -0.0168 -0.0279 -0.0256 482 SER B N   
4830  C CA  . SER B 181 ? 0.2847 0.3106 0.3039 -0.0172 -0.0305 -0.0261 482 SER B CA  
4831  C C   . SER B 181 ? 0.2688 0.2865 0.2812 -0.0141 -0.0305 -0.0261 482 SER B C   
4832  O O   . SER B 181 ? 0.3029 0.3138 0.3122 -0.0154 -0.0312 -0.0255 482 SER B O   
4833  C CB  . SER B 181 ? 0.3262 0.3559 0.3482 -0.0159 -0.0334 -0.0280 482 SER B CB  
4834  O OG  . SER B 181 ? 0.3022 0.3369 0.3242 -0.0105 -0.0337 -0.0290 482 SER B OG  
4835  N N   . GLN B 182 ? 0.2190 0.2376 0.2288 -0.0101 -0.0296 -0.0268 483 GLN B N   
4836  C CA  . GLN B 182 ? 0.3076 0.3185 0.3104 -0.0086 -0.0290 -0.0270 483 GLN B CA  
4837  C C   . GLN B 182 ? 0.3070 0.3204 0.3080 -0.0072 -0.0265 -0.0269 483 GLN B C   
4838  O O   . GLN B 182 ? 0.3098 0.3310 0.3144 -0.0054 -0.0250 -0.0271 483 GLN B O   
4839  C CB  . GLN B 182 ? 0.3742 0.3794 0.3723 -0.0050 -0.0303 -0.0284 483 GLN B CB  
4840  C CG  . GLN B 182 ? 0.4509 0.4520 0.4485 -0.0059 -0.0324 -0.0285 483 GLN B CG  
4841  C CD  . GLN B 182 ? 0.4948 0.4923 0.4883 -0.0015 -0.0334 -0.0295 483 GLN B CD  
4842  O OE1 . GLN B 182 ? 0.4325 0.4223 0.4190 0.0005  -0.0326 -0.0299 483 GLN B OE1 
4843  N NE2 . GLN B 182 ? 0.3331 0.3357 0.3301 0.0001  -0.0353 -0.0299 483 GLN B NE2 
4844  N N   . LEU B 183 ? 0.2706 0.2778 0.2655 -0.0077 -0.0259 -0.0269 484 LEU B N   
4845  C CA  . LEU B 183 ? 0.3805 0.3889 0.3720 -0.0064 -0.0235 -0.0271 484 LEU B CA  
4846  C C   . LEU B 183 ? 0.4010 0.4096 0.3899 -0.0011 -0.0224 -0.0290 484 LEU B C   
4847  O O   . LEU B 183 ? 0.2920 0.3066 0.2818 0.0011  -0.0199 -0.0291 484 LEU B O   
4848  C CB  . LEU B 183 ? 0.3113 0.3129 0.2959 -0.0082 -0.0239 -0.0274 484 LEU B CB  
4849  C CG  . LEU B 183 ? 0.2369 0.2392 0.2232 -0.0120 -0.0249 -0.0253 484 LEU B CG  
4850  C CD1 . LEU B 183 ? 0.2340 0.2321 0.2139 -0.0133 -0.0256 -0.0259 484 LEU B CD1 
4851  C CD2 . LEU B 183 ? 0.2295 0.2378 0.2195 -0.0131 -0.0230 -0.0231 484 LEU B CD2 
4852  N N   . ILE B 184 ? 0.2385 0.2404 0.2237 0.0013  -0.0239 -0.0303 485 ILE B N   
4853  C CA  . ILE B 184 ? 0.2455 0.2450 0.2265 0.0075  -0.0230 -0.0319 485 ILE B CA  
4854  C C   . ILE B 184 ? 0.3071 0.3099 0.2925 0.0100  -0.0251 -0.0317 485 ILE B C   
4855  O O   . ILE B 184 ? 0.2986 0.2957 0.2827 0.0080  -0.0272 -0.0315 485 ILE B O   
4856  C CB  . ILE B 184 ? 0.3450 0.3307 0.3147 0.0084  -0.0228 -0.0335 485 ILE B CB  
4857  C CG1 . ILE B 184 ? 0.4484 0.4322 0.4138 0.0055  -0.0214 -0.0341 485 ILE B CG1 
4858  C CG2 . ILE B 184 ? 0.2643 0.2449 0.2281 0.0157  -0.0218 -0.0351 485 ILE B CG2 
4859  C CD1 . ILE B 184 ? 0.5685 0.5391 0.5228 0.0047  -0.0215 -0.0361 485 ILE B CD1 
4860  N N   . ARG B 185 ? 0.3026 0.3160 0.2935 0.0141  -0.0245 -0.0319 486 ARG B N   
4861  C CA  . ARG B 185 ? 0.3167 0.3348 0.3111 0.0179  -0.0267 -0.0320 486 ARG B CA  
4862  C C   . ARG B 185 ? 0.4127 0.4391 0.4084 0.0253  -0.0250 -0.0328 486 ARG B C   
4863  O O   . ARG B 185 ? 0.3871 0.4177 0.3831 0.0262  -0.0219 -0.0331 486 ARG B O   
4864  C CB  . ARG B 185 ? 0.3072 0.3357 0.3115 0.0131  -0.0287 -0.0312 486 ARG B CB  
4865  C CG  . ARG B 185 ? 0.3210 0.3429 0.3248 0.0067  -0.0301 -0.0304 486 ARG B CG  
4866  C CD  . ARG B 185 ? 0.3411 0.3703 0.3520 0.0038  -0.0325 -0.0304 486 ARG B CD  
4867  N NE  . ARG B 185 ? 0.4322 0.4601 0.4410 0.0082  -0.0352 -0.0312 486 ARG B NE  
4868  C CZ  . ARG B 185 ? 0.4448 0.4762 0.4570 0.0063  -0.0381 -0.0316 486 ARG B CZ  
4869  N NH1 . ARG B 185 ? 0.3515 0.3866 0.3692 0.0000  -0.0385 -0.0314 486 ARG B NH1 
4870  N NH2 . ARG B 185 ? 0.3711 0.4010 0.3800 0.0109  -0.0407 -0.0321 486 ARG B NH2 
4871  N N   . TYR B 186 ? 0.2502 0.2799 0.2468 0.0310  -0.0271 -0.0332 487 TYR B N   
4872  C CA  . TYR B 186 ? 0.2821 0.3214 0.2806 0.0394  -0.0258 -0.0339 487 TYR B CA  
4873  C C   . TYR B 186 ? 0.2688 0.3293 0.2810 0.0381  -0.0269 -0.0336 487 TYR B C   
4874  O O   . TYR B 186 ? 0.3224 0.3873 0.3403 0.0328  -0.0299 -0.0332 487 TYR B O   
4875  C CB  . TYR B 186 ? 0.2655 0.2954 0.2553 0.0481  -0.0275 -0.0342 487 TYR B CB  
4876  C CG  . TYR B 186 ? 0.3923 0.4005 0.3676 0.0492  -0.0260 -0.0347 487 TYR B CG  
4877  C CD1 . TYR B 186 ? 0.3930 0.3864 0.3602 0.0480  -0.0280 -0.0342 487 TYR B CD1 
4878  C CD2 . TYR B 186 ? 0.3079 0.3104 0.2770 0.0511  -0.0223 -0.0359 487 TYR B CD2 
4879  C CE1 . TYR B 186 ? 0.4625 0.4361 0.4164 0.0478  -0.0265 -0.0347 487 TYR B CE1 
4880  C CE2 . TYR B 186 ? 0.3331 0.3152 0.2883 0.0512  -0.0212 -0.0368 487 TYR B CE2 
4881  C CZ  . TYR B 186 ? 0.4014 0.3692 0.3494 0.0492  -0.0233 -0.0362 487 TYR B CZ  
4882  O OH  . TYR B 186 ? 0.3451 0.2926 0.2792 0.0480  -0.0220 -0.0372 487 TYR B OH  
4883  N N   . ALA B 187 ? 0.2541 0.3281 0.2713 0.0428  -0.0243 -0.0340 488 ALA B N   
4884  C CA  . ALA B 187 ? 0.3378 0.4342 0.3689 0.0410  -0.0248 -0.0340 488 ALA B CA  
4885  C C   . ALA B 187 ? 0.3453 0.4496 0.3797 0.0465  -0.0292 -0.0345 488 ALA B C   
4886  O O   . ALA B 187 ? 0.3056 0.3991 0.3309 0.0544  -0.0309 -0.0347 488 ALA B O   
4887  C CB  . ALA B 187 ? 0.3520 0.4621 0.3876 0.0452  -0.0203 -0.0342 488 ALA B CB  
4888  N N   . GLY B 188 ? 0.3474 0.4703 0.3942 0.0419  -0.0312 -0.0347 489 GLY B N   
4889  C CA  . GLY B 188 ? 0.3308 0.4663 0.3828 0.0468  -0.0356 -0.0354 489 GLY B CA  
4890  C C   . GLY B 188 ? 0.3623 0.5250 0.4288 0.0464  -0.0347 -0.0360 489 GLY B C   
4891  O O   . GLY B 188 ? 0.2451 0.4162 0.3196 0.0371  -0.0322 -0.0358 489 GLY B O   
4892  N N   . TYR B 189 ? 0.3371 0.5136 0.4068 0.0568  -0.0366 -0.0367 490 TYR B N   
4893  C CA  . TYR B 189 ? 0.3683 0.5739 0.4528 0.0579  -0.0356 -0.0374 490 TYR B CA  
4894  C C   . TYR B 189 ? 0.4161 0.6380 0.5074 0.0614  -0.0419 -0.0384 490 TYR B C   
4895  O O   . TYR B 189 ? 0.4044 0.6217 0.4884 0.0733  -0.0447 -0.0383 490 TYR B O   
4896  C CB  . TYR B 189 ? 0.3007 0.5115 0.3833 0.0695  -0.0309 -0.0372 490 TYR B CB  
4897  C CG  . TYR B 189 ? 0.3168 0.5084 0.3890 0.0686  -0.0253 -0.0365 490 TYR B CG  
4898  C CD1 . TYR B 189 ? 0.3159 0.4825 0.3717 0.0760  -0.0250 -0.0364 490 TYR B CD1 
4899  C CD2 . TYR B 189 ? 0.3192 0.5174 0.3972 0.0602  -0.0205 -0.0361 490 TYR B CD2 
4900  C CE1 . TYR B 189 ? 0.3308 0.4807 0.3770 0.0747  -0.0203 -0.0363 490 TYR B CE1 
4901  C CE2 . TYR B 189 ? 0.3215 0.5030 0.3894 0.0597  -0.0158 -0.0355 490 TYR B CE2 
4902  C CZ  . TYR B 189 ? 0.3769 0.5349 0.4293 0.0669  -0.0159 -0.0359 490 TYR B CZ  
4903  O OH  . TYR B 189 ? 0.3787 0.5210 0.4210 0.0657  -0.0117 -0.0358 490 TYR B OH  
4904  N N   . LYS B 190 ? 0.3768 0.6171 0.4811 0.0512  -0.0442 -0.0394 491 LYS B N   
4905  C CA  . LYS B 190 ? 0.4063 0.6671 0.5190 0.0539  -0.0503 -0.0409 491 LYS B CA  
4906  C C   . LYS B 190 ? 0.3810 0.6677 0.5031 0.0647  -0.0490 -0.0411 491 LYS B C   
4907  O O   . LYS B 190 ? 0.4006 0.7026 0.5322 0.0617  -0.0438 -0.0410 491 LYS B O   
4908  C CB  . LYS B 190 ? 0.4423 0.7154 0.5661 0.0387  -0.0530 -0.0424 491 LYS B CB  
4909  C CG  . LYS B 190 ? 0.5456 0.8264 0.6712 0.0388  -0.0611 -0.0443 491 LYS B CG  
4910  C CD  . LYS B 190 ? 0.6603 0.9123 0.7707 0.0379  -0.0639 -0.0439 491 LYS B CD  
4911  C CE  . LYS B 190 ? 0.7349 0.9915 0.8426 0.0433  -0.0716 -0.0451 491 LYS B CE  
4912  N NZ  . LYS B 190 ? 0.7671 1.0470 0.8876 0.0344  -0.0766 -0.0480 491 LYS B NZ  
4913  N N   . GLN B 191 ? 0.2984 0.5898 0.4172 0.0781  -0.0533 -0.0413 492 GLN B N   
4914  C CA  . GLN B 191 ? 0.3930 0.7104 0.5207 0.0902  -0.0526 -0.0415 492 GLN B CA  
4915  C C   . GLN B 191 ? 0.3930 0.7447 0.5389 0.0848  -0.0574 -0.0434 492 GLN B C   
4916  O O   . GLN B 191 ? 0.3463 0.6979 0.4943 0.0747  -0.0627 -0.0447 492 GLN B O   
4917  C CB  . GLN B 191 ? 0.4338 0.7395 0.5482 0.1084  -0.0549 -0.0405 492 GLN B CB  
4918  C CG  . GLN B 191 ? 0.5072 0.7769 0.6021 0.1127  -0.0510 -0.0390 492 GLN B CG  
4919  C CD  . GLN B 191 ? 0.6083 0.8763 0.7016 0.1178  -0.0433 -0.0387 492 GLN B CD  
4920  O OE1 . GLN B 191 ? 0.5909 0.8831 0.6981 0.1153  -0.0399 -0.0393 492 GLN B OE1 
4921  N NE2 . GLN B 191 ? 0.7268 0.9658 0.8025 0.1246  -0.0404 -0.0377 492 GLN B NE2 
4922  N N   . PRO B 192 ? 0.4394 0.8215 0.5987 0.0910  -0.0554 -0.0439 493 PRO B N   
4923  C CA  . PRO B 192 ? 0.4107 0.8286 0.5883 0.0861  -0.0604 -0.0459 493 PRO B CA  
4924  C C   . PRO B 192 ? 0.4141 0.8338 0.5881 0.0920  -0.0698 -0.0468 493 PRO B C   
4925  O O   . PRO B 192 ? 0.3248 0.7633 0.5096 0.0821  -0.0754 -0.0490 493 PRO B O   
4926  C CB  . PRO B 192 ? 0.3504 0.7982 0.5401 0.0970  -0.0562 -0.0458 493 PRO B CB  
4927  C CG  . PRO B 192 ? 0.3847 0.8125 0.5651 0.0997  -0.0472 -0.0440 493 PRO B CG  
4928  C CD  . PRO B 192 ? 0.3716 0.7580 0.5307 0.1015  -0.0481 -0.0428 493 PRO B CD  
4929  N N   . ASP B 193 ? 0.2792 0.6786 0.4371 0.1073  -0.0715 -0.0452 494 ASP B N   
4930  C CA  . ASP B 193 ? 0.3490 0.7499 0.5018 0.1147  -0.0802 -0.0456 494 ASP B CA  
4931  C C   . ASP B 193 ? 0.3402 0.7138 0.4809 0.1044  -0.0839 -0.0458 494 ASP B C   
4932  O O   . ASP B 193 ? 0.3828 0.7505 0.5149 0.1110  -0.0904 -0.0457 494 ASP B O   
4933  C CB  . ASP B 193 ? 0.3494 0.7418 0.4897 0.1367  -0.0803 -0.0434 494 ASP B CB  
4934  C CG  . ASP B 193 ? 0.4261 0.7767 0.5449 0.1408  -0.0758 -0.0411 494 ASP B CG  
4935  O OD1 . ASP B 193 ? 0.4620 0.7919 0.5765 0.1275  -0.0720 -0.0411 494 ASP B OD1 
4936  O OD2 . ASP B 193 ? 0.4859 0.8242 0.5916 0.1576  -0.0760 -0.0393 494 ASP B OD2 
4937  N N   . GLY B 194 ? 0.3490 0.7066 0.4888 0.0890  -0.0799 -0.0461 495 GLY B N   
4938  C CA  . GLY B 194 ? 0.3801 0.7123 0.5089 0.0795  -0.0825 -0.0464 495 GLY B CA  
4939  C C   . GLY B 194 ? 0.4473 0.7431 0.5562 0.0859  -0.0796 -0.0439 495 GLY B C   
4940  O O   . GLY B 194 ? 0.4501 0.7234 0.5502 0.0769  -0.0799 -0.0439 495 GLY B O   
4941  N N   . SER B 195 ? 0.3970 0.6862 0.4979 0.1011  -0.0769 -0.0420 496 SER B N   
4942  C CA  . SER B 195 ? 0.4066 0.6607 0.4887 0.1052  -0.0735 -0.0398 496 SER B CA  
4943  C C   . SER B 195 ? 0.4849 0.7259 0.5671 0.0945  -0.0666 -0.0396 496 SER B C   
4944  O O   . SER B 195 ? 0.5046 0.7633 0.6003 0.0872  -0.0635 -0.0406 496 SER B O   
4945  C CB  . SER B 195 ? 0.3798 0.6280 0.4519 0.1238  -0.0720 -0.0380 496 SER B CB  
4946  O OG  . SER B 195 ? 0.3602 0.6184 0.4388 0.1275  -0.0660 -0.0380 496 SER B OG  
4947  N N   . THR B 196 ? 0.4506 0.6608 0.5177 0.0932  -0.0643 -0.0383 497 THR B N   
4948  C CA  . THR B 196 ? 0.4398 0.6355 0.5047 0.0846  -0.0582 -0.0379 497 THR B CA  
4949  C C   . THR B 196 ? 0.4165 0.5912 0.4673 0.0947  -0.0538 -0.0365 497 THR B C   
4950  O O   . THR B 196 ? 0.4953 0.6536 0.5327 0.1036  -0.0556 -0.0353 497 THR B O   
4951  C CB  . THR B 196 ? 0.4911 0.6697 0.5516 0.0719  -0.0593 -0.0381 497 THR B CB  
4952  O OG1 . THR B 196 ? 0.5098 0.7059 0.5815 0.0631  -0.0638 -0.0398 497 THR B OG1 
4953  C CG2 . THR B 196 ? 0.4552 0.6221 0.5149 0.0630  -0.0535 -0.0376 497 THR B CG2 
4954  N N   . LEU B 197 ? 0.3463 0.5212 0.3993 0.0932  -0.0479 -0.0365 498 LEU B N   
4955  C CA  . LEU B 197 ? 0.3167 0.4692 0.3554 0.0998  -0.0433 -0.0357 498 LEU B CA  
4956  C C   . LEU B 197 ? 0.3637 0.4966 0.3969 0.0877  -0.0406 -0.0355 498 LEU B C   
4957  O O   . LEU B 197 ? 0.4101 0.5520 0.4532 0.0764  -0.0396 -0.0359 498 LEU B O   
4958  C CB  . LEU B 197 ? 0.3997 0.5656 0.4430 0.1076  -0.0384 -0.0362 498 LEU B CB  
4959  C CG  . LEU B 197 ? 0.4382 0.5827 0.4675 0.1136  -0.0330 -0.0361 498 LEU B CG  
4960  C CD1 . LEU B 197 ? 0.4127 0.5342 0.4245 0.1247  -0.0346 -0.0353 498 LEU B CD1 
4961  C CD2 . LEU B 197 ? 0.4436 0.6061 0.4798 0.1207  -0.0282 -0.0369 498 LEU B CD2 
4962  N N   . GLY B 198 ? 0.3973 0.5036 0.4147 0.0901  -0.0397 -0.0347 499 GLY B N   
4963  C CA  . GLY B 198 ? 0.3059 0.3947 0.3182 0.0793  -0.0377 -0.0345 499 GLY B CA  
4964  C C   . GLY B 198 ? 0.3743 0.4598 0.3882 0.0703  -0.0417 -0.0342 499 GLY B C   
4965  O O   . GLY B 198 ? 0.4288 0.5153 0.4409 0.0740  -0.0459 -0.0339 499 GLY B O   
4966  N N   . ASP B 199 ? 0.3624 0.4440 0.3793 0.0590  -0.0402 -0.0342 500 ASP B N   
4967  C CA  . ASP B 199 ? 0.3620 0.4367 0.3782 0.0507  -0.0431 -0.0340 500 ASP B CA  
4968  C C   . ASP B 199 ? 0.3390 0.4331 0.3686 0.0444  -0.0458 -0.0349 500 ASP B C   
4969  O O   . ASP B 199 ? 0.3408 0.4437 0.3788 0.0371  -0.0436 -0.0351 500 ASP B O   
4970  C CB  . ASP B 199 ? 0.4142 0.4738 0.4256 0.0427  -0.0401 -0.0335 500 ASP B CB  
4971  C CG  . ASP B 199 ? 0.4107 0.4613 0.4197 0.0358  -0.0425 -0.0332 500 ASP B CG  
4972  O OD1 . ASP B 199 ? 0.3918 0.4511 0.4061 0.0338  -0.0461 -0.0338 500 ASP B OD1 
4973  O OD2 . ASP B 199 ? 0.3981 0.4332 0.3997 0.0324  -0.0408 -0.0327 500 ASP B OD2 
4974  N N   . PRO B 200 ? 0.3353 0.4353 0.3662 0.0460  -0.0507 -0.0355 501 PRO B N   
4975  C CA  . PRO B 200 ? 0.2700 0.3884 0.3131 0.0392  -0.0537 -0.0369 501 PRO B CA  
4976  C C   . PRO B 200 ? 0.2945 0.4074 0.3402 0.0268  -0.0527 -0.0372 501 PRO B C   
4977  O O   . PRO B 200 ? 0.3019 0.4289 0.3582 0.0195  -0.0530 -0.0382 501 PRO B O   
4978  C CB  . PRO B 200 ? 0.3382 0.4578 0.3777 0.0438  -0.0595 -0.0374 501 PRO B CB  
4979  C CG  . PRO B 200 ? 0.3021 0.4110 0.3304 0.0559  -0.0589 -0.0360 501 PRO B CG  
4980  C CD  . PRO B 200 ? 0.2947 0.3849 0.3151 0.0546  -0.0537 -0.0348 501 PRO B CD  
4981  N N   . ALA B 201 ? 0.3540 0.4468 0.3902 0.0243  -0.0514 -0.0362 502 ALA B N   
4982  C CA  . ALA B 201 ? 0.4046 0.4908 0.4420 0.0141  -0.0503 -0.0362 502 ALA B CA  
4983  C C   . ALA B 201 ? 0.3342 0.4268 0.3785 0.0089  -0.0462 -0.0357 502 ALA B C   
4984  O O   . ALA B 201 ? 0.3123 0.4040 0.3598 0.0003  -0.0456 -0.0357 502 ALA B O   
4985  C CB  . ALA B 201 ? 0.3517 0.4171 0.3780 0.0139  -0.0490 -0.0351 502 ALA B CB  
4986  N N   . ASN B 202 ? 0.2881 0.3862 0.3335 0.0142  -0.0432 -0.0351 503 ASN B N   
4987  C CA  . ASN B 202 ? 0.3319 0.4330 0.3810 0.0100  -0.0386 -0.0341 503 ASN B CA  
4988  C C   . ASN B 202 ? 0.3186 0.4415 0.3791 0.0099  -0.0374 -0.0346 503 ASN B C   
4989  O O   . ASN B 202 ? 0.2981 0.4255 0.3612 0.0085  -0.0329 -0.0337 503 ASN B O   
4990  C CB  . ASN B 202 ? 0.2629 0.3512 0.3027 0.0153  -0.0353 -0.0332 503 ASN B CB  
4991  C CG  . ASN B 202 ? 0.3279 0.3969 0.3583 0.0127  -0.0357 -0.0326 503 ASN B CG  
4992  O OD1 . ASN B 202 ? 0.3795 0.4447 0.4111 0.0057  -0.0367 -0.0323 503 ASN B OD1 
4993  N ND2 . ASN B 202 ? 0.3016 0.3582 0.3223 0.0183  -0.0348 -0.0325 503 ASN B ND2 
4994  N N   . VAL B 203 ? 0.3054 0.4429 0.3727 0.0114  -0.0412 -0.0361 504 VAL B N   
4995  C CA  . VAL B 203 ? 0.3355 0.4971 0.4151 0.0114  -0.0404 -0.0367 504 VAL B CA  
4996  C C   . VAL B 203 ? 0.4184 0.5863 0.5055 -0.0002 -0.0373 -0.0362 504 VAL B C   
4997  O O   . VAL B 203 ? 0.3072 0.4864 0.3999 -0.0006 -0.0328 -0.0354 504 VAL B O   
4998  C CB  . VAL B 203 ? 0.3716 0.5480 0.4571 0.0141  -0.0461 -0.0386 504 VAL B CB  
4999  C CG1 . VAL B 203 ? 0.3605 0.5634 0.4610 0.0091  -0.0458 -0.0396 504 VAL B CG1 
5000  C CG2 . VAL B 203 ? 0.3584 0.5333 0.4376 0.0280  -0.0478 -0.0385 504 VAL B CG2 
5001  N N   . GLN B 204 ? 0.3953 0.5548 0.4815 -0.0096 -0.0393 -0.0366 505 GLN B N   
5002  C CA  . GLN B 204 ? 0.3364 0.4992 0.4280 -0.0210 -0.0364 -0.0359 505 GLN B CA  
5003  C C   . GLN B 204 ? 0.3166 0.4693 0.4031 -0.0214 -0.0306 -0.0333 505 GLN B C   
5004  O O   . GLN B 204 ? 0.2826 0.4454 0.3748 -0.0257 -0.0263 -0.0322 505 GLN B O   
5005  C CB  . GLN B 204 ? 0.3769 0.5280 0.4655 -0.0297 -0.0395 -0.0368 505 GLN B CB  
5006  C CG  . GLN B 204 ? 0.6116 0.7705 0.7077 -0.0420 -0.0379 -0.0369 505 GLN B CG  
5007  C CD  . GLN B 204 ? 0.6901 0.8301 0.7794 -0.0503 -0.0385 -0.0368 505 GLN B CD  
5008  O OE1 . GLN B 204 ? 0.6186 0.7421 0.6989 -0.0470 -0.0408 -0.0371 505 GLN B OE1 
5009  N NE2 . GLN B 204 ? 0.6891 0.8310 0.7822 -0.0611 -0.0361 -0.0363 505 GLN B NE2 
5010  N N   . PHE B 205 ? 0.2787 0.4118 0.3541 -0.0174 -0.0304 -0.0324 506 PHE B N   
5011  C CA  . PHE B 205 ? 0.3310 0.4548 0.4008 -0.0178 -0.0257 -0.0302 506 PHE B CA  
5012  C C   . PHE B 205 ? 0.3446 0.4793 0.4164 -0.0110 -0.0219 -0.0299 506 PHE B C   
5013  O O   . PHE B 205 ? 0.2403 0.3766 0.3120 -0.0134 -0.0172 -0.0283 506 PHE B O   
5014  C CB  . PHE B 205 ? 0.3457 0.4488 0.4041 -0.0148 -0.0268 -0.0297 506 PHE B CB  
5015  C CG  . PHE B 205 ? 0.3785 0.4726 0.4308 -0.0152 -0.0227 -0.0277 506 PHE B CG  
5016  C CD1 . PHE B 205 ? 0.4285 0.5161 0.4794 -0.0226 -0.0209 -0.0258 506 PHE B CD1 
5017  C CD2 . PHE B 205 ? 0.3616 0.4532 0.4084 -0.0079 -0.0207 -0.0278 506 PHE B CD2 
5018  C CE1 . PHE B 205 ? 0.4057 0.4859 0.4505 -0.0225 -0.0176 -0.0239 506 PHE B CE1 
5019  C CE2 . PHE B 205 ? 0.3925 0.4764 0.4332 -0.0085 -0.0174 -0.0264 506 PHE B CE2 
5020  C CZ  . PHE B 205 ? 0.2994 0.3782 0.3392 -0.0157 -0.0160 -0.0243 506 PHE B CZ  
5021  N N   . THR B 206 ? 0.3185 0.4599 0.3909 -0.0018 -0.0238 -0.0314 507 THR B N   
5022  C CA  . THR B 206 ? 0.2887 0.4413 0.3630 0.0058  -0.0202 -0.0315 507 THR B CA  
5023  C C   . THR B 206 ? 0.3522 0.5272 0.4391 0.0007  -0.0172 -0.0312 507 THR B C   
5024  O O   . THR B 206 ? 0.3478 0.5286 0.4353 0.0018  -0.0119 -0.0302 507 THR B O   
5025  C CB  . THR B 206 ? 0.2408 0.3957 0.3130 0.0170  -0.0233 -0.0331 507 THR B CB  
5026  O OG1 . THR B 206 ? 0.2730 0.4055 0.3325 0.0205  -0.0251 -0.0330 507 THR B OG1 
5027  C CG2 . THR B 206 ? 0.2531 0.4190 0.3264 0.0265  -0.0196 -0.0334 507 THR B CG2 
5028  N N   . GLU B 207 ? 0.3123 0.5002 0.4090 -0.0056 -0.0204 -0.0322 508 GLU B N   
5029  C CA  . GLU B 207 ? 0.3711 0.5808 0.4804 -0.0126 -0.0176 -0.0319 508 GLU B CA  
5030  C C   . GLU B 207 ? 0.3275 0.5299 0.4345 -0.0218 -0.0123 -0.0295 508 GLU B C   
5031  O O   . GLU B 207 ? 0.3314 0.5476 0.4441 -0.0237 -0.0070 -0.0283 508 GLU B O   
5032  C CB  . GLU B 207 ? 0.4399 0.6611 0.5584 -0.0199 -0.0225 -0.0337 508 GLU B CB  
5033  C CG  . GLU B 207 ? 0.5907 0.8235 0.7131 -0.0117 -0.0281 -0.0361 508 GLU B CG  
5034  C CD  . GLU B 207 ? 0.7298 0.9692 0.8583 -0.0203 -0.0337 -0.0381 508 GLU B CD  
5035  O OE1 . GLU B 207 ? 0.7651 0.9882 0.8885 -0.0294 -0.0347 -0.0380 508 GLU B OE1 
5036  O OE2 . GLU B 207 ? 0.7738 1.0350 0.9120 -0.0176 -0.0372 -0.0401 508 GLU B OE2 
5037  N N   . ILE B 208 ? 0.2994 0.4805 0.3978 -0.0274 -0.0135 -0.0284 509 ILE B N   
5038  C CA  . ILE B 208 ? 0.2523 0.4242 0.3466 -0.0351 -0.0089 -0.0257 509 ILE B CA  
5039  C C   . ILE B 208 ? 0.2951 0.4644 0.3833 -0.0285 -0.0039 -0.0242 509 ILE B C   
5040  O O   . ILE B 208 ? 0.3525 0.5286 0.4426 -0.0323 0.0016  -0.0222 509 ILE B O   
5041  C CB  . ILE B 208 ? 0.3676 0.5167 0.4528 -0.0398 -0.0115 -0.0249 509 ILE B CB  
5042  C CG1 . ILE B 208 ? 0.4312 0.5823 0.5216 -0.0476 -0.0157 -0.0265 509 ILE B CG1 
5043  C CG2 . ILE B 208 ? 0.3381 0.4759 0.4169 -0.0450 -0.0068 -0.0216 509 ILE B CG2 
5044  C CD1 . ILE B 208 ? 0.4225 0.5516 0.5038 -0.0502 -0.0187 -0.0264 509 ILE B CD1 
5045  N N   . CYS B 209 ? 0.2857 0.4445 0.3656 -0.0187 -0.0055 -0.0252 510 CYS B N   
5046  C CA  . CYS B 209 ? 0.2848 0.4402 0.3577 -0.0121 -0.0012 -0.0245 510 CYS B CA  
5047  C C   . CYS B 209 ? 0.3529 0.5300 0.4339 -0.0085 0.0032  -0.0248 510 CYS B C   
5048  O O   . CYS B 209 ? 0.3506 0.5306 0.4297 -0.0097 0.0089  -0.0231 510 CYS B O   
5049  C CB  . CYS B 209 ? 0.2777 0.4194 0.3409 -0.0026 -0.0041 -0.0261 510 CYS B CB  
5050  S SG  . CYS B 209 ? 0.3373 0.4543 0.3899 -0.0064 -0.0076 -0.0254 510 CYS B SG  
5051  N N   . ILE B 210 ? 0.3537 0.5469 0.4434 -0.0035 0.0009  -0.0268 511 ILE B N   
5052  C CA  . ILE B 210 ? 0.3437 0.5599 0.4421 0.0011  0.0051  -0.0272 511 ILE B CA  
5053  C C   . ILE B 210 ? 0.3295 0.5598 0.4368 -0.0100 0.0097  -0.0252 511 ILE B C   
5054  O O   . ILE B 210 ? 0.3374 0.5778 0.4460 -0.0087 0.0160  -0.0241 511 ILE B O   
5055  C CB  . ILE B 210 ? 0.3832 0.6158 0.4904 0.0082  0.0008  -0.0296 511 ILE B CB  
5056  C CG1 . ILE B 210 ? 0.3555 0.5725 0.4515 0.0205  -0.0023 -0.0311 511 ILE B CG1 
5057  C CG2 . ILE B 210 ? 0.3375 0.5987 0.4568 0.0116  0.0051  -0.0299 511 ILE B CG2 
5058  C CD1 . ILE B 210 ? 0.2758 0.5018 0.3768 0.0269  -0.0081 -0.0329 511 ILE B CD1 
5059  N N   . GLN B 211 ? 0.3768 0.6064 0.4891 -0.0214 0.0071  -0.0247 512 GLN B N   
5060  C CA  . GLN B 211 ? 0.3824 0.6231 0.5022 -0.0334 0.0115  -0.0227 512 GLN B CA  
5061  C C   . GLN B 211 ? 0.4116 0.6385 0.5213 -0.0366 0.0174  -0.0194 512 GLN B C   
5062  O O   . GLN B 211 ? 0.3712 0.6100 0.4853 -0.0423 0.0235  -0.0174 512 GLN B O   
5063  C CB  . GLN B 211 ? 0.3968 0.6340 0.5208 -0.0449 0.0072  -0.0231 512 GLN B CB  
5064  C CG  . GLN B 211 ? 0.5824 0.8301 0.7139 -0.0585 0.0114  -0.0213 512 GLN B CG  
5065  C CD  . GLN B 211 ? 0.7972 1.0371 0.9301 -0.0698 0.0069  -0.0221 512 GLN B CD  
5066  O OE1 . GLN B 211 ? 0.8782 1.1076 1.0076 -0.0666 0.0005  -0.0242 512 GLN B OE1 
5067  N NE2 . GLN B 211 ? 0.8152 1.0591 0.9522 -0.0831 0.0105  -0.0204 512 GLN B NE2 
5068  N N   . GLN B 212 ? 0.4103 0.6131 0.5063 -0.0330 0.0157  -0.0188 513 GLN B N   
5069  C CA  . GLN B 212 ? 0.4282 0.6172 0.5133 -0.0348 0.0202  -0.0159 513 GLN B CA  
5070  C C   . GLN B 212 ? 0.4831 0.6769 0.5634 -0.0254 0.0250  -0.0161 513 GLN B C   
5071  O O   . GLN B 212 ? 0.5000 0.6834 0.5704 -0.0261 0.0289  -0.0138 513 GLN B O   
5072  C CB  . GLN B 212 ? 0.4624 0.6256 0.5353 -0.0347 0.0160  -0.0153 513 GLN B CB  
5073  C CG  . GLN B 212 ? 0.4933 0.6480 0.5681 -0.0437 0.0121  -0.0149 513 GLN B CG  
5074  C CD  . GLN B 212 ? 0.5690 0.7288 0.6481 -0.0555 0.0161  -0.0122 513 GLN B CD  
5075  O OE1 . GLN B 212 ? 0.6171 0.7835 0.7044 -0.0630 0.0141  -0.0131 513 GLN B OE1 
5076  N NE2 . GLN B 212 ? 0.4768 0.6329 0.5496 -0.0575 0.0219  -0.0088 513 GLN B NE2 
5077  N N   . GLY B 213 ? 0.3961 0.6043 0.4820 -0.0161 0.0247  -0.0188 514 GLY B N   
5078  C CA  . GLY B 213 ? 0.4154 0.6290 0.4968 -0.0066 0.0298  -0.0194 514 GLY B CA  
5079  C C   . GLY B 213 ? 0.4356 0.6386 0.5085 0.0060  0.0266  -0.0223 514 GLY B C   
5080  O O   . GLY B 213 ? 0.4045 0.6113 0.4730 0.0151  0.0305  -0.0235 514 GLY B O   
5081  N N   . TRP B 214 ? 0.4342 0.6235 0.5040 0.0069  0.0200  -0.0237 515 TRP B N   
5082  C CA  . TRP B 214 ? 0.3430 0.5201 0.4036 0.0179  0.0172  -0.0262 515 TRP B CA  
5083  C C   . TRP B 214 ? 0.3222 0.5164 0.3892 0.0284  0.0179  -0.0284 515 TRP B C   
5084  O O   . TRP B 214 ? 0.3975 0.6095 0.4773 0.0273  0.0158  -0.0287 515 TRP B O   
5085  C CB  . TRP B 214 ? 0.3517 0.5131 0.4089 0.0158  0.0103  -0.0268 515 TRP B CB  
5086  C CG  . TRP B 214 ? 0.3764 0.5218 0.4222 0.0251  0.0079  -0.0290 515 TRP B CG  
5087  C CD1 . TRP B 214 ? 0.3893 0.5204 0.4220 0.0294  0.0102  -0.0297 515 TRP B CD1 
5088  C CD2 . TRP B 214 ? 0.3656 0.5064 0.4108 0.0306  0.0028  -0.0307 515 TRP B CD2 
5089  N NE1 . TRP B 214 ? 0.3366 0.4540 0.3608 0.0367  0.0070  -0.0318 515 TRP B NE1 
5090  C CE2 . TRP B 214 ? 0.4091 0.5318 0.4405 0.0378  0.0026  -0.0322 515 TRP B CE2 
5091  C CE3 . TRP B 214 ? 0.3027 0.4524 0.3569 0.0299  -0.0017 -0.0311 515 TRP B CE3 
5092  C CZ2 . TRP B 214 ? 0.2570 0.3695 0.2830 0.0441  -0.0014 -0.0337 515 TRP B CZ2 
5093  C CZ3 . TRP B 214 ? 0.3493 0.4897 0.3981 0.0370  -0.0059 -0.0325 515 TRP B CZ3 
5094  C CH2 . TRP B 214 ? 0.3405 0.4620 0.3752 0.0440  -0.0055 -0.0336 515 TRP B CH2 
5095  N N   . LYS B 215 ? 0.3001 0.4884 0.3575 0.0390  0.0206  -0.0300 516 LYS B N   
5096  C CA  . LYS B 215 ? 0.3607 0.5616 0.4211 0.0516  0.0215  -0.0321 516 LYS B CA  
5097  C C   . LYS B 215 ? 0.4053 0.5891 0.4573 0.0589  0.0158  -0.0339 516 LYS B C   
5098  O O   . LYS B 215 ? 0.5094 0.6718 0.5464 0.0635  0.0159  -0.0351 516 LYS B O   
5099  C CB  . LYS B 215 ? 0.5445 0.7468 0.5974 0.0596  0.0283  -0.0329 516 LYS B CB  
5100  C CG  . LYS B 215 ? 0.7186 0.9335 0.7762 0.0520  0.0347  -0.0307 516 LYS B CG  
5101  C CD  . LYS B 215 ? 0.8027 1.0484 0.8749 0.0557  0.0393  -0.0306 516 LYS B CD  
5102  C CE  . LYS B 215 ? 0.8110 1.0725 0.8940 0.0424  0.0431  -0.0276 516 LYS B CE  
5103  N NZ  . LYS B 215 ? 0.7667 1.0275 0.8581 0.0306  0.0374  -0.0263 516 LYS B NZ  
5104  N N   . PRO B 216 ? 0.4158 0.6082 0.4765 0.0596  0.0108  -0.0342 517 PRO B N   
5105  C CA  . PRO B 216 ? 0.4202 0.5948 0.4724 0.0646  0.0052  -0.0353 517 PRO B CA  
5106  C C   . PRO B 216 ? 0.4801 0.6519 0.5246 0.0800  0.0062  -0.0371 517 PRO B C   
5107  O O   . PRO B 216 ? 0.4827 0.6752 0.5351 0.0879  0.0088  -0.0376 517 PRO B O   
5108  C CB  . PRO B 216 ? 0.3736 0.5617 0.4385 0.0596  0.0000  -0.0348 517 PRO B CB  
5109  C CG  . PRO B 216 ? 0.3797 0.5981 0.4600 0.0596  0.0031  -0.0346 517 PRO B CG  
5110  C CD  . PRO B 216 ? 0.4151 0.6353 0.4937 0.0560  0.0101  -0.0336 517 PRO B CD  
5111  N N   . PRO B 217 ? 0.4905 0.6369 0.5195 0.0848  0.0043  -0.0381 518 PRO B N   
5112  C CA  . PRO B 217 ? 0.4459 0.5863 0.4661 0.0999  0.0045  -0.0398 518 PRO B CA  
5113  C C   . PRO B 217 ? 0.4212 0.5744 0.4493 0.1065  -0.0001 -0.0395 518 PRO B C   
5114  O O   . PRO B 217 ? 0.4533 0.6109 0.4787 0.1203  0.0008  -0.0404 518 PRO B O   
5115  C CB  . PRO B 217 ? 0.4257 0.5337 0.4272 0.0998  0.0032  -0.0407 518 PRO B CB  
5116  C CG  . PRO B 217 ? 0.4867 0.5874 0.4876 0.0863  0.0038  -0.0399 518 PRO B CG  
5117  C CD  . PRO B 217 ? 0.4702 0.5919 0.4882 0.0769  0.0024  -0.0379 518 PRO B CD  
5118  N N   . ARG B 218 ? 0.4658 0.6252 0.5031 0.0975  -0.0050 -0.0383 519 ARG B N   
5119  C CA  . ARG B 218 ? 0.4605 0.6310 0.5042 0.1028  -0.0102 -0.0381 519 ARG B CA  
5120  C C   . ARG B 218 ? 0.5119 0.6605 0.5398 0.1143  -0.0126 -0.0385 519 ARG B C   
5121  O O   . ARG B 218 ? 0.5785 0.7350 0.6062 0.1273  -0.0137 -0.0387 519 ARG B O   
5122  C CB  . ARG B 218 ? 0.5023 0.7057 0.5616 0.1088  -0.0089 -0.0384 519 ARG B CB  
5123  C CG  . ARG B 218 ? 0.5258 0.7499 0.6000 0.0964  -0.0060 -0.0378 519 ARG B CG  
5124  C CD  . ARG B 218 ? 0.5642 0.8235 0.6571 0.0979  -0.0069 -0.0380 519 ARG B CD  
5125  N NE  . ARG B 218 ? 0.7313 1.0031 0.8371 0.0817  -0.0081 -0.0373 519 ARG B NE  
5126  C CZ  . ARG B 218 ? 0.7845 1.0610 0.8967 0.0752  -0.0144 -0.0375 519 ARG B CZ  
5127  N NH1 . ARG B 218 ? 0.8040 1.0892 0.9261 0.0601  -0.0149 -0.0371 519 ARG B NH1 
5128  N NH2 . ARG B 218 ? 0.7431 1.0145 0.8505 0.0839  -0.0201 -0.0380 519 ARG B NH2 
5129  N N   . GLY B 219 ? 0.5190 0.6398 0.5332 0.1094  -0.0131 -0.0384 520 GLY B N   
5130  C CA  . GLY B 219 ? 0.4661 0.5631 0.4647 0.1164  -0.0156 -0.0384 520 GLY B CA  
5131  C C   . GLY B 219 ? 0.4527 0.5412 0.4513 0.1075  -0.0207 -0.0372 520 GLY B C   
5132  O O   . GLY B 219 ? 0.4228 0.5234 0.4331 0.0967  -0.0226 -0.0367 520 GLY B O   
5133  N N   . ARG B 220 ? 0.4308 0.4964 0.4147 0.1122  -0.0226 -0.0368 521 ARG B N   
5134  C CA  . ARG B 220 ? 0.3459 0.4029 0.3282 0.1055  -0.0272 -0.0357 521 ARG B CA  
5135  C C   . ARG B 220 ? 0.4180 0.4591 0.3960 0.0926  -0.0264 -0.0356 521 ARG B C   
5136  O O   . ARG B 220 ? 0.4003 0.4397 0.3811 0.0847  -0.0296 -0.0348 521 ARG B O   
5137  C CB  . ARG B 220 ? 0.3257 0.3654 0.2937 0.1158  -0.0293 -0.0348 521 ARG B CB  
5138  C CG  . ARG B 220 ? 0.3574 0.3937 0.3252 0.1115  -0.0343 -0.0334 521 ARG B CG  
5139  C CD  . ARG B 220 ? 0.3967 0.4182 0.3503 0.1235  -0.0360 -0.0321 521 ARG B CD  
5140  N NE  . ARG B 220 ? 0.5178 0.5346 0.4688 0.1208  -0.0405 -0.0305 521 ARG B NE  
5141  C CZ  . ARG B 220 ? 0.5997 0.5936 0.5340 0.1259  -0.0412 -0.0289 521 ARG B CZ  
5142  N NH1 . ARG B 220 ? 0.5960 0.5686 0.5148 0.1332  -0.0377 -0.0287 521 ARG B NH1 
5143  N NH2 . ARG B 220 ? 0.6105 0.6018 0.5428 0.1233  -0.0451 -0.0274 521 ARG B NH2 
5144  N N   . PHE B 221 ? 0.4739 0.5039 0.4450 0.0907  -0.0222 -0.0367 522 PHE B N   
5145  C CA  . PHE B 221 ? 0.4331 0.4485 0.3995 0.0795  -0.0216 -0.0367 522 PHE B CA  
5146  C C   . PHE B 221 ? 0.4193 0.4404 0.3889 0.0752  -0.0177 -0.0377 522 PHE B C   
5147  O O   . PHE B 221 ? 0.4397 0.4453 0.3985 0.0741  -0.0152 -0.0389 522 PHE B O   
5148  C CB  . PHE B 221 ? 0.4056 0.3937 0.3543 0.0812  -0.0214 -0.0370 522 PHE B CB  
5149  C CG  . PHE B 221 ? 0.4290 0.4092 0.3725 0.0848  -0.0248 -0.0356 522 PHE B CG  
5150  C CD1 . PHE B 221 ? 0.4038 0.3757 0.3374 0.0972  -0.0248 -0.0354 522 PHE B CD1 
5151  C CD2 . PHE B 221 ? 0.3993 0.3798 0.3470 0.0765  -0.0279 -0.0344 522 PHE B CD2 
5152  C CE1 . PHE B 221 ? 0.5117 0.4756 0.4393 0.1008  -0.0279 -0.0337 522 PHE B CE1 
5153  C CE2 . PHE B 221 ? 0.5256 0.4986 0.4676 0.0798  -0.0308 -0.0330 522 PHE B CE2 
5154  C CZ  . PHE B 221 ? 0.4885 0.4532 0.4203 0.0918  -0.0309 -0.0325 522 PHE B CZ  
5155  N N   . ASP B 222 ? 0.3248 0.3684 0.3090 0.0724  -0.0171 -0.0372 523 ASP B N   
5156  C CA  . ASP B 222 ? 0.3277 0.3777 0.3154 0.0673  -0.0133 -0.0375 523 ASP B CA  
5157  C C   . ASP B 222 ? 0.3316 0.3757 0.3207 0.0550  -0.0145 -0.0366 523 ASP B C   
5158  O O   . ASP B 222 ? 0.3758 0.4286 0.3743 0.0488  -0.0171 -0.0354 523 ASP B O   
5159  C CB  . ASP B 222 ? 0.2969 0.3731 0.2994 0.0683  -0.0117 -0.0371 523 ASP B CB  
5160  C CG  . ASP B 222 ? 0.3449 0.4307 0.3479 0.0812  -0.0107 -0.0379 523 ASP B CG  
5161  O OD1 . ASP B 222 ? 0.4014 0.4709 0.3909 0.0899  -0.0096 -0.0390 523 ASP B OD1 
5162  O OD2 . ASP B 222 ? 0.3841 0.4936 0.4008 0.0827  -0.0108 -0.0375 523 ASP B OD2 
5163  N N   . VAL B 223 ? 0.3508 0.3806 0.3303 0.0516  -0.0126 -0.0373 524 VAL B N   
5164  C CA  . VAL B 223 ? 0.3423 0.3692 0.3239 0.0409  -0.0136 -0.0362 524 VAL B CA  
5165  C C   . VAL B 223 ? 0.3123 0.3569 0.3057 0.0361  -0.0119 -0.0348 524 VAL B C   
5166  O O   . VAL B 223 ? 0.3083 0.3614 0.3029 0.0390  -0.0081 -0.0351 524 VAL B O   
5167  C CB  . VAL B 223 ? 0.4090 0.4196 0.3784 0.0385  -0.0122 -0.0374 524 VAL B CB  
5168  C CG1 . VAL B 223 ? 0.3660 0.3763 0.3386 0.0285  -0.0134 -0.0360 524 VAL B CG1 
5169  C CG2 . VAL B 223 ? 0.3727 0.3646 0.3300 0.0418  -0.0136 -0.0388 524 VAL B CG2 
5170  N N   . LEU B 224 ? 0.2988 0.3486 0.3003 0.0288  -0.0143 -0.0332 525 LEU B N   
5171  C CA  . LEU B 224 ? 0.3104 0.3754 0.3224 0.0235  -0.0126 -0.0317 525 LEU B CA  
5172  C C   . LEU B 224 ? 0.2788 0.3396 0.2865 0.0188  -0.0096 -0.0308 525 LEU B C   
5173  O O   . LEU B 224 ? 0.2566 0.3034 0.2554 0.0172  -0.0104 -0.0311 525 LEU B O   
5174  C CB  . LEU B 224 ? 0.2413 0.3099 0.2610 0.0168  -0.0161 -0.0306 525 LEU B CB  
5175  C CG  . LEU B 224 ? 0.2760 0.3554 0.3029 0.0203  -0.0188 -0.0314 525 LEU B CG  
5176  C CD1 . LEU B 224 ? 0.2381 0.3117 0.2659 0.0155  -0.0231 -0.0312 525 LEU B CD1 
5177  C CD2 . LEU B 224 ? 0.2484 0.3487 0.2873 0.0184  -0.0168 -0.0310 525 LEU B CD2 
5178  N N   . PRO B 225 ? 0.2444 0.3179 0.2583 0.0164  -0.0062 -0.0295 526 PRO B N   
5179  C CA  . PRO B 225 ? 0.2609 0.3303 0.2704 0.0115  -0.0036 -0.0280 526 PRO B CA  
5180  C C   . PRO B 225 ? 0.3001 0.3638 0.3111 0.0035  -0.0062 -0.0260 526 PRO B C   
5181  O O   . PRO B 225 ? 0.2804 0.3474 0.2984 0.0005  -0.0088 -0.0256 526 PRO B O   
5182  C CB  . PRO B 225 ? 0.2566 0.3426 0.2733 0.0110  0.0011  -0.0268 526 PRO B CB  
5183  C CG  . PRO B 225 ? 0.3171 0.4165 0.3456 0.0104  -0.0006 -0.0270 526 PRO B CG  
5184  C CD  . PRO B 225 ? 0.2766 0.3695 0.3022 0.0170  -0.0046 -0.0292 526 PRO B CD  
5185  N N   . LEU B 226 ? 0.2894 0.3446 0.2934 0.0005  -0.0055 -0.0248 527 LEU B N   
5186  C CA  . LEU B 226 ? 0.3051 0.3561 0.3104 -0.0062 -0.0071 -0.0225 527 LEU B CA  
5187  C C   . LEU B 226 ? 0.3320 0.3927 0.3440 -0.0111 -0.0041 -0.0199 527 LEU B C   
5188  O O   . LEU B 226 ? 0.3642 0.4325 0.3763 -0.0103 0.0001  -0.0193 527 LEU B O   
5189  C CB  . LEU B 226 ? 0.2562 0.2964 0.2519 -0.0072 -0.0076 -0.0218 527 LEU B CB  
5190  C CG  . LEU B 226 ? 0.3236 0.3535 0.3131 -0.0048 -0.0109 -0.0241 527 LEU B CG  
5191  C CD1 . LEU B 226 ? 0.3003 0.3229 0.2808 -0.0058 -0.0111 -0.0239 527 LEU B CD1 
5192  C CD2 . LEU B 226 ? 0.2848 0.3112 0.2784 -0.0070 -0.0146 -0.0240 527 LEU B CD2 
5193  N N   . LEU B 227 ? 0.3027 0.3629 0.3199 -0.0165 -0.0061 -0.0186 528 LEU B N   
5194  C CA  . LEU B 227 ? 0.3050 0.3715 0.3276 -0.0229 -0.0035 -0.0162 528 LEU B CA  
5195  C C   . LEU B 227 ? 0.3283 0.3826 0.3455 -0.0272 -0.0046 -0.0136 528 LEU B C   
5196  O O   . LEU B 227 ? 0.2954 0.3433 0.3134 -0.0288 -0.0081 -0.0140 528 LEU B O   
5197  C CB  . LEU B 227 ? 0.3732 0.4494 0.4061 -0.0257 -0.0050 -0.0173 528 LEU B CB  
5198  C CG  . LEU B 227 ? 0.4041 0.4963 0.4458 -0.0295 -0.0013 -0.0167 528 LEU B CG  
5199  C CD1 . LEU B 227 ? 0.3501 0.4460 0.3995 -0.0364 -0.0036 -0.0169 528 LEU B CD1 
5200  C CD2 . LEU B 227 ? 0.3230 0.4160 0.3612 -0.0326 0.0041  -0.0136 528 LEU B CD2 
5201  N N   . LEU B 228 ? 0.2888 0.3399 0.2998 -0.0284 -0.0015 -0.0109 529 LEU B N   
5202  C CA  . LEU B 228 ? 0.2730 0.3120 0.2766 -0.0297 -0.0029 -0.0086 529 LEU B CA  
5203  C C   . LEU B 228 ? 0.3281 0.3649 0.3306 -0.0355 0.0002  -0.0046 529 LEU B C   
5204  O O   . LEU B 228 ? 0.3167 0.3599 0.3191 -0.0373 0.0048  -0.0029 529 LEU B O   
5205  C CB  . LEU B 228 ? 0.2744 0.3091 0.2689 -0.0252 -0.0029 -0.0088 529 LEU B CB  
5206  C CG  . LEU B 228 ? 0.2818 0.3163 0.2755 -0.0201 -0.0056 -0.0127 529 LEU B CG  
5207  C CD1 . LEU B 228 ? 0.3364 0.3665 0.3205 -0.0169 -0.0056 -0.0133 529 LEU B CD1 
5208  C CD2 . LEU B 228 ? 0.2990 0.3278 0.2950 -0.0204 -0.0101 -0.0138 529 LEU B CD2 
5209  N N   . GLN B 229 ? 0.2924 0.3194 0.2930 -0.0382 -0.0019 -0.0030 530 GLN B N   
5210  C CA  . GLN B 229 ? 0.2921 0.3134 0.2903 -0.0440 0.0009  0.0008  530 GLN B CA  
5211  C C   . GLN B 229 ? 0.2980 0.3065 0.2860 -0.0416 -0.0002 0.0038  530 GLN B C   
5212  O O   . GLN B 229 ? 0.3152 0.3175 0.3017 -0.0386 -0.0043 0.0028  530 GLN B O   
5213  C CB  . GLN B 229 ? 0.2944 0.3143 0.2989 -0.0493 -0.0005 -0.0003 530 GLN B CB  
5214  C CG  . GLN B 229 ? 0.3645 0.3725 0.3635 -0.0547 0.0014  0.0035  530 GLN B CG  
5215  C CD  . GLN B 229 ? 0.3540 0.3595 0.3580 -0.0607 0.0001  0.0019  530 GLN B CD  
5216  O OE1 . GLN B 229 ? 0.3948 0.4025 0.4036 -0.0590 -0.0039 -0.0017 530 GLN B OE1 
5217  N NE2 . GLN B 229 ? 0.4288 0.4292 0.4310 -0.0683 0.0035  0.0046  530 GLN B NE2 
5218  N N   . ALA B 230 ? 0.3298 0.3355 0.3108 -0.0427 0.0034  0.0077  531 ALA B N   
5219  C CA  . ALA B 230 ? 0.3780 0.3725 0.3483 -0.0399 0.0025  0.0112  531 ALA B CA  
5220  C C   . ALA B 230 ? 0.4037 0.3882 0.3692 -0.0450 0.0057  0.0158  531 ALA B C   
5221  O O   . ALA B 230 ? 0.3985 0.3865 0.3650 -0.0504 0.0105  0.0176  531 ALA B O   
5222  C CB  . ALA B 230 ? 0.2924 0.2905 0.2557 -0.0359 0.0039  0.0122  531 ALA B CB  
5223  N N   . ASN B 231 ? 0.4077 0.3793 0.3675 -0.0432 0.0033  0.0177  532 ASN B N   
5224  C CA  . ASN B 231 ? 0.3768 0.3347 0.3279 -0.0464 0.0062  0.0228  532 ASN B CA  
5225  C C   . ASN B 231 ? 0.3655 0.3222 0.3216 -0.0556 0.0096  0.0228  532 ASN B C   
5226  O O   . ASN B 231 ? 0.3884 0.3374 0.3382 -0.0608 0.0141  0.0270  532 ASN B O   
5227  C CB  . ASN B 231 ? 0.4194 0.3757 0.3604 -0.0447 0.0095  0.0274  532 ASN B CB  
5228  C CG  . ASN B 231 ? 0.5633 0.5021 0.4916 -0.0440 0.0108  0.0332  532 ASN B CG  
5229  O OD1 . ASN B 231 ? 0.5752 0.5043 0.5002 -0.0399 0.0072  0.0335  532 ASN B OD1 
5230  N ND2 . ASN B 231 ? 0.5765 0.5110 0.4972 -0.0479 0.0161  0.0379  532 ASN B ND2 
5231  N N   . GLY B 232 ? 0.3886 0.3526 0.3555 -0.0582 0.0074  0.0181  533 GLY B N   
5232  C CA  . GLY B 232 ? 0.4244 0.3892 0.3969 -0.0674 0.0098  0.0173  533 GLY B CA  
5233  C C   . GLY B 232 ? 0.4315 0.4106 0.4101 -0.0730 0.0145  0.0176  533 GLY B C   
5234  O O   . GLY B 232 ? 0.4265 0.4085 0.4106 -0.0817 0.0168  0.0170  533 GLY B O   
5235  N N   . ASN B 233 ? 0.4037 0.3924 0.3815 -0.0684 0.0163  0.0183  534 ASN B N   
5236  C CA  . ASN B 233 ? 0.4138 0.4179 0.3977 -0.0724 0.0211  0.0182  534 ASN B CA  
5237  C C   . ASN B 233 ? 0.4123 0.4334 0.4101 -0.0721 0.0188  0.0127  534 ASN B C   
5238  O O   . ASN B 233 ? 0.3671 0.3875 0.3683 -0.0680 0.0135  0.0091  534 ASN B O   
5239  C CB  . ASN B 233 ? 0.4520 0.4597 0.4291 -0.0666 0.0236  0.0202  534 ASN B CB  
5240  C CG  . ASN B 233 ? 0.4500 0.4426 0.4129 -0.0670 0.0263  0.0262  534 ASN B CG  
5241  O OD1 . ASN B 233 ? 0.4630 0.4475 0.4226 -0.0744 0.0300  0.0297  534 ASN B OD1 
5242  N ND2 . ASN B 233 ? 0.4774 0.4656 0.4314 -0.0593 0.0243  0.0273  534 ASN B ND2 
5243  N N   . ASP B 234 ? 0.3849 0.4218 0.3904 -0.0762 0.0230  0.0123  535 ASP B N   
5244  C CA  . ASP B 234 ? 0.3906 0.4450 0.4089 -0.0746 0.0210  0.0074  535 ASP B CA  
5245  C C   . ASP B 234 ? 0.3476 0.4044 0.3643 -0.0639 0.0176  0.0047  535 ASP B C   
5246  O O   . ASP B 234 ? 0.3403 0.3929 0.3484 -0.0590 0.0191  0.0065  535 ASP B O   
5247  C CB  . ASP B 234 ? 0.3802 0.4535 0.4071 -0.0793 0.0265  0.0077  535 ASP B CB  
5248  C CG  . ASP B 234 ? 0.3986 0.4719 0.4293 -0.0916 0.0295  0.0095  535 ASP B CG  
5249  O OD1 . ASP B 234 ? 0.4209 0.5080 0.4569 -0.0970 0.0352  0.0109  535 ASP B OD1 
5250  O OD2 . ASP B 234 ? 0.3791 0.4387 0.4071 -0.0960 0.0263  0.0094  535 ASP B OD2 
5251  N N   . PRO B 235 ? 0.3802 0.4427 0.4040 -0.0603 0.0130  0.0004  536 PRO B N   
5252  C CA  . PRO B 235 ? 0.3339 0.3965 0.3550 -0.0510 0.0101  -0.0022 536 PRO B CA  
5253  C C   . PRO B 235 ? 0.3014 0.3775 0.3245 -0.0468 0.0139  -0.0030 536 PRO B C   
5254  O O   . PRO B 235 ? 0.3319 0.4218 0.3622 -0.0504 0.0179  -0.0027 536 PRO B O   
5255  C CB  . PRO B 235 ? 0.2799 0.3449 0.3081 -0.0496 0.0049  -0.0060 536 PRO B CB  
5256  C CG  . PRO B 235 ? 0.3060 0.3819 0.3440 -0.0570 0.0062  -0.0065 536 PRO B CG  
5257  C CD  . PRO B 235 ? 0.3308 0.3998 0.3645 -0.0650 0.0104  -0.0024 536 PRO B CD  
5258  N N   . GLU B 236 ? 0.2789 0.3511 0.2953 -0.0393 0.0127  -0.0043 537 GLU B N   
5259  C CA  . GLU B 236 ? 0.2888 0.3699 0.3036 -0.0340 0.0163  -0.0054 537 GLU B CA  
5260  C C   . GLU B 236 ? 0.2754 0.3571 0.2903 -0.0261 0.0127  -0.0096 537 GLU B C   
5261  O O   . GLU B 236 ? 0.2884 0.3593 0.2993 -0.0241 0.0080  -0.0109 537 GLU B O   
5262  C CB  . GLU B 236 ? 0.3492 0.4222 0.3520 -0.0331 0.0191  -0.0025 537 GLU B CB  
5263  C CG  . GLU B 236 ? 0.4248 0.4954 0.4254 -0.0406 0.0232  0.0024  537 GLU B CG  
5264  C CD  . GLU B 236 ? 0.5119 0.5717 0.4988 -0.0391 0.0248  0.0057  537 GLU B CD  
5265  O OE1 . GLU B 236 ? 0.4699 0.5307 0.4503 -0.0332 0.0254  0.0041  537 GLU B OE1 
5266  O OE2 . GLU B 236 ? 0.5354 0.5853 0.5173 -0.0437 0.0253  0.0097  537 GLU B OE2 
5267  N N   . LEU B 237 ? 0.2701 0.3643 0.2890 -0.0214 0.0154  -0.0117 538 LEU B N   
5268  C CA  . LEU B 237 ? 0.2619 0.3558 0.2798 -0.0133 0.0127  -0.0156 538 LEU B CA  
5269  C C   . LEU B 237 ? 0.3414 0.4252 0.3468 -0.0077 0.0133  -0.0167 538 LEU B C   
5270  O O   . LEU B 237 ? 0.3753 0.4606 0.3750 -0.0074 0.0177  -0.0154 538 LEU B O   
5271  C CB  . LEU B 237 ? 0.2582 0.3697 0.2851 -0.0093 0.0154  -0.0174 538 LEU B CB  
5272  C CG  . LEU B 237 ? 0.3358 0.4599 0.3761 -0.0134 0.0137  -0.0176 538 LEU B CG  
5273  C CD1 . LEU B 237 ? 0.3321 0.4758 0.3804 -0.0085 0.0171  -0.0190 538 LEU B CD1 
5274  C CD2 . LEU B 237 ? 0.3586 0.4744 0.3993 -0.0116 0.0072  -0.0197 538 LEU B CD2 
5275  N N   . PHE B 238 ? 0.3532 0.4269 0.3538 -0.0037 0.0089  -0.0194 539 PHE B N   
5276  C CA  . PHE B 238 ? 0.2810 0.3445 0.2695 0.0010  0.0088  -0.0214 539 PHE B CA  
5277  C C   . PHE B 238 ? 0.3407 0.3996 0.3278 0.0070  0.0059  -0.0250 539 PHE B C   
5278  O O   . PHE B 238 ? 0.3671 0.4229 0.3585 0.0057  0.0018  -0.0254 539 PHE B O   
5279  C CB  . PHE B 238 ? 0.2826 0.3337 0.2633 -0.0027 0.0058  -0.0200 539 PHE B CB  
5280  C CG  . PHE B 238 ? 0.3419 0.3944 0.3216 -0.0078 0.0083  -0.0160 539 PHE B CG  
5281  C CD1 . PHE B 238 ? 0.3286 0.3812 0.3144 -0.0135 0.0070  -0.0131 539 PHE B CD1 
5282  C CD2 . PHE B 238 ? 0.3039 0.3561 0.2749 -0.0067 0.0119  -0.0151 539 PHE B CD2 
5283  C CE1 . PHE B 238 ? 0.4139 0.4654 0.3971 -0.0180 0.0095  -0.0091 539 PHE B CE1 
5284  C CE2 . PHE B 238 ? 0.4099 0.4620 0.3784 -0.0111 0.0143  -0.0109 539 PHE B CE2 
5285  C CZ  . PHE B 238 ? 0.4828 0.5341 0.4573 -0.0168 0.0132  -0.0077 539 PHE B CZ  
5286  N N   . GLN B 239 ? 0.3096 0.3664 0.2894 0.0135  0.0081  -0.0276 540 GLN B N   
5287  C CA  . GLN B 239 ? 0.3803 0.4292 0.3556 0.0197  0.0059  -0.0310 540 GLN B CA  
5288  C C   . GLN B 239 ? 0.3553 0.3874 0.3194 0.0179  0.0026  -0.0325 540 GLN B C   
5289  O O   . GLN B 239 ? 0.3892 0.4157 0.3437 0.0176  0.0040  -0.0332 540 GLN B O   
5290  C CB  . GLN B 239 ? 0.4048 0.4578 0.3762 0.0283  0.0100  -0.0334 540 GLN B CB  
5291  C CG  . GLN B 239 ? 0.4928 0.5337 0.4561 0.0355  0.0082  -0.0368 540 GLN B CG  
5292  C CD  . GLN B 239 ? 0.6443 0.6812 0.5969 0.0437  0.0123  -0.0397 540 GLN B CD  
5293  O OE1 . GLN B 239 ? 0.6280 0.6610 0.5720 0.0425  0.0148  -0.0403 540 GLN B OE1 
5294  N NE2 . GLN B 239 ? 0.7422 0.7795 0.6942 0.0527  0.0130  -0.0416 540 GLN B NE2 
5295  N N   . ILE B 240 ? 0.3088 0.3336 0.2740 0.0164  -0.0017 -0.0330 541 ILE B N   
5296  C CA  . ILE B 240 ? 0.3566 0.3667 0.3117 0.0145  -0.0045 -0.0348 541 ILE B CA  
5297  C C   . ILE B 240 ? 0.4602 0.4612 0.4036 0.0205  -0.0027 -0.0384 541 ILE B C   
5298  O O   . ILE B 240 ? 0.4415 0.4427 0.3850 0.0271  -0.0014 -0.0398 541 ILE B O   
5299  C CB  . ILE B 240 ? 0.3686 0.3731 0.3268 0.0125  -0.0087 -0.0348 541 ILE B CB  
5300  C CG1 . ILE B 240 ? 0.4143 0.4266 0.3831 0.0071  -0.0104 -0.0317 541 ILE B CG1 
5301  C CG2 . ILE B 240 ? 0.3555 0.3465 0.3040 0.0097  -0.0112 -0.0367 541 ILE B CG2 
5302  C CD1 . ILE B 240 ? 0.3813 0.3888 0.3530 0.0054  -0.0141 -0.0317 541 ILE B CD1 
5303  N N   . PRO B 241 ? 0.4069 0.3994 0.3392 0.0189  -0.0025 -0.0402 542 PRO B N   
5304  C CA  . PRO B 241 ? 0.4370 0.4184 0.3564 0.0242  -0.0007 -0.0441 542 PRO B CA  
5305  C C   . PRO B 241 ? 0.4135 0.3832 0.3293 0.0267  -0.0029 -0.0461 542 PRO B C   
5306  O O   . PRO B 241 ? 0.3376 0.3015 0.2545 0.0213  -0.0066 -0.0457 542 PRO B O   
5307  C CB  . PRO B 241 ? 0.4142 0.3878 0.3230 0.0194  -0.0020 -0.0457 542 PRO B CB  
5308  C CG  . PRO B 241 ? 0.4012 0.3861 0.3181 0.0140  -0.0027 -0.0417 542 PRO B CG  
5309  C CD  . PRO B 241 ? 0.4071 0.3988 0.3373 0.0122  -0.0045 -0.0388 542 PRO B CD  
5310  N N   . PRO B 242 ? 0.3682 0.3346 0.2799 0.0352  -0.0003 -0.0480 543 PRO B N   
5311  C CA  . PRO B 242 ? 0.4465 0.4020 0.3551 0.0384  -0.0022 -0.0490 543 PRO B CA  
5312  C C   . PRO B 242 ? 0.5045 0.4408 0.4010 0.0335  -0.0047 -0.0514 543 PRO B C   
5313  O O   . PRO B 242 ? 0.5000 0.4294 0.3972 0.0315  -0.0072 -0.0508 543 PRO B O   
5314  C CB  . PRO B 242 ? 0.4617 0.4164 0.3654 0.0497  0.0016  -0.0508 543 PRO B CB  
5315  C CG  . PRO B 242 ? 0.5041 0.4781 0.4169 0.0514  0.0050  -0.0492 543 PRO B CG  
5316  C CD  . PRO B 242 ? 0.4438 0.4180 0.3546 0.0429  0.0045  -0.0487 543 PRO B CD  
5317  N N   . GLU B 243 ? 0.4546 0.3826 0.3400 0.0307  -0.0041 -0.0542 544 GLU B N   
5318  C CA  . GLU B 243 ? 0.4687 0.3798 0.3429 0.0245  -0.0066 -0.0568 544 GLU B CA  
5319  C C   . GLU B 243 ? 0.3983 0.3142 0.2809 0.0150  -0.0106 -0.0546 544 GLU B C   
5320  O O   . GLU B 243 ? 0.4608 0.3647 0.3366 0.0093  -0.0128 -0.0563 544 GLU B O   
5321  C CB  . GLU B 243 ? 0.5153 0.4188 0.3763 0.0230  -0.0055 -0.0605 544 GLU B CB  
5322  C CG  . GLU B 243 ? 0.4589 0.3764 0.3255 0.0181  -0.0062 -0.0589 544 GLU B CG  
5323  C CD  . GLU B 243 ? 0.5106 0.4409 0.3812 0.0246  -0.0020 -0.0575 544 GLU B CD  
5324  O OE1 . GLU B 243 ? 0.5217 0.4550 0.3955 0.0326  0.0010  -0.0570 544 GLU B OE1 
5325  O OE2 . GLU B 243 ? 0.5874 0.5252 0.4577 0.0218  -0.0016 -0.0567 544 GLU B OE2 
5326  N N   . LEU B 244 ? 0.3432 0.2758 0.2397 0.0131  -0.0114 -0.0509 545 LEU B N   
5327  C CA  . LEU B 244 ? 0.3605 0.2976 0.2649 0.0057  -0.0149 -0.0487 545 LEU B CA  
5328  C C   . LEU B 244 ? 0.3557 0.2937 0.2678 0.0067  -0.0160 -0.0466 545 LEU B C   
5329  O O   . LEU B 244 ? 0.3895 0.3295 0.3068 0.0011  -0.0186 -0.0451 545 LEU B O   
5330  C CB  . LEU B 244 ? 0.3091 0.2612 0.2226 0.0028  -0.0154 -0.0458 545 LEU B CB  
5331  C CG  . LEU B 244 ? 0.4595 0.4127 0.3661 0.0011  -0.0148 -0.0470 545 LEU B CG  
5332  C CD1 . LEU B 244 ? 0.4676 0.4345 0.3835 -0.0010 -0.0151 -0.0430 545 LEU B CD1 
5333  C CD2 . LEU B 244 ? 0.4808 0.4246 0.3784 -0.0048 -0.0177 -0.0498 545 LEU B CD2 
5334  N N   . VAL B 245 ? 0.3699 0.3075 0.2827 0.0142  -0.0142 -0.0465 546 VAL B N   
5335  C CA  . VAL B 245 ? 0.3622 0.3021 0.2820 0.0160  -0.0155 -0.0444 546 VAL B CA  
5336  C C   . VAL B 245 ? 0.4100 0.3318 0.3183 0.0176  -0.0157 -0.0462 546 VAL B C   
5337  O O   . VAL B 245 ? 0.3731 0.2871 0.2739 0.0253  -0.0137 -0.0476 546 VAL B O   
5338  C CB  . VAL B 245 ? 0.4184 0.3710 0.3468 0.0230  -0.0138 -0.0429 546 VAL B CB  
5339  C CG1 . VAL B 245 ? 0.4394 0.3927 0.3726 0.0257  -0.0156 -0.0414 546 VAL B CG1 
5340  C CG2 . VAL B 245 ? 0.3499 0.3189 0.2893 0.0197  -0.0134 -0.0407 546 VAL B CG2 
5341  N N   . LEU B 246 ? 0.3999 0.3148 0.3064 0.0106  -0.0178 -0.0461 547 LEU B N   
5342  C CA  . LEU B 246 ? 0.3836 0.2802 0.2786 0.0108  -0.0176 -0.0474 547 LEU B CA  
5343  C C   . LEU B 246 ? 0.4202 0.3173 0.3187 0.0166  -0.0180 -0.0451 547 LEU B C   
5344  O O   . LEU B 246 ? 0.3702 0.2786 0.2797 0.0145  -0.0198 -0.0426 547 LEU B O   
5345  C CB  . LEU B 246 ? 0.4666 0.3577 0.3593 0.0006  -0.0194 -0.0479 547 LEU B CB  
5346  C CG  . LEU B 246 ? 0.5677 0.4392 0.4482 -0.0014 -0.0190 -0.0489 547 LEU B CG  
5347  C CD1 . LEU B 246 ? 0.5952 0.4492 0.4602 0.0037  -0.0167 -0.0520 547 LEU B CD1 
5348  C CD2 . LEU B 246 ? 0.6045 0.4741 0.4843 -0.0126 -0.0205 -0.0497 547 LEU B CD2 
5349  N N   . GLU B 247 ? 0.4429 0.3276 0.3313 0.0244  -0.0164 -0.0460 548 GLU B N   
5350  C CA  . GLU B 247 ? 0.4403 0.3245 0.3301 0.0308  -0.0171 -0.0438 548 GLU B CA  
5351  C C   . GLU B 247 ? 0.4827 0.3438 0.3571 0.0315  -0.0164 -0.0443 548 GLU B C   
5352  O O   . GLU B 247 ? 0.4911 0.3353 0.3522 0.0293  -0.0148 -0.0469 548 GLU B O   
5353  C CB  . GLU B 247 ? 0.4265 0.3203 0.3201 0.0420  -0.0159 -0.0436 548 GLU B CB  
5354  C CG  . GLU B 247 ? 0.4898 0.4070 0.3994 0.0408  -0.0163 -0.0426 548 GLU B CG  
5355  C CD  . GLU B 247 ? 0.5304 0.4590 0.4443 0.0510  -0.0148 -0.0426 548 GLU B CD  
5356  O OE1 . GLU B 247 ? 0.5845 0.5068 0.4899 0.0570  -0.0120 -0.0446 548 GLU B OE1 
5357  O OE2 . GLU B 247 ? 0.5073 0.4518 0.4331 0.0531  -0.0163 -0.0407 548 GLU B OE2 
5358  N N   . VAL B 248 ? 0.3723 0.2318 0.2474 0.0343  -0.0176 -0.0418 549 VAL B N   
5359  C CA  . VAL B 248 ? 0.4209 0.2581 0.2811 0.0347  -0.0169 -0.0413 549 VAL B CA  
5360  C C   . VAL B 248 ? 0.4546 0.2891 0.3109 0.0474  -0.0170 -0.0396 549 VAL B C   
5361  O O   . VAL B 248 ? 0.4622 0.3111 0.3289 0.0503  -0.0191 -0.0373 549 VAL B O   
5362  C CB  . VAL B 248 ? 0.4573 0.2940 0.3203 0.0252  -0.0182 -0.0394 549 VAL B CB  
5363  C CG1 . VAL B 248 ? 0.4622 0.2751 0.3089 0.0253  -0.0168 -0.0385 549 VAL B CG1 
5364  C CG2 . VAL B 248 ? 0.4166 0.2593 0.2851 0.0135  -0.0185 -0.0410 549 VAL B CG2 
5365  N N   . PRO B 249 ? 0.4577 0.2742 0.2989 0.0554  -0.0148 -0.0408 550 PRO B N   
5366  C CA  . PRO B 249 ? 0.4821 0.2947 0.3181 0.0683  -0.0152 -0.0388 550 PRO B CA  
5367  C C   . PRO B 249 ? 0.5127 0.3121 0.3411 0.0658  -0.0161 -0.0359 550 PRO B C   
5368  O O   . PRO B 249 ? 0.4636 0.2438 0.2807 0.0576  -0.0146 -0.0362 550 PRO B O   
5369  C CB  . PRO B 249 ? 0.4541 0.2473 0.2735 0.0767  -0.0121 -0.0411 550 PRO B CB  
5370  C CG  . PRO B 249 ? 0.5963 0.3728 0.4060 0.0651  -0.0104 -0.0439 550 PRO B CG  
5371  C CD  . PRO B 249 ? 0.4575 0.2541 0.2838 0.0529  -0.0122 -0.0441 550 PRO B CD  
5372  N N   . ILE B 250 ? 0.4750 0.2854 0.3097 0.0723  -0.0185 -0.0331 551 ILE B N   
5373  C CA  . ILE B 250 ? 0.4351 0.2362 0.2642 0.0694  -0.0196 -0.0301 551 ILE B CA  
5374  C C   . ILE B 250 ? 0.5091 0.2861 0.3185 0.0796  -0.0183 -0.0285 551 ILE B C   
5375  O O   . ILE B 250 ? 0.5265 0.3074 0.3345 0.0931  -0.0191 -0.0278 551 ILE B O   
5376  C CB  . ILE B 250 ? 0.4191 0.2431 0.2637 0.0702  -0.0232 -0.0281 551 ILE B CB  
5377  C CG1 . ILE B 250 ? 0.3945 0.2402 0.2573 0.0608  -0.0242 -0.0296 551 ILE B CG1 
5378  C CG2 . ILE B 250 ? 0.5209 0.3340 0.3580 0.0670  -0.0238 -0.0251 551 ILE B CG2 
5379  C CD1 . ILE B 250 ? 0.4031 0.2415 0.2646 0.0474  -0.0226 -0.0306 551 ILE B CD1 
5380  N N   . ARG B 251 ? 0.4801 0.2323 0.2739 0.0731  -0.0160 -0.0277 552 ARG B N   
5381  C CA  . ARG B 251 ? 0.5296 0.2554 0.3024 0.0813  -0.0145 -0.0254 552 ARG B CA  
5382  C C   . ARG B 251 ? 0.5133 0.2284 0.2799 0.0730  -0.0142 -0.0222 552 ARG B C   
5383  O O   . ARG B 251 ? 0.5607 0.2876 0.3384 0.0608  -0.0147 -0.0224 552 ARG B O   
5384  C CB  . ARG B 251 ? 0.5983 0.2975 0.3529 0.0825  -0.0108 -0.0280 552 ARG B CB  
5385  C CG  . ARG B 251 ? 0.6396 0.3272 0.3901 0.0663  -0.0084 -0.0306 552 ARG B CG  
5386  C CD  . ARG B 251 ? 0.5595 0.2693 0.3270 0.0594  -0.0093 -0.0343 552 ARG B CD  
5387  N NE  . ARG B 251 ? 0.6111 0.3061 0.3705 0.0471  -0.0071 -0.0376 552 ARG B NE  
5388  C CZ  . ARG B 251 ? 0.6501 0.3596 0.4208 0.0379  -0.0077 -0.0406 552 ARG B CZ  
5389  N NH1 . ARG B 251 ? 0.6511 0.3460 0.4126 0.0270  -0.0061 -0.0437 552 ARG B NH1 
5390  N NH2 . ARG B 251 ? 0.5676 0.3059 0.3582 0.0394  -0.0101 -0.0406 552 ARG B NH2 
5391  N N   . HIS B 252 ? 0.5382 0.2306 0.2862 0.0804  -0.0131 -0.0191 553 HIS B N   
5392  C CA  . HIS B 252 ? 0.6102 0.2919 0.3505 0.0744  -0.0124 -0.0155 553 HIS B CA  
5393  C C   . HIS B 252 ? 0.6847 0.3305 0.4011 0.0697  -0.0079 -0.0147 553 HIS B C   
5394  O O   . HIS B 252 ? 0.6757 0.3008 0.3762 0.0786  -0.0062 -0.0153 553 HIS B O   
5395  C CB  . HIS B 252 ? 0.5748 0.2624 0.3138 0.0873  -0.0155 -0.0116 553 HIS B CB  
5396  C CG  . HIS B 252 ? 0.5631 0.2452 0.2968 0.0816  -0.0153 -0.0078 553 HIS B CG  
5397  N ND1 . HIS B 252 ? 0.6246 0.2760 0.3359 0.0800  -0.0118 -0.0046 553 HIS B ND1 
5398  C CD2 . HIS B 252 ? 0.5728 0.2753 0.3197 0.0778  -0.0180 -0.0065 553 HIS B CD2 
5399  C CE1 . HIS B 252 ? 0.6094 0.2638 0.3208 0.0753  -0.0121 -0.0015 553 HIS B CE1 
5400  N NE2 . HIS B 252 ? 0.5472 0.2322 0.2798 0.0741  -0.0159 -0.0027 553 HIS B NE2 
5401  N N   . PRO B 253 ? 0.6582 0.2960 0.3714 0.0554  -0.0056 -0.0137 554 PRO B N   
5402  C CA  . PRO B 253 ? 0.7302 0.3339 0.4210 0.0484  -0.0010 -0.0133 554 PRO B CA  
5403  C C   . PRO B 253 ? 0.7444 0.3200 0.4117 0.0595  0.0006  -0.0089 554 PRO B C   
5404  O O   . PRO B 253 ? 0.7854 0.3291 0.4313 0.0582  0.0043  -0.0090 554 PRO B O   
5405  C CB  . PRO B 253 ? 0.6996 0.3085 0.3967 0.0308  0.0007  -0.0127 554 PRO B CB  
5406  C CG  . PRO B 253 ? 0.6940 0.3311 0.4088 0.0335  -0.0028 -0.0106 554 PRO B CG  
5407  C CD  . PRO B 253 ? 0.6421 0.3013 0.3714 0.0450  -0.0069 -0.0127 554 PRO B CD  
5408  N N   . LYS B 254 ? 0.7461 0.3315 0.4157 0.0706  -0.0023 -0.0050 555 LYS B N   
5409  C CA  . LYS B 254 ? 0.8488 0.4084 0.4955 0.0823  -0.0012 -0.0003 555 LYS B CA  
5410  C C   . LYS B 254 ? 0.8439 0.4097 0.4901 0.1029  -0.0046 0.0002  555 LYS B C   
5411  O O   . LYS B 254 ? 0.8697 0.4087 0.4941 0.1145  -0.0030 0.0024  555 LYS B O   
5412  C CB  . LYS B 254 ? 1.0254 0.5872 0.6705 0.0788  -0.0014 0.0045  555 LYS B CB  
5413  C CG  . LYS B 254 ? 1.1231 0.6789 0.7678 0.0589  0.0026  0.0047  555 LYS B CG  
5414  C CD  . LYS B 254 ? 1.2674 0.7843 0.8868 0.0522  0.0084  0.0057  555 LYS B CD  
5415  C CE  . LYS B 254 ? 1.3166 0.8303 0.9365 0.0323  0.0124  0.0063  555 LYS B CE  
5416  N NZ  . LYS B 254 ? 1.2638 0.8038 0.8995 0.0294  0.0105  0.0085  555 LYS B NZ  
5417  N N   . PHE B 255 ? 0.7459 0.3464 0.4151 0.1080  -0.0092 -0.0017 556 PHE B N   
5418  C CA  . PHE B 255 ? 0.7394 0.3515 0.4112 0.1271  -0.0128 -0.0011 556 PHE B CA  
5419  C C   . PHE B 255 ? 0.7472 0.3630 0.4236 0.1315  -0.0120 -0.0058 556 PHE B C   
5420  O O   . PHE B 255 ? 0.6448 0.2863 0.3422 0.1253  -0.0134 -0.0095 556 PHE B O   
5421  C CB  . PHE B 255 ? 0.7485 0.3963 0.4421 0.1294  -0.0182 -0.0006 556 PHE B CB  
5422  C CG  . PHE B 255 ? 0.7767 0.4214 0.4647 0.1268  -0.0192 0.0038  556 PHE B CG  
5423  C CD1 . PHE B 255 ? 0.7704 0.4427 0.4773 0.1204  -0.0226 0.0035  556 PHE B CD1 
5424  C CD2 . PHE B 255 ? 0.8157 0.4282 0.4781 0.1306  -0.0165 0.0083  556 PHE B CD2 
5425  C CE1 . PHE B 255 ? 0.7019 0.3709 0.4025 0.1183  -0.0233 0.0074  556 PHE B CE1 
5426  C CE2 . PHE B 255 ? 0.8195 0.4287 0.4755 0.1282  -0.0171 0.0126  556 PHE B CE2 
5427  C CZ  . PHE B 255 ? 0.7621 0.4002 0.4375 0.1222  -0.0205 0.0120  556 PHE B CZ  
5428  N N   . GLU B 256 ? 0.7733 0.3622 0.4290 0.1429  -0.0095 -0.0055 557 GLU B N   
5429  C CA  . GLU B 256 ? 0.7746 0.3638 0.4317 0.1477  -0.0080 -0.0101 557 GLU B CA  
5430  C C   . GLU B 256 ? 0.7558 0.3810 0.4344 0.1590  -0.0120 -0.0116 557 GLU B C   
5431  O O   . GLU B 256 ? 0.7464 0.3848 0.4359 0.1581  -0.0113 -0.0158 557 GLU B O   
5432  C CB  . GLU B 256 ? 0.8386 0.3901 0.4672 0.1593  -0.0044 -0.0092 557 GLU B CB  
5433  C CG  . GLU B 256 ? 1.0494 0.5996 0.6693 0.1819  -0.0067 -0.0055 557 GLU B CG  
5434  C CD  . GLU B 256 ? 1.1864 0.7321 0.7991 0.1846  -0.0089 0.0006  557 GLU B CD  
5435  O OE1 . GLU B 256 ? 1.1854 0.7220 0.7950 0.1694  -0.0075 0.0023  557 GLU B OE1 
5436  O OE2 . GLU B 256 ? 1.1922 0.7441 0.8018 0.2027  -0.0120 0.0037  557 GLU B OE2 
5437  N N   . TRP B 257 ? 0.7204 0.3628 0.4056 0.1688  -0.0162 -0.0082 558 TRP B N   
5438  C CA  . TRP B 257 ? 0.7310 0.4082 0.4363 0.1793  -0.0201 -0.0095 558 TRP B CA  
5439  C C   . TRP B 257 ? 0.6517 0.3624 0.3842 0.1662  -0.0224 -0.0122 558 TRP B C   
5440  O O   . TRP B 257 ? 0.6550 0.3949 0.4055 0.1721  -0.0249 -0.0140 558 TRP B O   
5441  C CB  . TRP B 257 ? 0.7205 0.4057 0.4236 0.1940  -0.0245 -0.0052 558 TRP B CB  
5442  C CG  . TRP B 257 ? 0.6954 0.3772 0.3958 0.1856  -0.0263 -0.0016 558 TRP B CG  
5443  C CD1 . TRP B 257 ? 0.7475 0.3986 0.4245 0.1874  -0.0247 0.0028  558 TRP B CD1 
5444  C CD2 . TRP B 257 ? 0.7218 0.4307 0.4425 0.1744  -0.0297 -0.0020 558 TRP B CD2 
5445  N NE1 . TRP B 257 ? 0.7525 0.4113 0.4344 0.1781  -0.0268 0.0051  558 TRP B NE1 
5446  C CE2 . TRP B 257 ? 0.7357 0.4296 0.4442 0.1703  -0.0300 0.0021  558 TRP B CE2 
5447  C CE3 . TRP B 257 ? 0.7465 0.4898 0.4935 0.1676  -0.0324 -0.0054 558 TRP B CE3 
5448  C CZ2 . TRP B 257 ? 0.7298 0.4423 0.4515 0.1602  -0.0328 0.0025  558 TRP B CZ2 
5449  C CZ3 . TRP B 257 ? 0.7908 0.5510 0.5504 0.1573  -0.0353 -0.0048 558 TRP B CZ3 
5450  C CH2 . TRP B 257 ? 0.7062 0.4513 0.4532 0.1541  -0.0355 -0.0011 558 TRP B CH2 
5451  N N   . PHE B 258 ? 0.6273 0.3348 0.3631 0.1488  -0.0214 -0.0124 559 PHE B N   
5452  C CA  . PHE B 258 ? 0.5903 0.3285 0.3508 0.1375  -0.0238 -0.0145 559 PHE B CA  
5453  C C   . PHE B 258 ? 0.6265 0.3796 0.3997 0.1361  -0.0226 -0.0188 559 PHE B C   
5454  O O   . PHE B 258 ? 0.5618 0.3453 0.3557 0.1356  -0.0252 -0.0202 559 PHE B O   
5455  C CB  . PHE B 258 ? 0.5483 0.2784 0.3084 0.1200  -0.0223 -0.0141 559 PHE B CB  
5456  C CG  . PHE B 258 ? 0.5783 0.3372 0.3601 0.1112  -0.0255 -0.0146 559 PHE B CG  
5457  C CD1 . PHE B 258 ? 0.5082 0.2730 0.2912 0.1112  -0.0284 -0.0116 559 PHE B CD1 
5458  C CD2 . PHE B 258 ? 0.5330 0.3116 0.3325 0.1031  -0.0256 -0.0181 559 PHE B CD2 
5459  C CE1 . PHE B 258 ? 0.5383 0.3275 0.3398 0.1032  -0.0312 -0.0124 559 PHE B CE1 
5460  C CE2 . PHE B 258 ? 0.5556 0.3584 0.3736 0.0953  -0.0283 -0.0185 559 PHE B CE2 
5461  C CZ  . PHE B 258 ? 0.5896 0.3975 0.4086 0.0953  -0.0311 -0.0159 559 PHE B CZ  
5462  N N   . LYS B 259 ? 0.6141 0.3454 0.3740 0.1354  -0.0185 -0.0211 560 LYS B N   
5463  C CA  . LYS B 259 ? 0.6563 0.3999 0.4259 0.1348  -0.0169 -0.0252 560 LYS B CA  
5464  C C   . LYS B 259 ? 0.6497 0.4146 0.4285 0.1505  -0.0186 -0.0255 560 LYS B C   
5465  O O   . LYS B 259 ? 0.6306 0.4178 0.4252 0.1491  -0.0184 -0.0282 560 LYS B O   
5466  C CB  . LYS B 259 ? 0.6876 0.4009 0.4380 0.1323  -0.0124 -0.0277 560 LYS B CB  
5467  C CG  . LYS B 259 ? 0.7523 0.4363 0.4786 0.1466  -0.0102 -0.0264 560 LYS B CG  
5468  C CD  . LYS B 259 ? 0.7914 0.4488 0.5009 0.1440  -0.0056 -0.0302 560 LYS B CD  
5469  C CE  . LYS B 259 ? 0.8333 0.4583 0.5167 0.1585  -0.0031 -0.0290 560 LYS B CE  
5470  N NZ  . LYS B 259 ? 0.8781 0.4818 0.5469 0.1577  -0.0035 -0.0243 560 LYS B NZ  
5471  N N   . ASP B 260 ? 0.6384 0.3982 0.4081 0.1655  -0.0201 -0.0226 561 ASP B N   
5472  C CA  . ASP B 260 ? 0.7549 0.5380 0.5345 0.1810  -0.0220 -0.0227 561 ASP B CA  
5473  C C   . ASP B 260 ? 0.6996 0.5207 0.5050 0.1767  -0.0264 -0.0227 561 ASP B C   
5474  O O   . ASP B 260 ? 0.7383 0.5847 0.5569 0.1856  -0.0276 -0.0237 561 ASP B O   
5475  C CB  . ASP B 260 ? 0.9314 0.7004 0.6947 0.1984  -0.0233 -0.0193 561 ASP B CB  
5476  C CG  . ASP B 260 ? 1.0583 0.7870 0.7938 0.2041  -0.0187 -0.0192 561 ASP B CG  
5477  O OD1 . ASP B 260 ? 1.0452 0.7593 0.7751 0.1959  -0.0147 -0.0225 561 ASP B OD1 
5478  O OD2 . ASP B 260 ? 1.1039 0.8146 0.8223 0.2169  -0.0193 -0.0157 561 ASP B OD2 
5479  N N   . LEU B 261 ? 0.5848 0.4106 0.3973 0.1634  -0.0287 -0.0216 562 LEU B N   
5480  C CA  . LEU B 261 ? 0.5984 0.4578 0.4344 0.1576  -0.0324 -0.0221 562 LEU B CA  
5481  C C   . LEU B 261 ? 0.5713 0.4487 0.4230 0.1506  -0.0304 -0.0256 562 LEU B C   
5482  O O   . LEU B 261 ? 0.5678 0.4744 0.4389 0.1482  -0.0330 -0.0263 562 LEU B O   
5483  C CB  . LEU B 261 ? 0.5227 0.3801 0.3610 0.1446  -0.0345 -0.0206 562 LEU B CB  
5484  C CG  . LEU B 261 ? 0.5660 0.4073 0.3892 0.1504  -0.0366 -0.0169 562 LEU B CG  
5485  C CD1 . LEU B 261 ? 0.4827 0.3186 0.3061 0.1365  -0.0371 -0.0157 562 LEU B CD1 
5486  C CD2 . LEU B 261 ? 0.6108 0.4732 0.4410 0.1632  -0.0415 -0.0155 562 LEU B CD2 
5487  N N   . GLY B 262 ? 0.5261 0.3863 0.3689 0.1470  -0.0260 -0.0277 563 GLY B N   
5488  C CA  . GLY B 262 ? 0.5293 0.4044 0.3844 0.1411  -0.0238 -0.0307 563 GLY B CA  
5489  C C   . GLY B 262 ? 0.5846 0.4727 0.4542 0.1248  -0.0250 -0.0313 563 GLY B C   
5490  O O   . GLY B 262 ? 0.5590 0.4683 0.4438 0.1209  -0.0246 -0.0329 563 GLY B O   
5491  N N   . LEU B 263 ? 0.4144 0.2902 0.2792 0.1155  -0.0261 -0.0298 564 LEU B N   
5492  C CA  . LEU B 263 ? 0.4330 0.3214 0.3111 0.1016  -0.0274 -0.0301 564 LEU B CA  
5493  C C   . LEU B 263 ? 0.4343 0.3119 0.3092 0.0911  -0.0243 -0.0322 564 LEU B C   
5494  O O   . LEU B 263 ? 0.4470 0.3006 0.3057 0.0906  -0.0217 -0.0329 564 LEU B O   
5495  C CB  . LEU B 263 ? 0.4825 0.3657 0.3583 0.0968  -0.0301 -0.0277 564 LEU B CB  
5496  C CG  . LEU B 263 ? 0.5927 0.4870 0.4711 0.1068  -0.0339 -0.0257 564 LEU B CG  
5497  C CD1 . LEU B 263 ? 0.5096 0.3929 0.3807 0.1029  -0.0358 -0.0233 564 LEU B CD1 
5498  C CD2 . LEU B 263 ? 0.5397 0.4653 0.4389 0.1060  -0.0367 -0.0268 564 LEU B CD2 
5499  N N   . LYS B 264 ? 0.4543 0.3494 0.3439 0.0823  -0.0247 -0.0332 565 LYS B N   
5500  C CA  . LYS B 264 ? 0.5182 0.4062 0.4065 0.0710  -0.0228 -0.0348 565 LYS B CA  
5501  C C   . LYS B 264 ? 0.4722 0.3774 0.3759 0.0611  -0.0249 -0.0341 565 LYS B C   
5502  O O   . LYS B 264 ? 0.4669 0.3891 0.3818 0.0630  -0.0274 -0.0330 565 LYS B O   
5503  C CB  . LYS B 264 ? 0.4719 0.3602 0.3586 0.0733  -0.0198 -0.0374 565 LYS B CB  
5504  C CG  . LYS B 264 ? 0.4355 0.3491 0.3374 0.0772  -0.0199 -0.0378 565 LYS B CG  
5505  C CD  . LYS B 264 ? 0.4916 0.4052 0.3916 0.0767  -0.0165 -0.0403 565 LYS B CD  
5506  C CE  . LYS B 264 ? 0.6346 0.5625 0.5395 0.0878  -0.0149 -0.0409 565 LYS B CE  
5507  N NZ  . LYS B 264 ? 0.7026 0.6338 0.6074 0.0864  -0.0114 -0.0432 565 LYS B NZ  
5508  N N   . TRP B 265 ? 0.3660 0.2663 0.2694 0.0506  -0.0240 -0.0349 566 TRP B N   
5509  C CA  . TRP B 265 ? 0.4086 0.3243 0.3256 0.0419  -0.0254 -0.0345 566 TRP B CA  
5510  C C   . TRP B 265 ? 0.4632 0.3767 0.3796 0.0347  -0.0236 -0.0362 566 TRP B C   
5511  O O   . TRP B 265 ? 0.4798 0.3785 0.3847 0.0348  -0.0216 -0.0379 566 TRP B O   
5512  C CB  . TRP B 265 ? 0.3186 0.2318 0.2364 0.0364  -0.0273 -0.0328 566 TRP B CB  
5513  C CG  . TRP B 265 ? 0.3168 0.2480 0.2491 0.0319  -0.0293 -0.0321 566 TRP B CG  
5514  C CD1 . TRP B 265 ? 0.3287 0.2639 0.2668 0.0229  -0.0295 -0.0320 566 TRP B CD1 
5515  C CD2 . TRP B 265 ? 0.2921 0.2397 0.2347 0.0361  -0.0314 -0.0317 566 TRP B CD2 
5516  N NE1 . TRP B 265 ? 0.2787 0.2295 0.2288 0.0216  -0.0314 -0.0315 566 TRP B NE1 
5517  C CE2 . TRP B 265 ? 0.2779 0.2365 0.2310 0.0289  -0.0326 -0.0314 566 TRP B CE2 
5518  C CE3 . TRP B 265 ? 0.3143 0.2686 0.2580 0.0453  -0.0325 -0.0316 566 TRP B CE3 
5519  C CZ2 . TRP B 265 ? 0.2846 0.2592 0.2487 0.0295  -0.0347 -0.0312 566 TRP B CZ2 
5520  C CZ3 . TRP B 265 ? 0.3427 0.3154 0.2986 0.0458  -0.0349 -0.0314 566 TRP B CZ3 
5521  C CH2 . TRP B 265 ? 0.3158 0.2978 0.2815 0.0373  -0.0359 -0.0314 566 TRP B CH2 
5522  N N   . TYR B 266 ? 0.4023 0.3302 0.3305 0.0285  -0.0244 -0.0359 567 TYR B N   
5523  C CA  . TYR B 266 ? 0.3848 0.3120 0.3128 0.0216  -0.0234 -0.0372 567 TYR B CA  
5524  C C   . TYR B 266 ? 0.4314 0.3519 0.3573 0.0131  -0.0242 -0.0367 567 TYR B C   
5525  O O   . TYR B 266 ? 0.3922 0.3136 0.3208 0.0116  -0.0256 -0.0351 567 TYR B O   
5526  C CB  . TYR B 266 ? 0.3124 0.2574 0.2529 0.0198  -0.0235 -0.0367 567 TYR B CB  
5527  C CG  . TYR B 266 ? 0.3523 0.3096 0.3040 0.0183  -0.0256 -0.0348 567 TYR B CG  
5528  C CD1 . TYR B 266 ? 0.3461 0.3054 0.3022 0.0112  -0.0270 -0.0338 567 TYR B CD1 
5529  C CD2 . TYR B 266 ? 0.3291 0.2967 0.2871 0.0240  -0.0264 -0.0342 567 TYR B CD2 
5530  C CE1 . TYR B 266 ? 0.2777 0.2464 0.2426 0.0100  -0.0288 -0.0325 567 TYR B CE1 
5531  C CE2 . TYR B 266 ? 0.3143 0.2925 0.2818 0.0219  -0.0286 -0.0330 567 TYR B CE2 
5532  C CZ  . TYR B 266 ? 0.3352 0.3128 0.3055 0.0148  -0.0297 -0.0322 567 TYR B CZ  
5533  O OH  . TYR B 266 ? 0.3264 0.3125 0.3045 0.0128  -0.0317 -0.0314 567 TYR B OH  
5534  N N   . GLY B 267 ? 0.3416 0.2564 0.2627 0.0075  -0.0234 -0.0383 568 GLY B N   
5535  C CA  . GLY B 267 ? 0.3588 0.2687 0.2781 -0.0007 -0.0240 -0.0382 568 GLY B CA  
5536  C C   . GLY B 267 ? 0.3208 0.2452 0.2519 -0.0059 -0.0256 -0.0368 568 GLY B C   
5537  O O   . GLY B 267 ? 0.4074 0.3314 0.3398 -0.0110 -0.0262 -0.0360 568 GLY B O   
5538  N N   . LEU B 268 ? 0.3245 0.2612 0.2636 -0.0045 -0.0258 -0.0364 569 LEU B N   
5539  C CA  . LEU B 268 ? 0.3661 0.3139 0.3139 -0.0093 -0.0270 -0.0353 569 LEU B CA  
5540  C C   . LEU B 268 ? 0.3338 0.2915 0.2913 -0.0075 -0.0280 -0.0333 569 LEU B C   
5541  O O   . LEU B 268 ? 0.3715 0.3365 0.3339 -0.0041 -0.0277 -0.0329 569 LEU B O   
5542  C CB  . LEU B 268 ? 0.4034 0.3562 0.3516 -0.0100 -0.0265 -0.0361 569 LEU B CB  
5543  C CG  . LEU B 268 ? 0.3082 0.2705 0.2631 -0.0145 -0.0278 -0.0348 569 LEU B CG  
5544  C CD1 . LEU B 268 ? 0.3661 0.3253 0.3184 -0.0204 -0.0289 -0.0354 569 LEU B CD1 
5545  C CD2 . LEU B 268 ? 0.3045 0.2721 0.2594 -0.0140 -0.0271 -0.0349 569 LEU B CD2 
5546  N N   . PRO B 269 ? 0.3217 0.2802 0.2822 -0.0100 -0.0291 -0.0322 570 PRO B N   
5547  C CA  . PRO B 269 ? 0.2641 0.2312 0.2330 -0.0091 -0.0302 -0.0307 570 PRO B CA  
5548  C C   . PRO B 269 ? 0.2944 0.2694 0.2693 -0.0123 -0.0305 -0.0298 570 PRO B C   
5549  O O   . PRO B 269 ? 0.3475 0.3226 0.3223 -0.0159 -0.0308 -0.0295 570 PRO B O   
5550  C CB  . PRO B 269 ? 0.2454 0.2081 0.2126 -0.0101 -0.0307 -0.0302 570 PRO B CB  
5551  C CG  . PRO B 269 ? 0.2510 0.2074 0.2125 -0.0146 -0.0299 -0.0308 570 PRO B CG  
5552  C CD  . PRO B 269 ? 0.3096 0.2606 0.2651 -0.0140 -0.0290 -0.0324 570 PRO B CD  
5553  N N   . ALA B 270 ? 0.2933 0.2751 0.2732 -0.0108 -0.0303 -0.0291 571 ALA B N   
5554  C CA  . ALA B 270 ? 0.2720 0.2593 0.2556 -0.0131 -0.0301 -0.0279 571 ALA B CA  
5555  C C   . ALA B 270 ? 0.3855 0.3785 0.3756 -0.0129 -0.0304 -0.0266 571 ALA B C   
5556  O O   . ALA B 270 ? 0.3212 0.3184 0.3137 -0.0115 -0.0295 -0.0266 571 ALA B O   
5557  C CB  . ALA B 270 ? 0.2667 0.2545 0.2468 -0.0126 -0.0288 -0.0285 571 ALA B CB  
5558  N N   . VAL B 271 ? 0.3204 0.3134 0.3131 -0.0144 -0.0314 -0.0258 572 VAL B N   
5559  C CA  . VAL B 271 ? 0.2640 0.2600 0.2615 -0.0149 -0.0318 -0.0250 572 VAL B CA  
5560  C C   . VAL B 271 ? 0.2177 0.2163 0.2169 -0.0165 -0.0308 -0.0232 572 VAL B C   
5561  O O   . VAL B 271 ? 0.2667 0.2641 0.2640 -0.0172 -0.0308 -0.0221 572 VAL B O   
5562  C CB  . VAL B 271 ? 0.2830 0.2763 0.2809 -0.0154 -0.0330 -0.0251 572 VAL B CB  
5563  C CG1 . VAL B 271 ? 0.2864 0.2807 0.2878 -0.0167 -0.0333 -0.0244 572 VAL B CG1 
5564  C CG2 . VAL B 271 ? 0.2433 0.2340 0.2391 -0.0136 -0.0340 -0.0265 572 VAL B CG2 
5565  N N   . SER B 272 ? 0.2516 0.2539 0.2541 -0.0173 -0.0299 -0.0228 573 SER B N   
5566  C CA  . SER B 272 ? 0.3210 0.3247 0.3238 -0.0190 -0.0283 -0.0208 573 SER B CA  
5567  C C   . SER B 272 ? 0.2993 0.3033 0.3056 -0.0219 -0.0279 -0.0197 573 SER B C   
5568  O O   . SER B 272 ? 0.3047 0.3087 0.3105 -0.0238 -0.0262 -0.0177 573 SER B O   
5569  C CB  . SER B 272 ? 0.2956 0.3038 0.2978 -0.0180 -0.0263 -0.0209 573 SER B CB  
5570  O OG  . SER B 272 ? 0.2649 0.2781 0.2707 -0.0168 -0.0261 -0.0225 573 SER B OG  
5571  N N   . ASN B 273 ? 0.2800 0.2830 0.2886 -0.0226 -0.0296 -0.0211 574 ASN B N   
5572  C CA  . ASN B 273 ? 0.2232 0.2255 0.2343 -0.0262 -0.0294 -0.0207 574 ASN B CA  
5573  C C   . ASN B 273 ? 0.2881 0.2819 0.2962 -0.0267 -0.0304 -0.0204 574 ASN B C   
5574  O O   . ASN B 273 ? 0.3309 0.3218 0.3397 -0.0298 -0.0307 -0.0208 574 ASN B O   
5575  C CB  . ASN B 273 ? 0.2776 0.2864 0.2936 -0.0273 -0.0306 -0.0229 574 ASN B CB  
5576  C CG  . ASN B 273 ? 0.3529 0.3603 0.3679 -0.0246 -0.0333 -0.0251 574 ASN B CG  
5577  O OD1 . ASN B 273 ? 0.3051 0.3069 0.3160 -0.0221 -0.0338 -0.0250 574 ASN B OD1 
5578  N ND2 . ASN B 273 ? 0.3134 0.3266 0.3321 -0.0250 -0.0349 -0.0270 574 ASN B ND2 
5579  N N   . MET B 274 ? 0.2555 0.2456 0.2602 -0.0237 -0.0309 -0.0199 575 MET B N   
5580  C CA  . MET B 274 ? 0.2460 0.2291 0.2478 -0.0228 -0.0315 -0.0196 575 MET B CA  
5581  C C   . MET B 274 ? 0.3650 0.3435 0.3636 -0.0224 -0.0301 -0.0166 575 MET B C   
5582  O O   . MET B 274 ? 0.3741 0.3550 0.3721 -0.0228 -0.0288 -0.0147 575 MET B O   
5583  C CB  . MET B 274 ? 0.2254 0.2088 0.2260 -0.0196 -0.0326 -0.0207 575 MET B CB  
5584  C CG  . MET B 274 ? 0.2823 0.2670 0.2841 -0.0196 -0.0341 -0.0233 575 MET B CG  
5585  S SD  . MET B 274 ? 0.3434 0.3271 0.3428 -0.0168 -0.0346 -0.0242 575 MET B SD  
5586  C CE  . MET B 274 ? 0.2827 0.2599 0.2796 -0.0159 -0.0348 -0.0247 575 MET B CE  
5587  N N   . LEU B 275 ? 0.3330 0.3040 0.3284 -0.0211 -0.0303 -0.0162 576 LEU B N   
5588  C CA  . LEU B 275 ? 0.2656 0.2303 0.2564 -0.0195 -0.0292 -0.0132 576 LEU B CA  
5589  C C   . LEU B 275 ? 0.3496 0.3146 0.3387 -0.0142 -0.0300 -0.0128 576 LEU B C   
5590  O O   . LEU B 275 ? 0.3405 0.3045 0.3299 -0.0125 -0.0308 -0.0148 576 LEU B O   
5591  C CB  . LEU B 275 ? 0.3421 0.2962 0.3296 -0.0221 -0.0283 -0.0128 576 LEU B CB  
5592  C CG  . LEU B 275 ? 0.4137 0.3585 0.3947 -0.0202 -0.0267 -0.0092 576 LEU B CG  
5593  C CD1 . LEU B 275 ? 0.4110 0.3479 0.3895 -0.0261 -0.0249 -0.0081 576 LEU B CD1 
5594  C CD2 . LEU B 275 ? 0.3826 0.3195 0.3590 -0.0150 -0.0273 -0.0092 576 LEU B CD2 
5595  N N   . LEU B 276 ? 0.2567 0.2243 0.2442 -0.0116 -0.0298 -0.0102 577 LEU B N   
5596  C CA  . LEU B 276 ? 0.2759 0.2469 0.2626 -0.0066 -0.0307 -0.0095 577 LEU B CA  
5597  C C   . LEU B 276 ? 0.3471 0.3092 0.3283 -0.0026 -0.0300 -0.0068 577 LEU B C   
5598  O O   . LEU B 276 ? 0.3076 0.2653 0.2847 -0.0026 -0.0292 -0.0038 577 LEU B O   
5599  C CB  . LEU B 276 ? 0.3056 0.2857 0.2934 -0.0062 -0.0315 -0.0086 577 LEU B CB  
5600  C CG  . LEU B 276 ? 0.3150 0.3008 0.3023 -0.0015 -0.0327 -0.0073 577 LEU B CG  
5601  C CD1 . LEU B 276 ? 0.2802 0.2697 0.2707 0.0002  -0.0331 -0.0094 577 LEU B CD1 
5602  C CD2 . LEU B 276 ? 0.2859 0.2805 0.2738 -0.0026 -0.0338 -0.0071 577 LEU B CD2 
5603  N N   . GLU B 277 ? 0.3575 0.3162 0.3375 0.0012  -0.0301 -0.0077 578 GLU B N   
5604  C CA  . GLU B 277 ? 0.3444 0.2931 0.3180 0.0063  -0.0293 -0.0054 578 GLU B CA  
5605  C C   . GLU B 277 ? 0.3448 0.3021 0.3195 0.0132  -0.0302 -0.0042 578 GLU B C   
5606  O O   . GLU B 277 ? 0.3651 0.3306 0.3441 0.0145  -0.0307 -0.0064 578 GLU B O   
5607  C CB  . GLU B 277 ? 0.4316 0.3689 0.4020 0.0061  -0.0284 -0.0076 578 GLU B CB  
5608  C CG  . GLU B 277 ? 0.6911 0.6138 0.6527 0.0107  -0.0272 -0.0053 578 GLU B CG  
5609  C CD  . GLU B 277 ? 0.9424 0.8632 0.9017 0.0181  -0.0269 -0.0063 578 GLU B CD  
5610  O OE1 . GLU B 277 ? 1.0698 0.9844 1.0276 0.0168  -0.0265 -0.0096 578 GLU B OE1 
5611  O OE2 . GLU B 277 ? 0.9664 0.8929 0.9254 0.0253  -0.0272 -0.0040 578 GLU B OE2 
5612  N N   . ILE B 278 ? 0.3195 0.2756 0.2900 0.0176  -0.0304 -0.0005 579 ILE B N   
5613  C CA  . ILE B 278 ? 0.3526 0.3184 0.3240 0.0250  -0.0317 0.0011  579 ILE B CA  
5614  C C   . ILE B 278 ? 0.4397 0.3939 0.4025 0.0323  -0.0309 0.0047  579 ILE B C   
5615  O O   . ILE B 278 ? 0.4236 0.3701 0.3805 0.0319  -0.0305 0.0079  579 ILE B O   
5616  C CB  . ILE B 278 ? 0.3503 0.3302 0.3255 0.0236  -0.0337 0.0020  579 ILE B CB  
5617  C CG1 . ILE B 278 ? 0.2898 0.2783 0.2716 0.0164  -0.0342 -0.0015 579 ILE B CG1 
5618  C CG2 . ILE B 278 ? 0.2818 0.2737 0.2587 0.0310  -0.0354 0.0034  579 ILE B CG2 
5619  C CD1 . ILE B 278 ? 0.2929 0.2920 0.2763 0.0140  -0.0360 -0.0010 579 ILE B CD1 
5620  N N   . GLY B 279 ? 0.3407 0.2931 0.3021 0.0395  -0.0304 0.0044  580 GLY B N   
5621  C CA  . GLY B 279 ? 0.3606 0.3013 0.3128 0.0483  -0.0296 0.0078  580 GLY B CA  
5622  C C   . GLY B 279 ? 0.4918 0.4104 0.4341 0.0452  -0.0276 0.0094  580 GLY B C   
5623  O O   . GLY B 279 ? 0.5149 0.4234 0.4484 0.0497  -0.0271 0.0136  580 GLY B O   
5624  N N   . GLY B 280 ? 0.3922 0.3030 0.3353 0.0371  -0.0264 0.0061  581 GLY B N   
5625  C CA  . GLY B 280 ? 0.3972 0.2888 0.3322 0.0319  -0.0245 0.0070  581 GLY B CA  
5626  C C   . GLY B 280 ? 0.3993 0.2930 0.3355 0.0244  -0.0244 0.0089  581 GLY B C   
5627  O O   . GLY B 280 ? 0.4383 0.3187 0.3697 0.0180  -0.0225 0.0094  581 GLY B O   
5628  N N   . LEU B 281 ? 0.3520 0.2622 0.2943 0.0246  -0.0260 0.0099  582 LEU B N   
5629  C CA  . LEU B 281 ? 0.3987 0.3119 0.3421 0.0177  -0.0256 0.0112  582 LEU B CA  
5630  C C   . LEU B 281 ? 0.3959 0.3171 0.3481 0.0095  -0.0258 0.0069  582 LEU B C   
5631  O O   . LEU B 281 ? 0.3844 0.3155 0.3433 0.0100  -0.0272 0.0035  582 LEU B O   
5632  C CB  . LEU B 281 ? 0.3639 0.2903 0.3086 0.0216  -0.0274 0.0137  582 LEU B CB  
5633  C CG  . LEU B 281 ? 0.3872 0.3082 0.3232 0.0308  -0.0279 0.0184  582 LEU B CG  
5634  C CD1 . LEU B 281 ? 0.4544 0.3907 0.3922 0.0336  -0.0304 0.0203  582 LEU B CD1 
5635  C CD2 . LEU B 281 ? 0.3732 0.2731 0.2974 0.0299  -0.0250 0.0223  582 LEU B CD2 
5636  N N   . GLU B 282 ? 0.3886 0.3058 0.3403 0.0021  -0.0241 0.0072  583 GLU B N   
5637  C CA  . GLU B 282 ? 0.3515 0.2757 0.3110 -0.0052 -0.0242 0.0034  583 GLU B CA  
5638  C C   . GLU B 282 ? 0.3819 0.3173 0.3451 -0.0083 -0.0242 0.0040  583 GLU B C   
5639  O O   . GLU B 282 ? 0.3592 0.2906 0.3184 -0.0109 -0.0222 0.0069  583 GLU B O   
5640  C CB  . GLU B 282 ? 0.4225 0.3346 0.3795 -0.0116 -0.0224 0.0024  583 GLU B CB  
5641  C CG  . GLU B 282 ? 0.5046 0.4033 0.4561 -0.0087 -0.0225 0.0011  583 GLU B CG  
5642  C CD  . GLU B 282 ? 0.5912 0.4787 0.5404 -0.0165 -0.0212 -0.0007 583 GLU B CD  
5643  O OE1 . GLU B 282 ? 0.7052 0.5909 0.6559 -0.0176 -0.0223 -0.0047 583 GLU B OE1 
5644  O OE2 . GLU B 282 ? 0.5867 0.4677 0.5325 -0.0219 -0.0190 0.0018  583 GLU B OE2 
5645  N N   . PHE B 283 ? 0.3877 0.3362 0.3577 -0.0080 -0.0260 0.0013  584 PHE B N   
5646  C CA  . PHE B 283 ? 0.3077 0.2661 0.2809 -0.0106 -0.0259 0.0010  584 PHE B CA  
5647  C C   . PHE B 283 ? 0.3292 0.2911 0.3082 -0.0162 -0.0254 -0.0022 584 PHE B C   
5648  O O   . PHE B 283 ? 0.3043 0.2724 0.2883 -0.0162 -0.0269 -0.0055 584 PHE B O   
5649  C CB  . PHE B 283 ? 0.3017 0.2707 0.2771 -0.0069 -0.0283 0.0001  584 PHE B CB  
5650  C CG  . PHE B 283 ? 0.3902 0.3586 0.3607 -0.0010 -0.0293 0.0033  584 PHE B CG  
5651  C CD1 . PHE B 283 ? 0.3346 0.3017 0.3048 0.0041  -0.0304 0.0033  584 PHE B CD1 
5652  C CD2 . PHE B 283 ? 0.3647 0.3337 0.3300 0.0000  -0.0290 0.0064  584 PHE B CD2 
5653  C CE1 . PHE B 283 ? 0.3309 0.2987 0.2968 0.0106  -0.0315 0.0064  584 PHE B CE1 
5654  C CE2 . PHE B 283 ? 0.3242 0.2933 0.2845 0.0061  -0.0304 0.0096  584 PHE B CE2 
5655  C CZ  . PHE B 283 ? 0.3207 0.2896 0.2816 0.0116  -0.0318 0.0096  584 PHE B CZ  
5656  N N   . SER B 284 ? 0.3204 0.2785 0.2986 -0.0209 -0.0231 -0.0012 585 SER B N   
5657  C CA  . SER B 284 ? 0.3335 0.2959 0.3177 -0.0261 -0.0226 -0.0040 585 SER B CA  
5658  C C   . SER B 284 ? 0.3210 0.2952 0.3099 -0.0263 -0.0228 -0.0058 585 SER B C   
5659  O O   . SER B 284 ? 0.2921 0.2717 0.2864 -0.0287 -0.0231 -0.0085 585 SER B O   
5660  C CB  . SER B 284 ? 0.3334 0.2898 0.3158 -0.0318 -0.0199 -0.0023 585 SER B CB  
5661  O OG  . SER B 284 ? 0.4141 0.3691 0.3916 -0.0316 -0.0175 0.0017  585 SER B OG  
5662  N N   . ALA B 285 ? 0.3288 0.3067 0.3151 -0.0236 -0.0228 -0.0044 586 ALA B N   
5663  C CA  . ALA B 285 ? 0.3220 0.3088 0.3109 -0.0232 -0.0229 -0.0064 586 ALA B CA  
5664  C C   . ALA B 285 ? 0.3333 0.3224 0.3203 -0.0194 -0.0253 -0.0071 586 ALA B C   
5665  O O   . ALA B 285 ? 0.3248 0.3133 0.3071 -0.0173 -0.0255 -0.0048 586 ALA B O   
5666  C CB  . ALA B 285 ? 0.3084 0.2981 0.2952 -0.0249 -0.0201 -0.0045 586 ALA B CB  
5667  N N   . CYS B 286 ? 0.2440 0.2359 0.2345 -0.0188 -0.0270 -0.0101 587 CYS B N   
5668  C CA  . CYS B 286 ? 0.2642 0.2584 0.2537 -0.0165 -0.0291 -0.0110 587 CYS B CA  
5669  C C   . CYS B 286 ? 0.3835 0.3809 0.3752 -0.0171 -0.0298 -0.0144 587 CYS B C   
5670  O O   . CYS B 286 ? 0.4152 0.4125 0.4083 -0.0165 -0.0311 -0.0157 587 CYS B O   
5671  C CB  . CYS B 286 ? 0.2776 0.2686 0.2674 -0.0144 -0.0302 -0.0103 587 CYS B CB  
5672  S SG  . CYS B 286 ? 0.3299 0.3169 0.3234 -0.0158 -0.0303 -0.0126 587 CYS B SG  
5673  N N   . PRO B 287 ? 0.3587 0.3583 0.3499 -0.0179 -0.0288 -0.0156 588 PRO B N   
5674  C CA  . PRO B 287 ? 0.2782 0.2784 0.2702 -0.0178 -0.0293 -0.0185 588 PRO B CA  
5675  C C   . PRO B 287 ? 0.2595 0.2595 0.2494 -0.0178 -0.0309 -0.0197 588 PRO B C   
5676  O O   . PRO B 287 ? 0.3183 0.3203 0.3056 -0.0179 -0.0317 -0.0191 588 PRO B O   
5677  C CB  . PRO B 287 ? 0.3040 0.3061 0.2939 -0.0176 -0.0276 -0.0192 588 PRO B CB  
5678  C CG  . PRO B 287 ? 0.3614 0.3644 0.3480 -0.0178 -0.0268 -0.0169 588 PRO B CG  
5679  C CD  . PRO B 287 ? 0.3379 0.3390 0.3264 -0.0183 -0.0269 -0.0142 588 PRO B CD  
5680  N N   . PHE B 288 ? 0.2348 0.2331 0.2260 -0.0179 -0.0316 -0.0214 589 PHE B N   
5681  C CA  . PHE B 288 ? 0.2391 0.2376 0.2288 -0.0189 -0.0327 -0.0224 589 PHE B CA  
5682  C C   . PHE B 288 ? 0.3040 0.2985 0.2914 -0.0194 -0.0324 -0.0247 589 PHE B C   
5683  O O   . PHE B 288 ? 0.2361 0.2284 0.2243 -0.0179 -0.0318 -0.0251 589 PHE B O   
5684  C CB  . PHE B 288 ? 0.2532 0.2530 0.2458 -0.0183 -0.0334 -0.0215 589 PHE B CB  
5685  C CG  . PHE B 288 ? 0.3361 0.3327 0.3309 -0.0174 -0.0330 -0.0217 589 PHE B CG  
5686  C CD1 . PHE B 288 ? 0.2899 0.2840 0.2839 -0.0178 -0.0330 -0.0233 589 PHE B CD1 
5687  C CD2 . PHE B 288 ? 0.3252 0.3205 0.3218 -0.0165 -0.0328 -0.0204 589 PHE B CD2 
5688  C CE1 . PHE B 288 ? 0.2936 0.2851 0.2886 -0.0167 -0.0332 -0.0237 589 PHE B CE1 
5689  C CE2 . PHE B 288 ? 0.3703 0.3626 0.3682 -0.0162 -0.0329 -0.0212 589 PHE B CE2 
5690  C CZ  . PHE B 288 ? 0.2983 0.2893 0.2955 -0.0161 -0.0333 -0.0229 589 PHE B CZ  
5691  N N   . SER B 289 ? 0.2998 0.2930 0.2838 -0.0215 -0.0327 -0.0260 590 SER B N   
5692  C CA  . SER B 289 ? 0.2424 0.2292 0.2220 -0.0218 -0.0321 -0.0279 590 SER B CA  
5693  C C   . SER B 289 ? 0.2682 0.2534 0.2457 -0.0252 -0.0324 -0.0288 590 SER B C   
5694  O O   . SER B 289 ? 0.2808 0.2716 0.2600 -0.0277 -0.0332 -0.0285 590 SER B O   
5695  C CB  . SER B 289 ? 0.2533 0.2370 0.2277 -0.0212 -0.0314 -0.0293 590 SER B CB  
5696  O OG  . SER B 289 ? 0.2957 0.2817 0.2676 -0.0240 -0.0322 -0.0299 590 SER B OG  
5697  N N   . GLY B 290 ? 0.3120 0.2902 0.2860 -0.0253 -0.0316 -0.0296 591 GLY B N   
5698  C CA  . GLY B 290 ? 0.2722 0.2473 0.2428 -0.0296 -0.0311 -0.0304 591 GLY B CA  
5699  C C   . GLY B 290 ? 0.3623 0.3255 0.3243 -0.0299 -0.0301 -0.0320 591 GLY B C   
5700  O O   . GLY B 290 ? 0.3583 0.3173 0.3156 -0.0293 -0.0299 -0.0334 591 GLY B O   
5701  N N   . TRP B 291 ? 0.3544 0.3112 0.3131 -0.0303 -0.0290 -0.0316 592 TRP B N   
5702  C CA  . TRP B 291 ? 0.3107 0.2543 0.2601 -0.0288 -0.0279 -0.0324 592 TRP B CA  
5703  C C   . TRP B 291 ? 0.3177 0.2580 0.2665 -0.0252 -0.0275 -0.0309 592 TRP B C   
5704  O O   . TRP B 291 ? 0.2788 0.2260 0.2334 -0.0254 -0.0279 -0.0297 592 TRP B O   
5705  C CB  . TRP B 291 ? 0.2948 0.2297 0.2363 -0.0352 -0.0267 -0.0339 592 TRP B CB  
5706  C CG  . TRP B 291 ? 0.3963 0.3357 0.3406 -0.0408 -0.0261 -0.0331 592 TRP B CG  
5707  C CD1 . TRP B 291 ? 0.4283 0.3634 0.3705 -0.0411 -0.0246 -0.0316 592 TRP B CD1 
5708  C CD2 . TRP B 291 ? 0.4223 0.3726 0.3722 -0.0467 -0.0268 -0.0336 592 TRP B CD2 
5709  N NE1 . TRP B 291 ? 0.4114 0.3543 0.3578 -0.0470 -0.0238 -0.0312 592 TRP B NE1 
5710  C CE2 . TRP B 291 ? 0.4237 0.3767 0.3754 -0.0504 -0.0253 -0.0324 592 TRP B CE2 
5711  C CE3 . TRP B 291 ? 0.4912 0.4500 0.4446 -0.0488 -0.0286 -0.0348 592 TRP B CE3 
5712  C CZ2 . TRP B 291 ? 0.4707 0.4361 0.4286 -0.0560 -0.0254 -0.0326 592 TRP B CZ2 
5713  C CZ3 . TRP B 291 ? 0.4508 0.4214 0.4098 -0.0542 -0.0293 -0.0349 592 TRP B CZ3 
5714  C CH2 . TRP B 291 ? 0.5409 0.5154 0.5027 -0.0577 -0.0277 -0.0339 592 TRP B CH2 
5715  N N   . TYR B 292 ? 0.4125 0.3420 0.3535 -0.0213 -0.0269 -0.0311 593 TYR B N   
5716  C CA  . TYR B 292 ? 0.3919 0.3191 0.3319 -0.0165 -0.0273 -0.0298 593 TYR B CA  
5717  C C   . TYR B 292 ? 0.3332 0.2534 0.2677 -0.0196 -0.0258 -0.0286 593 TYR B C   
5718  O O   . TYR B 292 ? 0.3084 0.2197 0.2358 -0.0245 -0.0240 -0.0289 593 TYR B O   
5719  C CB  . TYR B 292 ? 0.3041 0.2232 0.2375 -0.0099 -0.0273 -0.0301 593 TYR B CB  
5720  C CG  . TYR B 292 ? 0.3442 0.2736 0.2851 -0.0045 -0.0289 -0.0303 593 TYR B CG  
5721  C CD1 . TYR B 292 ? 0.2858 0.2158 0.2261 -0.0016 -0.0285 -0.0316 593 TYR B CD1 
5722  C CD2 . TYR B 292 ? 0.3097 0.2482 0.2579 -0.0026 -0.0306 -0.0294 593 TYR B CD2 
5723  C CE1 . TYR B 292 ? 0.3259 0.2667 0.2737 0.0028  -0.0295 -0.0316 593 TYR B CE1 
5724  C CE2 . TYR B 292 ? 0.3541 0.3025 0.3094 0.0011  -0.0319 -0.0296 593 TYR B CE2 
5725  C CZ  . TYR B 292 ? 0.3149 0.2650 0.2704 0.0036  -0.0312 -0.0306 593 TYR B CZ  
5726  O OH  . TYR B 292 ? 0.3298 0.2911 0.2929 0.0067  -0.0321 -0.0307 593 TYR B OH  
5727  N N   . MET B 293 ? 0.3015 0.2257 0.2389 -0.0171 -0.0265 -0.0273 594 MET B N   
5728  C CA  . MET B 293 ? 0.3245 0.2398 0.2540 -0.0169 -0.0252 -0.0258 594 MET B CA  
5729  C C   . MET B 293 ? 0.3428 0.2497 0.2652 -0.0095 -0.0262 -0.0254 594 MET B C   
5730  O O   . MET B 293 ? 0.3500 0.2643 0.2778 -0.0043 -0.0285 -0.0259 594 MET B O   
5731  C CB  . MET B 293 ? 0.2810 0.2046 0.2160 -0.0173 -0.0255 -0.0249 594 MET B CB  
5732  C CG  . MET B 293 ? 0.3708 0.2857 0.2971 -0.0178 -0.0236 -0.0233 594 MET B CG  
5733  S SD  . MET B 293 ? 0.3694 0.2943 0.3015 -0.0193 -0.0230 -0.0227 594 MET B SD  
5734  C CE  . MET B 293 ? 0.3236 0.2537 0.2594 -0.0119 -0.0267 -0.0233 594 MET B CE  
5735  N N   . GLY B 294 ? 0.3841 0.2756 0.2940 -0.0092 -0.0244 -0.0244 595 GLY B N   
5736  C CA  . GLY B 294 ? 0.4057 0.2880 0.3075 -0.0011 -0.0253 -0.0239 595 GLY B CA  
5737  C C   . GLY B 294 ? 0.4580 0.3476 0.3629 0.0061  -0.0281 -0.0231 595 GLY B C   
5738  O O   . GLY B 294 ? 0.3560 0.2471 0.2608 0.0134  -0.0299 -0.0235 595 GLY B O   
5739  N N   . THR B 295 ? 0.4114 0.3060 0.3189 0.0043  -0.0285 -0.0222 596 THR B N   
5740  C CA  . THR B 295 ? 0.4111 0.3122 0.3206 0.0105  -0.0316 -0.0218 596 THR B CA  
5741  C C   . THR B 295 ? 0.3329 0.2494 0.2550 0.0124  -0.0344 -0.0237 596 THR B C   
5742  O O   . THR B 295 ? 0.3445 0.2670 0.2685 0.0182  -0.0374 -0.0239 596 THR B O   
5743  C CB  . THR B 295 ? 0.3311 0.2342 0.2402 0.0078  -0.0313 -0.0209 596 THR B CB  
5744  O OG1 . THR B 295 ? 0.3288 0.2403 0.2469 0.0010  -0.0300 -0.0219 596 THR B OG1 
5745  C CG2 . THR B 295 ? 0.3685 0.2565 0.2636 0.0072  -0.0286 -0.0185 596 THR B CG2 
5746  N N   . GLU B 296 ? 0.3250 0.2485 0.2556 0.0074  -0.0336 -0.0249 597 GLU B N   
5747  C CA  . GLU B 296 ? 0.3161 0.2527 0.2575 0.0088  -0.0357 -0.0263 597 GLU B CA  
5748  C C   . GLU B 296 ? 0.3199 0.2567 0.2596 0.0156  -0.0368 -0.0266 597 GLU B C   
5749  O O   . GLU B 296 ? 0.3123 0.2594 0.2580 0.0194  -0.0393 -0.0272 597 GLU B O   
5750  C CB  . GLU B 296 ? 0.3754 0.3173 0.3238 0.0033  -0.0343 -0.0272 597 GLU B CB  
5751  C CG  . GLU B 296 ? 0.3391 0.2834 0.2907 -0.0024 -0.0334 -0.0269 597 GLU B CG  
5752  C CD  . GLU B 296 ? 0.3475 0.2973 0.3052 -0.0067 -0.0325 -0.0275 597 GLU B CD  
5753  O OE1 . GLU B 296 ? 0.3033 0.2618 0.2687 -0.0064 -0.0337 -0.0280 597 GLU B OE1 
5754  O OE2 . GLU B 296 ? 0.3545 0.2998 0.3090 -0.0105 -0.0307 -0.0275 597 GLU B OE2 
5755  N N   . ILE B 297 ? 0.3132 0.2386 0.2444 0.0173  -0.0347 -0.0264 598 ILE B N   
5756  C CA  . ILE B 297 ? 0.4132 0.3372 0.3412 0.0249  -0.0352 -0.0267 598 ILE B CA  
5757  C C   . ILE B 297 ? 0.3781 0.2954 0.2973 0.0322  -0.0367 -0.0252 598 ILE B C   
5758  O O   . ILE B 297 ? 0.3785 0.3051 0.3014 0.0390  -0.0393 -0.0253 598 ILE B O   
5759  C CB  . ILE B 297 ? 0.3709 0.2832 0.2915 0.0240  -0.0323 -0.0274 598 ILE B CB  
5760  C CG1 . ILE B 297 ? 0.3411 0.2605 0.2696 0.0170  -0.0312 -0.0288 598 ILE B CG1 
5761  C CG2 . ILE B 297 ? 0.3163 0.2259 0.2323 0.0333  -0.0323 -0.0278 598 ILE B CG2 
5762  C CD1 . ILE B 297 ? 0.3255 0.2318 0.2452 0.0137  -0.0285 -0.0298 598 ILE B CD1 
5763  N N   . GLY B 298 ? 0.3217 0.2233 0.2290 0.0308  -0.0350 -0.0236 599 GLY B N   
5764  C CA  . GLY B 298 ? 0.3679 0.2593 0.2635 0.0385  -0.0359 -0.0217 599 GLY B CA  
5765  C C   . GLY B 298 ? 0.4333 0.3351 0.3327 0.0415  -0.0395 -0.0211 599 GLY B C   
5766  O O   . GLY B 298 ? 0.4693 0.3711 0.3639 0.0502  -0.0419 -0.0201 599 GLY B O   
5767  N N   . VAL B 299 ? 0.3890 0.2994 0.2963 0.0347  -0.0401 -0.0218 600 VAL B N   
5768  C CA  . VAL B 299 ? 0.4137 0.3330 0.3236 0.0369  -0.0436 -0.0218 600 VAL B CA  
5769  C C   . VAL B 299 ? 0.4346 0.3730 0.3586 0.0375  -0.0469 -0.0240 600 VAL B C   
5770  O O   . VAL B 299 ? 0.3600 0.3067 0.2855 0.0437  -0.0506 -0.0243 600 VAL B O   
5771  C CB  . VAL B 299 ? 0.3984 0.3147 0.3067 0.0302  -0.0422 -0.0213 600 VAL B CB  
5772  C CG1 . VAL B 299 ? 0.3962 0.3200 0.3052 0.0328  -0.0459 -0.0217 600 VAL B CG1 
5773  C CG2 . VAL B 299 ? 0.3623 0.2606 0.2568 0.0287  -0.0385 -0.0189 600 VAL B CG2 
5774  N N   . ARG B 300 ? 0.3788 0.3249 0.3134 0.0310  -0.0457 -0.0256 601 ARG B N   
5775  C CA  . ARG B 300 ? 0.3581 0.3211 0.3054 0.0299  -0.0484 -0.0275 601 ARG B CA  
5776  C C   . ARG B 300 ? 0.3990 0.3704 0.3519 0.0342  -0.0487 -0.0282 601 ARG B C   
5777  O O   . ARG B 300 ? 0.4011 0.3843 0.3588 0.0387  -0.0519 -0.0289 601 ARG B O   
5778  C CB  . ARG B 300 ? 0.2853 0.2519 0.2401 0.0215  -0.0470 -0.0285 601 ARG B CB  
5779  C CG  . ARG B 300 ? 0.3322 0.2909 0.2814 0.0177  -0.0459 -0.0278 601 ARG B CG  
5780  C CD  . ARG B 300 ? 0.3137 0.2747 0.2601 0.0199  -0.0492 -0.0283 601 ARG B CD  
5781  N NE  . ARG B 300 ? 0.2809 0.2556 0.2368 0.0196  -0.0527 -0.0305 601 ARG B NE  
5782  C CZ  . ARG B 300 ? 0.2692 0.2497 0.2328 0.0140  -0.0528 -0.0320 601 ARG B CZ  
5783  N NH1 . ARG B 300 ? 0.2766 0.2514 0.2397 0.0094  -0.0498 -0.0317 601 ARG B NH1 
5784  N NH2 . ARG B 300 ? 0.2851 0.2770 0.2567 0.0129  -0.0557 -0.0339 601 ARG B NH2 
5785  N N   . ASP B 301 ? 0.3947 0.3613 0.3472 0.0328  -0.0454 -0.0281 602 ASP B N   
5786  C CA  . ASP B 301 ? 0.4125 0.3874 0.3702 0.0369  -0.0450 -0.0288 602 ASP B CA  
5787  C C   . ASP B 301 ? 0.4258 0.4000 0.3776 0.0472  -0.0466 -0.0282 602 ASP B C   
5788  O O   . ASP B 301 ? 0.3631 0.3519 0.3224 0.0519  -0.0484 -0.0290 602 ASP B O   
5789  C CB  . ASP B 301 ? 0.3425 0.3096 0.2978 0.0341  -0.0412 -0.0290 602 ASP B CB  
5790  C CG  . ASP B 301 ? 0.3762 0.3471 0.3387 0.0251  -0.0400 -0.0295 602 ASP B CG  
5791  O OD1 . ASP B 301 ? 0.3681 0.3509 0.3400 0.0221  -0.0417 -0.0301 602 ASP B OD1 
5792  O OD2 . ASP B 301 ? 0.4193 0.3812 0.3775 0.0211  -0.0375 -0.0294 602 ASP B OD2 
5793  N N   . TYR B 302 ? 0.4095 0.3672 0.3477 0.0510  -0.0460 -0.0266 603 TYR B N   
5794  C CA  . TYR B 302 ? 0.3574 0.3120 0.2881 0.0621  -0.0472 -0.0256 603 TYR B CA  
5795  C C   . TYR B 302 ? 0.4200 0.3818 0.3502 0.0670  -0.0517 -0.0249 603 TYR B C   
5796  O O   . TYR B 302 ? 0.4105 0.3793 0.3403 0.0766  -0.0541 -0.0247 603 TYR B O   
5797  C CB  . TYR B 302 ? 0.3359 0.2668 0.2500 0.0645  -0.0440 -0.0240 603 TYR B CB  
5798  C CG  . TYR B 302 ? 0.3538 0.2777 0.2657 0.0640  -0.0403 -0.0250 603 TYR B CG  
5799  C CD1 . TYR B 302 ? 0.3730 0.2744 0.2699 0.0641  -0.0371 -0.0242 603 TYR B CD1 
5800  C CD2 . TYR B 302 ? 0.3570 0.2961 0.2810 0.0630  -0.0398 -0.0269 603 TYR B CD2 
5801  C CE1 . TYR B 302 ? 0.4369 0.3311 0.3307 0.0634  -0.0339 -0.0257 603 TYR B CE1 
5802  C CE2 . TYR B 302 ? 0.4030 0.3354 0.3238 0.0628  -0.0364 -0.0281 603 TYR B CE2 
5803  C CZ  . TYR B 302 ? 0.4147 0.3246 0.3204 0.0631  -0.0337 -0.0277 603 TYR B CZ  
5804  O OH  . TYR B 302 ? 0.4458 0.3484 0.3473 0.0627  -0.0306 -0.0293 603 TYR B OH  
5805  N N   . CYS B 303 ? 0.3972 0.3578 0.3268 0.0612  -0.0532 -0.0248 604 CYS B N   
5806  C CA  . CYS B 303 ? 0.4508 0.4139 0.3757 0.0665  -0.0573 -0.0239 604 CYS B CA  
5807  C C   . CYS B 303 ? 0.4383 0.4185 0.3742 0.0619  -0.0613 -0.0260 604 CYS B C   
5808  O O   . CYS B 303 ? 0.3708 0.3557 0.3036 0.0665  -0.0656 -0.0258 604 CYS B O   
5809  C CB  . CYS B 303 ? 0.3844 0.3273 0.2938 0.0661  -0.0556 -0.0215 604 CYS B CB  
5810  S SG  . CYS B 303 ? 0.4447 0.3647 0.3378 0.0721  -0.0515 -0.0189 604 CYS B SG  
5811  N N   . ASP B 304 ? 0.3765 0.3647 0.3237 0.0530  -0.0603 -0.0279 605 ASP B N   
5812  C CA  . ASP B 304 ? 0.3657 0.3704 0.3234 0.0490  -0.0642 -0.0303 605 ASP B CA  
5813  C C   . ASP B 304 ? 0.3872 0.4091 0.3514 0.0560  -0.0680 -0.0311 605 ASP B C   
5814  O O   . ASP B 304 ? 0.4379 0.4641 0.4051 0.0609  -0.0664 -0.0307 605 ASP B O   
5815  C CB  . ASP B 304 ? 0.2963 0.3070 0.2652 0.0396  -0.0620 -0.0319 605 ASP B CB  
5816  C CG  . ASP B 304 ? 0.4040 0.4040 0.3695 0.0321  -0.0600 -0.0319 605 ASP B CG  
5817  O OD1 . ASP B 304 ? 0.4280 0.4157 0.3829 0.0333  -0.0594 -0.0306 605 ASP B OD1 
5818  O OD2 . ASP B 304 ? 0.4255 0.4300 0.3992 0.0252  -0.0587 -0.0331 605 ASP B OD2 
5819  N N   . ASN B 305 ? 0.3502 0.3827 0.3163 0.0567  -0.0732 -0.0325 606 ASN B N   
5820  C CA  . ASN B 305 ? 0.3339 0.3863 0.3078 0.0628  -0.0776 -0.0336 606 ASN B CA  
5821  C C   . ASN B 305 ? 0.3508 0.4200 0.3404 0.0579  -0.0762 -0.0354 606 ASN B C   
5822  O O   . ASN B 305 ? 0.3759 0.4602 0.3722 0.0642  -0.0774 -0.0356 606 ASN B O   
5823  C CB  . ASN B 305 ? 0.3727 0.4345 0.3467 0.0621  -0.0837 -0.0354 606 ASN B CB  
5824  C CG  . ASN B 305 ? 0.5901 0.6384 0.5479 0.0697  -0.0856 -0.0332 606 ASN B CG  
5825  O OD1 . ASN B 305 ? 0.5862 0.6286 0.5360 0.0799  -0.0851 -0.0306 606 ASN B OD1 
5826  N ND2 . ASN B 305 ? 0.6163 0.6585 0.5682 0.0649  -0.0874 -0.0341 606 ASN B ND2 
5827  N N   . SER B 306 ? 0.4013 0.4681 0.3965 0.0474  -0.0735 -0.0365 607 SER B N   
5828  C CA  . SER B 306 ? 0.4238 0.5043 0.4326 0.0415  -0.0717 -0.0378 607 SER B CA  
5829  C C   . SER B 306 ? 0.4339 0.5078 0.4423 0.0431  -0.0661 -0.0362 607 SER B C   
5830  O O   . SER B 306 ? 0.3729 0.4573 0.3914 0.0388  -0.0639 -0.0369 607 SER B O   
5831  C CB  . SER B 306 ? 0.4652 0.5442 0.4784 0.0296  -0.0714 -0.0396 607 SER B CB  
5832  O OG  . SER B 306 ? 0.7507 0.8318 0.7617 0.0276  -0.0762 -0.0414 607 SER B OG  
5833  N N   . ARG B 307 ? 0.4477 0.5040 0.4442 0.0484  -0.0636 -0.0342 608 ARG B N   
5834  C CA  . ARG B 307 ? 0.2893 0.3366 0.2832 0.0491  -0.0585 -0.0331 608 ARG B CA  
5835  C C   . ARG B 307 ? 0.3171 0.3638 0.3056 0.0610  -0.0581 -0.0321 608 ARG B C   
5836  O O   . ARG B 307 ? 0.3808 0.4446 0.3759 0.0668  -0.0608 -0.0327 608 ARG B O   
5837  C CB  . ARG B 307 ? 0.3440 0.3714 0.3289 0.0440  -0.0557 -0.0321 608 ARG B CB  
5838  C CG  . ARG B 307 ? 0.3652 0.3938 0.3556 0.0335  -0.0559 -0.0331 608 ARG B CG  
5839  C CD  . ARG B 307 ? 0.4050 0.4433 0.4063 0.0275  -0.0536 -0.0339 608 ARG B CD  
5840  N NE  . ARG B 307 ? 0.3508 0.3825 0.3496 0.0285  -0.0494 -0.0330 608 ARG B NE  
5841  C CZ  . ARG B 307 ? 0.4032 0.4203 0.3951 0.0257  -0.0467 -0.0321 608 ARG B CZ  
5842  N NH1 . ARG B 307 ? 0.3222 0.3300 0.3092 0.0221  -0.0473 -0.0317 608 ARG B NH1 
5843  N NH2 . ARG B 307 ? 0.4003 0.4126 0.3899 0.0265  -0.0433 -0.0317 608 ARG B NH2 
5844  N N   . TYR B 308 ? 0.3247 0.3528 0.3014 0.0648  -0.0547 -0.0306 609 TYR B N   
5845  C CA  . TYR B 308 ? 0.4104 0.4367 0.3811 0.0766  -0.0540 -0.0299 609 TYR B CA  
5846  C C   . TYR B 308 ? 0.4007 0.4250 0.3634 0.0857  -0.0580 -0.0286 609 TYR B C   
5847  O O   . TYR B 308 ? 0.4430 0.4725 0.4038 0.0970  -0.0588 -0.0281 609 TYR B O   
5848  C CB  . TYR B 308 ? 0.3646 0.3699 0.3238 0.0774  -0.0492 -0.0291 609 TYR B CB  
5849  C CG  . TYR B 308 ? 0.3785 0.3901 0.3451 0.0739  -0.0455 -0.0304 609 TYR B CG  
5850  C CD1 . TYR B 308 ? 0.3574 0.3701 0.3303 0.0626  -0.0439 -0.0311 609 TYR B CD1 
5851  C CD2 . TYR B 308 ? 0.4152 0.4320 0.3819 0.0826  -0.0435 -0.0309 609 TYR B CD2 
5852  C CE1 . TYR B 308 ? 0.3653 0.3836 0.3439 0.0597  -0.0405 -0.0320 609 TYR B CE1 
5853  C CE2 . TYR B 308 ? 0.3685 0.3913 0.3412 0.0796  -0.0399 -0.0320 609 TYR B CE2 
5854  C CZ  . TYR B 308 ? 0.4043 0.4276 0.3827 0.0680  -0.0385 -0.0325 609 TYR B CZ  
5855  O OH  . TYR B 308 ? 0.3434 0.3720 0.3264 0.0653  -0.0348 -0.0333 609 TYR B OH  
5856  N N   . ASN B 309 ? 0.3598 0.3766 0.3171 0.0818  -0.0604 -0.0279 610 ASN B N   
5857  C CA  . ASN B 309 ? 0.4238 0.4430 0.3755 0.0890  -0.0652 -0.0270 610 ASN B CA  
5858  C C   . ASN B 309 ? 0.4194 0.4262 0.3572 0.1023  -0.0647 -0.0246 610 ASN B C   
5859  O O   . ASN B 309 ? 0.3799 0.3990 0.3192 0.1128  -0.0680 -0.0244 610 ASN B O   
5860  C CB  . ASN B 309 ? 0.4676 0.5143 0.4343 0.0890  -0.0701 -0.0291 610 ASN B CB  
5861  C CG  . ASN B 309 ? 0.4625 0.5144 0.4243 0.0956  -0.0760 -0.0286 610 ASN B CG  
5862  O OD1 . ASN B 309 ? 0.4209 0.4565 0.3698 0.0960  -0.0767 -0.0270 610 ASN B OD1 
5863  N ND2 . ASN B 309 ? 0.3781 0.4539 0.3503 0.1008  -0.0803 -0.0299 610 ASN B ND2 
5864  N N   . ILE B 310 ? 0.4226 0.4044 0.3463 0.1018  -0.0605 -0.0229 611 ILE B N   
5865  C CA  . ILE B 310 ? 0.3665 0.3321 0.2752 0.1137  -0.0589 -0.0208 611 ILE B CA  
5866  C C   . ILE B 310 ? 0.4758 0.4249 0.3680 0.1188  -0.0607 -0.0178 611 ILE B C   
5867  O O   . ILE B 310 ? 0.5068 0.4389 0.3839 0.1287  -0.0592 -0.0155 611 ILE B O   
5868  C CB  . ILE B 310 ? 0.4032 0.3494 0.3043 0.1107  -0.0529 -0.0208 611 ILE B CB  
5869  C CG1 . ILE B 310 ? 0.4099 0.3361 0.3016 0.1005  -0.0505 -0.0197 611 ILE B CG1 
5870  C CG2 . ILE B 310 ? 0.4856 0.4468 0.4016 0.1050  -0.0508 -0.0235 611 ILE B CG2 
5871  C CD1 . ILE B 310 ? 0.4291 0.3335 0.3102 0.0976  -0.0452 -0.0196 611 ILE B CD1 
5872  N N   . LEU B 311 ? 0.4128 0.3647 0.3061 0.1123  -0.0633 -0.0177 612 LEU B N   
5873  C CA  . LEU B 311 ? 0.4644 0.3999 0.3409 0.1165  -0.0645 -0.0146 612 LEU B CA  
5874  C C   . LEU B 311 ? 0.4085 0.3446 0.2762 0.1324  -0.0679 -0.0125 612 LEU B C   
5875  O O   . LEU B 311 ? 0.4292 0.3424 0.2784 0.1396  -0.0658 -0.0093 612 LEU B O   
5876  C CB  . LEU B 311 ? 0.4108 0.3548 0.2918 0.1089  -0.0678 -0.0155 612 LEU B CB  
5877  C CG  . LEU B 311 ? 0.4414 0.3760 0.3233 0.0953  -0.0638 -0.0162 612 LEU B CG  
5878  C CD1 . LEU B 311 ? 0.4743 0.4180 0.3599 0.0899  -0.0673 -0.0173 612 LEU B CD1 
5879  C CD2 . LEU B 311 ? 0.3893 0.2966 0.2533 0.0951  -0.0591 -0.0130 612 LEU B CD2 
5880  N N   . GLU B 312 ? 0.4739 0.4360 0.3544 0.1383  -0.0730 -0.0142 613 GLU B N   
5881  C CA  . GLU B 312 ? 0.4810 0.4468 0.3542 0.1545  -0.0768 -0.0122 613 GLU B CA  
5882  C C   . GLU B 312 ? 0.5014 0.4490 0.3625 0.1648  -0.0724 -0.0102 613 GLU B C   
5883  O O   . GLU B 312 ? 0.5417 0.4710 0.3843 0.1759  -0.0725 -0.0067 613 GLU B O   
5884  C CB  . GLU B 312 ? 0.5887 0.5891 0.4808 0.1583  -0.0823 -0.0149 613 GLU B CB  
5885  C CG  . GLU B 312 ? 0.7791 0.7950 0.6740 0.1583  -0.0895 -0.0154 613 GLU B CG  
5886  C CD  . GLU B 312 ? 0.8990 0.9468 0.8081 0.1666  -0.0953 -0.0172 613 GLU B CD  
5887  O OE1 . GLU B 312 ? 0.8506 0.8993 0.7527 0.1823  -0.0969 -0.0150 613 GLU B OE1 
5888  O OE2 . GLU B 312 ? 0.9442 1.0162 0.8713 0.1575  -0.0982 -0.0208 613 GLU B OE2 
5889  N N   . GLU B 313 ? 0.4901 0.4414 0.3602 0.1615  -0.0684 -0.0125 614 GLU B N   
5890  C CA  . GLU B 313 ? 0.5246 0.4596 0.3834 0.1717  -0.0643 -0.0114 614 GLU B CA  
5891  C C   . GLU B 313 ? 0.4917 0.3901 0.3284 0.1696  -0.0597 -0.0087 614 GLU B C   
5892  O O   . GLU B 313 ? 0.6080 0.4866 0.4270 0.1815  -0.0583 -0.0060 614 GLU B O   
5893  C CB  . GLU B 313 ? 0.5191 0.4649 0.3915 0.1673  -0.0606 -0.0146 614 GLU B CB  
5894  C CG  . GLU B 313 ? 0.6744 0.6114 0.5379 0.1812  -0.0577 -0.0141 614 GLU B CG  
5895  C CD  . GLU B 313 ? 0.8901 0.8330 0.7634 0.1764  -0.0532 -0.0172 614 GLU B CD  
5896  O OE1 . GLU B 313 ? 0.9791 0.9097 0.8427 0.1862  -0.0496 -0.0173 614 GLU B OE1 
5897  O OE2 . GLU B 313 ? 0.8783 0.8370 0.7677 0.1633  -0.0531 -0.0195 614 GLU B OE2 
5898  N N   . VAL B 314 ? 0.4847 0.3736 0.3217 0.1544  -0.0571 -0.0092 615 VAL B N   
5899  C CA  . VAL B 314 ? 0.4692 0.3253 0.2866 0.1503  -0.0525 -0.0068 615 VAL B CA  
5900  C C   . VAL B 314 ? 0.5689 0.4107 0.3690 0.1576  -0.0546 -0.0026 615 VAL B C   
5901  O O   . VAL B 314 ? 0.6111 0.4249 0.3902 0.1636  -0.0516 0.0004  615 VAL B O   
5902  C CB  . VAL B 314 ? 0.5001 0.3541 0.3243 0.1325  -0.0496 -0.0085 615 VAL B CB  
5903  C CG1 . VAL B 314 ? 0.4706 0.2939 0.2755 0.1269  -0.0453 -0.0058 615 VAL B CG1 
5904  C CG2 . VAL B 314 ? 0.4955 0.3581 0.3323 0.1265  -0.0468 -0.0120 615 VAL B CG2 
5905  N N   . ALA B 315 ? 0.5020 0.3613 0.3092 0.1572  -0.0598 -0.0024 616 ALA B N   
5906  C CA  . ALA B 315 ? 0.4989 0.3457 0.2891 0.1643  -0.0622 0.0016  616 ALA B CA  
5907  C C   . ALA B 315 ? 0.6360 0.4781 0.4147 0.1832  -0.0643 0.0042  616 ALA B C   
5908  O O   . ALA B 315 ? 0.5957 0.4127 0.3522 0.1907  -0.0631 0.0085  616 ALA B O   
5909  C CB  . ALA B 315 ? 0.4844 0.3530 0.2852 0.1602  -0.0678 0.0006  616 ALA B CB  
5910  N N   . LYS B 316 ? 0.6268 0.4925 0.4198 0.1914  -0.0671 0.0017  617 LYS B N   
5911  C CA  . LYS B 316 ? 0.7482 0.6109 0.5312 0.2106  -0.0687 0.0039  617 LYS B CA  
5912  C C   . LYS B 316 ? 0.7144 0.5415 0.4763 0.2150  -0.0623 0.0061  617 LYS B C   
5913  O O   . LYS B 316 ? 0.6884 0.4925 0.4283 0.2264  -0.0620 0.0104  617 LYS B O   
5914  C CB  . LYS B 316 ? 0.8145 0.7097 0.6184 0.2170  -0.0715 0.0005  617 LYS B CB  
5915  C CG  . LYS B 316 ? 0.8954 0.8247 0.7145 0.2209  -0.0794 -0.0006 617 LYS B CG  
5916  C CD  . LYS B 316 ? 0.9555 0.9151 0.7938 0.2278  -0.0810 -0.0036 617 LYS B CD  
5917  C CE  . LYS B 316 ? 0.9727 0.9677 0.8261 0.2323  -0.0892 -0.0048 617 LYS B CE  
5918  N NZ  . LYS B 316 ? 0.9420 0.9533 0.8107 0.2149  -0.0917 -0.0078 617 LYS B NZ  
5919  N N   . LYS B 317 ? 0.7178 0.5387 0.4849 0.2055  -0.0570 0.0032  618 LYS B N   
5920  C CA  . LYS B 317 ? 0.7035 0.4897 0.4502 0.2079  -0.0508 0.0045  618 LYS B CA  
5921  C C   . LYS B 317 ? 0.7224 0.4764 0.4477 0.2013  -0.0478 0.0083  618 LYS B C   
5922  O O   . LYS B 317 ? 0.6904 0.4124 0.3932 0.2072  -0.0439 0.0108  618 LYS B O   
5923  C CB  . LYS B 317 ? 0.6463 0.4339 0.4033 0.1974  -0.0462 0.0002  618 LYS B CB  
5924  C CG  . LYS B 317 ? 0.7776 0.5952 0.5541 0.2042  -0.0480 -0.0033 618 LYS B CG  
5925  C CD  . LYS B 317 ? 0.8424 0.6502 0.6180 0.2021  -0.0426 -0.0063 618 LYS B CD  
5926  C CE  . LYS B 317 ? 1.0388 0.8243 0.7946 0.2192  -0.0400 -0.0049 618 LYS B CE  
5927  N NZ  . LYS B 317 ? 1.1166 0.9279 0.8827 0.2361  -0.0431 -0.0055 618 LYS B NZ  
5928  N N   . MET B 318 ? 0.6688 0.4301 0.3997 0.1897  -0.0495 0.0088  619 MET B N   
5929  C CA  . MET B 318 ? 0.6926 0.4261 0.4035 0.1842  -0.0467 0.0128  619 MET B CA  
5930  C C   . MET B 318 ? 0.7248 0.4508 0.4193 0.1982  -0.0504 0.0178  619 MET B C   
5931  O O   . MET B 318 ? 0.7320 0.4336 0.4077 0.1950  -0.0478 0.0218  619 MET B O   
5932  C CB  . MET B 318 ? 0.6256 0.3693 0.3484 0.1662  -0.0462 0.0113  619 MET B CB  
5933  C CG  . MET B 318 ? 0.5697 0.3094 0.3005 0.1511  -0.0411 0.0080  619 MET B CG  
5934  S SD  . MET B 318 ? 0.6116 0.3680 0.3590 0.1323  -0.0411 0.0059  619 MET B SD  
5935  C CE  . MET B 318 ? 0.5565 0.2869 0.2812 0.1292  -0.0385 0.0112  619 MET B CE  
5936  N N   . ASN B 319 ? 0.7178 0.4650 0.4191 0.2135  -0.0562 0.0177  620 ASN B N   
5937  C CA  . ASN B 319 ? 0.8323 0.5764 0.5193 0.2284  -0.0609 0.0222  620 ASN B CA  
5938  C C   . ASN B 319 ? 0.8624 0.6128 0.5494 0.2203  -0.0638 0.0237  620 ASN B C   
5939  O O   . ASN B 319 ? 0.8136 0.5479 0.4809 0.2277  -0.0650 0.0286  620 ASN B O   
5940  C CB  . ASN B 319 ? 0.9357 0.6401 0.5923 0.2392  -0.0567 0.0273  620 ASN B CB  
5941  C CG  . ASN B 319 ? 1.0663 0.7636 0.7206 0.2497  -0.0541 0.0257  620 ASN B CG  
5942  O OD1 . ASN B 319 ? 1.1335 0.8575 0.8026 0.2606  -0.0582 0.0234  620 ASN B OD1 
5943  N ND2 . ASN B 319 ? 1.1116 0.7731 0.7473 0.2460  -0.0471 0.0268  620 ASN B ND2 
5944  N N   . LEU B 320 ? 0.7716 0.5447 0.4798 0.2056  -0.0649 0.0196  621 LEU B N   
5945  C CA  . LEU B 320 ? 0.7834 0.5622 0.4917 0.1976  -0.0672 0.0204  621 LEU B CA  
5946  C C   . LEU B 320 ? 0.8251 0.6281 0.5380 0.2091  -0.0758 0.0207  621 LEU B C   
5947  O O   . LEU B 320 ? 0.8047 0.6313 0.5311 0.2183  -0.0805 0.0184  621 LEU B O   
5948  C CB  . LEU B 320 ? 0.7120 0.5063 0.4405 0.1792  -0.0655 0.0158  621 LEU B CB  
5949  C CG  . LEU B 320 ? 0.6481 0.4216 0.3734 0.1666  -0.0576 0.0153  621 LEU B CG  
5950  C CD1 . LEU B 320 ? 0.5683 0.3586 0.3128 0.1498  -0.0567 0.0112  621 LEU B CD1 
5951  C CD2 . LEU B 320 ? 0.6415 0.3805 0.3408 0.1657  -0.0526 0.0204  621 LEU B CD2 
5952  N N   . ASP B 321 ? 0.9148 0.7124 0.6162 0.2084  -0.0779 0.0234  622 ASP B N   
5953  C CA  . ASP B 321 ? 0.8838 0.7061 0.5905 0.2162  -0.0866 0.0229  622 ASP B CA  
5954  C C   . ASP B 321 ? 0.6888 0.5427 0.4221 0.2037  -0.0899 0.0167  622 ASP B C   
5955  O O   . ASP B 321 ? 0.6458 0.4973 0.3818 0.1896  -0.0875 0.0153  622 ASP B O   
5956  C CB  . ASP B 321 ? 0.9697 0.7751 0.6545 0.2187  -0.0875 0.0276  622 ASP B CB  
5957  C CG  . ASP B 321 ? 1.0274 0.8592 0.7179 0.2243  -0.0968 0.0263  622 ASP B CG  
5958  O OD1 . ASP B 321 ? 1.0853 0.9119 0.7665 0.2192  -0.0976 0.0275  622 ASP B OD1 
5959  O OD2 . ASP B 321 ? 0.9347 0.7931 0.6394 0.2333  -0.1033 0.0237  622 ASP B OD2 
5960  N N   . MET B 322 ? 0.6123 0.4953 0.3648 0.2087  -0.0949 0.0131  623 MET B N   
5961  C CA  . MET B 322 ? 0.6304 0.5430 0.4080 0.1971  -0.0979 0.0072  623 MET B CA  
5962  C C   . MET B 322 ? 0.6321 0.5715 0.4167 0.2014  -0.1071 0.0053  623 MET B C   
5963  O O   . MET B 322 ? 0.7594 0.7258 0.5651 0.1937  -0.1106 0.0003  623 MET B O   
5964  C CB  . MET B 322 ? 0.6340 0.5618 0.4303 0.1966  -0.0962 0.0039  623 MET B CB  
5965  C CG  . MET B 322 ? 0.7363 0.6394 0.5264 0.1923  -0.0876 0.0050  623 MET B CG  
5966  S SD  . MET B 322 ? 0.7391 0.6589 0.5468 0.1964  -0.0861 0.0018  623 MET B SD  
5967  C CE  . MET B 322 ? 0.6128 0.5684 0.4496 0.1825  -0.0897 -0.0041 623 MET B CE  
5968  N N   . ARG B 323 ? 0.6468 0.5788 0.4133 0.2131  -0.1113 0.0092  624 ARG B N   
5969  C CA  . ARG B 323 ? 0.7795 0.7374 0.5516 0.2172  -0.1208 0.0072  624 ARG B CA  
5970  C C   . ARG B 323 ? 0.7065 0.6662 0.4790 0.2038  -0.1220 0.0047  624 ARG B C   
5971  O O   . ARG B 323 ? 0.7529 0.7365 0.5337 0.2034  -0.1298 0.0014  624 ARG B O   
5972  C CB  . ARG B 323 ? 0.8858 0.8364 0.6377 0.2360  -0.1254 0.0124  624 ARG B CB  
5973  C CG  . ARG B 323 ? 0.9621 0.9314 0.7214 0.2521  -0.1298 0.0126  624 ARG B CG  
5974  C CD  . ARG B 323 ? 1.1329 1.0913 0.8716 0.2689  -0.1321 0.0177  624 ARG B CD  
5975  N NE  . ARG B 323 ? 1.2494 1.1666 0.9627 0.2731  -0.1244 0.0236  624 ARG B NE  
5976  C CZ  . ARG B 323 ? 1.3429 1.2335 1.0346 0.2697  -0.1217 0.0275  624 ARG B CZ  
5977  N NH1 . ARG B 323 ? 1.3904 1.2908 1.0819 0.2630  -0.1264 0.0261  624 ARG B NH1 
5978  N NH2 . ARG B 323 ? 1.3731 1.2269 1.0431 0.2723  -0.1140 0.0327  624 ARG B NH2 
5979  N N   . LYS B 324 ? 0.6347 0.5704 0.3985 0.1929  -0.1147 0.0060  625 LYS B N   
5980  C CA  . LYS B 324 ? 0.6969 0.6325 0.4595 0.1813  -0.1151 0.0038  625 LYS B CA  
5981  C C   . LYS B 324 ? 0.6727 0.5964 0.4416 0.1658  -0.1068 0.0023  625 LYS B C   
5982  O O   . LYS B 324 ? 0.7069 0.6108 0.4701 0.1652  -0.0998 0.0052  625 LYS B O   
5983  C CB  . LYS B 324 ? 0.8429 0.7589 0.5796 0.1879  -0.1157 0.0088  625 LYS B CB  
5984  C CG  . LYS B 324 ? 0.9981 0.8811 0.7139 0.1937  -0.1084 0.0153  625 LYS B CG  
5985  C CD  . LYS B 324 ? 1.0602 0.9241 0.7494 0.2014  -0.1092 0.0208  625 LYS B CD  
5986  C CE  . LYS B 324 ? 1.0968 0.9247 0.7659 0.1996  -0.0996 0.0265  625 LYS B CE  
5987  N NZ  . LYS B 324 ? 1.1398 0.9517 0.7911 0.1944  -0.0968 0.0293  625 LYS B NZ  
5988  N N   . THR B 325 ? 0.5489 0.4845 0.3292 0.1535  -0.1078 -0.0023 626 THR B N   
5989  C CA  . THR B 325 ? 0.5971 0.5240 0.3847 0.1395  -0.1004 -0.0039 626 THR B CA  
5990  C C   . THR B 325 ? 0.5364 0.4350 0.3045 0.1365  -0.0934 0.0005  626 THR B C   
5991  O O   . THR B 325 ? 0.5580 0.4436 0.3277 0.1289  -0.0860 0.0013  626 THR B O   
5992  C CB  . THR B 325 ? 0.6783 0.6234 0.4812 0.1280  -0.1031 -0.0098 626 THR B CB  
5993  O OG1 . THR B 325 ? 0.7278 0.6714 0.5189 0.1282  -0.1066 -0.0101 626 THR B OG1 
5994  C CG2 . THR B 325 ? 0.6029 0.5765 0.4260 0.1289  -0.1095 -0.0143 626 THR B CG2 
5995  N N   . SER B 326 ? 0.5631 0.4525 0.3126 0.1423  -0.0955 0.0035  627 SER B N   
5996  C CA  . SER B 326 ? 0.6025 0.4666 0.3336 0.1384  -0.0885 0.0076  627 SER B CA  
5997  C C   . SER B 326 ? 0.6385 0.4780 0.3556 0.1433  -0.0825 0.0132  627 SER B C   
5998  O O   . SER B 326 ? 0.5815 0.3988 0.2839 0.1387  -0.0757 0.0169  627 SER B O   
5999  C CB  . SER B 326 ? 0.6014 0.4627 0.3154 0.1436  -0.0925 0.0093  627 SER B CB  
6000  O OG  . SER B 326 ? 0.7106 0.5654 0.4091 0.1583  -0.0964 0.0138  627 SER B OG  
6001  N N   . SER B 327 ? 0.6350 0.4776 0.3561 0.1522  -0.0845 0.0139  628 SER B N   
6002  C CA  . SER B 327 ? 0.6970 0.5154 0.4072 0.1544  -0.0779 0.0179  628 SER B CA  
6003  C C   . SER B 327 ? 0.6291 0.4441 0.3516 0.1405  -0.0710 0.0155  628 SER B C   
6004  O O   . SER B 327 ? 0.5795 0.3721 0.2918 0.1387  -0.0646 0.0185  628 SER B O   
6005  C CB  . SER B 327 ? 0.6354 0.4580 0.3462 0.1685  -0.0817 0.0189  628 SER B CB  
6006  O OG  . SER B 327 ? 0.6232 0.4676 0.3577 0.1649  -0.0832 0.0138  628 SER B OG  
6007  N N   . LEU B 328 ? 0.5144 0.3503 0.2573 0.1307  -0.0724 0.0102  629 LEU B N   
6008  C CA  . LEU B 328 ? 0.5433 0.3796 0.2997 0.1181  -0.0669 0.0075  629 LEU B CA  
6009  C C   . LEU B 328 ? 0.5189 0.3501 0.2791 0.1213  -0.0646 0.0077  629 LEU B C   
6010  O O   . LEU B 328 ? 0.4987 0.3177 0.2593 0.1134  -0.0584 0.0079  629 LEU B O   
6011  C CB  . LEU B 328 ? 0.5409 0.3590 0.2872 0.1081  -0.0597 0.0097  629 LEU B CB  
6012  C CG  . LEU B 328 ? 0.6253 0.4465 0.3653 0.1059  -0.0611 0.0098  629 LEU B CG  
6013  C CD1 . LEU B 328 ? 0.5328 0.3407 0.2672 0.0947  -0.0533 0.0112  629 LEU B CD1 
6014  C CD2 . LEU B 328 ? 0.5545 0.4019 0.3124 0.1034  -0.0673 0.0042  629 LEU B CD2 
6015  N N   . TRP B 329 ? 0.5459 0.3876 0.3090 0.1331  -0.0699 0.0074  630 TRP B N   
6016  C CA  . TRP B 329 ? 0.5268 0.3657 0.2940 0.1374  -0.0679 0.0071  630 TRP B CA  
6017  C C   . TRP B 329 ? 0.5024 0.3554 0.2906 0.1263  -0.0659 0.0025  630 TRP B C   
6018  O O   . TRP B 329 ? 0.5063 0.3486 0.2947 0.1236  -0.0611 0.0024  630 TRP B O   
6019  C CB  . TRP B 329 ? 0.5064 0.3580 0.2745 0.1528  -0.0741 0.0075  630 TRP B CB  
6020  C CG  . TRP B 329 ? 0.5906 0.4751 0.3785 0.1531  -0.0812 0.0031  630 TRP B CG  
6021  C CD1 . TRP B 329 ? 0.6186 0.5171 0.4062 0.1563  -0.0878 0.0026  630 TRP B CD1 
6022  C CD2 . TRP B 329 ? 0.4657 0.3729 0.2758 0.1497  -0.0825 -0.0013 630 TRP B CD2 
6023  N NE1 . TRP B 329 ? 0.5713 0.4996 0.3799 0.1544  -0.0931 -0.0021 630 TRP B NE1 
6024  C CE2 . TRP B 329 ? 0.4905 0.4246 0.3132 0.1503  -0.0897 -0.0044 630 TRP B CE2 
6025  C CE3 . TRP B 329 ? 0.5857 0.4928 0.4054 0.1460  -0.0781 -0.0030 630 TRP B CE3 
6026  C CZ2 . TRP B 329 ? 0.4742 0.4346 0.3190 0.1467  -0.0922 -0.0088 630 TRP B CZ2 
6027  C CZ3 . TRP B 329 ? 0.6036 0.5369 0.4448 0.1433  -0.0806 -0.0072 630 TRP B CZ3 
6028  C CH2 . TRP B 329 ? 0.5102 0.4697 0.3639 0.1433  -0.0874 -0.0099 630 TRP B CH2 
6029  N N   . LYS B 330 ? 0.4536 0.3294 0.2587 0.1198  -0.0695 -0.0014 631 LYS B N   
6030  C CA  . LYS B 330 ? 0.4405 0.3277 0.2639 0.1092  -0.0672 -0.0053 631 LYS B CA  
6031  C C   . LYS B 330 ? 0.5270 0.3970 0.3459 0.0980  -0.0603 -0.0045 631 LYS B C   
6032  O O   . LYS B 330 ? 0.4680 0.3352 0.2932 0.0929  -0.0565 -0.0056 631 LYS B O   
6033  C CB  . LYS B 330 ? 0.4484 0.3600 0.2883 0.1038  -0.0719 -0.0094 631 LYS B CB  
6034  C CG  . LYS B 330 ? 0.4976 0.4313 0.3471 0.1122  -0.0787 -0.0112 631 LYS B CG  
6035  C CD  . LYS B 330 ? 0.5217 0.4776 0.3881 0.1040  -0.0824 -0.0157 631 LYS B CD  
6036  C CE  . LYS B 330 ? 0.5426 0.5233 0.4217 0.1101  -0.0885 -0.0181 631 LYS B CE  
6037  N NZ  . LYS B 330 ? 0.4721 0.4726 0.3666 0.1009  -0.0920 -0.0226 631 LYS B NZ  
6038  N N   . ASP B 331 ? 0.4763 0.3356 0.2842 0.0942  -0.0586 -0.0025 632 ASP B N   
6039  C CA  . ASP B 331 ? 0.4551 0.3004 0.2593 0.0833  -0.0520 -0.0016 632 ASP B CA  
6040  C C   . ASP B 331 ? 0.4745 0.2978 0.2666 0.0844  -0.0469 0.0011  632 ASP B C   
6041  O O   . ASP B 331 ? 0.4967 0.3152 0.2935 0.0756  -0.0424 0.0001  632 ASP B O   
6042  C CB  . ASP B 331 ? 0.5469 0.3848 0.3397 0.0806  -0.0508 0.0004  632 ASP B CB  
6043  C CG  . ASP B 331 ? 0.5326 0.3892 0.3327 0.0820  -0.0567 -0.0022 632 ASP B CG  
6044  O OD1 . ASP B 331 ? 0.4981 0.3620 0.2959 0.0917  -0.0625 -0.0020 632 ASP B OD1 
6045  O OD2 . ASP B 331 ? 0.5074 0.3713 0.3152 0.0734  -0.0556 -0.0046 632 ASP B OD2 
6046  N N   . GLN B 332 ? 0.4861 0.2954 0.2620 0.0955  -0.0479 0.0046  633 GLN B N   
6047  C CA  . GLN B 332 ? 0.5117 0.2967 0.2733 0.0973  -0.0431 0.0073  633 GLN B CA  
6048  C C   . GLN B 332 ? 0.4925 0.2830 0.2652 0.0974  -0.0425 0.0042  633 GLN B C   
6049  O O   . GLN B 332 ? 0.5386 0.3154 0.3082 0.0904  -0.0375 0.0039  633 GLN B O   
6050  C CB  . GLN B 332 ? 0.5601 0.3295 0.3018 0.1110  -0.0448 0.0116  633 GLN B CB  
6051  C CG  . GLN B 332 ? 0.8051 0.5496 0.5253 0.1084  -0.0403 0.0164  633 GLN B CG  
6052  C CD  . GLN B 332 ? 0.8700 0.5955 0.5684 0.1225  -0.0415 0.0212  633 GLN B CD  
6053  O OE1 . GLN B 332 ? 0.8166 0.5543 0.5158 0.1348  -0.0477 0.0214  633 GLN B OE1 
6054  N NE2 . GLN B 332 ? 1.0524 0.7478 0.7308 0.1208  -0.0355 0.0250  633 GLN B NE2 
6055  N N   . ALA B 333 ? 0.4748 0.2852 0.2595 0.1054  -0.0477 0.0020  634 ALA B N   
6056  C CA  . ALA B 333 ? 0.4956 0.3134 0.2914 0.1061  -0.0471 -0.0010 634 ALA B CA  
6057  C C   . ALA B 333 ? 0.5082 0.3354 0.3193 0.0922  -0.0445 -0.0043 634 ALA B C   
6058  O O   . ALA B 333 ? 0.5066 0.3273 0.3191 0.0884  -0.0411 -0.0057 634 ALA B O   
6059  C CB  . ALA B 333 ? 0.4790 0.3201 0.2865 0.1165  -0.0530 -0.0027 634 ALA B CB  
6060  N N   . LEU B 334 ? 0.5288 0.3704 0.3503 0.0849  -0.0462 -0.0057 635 LEU B N   
6061  C CA  . LEU B 334 ? 0.4083 0.2594 0.2440 0.0727  -0.0441 -0.0085 635 LEU B CA  
6062  C C   . LEU B 334 ? 0.4748 0.3069 0.3021 0.0640  -0.0381 -0.0075 635 LEU B C   
6063  O O   . LEU B 334 ? 0.5136 0.3481 0.3489 0.0576  -0.0358 -0.0097 635 LEU B O   
6064  C CB  . LEU B 334 ? 0.4180 0.2833 0.2621 0.0675  -0.0465 -0.0097 635 LEU B CB  
6065  C CG  . LEU B 334 ? 0.4495 0.3252 0.3078 0.0561  -0.0448 -0.0124 635 LEU B CG  
6066  C CD1 . LEU B 334 ? 0.4366 0.3288 0.3107 0.0562  -0.0467 -0.0155 635 LEU B CD1 
6067  C CD2 . LEU B 334 ? 0.4310 0.3151 0.2925 0.0523  -0.0465 -0.0131 635 LEU B CD2 
6068  N N   . VAL B 335 ? 0.4336 0.2472 0.2446 0.0632  -0.0354 -0.0042 636 VAL B N   
6069  C CA  . VAL B 335 ? 0.5270 0.3234 0.3303 0.0536  -0.0296 -0.0032 636 VAL B CA  
6070  C C   . VAL B 335 ? 0.5785 0.3614 0.3758 0.0557  -0.0274 -0.0038 636 VAL B C   
6071  O O   . VAL B 335 ? 0.4469 0.2286 0.2491 0.0470  -0.0246 -0.0059 636 VAL B O   
6072  C CB  . VAL B 335 ? 0.5869 0.3653 0.3725 0.0525  -0.0267 0.0008  636 VAL B CB  
6073  C CG1 . VAL B 335 ? 0.5654 0.3252 0.3422 0.0425  -0.0205 0.0018  636 VAL B CG1 
6074  C CG2 . VAL B 335 ? 0.5024 0.2942 0.2941 0.0490  -0.0280 0.0008  636 VAL B CG2 
6075  N N   . GLU B 336 ? 0.5172 0.2903 0.3034 0.0679  -0.0290 -0.0022 637 GLU B N   
6076  C CA  . GLU B 336 ? 0.5858 0.3437 0.3641 0.0713  -0.0267 -0.0029 637 GLU B CA  
6077  C C   . GLU B 336 ? 0.5681 0.3430 0.3633 0.0689  -0.0276 -0.0072 637 GLU B C   
6078  O O   . GLU B 336 ? 0.5154 0.2801 0.3078 0.0640  -0.0245 -0.0089 637 GLU B O   
6079  C CB  . GLU B 336 ? 0.5298 0.2772 0.2946 0.0870  -0.0287 -0.0005 637 GLU B CB  
6080  C CG  . GLU B 336 ? 0.6376 0.3659 0.3829 0.0909  -0.0278 0.0043  637 GLU B CG  
6081  C CD  . GLU B 336 ? 0.7188 0.4179 0.4464 0.0823  -0.0216 0.0064  637 GLU B CD  
6082  O OE1 . GLU B 336 ? 0.7381 0.4294 0.4664 0.0750  -0.0183 0.0040  637 GLU B OE1 
6083  O OE2 . GLU B 336 ? 0.7898 0.4736 0.5021 0.0825  -0.0200 0.0105  637 GLU B OE2 
6084  N N   . ILE B 337 ? 0.5492 0.3496 0.3612 0.0723  -0.0320 -0.0089 638 ILE B N   
6085  C CA  . ILE B 337 ? 0.4892 0.3068 0.3176 0.0698  -0.0326 -0.0126 638 ILE B CA  
6086  C C   . ILE B 337 ? 0.5008 0.3193 0.3358 0.0558  -0.0297 -0.0143 638 ILE B C   
6087  O O   . ILE B 337 ? 0.4255 0.2440 0.2643 0.0522  -0.0280 -0.0167 638 ILE B O   
6088  C CB  . ILE B 337 ? 0.4222 0.2666 0.2671 0.0738  -0.0376 -0.0139 638 ILE B CB  
6089  C CG1 . ILE B 337 ? 0.4929 0.3399 0.3332 0.0884  -0.0407 -0.0127 638 ILE B CG1 
6090  C CG2 . ILE B 337 ? 0.4146 0.2771 0.2771 0.0683  -0.0376 -0.0173 638 ILE B CG2 
6091  C CD1 . ILE B 337 ? 0.5166 0.3874 0.3695 0.0916  -0.0460 -0.0133 638 ILE B CD1 
6092  N N   . ASN B 338 ? 0.4699 0.2898 0.3060 0.0482  -0.0292 -0.0132 639 ASN B N   
6093  C CA  . ASN B 338 ? 0.4403 0.2638 0.2839 0.0358  -0.0267 -0.0147 639 ASN B CA  
6094  C C   . ASN B 338 ? 0.4707 0.2728 0.3013 0.0295  -0.0223 -0.0143 639 ASN B C   
6095  O O   . ASN B 338 ? 0.4969 0.3018 0.3334 0.0212  -0.0206 -0.0165 639 ASN B O   
6096  C CB  . ASN B 338 ? 0.4072 0.2405 0.2567 0.0306  -0.0274 -0.0139 639 ASN B CB  
6097  C CG  . ASN B 338 ? 0.4293 0.2855 0.2955 0.0319  -0.0312 -0.0159 639 ASN B CG  
6098  O OD1 . ASN B 338 ? 0.4290 0.2968 0.3074 0.0258  -0.0310 -0.0180 639 ASN B OD1 
6099  N ND2 . ASN B 338 ? 0.4538 0.3165 0.3200 0.0402  -0.0349 -0.0153 639 ASN B ND2 
6100  N N   . ILE B 339 ? 0.4538 0.2344 0.2663 0.0334  -0.0204 -0.0115 640 ILE B N   
6101  C CA  . ILE B 339 ? 0.4569 0.2142 0.2549 0.0281  -0.0162 -0.0113 640 ILE B CA  
6102  C C   . ILE B 339 ? 0.5499 0.3050 0.3487 0.0310  -0.0162 -0.0144 640 ILE B C   
6103  O O   . ILE B 339 ? 0.5016 0.2506 0.2994 0.0222  -0.0138 -0.0167 640 ILE B O   
6104  C CB  . ILE B 339 ? 0.4843 0.2170 0.2609 0.0338  -0.0143 -0.0074 640 ILE B CB  
6105  C CG1 . ILE B 339 ? 0.4982 0.2310 0.2720 0.0288  -0.0131 -0.0043 640 ILE B CG1 
6106  C CG2 . ILE B 339 ? 0.5091 0.2143 0.2683 0.0300  -0.0101 -0.0076 640 ILE B CG2 
6107  C CD1 . ILE B 339 ? 0.5485 0.2569 0.3003 0.0344  -0.0111 0.0002  640 ILE B CD1 
6108  N N   . ALA B 340 ? 0.5030 0.2643 0.3039 0.0434  -0.0190 -0.0148 641 ALA B N   
6109  C CA  . ALA B 340 ? 0.5761 0.3353 0.3767 0.0478  -0.0187 -0.0176 641 ALA B CA  
6110  C C   . ALA B 340 ? 0.5941 0.3716 0.4114 0.0393  -0.0191 -0.0210 641 ALA B C   
6111  O O   . ALA B 340 ? 0.5077 0.2773 0.3215 0.0351  -0.0171 -0.0236 641 ALA B O   
6112  C CB  . ALA B 340 ? 0.5648 0.3318 0.3669 0.0630  -0.0216 -0.0172 641 ALA B CB  
6113  N N   . VAL B 341 ? 0.4621 0.2631 0.2964 0.0370  -0.0217 -0.0212 642 VAL B N   
6114  C CA  . VAL B 341 ? 0.5084 0.3264 0.3579 0.0296  -0.0222 -0.0238 642 VAL B CA  
6115  C C   . VAL B 341 ? 0.4659 0.2749 0.3117 0.0172  -0.0194 -0.0249 642 VAL B C   
6116  O O   . VAL B 341 ? 0.4674 0.2767 0.3150 0.0132  -0.0186 -0.0276 642 VAL B O   
6117  C CB  . VAL B 341 ? 0.4177 0.2586 0.2834 0.0287  -0.0252 -0.0234 642 VAL B CB  
6118  C CG1 . VAL B 341 ? 0.4044 0.2597 0.2836 0.0201  -0.0252 -0.0254 642 VAL B CG1 
6119  C CG2 . VAL B 341 ? 0.3714 0.2245 0.2430 0.0397  -0.0282 -0.0234 642 VAL B CG2 
6120  N N   . LEU B 342 ? 0.4441 0.2453 0.2844 0.0110  -0.0179 -0.0228 643 LEU B N   
6121  C CA  . LEU B 342 ? 0.4668 0.2628 0.3055 -0.0016 -0.0153 -0.0238 643 LEU B CA  
6122  C C   . LEU B 342 ? 0.4871 0.2606 0.3103 -0.0036 -0.0127 -0.0253 643 LEU B C   
6123  O O   . LEU B 342 ? 0.5201 0.2943 0.3453 -0.0115 -0.0121 -0.0282 643 LEU B O   
6124  C CB  . LEU B 342 ? 0.4108 0.2042 0.2468 -0.0075 -0.0137 -0.0211 643 LEU B CB  
6125  C CG  . LEU B 342 ? 0.4031 0.2188 0.2546 -0.0078 -0.0158 -0.0205 643 LEU B CG  
6126  C CD1 . LEU B 342 ? 0.4604 0.2714 0.3062 -0.0094 -0.0142 -0.0173 643 LEU B CD1 
6127  C CD2 . LEU B 342 ? 0.3874 0.2191 0.2526 -0.0162 -0.0161 -0.0227 643 LEU B CD2 
6128  N N   . TYR B 343 ? 0.4605 0.2131 0.2672 0.0034  -0.0114 -0.0235 644 TYR B N   
6129  C CA  . TYR B 343 ? 0.5185 0.2462 0.3080 0.0025  -0.0088 -0.0250 644 TYR B CA  
6130  C C   . TYR B 343 ? 0.6125 0.3450 0.4058 0.0056  -0.0098 -0.0289 644 TYR B C   
6131  O O   . TYR B 343 ? 0.5128 0.2335 0.2987 -0.0012 -0.0080 -0.0318 644 TYR B O   
6132  C CB  . TYR B 343 ? 0.5071 0.2133 0.2789 0.0132  -0.0077 -0.0221 644 TYR B CB  
6133  C CG  . TYR B 343 ? 0.5783 0.2567 0.3306 0.0156  -0.0051 -0.0236 644 TYR B CG  
6134  C CD1 . TYR B 343 ? 0.6031 0.2591 0.3411 0.0042  -0.0015 -0.0241 644 TYR B CD1 
6135  C CD2 . TYR B 343 ? 0.5424 0.2162 0.2896 0.0293  -0.0060 -0.0246 644 TYR B CD2 
6136  C CE1 . TYR B 343 ? 0.6561 0.2837 0.3742 0.0061  0.0010  -0.0257 644 TYR B CE1 
6137  C CE2 . TYR B 343 ? 0.6591 0.3051 0.3865 0.0325  -0.0033 -0.0261 644 TYR B CE2 
6138  C CZ  . TYR B 343 ? 0.6646 0.2866 0.3770 0.0207  0.0001  -0.0267 644 TYR B CZ  
6139  O OH  . TYR B 343 ? 0.7253 0.3171 0.4164 0.0230  0.0029  -0.0285 644 TYR B OH  
6140  N N   . SER B 344 ? 0.5236 0.2731 0.3277 0.0158  -0.0124 -0.0291 645 SER B N   
6141  C CA  . SER B 344 ? 0.5126 0.2663 0.3192 0.0203  -0.0128 -0.0324 645 SER B CA  
6142  C C   . SER B 344 ? 0.4679 0.2349 0.2855 0.0093  -0.0132 -0.0353 645 SER B C   
6143  O O   . SER B 344 ? 0.5192 0.2769 0.3299 0.0061  -0.0120 -0.0385 645 SER B O   
6144  C CB  . SER B 344 ? 0.4635 0.2348 0.2804 0.0328  -0.0152 -0.0315 645 SER B CB  
6145  O OG  . SER B 344 ? 0.5428 0.3004 0.3475 0.0442  -0.0150 -0.0291 645 SER B OG  
6146  N N   . PHE B 345 ? 0.4182 0.2062 0.2518 0.0038  -0.0150 -0.0342 646 PHE B N   
6147  C CA  . PHE B 345 ? 0.4981 0.2999 0.3424 -0.0058 -0.0158 -0.0364 646 PHE B CA  
6148  C C   . PHE B 345 ? 0.5863 0.3739 0.4211 -0.0175 -0.0139 -0.0381 646 PHE B C   
6149  O O   . PHE B 345 ? 0.4946 0.2822 0.3286 -0.0228 -0.0139 -0.0413 646 PHE B O   
6150  C CB  . PHE B 345 ? 0.3811 0.2050 0.2422 -0.0086 -0.0177 -0.0345 646 PHE B CB  
6151  C CG  . PHE B 345 ? 0.3631 0.2064 0.2376 -0.0017 -0.0200 -0.0345 646 PHE B CG  
6152  C CD1 . PHE B 345 ? 0.4229 0.2668 0.2965 0.0093  -0.0207 -0.0334 646 PHE B CD1 
6153  C CD2 . PHE B 345 ? 0.3851 0.2465 0.2730 -0.0064 -0.0214 -0.0353 646 PHE B CD2 
6154  C CE1 . PHE B 345 ? 0.3963 0.2591 0.2829 0.0143  -0.0226 -0.0334 646 PHE B CE1 
6155  C CE2 . PHE B 345 ? 0.3381 0.2160 0.2376 -0.0011 -0.0230 -0.0351 646 PHE B CE2 
6156  C CZ  . PHE B 345 ? 0.4026 0.2815 0.3018 0.0087  -0.0235 -0.0342 646 PHE B CZ  
6157  N N   . GLN B 346 ? 0.5272 0.3027 0.3541 -0.0220 -0.0121 -0.0359 647 GLN B N   
6158  C CA  . GLN B 346 ? 0.5462 0.3086 0.3642 -0.0344 -0.0100 -0.0374 647 GLN B CA  
6159  C C   . GLN B 346 ? 0.5799 0.3191 0.3807 -0.0339 -0.0084 -0.0404 647 GLN B C   
6160  O O   . GLN B 346 ? 0.6078 0.3435 0.4057 -0.0435 -0.0081 -0.0438 647 GLN B O   
6161  C CB  . GLN B 346 ? 0.5018 0.2549 0.3136 -0.0388 -0.0077 -0.0340 647 GLN B CB  
6162  C CG  . GLN B 346 ? 0.5414 0.3174 0.3696 -0.0430 -0.0088 -0.0320 647 GLN B CG  
6163  C CD  . GLN B 346 ? 0.6394 0.4079 0.4618 -0.0439 -0.0065 -0.0281 647 GLN B CD  
6164  O OE1 . GLN B 346 ? 0.6930 0.4387 0.4988 -0.0411 -0.0043 -0.0265 647 GLN B OE1 
6165  N NE2 . GLN B 346 ? 0.5828 0.3699 0.4180 -0.0471 -0.0070 -0.0266 647 GLN B NE2 
6166  N N   . SER B 347 ? 0.5442 0.2676 0.3334 -0.0221 -0.0075 -0.0395 648 SER B N   
6167  C CA  . SER B 347 ? 0.5741 0.2741 0.3458 -0.0195 -0.0058 -0.0425 648 SER B CA  
6168  C C   . SER B 347 ? 0.6830 0.3941 0.4610 -0.0195 -0.0073 -0.0468 648 SER B C   
6169  O O   . SER B 347 ? 0.6209 0.3174 0.3875 -0.0252 -0.0062 -0.0507 648 SER B O   
6170  C CB  . SER B 347 ? 0.5777 0.2627 0.3378 -0.0044 -0.0048 -0.0404 648 SER B CB  
6171  O OG  . SER B 347 ? 0.6142 0.2821 0.3629 -0.0054 -0.0029 -0.0367 648 SER B OG  
6172  N N   . ASP B 348 ? 0.5567 0.2929 0.3518 -0.0135 -0.0097 -0.0462 649 ASP B N   
6173  C CA  . ASP B 348 ? 0.5491 0.2965 0.3500 -0.0133 -0.0108 -0.0497 649 ASP B CA  
6174  C C   . ASP B 348 ? 0.5539 0.3170 0.3657 -0.0262 -0.0126 -0.0512 649 ASP B C   
6175  O O   . ASP B 348 ? 0.4861 0.2601 0.3031 -0.0269 -0.0139 -0.0538 649 ASP B O   
6176  C CB  . ASP B 348 ? 0.5302 0.2962 0.3430 -0.0012 -0.0121 -0.0483 649 ASP B CB  
6177  C CG  . ASP B 348 ? 0.5810 0.3325 0.3821 0.0126  -0.0104 -0.0480 649 ASP B CG  
6178  O OD1 . ASP B 348 ? 0.5624 0.2876 0.3448 0.0129  -0.0082 -0.0491 649 ASP B OD1 
6179  O OD2 . ASP B 348 ? 0.5680 0.3341 0.3782 0.0231  -0.0113 -0.0466 649 ASP B OD2 
6180  N N   . LYS B 349 ? 0.5080 0.2727 0.3227 -0.0360 -0.0125 -0.0495 650 LYS B N   
6181  C CA  . LYS B 349 ? 0.5191 0.2999 0.3444 -0.0478 -0.0143 -0.0508 650 LYS B CA  
6182  C C   . LYS B 349 ? 0.5095 0.3173 0.3533 -0.0438 -0.0169 -0.0498 650 LYS B C   
6183  O O   . LYS B 349 ? 0.5129 0.3327 0.3627 -0.0484 -0.0187 -0.0520 650 LYS B O   
6184  C CB  . LYS B 349 ? 0.6266 0.3964 0.4415 -0.0564 -0.0142 -0.0556 650 LYS B CB  
6185  C CG  . LYS B 349 ? 0.7888 0.5300 0.5844 -0.0622 -0.0114 -0.0567 650 LYS B CG  
6186  C CD  . LYS B 349 ? 0.9823 0.7135 0.7680 -0.0730 -0.0117 -0.0620 650 LYS B CD  
6187  C CE  . LYS B 349 ? 1.1366 0.8617 0.9188 -0.0883 -0.0107 -0.0623 650 LYS B CE  
6188  N NZ  . LYS B 349 ? 1.2502 0.9667 1.0231 -0.1001 -0.0115 -0.0679 650 LYS B NZ  
6189  N N   . VAL B 350 ? 0.4663 0.2828 0.3180 -0.0352 -0.0172 -0.0465 651 VAL B N   
6190  C CA  . VAL B 350 ? 0.3968 0.2371 0.2655 -0.0321 -0.0193 -0.0449 651 VAL B CA  
6191  C C   . VAL B 350 ? 0.4595 0.3098 0.3373 -0.0365 -0.0197 -0.0420 651 VAL B C   
6192  O O   . VAL B 350 ? 0.3767 0.2185 0.2500 -0.0343 -0.0185 -0.0398 651 VAL B O   
6193  C CB  . VAL B 350 ? 0.4531 0.2968 0.3243 -0.0198 -0.0194 -0.0437 651 VAL B CB  
6194  C CG1 . VAL B 350 ? 0.4130 0.2797 0.3012 -0.0177 -0.0214 -0.0419 651 VAL B CG1 
6195  C CG2 . VAL B 350 ? 0.3804 0.2147 0.2423 -0.0147 -0.0184 -0.0466 651 VAL B CG2 
6196  N N   . THR B 351 ? 0.3896 0.2573 0.2791 -0.0422 -0.0214 -0.0420 652 THR B N   
6197  C CA  . THR B 351 ? 0.3966 0.2748 0.2949 -0.0460 -0.0215 -0.0396 652 THR B CA  
6198  C C   . THR B 351 ? 0.4164 0.2972 0.3186 -0.0380 -0.0215 -0.0367 652 THR B C   
6199  O O   . THR B 351 ? 0.4014 0.2891 0.3089 -0.0305 -0.0227 -0.0363 652 THR B O   
6200  C CB  . THR B 351 ? 0.4062 0.3046 0.3174 -0.0499 -0.0236 -0.0398 652 THR B CB  
6201  O OG1 . THR B 351 ? 0.4774 0.3749 0.3850 -0.0567 -0.0243 -0.0429 652 THR B OG1 
6202  C CG2 . THR B 351 ? 0.3572 0.2650 0.2758 -0.0544 -0.0231 -0.0378 652 THR B CG2 
6203  N N   . ILE B 352 ? 0.3565 0.2318 0.2555 -0.0400 -0.0200 -0.0348 653 ILE B N   
6204  C CA  . ILE B 352 ? 0.3524 0.2310 0.2548 -0.0337 -0.0202 -0.0321 653 ILE B CA  
6205  C C   . ILE B 352 ? 0.3958 0.2740 0.2976 -0.0399 -0.0184 -0.0304 653 ILE B C   
6206  O O   . ILE B 352 ? 0.4321 0.3024 0.3275 -0.0479 -0.0164 -0.0310 653 ILE B O   
6207  C CB  . ILE B 352 ? 0.3692 0.2334 0.2612 -0.0251 -0.0198 -0.0314 653 ILE B CB  
6208  C CG1 . ILE B 352 ? 0.3618 0.2343 0.2599 -0.0177 -0.0214 -0.0293 653 ILE B CG1 
6209  C CG2 . ILE B 352 ? 0.3620 0.2049 0.2384 -0.0285 -0.0171 -0.0309 653 ILE B CG2 
6210  C CD1 . ILE B 352 ? 0.3669 0.2326 0.2592 -0.0076 -0.0221 -0.0290 653 ILE B CD1 
6211  N N   . VAL B 353 ? 0.3940 0.2814 0.3025 -0.0366 -0.0190 -0.0284 654 VAL B N   
6212  C CA  . VAL B 353 ? 0.3556 0.2436 0.2635 -0.0412 -0.0169 -0.0266 654 VAL B CA  
6213  C C   . VAL B 353 ? 0.3413 0.2229 0.2439 -0.0342 -0.0168 -0.0244 654 VAL B C   
6214  O O   . VAL B 353 ? 0.3592 0.2470 0.2666 -0.0268 -0.0192 -0.0243 654 VAL B O   
6215  C CB  . VAL B 353 ? 0.3997 0.3071 0.3211 -0.0446 -0.0175 -0.0267 654 VAL B CB  
6216  C CG1 . VAL B 353 ? 0.3003 0.2190 0.2308 -0.0373 -0.0200 -0.0263 654 VAL B CG1 
6217  C CG2 . VAL B 353 ? 0.3598 0.2686 0.2803 -0.0502 -0.0145 -0.0252 654 VAL B CG2 
6218  N N   . ASP B 354 ? 0.3476 0.2167 0.2397 -0.0369 -0.0139 -0.0225 655 ASP B N   
6219  C CA  . ASP B 354 ? 0.4119 0.2754 0.2981 -0.0301 -0.0141 -0.0202 655 ASP B CA  
6220  C C   . ASP B 354 ? 0.4364 0.3139 0.3312 -0.0307 -0.0140 -0.0193 655 ASP B C   
6221  O O   . ASP B 354 ? 0.4015 0.2901 0.3044 -0.0370 -0.0128 -0.0199 655 ASP B O   
6222  C CB  . ASP B 354 ? 0.4156 0.2581 0.2850 -0.0317 -0.0109 -0.0181 655 ASP B CB  
6223  C CG  . ASP B 354 ? 0.5013 0.3428 0.3687 -0.0420 -0.0068 -0.0170 655 ASP B CG  
6224  O OD1 . ASP B 354 ? 0.6319 0.4666 0.4954 -0.0503 -0.0048 -0.0181 655 ASP B OD1 
6225  O OD2 . ASP B 354 ? 0.5194 0.3675 0.3891 -0.0422 -0.0056 -0.0153 655 ASP B OD2 
6226  N N   . HIS B 355 ? 0.4511 0.3285 0.3439 -0.0235 -0.0156 -0.0181 656 HIS B N   
6227  C CA  . HIS B 355 ? 0.3945 0.2844 0.2947 -0.0231 -0.0159 -0.0178 656 HIS B CA  
6228  C C   . HIS B 355 ? 0.4044 0.2935 0.3014 -0.0297 -0.0116 -0.0163 656 HIS B C   
6229  O O   . HIS B 355 ? 0.4347 0.3368 0.3404 -0.0317 -0.0109 -0.0167 656 HIS B O   
6230  C CB  . HIS B 355 ? 0.3695 0.2587 0.2668 -0.0147 -0.0187 -0.0172 656 HIS B CB  
6231  C CG  . HIS B 355 ? 0.4033 0.2762 0.2855 -0.0108 -0.0179 -0.0149 656 HIS B CG  
6232  N ND1 . HIS B 355 ? 0.4591 0.3201 0.3336 -0.0074 -0.0185 -0.0147 656 HIS B ND1 
6233  C CD2 . HIS B 355 ? 0.3561 0.2221 0.2286 -0.0089 -0.0166 -0.0126 656 HIS B CD2 
6234  C CE1 . HIS B 355 ? 0.4793 0.3262 0.3399 -0.0034 -0.0176 -0.0121 656 HIS B CE1 
6235  N NE2 . HIS B 355 ? 0.4418 0.2915 0.3007 -0.0045 -0.0165 -0.0107 656 HIS B NE2 
6236  N N   . HIS B 356 ? 0.3466 0.2207 0.2313 -0.0335 -0.0083 -0.0145 657 HIS B N   
6237  C CA  . HIS B 356 ? 0.4198 0.2947 0.3023 -0.0407 -0.0037 -0.0129 657 HIS B CA  
6238  C C   . HIS B 356 ? 0.4034 0.2915 0.2970 -0.0491 -0.0024 -0.0146 657 HIS B C   
6239  O O   . HIS B 356 ? 0.4263 0.3288 0.3285 -0.0513 -0.0009 -0.0147 657 HIS B O   
6240  C CB  . HIS B 356 ? 0.4528 0.3074 0.3186 -0.0435 -0.0001 -0.0103 657 HIS B CB  
6241  C CG  . HIS B 356 ? 0.4902 0.3321 0.3441 -0.0344 -0.0016 -0.0082 657 HIS B CG  
6242  N ND1 . HIS B 356 ? 0.4903 0.3358 0.3422 -0.0298 -0.0017 -0.0067 657 HIS B ND1 
6243  C CD2 . HIS B 356 ? 0.5465 0.3731 0.3899 -0.0282 -0.0035 -0.0076 657 HIS B CD2 
6244  C CE1 . HIS B 356 ? 0.5371 0.3706 0.3779 -0.0216 -0.0038 -0.0052 657 HIS B CE1 
6245  N NE2 . HIS B 356 ? 0.5612 0.3836 0.3971 -0.0201 -0.0049 -0.0055 657 HIS B NE2 
6246  N N   . SER B 357 ? 0.4119 0.2959 0.3055 -0.0530 -0.0032 -0.0162 658 SER B N   
6247  C CA  . SER B 357 ? 0.3912 0.2886 0.2952 -0.0607 -0.0028 -0.0181 658 SER B CA  
6248  C C   . SER B 357 ? 0.3186 0.2358 0.2376 -0.0565 -0.0058 -0.0195 658 SER B C   
6249  O O   . SER B 357 ? 0.3319 0.2643 0.2602 -0.0606 -0.0046 -0.0199 658 SER B O   
6250  C CB  . SER B 357 ? 0.3853 0.2734 0.2850 -0.0646 -0.0038 -0.0200 658 SER B CB  
6251  O OG  . SER B 357 ? 0.5816 0.4841 0.4916 -0.0714 -0.0044 -0.0221 658 SER B OG  
6252  N N   . ALA B 358 ? 0.3318 0.2490 0.2528 -0.0481 -0.0095 -0.0202 659 ALA B N   
6253  C CA  . ALA B 358 ? 0.3382 0.2713 0.2719 -0.0446 -0.0122 -0.0214 659 ALA B CA  
6254  C C   . ALA B 358 ? 0.3851 0.3279 0.3234 -0.0428 -0.0108 -0.0206 659 ALA B C   
6255  O O   . ALA B 358 ? 0.3079 0.2650 0.2561 -0.0436 -0.0109 -0.0212 659 ALA B O   
6256  C CB  . ALA B 358 ? 0.3399 0.2701 0.2741 -0.0371 -0.0160 -0.0222 659 ALA B CB  
6257  N N   . THR B 359 ? 0.3471 0.2820 0.2776 -0.0394 -0.0097 -0.0191 660 THR B N   
6258  C CA  . THR B 359 ? 0.2927 0.2355 0.2259 -0.0372 -0.0081 -0.0186 660 THR B CA  
6259  C C   . THR B 359 ? 0.2961 0.2462 0.2313 -0.0440 -0.0035 -0.0177 660 THR B C   
6260  O O   . THR B 359 ? 0.3124 0.2757 0.2553 -0.0431 -0.0024 -0.0181 660 THR B O   
6261  C CB  . THR B 359 ? 0.3370 0.2695 0.2602 -0.0320 -0.0083 -0.0174 660 THR B CB  
6262  O OG1 . THR B 359 ? 0.3710 0.2893 0.2821 -0.0350 -0.0058 -0.0155 660 THR B OG1 
6263  C CG2 . THR B 359 ? 0.2953 0.2255 0.2194 -0.0252 -0.0132 -0.0187 660 THR B CG2 
6264  N N   . GLU B 360 ? 0.3075 0.2495 0.2360 -0.0510 -0.0007 -0.0167 661 GLU B N   
6265  C CA  . GLU B 360 ? 0.4113 0.3618 0.3427 -0.0591 0.0037  -0.0160 661 GLU B CA  
6266  C C   . GLU B 360 ? 0.3924 0.3614 0.3379 -0.0615 0.0023  -0.0178 661 GLU B C   
6267  O O   . GLU B 360 ? 0.3546 0.3390 0.3079 -0.0625 0.0045  -0.0177 661 GLU B O   
6268  C CB  . GLU B 360 ? 0.4390 0.3753 0.3599 -0.0672 0.0066  -0.0148 661 GLU B CB  
6269  C CG  . GLU B 360 ? 0.6297 0.5755 0.5541 -0.0777 0.0112  -0.0144 661 GLU B CG  
6270  C CD  . GLU B 360 ? 0.9884 0.9445 0.9150 -0.0769 0.0154  -0.0127 661 GLU B CD  
6271  O OE1 . GLU B 360 ? 1.1911 1.1375 1.1088 -0.0712 0.0165  -0.0110 661 GLU B OE1 
6272  O OE2 . GLU B 360 ? 1.0091 0.9839 0.9464 -0.0816 0.0176  -0.0132 661 GLU B OE2 
6273  N N   . SER B 361 ? 0.3986 0.3665 0.3469 -0.0618 -0.0015 -0.0195 662 SER B N   
6274  C CA  A SER B 361 ? 0.3907 0.3756 0.3512 -0.0632 -0.0034 -0.0210 662 SER B CA  
6275  C CA  B SER B 361 ? 0.3921 0.3769 0.3526 -0.0632 -0.0034 -0.0210 662 SER B CA  
6276  C C   . SER B 361 ? 0.3922 0.3884 0.3609 -0.0550 -0.0050 -0.0212 662 SER B C   
6277  O O   . SER B 361 ? 0.3326 0.3454 0.3109 -0.0553 -0.0046 -0.0215 662 SER B O   
6278  C CB  A SER B 361 ? 0.3954 0.3750 0.3553 -0.0645 -0.0070 -0.0227 662 SER B CB  
6279  C CB  B SER B 361 ? 0.3927 0.3724 0.3528 -0.0643 -0.0071 -0.0227 662 SER B CB  
6280  O OG  A SER B 361 ? 0.3629 0.3321 0.3150 -0.0729 -0.0053 -0.0230 662 SER B OG  
6281  O OG  B SER B 361 ? 0.4105 0.3860 0.3708 -0.0560 -0.0106 -0.0231 662 SER B OG  
6282  N N   . PHE B 362 ? 0.3204 0.3079 0.2850 -0.0477 -0.0068 -0.0210 663 PHE B N   
6283  C CA  . PHE B 362 ? 0.3148 0.3106 0.2857 -0.0406 -0.0082 -0.0214 663 PHE B CA  
6284  C C   . PHE B 362 ? 0.3663 0.3714 0.3393 -0.0399 -0.0043 -0.0207 663 PHE B C   
6285  O O   . PHE B 362 ? 0.3643 0.3817 0.3452 -0.0362 -0.0045 -0.0211 663 PHE B O   
6286  C CB  . PHE B 362 ? 0.3436 0.3286 0.3094 -0.0341 -0.0109 -0.0218 663 PHE B CB  
6287  C CG  . PHE B 362 ? 0.4089 0.4001 0.3798 -0.0278 -0.0122 -0.0225 663 PHE B CG  
6288  C CD1 . PHE B 362 ? 0.2847 0.2824 0.2629 -0.0258 -0.0149 -0.0232 663 PHE B CD1 
6289  C CD2 . PHE B 362 ? 0.3205 0.3105 0.2879 -0.0240 -0.0105 -0.0224 663 PHE B CD2 
6290  C CE1 . PHE B 362 ? 0.2951 0.2962 0.2766 -0.0202 -0.0159 -0.0237 663 PHE B CE1 
6291  C CE2 . PHE B 362 ? 0.4070 0.4006 0.3776 -0.0184 -0.0115 -0.0234 663 PHE B CE2 
6292  C CZ  . PHE B 362 ? 0.3910 0.3895 0.3685 -0.0165 -0.0142 -0.0240 663 PHE B CZ  
6293  N N   . ILE B 363 ? 0.3678 0.3668 0.3332 -0.0428 -0.0006 -0.0194 664 ILE B N   
6294  C CA  . ILE B 363 ? 0.3827 0.3913 0.3498 -0.0424 0.0039  -0.0186 664 ILE B CA  
6295  C C   . ILE B 363 ? 0.3279 0.3548 0.3056 -0.0474 0.0058  -0.0187 664 ILE B C   
6296  O O   . ILE B 363 ? 0.3570 0.3982 0.3419 -0.0435 0.0073  -0.0189 664 ILE B O   
6297  C CB  . ILE B 363 ? 0.3219 0.3196 0.2776 -0.0455 0.0080  -0.0168 664 ILE B CB  
6298  C CG1 . ILE B 363 ? 0.3626 0.3456 0.3086 -0.0387 0.0058  -0.0169 664 ILE B CG1 
6299  C CG2 . ILE B 363 ? 0.3217 0.3314 0.2798 -0.0468 0.0136  -0.0159 664 ILE B CG2 
6300  C CD1 . ILE B 363 ? 0.3702 0.3585 0.3188 -0.0307 0.0049  -0.0182 664 ILE B CD1 
6301  N N   . LYS B 364 ? 0.3154 0.3426 0.2939 -0.0559 0.0057  -0.0188 665 LYS B N   
6302  C CA  . LYS B 364 ? 0.3771 0.4236 0.3663 -0.0612 0.0066  -0.0192 665 LYS B CA  
6303  C C   . LYS B 364 ? 0.3672 0.4258 0.3663 -0.0544 0.0026  -0.0204 665 LYS B C   
6304  O O   . LYS B 364 ? 0.3546 0.4314 0.3627 -0.0521 0.0039  -0.0203 665 LYS B O   
6305  C CB  . LYS B 364 ? 0.3726 0.4153 0.3599 -0.0717 0.0061  -0.0198 665 LYS B CB  
6306  C CG  . LYS B 364 ? 0.4803 0.5071 0.4557 -0.0788 0.0100  -0.0184 665 LYS B CG  
6307  C CD  . LYS B 364 ? 0.7044 0.7431 0.6826 -0.0869 0.0157  -0.0173 665 LYS B CD  
6308  C CE  . LYS B 364 ? 0.8900 0.9281 0.8672 -0.1000 0.0166  -0.0180 665 LYS B CE  
6309  N NZ  . LYS B 364 ? 0.9559 0.9675 0.9184 -0.1032 0.0159  -0.0178 665 LYS B NZ  
6310  N N   . HIS B 365 ? 0.2979 0.3465 0.2948 -0.0505 -0.0020 -0.0212 666 HIS B N   
6311  C CA  . HIS B 365 ? 0.3336 0.3905 0.3378 -0.0439 -0.0056 -0.0218 666 HIS B CA  
6312  C C   . HIS B 365 ? 0.3279 0.3895 0.3341 -0.0352 -0.0041 -0.0214 666 HIS B C   
6313  O O   . HIS B 365 ? 0.2632 0.3395 0.2774 -0.0310 -0.0043 -0.0214 666 HIS B O   
6314  C CB  . HIS B 365 ? 0.2817 0.3250 0.2816 -0.0414 -0.0098 -0.0225 666 HIS B CB  
6315  C CG  . HIS B 365 ? 0.3243 0.3720 0.3291 -0.0341 -0.0130 -0.0227 666 HIS B CG  
6316  N ND1 . HIS B 365 ? 0.2723 0.3338 0.2850 -0.0337 -0.0149 -0.0227 666 HIS B ND1 
6317  C CD2 . HIS B 365 ? 0.3172 0.3569 0.3196 -0.0271 -0.0145 -0.0227 666 HIS B CD2 
6318  C CE1 . HIS B 365 ? 0.3169 0.3772 0.3309 -0.0264 -0.0172 -0.0224 666 HIS B CE1 
6319  N NE2 . HIS B 365 ? 0.2910 0.3380 0.2990 -0.0228 -0.0168 -0.0225 666 HIS B NE2 
6320  N N   . MET B 366 ? 0.3181 0.3669 0.3163 -0.0318 -0.0028 -0.0213 667 MET B N   
6321  C CA  . MET B 366 ? 0.3350 0.3855 0.3329 -0.0237 -0.0014 -0.0214 667 MET B CA  
6322  C C   . MET B 366 ? 0.3426 0.4106 0.3468 -0.0233 0.0029  -0.0209 667 MET B C   
6323  O O   . MET B 366 ? 0.3121 0.3900 0.3219 -0.0165 0.0028  -0.0211 667 MET B O   
6324  C CB  . MET B 366 ? 0.3542 0.3892 0.3416 -0.0218 -0.0005 -0.0216 667 MET B CB  
6325  C CG  . MET B 366 ? 0.4435 0.4764 0.4286 -0.0135 -0.0001 -0.0225 667 MET B CG  
6326  S SD  . MET B 366 ? 0.4873 0.5017 0.4594 -0.0121 -0.0005 -0.0230 667 MET B SD  
6327  C CE  . MET B 366 ? 0.4817 0.4967 0.4508 -0.0035 0.0015  -0.0245 667 MET B CE  
6328  N N   . GLU B 367 ? 0.2907 0.3626 0.2938 -0.0305 0.0069  -0.0200 668 GLU B N   
6329  C CA  . GLU B 367 ? 0.3829 0.4733 0.3926 -0.0309 0.0116  -0.0195 668 GLU B CA  
6330  C C   . GLU B 367 ? 0.3124 0.4228 0.3345 -0.0309 0.0097  -0.0197 668 GLU B C   
6331  O O   . GLU B 367 ? 0.3840 0.5105 0.4132 -0.0250 0.0117  -0.0196 668 GLU B O   
6332  C CB  . GLU B 367 ? 0.3749 0.4650 0.3808 -0.0405 0.0164  -0.0183 668 GLU B CB  
6333  C CG  . GLU B 367 ? 0.4681 0.5391 0.4606 -0.0394 0.0183  -0.0176 668 GLU B CG  
6334  C CD  . GLU B 367 ? 0.5347 0.6029 0.5214 -0.0487 0.0235  -0.0159 668 GLU B CD  
6335  O OE1 . GLU B 367 ? 0.5319 0.5921 0.5096 -0.0467 0.0271  -0.0149 668 GLU B OE1 
6336  O OE2 . GLU B 367 ? 0.5201 0.5931 0.5104 -0.0583 0.0238  -0.0156 668 GLU B OE2 
6337  N N   . ASN B 368 ? 0.3285 0.4383 0.3530 -0.0367 0.0058  -0.0201 669 ASN B N   
6338  C CA  . ASN B 368 ? 0.3662 0.4948 0.4017 -0.0365 0.0032  -0.0204 669 ASN B CA  
6339  C C   . ASN B 368 ? 0.3035 0.4340 0.3417 -0.0247 0.0004  -0.0204 669 ASN B C   
6340  O O   . ASN B 368 ? 0.2947 0.4437 0.3414 -0.0196 0.0006  -0.0201 669 ASN B O   
6341  C CB  . ASN B 368 ? 0.3394 0.4639 0.3746 -0.0446 -0.0008 -0.0212 669 ASN B CB  
6342  C CG  . ASN B 368 ? 0.3876 0.5316 0.4332 -0.0446 -0.0039 -0.0216 669 ASN B CG  
6343  O OD1 . ASN B 368 ? 0.3592 0.5245 0.4136 -0.0457 -0.0017 -0.0214 669 ASN B OD1 
6344  N ND2 . ASN B 368 ? 0.4281 0.5663 0.4727 -0.0426 -0.0090 -0.0221 669 ASN B ND2 
6345  N N   . GLU B 369 ? 0.2714 0.3827 0.3019 -0.0203 -0.0024 -0.0207 670 GLU B N   
6346  C CA  . GLU B 369 ? 0.2935 0.4022 0.3241 -0.0098 -0.0046 -0.0206 670 GLU B CA  
6347  C C   . GLU B 369 ? 0.2790 0.3938 0.3102 -0.0015 -0.0008 -0.0205 670 GLU B C   
6348  O O   . GLU B 369 ? 0.3412 0.4649 0.3768 0.0067  -0.0015 -0.0201 670 GLU B O   
6349  C CB  . GLU B 369 ? 0.2648 0.3516 0.2868 -0.0084 -0.0074 -0.0211 670 GLU B CB  
6350  C CG  . GLU B 369 ? 0.2297 0.3115 0.2515 -0.0141 -0.0112 -0.0213 670 GLU B CG  
6351  C CD  . GLU B 369 ? 0.3379 0.4278 0.3651 -0.0102 -0.0147 -0.0207 670 GLU B CD  
6352  O OE1 . GLU B 369 ? 0.3444 0.4235 0.3681 -0.0057 -0.0172 -0.0205 670 GLU B OE1 
6353  O OE2 . GLU B 369 ? 0.3577 0.4651 0.3923 -0.0117 -0.0149 -0.0204 670 GLU B OE2 
6354  N N   . TYR B 370 ? 0.2838 0.3927 0.3094 -0.0026 0.0033  -0.0208 671 TYR B N   
6355  C CA  . TYR B 370 ? 0.2868 0.4025 0.3124 0.0053  0.0075  -0.0209 671 TYR B CA  
6356  C C   . TYR B 370 ? 0.3748 0.5166 0.4121 0.0062  0.0098  -0.0201 671 TYR B C   
6357  O O   . TYR B 370 ? 0.3747 0.5254 0.4152 0.0162  0.0108  -0.0200 671 TYR B O   
6358  C CB  . TYR B 370 ? 0.3414 0.4480 0.3587 0.0028  0.0119  -0.0212 671 TYR B CB  
6359  C CG  . TYR B 370 ? 0.3648 0.4494 0.3709 0.0074  0.0101  -0.0225 671 TYR B CG  
6360  C CD1 . TYR B 370 ? 0.3769 0.4455 0.3774 0.0027  0.0063  -0.0228 671 TYR B CD1 
6361  C CD2 . TYR B 370 ? 0.4149 0.4953 0.4160 0.0166  0.0122  -0.0236 671 TYR B CD2 
6362  C CE1 . TYR B 370 ? 0.3526 0.4036 0.3441 0.0064  0.0043  -0.0241 671 TYR B CE1 
6363  C CE2 . TYR B 370 ? 0.3708 0.4314 0.3615 0.0198  0.0102  -0.0252 671 TYR B CE2 
6364  C CZ  . TYR B 370 ? 0.4425 0.4896 0.4291 0.0143  0.0061  -0.0254 671 TYR B CZ  
6365  O OH  . TYR B 370 ? 0.4484 0.4782 0.4258 0.0168  0.0038  -0.0271 671 TYR B OH  
6366  N N   . ARG B 371 ? 0.3498 0.5041 0.3932 -0.0040 0.0105  -0.0196 672 ARG B N   
6367  C CA  . ARG B 371 ? 0.4037 0.5855 0.4594 -0.0047 0.0123  -0.0191 672 ARG B CA  
6368  C C   . ARG B 371 ? 0.4205 0.6133 0.4835 0.0022  0.0076  -0.0188 672 ARG B C   
6369  O O   . ARG B 371 ? 0.4499 0.6598 0.5195 0.0110  0.0090  -0.0183 672 ARG B O   
6370  C CB  . ARG B 371 ? 0.5714 0.7616 0.6310 -0.0189 0.0134  -0.0190 672 ARG B CB  
6371  C CG  . ARG B 371 ? 0.8720 1.0891 0.9419 -0.0223 0.0184  -0.0185 672 ARG B CG  
6372  C CD  . ARG B 371 ? 1.0438 1.2638 1.1143 -0.0380 0.0207  -0.0185 672 ARG B CD  
6373  N NE  . ARG B 371 ? 1.1179 1.3113 1.1748 -0.0434 0.0220  -0.0182 672 ARG B NE  
6374  C CZ  . ARG B 371 ? 1.0889 1.2692 1.1407 -0.0538 0.0197  -0.0186 672 ARG B CZ  
6375  N NH1 . ARG B 371 ? 1.0756 1.2666 1.1345 -0.0608 0.0161  -0.0195 672 ARG B NH1 
6376  N NH2 . ARG B 371 ? 0.9986 1.1551 1.0375 -0.0569 0.0210  -0.0181 672 ARG B NH2 
6377  N N   . CYS B 372 ? 0.3495 0.5329 0.4107 -0.0010 0.0021  -0.0189 673 CYS B N   
6378  C CA  . CYS B 372 ? 0.4846 0.6800 0.5525 0.0044  -0.0024 -0.0183 673 CYS B CA  
6379  C C   . CYS B 372 ? 0.4635 0.6445 0.5252 0.0164  -0.0048 -0.0178 673 CYS B C   
6380  O O   . CYS B 372 ? 0.5007 0.6926 0.5670 0.0245  -0.0071 -0.0167 673 CYS B O   
6381  C CB  . CYS B 372 ? 0.5047 0.7005 0.5744 -0.0056 -0.0070 -0.0188 673 CYS B CB  
6382  S SG  . CYS B 372 ? 0.5710 0.7367 0.6289 -0.0086 -0.0108 -0.0193 673 CYS B SG  
6383  N N   . ARG B 373 ? 0.3450 0.5022 0.3963 0.0177  -0.0042 -0.0183 674 ARG B N   
6384  C CA  . ARG B 373 ? 0.2734 0.4143 0.3179 0.0266  -0.0066 -0.0180 674 ARG B CA  
6385  C C   . ARG B 373 ? 0.3753 0.5050 0.4126 0.0348  -0.0030 -0.0187 674 ARG B C   
6386  O O   . ARG B 373 ? 0.3994 0.5172 0.4312 0.0433  -0.0044 -0.0185 674 ARG B O   
6387  C CB  . ARG B 373 ? 0.2732 0.3946 0.3112 0.0205  -0.0102 -0.0184 674 ARG B CB  
6388  C CG  . ARG B 373 ? 0.2876 0.3969 0.3212 0.0267  -0.0137 -0.0175 674 ARG B CG  
6389  C CD  . ARG B 373 ? 0.2686 0.3594 0.2959 0.0204  -0.0162 -0.0181 674 ARG B CD  
6390  N NE  . ARG B 373 ? 0.3453 0.4255 0.3687 0.0252  -0.0192 -0.0171 674 ARG B NE  
6391  C CZ  . ARG B 373 ? 0.3486 0.4115 0.3658 0.0226  -0.0208 -0.0175 674 ARG B CZ  
6392  N NH1 . ARG B 373 ? 0.2922 0.3467 0.3065 0.0161  -0.0202 -0.0190 674 ARG B NH1 
6393  N NH2 . ARG B 373 ? 0.3377 0.3923 0.3516 0.0267  -0.0230 -0.0161 674 ARG B NH2 
6394  N N   . GLY B 374 ? 0.3842 0.5166 0.4205 0.0324  0.0016  -0.0196 675 GLY B N   
6395  C CA  . GLY B 374 ? 0.3740 0.4954 0.4023 0.0399  0.0050  -0.0207 675 GLY B CA  
6396  C C   . GLY B 374 ? 0.3699 0.4671 0.3871 0.0365  0.0041  -0.0222 675 GLY B C   
6397  O O   . GLY B 374 ? 0.3111 0.3966 0.3201 0.0424  0.0061  -0.0236 675 GLY B O   
6398  N N   . GLY B 375 ? 0.3482 0.4380 0.3646 0.0276  0.0010  -0.0221 676 GLY B N   
6399  C CA  . GLY B 375 ? 0.3170 0.3868 0.3239 0.0242  0.0000  -0.0233 676 GLY B CA  
6400  C C   . GLY B 375 ? 0.3798 0.4425 0.3871 0.0171  -0.0044 -0.0229 676 GLY B C   
6401  O O   . GLY B 375 ? 0.4028 0.4750 0.4168 0.0145  -0.0066 -0.0218 676 GLY B O   
6402  N N   . CYS B 376 ? 0.3645 0.4110 0.3641 0.0145  -0.0057 -0.0240 677 CYS B N   
6403  C CA  . CYS B 376 ? 0.3649 0.4037 0.3638 0.0085  -0.0093 -0.0239 677 CYS B CA  
6404  C C   . CYS B 376 ? 0.3902 0.4117 0.3807 0.0094  -0.0110 -0.0254 677 CYS B C   
6405  O O   . CYS B 376 ? 0.4643 0.4802 0.4492 0.0076  -0.0096 -0.0262 677 CYS B O   
6406  C CB  . CYS B 376 ? 0.3017 0.3457 0.3024 0.0002  -0.0083 -0.0233 677 CYS B CB  
6407  S SG  . CYS B 376 ? 0.3714 0.4038 0.3692 -0.0061 -0.0122 -0.0234 677 CYS B SG  
6408  N N   . PRO B 377 ? 0.3305 0.3438 0.3196 0.0121  -0.0138 -0.0257 678 PRO B N   
6409  C CA  . PRO B 377 ? 0.2516 0.2501 0.2335 0.0120  -0.0157 -0.0275 678 PRO B CA  
6410  C C   . PRO B 377 ? 0.3078 0.3028 0.2886 0.0058  -0.0174 -0.0275 678 PRO B C   
6411  O O   . PRO B 377 ? 0.2872 0.2863 0.2723 0.0019  -0.0188 -0.0264 678 PRO B O   
6412  C CB  . PRO B 377 ? 0.3337 0.3264 0.3161 0.0145  -0.0182 -0.0273 678 PRO B CB  
6413  C CG  . PRO B 377 ? 0.3981 0.4018 0.3879 0.0135  -0.0188 -0.0251 678 PRO B CG  
6414  C CD  . PRO B 377 ? 0.3230 0.3403 0.3169 0.0144  -0.0158 -0.0244 678 PRO B CD  
6415  N N   . ALA B 378 ? 0.3474 0.3347 0.3215 0.0053  -0.0174 -0.0289 679 ALA B N   
6416  C CA  . ALA B 378 ? 0.3602 0.3442 0.3321 0.0007  -0.0187 -0.0287 679 ALA B CA  
6417  C C   . ALA B 378 ? 0.3366 0.3105 0.3015 0.0017  -0.0208 -0.0306 679 ALA B C   
6418  O O   . ALA B 378 ? 0.2703 0.2404 0.2297 0.0048  -0.0197 -0.0321 679 ALA B O   
6419  C CB  . ALA B 378 ? 0.3571 0.3460 0.3279 -0.0020 -0.0154 -0.0275 679 ALA B CB  
6420  N N   . ASP B 379 ? 0.3168 0.2871 0.2819 -0.0008 -0.0240 -0.0308 680 ASP B N   
6421  C CA  . ASP B 379 ? 0.3294 0.2924 0.2893 -0.0003 -0.0269 -0.0328 680 ASP B CA  
6422  C C   . ASP B 379 ? 0.3249 0.2860 0.2796 -0.0014 -0.0270 -0.0322 680 ASP B C   
6423  O O   . ASP B 379 ? 0.3171 0.2783 0.2732 -0.0034 -0.0284 -0.0311 680 ASP B O   
6424  C CB  . ASP B 379 ? 0.3075 0.2696 0.2717 -0.0020 -0.0303 -0.0332 680 ASP B CB  
6425  C CG  . ASP B 379 ? 0.3905 0.3474 0.3508 -0.0022 -0.0336 -0.0356 680 ASP B CG  
6426  O OD1 . ASP B 379 ? 0.3554 0.3112 0.3187 -0.0036 -0.0358 -0.0366 680 ASP B OD1 
6427  O OD2 . ASP B 379 ? 0.4329 0.3872 0.3868 -0.0011 -0.0341 -0.0365 680 ASP B OD2 
6428  N N   . TRP B 380 ? 0.2989 0.2572 0.2465 0.0005  -0.0251 -0.0327 681 TRP B N   
6429  C CA  . TRP B 380 ? 0.2731 0.2281 0.2137 0.0000  -0.0246 -0.0316 681 TRP B CA  
6430  C C   . TRP B 380 ? 0.2732 0.2248 0.2121 -0.0001 -0.0290 -0.0321 681 TRP B C   
6431  O O   . TRP B 380 ? 0.2834 0.2333 0.2201 -0.0010 -0.0289 -0.0303 681 TRP B O   
6432  C CB  . TRP B 380 ? 0.2885 0.2400 0.2204 0.0027  -0.0227 -0.0326 681 TRP B CB  
6433  C CG  . TRP B 380 ? 0.3009 0.2487 0.2241 0.0024  -0.0207 -0.0308 681 TRP B CG  
6434  C CD1 . TRP B 380 ? 0.2949 0.2447 0.2157 0.0012  -0.0156 -0.0288 681 TRP B CD1 
6435  C CD2 . TRP B 380 ? 0.3279 0.2695 0.2430 0.0036  -0.0237 -0.0307 681 TRP B CD2 
6436  N NE1 . TRP B 380 ? 0.3032 0.2467 0.2140 0.0012  -0.0147 -0.0272 681 TRP B NE1 
6437  C CE2 . TRP B 380 ? 0.3702 0.3083 0.2770 0.0032  -0.0198 -0.0282 681 TRP B CE2 
6438  C CE3 . TRP B 380 ? 0.2969 0.2363 0.2111 0.0050  -0.0291 -0.0322 681 TRP B CE3 
6439  C CZ2 . TRP B 380 ? 0.3146 0.2454 0.2110 0.0049  -0.0214 -0.0270 681 TRP B CZ2 
6440  C CZ3 . TRP B 380 ? 0.3198 0.2540 0.2247 0.0070  -0.0310 -0.0313 681 TRP B CZ3 
6441  C CH2 . TRP B 380 ? 0.3145 0.2436 0.2100 0.0073  -0.0272 -0.0285 681 TRP B CH2 
6442  N N   . VAL B 381 ? 0.2733 0.2239 0.2130 0.0008  -0.0327 -0.0345 682 VAL B N   
6443  C CA  . VAL B 381 ? 0.2734 0.2236 0.2128 0.0009  -0.0370 -0.0353 682 VAL B CA  
6444  C C   . VAL B 381 ? 0.3444 0.2978 0.2900 -0.0006 -0.0374 -0.0335 682 VAL B C   
6445  O O   . VAL B 381 ? 0.2847 0.2376 0.2284 0.0005  -0.0395 -0.0329 682 VAL B O   
6446  C CB  . VAL B 381 ? 0.2974 0.2476 0.2384 0.0006  -0.0405 -0.0385 682 VAL B CB  
6447  C CG1 . VAL B 381 ? 0.3118 0.2654 0.2557 -0.0001 -0.0451 -0.0393 682 VAL B CG1 
6448  C CG2 . VAL B 381 ? 0.3308 0.2760 0.2629 0.0025  -0.0408 -0.0408 682 VAL B CG2 
6449  N N   . TRP B 382 ? 0.3055 0.2622 0.2580 -0.0027 -0.0354 -0.0326 683 TRP B N   
6450  C CA  . TRP B 382 ? 0.2866 0.2458 0.2439 -0.0042 -0.0355 -0.0311 683 TRP B CA  
6451  C C   . TRP B 382 ? 0.3270 0.2849 0.2820 -0.0056 -0.0322 -0.0290 683 TRP B C   
6452  O O   . TRP B 382 ? 0.3131 0.2694 0.2676 -0.0061 -0.0324 -0.0280 683 TRP B O   
6453  C CB  . TRP B 382 ? 0.2564 0.2201 0.2219 -0.0059 -0.0356 -0.0314 683 TRP B CB  
6454  C CG  . TRP B 382 ? 0.2610 0.2263 0.2298 -0.0062 -0.0389 -0.0329 683 TRP B CG  
6455  C CD1 . TRP B 382 ? 0.2891 0.2530 0.2561 -0.0059 -0.0412 -0.0351 683 TRP B CD1 
6456  C CD2 . TRP B 382 ? 0.2400 0.2092 0.2146 -0.0074 -0.0400 -0.0325 683 TRP B CD2 
6457  N NE1 . TRP B 382 ? 0.3213 0.2887 0.2932 -0.0075 -0.0437 -0.0360 683 TRP B NE1 
6458  C CE2 . TRP B 382 ? 0.4155 0.3865 0.3922 -0.0082 -0.0428 -0.0343 683 TRP B CE2 
6459  C CE3 . TRP B 382 ? 0.3089 0.2804 0.2866 -0.0082 -0.0388 -0.0310 683 TRP B CE3 
6460  C CZ2 . TRP B 382 ? 0.3431 0.3193 0.3257 -0.0097 -0.0440 -0.0343 683 TRP B CZ2 
6461  C CZ3 . TRP B 382 ? 0.3626 0.3381 0.3451 -0.0089 -0.0401 -0.0311 683 TRP B CZ3 
6462  C CH2 . TRP B 382 ? 0.3103 0.2887 0.2956 -0.0097 -0.0424 -0.0326 683 TRP B CH2 
6463  N N   . ILE B 383 ? 0.3128 0.2712 0.2662 -0.0063 -0.0289 -0.0284 684 ILE B N   
6464  C CA  . ILE B 383 ? 0.2805 0.2390 0.2329 -0.0092 -0.0256 -0.0265 684 ILE B CA  
6465  C C   . ILE B 383 ? 0.3431 0.2937 0.2862 -0.0089 -0.0250 -0.0252 684 ILE B C   
6466  O O   . ILE B 383 ? 0.3269 0.2740 0.2678 -0.0114 -0.0236 -0.0239 684 ILE B O   
6467  C CB  . ILE B 383 ? 0.3335 0.2971 0.2877 -0.0100 -0.0221 -0.0262 684 ILE B CB  
6468  C CG1 . ILE B 383 ? 0.3254 0.2961 0.2881 -0.0096 -0.0226 -0.0269 684 ILE B CG1 
6469  C CG2 . ILE B 383 ? 0.2621 0.2264 0.2146 -0.0141 -0.0185 -0.0244 684 ILE B CG2 
6470  C CD1 . ILE B 383 ? 0.2893 0.2640 0.2580 -0.0124 -0.0233 -0.0262 684 ILE B CD1 
6471  N N   . VAL B 384 ? 0.2741 0.2205 0.2103 -0.0057 -0.0261 -0.0257 685 VAL B N   
6472  C CA  . VAL B 384 ? 0.2934 0.2312 0.2191 -0.0046 -0.0255 -0.0240 685 VAL B CA  
6473  C C   . VAL B 384 ? 0.2851 0.2196 0.2101 -0.0026 -0.0287 -0.0238 685 VAL B C   
6474  O O   . VAL B 384 ? 0.3293 0.2680 0.2589 -0.0002 -0.0326 -0.0255 685 VAL B O   
6475  C CB  . VAL B 384 ? 0.3403 0.2751 0.2581 -0.0012 -0.0262 -0.0246 685 VAL B CB  
6476  C CG1 . VAL B 384 ? 0.3048 0.2300 0.2104 0.0010  -0.0261 -0.0224 685 VAL B CG1 
6477  C CG2 . VAL B 384 ? 0.3011 0.2390 0.2187 -0.0026 -0.0222 -0.0247 685 VAL B CG2 
6478  N N   . PRO B 385 ? 0.3276 0.2546 0.2468 -0.0036 -0.0270 -0.0219 686 PRO B N   
6479  C CA  . PRO B 385 ? 0.3255 0.2491 0.2438 -0.0008 -0.0295 -0.0218 686 PRO B CA  
6480  C C   . PRO B 385 ? 0.4003 0.3224 0.3135 0.0054  -0.0333 -0.0220 686 PRO B C   
6481  O O   . PRO B 385 ? 0.3928 0.3116 0.2984 0.0073  -0.0333 -0.0214 686 PRO B O   
6482  C CB  . PRO B 385 ? 0.3869 0.2996 0.2967 -0.0033 -0.0261 -0.0196 686 PRO B CB  
6483  C CG  . PRO B 385 ? 0.4695 0.3855 0.3824 -0.0096 -0.0221 -0.0192 686 PRO B CG  
6484  C CD  . PRO B 385 ? 0.3927 0.3151 0.3075 -0.0083 -0.0222 -0.0200 686 PRO B CD  
6485  N N   . PRO B 386 ? 0.4057 0.3308 0.3223 0.0088  -0.0366 -0.0228 687 PRO B N   
6486  C CA  . PRO B 386 ? 0.3615 0.2885 0.2751 0.0149  -0.0409 -0.0233 687 PRO B CA  
6487  C C   . PRO B 386 ? 0.3692 0.2848 0.2691 0.0199  -0.0407 -0.0208 687 PRO B C   
6488  O O   . PRO B 386 ? 0.3610 0.2789 0.2579 0.0259  -0.0447 -0.0210 687 PRO B O   
6489  C CB  . PRO B 386 ? 0.3865 0.3217 0.3094 0.0165  -0.0434 -0.0247 687 PRO B CB  
6490  C CG  . PRO B 386 ? 0.2921 0.2219 0.2152 0.0137  -0.0399 -0.0237 687 PRO B CG  
6491  C CD  . PRO B 386 ? 0.3417 0.2695 0.2652 0.0075  -0.0364 -0.0233 687 PRO B CD  
6492  N N   . MET B 387 ? 0.3577 0.2613 0.2489 0.0177  -0.0365 -0.0184 688 MET B N   
6493  C CA  . MET B 387 ? 0.3656 0.2560 0.2415 0.0220  -0.0358 -0.0155 688 MET B CA  
6494  C C   . MET B 387 ? 0.4550 0.3369 0.3238 0.0162  -0.0305 -0.0136 688 MET B C   
6495  O O   . MET B 387 ? 0.4415 0.3272 0.3175 0.0094  -0.0274 -0.0144 688 MET B O   
6496  C CB  . MET B 387 ? 0.3766 0.2569 0.2459 0.0263  -0.0356 -0.0140 688 MET B CB  
6497  C CG  . MET B 387 ? 0.4471 0.3194 0.3160 0.0199  -0.0310 -0.0135 688 MET B CG  
6498  S SD  . MET B 387 ? 0.5387 0.3963 0.3981 0.0249  -0.0303 -0.0122 688 MET B SD  
6499  C CE  . MET B 387 ? 0.5911 0.4283 0.4292 0.0290  -0.0284 -0.0080 688 MET B CE  
6500  N N   . SER B 388 ? 0.4405 0.3119 0.2952 0.0192  -0.0295 -0.0110 689 SER B N   
6501  C CA  . SER B 388 ? 0.4524 0.3141 0.2982 0.0137  -0.0237 -0.0085 689 SER B CA  
6502  C C   . SER B 388 ? 0.4103 0.2830 0.2656 0.0074  -0.0213 -0.0102 689 SER B C   
6503  O O   . SER B 388 ? 0.4450 0.3156 0.3002 0.0005  -0.0162 -0.0091 689 SER B O   
6504  C CB  . SER B 388 ? 0.4668 0.3163 0.3078 0.0094  -0.0199 -0.0067 689 SER B CB  
6505  O OG  . SER B 388 ? 0.5762 0.4130 0.4061 0.0163  -0.0216 -0.0049 689 SER B OG  
6506  N N   . GLY B 389 ? 0.4199 0.3047 0.2833 0.0096  -0.0248 -0.0130 690 GLY B N   
6507  C CA  . GLY B 389 ? 0.3703 0.2654 0.2430 0.0052  -0.0229 -0.0149 690 GLY B CA  
6508  C C   . GLY B 389 ? 0.3903 0.2821 0.2570 0.0008  -0.0170 -0.0130 690 GLY B C   
6509  O O   . GLY B 389 ? 0.4256 0.3224 0.2994 -0.0052 -0.0133 -0.0131 690 GLY B O   
6510  N N   . SER B 390 ? 0.3624 0.2466 0.2159 0.0037  -0.0159 -0.0111 691 SER B N   
6511  C CA  . SER B 390 ? 0.4091 0.2923 0.2575 -0.0003 -0.0099 -0.0095 691 SER B CA  
6512  C C   . SER B 390 ? 0.3788 0.2533 0.2218 -0.0066 -0.0043 -0.0062 691 SER B C   
6513  O O   . SER B 390 ? 0.5140 0.3901 0.3551 -0.0114 0.0014  -0.0048 691 SER B O   
6514  C CB  . SER B 390 ? 0.4313 0.3089 0.2661 0.0047  -0.0102 -0.0085 691 SER B CB  
6515  O OG  . SER B 390 ? 0.4359 0.2991 0.2564 0.0072  -0.0101 -0.0050 691 SER B OG  
6516  N N   . ILE B 391 ? 0.4163 0.2814 0.2562 -0.0069 -0.0053 -0.0049 692 ILE B N   
6517  C CA  . ILE B 391 ? 0.4244 0.2809 0.2597 -0.0145 0.0001  -0.0024 692 ILE B CA  
6518  C C   . ILE B 391 ? 0.3786 0.2462 0.2290 -0.0211 0.0008  -0.0047 692 ILE B C   
6519  O O   . ILE B 391 ? 0.4486 0.3119 0.2976 -0.0288 0.0050  -0.0035 692 ILE B O   
6520  C CB  . ILE B 391 ? 0.5151 0.3522 0.3358 -0.0119 -0.0003 0.0004  692 ILE B CB  
6521  C CG1 . ILE B 391 ? 0.6572 0.4943 0.4838 -0.0081 -0.0053 -0.0016 692 ILE B CG1 
6522  C CG2 . ILE B 391 ? 0.4662 0.2931 0.2710 -0.0042 -0.0014 0.0030  692 ILE B CG2 
6523  C CD1 . ILE B 391 ? 0.6297 0.4470 0.4414 -0.0049 -0.0051 0.0011  692 ILE B CD1 
6524  N N   . THR B 392 ? 0.3919 0.2732 0.2558 -0.0186 -0.0030 -0.0079 693 THR B N   
6525  C CA  . THR B 392 ? 0.4494 0.3430 0.3273 -0.0244 -0.0021 -0.0099 693 THR B CA  
6526  C C   . THR B 392 ? 0.4451 0.3520 0.3299 -0.0259 0.0007  -0.0106 693 THR B C   
6527  O O   . THR B 392 ? 0.3976 0.3060 0.2791 -0.0209 0.0000  -0.0110 693 THR B O   
6528  C CB  . THR B 392 ? 0.3926 0.2932 0.2812 -0.0210 -0.0075 -0.0127 693 THR B CB  
6529  O OG1 . THR B 392 ? 0.4216 0.3307 0.3155 -0.0156 -0.0106 -0.0146 693 THR B OG1 
6530  C CG2 . THR B 392 ? 0.3984 0.2873 0.2802 -0.0171 -0.0105 -0.0122 693 THR B CG2 
6531  N N   . PRO B 393 ? 0.4212 0.3382 0.3149 -0.0325 0.0039  -0.0110 694 PRO B N   
6532  C CA  . PRO B 393 ? 0.4295 0.3594 0.3287 -0.0333 0.0074  -0.0113 694 PRO B CA  
6533  C C   . PRO B 393 ? 0.4124 0.3525 0.3205 -0.0271 0.0039  -0.0141 694 PRO B C   
6534  O O   . PRO B 393 ? 0.3876 0.3337 0.2957 -0.0245 0.0061  -0.0145 694 PRO B O   
6535  C CB  . PRO B 393 ? 0.4012 0.3404 0.3085 -0.0419 0.0109  -0.0111 694 PRO B CB  
6536  C CG  . PRO B 393 ? 0.4032 0.3379 0.3135 -0.0440 0.0071  -0.0121 694 PRO B CG  
6537  C CD  . PRO B 393 ? 0.4333 0.3501 0.3308 -0.0398 0.0049  -0.0110 694 PRO B CD  
6538  N N   . VAL B 394 ? 0.3569 0.2984 0.2717 -0.0245 -0.0013 -0.0160 695 VAL B N   
6539  C CA  . VAL B 394 ? 0.2990 0.2487 0.2214 -0.0195 -0.0043 -0.0185 695 VAL B CA  
6540  C C   . VAL B 394 ? 0.3469 0.2911 0.2613 -0.0136 -0.0057 -0.0193 695 VAL B C   
6541  O O   . VAL B 394 ? 0.3009 0.2507 0.2185 -0.0102 -0.0062 -0.0212 695 VAL B O   
6542  C CB  . VAL B 394 ? 0.3168 0.2678 0.2466 -0.0185 -0.0091 -0.0200 695 VAL B CB  
6543  C CG1 . VAL B 394 ? 0.3129 0.2721 0.2517 -0.0237 -0.0079 -0.0199 695 VAL B CG1 
6544  C CG2 . VAL B 394 ? 0.3366 0.2761 0.2591 -0.0169 -0.0121 -0.0195 695 VAL B CG2 
6545  N N   . PHE B 395 ? 0.3294 0.2622 0.2326 -0.0121 -0.0067 -0.0179 696 PHE B N   
6546  C CA  . PHE B 395 ? 0.3585 0.2866 0.2533 -0.0066 -0.0088 -0.0188 696 PHE B CA  
6547  C C   . PHE B 395 ? 0.3864 0.3183 0.2780 -0.0059 -0.0044 -0.0190 696 PHE B C   
6548  O O   . PHE B 395 ? 0.3676 0.3006 0.2576 -0.0015 -0.0063 -0.0214 696 PHE B O   
6549  C CB  . PHE B 395 ? 0.3574 0.2731 0.2395 -0.0049 -0.0098 -0.0166 696 PHE B CB  
6550  C CG  . PHE B 395 ? 0.3489 0.2601 0.2211 0.0007  -0.0123 -0.0173 696 PHE B CG  
6551  C CD1 . PHE B 395 ? 0.3424 0.2531 0.2151 0.0052  -0.0187 -0.0193 696 PHE B CD1 
6552  C CD2 . PHE B 395 ? 0.3650 0.2730 0.2271 0.0013  -0.0083 -0.0161 696 PHE B CD2 
6553  C CE1 . PHE B 395 ? 0.3475 0.2550 0.2108 0.0100  -0.0216 -0.0204 696 PHE B CE1 
6554  C CE2 . PHE B 395 ? 0.3925 0.2962 0.2443 0.0065  -0.0109 -0.0170 696 PHE B CE2 
6555  C CZ  . PHE B 395 ? 0.3590 0.2625 0.2114 0.0108  -0.0179 -0.0193 696 PHE B CZ  
6556  N N   . HIS B 396 ? 0.3794 0.3136 0.2701 -0.0104 0.0015  -0.0167 697 HIS B N   
6557  C CA  . HIS B 396 ? 0.4113 0.3499 0.2985 -0.0100 0.0068  -0.0164 697 HIS B CA  
6558  C C   . HIS B 396 ? 0.3934 0.3462 0.2928 -0.0098 0.0087  -0.0183 697 HIS B C   
6559  O O   . HIS B 396 ? 0.3662 0.3248 0.2641 -0.0086 0.0134  -0.0183 697 HIS B O   
6560  C CB  . HIS B 396 ? 0.3860 0.3206 0.2659 -0.0156 0.0127  -0.0127 697 HIS B CB  
6561  C CG  . HIS B 396 ? 0.4390 0.3579 0.3055 -0.0150 0.0111  -0.0104 697 HIS B CG  
6562  N ND1 . HIS B 396 ? 0.4306 0.3408 0.2832 -0.0104 0.0111  -0.0095 697 HIS B ND1 
6563  C CD2 . HIS B 396 ? 0.4068 0.3167 0.2710 -0.0173 0.0089  -0.0089 697 HIS B CD2 
6564  C CE1 . HIS B 396 ? 0.4658 0.3626 0.3081 -0.0097 0.0090  -0.0072 697 HIS B CE1 
6565  N NE2 . HIS B 396 ? 0.4402 0.3361 0.2892 -0.0137 0.0079  -0.0068 697 HIS B NE2 
6566  N N   . GLN B 397 ? 0.3965 0.3548 0.3071 -0.0102 0.0051  -0.0198 698 GLN B N   
6567  C CA  . GLN B 397 ? 0.3241 0.2955 0.2464 -0.0096 0.0064  -0.0211 698 GLN B CA  
6568  C C   . GLN B 397 ? 0.3509 0.3214 0.2741 -0.0031 0.0029  -0.0242 698 GLN B C   
6569  O O   . GLN B 397 ? 0.3917 0.3571 0.3163 -0.0019 -0.0024 -0.0255 698 GLN B O   
6570  C CB  . GLN B 397 ? 0.3154 0.2924 0.2482 -0.0141 0.0045  -0.0206 698 GLN B CB  
6571  C CG  . GLN B 397 ? 0.3434 0.3341 0.2879 -0.0126 0.0050  -0.0217 698 GLN B CG  
6572  C CD  . GLN B 397 ? 0.3941 0.3967 0.3412 -0.0138 0.0112  -0.0207 698 GLN B CD  
6573  O OE1 . GLN B 397 ? 0.3689 0.3746 0.3158 -0.0204 0.0147  -0.0187 698 GLN B OE1 
6574  N NE2 . GLN B 397 ? 0.3330 0.3420 0.2819 -0.0076 0.0128  -0.0221 698 GLN B NE2 
6575  N N   . GLU B 398 ? 0.3142 0.2894 0.2365 0.0010  0.0061  -0.0254 699 GLU B N   
6576  C CA  . GLU B 398 ? 0.3042 0.2782 0.2279 0.0067  0.0032  -0.0285 699 GLU B CA  
6577  C C   . GLU B 398 ? 0.3207 0.3022 0.2567 0.0062  0.0013  -0.0286 699 GLU B C   
6578  O O   . GLU B 398 ? 0.3144 0.3067 0.2584 0.0033  0.0039  -0.0268 699 GLU B O   
6579  C CB  . GLU B 398 ? 0.3122 0.2890 0.2315 0.0119  0.0076  -0.0298 699 GLU B CB  
6580  C CG  . GLU B 398 ? 0.3247 0.2920 0.2299 0.0138  0.0086  -0.0306 699 GLU B CG  
6581  C CD  . GLU B 398 ? 0.4031 0.3734 0.3036 0.0193  0.0135  -0.0321 699 GLU B CD  
6582  O OE1 . GLU B 398 ? 0.4148 0.3769 0.3026 0.0219  0.0140  -0.0334 699 GLU B OE1 
6583  O OE2 . GLU B 398 ? 0.4344 0.4157 0.3434 0.0214  0.0168  -0.0320 699 GLU B OE2 
6584  N N   . MET B 399 ? 0.3703 0.3462 0.3074 0.0087  -0.0034 -0.0307 700 MET B N   
6585  C CA  . MET B 399 ? 0.3524 0.3331 0.2993 0.0086  -0.0057 -0.0306 700 MET B CA  
6586  C C   . MET B 399 ? 0.3742 0.3499 0.3195 0.0141  -0.0073 -0.0332 700 MET B C   
6587  O O   . MET B 399 ? 0.4229 0.3890 0.3598 0.0161  -0.0087 -0.0355 700 MET B O   
6588  C CB  . MET B 399 ? 0.3113 0.2883 0.2609 0.0044  -0.0101 -0.0300 700 MET B CB  
6589  C CG  . MET B 399 ? 0.3629 0.3416 0.3125 -0.0009 -0.0088 -0.0277 700 MET B CG  
6590  S SD  . MET B 399 ? 0.3674 0.3390 0.3170 -0.0038 -0.0139 -0.0275 700 MET B SD  
6591  C CE  . MET B 399 ? 0.3457 0.3153 0.2909 -0.0089 -0.0112 -0.0249 700 MET B CE  
6592  N N   . LEU B 400 ? 0.3466 0.3283 0.2992 0.0163  -0.0070 -0.0328 701 LEU B N   
6593  C CA  . LEU B 400 ? 0.3080 0.2827 0.2587 0.0211  -0.0087 -0.0348 701 LEU B CA  
6594  C C   . LEU B 400 ? 0.3645 0.3371 0.3206 0.0184  -0.0128 -0.0341 701 LEU B C   
6595  O O   . LEU B 400 ? 0.3544 0.3358 0.3185 0.0158  -0.0130 -0.0319 701 LEU B O   
6596  C CB  . LEU B 400 ? 0.3463 0.3281 0.2995 0.0276  -0.0049 -0.0345 701 LEU B CB  
6597  C CG  . LEU B 400 ? 0.3690 0.3533 0.3165 0.0316  -0.0001 -0.0354 701 LEU B CG  
6598  C CD1 . LEU B 400 ? 0.3689 0.3648 0.3219 0.0380  0.0037  -0.0345 701 LEU B CD1 
6599  C CD2 . LEU B 400 ? 0.3082 0.2774 0.2435 0.0345  -0.0011 -0.0389 701 LEU B CD2 
6600  N N   . ASN B 401 ? 0.3634 0.3247 0.3150 0.0184  -0.0161 -0.0362 702 ASN B N   
6601  C CA  . ASN B 401 ? 0.4219 0.3808 0.3780 0.0156  -0.0196 -0.0357 702 ASN B CA  
6602  C C   . ASN B 401 ? 0.3838 0.3364 0.3384 0.0198  -0.0195 -0.0363 702 ASN B C   
6603  O O   . ASN B 401 ? 0.3282 0.2712 0.2750 0.0231  -0.0190 -0.0389 702 ASN B O   
6604  C CB  . ASN B 401 ? 0.3636 0.3157 0.3168 0.0112  -0.0234 -0.0372 702 ASN B CB  
6605  C CG  . ASN B 401 ? 0.3922 0.3457 0.3516 0.0075  -0.0261 -0.0359 702 ASN B CG  
6606  O OD1 . ASN B 401 ? 0.4136 0.3736 0.3791 0.0076  -0.0251 -0.0336 702 ASN B OD1 
6607  N ND2 . ASN B 401 ? 0.3645 0.3128 0.3226 0.0044  -0.0295 -0.0375 702 ASN B ND2 
6608  N N   . TYR B 402 ? 0.3363 0.2936 0.2973 0.0201  -0.0198 -0.0340 703 TYR B N   
6609  C CA  . TYR B 402 ? 0.3470 0.2969 0.3059 0.0242  -0.0199 -0.0339 703 TYR B CA  
6610  C C   . TYR B 402 ? 0.3954 0.3495 0.3608 0.0217  -0.0216 -0.0312 703 TYR B C   
6611  O O   . TYR B 402 ? 0.3159 0.2801 0.2877 0.0179  -0.0223 -0.0296 703 TYR B O   
6612  C CB  . TYR B 402 ? 0.2980 0.2508 0.2552 0.0323  -0.0164 -0.0336 703 TYR B CB  
6613  C CG  . TYR B 402 ? 0.3066 0.2768 0.2714 0.0336  -0.0139 -0.0315 703 TYR B CG  
6614  C CD1 . TYR B 402 ? 0.3237 0.3046 0.2961 0.0349  -0.0141 -0.0286 703 TYR B CD1 
6615  C CD2 . TYR B 402 ? 0.4092 0.3854 0.3731 0.0330  -0.0114 -0.0323 703 TYR B CD2 
6616  C CE1 . TYR B 402 ? 0.3048 0.3030 0.2845 0.0350  -0.0121 -0.0271 703 TYR B CE1 
6617  C CE2 . TYR B 402 ? 0.3889 0.3812 0.3598 0.0328  -0.0088 -0.0305 703 TYR B CE2 
6618  C CZ  . TYR B 402 ? 0.3253 0.3291 0.3045 0.0336  -0.0093 -0.0280 703 TYR B CZ  
6619  O OH  . TYR B 402 ? 0.3786 0.3996 0.3651 0.0323  -0.0069 -0.0266 703 TYR B OH  
6620  N N   . ARG B 403 ? 0.4172 0.3623 0.3800 0.0235  -0.0224 -0.0306 704 ARG B N   
6621  C CA  . ARG B 403 ? 0.3986 0.3451 0.3656 0.0207  -0.0241 -0.0282 704 ARG B CA  
6622  C C   . ARG B 403 ? 0.4204 0.3723 0.3895 0.0270  -0.0228 -0.0253 704 ARG B C   
6623  O O   . ARG B 403 ? 0.3769 0.3202 0.3404 0.0331  -0.0216 -0.0252 704 ARG B O   
6624  C CB  . ARG B 403 ? 0.5255 0.4579 0.4876 0.0172  -0.0258 -0.0292 704 ARG B CB  
6625  C CG  . ARG B 403 ? 0.7135 0.6468 0.6791 0.0145  -0.0269 -0.0264 704 ARG B CG  
6626  C CD  . ARG B 403 ? 0.9305 0.8540 0.8937 0.0082  -0.0285 -0.0275 704 ARG B CD  
6627  N NE  . ARG B 403 ? 1.0737 1.0004 1.0387 0.0030  -0.0302 -0.0302 704 ARG B NE  
6628  C CZ  . ARG B 403 ? 1.1273 1.0644 1.0986 -0.0006 -0.0314 -0.0296 704 ARG B CZ  
6629  N NH1 . ARG B 403 ? 1.1574 1.1027 1.1339 -0.0003 -0.0310 -0.0268 704 ARG B NH1 
6630  N NH2 . ARG B 403 ? 1.1344 1.0734 1.1062 -0.0040 -0.0330 -0.0320 704 ARG B NH2 
6631  N N   . LEU B 404 ? 0.3394 0.3055 0.3161 0.0258  -0.0231 -0.0233 705 LEU B N   
6632  C CA  . LEU B 404 ? 0.3325 0.3064 0.3123 0.0309  -0.0229 -0.0204 705 LEU B CA  
6633  C C   . LEU B 404 ? 0.2985 0.2700 0.2792 0.0276  -0.0250 -0.0182 705 LEU B C   
6634  O O   . LEU B 404 ? 0.3016 0.2717 0.2838 0.0207  -0.0264 -0.0189 705 LEU B O   
6635  C CB  . LEU B 404 ? 0.3081 0.3006 0.2956 0.0309  -0.0221 -0.0198 705 LEU B CB  
6636  C CG  . LEU B 404 ? 0.3644 0.3626 0.3520 0.0338  -0.0193 -0.0214 705 LEU B CG  
6637  C CD1 . LEU B 404 ? 0.3822 0.3987 0.3781 0.0307  -0.0187 -0.0207 705 LEU B CD1 
6638  C CD2 . LEU B 404 ? 0.3412 0.3370 0.3251 0.0438  -0.0173 -0.0210 705 LEU B CD2 
6639  N N   . THR B 405 ? 0.3174 0.2887 0.2968 0.0331  -0.0251 -0.0156 706 THR B N   
6640  C CA  . THR B 405 ? 0.3467 0.3173 0.3266 0.0306  -0.0268 -0.0130 706 THR B CA  
6641  C C   . THR B 405 ? 0.3026 0.2895 0.2882 0.0337  -0.0278 -0.0108 706 THR B C   
6642  O O   . THR B 405 ? 0.3554 0.3512 0.3430 0.0400  -0.0269 -0.0105 706 THR B O   
6643  C CB  . THR B 405 ? 0.3378 0.2913 0.3091 0.0337  -0.0264 -0.0115 706 THR B CB  
6644  O OG1 . THR B 405 ? 0.5587 0.5106 0.5296 0.0304  -0.0276 -0.0089 706 THR B OG1 
6645  C CG2 . THR B 405 ? 0.3332 0.2852 0.3005 0.0441  -0.0252 -0.0098 706 THR B CG2 
6646  N N   . PRO B 406 ? 0.3346 0.3270 0.3229 0.0293  -0.0296 -0.0094 707 PRO B N   
6647  C CA  . PRO B 406 ? 0.3867 0.3724 0.3738 0.0224  -0.0305 -0.0095 707 PRO B CA  
6648  C C   . PRO B 406 ? 0.3345 0.3188 0.3236 0.0160  -0.0301 -0.0126 707 PRO B C   
6649  O O   . PRO B 406 ? 0.2688 0.2602 0.2611 0.0156  -0.0296 -0.0144 707 PRO B O   
6650  C CB  . PRO B 406 ? 0.3626 0.3600 0.3533 0.0206  -0.0323 -0.0079 707 PRO B CB  
6651  C CG  . PRO B 406 ? 0.3667 0.3737 0.3587 0.0279  -0.0328 -0.0061 707 PRO B CG  
6652  C CD  . PRO B 406 ? 0.3705 0.3793 0.3639 0.0316  -0.0311 -0.0078 707 PRO B CD  
6653  N N   . SER B 407 ? 0.3454 0.3213 0.3326 0.0110  -0.0304 -0.0131 708 SER B N   
6654  C CA  . SER B 407 ? 0.3574 0.3318 0.3459 0.0062  -0.0304 -0.0160 708 SER B CA  
6655  C C   . SER B 407 ? 0.2949 0.2674 0.2841 0.0007  -0.0312 -0.0160 708 SER B C   
6656  O O   . SER B 407 ? 0.3678 0.3366 0.3551 0.0003  -0.0311 -0.0139 708 SER B O   
6657  C CB  . SER B 407 ? 0.5360 0.4999 0.5200 0.0075  -0.0296 -0.0179 708 SER B CB  
6658  O OG  . SER B 407 ? 0.6828 0.6348 0.6622 0.0067  -0.0295 -0.0171 708 SER B OG  
6659  N N   . PHE B 408 ? 0.2514 0.2267 0.2430 -0.0032 -0.0316 -0.0181 709 PHE B N   
6660  C CA  . PHE B 408 ? 0.2529 0.2266 0.2453 -0.0076 -0.0321 -0.0187 709 PHE B CA  
6661  C C   . PHE B 408 ? 0.3151 0.2811 0.3056 -0.0093 -0.0323 -0.0205 709 PHE B C   
6662  O O   . PHE B 408 ? 0.3457 0.3100 0.3349 -0.0081 -0.0325 -0.0225 709 PHE B O   
6663  C CB  . PHE B 408 ? 0.2484 0.2289 0.2437 -0.0100 -0.0327 -0.0199 709 PHE B CB  
6664  C CG  . PHE B 408 ? 0.2740 0.2612 0.2706 -0.0099 -0.0327 -0.0186 709 PHE B CG  
6665  C CD1 . PHE B 408 ? 0.2301 0.2231 0.2277 -0.0092 -0.0328 -0.0191 709 PHE B CD1 
6666  C CD2 . PHE B 408 ? 0.2443 0.2320 0.2405 -0.0109 -0.0327 -0.0170 709 PHE B CD2 
6667  C CE1 . PHE B 408 ? 0.3357 0.3353 0.3343 -0.0100 -0.0333 -0.0184 709 PHE B CE1 
6668  C CE2 . PHE B 408 ? 0.3060 0.2996 0.3024 -0.0109 -0.0331 -0.0162 709 PHE B CE2 
6669  C CZ  . PHE B 408 ? 0.2361 0.2357 0.2337 -0.0106 -0.0336 -0.0171 709 PHE B CZ  
6670  N N   . GLU B 409 ? 0.3315 0.2933 0.3215 -0.0125 -0.0323 -0.0201 710 GLU B N   
6671  C CA  . GLU B 409 ? 0.3628 0.3174 0.3509 -0.0152 -0.0327 -0.0220 710 GLU B CA  
6672  C C   . GLU B 409 ? 0.4339 0.3930 0.4259 -0.0202 -0.0334 -0.0228 710 GLU B C   
6673  O O   . GLU B 409 ? 0.3018 0.2666 0.2965 -0.0213 -0.0327 -0.0212 710 GLU B O   
6674  C CB  . GLU B 409 ? 0.4340 0.3771 0.4167 -0.0148 -0.0316 -0.0206 710 GLU B CB  
6675  C CG  . GLU B 409 ? 0.4197 0.3585 0.3982 -0.0084 -0.0306 -0.0192 710 GLU B CG  
6676  C CD  . GLU B 409 ? 0.6173 0.5523 0.5929 -0.0057 -0.0309 -0.0221 710 GLU B CD  
6677  O OE1 . GLU B 409 ? 0.6607 0.5953 0.6368 -0.0091 -0.0320 -0.0250 710 GLU B OE1 
6678  O OE2 . GLU B 409 ? 0.7286 0.6619 0.7014 0.0002  -0.0299 -0.0213 710 GLU B OE2 
6679  N N   . TYR B 410 ? 0.3445 0.3018 0.3365 -0.0230 -0.0347 -0.0255 711 TYR B N   
6680  C CA  . TYR B 410 ? 0.3308 0.2930 0.3269 -0.0280 -0.0353 -0.0263 711 TYR B CA  
6681  C C   . TYR B 410 ? 0.3508 0.3071 0.3455 -0.0322 -0.0337 -0.0246 711 TYR B C   
6682  O O   . TYR B 410 ? 0.3547 0.2999 0.3438 -0.0315 -0.0327 -0.0237 711 TYR B O   
6683  C CB  . TYR B 410 ? 0.3442 0.3074 0.3408 -0.0300 -0.0378 -0.0298 711 TYR B CB  
6684  C CG  . TYR B 410 ? 0.5737 0.5423 0.5708 -0.0264 -0.0392 -0.0311 711 TYR B CG  
6685  C CD1 . TYR B 410 ? 0.7027 0.6664 0.6953 -0.0241 -0.0403 -0.0331 711 TYR B CD1 
6686  C CD2 . TYR B 410 ? 0.5469 0.5243 0.5479 -0.0250 -0.0393 -0.0304 711 TYR B CD2 
6687  C CE1 . TYR B 410 ? 0.6651 0.6328 0.6571 -0.0211 -0.0413 -0.0339 711 TYR B CE1 
6688  C CE2 . TYR B 410 ? 0.6355 0.6156 0.6354 -0.0218 -0.0404 -0.0313 711 TYR B CE2 
6689  C CZ  . TYR B 410 ? 0.5793 0.5546 0.5747 -0.0201 -0.0413 -0.0329 711 TYR B CZ  
6690  O OH  . TYR B 410 ? 0.5108 0.4879 0.5043 -0.0172 -0.0420 -0.0333 711 TYR B OH  
6691  N N   . GLN B 411 ? 0.3545 0.3180 0.3540 -0.0363 -0.0332 -0.0242 712 GLN B N   
6692  C CA  . GLN B 411 ? 0.3625 0.3215 0.3611 -0.0417 -0.0312 -0.0225 712 GLN B CA  
6693  C C   . GLN B 411 ? 0.3496 0.3192 0.3551 -0.0473 -0.0319 -0.0244 712 GLN B C   
6694  O O   . GLN B 411 ? 0.3453 0.3260 0.3558 -0.0452 -0.0335 -0.0259 712 GLN B O   
6695  C CB  . GLN B 411 ? 0.3754 0.3341 0.3725 -0.0399 -0.0286 -0.0185 712 GLN B CB  
6696  C CG  . GLN B 411 ? 0.3322 0.3032 0.3341 -0.0376 -0.0283 -0.0180 712 GLN B CG  
6697  C CD  . GLN B 411 ? 0.3860 0.3562 0.3851 -0.0360 -0.0260 -0.0143 712 GLN B CD  
6698  O OE1 . GLN B 411 ? 0.3992 0.3612 0.3939 -0.0380 -0.0241 -0.0117 712 GLN B OE1 
6699  N NE2 . GLN B 411 ? 0.3010 0.2787 0.3017 -0.0325 -0.0262 -0.0141 712 GLN B NE2 
6700  N N   . PRO B 412 ? 0.4021 0.3685 0.4076 -0.0544 -0.0308 -0.0242 713 PRO B N   
6701  C CA  . PRO B 412 ? 0.4184 0.3977 0.4318 -0.0600 -0.0316 -0.0262 713 PRO B CA  
6702  C C   . PRO B 412 ? 0.4391 0.4321 0.4586 -0.0581 -0.0297 -0.0243 713 PRO B C   
6703  O O   . PRO B 412 ? 0.3602 0.3505 0.3769 -0.0551 -0.0272 -0.0212 713 PRO B O   
6704  C CB  . PRO B 412 ? 0.5027 0.4740 0.5138 -0.0690 -0.0300 -0.0260 713 PRO B CB  
6705  C CG  . PRO B 412 ? 0.4749 0.4288 0.4764 -0.0671 -0.0275 -0.0228 713 PRO B CG  
6706  C CD  . PRO B 412 ? 0.4626 0.4133 0.4607 -0.0576 -0.0287 -0.0225 713 PRO B CD  
6707  N N   . ASP B 413 ? 0.4152 0.4231 0.4425 -0.0590 -0.0313 -0.0265 714 ASP B N   
6708  C CA  . ASP B 413 ? 0.4826 0.5038 0.5157 -0.0570 -0.0293 -0.0252 714 ASP B CA  
6709  C C   . ASP B 413 ? 0.4856 0.5072 0.5194 -0.0630 -0.0250 -0.0224 714 ASP B C   
6710  O O   . ASP B 413 ? 0.4174 0.4358 0.4516 -0.0710 -0.0244 -0.0227 714 ASP B O   
6711  C CB  . ASP B 413 ? 0.5308 0.5685 0.5722 -0.0566 -0.0317 -0.0281 714 ASP B CB  
6712  C CG  . ASP B 413 ? 0.6187 0.6562 0.6583 -0.0493 -0.0353 -0.0300 714 ASP B CG  
6713  O OD1 . ASP B 413 ? 0.5909 0.6218 0.6255 -0.0435 -0.0346 -0.0287 714 ASP B OD1 
6714  O OD2 . ASP B 413 ? 0.6845 0.7286 0.7273 -0.0498 -0.0387 -0.0329 714 ASP B OD2 
6715  N N   . PRO B 414 ? 0.3632 0.3880 0.3964 -0.0599 -0.0219 -0.0196 715 PRO B N   
6716  C CA  . PRO B 414 ? 0.3721 0.3951 0.4039 -0.0652 -0.0174 -0.0163 715 PRO B CA  
6717  C C   . PRO B 414 ? 0.3646 0.4006 0.4046 -0.0730 -0.0157 -0.0171 715 PRO B C   
6718  O O   . PRO B 414 ? 0.4207 0.4514 0.4588 -0.0807 -0.0126 -0.0150 715 PRO B O   
6719  C CB  . PRO B 414 ? 0.3801 0.4063 0.4097 -0.0591 -0.0150 -0.0141 715 PRO B CB  
6720  C CG  . PRO B 414 ? 0.3222 0.3500 0.3516 -0.0512 -0.0183 -0.0163 715 PRO B CG  
6721  C CD  . PRO B 414 ? 0.3687 0.3989 0.4020 -0.0518 -0.0223 -0.0197 715 PRO B CD  
6722  N N   . TRP B 415 ? 0.4126 0.4659 0.4617 -0.0713 -0.0175 -0.0198 716 TRP B N   
6723  C CA  . TRP B 415 ? 0.4334 0.5028 0.4920 -0.0785 -0.0159 -0.0206 716 TRP B CA  
6724  C C   . TRP B 415 ? 0.4981 0.5639 0.5581 -0.0880 -0.0180 -0.0228 716 TRP B C   
6725  O O   . TRP B 415 ? 0.5156 0.5929 0.5827 -0.0965 -0.0163 -0.0232 716 TRP B O   
6726  C CB  . TRP B 415 ? 0.4051 0.4946 0.4728 -0.0727 -0.0176 -0.0230 716 TRP B CB  
6727  C CG  . TRP B 415 ? 0.4107 0.4988 0.4777 -0.0663 -0.0231 -0.0261 716 TRP B CG  
6728  C CD1 . TRP B 415 ? 0.3910 0.4843 0.4621 -0.0690 -0.0276 -0.0295 716 TRP B CD1 
6729  C CD2 . TRP B 415 ? 0.3898 0.4708 0.4509 -0.0565 -0.0246 -0.0261 716 TRP B CD2 
6730  N NE1 . TRP B 415 ? 0.3893 0.4787 0.4569 -0.0609 -0.0316 -0.0312 716 TRP B NE1 
6731  C CE2 . TRP B 415 ? 0.3855 0.4672 0.4472 -0.0535 -0.0296 -0.0291 716 TRP B CE2 
6732  C CE3 . TRP B 415 ? 0.3620 0.4362 0.4170 -0.0504 -0.0222 -0.0239 716 TRP B CE3 
6733  C CZ2 . TRP B 415 ? 0.3734 0.4486 0.4297 -0.0450 -0.0318 -0.0296 716 TRP B CZ2 
6734  C CZ3 . TRP B 415 ? 0.4523 0.5204 0.5025 -0.0426 -0.0247 -0.0249 716 TRP B CZ3 
6735  C CH2 . TRP B 415 ? 0.4111 0.4794 0.4619 -0.0401 -0.0292 -0.0275 716 TRP B CH2 
6736  N N   . ASN B 416 ? 0.4748 0.5252 0.5279 -0.0871 -0.0215 -0.0243 717 ASN B N   
6737  C CA  . ASN B 416 ? 0.5490 0.5924 0.6009 -0.0963 -0.0233 -0.0265 717 ASN B CA  
6738  C C   . ASN B 416 ? 0.5114 0.5354 0.5540 -0.1028 -0.0197 -0.0235 717 ASN B C   
6739  O O   . ASN B 416 ? 0.6041 0.6232 0.6461 -0.1129 -0.0196 -0.0249 717 ASN B O   
6740  C CB  . ASN B 416 ? 0.4815 0.5172 0.5294 -0.0921 -0.0287 -0.0300 717 ASN B CB  
6741  C CG  . ASN B 416 ? 0.4688 0.5217 0.5242 -0.0859 -0.0326 -0.0328 717 ASN B CG  
6742  O OD1 . ASN B 416 ? 0.5121 0.5848 0.5775 -0.0877 -0.0326 -0.0336 717 ASN B OD1 
6743  N ND2 . ASN B 416 ? 0.4492 0.4948 0.4993 -0.0781 -0.0358 -0.0340 717 ASN B ND2 
6744  N N   . THR B 417 ? 0.5131 0.5255 0.5479 -0.0974 -0.0167 -0.0195 718 THR B N   
6745  C CA  . THR B 417 ? 0.5644 0.5571 0.5890 -0.1020 -0.0133 -0.0161 718 THR B CA  
6746  C C   . THR B 417 ? 0.5364 0.5320 0.5604 -0.1043 -0.0075 -0.0114 718 THR B C   
6747  O O   . THR B 417 ? 0.5647 0.5470 0.5818 -0.1113 -0.0040 -0.0086 718 THR B O   
6748  C CB  . THR B 417 ? 0.5374 0.5117 0.5512 -0.0935 -0.0147 -0.0150 718 THR B CB  
6749  O OG1 . THR B 417 ? 0.4813 0.4633 0.4966 -0.0837 -0.0150 -0.0137 718 THR B OG1 
6750  C CG2 . THR B 417 ? 0.4963 0.4646 0.5085 -0.0925 -0.0195 -0.0194 718 THR B CG2 
6751  N N   . HIS B 418 ? 0.4373 0.4486 0.4672 -0.0986 -0.0063 -0.0105 719 HIS B N   
6752  C CA  . HIS B 418 ? 0.4154 0.4285 0.4430 -0.0995 -0.0007 -0.0060 719 HIS B CA  
6753  C C   . HIS B 418 ? 0.4874 0.5093 0.5207 -0.1112 0.0034  -0.0052 719 HIS B C   
6754  O O   . HIS B 418 ? 0.5037 0.5436 0.5485 -0.1156 0.0020  -0.0086 719 HIS B O   
6755  C CB  . HIS B 418 ? 0.3913 0.4191 0.4234 -0.0906 -0.0004 -0.0060 719 HIS B CB  
6756  C CG  . HIS B 418 ? 0.4614 0.4919 0.4905 -0.0911 0.0053  -0.0017 719 HIS B CG  
6757  N ND1 . HIS B 418 ? 0.3856 0.4002 0.4029 -0.0884 0.0075  0.0025  719 HIS B ND1 
6758  C CD2 . HIS B 418 ? 0.4158 0.4636 0.4520 -0.0936 0.0094  -0.0011 719 HIS B CD2 
6759  C CE1 . HIS B 418 ? 0.4877 0.5088 0.5041 -0.0895 0.0126  0.0057  719 HIS B CE1 
6760  N NE2 . HIS B 418 ? 0.4482 0.4894 0.4761 -0.0926 0.0142  0.0035  719 HIS B NE2 
6761  N N   . VAL B 419 ? 0.5369 0.5470 0.5620 -0.1163 0.0085  -0.0006 720 VAL B N   
6762  C CA  . VAL B 419 ? 0.6321 0.6503 0.6618 -0.1282 0.0135  0.0010  720 VAL B CA  
6763  C C   . VAL B 419 ? 0.5018 0.5313 0.5325 -0.1250 0.0189  0.0047  720 VAL B C   
6764  O O   . VAL B 419 ? 0.4876 0.5040 0.5071 -0.1199 0.0213  0.0089  720 VAL B O   
6765  C CB  . VAL B 419 ? 0.7920 0.7872 0.8108 -0.1380 0.0160  0.0035  720 VAL B CB  
6766  C CG1 . VAL B 419 ? 0.6895 0.6798 0.7106 -0.1441 0.0111  -0.0015 720 VAL B CG1 
6767  C CG2 . VAL B 419 ? 0.8637 0.8344 0.8665 -0.1304 0.0165  0.0077  720 VAL B CG2 
6768  N N   . TRP B 420 ? 0.4922 0.5468 0.5360 -0.1272 0.0205  0.0028  721 TRP B N   
6769  C CA  . TRP B 420 ? 0.5772 0.6467 0.6238 -0.1227 0.0252  0.0050  721 TRP B CA  
6770  C C   . TRP B 420 ? 0.7523 0.8162 0.7925 -0.1307 0.0329  0.0105  721 TRP B C   
6771  O O   . TRP B 420 ? 0.7716 0.8279 0.8101 -0.1427 0.0353  0.0119  721 TRP B O   
6772  C CB  . TRP B 420 ? 0.4629 0.5614 0.5259 -0.1225 0.0246  0.0012  721 TRP B CB  
6773  C CG  . TRP B 420 ? 0.4203 0.5237 0.4874 -0.1122 0.0180  -0.0032 721 TRP B CG  
6774  C CD1 . TRP B 420 ? 0.4029 0.5044 0.4734 -0.1130 0.0117  -0.0073 721 TRP B CD1 
6775  C CD2 . TRP B 420 ? 0.3373 0.4468 0.4039 -0.0996 0.0171  -0.0039 721 TRP B CD2 
6776  N NE1 . TRP B 420 ? 0.3212 0.4275 0.3936 -0.1015 0.0072  -0.0100 721 TRP B NE1 
6777  C CE2 . TRP B 420 ? 0.3639 0.4746 0.4339 -0.0934 0.0104  -0.0082 721 TRP B CE2 
6778  C CE3 . TRP B 420 ? 0.3647 0.4780 0.4275 -0.0931 0.0214  -0.0016 721 TRP B CE3 
6779  C CZ2 . TRP B 420 ? 0.4827 0.5973 0.5522 -0.0815 0.0081  -0.0098 721 TRP B CZ2 
6780  C CZ3 . TRP B 420 ? 0.4586 0.5757 0.5209 -0.0813 0.0189  -0.0038 721 TRP B CZ3 
6781  C CH2 . TRP B 420 ? 0.4972 0.6145 0.5628 -0.0759 0.0124  -0.0077 721 TRP B CH2 
6782  N N   . LYS B 421 ? 0.8549 0.9226 0.8908 -0.1241 0.0369  0.0135  722 LYS B N   
6783  C CA  . LYS B 421 ? 0.8673 0.9279 0.8941 -0.1292 0.0443  0.0194  722 LYS B CA  
6784  C C   . LYS B 421 ? 1.0224 1.1061 1.0569 -0.1301 0.0507  0.0204  722 LYS B C   
6785  O O   . LYS B 421 ? 1.0875 1.1706 1.1187 -0.1390 0.0577  0.0246  722 LYS B O   
6786  C CB  . LYS B 421 ? 0.8532 0.8928 0.8636 -0.1202 0.0437  0.0231  722 LYS B CB  
6787  C CG  . LYS B 421 ? 0.8767 0.8989 0.8817 -0.1146 0.0365  0.0211  722 LYS B CG  
6788  C CD  . LYS B 421 ? 0.9196 0.9178 0.9073 -0.1102 0.0369  0.0259  722 LYS B CD  
6789  C CE  . LYS B 421 ? 0.9299 0.9114 0.9130 -0.1062 0.0305  0.0240  722 LYS B CE  
6790  N NZ  . LYS B 421 ? 0.9671 0.9235 0.9338 -0.1051 0.0315  0.0291  722 LYS B NZ  
6807  N N   . ARG C 3   ? 0.9150 0.8963 0.8249 -0.1438 -0.0336 -0.0276 304 ARG C N   
6808  C CA  . ARG C 3   ? 0.9470 0.9550 0.8757 -0.1440 -0.0334 -0.0233 304 ARG C CA  
6809  C C   . ARG C 3   ? 0.9148 0.9430 0.8594 -0.1304 -0.0319 -0.0215 304 ARG C C   
6810  O O   . ARG C 3   ? 0.9942 1.0372 0.9527 -0.1249 -0.0285 -0.0190 304 ARG C O   
6811  C CB  . ARG C 3   ? 1.0103 1.0362 0.9420 -0.1586 -0.0401 -0.0210 304 ARG C CB  
6812  C CG  . ARG C 3   ? 1.0901 1.1451 1.0410 -0.1598 -0.0393 -0.0168 304 ARG C CG  
6813  C CD  . ARG C 3   ? 1.1757 1.2395 1.1256 -0.1775 -0.0433 -0.0149 304 ARG C CD  
6814  N NE  . ARG C 3   ? 1.2508 1.3314 1.2138 -0.1790 -0.0395 -0.0115 304 ARG C NE  
6815  C CZ  . ARG C 3   ? 1.3322 1.3961 1.2906 -0.1778 -0.0337 -0.0114 304 ARG C CZ  
6816  N NH1 . ARG C 3   ? 1.3572 1.3878 1.2992 -0.1743 -0.0311 -0.0146 304 ARG C NH1 
6817  N NH2 . ARG C 3   ? 1.3430 1.4239 1.3130 -0.1797 -0.0304 -0.0081 304 ARG C NH2 
6818  N N   . PHE C 4   ? 0.6596 0.6872 0.6007 -0.1250 -0.0346 -0.0227 305 PHE C N   
6819  C CA  . PHE C 4   ? 0.6327 0.6759 0.5856 -0.1125 -0.0341 -0.0210 305 PHE C CA  
6820  C C   . PHE C 4   ? 0.6039 0.6275 0.5454 -0.1045 -0.0319 -0.0239 305 PHE C C   
6821  O O   . PHE C 4   ? 0.5922 0.5999 0.5185 -0.1099 -0.0342 -0.0266 305 PHE C O   
6822  C CB  . PHE C 4   ? 0.8248 0.8943 0.7871 -0.1148 -0.0414 -0.0183 305 PHE C CB  
6823  C CG  . PHE C 4   ? 1.0102 1.1056 0.9874 -0.1212 -0.0431 -0.0151 305 PHE C CG  
6824  C CD1 . PHE C 4   ? 1.1152 1.2105 1.0877 -0.1365 -0.0458 -0.0149 305 PHE C CD1 
6825  C CD2 . PHE C 4   ? 1.0063 1.1265 1.0013 -0.1121 -0.0422 -0.0122 305 PHE C CD2 
6826  C CE1 . PHE C 4   ? 1.1007 1.2218 1.0872 -0.1432 -0.0470 -0.0118 305 PHE C CE1 
6827  C CE2 . PHE C 4   ? 0.9746 1.1208 0.9837 -0.1176 -0.0431 -0.0095 305 PHE C CE2 
6828  C CZ  . PHE C 4   ? 1.0165 1.1640 1.0218 -0.1335 -0.0454 -0.0091 305 PHE C CZ  
6829  N N   . LEU C 5   ? 0.4823 0.5067 0.4304 -0.0923 -0.0273 -0.0234 306 LEU C N   
6830  C CA  . LEU C 5   ? 0.4657 0.4755 0.4047 -0.0849 -0.0252 -0.0255 306 LEU C CA  
6831  C C   . LEU C 5   ? 0.4502 0.4750 0.3986 -0.0754 -0.0269 -0.0229 306 LEU C C   
6832  O O   . LEU C 5   ? 0.4502 0.4903 0.4125 -0.0700 -0.0255 -0.0205 306 LEU C O   
6833  C CB  . LEU C 5   ? 0.4252 0.4170 0.3601 -0.0794 -0.0177 -0.0279 306 LEU C CB  
6834  C CG  . LEU C 5   ? 0.4730 0.4442 0.3953 -0.0861 -0.0156 -0.0311 306 LEU C CG  
6835  C CD1 . LEU C 5   ? 0.4899 0.4495 0.4129 -0.0790 -0.0085 -0.0324 306 LEU C CD1 
6836  C CD2 . LEU C 5   ? 0.4728 0.4283 0.3781 -0.0897 -0.0176 -0.0344 306 LEU C CD2 
6837  N N   . LYS C 6   ? 0.4760 0.4955 0.4156 -0.0733 -0.0298 -0.0233 307 LYS C N   
6838  C CA  . LYS C 6   ? 0.5063 0.5371 0.4523 -0.0643 -0.0320 -0.0206 307 LYS C CA  
6839  C C   . LYS C 6   ? 0.4217 0.4377 0.3621 -0.0559 -0.0265 -0.0218 307 LYS C C   
6840  O O   . LYS C 6   ? 0.4915 0.4892 0.4195 -0.0579 -0.0232 -0.0248 307 LYS C O   
6841  C CB  . LYS C 6   ? 0.5404 0.5778 0.4811 -0.0676 -0.0401 -0.0193 307 LYS C CB  
6842  C CG  . LYS C 6   ? 0.5760 0.6348 0.5261 -0.0747 -0.0464 -0.0172 307 LYS C CG  
6843  C CD  . LYS C 6   ? 0.7161 0.7855 0.6638 -0.0752 -0.0551 -0.0150 307 LYS C CD  
6844  C CE  . LYS C 6   ? 0.7184 0.8101 0.6750 -0.0840 -0.0617 -0.0132 307 LYS C CE  
6845  N NZ  . LYS C 6   ? 0.7286 0.8379 0.7026 -0.0826 -0.0583 -0.0117 307 LYS C NZ  
6846  N N   . VAL C 7   ? 0.3694 0.3935 0.3189 -0.0466 -0.0254 -0.0195 308 VAL C N   
6847  C CA  . VAL C 7   ? 0.3345 0.3464 0.2787 -0.0393 -0.0213 -0.0199 308 VAL C CA  
6848  C C   . VAL C 7   ? 0.3798 0.3988 0.3247 -0.0329 -0.0262 -0.0168 308 VAL C C   
6849  O O   . VAL C 7   ? 0.4425 0.4790 0.3983 -0.0298 -0.0303 -0.0142 308 VAL C O   
6850  C CB  . VAL C 7   ? 0.3959 0.4060 0.3478 -0.0339 -0.0145 -0.0204 308 VAL C CB  
6851  C CG1 . VAL C 7   ? 0.4744 0.4759 0.4245 -0.0394 -0.0100 -0.0232 308 VAL C CG1 
6852  C CG2 . VAL C 7   ? 0.3616 0.3894 0.3282 -0.0287 -0.0156 -0.0179 308 VAL C CG2 
6853  N N   . LYS C 8   ? 0.3879 0.3934 0.3209 -0.0306 -0.0257 -0.0169 309 LYS C N   
6854  C CA  . LYS C 8   ? 0.4065 0.4140 0.3359 -0.0252 -0.0309 -0.0139 309 LYS C CA  
6855  C C   . LYS C 8   ? 0.4093 0.4068 0.3363 -0.0177 -0.0266 -0.0132 309 LYS C C   
6856  O O   . LYS C 8   ? 0.3887 0.3730 0.3097 -0.0192 -0.0203 -0.0154 309 LYS C O   
6857  C CB  . LYS C 8   ? 0.3991 0.3978 0.3130 -0.0309 -0.0352 -0.0142 309 LYS C CB  
6858  C CG  . LYS C 8   ? 0.3681 0.3647 0.2745 -0.0258 -0.0407 -0.0108 309 LYS C CG  
6859  C CD  . LYS C 8   ? 0.3805 0.3719 0.2726 -0.0329 -0.0461 -0.0110 309 LYS C CD  
6860  C CE  . LYS C 8   ? 0.4930 0.4798 0.3750 -0.0282 -0.0517 -0.0074 309 LYS C CE  
6861  N NZ  . LYS C 8   ? 0.6131 0.5920 0.4786 -0.0355 -0.0561 -0.0079 309 LYS C NZ  
6862  N N   . ASN C 9   ? 0.3235 0.3274 0.2549 -0.0097 -0.0300 -0.0100 310 ASN C N   
6863  C CA  . ASN C 9   ? 0.3828 0.3744 0.3078 -0.0035 -0.0278 -0.0088 310 ASN C CA  
6864  C C   . ASN C 9   ? 0.4247 0.4067 0.3346 -0.0040 -0.0328 -0.0067 310 ASN C C   
6865  O O   . ASN C 9   ? 0.4186 0.4094 0.3289 -0.0019 -0.0403 -0.0041 310 ASN C O   
6866  C CB  . ASN C 9   ? 0.3631 0.3633 0.2985 0.0060  -0.0286 -0.0068 310 ASN C CB  
6867  C CG  . ASN C 9   ? 0.3983 0.3834 0.3260 0.0114  -0.0258 -0.0060 310 ASN C CG  
6868  O OD1 . ASN C 9   ? 0.4570 0.4304 0.3717 0.0125  -0.0288 -0.0039 310 ASN C OD1 
6869  N ND2 . ASN C 9   ? 0.3962 0.3803 0.3305 0.0140  -0.0202 -0.0074 310 ASN C ND2 
6870  N N   . TRP C 10  ? 0.3759 0.3410 0.2726 -0.0072 -0.0287 -0.0077 311 TRP C N   
6871  C CA  . TRP C 10  ? 0.4664 0.4209 0.3467 -0.0092 -0.0327 -0.0059 311 TRP C CA  
6872  C C   . TRP C 10  ? 0.4784 0.4262 0.3527 -0.0016 -0.0362 -0.0018 311 TRP C C   
6873  O O   . TRP C 10  ? 0.4937 0.4341 0.3547 -0.0020 -0.0414 0.0008  311 TRP C O   
6874  C CB  . TRP C 10  ? 0.3873 0.3275 0.2553 -0.0161 -0.0263 -0.0088 311 TRP C CB  
6875  C CG  . TRP C 10  ? 0.4571 0.4012 0.3268 -0.0231 -0.0247 -0.0126 311 TRP C CG  
6876  C CD1 . TRP C 10  ? 0.3669 0.3150 0.2467 -0.0249 -0.0192 -0.0159 311 TRP C CD1 
6877  C CD2 . TRP C 10  ? 0.4845 0.4275 0.3445 -0.0294 -0.0292 -0.0133 311 TRP C CD2 
6878  N NE1 . TRP C 10  ? 0.3954 0.3436 0.2715 -0.0319 -0.0199 -0.0187 311 TRP C NE1 
6879  C CE2 . TRP C 10  ? 0.4263 0.3714 0.2901 -0.0350 -0.0259 -0.0174 311 TRP C CE2 
6880  C CE3 . TRP C 10  ? 0.5494 0.4887 0.3963 -0.0310 -0.0359 -0.0109 311 TRP C CE3 
6881  C CZ2 . TRP C 10  ? 0.4766 0.4196 0.3315 -0.0423 -0.0290 -0.0195 311 TRP C CZ2 
6882  C CZ3 . TRP C 10  ? 0.6211 0.5597 0.4597 -0.0384 -0.0391 -0.0129 311 TRP C CZ3 
6883  C CH2 . TRP C 10  ? 0.6272 0.5673 0.4696 -0.0442 -0.0356 -0.0173 311 TRP C CH2 
6884  N N   . GLU C 11  ? 0.3865 0.3352 0.2690 0.0052  -0.0338 -0.0012 312 GLU C N   
6885  C CA  . GLU C 11  ? 0.4926 0.4337 0.3693 0.0134  -0.0376 0.0025  312 GLU C CA  
6886  C C   . GLU C 11  ? 0.5047 0.4608 0.3899 0.0212  -0.0457 0.0052  312 GLU C C   
6887  O O   . GLU C 11  ? 0.5052 0.4562 0.3811 0.0259  -0.0525 0.0088  312 GLU C O   
6888  C CB  . GLU C 11  ? 0.4992 0.4341 0.3801 0.0173  -0.0316 0.0016  312 GLU C CB  
6889  C CG  . GLU C 11  ? 0.6162 0.5372 0.4870 0.0244  -0.0342 0.0049  312 GLU C CG  
6890  C CD  . GLU C 11  ? 0.6760 0.5946 0.5536 0.0297  -0.0299 0.0038  312 GLU C CD  
6891  O OE1 . GLU C 11  ? 0.6081 0.5310 0.4942 0.0257  -0.0233 0.0005  312 GLU C OE1 
6892  O OE2 . GLU C 11  ? 0.7557 0.6673 0.6292 0.0383  -0.0334 0.0063  312 GLU C OE2 
6893  N N   . THR C 12  ? 0.4691 0.4443 0.3716 0.0224  -0.0453 0.0035  313 THR C N   
6894  C CA  . THR C 12  ? 0.4688 0.4623 0.3828 0.0303  -0.0518 0.0056  313 THR C CA  
6895  C C   . THR C 12  ? 0.4945 0.5048 0.4135 0.0248  -0.0575 0.0058  313 THR C C   
6896  O O   . THR C 12  ? 0.5352 0.5621 0.4625 0.0308  -0.0642 0.0082  313 THR C O   
6897  C CB  . THR C 12  ? 0.4703 0.4760 0.4007 0.0354  -0.0473 0.0039  313 THR C CB  
6898  O OG1 . THR C 12  ? 0.4321 0.4464 0.3712 0.0266  -0.0425 0.0006  313 THR C OG1 
6899  C CG2 . THR C 12  ? 0.4891 0.4782 0.4145 0.0403  -0.0418 0.0033  313 THR C CG2 
6900  N N   . GLU C 13  ? 0.4743 0.4813 0.3887 0.0136  -0.0551 0.0033  314 GLU C N   
6901  C CA  . GLU C 13  ? 0.5752 0.5960 0.4931 0.0059  -0.0597 0.0027  314 GLU C CA  
6902  C C   . GLU C 13  ? 0.4703 0.5124 0.4070 0.0047  -0.0584 0.0013  314 GLU C C   
6903  O O   . GLU C 13  ? 0.4718 0.5265 0.4123 -0.0026 -0.0622 0.0008  314 GLU C O   
6904  C CB  . GLU C 13  ? 0.6581 0.6856 0.5710 0.0085  -0.0700 0.0065  314 GLU C CB  
6905  C CG  . GLU C 13  ? 0.7412 0.7487 0.6351 0.0111  -0.0727 0.0090  314 GLU C CG  
6906  C CD  . GLU C 13  ? 0.9390 0.9342 0.8169 0.0003  -0.0728 0.0076  314 GLU C CD  
6907  O OE1 . GLU C 13  ? 1.0471 1.0382 0.9249 -0.0079 -0.0661 0.0035  314 GLU C OE1 
6908  O OE2 . GLU C 13  ? 0.9359 0.9254 0.8007 0.0004  -0.0797 0.0105  314 GLU C OE2 
6909  N N   . VAL C 14  ? 0.4866 0.5331 0.4343 0.0110  -0.0533 0.0006  315 VAL C N   
6910  C CA  . VAL C 14  ? 0.4867 0.5527 0.4513 0.0093  -0.0513 -0.0007 315 VAL C CA  
6911  C C   . VAL C 14  ? 0.4833 0.5453 0.4460 -0.0029 -0.0474 -0.0038 315 VAL C C   
6912  O O   . VAL C 14  ? 0.4477 0.4911 0.4007 -0.0065 -0.0418 -0.0061 315 VAL C O   
6913  C CB  . VAL C 14  ? 0.4902 0.5572 0.4636 0.0177  -0.0456 -0.0012 315 VAL C CB  
6914  C CG1 . VAL C 14  ? 0.4397 0.5238 0.4282 0.0140  -0.0419 -0.0029 315 VAL C CG1 
6915  C CG2 . VAL C 14  ? 0.5055 0.5780 0.4816 0.0308  -0.0499 0.0017  315 VAL C CG2 
6916  N N   . VAL C 15  ? 0.4125 0.4919 0.3841 -0.0094 -0.0502 -0.0040 316 VAL C N   
6917  C CA  . VAL C 15  ? 0.4325 0.5082 0.4025 -0.0209 -0.0469 -0.0069 316 VAL C CA  
6918  C C   . VAL C 15  ? 0.4417 0.5335 0.4274 -0.0217 -0.0435 -0.0073 316 VAL C C   
6919  O O   . VAL C 15  ? 0.3561 0.4702 0.3544 -0.0188 -0.0472 -0.0052 316 VAL C O   
6920  C CB  . VAL C 15  ? 0.4866 0.5651 0.4496 -0.0307 -0.0534 -0.0070 316 VAL C CB  
6921  C CG1 . VAL C 15  ? 0.4607 0.5323 0.4204 -0.0423 -0.0498 -0.0103 316 VAL C CG1 
6922  C CG2 . VAL C 15  ? 0.4687 0.5309 0.4149 -0.0299 -0.0566 -0.0065 316 VAL C CG2 
6923  N N   . LEU C 16  ? 0.4713 0.5523 0.4560 -0.0252 -0.0365 -0.0099 317 LEU C N   
6924  C CA  . LEU C 16  ? 0.4592 0.5518 0.4559 -0.0274 -0.0327 -0.0103 317 LEU C CA  
6925  C C   . LEU C 16  ? 0.4519 0.5385 0.4436 -0.0399 -0.0319 -0.0123 317 LEU C C   
6926  O O   . LEU C 16  ? 0.4443 0.5128 0.4225 -0.0447 -0.0317 -0.0143 317 LEU C O   
6927  C CB  . LEU C 16  ? 0.3944 0.4784 0.3935 -0.0205 -0.0255 -0.0113 317 LEU C CB  
6928  C CG  . LEU C 16  ? 0.3880 0.4716 0.3884 -0.0084 -0.0256 -0.0098 317 LEU C CG  
6929  C CD1 . LEU C 16  ? 0.3516 0.4214 0.3500 -0.0043 -0.0186 -0.0114 317 LEU C CD1 
6930  C CD2 . LEU C 16  ? 0.4486 0.5555 0.4627 -0.0020 -0.0284 -0.0077 317 LEU C CD2 
6931  N N   . THR C 17  ? 0.3233 0.4244 0.3249 -0.0453 -0.0313 -0.0117 318 THR C N   
6932  C CA  . THR C 17  ? 0.4054 0.5017 0.4020 -0.0580 -0.0316 -0.0132 318 THR C CA  
6933  C C   . THR C 17  ? 0.4130 0.5047 0.4132 -0.0595 -0.0250 -0.0140 318 THR C C   
6934  O O   . THR C 17  ? 0.3637 0.4720 0.3765 -0.0570 -0.0232 -0.0124 318 THR C O   
6935  C CB  . THR C 17  ? 0.4391 0.5569 0.4424 -0.0661 -0.0382 -0.0113 318 THR C CB  
6936  O OG1 . THR C 17  ? 0.5580 0.6793 0.5568 -0.0648 -0.0451 -0.0103 318 THR C OG1 
6937  C CG2 . THR C 17  ? 0.3703 0.4796 0.3661 -0.0802 -0.0384 -0.0128 318 THR C CG2 
6938  N N   . ASP C 18  ? 0.3666 0.4362 0.3555 -0.0634 -0.0215 -0.0166 319 ASP C N   
6939  C CA  . ASP C 18  ? 0.3853 0.4471 0.3755 -0.0635 -0.0154 -0.0174 319 ASP C CA  
6940  C C   . ASP C 18  ? 0.4120 0.4725 0.3993 -0.0758 -0.0164 -0.0175 319 ASP C C   
6941  O O   . ASP C 18  ? 0.4347 0.4806 0.4096 -0.0832 -0.0184 -0.0194 319 ASP C O   
6942  C CB  . ASP C 18  ? 0.3364 0.3753 0.3166 -0.0588 -0.0107 -0.0200 319 ASP C CB  
6943  C CG  . ASP C 18  ? 0.3859 0.4183 0.3686 -0.0570 -0.0049 -0.0204 319 ASP C CG  
6944  O OD1 . ASP C 18  ? 0.4155 0.4436 0.3957 -0.0647 -0.0044 -0.0206 319 ASP C OD1 
6945  O OD2 . ASP C 18  ? 0.4650 0.4960 0.4514 -0.0483 -0.0013 -0.0204 319 ASP C OD2 
6946  N N   . THR C 19  ? 0.3691 0.4443 0.3667 -0.0783 -0.0150 -0.0155 320 THR C N   
6947  C CA  . THR C 19  ? 0.4287 0.4998 0.4227 -0.0899 -0.0147 -0.0152 320 THR C CA  
6948  C C   . THR C 19  ? 0.4548 0.5140 0.4477 -0.0875 -0.0085 -0.0154 320 THR C C   
6949  O O   . THR C 19  ? 0.4399 0.4870 0.4252 -0.0961 -0.0079 -0.0157 320 THR C O   
6950  C CB  . THR C 19  ? 0.4395 0.5371 0.4450 -0.0971 -0.0178 -0.0123 320 THR C CB  
6951  O OG1 . THR C 19  ? 0.4256 0.5420 0.4455 -0.0880 -0.0146 -0.0105 320 THR C OG1 
6952  C CG2 . THR C 19  ? 0.3806 0.4908 0.3871 -0.1005 -0.0247 -0.0118 320 THR C CG2 
6953  N N   . LEU C 20  ? 0.3899 0.4513 0.3893 -0.0761 -0.0045 -0.0153 321 LEU C N   
6954  C CA  . LEU C 20  ? 0.3608 0.4139 0.3604 -0.0732 0.0008  -0.0152 321 LEU C CA  
6955  C C   . LEU C 20  ? 0.3876 0.4141 0.3739 -0.0740 0.0028  -0.0176 321 LEU C C   
6956  O O   . LEU C 20  ? 0.3579 0.3751 0.3416 -0.0750 0.0059  -0.0172 321 LEU C O   
6957  C CB  . LEU C 20  ? 0.3600 0.4209 0.3683 -0.0611 0.0040  -0.0149 321 LEU C CB  
6958  C CG  . LEU C 20  ? 0.4003 0.4552 0.4099 -0.0569 0.0092  -0.0146 321 LEU C CG  
6959  C CD1 . LEU C 20  ? 0.3792 0.4444 0.3933 -0.0640 0.0103  -0.0123 321 LEU C CD1 
6960  C CD2 . LEU C 20  ? 0.3398 0.4007 0.3560 -0.0453 0.0115  -0.0149 321 LEU C CD2 
6961  N N   . HIS C 21  ? 0.3492 0.3634 0.3265 -0.0730 0.0011  -0.0201 322 HIS C N   
6962  C CA  . HIS C 21  ? 0.3088 0.2988 0.2737 -0.0724 0.0035  -0.0229 322 HIS C CA  
6963  C C   . HIS C 21  ? 0.3387 0.3159 0.2942 -0.0824 0.0025  -0.0230 322 HIS C C   
6964  O O   . HIS C 21  ? 0.4439 0.4013 0.3903 -0.0809 0.0051  -0.0248 322 HIS C O   
6965  C CB  . HIS C 21  ? 0.4337 0.4146 0.3901 -0.0705 0.0019  -0.0256 322 HIS C CB  
6966  C CG  . HIS C 21  ? 0.4334 0.4144 0.3828 -0.0802 -0.0034 -0.0261 322 HIS C CG  
6967  N ND1 . HIS C 21  ? 0.4671 0.4677 0.4239 -0.0829 -0.0081 -0.0240 322 HIS C ND1 
6968  C CD2 . HIS C 21  ? 0.4882 0.4521 0.4236 -0.0879 -0.0051 -0.0284 322 HIS C CD2 
6969  C CE1 . HIS C 21  ? 0.5293 0.5259 0.4773 -0.0926 -0.0127 -0.0249 322 HIS C CE1 
6970  N NE2 . HIS C 21  ? 0.4786 0.4520 0.4128 -0.0961 -0.0109 -0.0277 322 HIS C NE2 
6971  N N   . LEU C 22  ? 0.3978 0.3859 0.3552 -0.0927 -0.0012 -0.0211 323 LEU C N   
6972  C CA  . LEU C 22  ? 0.4866 0.4617 0.4338 -0.1038 -0.0025 -0.0208 323 LEU C CA  
6973  C C   . LEU C 22  ? 0.5267 0.4975 0.4754 -0.1033 0.0012  -0.0188 323 LEU C C   
6974  O O   . LEU C 22  ? 0.5690 0.5217 0.5063 -0.1101 0.0010  -0.0188 323 LEU C O   
6975  C CB  . LEU C 22  ? 0.4402 0.4310 0.3900 -0.1160 -0.0076 -0.0189 323 LEU C CB  
6976  C CG  . LEU C 22  ? 0.5770 0.5721 0.5241 -0.1177 -0.0123 -0.0206 323 LEU C CG  
6977  C CD1 . LEU C 22  ? 0.5053 0.5225 0.4590 -0.1288 -0.0176 -0.0181 323 LEU C CD1 
6978  C CD2 . LEU C 22  ? 0.5744 0.5415 0.5025 -0.1204 -0.0132 -0.0246 323 LEU C CD2 
6979  N N   . LYS C 23  ? 0.4242 0.4099 0.3856 -0.0956 0.0043  -0.0170 324 LYS C N   
6980  C CA  . LYS C 23  ? 0.4780 0.4598 0.4405 -0.0942 0.0078  -0.0150 324 LYS C CA  
6981  C C   . LYS C 23  ? 0.5337 0.4997 0.4927 -0.0833 0.0113  -0.0169 324 LYS C C   
6982  O O   . LYS C 23  ? 0.6260 0.5919 0.5881 -0.0794 0.0142  -0.0153 324 LYS C O   
6983  C CB  . LYS C 23  ? 0.4593 0.4667 0.4367 -0.0927 0.0092  -0.0120 324 LYS C CB  
6984  C CG  . LYS C 23  ? 0.6495 0.6776 0.6331 -0.1024 0.0059  -0.0102 324 LYS C CG  
6985  C CD  . LYS C 23  ? 0.8402 0.8901 0.8353 -0.1040 0.0081  -0.0069 324 LYS C CD  
6986  C CE  . LYS C 23  ? 0.9309 0.9706 0.9185 -0.1131 0.0097  -0.0046 324 LYS C CE  
6987  N NZ  . LYS C 23  ? 0.9563 0.9949 0.9372 -0.1287 0.0060  -0.0033 324 LYS C NZ  
6988  N N   . SER C 24  ? 0.4342 0.3879 0.3867 -0.0785 0.0112  -0.0203 325 SER C N   
6989  C CA  . SER C 24  ? 0.5153 0.4572 0.4660 -0.0683 0.0147  -0.0221 325 SER C CA  
6990  C C   . SER C 24  ? 0.5670 0.4856 0.5050 -0.0701 0.0154  -0.0227 325 SER C C   
6991  O O   . SER C 24  ? 0.5353 0.4429 0.4632 -0.0794 0.0128  -0.0227 325 SER C O   
6992  C CB  . SER C 24  ? 0.4627 0.4027 0.4122 -0.0621 0.0151  -0.0252 325 SER C CB  
6993  O OG  . SER C 24  ? 0.6742 0.6033 0.6126 -0.0681 0.0124  -0.0276 325 SER C OG  
6994  N N   . THR C 25  ? 0.7885 0.6993 0.7268 -0.0612 0.0185  -0.0233 326 THR C N   
6995  C CA  . THR C 25  ? 1.0199 0.9111 0.9479 -0.0622 0.0187  -0.0227 326 THR C CA  
6996  C C   . THR C 25  ? 0.9699 0.8442 0.8915 -0.0526 0.0210  -0.0258 326 THR C C   
6997  O O   . THR C 25  ? 0.9799 0.8337 0.8880 -0.0543 0.0201  -0.0279 326 THR C O   
6998  C CB  . THR C 25  ? 1.1826 1.0816 1.1166 -0.0632 0.0195  -0.0185 326 THR C CB  
6999  O OG1 . THR C 25  ? 1.3215 1.2001 1.2443 -0.0641 0.0193  -0.0174 326 THR C OG1 
7000  C CG2 . THR C 25  ? 1.1320 1.0455 1.0785 -0.0535 0.0223  -0.0181 326 THR C CG2 
7001  N N   . LEU C 26  ? 0.9670 0.8492 0.8973 -0.0427 0.0238  -0.0263 327 LEU C N   
7002  C CA  . LEU C 26  ? 1.0074 0.8766 0.9329 -0.0336 0.0261  -0.0292 327 LEU C CA  
7003  C C   . LEU C 26  ? 0.9025 0.7721 0.8263 -0.0311 0.0272  -0.0333 327 LEU C C   
7004  O O   . LEU C 26  ? 0.8767 0.7563 0.8031 -0.0360 0.0259  -0.0335 327 LEU C O   
7005  C CB  . LEU C 26  ? 1.1129 0.9904 1.0480 -0.0248 0.0283  -0.0278 327 LEU C CB  
7006  C CG  . LEU C 26  ? 1.1665 1.0347 1.0995 -0.0144 0.0306  -0.0301 327 LEU C CG  
7007  C CD1 . LEU C 26  ? 1.2301 1.0766 1.1509 -0.0137 0.0294  -0.0297 327 LEU C CD1 
7008  C CD2 . LEU C 26  ? 1.0859 0.9684 1.0311 -0.0070 0.0325  -0.0289 327 LEU C CD2 
7009  N N   . GLU C 27  ? 0.8568 0.7161 0.7762 -0.0231 0.0298  -0.0365 328 GLU C N   
7010  C CA  . GLU C 27  ? 0.7404 0.5982 0.6563 -0.0204 0.0317  -0.0407 328 GLU C CA  
7011  C C   . GLU C 27  ? 0.5974 0.4746 0.5252 -0.0174 0.0334  -0.0403 328 GLU C C   
7012  O O   . GLU C 27  ? 0.5870 0.4763 0.5256 -0.0138 0.0343  -0.0379 328 GLU C O   
7013  C CB  . GLU C 27  ? 0.8362 0.6796 0.7451 -0.0116 0.0347  -0.0442 328 GLU C CB  
7014  C CG  . GLU C 27  ? 1.0176 0.8369 0.9106 -0.0139 0.0331  -0.0457 328 GLU C CG  
7015  C CD  . GLU C 27  ? 1.2290 1.0342 1.1127 -0.0058 0.0363  -0.0509 328 GLU C CD  
7016  O OE1 . GLU C 27  ? 1.2196 1.0348 1.1113 0.0032  0.0402  -0.0524 328 GLU C OE1 
7017  O OE2 . GLU C 27  ? 1.3597 1.1439 1.2275 -0.0087 0.0352  -0.0536 328 GLU C OE2 
7018  N N   . THR C 28  ? 0.5747 0.4534 0.4990 -0.0194 0.0336  -0.0427 329 THR C N   
7019  C CA  . THR C 28  ? 0.5376 0.4295 0.4691 -0.0158 0.0358  -0.0432 329 THR C CA  
7020  C C   . THR C 28  ? 0.4981 0.3863 0.4281 -0.0080 0.0404  -0.0465 329 THR C C   
7021  O O   . THR C 28  ? 0.6033 0.5028 0.5406 -0.0044 0.0428  -0.0464 329 THR C O   
7022  C CB  . THR C 28  ? 0.6469 0.5415 0.5740 -0.0215 0.0337  -0.0439 329 THR C CB  
7023  O OG1 . THR C 28  ? 0.5015 0.3809 0.4148 -0.0231 0.0341  -0.0479 329 THR C OG1 
7024  C CG2 . THR C 28  ? 0.7088 0.6108 0.6392 -0.0290 0.0291  -0.0406 329 THR C CG2 
7025  N N   . GLY C 29  ? 0.4488 0.3213 0.3691 -0.0052 0.0417  -0.0495 330 GLY C N   
7026  C CA  . GLY C 29  ? 0.4828 0.3516 0.3999 0.0020  0.0463  -0.0534 330 GLY C CA  
7027  C C   . GLY C 29  ? 0.4945 0.3545 0.3993 -0.0007 0.0473  -0.0575 330 GLY C C   
7028  O O   . GLY C 29  ? 0.5478 0.3990 0.4455 0.0050  0.0511  -0.0616 330 GLY C O   
7029  N N   . CYS C 30  ? 0.4196 0.2818 0.3212 -0.0088 0.0439  -0.0564 331 CYS C N   
7030  C CA  . CYS C 30  ? 0.4227 0.2759 0.3113 -0.0117 0.0445  -0.0602 331 CYS C CA  
7031  C C   . CYS C 30  ? 0.5447 0.3772 0.4185 -0.0150 0.0425  -0.0628 331 CYS C C   
7032  O O   . CYS C 30  ? 0.4955 0.3217 0.3693 -0.0173 0.0396  -0.0607 331 CYS C O   
7033  C CB  . CYS C 30  ? 0.4218 0.2844 0.3112 -0.0188 0.0411  -0.0582 331 CYS C CB  
7034  S SG  . CYS C 30  ? 0.4149 0.2991 0.3195 -0.0165 0.0421  -0.0545 331 CYS C SG  
7035  N N   . THR C 31  ? 0.4288 0.2496 0.2887 -0.0156 0.0441  -0.0674 332 THR C N   
7036  C CA  . THR C 31  ? 0.5244 0.3241 0.3673 -0.0207 0.0415  -0.0702 332 THR C CA  
7037  C C   . THR C 31  ? 0.5276 0.3275 0.3619 -0.0296 0.0382  -0.0710 332 THR C C   
7038  O O   . THR C 31  ? 0.5698 0.3855 0.4114 -0.0308 0.0380  -0.0691 332 THR C O   
7039  C CB  . THR C 31  ? 0.6525 0.4342 0.4836 -0.0124 0.0463  -0.0758 332 THR C CB  
7040  O OG1 . THR C 31  ? 0.7114 0.4950 0.5369 -0.0095 0.0507  -0.0799 332 THR C OG1 
7041  C CG2 . THR C 31  ? 0.6204 0.4056 0.4619 -0.0019 0.0496  -0.0749 332 THR C CG2 
7042  N N   . GLU C 32  ? 0.5588 0.3400 0.3765 -0.0361 0.0352  -0.0738 333 GLU C N   
7043  C CA  . GLU C 32  ? 0.6524 0.4331 0.4606 -0.0451 0.0313  -0.0747 333 GLU C CA  
7044  C C   . GLU C 32  ? 0.6312 0.4130 0.4333 -0.0408 0.0359  -0.0784 333 GLU C C   
7045  O O   . GLU C 32  ? 0.6500 0.4389 0.4494 -0.0464 0.0331  -0.0776 333 GLU C O   
7046  C CB  . GLU C 32  ? 0.7889 0.5475 0.5787 -0.0535 0.0272  -0.0773 333 GLU C CB  
7047  C CG  . GLU C 32  ? 1.0283 0.7922 0.8225 -0.0646 0.0201  -0.0727 333 GLU C CG  
7048  C CD  . GLU C 32  ? 1.2372 0.9851 1.0266 -0.0661 0.0192  -0.0722 333 GLU C CD  
7049  O OE1 . GLU C 32  ? 1.2722 1.0009 1.0516 -0.0587 0.0232  -0.0761 333 GLU C OE1 
7050  O OE2 . GLU C 32  ? 1.3283 1.0828 1.1236 -0.0745 0.0144  -0.0678 333 GLU C OE2 
7051  N N   . TYR C 33  ? 0.5032 0.2791 0.3031 -0.0308 0.0428  -0.0822 334 TYR C N   
7052  C CA  . TYR C 33  ? 0.5134 0.2895 0.3060 -0.0270 0.0480  -0.0862 334 TYR C CA  
7053  C C   . TYR C 33  ? 0.4895 0.2838 0.2971 -0.0187 0.0538  -0.0848 334 TYR C C   
7054  O O   . TYR C 33  ? 0.5785 0.3759 0.3815 -0.0161 0.0586  -0.0875 334 TYR C O   
7055  C CB  . TYR C 33  ? 0.6377 0.3905 0.4114 -0.0228 0.0519  -0.0932 334 TYR C CB  
7056  C CG  . TYR C 33  ? 0.7557 0.4891 0.5106 -0.0329 0.0461  -0.0954 334 TYR C CG  
7057  C CD1 . TYR C 33  ? 0.7471 0.4782 0.4893 -0.0401 0.0441  -0.0973 334 TYR C CD1 
7058  C CD2 . TYR C 33  ? 0.7861 0.5038 0.5356 -0.0362 0.0421  -0.0951 334 TYR C CD2 
7059  C CE1 . TYR C 33  ? 0.9146 0.6288 0.6395 -0.0504 0.0382  -0.0991 334 TYR C CE1 
7060  C CE2 . TYR C 33  ? 0.8371 0.5372 0.5690 -0.0469 0.0365  -0.0969 334 TYR C CE2 
7061  C CZ  . TYR C 33  ? 0.9693 0.6683 0.6893 -0.0540 0.0344  -0.0990 334 TYR C CZ  
7062  O OH  . TYR C 33  ? 1.0924 0.7745 0.7945 -0.0655 0.0283  -0.1009 334 TYR C OH  
7063  N N   . ILE C 34  ? 0.4599 0.2667 0.2848 -0.0152 0.0535  -0.0805 335 ILE C N   
7064  C CA  . ILE C 34  ? 0.4504 0.2750 0.2896 -0.0086 0.0584  -0.0789 335 ILE C CA  
7065  C C   . ILE C 34  ? 0.5473 0.3881 0.4026 -0.0117 0.0542  -0.0726 335 ILE C C   
7066  O O   . ILE C 34  ? 0.5475 0.3870 0.4082 -0.0133 0.0503  -0.0699 335 ILE C O   
7067  C CB  . ILE C 34  ? 0.5966 0.4193 0.4402 0.0022  0.0640  -0.0815 335 ILE C CB  
7068  C CG1 . ILE C 34  ? 0.6288 0.4329 0.4552 0.0063  0.0680  -0.0882 335 ILE C CG1 
7069  C CG2 . ILE C 34  ? 0.5898 0.4313 0.4462 0.0077  0.0694  -0.0806 335 ILE C CG2 
7070  C CD1 . ILE C 34  ? 0.7671 0.5615 0.5938 0.0158  0.0704  -0.0905 335 ILE C CD1 
7071  N N   . CYS C 35  ? 0.4335 0.2886 0.2954 -0.0127 0.0550  -0.0703 336 CYS C N   
7072  C CA  . CYS C 35  ? 0.4393 0.3095 0.3162 -0.0138 0.0522  -0.0648 336 CYS C CA  
7073  C C   . CYS C 35  ? 0.4475 0.3285 0.3364 -0.0066 0.0573  -0.0643 336 CYS C C   
7074  O O   . CYS C 35  ? 0.4636 0.3482 0.3507 -0.0036 0.0626  -0.0666 336 CYS C O   
7075  C CB  . CYS C 35  ? 0.4498 0.3276 0.3259 -0.0193 0.0490  -0.0621 336 CYS C CB  
7076  S SG  . CYS C 35  ? 0.4271 0.3214 0.3203 -0.0193 0.0457  -0.0560 336 CYS C SG  
7077  N N   . MET C 36  ? 0.4218 0.3088 0.3226 -0.0044 0.0556  -0.0613 337 MET C N   
7078  C CA  . MET C 36  ? 0.4205 0.3189 0.3336 0.0016  0.0592  -0.0602 337 MET C CA  
7079  C C   . MET C 36  ? 0.4179 0.3291 0.3421 -0.0010 0.0562  -0.0554 337 MET C C   
7080  O O   . MET C 36  ? 0.3940 0.3133 0.3291 0.0025  0.0569  -0.0535 337 MET C O   
7081  C CB  . MET C 36  ? 0.4707 0.3636 0.3867 0.0075  0.0600  -0.0612 337 MET C CB  
7082  C CG  . MET C 36  ? 0.5798 0.4567 0.4828 0.0105  0.0623  -0.0662 337 MET C CG  
7083  S SD  . MET C 36  ? 0.7197 0.5933 0.6267 0.0215  0.0658  -0.0682 337 MET C SD  
7084  C CE  . MET C 36  ? 0.6985 0.5801 0.6190 0.0205  0.0611  -0.0624 337 MET C CE  
7085  N N   . GLY C 37  ? 0.3564 0.2689 0.2772 -0.0067 0.0528  -0.0535 338 GLY C N   
7086  C CA  . GLY C 37  ? 0.3905 0.3131 0.3199 -0.0085 0.0497  -0.0493 338 GLY C CA  
7087  C C   . GLY C 37  ? 0.4051 0.3377 0.3424 -0.0057 0.0530  -0.0481 338 GLY C C   
7088  O O   . GLY C 37  ? 0.4670 0.4068 0.4125 -0.0058 0.0508  -0.0449 338 GLY C O   
7089  N N   . SER C 38  ? 0.2998 0.2335 0.2347 -0.0036 0.0582  -0.0506 339 SER C N   
7090  C CA  . SER C 38  ? 0.3988 0.3430 0.3412 -0.0023 0.0613  -0.0494 339 SER C CA  
7091  C C   . SER C 38  ? 0.4304 0.3804 0.3816 0.0033  0.0646  -0.0507 339 SER C C   
7092  O O   . SER C 38  ? 0.3765 0.3364 0.3341 0.0041  0.0675  -0.0501 339 SER C O   
7093  C CB  . SER C 38  ? 0.3295 0.2745 0.2645 -0.0049 0.0649  -0.0505 339 SER C CB  
7094  O OG  . SER C 38  ? 0.3612 0.3035 0.2906 -0.0024 0.0700  -0.0548 339 SER C OG  
7095  N N   . ILE C 39  ? 0.3968 0.3405 0.3479 0.0070  0.0640  -0.0522 340 ILE C N   
7096  C CA  . ILE C 39  ? 0.3598 0.3085 0.3193 0.0132  0.0660  -0.0528 340 ILE C CA  
7097  C C   . ILE C 39  ? 0.3304 0.2853 0.2995 0.0128  0.0624  -0.0489 340 ILE C C   
7098  O O   . ILE C 39  ? 0.3620 0.3121 0.3300 0.0099  0.0580  -0.0468 340 ILE C O   
7099  C CB  . ILE C 39  ? 0.4735 0.4104 0.4272 0.0176  0.0662  -0.0556 340 ILE C CB  
7100  C CG1 . ILE C 39  ? 0.4994 0.4276 0.4410 0.0174  0.0695  -0.0598 340 ILE C CG1 
7101  C CG2 . ILE C 39  ? 0.4867 0.4288 0.4487 0.0253  0.0682  -0.0561 340 ILE C CG2 
7102  C CD1 . ILE C 39  ? 0.4492 0.3865 0.3925 0.0208  0.0758  -0.0624 340 ILE C CD1 
7103  N N   . MET C 40  ? 0.3164 0.2828 0.2949 0.0153  0.0642  -0.0481 341 MET C N   
7104  C CA  . MET C 40  ? 0.4231 0.3953 0.4096 0.0145  0.0609  -0.0446 341 MET C CA  
7105  C C   . MET C 40  ? 0.3726 0.3392 0.3607 0.0175  0.0580  -0.0436 341 MET C C   
7106  O O   . MET C 40  ? 0.3896 0.3538 0.3779 0.0147  0.0543  -0.0411 341 MET C O   
7107  C CB  . MET C 40  ? 0.4568 0.4424 0.4520 0.0157  0.0633  -0.0442 341 MET C CB  
7108  C CG  . MET C 40  ? 0.6771 0.6682 0.6787 0.0137  0.0600  -0.0409 341 MET C CG  
7109  S SD  . MET C 40  ? 0.7755 0.7716 0.7760 0.0072  0.0603  -0.0394 341 MET C SD  
7110  C CE  . MET C 40  ? 0.4646 0.4678 0.4644 0.0070  0.0662  -0.0421 341 MET C CE  
7111  N N   . HIS C 41  ? 0.4728 0.4368 0.4612 0.0235  0.0597  -0.0455 342 HIS C N   
7112  C CA  A HIS C 41  ? 0.5322 0.4881 0.5198 0.0266  0.0570  -0.0445 342 HIS C CA  
7113  C CA  B HIS C 41  ? 0.5313 0.4871 0.5189 0.0264  0.0569  -0.0445 342 HIS C CA  
7114  C C   . HIS C 41  ? 0.5537 0.4955 0.5314 0.0291  0.0581  -0.0477 342 HIS C C   
7115  O O   . HIS C 41  ? 0.5197 0.4607 0.4972 0.0360  0.0610  -0.0503 342 HIS C O   
7116  C CB  A HIS C 41  ? 0.5364 0.5003 0.5327 0.0327  0.0571  -0.0435 342 HIS C CB  
7117  C CB  B HIS C 41  ? 0.5412 0.5050 0.5375 0.0321  0.0568  -0.0432 342 HIS C CB  
7118  C CG  A HIS C 41  ? 0.5343 0.5135 0.5400 0.0309  0.0573  -0.0417 342 HIS C CG  
7119  C CG  B HIS C 41  ? 0.6331 0.5874 0.6273 0.0348  0.0535  -0.0415 342 HIS C CG  
7120  N ND1 A HIS C 41  ? 0.5419 0.5243 0.5512 0.0277  0.0539  -0.0385 342 HIS C ND1 
7121  N ND1 B HIS C 41  ? 0.6412 0.5834 0.6280 0.0303  0.0506  -0.0403 342 HIS C ND1 
7122  C CD2 A HIS C 41  ? 0.5318 0.5238 0.5433 0.0316  0.0605  -0.0429 342 HIS C CD2 
7123  C CD2 B HIS C 41  ? 0.6644 0.6195 0.6624 0.0412  0.0525  -0.0405 342 HIS C CD2 
7124  C CE1 A HIS C 41  ? 0.5124 0.5072 0.5285 0.0264  0.0547  -0.0378 342 HIS C CE1 
7125  C CE1 B HIS C 41  ? 0.6711 0.6060 0.6564 0.0332  0.0482  -0.0385 342 HIS C CE1 
7126  N NE2 A HIS C 41  ? 0.4650 0.4663 0.4829 0.0282  0.0586  -0.0402 342 HIS C NE2 
7127  N NE2 B HIS C 41  ? 0.6769 0.6187 0.6685 0.0402  0.0491  -0.0386 342 HIS C NE2 
7128  N N   . PRO C 42  ? 0.5754 0.5057 0.5441 0.0239  0.0558  -0.0477 343 PRO C N   
7129  C CA  . PRO C 42  ? 0.6512 0.5653 0.6085 0.0256  0.0562  -0.0508 343 PRO C CA  
7130  C C   . PRO C 42  ? 0.7758 0.6782 0.7299 0.0270  0.0530  -0.0491 343 PRO C C   
7131  O O   . PRO C 42  ? 0.8752 0.7633 0.8206 0.0311  0.0536  -0.0516 343 PRO C O   
7132  C CB  . PRO C 42  ? 0.5967 0.5054 0.5458 0.0179  0.0548  -0.0513 343 PRO C CB  
7133  C CG  . PRO C 42  ? 0.5782 0.4987 0.5349 0.0126  0.0522  -0.0476 343 PRO C CG  
7134  C CD  . PRO C 42  ? 0.6026 0.5348 0.5708 0.0163  0.0527  -0.0453 343 PRO C CD  
7135  N N   . ASP C 51  ? 1.3213 1.1661 1.2632 0.0715  0.0106  -0.0014 352 ASP C N   
7136  C CA  . ASP C 51  ? 1.3849 1.2041 1.3099 0.0656  0.0097  -0.0001 352 ASP C CA  
7137  C C   . ASP C 51  ? 1.3502 1.1729 1.2738 0.0508  0.0113  0.0011  352 ASP C C   
7138  O O   . ASP C 51  ? 1.3678 1.2109 1.3032 0.0465  0.0140  -0.0007 352 ASP C O   
7139  C CB  . ASP C 51  ? 1.4286 1.2336 1.3476 0.0706  0.0120  -0.0049 352 ASP C CB  
7140  C CG  . ASP C 51  ? 1.4760 1.2493 1.3748 0.0690  0.0094  -0.0030 352 ASP C CG  
7141  O OD1 . ASP C 51  ? 1.5343 1.2966 1.4242 0.0662  0.0055  0.0024  352 ASP C OD1 
7142  O OD2 . ASP C 51  ? 1.4433 1.2018 1.3340 0.0699  0.0112  -0.0070 352 ASP C OD2 
7143  N N   . VAL C 52  ? 1.2388 1.0416 1.1475 0.0430  0.0096  0.0041  353 VAL C N   
7144  C CA  . VAL C 52  ? 1.0504 0.8579 0.9575 0.0293  0.0105  0.0064  353 VAL C CA  
7145  C C   . VAL C 52  ? 0.9102 0.6963 0.8025 0.0206  0.0103  0.0067  353 VAL C C   
7146  O O   . VAL C 52  ? 0.9780 0.7420 0.8586 0.0251  0.0088  0.0057  353 VAL C O   
7147  C CB  . VAL C 52  ? 1.0364 0.8469 0.9413 0.0265  0.0078  0.0121  353 VAL C CB  
7148  C CG1 . VAL C 52  ? 1.0376 0.8720 0.9576 0.0317  0.0082  0.0115  353 VAL C CG1 
7149  C CG2 . VAL C 52  ? 0.9473 0.7342 0.8375 0.0317  0.0033  0.0162  353 VAL C CG2 
7150  N N   . ALA C 53  ? 0.7612 0.5540 0.6535 0.0078  0.0117  0.0080  354 ALA C N   
7151  C CA  . ALA C 53  ? 0.7537 0.5305 0.6337 -0.0029 0.0115  0.0082  354 ALA C CA  
7152  C C   . ALA C 53  ? 0.8766 0.6298 0.7388 -0.0074 0.0081  0.0136  354 ALA C C   
7153  O O   . ALA C 53  ? 0.8213 0.5771 0.6824 -0.0076 0.0065  0.0182  354 ALA C O   
7154  C CB  . ALA C 53  ? 0.7268 0.5224 0.6146 -0.0147 0.0141  0.0081  354 ALA C CB  
7155  N N   . THR C 54  ? 0.9950 0.7236 0.8417 -0.0116 0.0068  0.0130  355 THR C N   
7156  C CA  . THR C 54  ? 1.0613 0.7642 0.8886 -0.0176 0.0033  0.0181  355 THR C CA  
7157  C C   . THR C 54  ? 1.0708 0.7814 0.8960 -0.0345 0.0042  0.0219  355 THR C C   
7158  O O   . THR C 54  ? 1.0592 0.7929 0.8971 -0.0412 0.0073  0.0200  355 THR C O   
7159  C CB  . THR C 54  ? 1.0034 0.6753 0.8131 -0.0168 0.0015  0.0159  355 THR C CB  
7160  O OG1 . THR C 54  ? 1.0387 0.7119 0.8469 -0.0291 0.0032  0.0132  355 THR C OG1 
7161  C CG2 . THR C 54  ? 1.0068 0.6752 0.8207 0.0002  0.0019  0.0110  355 THR C CG2 
7162  N N   . LYS C 55  ? 1.0087 0.7000 0.8174 -0.0413 0.0014  0.0276  356 LYS C N   
7163  C CA  . LYS C 55  ? 0.9474 0.6450 0.7525 -0.0582 0.0025  0.0317  356 LYS C CA  
7164  C C   . LYS C 55  ? 0.9490 0.6496 0.7544 -0.0698 0.0041  0.0286  356 LYS C C   
7165  O O   . LYS C 55  ? 0.8555 0.5807 0.6725 -0.0788 0.0070  0.0284  356 LYS C O   
7166  C CB  . LYS C 55  ? 0.9354 0.6055 0.7186 -0.0643 -0.0011 0.0381  356 LYS C CB  
7167  C CG  . LYS C 55  ? 0.8942 0.5765 0.6785 -0.0693 -0.0006 0.0439  356 LYS C CG  
7168  C CD  . LYS C 55  ? 0.8844 0.5361 0.6446 -0.0757 -0.0044 0.0505  356 LYS C CD  
7169  C CE  . LYS C 55  ? 0.9593 0.6151 0.7187 -0.0702 -0.0058 0.0555  356 LYS C CE  
7170  N NZ  . LYS C 55  ? 1.0767 0.7033 0.8116 -0.0776 -0.0095 0.0627  356 LYS C NZ  
7171  N N   . ASP C 56  ? 0.9240 0.5998 0.7165 -0.0694 0.0022  0.0259  357 ASP C N   
7172  C CA  . ASP C 56  ? 0.9557 0.6298 0.7447 -0.0818 0.0027  0.0233  357 ASP C CA  
7173  C C   . ASP C 56  ? 0.8510 0.5493 0.6583 -0.0775 0.0056  0.0173  357 ASP C C   
7174  O O   . ASP C 56  ? 0.8447 0.5530 0.6549 -0.0888 0.0064  0.0158  357 ASP C O   
7175  C CB  . ASP C 56  ? 1.0904 0.7262 0.8564 -0.0830 -0.0007 0.0224  357 ASP C CB  
7176  C CG  . ASP C 56  ? 1.2106 0.8192 0.9555 -0.0894 -0.0040 0.0289  357 ASP C CG  
7177  O OD1 . ASP C 56  ? 1.2342 0.8513 0.9775 -0.1038 -0.0035 0.0338  357 ASP C OD1 
7178  O OD2 . ASP C 56  ? 1.2790 0.8580 1.0088 -0.0797 -0.0069 0.0292  357 ASP C OD2 
7179  N N   . GLN C 57  ? 0.7517 0.4598 0.5711 -0.0619 0.0069  0.0139  358 GLN C N   
7180  C CA  . GLN C 57  ? 0.6961 0.4301 0.5338 -0.0585 0.0099  0.0091  358 GLN C CA  
7181  C C   . GLN C 57  ? 0.6591 0.4239 0.5124 -0.0643 0.0123  0.0112  358 GLN C C   
7182  O O   . GLN C 57  ? 0.6644 0.4486 0.5289 -0.0682 0.0141  0.0086  358 GLN C O   
7183  C CB  . GLN C 57  ? 0.7726 0.5099 0.6187 -0.0413 0.0109  0.0055  358 GLN C CB  
7184  C CG  . GLN C 57  ? 0.9013 0.6148 0.7362 -0.0335 0.0100  0.0013  358 GLN C CG  
7185  C CD  . GLN C 57  ? 0.9527 0.6757 0.7991 -0.0172 0.0118  -0.0023 358 GLN C CD  
7186  O OE1 . GLN C 57  ? 0.8973 0.6229 0.7475 -0.0080 0.0110  0.0000  358 GLN C OE1 
7187  N NE2 . GLN C 57  ? 1.0234 0.7531 0.8756 -0.0140 0.0141  -0.0078 358 GLN C NE2 
7188  N N   . LEU C 58  ? 0.5374 0.3065 0.3912 -0.0643 0.0122  0.0159  359 LEU C N   
7189  C CA  . LEU C 58  ? 0.5502 0.3485 0.4190 -0.0668 0.0149  0.0172  359 LEU C CA  
7190  C C   . LEU C 58  ? 0.5393 0.3481 0.4079 -0.0826 0.0159  0.0192  359 LEU C C   
7191  O O   . LEU C 58  ? 0.5913 0.4261 0.4744 -0.0846 0.0185  0.0178  359 LEU C O   
7192  C CB  . LEU C 58  ? 0.5698 0.3688 0.4378 -0.0619 0.0145  0.0213  359 LEU C CB  
7193  C CG  . LEU C 58  ? 0.5489 0.3761 0.4325 -0.0597 0.0174  0.0214  359 LEU C CG  
7194  C CD1 . LEU C 58  ? 0.6159 0.4596 0.5151 -0.0503 0.0192  0.0160  359 LEU C CD1 
7195  C CD2 . LEU C 58  ? 0.5435 0.3676 0.4235 -0.0544 0.0162  0.0253  359 LEU C CD2 
7196  N N   . PHE C 59  ? 0.5863 0.3754 0.4384 -0.0938 0.0139  0.0226  360 PHE C N   
7197  C CA  . PHE C 59  ? 0.6980 0.4974 0.5491 -0.1103 0.0147  0.0251  360 PHE C CA  
7198  C C   . PHE C 59  ? 0.6781 0.4985 0.5423 -0.1136 0.0160  0.0210  360 PHE C C   
7199  O O   . PHE C 59  ? 0.6247 0.4732 0.5030 -0.1165 0.0187  0.0213  360 PHE C O   
7200  C CB  . PHE C 59  ? 0.8603 0.6311 0.6897 -0.1224 0.0116  0.0284  360 PHE C CB  
7201  C CG  . PHE C 59  ? 0.9740 0.7274 0.7893 -0.1240 0.0104  0.0342  360 PHE C CG  
7202  C CD1 . PHE C 59  ? 0.9740 0.7452 0.7941 -0.1293 0.0128  0.0385  360 PHE C CD1 
7203  C CD2 . PHE C 59  ? 0.9906 0.7086 0.7866 -0.1203 0.0067  0.0354  360 PHE C CD2 
7204  C CE1 . PHE C 59  ? 0.9347 0.6889 0.7403 -0.1314 0.0115  0.0442  360 PHE C CE1 
7205  C CE2 . PHE C 59  ? 0.9977 0.6981 0.7792 -0.1217 0.0050  0.0412  360 PHE C CE2 
7206  C CZ  . PHE C 59  ? 0.9469 0.6655 0.7332 -0.1276 0.0073  0.0458  360 PHE C CZ  
7207  N N   . PRO C 60  ? 0.6460 0.4540 0.5058 -0.1126 0.0141  0.0169  361 PRO C N   
7208  C CA  . PRO C 60  ? 0.5923 0.4201 0.4632 -0.1171 0.0147  0.0136  361 PRO C CA  
7209  C C   . PRO C 60  ? 0.5247 0.3786 0.4151 -0.1062 0.0174  0.0108  361 PRO C C   
7210  O O   . PRO C 60  ? 0.5877 0.4649 0.4898 -0.1104 0.0184  0.0098  361 PRO C O   
7211  C CB  . PRO C 60  ? 0.6370 0.4414 0.4960 -0.1170 0.0119  0.0098  361 PRO C CB  
7212  C CG  . PRO C 60  ? 0.6796 0.4610 0.5298 -0.1045 0.0114  0.0091  361 PRO C CG  
7213  C CD  . PRO C 60  ? 0.6692 0.4466 0.5149 -0.1055 0.0116  0.0146  361 PRO C CD  
7214  N N   . LEU C 61  ? 0.4441 0.2945 0.3379 -0.0922 0.0183  0.0094  362 LEU C N   
7215  C CA  . LEU C 61  ? 0.4302 0.3039 0.3411 -0.0828 0.0208  0.0070  362 LEU C CA  
7216  C C   . LEU C 61  ? 0.4820 0.3785 0.4024 -0.0864 0.0232  0.0100  362 LEU C C   
7217  O O   . LEU C 61  ? 0.4899 0.4094 0.4232 -0.0863 0.0249  0.0085  362 LEU C O   
7218  C CB  . LEU C 61  ? 0.4514 0.3167 0.3633 -0.0686 0.0211  0.0052  362 LEU C CB  
7219  C CG  . LEU C 61  ? 0.5940 0.4404 0.4989 -0.0623 0.0197  0.0014  362 LEU C CG  
7220  C CD1 . LEU C 61  ? 0.5620 0.4050 0.4701 -0.0484 0.0204  0.0002  362 LEU C CD1 
7221  C CD2 . LEU C 61  ? 0.5192 0.3759 0.4306 -0.0635 0.0202  -0.0027 362 LEU C CD2 
7222  N N   . ALA C 62  ? 0.4693 0.3587 0.3823 -0.0893 0.0233  0.0142  363 ALA C N   
7223  C CA  . ALA C 62  ? 0.4346 0.3442 0.3544 -0.0933 0.0261  0.0171  363 ALA C CA  
7224  C C   . ALA C 62  ? 0.4388 0.3655 0.3632 -0.1055 0.0269  0.0178  363 ALA C C   
7225  O O   . ALA C 62  ? 0.3816 0.3338 0.3193 -0.1047 0.0296  0.0170  363 ALA C O   
7226  C CB  . ALA C 62  ? 0.4952 0.3908 0.4029 -0.0962 0.0257  0.0219  363 ALA C CB  
7227  N N   . LYS C 63  ? 0.5220 0.4348 0.4354 -0.1168 0.0245  0.0191  364 LYS C N   
7228  C CA  . LYS C 63  ? 0.5537 0.4834 0.4712 -0.1298 0.0248  0.0200  364 LYS C CA  
7229  C C   . LYS C 63  ? 0.5186 0.4704 0.4516 -0.1252 0.0252  0.0160  364 LYS C C   
7230  O O   . LYS C 63  ? 0.4813 0.4600 0.4265 -0.1281 0.0274  0.0164  364 LYS C O   
7231  C CB  . LYS C 63  ? 0.5082 0.4160 0.4097 -0.1425 0.0214  0.0214  364 LYS C CB  
7232  C CG  . LYS C 63  ? 0.5313 0.4580 0.4372 -0.1575 0.0212  0.0227  364 LYS C CG  
7233  C CD  . LYS C 63  ? 0.7105 0.6140 0.5989 -0.1716 0.0175  0.0241  364 LYS C CD  
7234  C CE  . LYS C 63  ? 0.7768 0.7016 0.6697 -0.1885 0.0174  0.0263  364 LYS C CE  
7235  N NZ  . LYS C 63  ? 0.7235 0.6735 0.6325 -0.1863 0.0168  0.0226  364 LYS C NZ  
7236  N N   . GLU C 64  ? 0.4425 0.3832 0.3748 -0.1177 0.0232  0.0120  365 GLU C N   
7237  C CA  . GLU C 64  ? 0.4711 0.4299 0.4159 -0.1140 0.0229  0.0085  365 GLU C CA  
7238  C C   . GLU C 64  ? 0.4152 0.3972 0.3751 -0.1043 0.0262  0.0077  365 GLU C C   
7239  O O   . GLU C 64  ? 0.3340 0.3394 0.3056 -0.1051 0.0268  0.0070  365 GLU C O   
7240  C CB  . GLU C 64  ? 0.5481 0.4891 0.4877 -0.1070 0.0207  0.0044  365 GLU C CB  
7241  C CG  . GLU C 64  ? 0.7452 0.7023 0.6954 -0.1036 0.0200  0.0010  365 GLU C CG  
7242  C CD  . GLU C 64  ? 0.9890 0.9591 0.9411 -0.1161 0.0177  0.0017  365 GLU C CD  
7243  O OE1 . GLU C 64  ? 1.0459 1.0003 0.9855 -0.1270 0.0150  0.0026  365 GLU C OE1 
7244  O OE2 . GLU C 64  ? 1.0190 1.0147 0.9847 -0.1150 0.0182  0.0015  365 GLU C OE2 
7245  N N   . PHE C 65  ? 0.3887 0.3643 0.3479 -0.0951 0.0280  0.0080  366 PHE C N   
7246  C CA  . PHE C 65  ? 0.3797 0.3751 0.3512 -0.0867 0.0310  0.0072  366 PHE C CA  
7247  C C   . PHE C 65  ? 0.3143 0.3306 0.2912 -0.0936 0.0337  0.0099  366 PHE C C   
7248  O O   . PHE C 65  ? 0.3564 0.3954 0.3454 -0.0906 0.0354  0.0086  366 PHE C O   
7249  C CB  . PHE C 65  ? 0.3569 0.3413 0.3255 -0.0769 0.0320  0.0071  366 PHE C CB  
7250  C CG  . PHE C 65  ? 0.3644 0.3666 0.3427 -0.0701 0.0351  0.0066  366 PHE C CG  
7251  C CD1 . PHE C 65  ? 0.3369 0.3510 0.3253 -0.0621 0.0356  0.0032  366 PHE C CD1 
7252  C CD2 . PHE C 65  ? 0.3539 0.3601 0.3299 -0.0721 0.0373  0.0095  366 PHE C CD2 
7253  C CE1 . PHE C 65  ? 0.3858 0.4140 0.3814 -0.0559 0.0383  0.0024  366 PHE C CE1 
7254  C CE2 . PHE C 65  ? 0.3980 0.4196 0.3816 -0.0658 0.0403  0.0085  366 PHE C CE2 
7255  C CZ  . PHE C 65  ? 0.4163 0.4483 0.4095 -0.0576 0.0407  0.0049  366 PHE C CZ  
7256  N N   . ILE C 66  ? 0.3573 0.3664 0.3251 -0.1025 0.0342  0.0138  367 ILE C N   
7257  C CA  . ILE C 66  ? 0.4015 0.4315 0.3741 -0.1094 0.0375  0.0165  367 ILE C CA  
7258  C C   . ILE C 66  ? 0.4139 0.4642 0.3950 -0.1175 0.0370  0.0162  367 ILE C C   
7259  O O   . ILE C 66  ? 0.4124 0.4892 0.4054 -0.1167 0.0399  0.0160  367 ILE C O   
7260  C CB  . ILE C 66  ? 0.4317 0.4477 0.3908 -0.1186 0.0380  0.0212  367 ILE C CB  
7261  C CG1 . ILE C 66  ? 0.4662 0.4661 0.4188 -0.1090 0.0383  0.0216  367 ILE C CG1 
7262  C CG2 . ILE C 66  ? 0.4214 0.4603 0.3848 -0.1276 0.0419  0.0241  367 ILE C CG2 
7263  C CD1 . ILE C 66  ? 0.4281 0.4462 0.3907 -0.0996 0.0420  0.0201  367 ILE C CD1 
7264  N N   . ASP C 67  ? 0.3937 0.4324 0.3687 -0.1250 0.0331  0.0159  368 ASP C N   
7265  C CA  . ASP C 67  ? 0.4368 0.4949 0.4200 -0.1325 0.0316  0.0153  368 ASP C CA  
7266  C C   . ASP C 67  ? 0.3777 0.4556 0.3760 -0.1208 0.0321  0.0118  368 ASP C C   
7267  O O   . ASP C 67  ? 0.3230 0.4282 0.3335 -0.1222 0.0334  0.0120  368 ASP C O   
7268  C CB  . ASP C 67  ? 0.4433 0.4816 0.4158 -0.1406 0.0268  0.0147  368 ASP C CB  
7269  C CG  . ASP C 67  ? 0.4711 0.4921 0.4284 -0.1550 0.0258  0.0185  368 ASP C CG  
7270  O OD1 . ASP C 67  ? 0.5090 0.5364 0.4649 -0.1605 0.0288  0.0221  368 ASP C OD1 
7271  O OD2 . ASP C 67  ? 0.5014 0.5008 0.4467 -0.1610 0.0219  0.0178  368 ASP C OD2 
7272  N N   . GLN C 68  ? 0.2971 0.3612 0.2943 -0.1090 0.0311  0.0088  369 GLN C N   
7273  C CA  . GLN C 68  ? 0.3768 0.4551 0.3856 -0.0980 0.0311  0.0056  369 GLN C CA  
7274  C C   . GLN C 68  ? 0.3873 0.4855 0.4060 -0.0907 0.0354  0.0057  369 GLN C C   
7275  O O   . GLN C 68  ? 0.4073 0.5276 0.4377 -0.0866 0.0359  0.0045  369 GLN C O   
7276  C CB  . GLN C 68  ? 0.4384 0.4955 0.4418 -0.0885 0.0296  0.0027  369 GLN C CB  
7277  C CG  . GLN C 68  ? 0.5659 0.6319 0.5780 -0.0778 0.0292  -0.0004 369 GLN C CG  
7278  C CD  . GLN C 68  ? 0.5932 0.6404 0.6004 -0.0683 0.0293  -0.0026 369 GLN C CD  
7279  O OE1 . GLN C 68  ? 0.5122 0.5647 0.5250 -0.0584 0.0309  -0.0042 369 GLN C OE1 
7280  N NE2 . GLN C 68  ? 0.5515 0.5766 0.5477 -0.0712 0.0278  -0.0027 369 GLN C NE2 
7281  N N   . TYR C 69  ? 0.3270 0.4175 0.3406 -0.0887 0.0384  0.0071  370 TYR C N   
7282  C CA  . TYR C 69  ? 0.3467 0.4549 0.3678 -0.0826 0.0428  0.0070  370 TYR C CA  
7283  C C   . TYR C 69  ? 0.3806 0.5152 0.4097 -0.0903 0.0450  0.0088  370 TYR C C   
7284  O O   . TYR C 69  ? 0.3623 0.5189 0.4025 -0.0837 0.0475  0.0073  370 TYR C O   
7285  C CB  . TYR C 69  ? 0.3320 0.4265 0.3443 -0.0811 0.0451  0.0085  370 TYR C CB  
7286  C CG  . TYR C 69  ? 0.4306 0.5434 0.4485 -0.0773 0.0499  0.0086  370 TYR C CG  
7287  C CD1 . TYR C 69  ? 0.5035 0.6231 0.5279 -0.0648 0.0514  0.0053  370 TYR C CD1 
7288  C CD2 . TYR C 69  ? 0.3272 0.4499 0.3429 -0.0863 0.0531  0.0119  370 TYR C CD2 
7289  C CE1 . TYR C 69  ? 0.4326 0.5674 0.4608 -0.0606 0.0559  0.0048  370 TYR C CE1 
7290  C CE2 . TYR C 69  ? 0.3457 0.4856 0.3658 -0.0823 0.0581  0.0115  370 TYR C CE2 
7291  C CZ  . TYR C 69  ? 0.4183 0.5637 0.4446 -0.0689 0.0595  0.0077  370 TYR C CZ  
7292  O OH  . TYR C 69  ? 0.4477 0.6083 0.4772 -0.0639 0.0645  0.0067  370 TYR C OH  
7293  N N   . TYR C 70  ? 0.3165 0.4495 0.3399 -0.1043 0.0443  0.0121  371 TYR C N   
7294  C CA  . TYR C 70  ? 0.3355 0.4956 0.3667 -0.1127 0.0470  0.0141  371 TYR C CA  
7295  C C   . TYR C 70  ? 0.3147 0.4957 0.3579 -0.1137 0.0444  0.0128  371 TYR C C   
7296  O O   . TYR C 70  ? 0.3647 0.5750 0.4200 -0.1138 0.0471  0.0130  371 TYR C O   
7297  C CB  . TYR C 70  ? 0.3494 0.5007 0.3695 -0.1286 0.0473  0.0184  371 TYR C CB  
7298  C CG  . TYR C 70  ? 0.3194 0.4669 0.3334 -0.1274 0.0519  0.0204  371 TYR C CG  
7299  C CD1 . TYR C 70  ? 0.3042 0.4235 0.3055 -0.1232 0.0508  0.0208  371 TYR C CD1 
7300  C CD2 . TYR C 70  ? 0.3369 0.5103 0.3582 -0.1292 0.0572  0.0215  371 TYR C CD2 
7301  C CE1 . TYR C 70  ? 0.3980 0.5139 0.3932 -0.1219 0.0545  0.0227  371 TYR C CE1 
7302  C CE2 . TYR C 70  ? 0.3511 0.5208 0.3657 -0.1281 0.0615  0.0231  371 TYR C CE2 
7303  C CZ  . TYR C 70  ? 0.3992 0.5398 0.4005 -0.1246 0.0598  0.0238  371 TYR C CZ  
7304  O OH  . TYR C 70  ? 0.4181 0.5549 0.4120 -0.1236 0.0635  0.0256  371 TYR C OH  
7305  N N   . SER C 71  ? 0.2949 0.4620 0.3348 -0.1140 0.0392  0.0113  372 SER C N   
7306  C CA  . SER C 71  ? 0.4267 0.6124 0.4774 -0.1133 0.0360  0.0099  372 SER C CA  
7307  C C   . SER C 71  ? 0.4604 0.6615 0.5228 -0.0974 0.0376  0.0070  372 SER C C   
7308  O O   . SER C 71  ? 0.5639 0.7926 0.6391 -0.0956 0.0379  0.0068  372 SER C O   
7309  C CB  . SER C 71  ? 0.4204 0.5847 0.4627 -0.1164 0.0303  0.0086  372 SER C CB  
7310  O OG  . SER C 71  ? 0.6169 0.7989 0.6680 -0.1179 0.0265  0.0078  372 SER C OG  
7311  N N   . SER C 72  ? 0.3814 0.5649 0.4392 -0.0858 0.0388  0.0049  373 SER C N   
7312  C CA  . SER C 72  ? 0.3835 0.5764 0.4496 -0.0709 0.0399  0.0021  373 SER C CA  
7313  C C   . SER C 72  ? 0.4782 0.6967 0.5539 -0.0668 0.0449  0.0022  373 SER C C   
7314  O O   . SER C 72  ? 0.5439 0.7794 0.6295 -0.0570 0.0450  0.0004  373 SER C O   
7315  C CB  . SER C 72  ? 0.3795 0.5482 0.4374 -0.0616 0.0405  0.0001  373 SER C CB  
7316  O OG  . SER C 72  ? 0.4627 0.6297 0.5173 -0.0604 0.0451  0.0009  373 SER C OG  
7317  N N   . ILE C 73  ? 0.4583 0.6793 0.5305 -0.0738 0.0490  0.0044  374 ILE C N   
7318  C CA  . ILE C 73  ? 0.4551 0.7006 0.5351 -0.0711 0.0546  0.0046  374 ILE C CA  
7319  C C   . ILE C 73  ? 0.4900 0.7628 0.5787 -0.0827 0.0552  0.0071  374 ILE C C   
7320  O O   . ILE C 73  ? 0.4438 0.7369 0.5373 -0.0848 0.0606  0.0081  374 ILE C O   
7321  C CB  . ILE C 73  ? 0.4477 0.6815 0.5184 -0.0712 0.0593  0.0054  374 ILE C CB  
7322  C CG1 . ILE C 73  ? 0.4573 0.6788 0.5176 -0.0868 0.0589  0.0093  374 ILE C CG1 
7323  C CG2 . ILE C 73  ? 0.3547 0.5644 0.4181 -0.0599 0.0583  0.0028  374 ILE C CG2 
7324  C CD1 . ILE C 73  ? 0.4085 0.6227 0.4596 -0.0887 0.0636  0.0110  374 ILE C CD1 
7325  N N   . LYS C 74  ? 0.5180 0.7920 0.6084 -0.0908 0.0499  0.0081  375 LYS C N   
7326  C CA  . LYS C 74  ? 0.5306 0.8316 0.6299 -0.1029 0.0492  0.0105  375 LYS C CA  
7327  C C   . LYS C 74  ? 0.4876 0.7937 0.5821 -0.1164 0.0539  0.0139  375 LYS C C   
7328  O O   . LYS C 74  ? 0.5494 0.8859 0.6541 -0.1210 0.0576  0.0153  375 LYS C O   
7329  C CB  . LYS C 74  ? 0.6017 0.9365 0.7184 -0.0930 0.0502  0.0088  375 LYS C CB  
7330  C CG  . LYS C 74  ? 0.6735 1.0035 0.7942 -0.0805 0.0450  0.0060  375 LYS C CG  
7331  C CD  . LYS C 74  ? 0.8151 1.1384 0.9333 -0.0904 0.0377  0.0070  375 LYS C CD  
7332  C CE  . LYS C 74  ? 0.8045 1.1211 0.9247 -0.0782 0.0326  0.0045  375 LYS C CE  
7333  N NZ  . LYS C 74  ? 0.7875 1.0731 0.8968 -0.0679 0.0332  0.0022  375 LYS C NZ  
7334  N N   . ARG C 75  ? 0.4309 0.7068 0.5094 -0.1226 0.0536  0.0155  376 ARG C N   
7335  C CA  . ARG C 75  ? 0.4568 0.7308 0.5269 -0.1366 0.0570  0.0194  376 ARG C CA  
7336  C C   . ARG C 75  ? 0.4202 0.6671 0.4755 -0.1507 0.0523  0.0219  376 ARG C C   
7337  O O   . ARG C 75  ? 0.4074 0.6385 0.4498 -0.1599 0.0540  0.0250  376 ARG C O   
7338  C CB  . ARG C 75  ? 0.4544 0.7175 0.5173 -0.1294 0.0623  0.0192  376 ARG C CB  
7339  C CG  . ARG C 75  ? 0.4513 0.7401 0.5258 -0.1174 0.0681  0.0168  376 ARG C CG  
7340  C CD  . ARG C 75  ? 0.5228 0.8439 0.6053 -0.1272 0.0733  0.0193  376 ARG C CD  
7341  N NE  . ARG C 75  ? 0.5736 0.9160 0.6646 -0.1148 0.0798  0.0167  376 ARG C NE  
7342  C CZ  . ARG C 75  ? 0.5510 0.9154 0.6567 -0.1018 0.0802  0.0132  376 ARG C CZ  
7343  N NH1 . ARG C 75  ? 0.4584 0.8392 0.5695 -0.0903 0.0864  0.0107  376 ARG C NH1 
7344  N NH2 . ARG C 75  ? 0.5213 0.8904 0.6352 -0.1000 0.0742  0.0123  376 ARG C NH2 
7345  N N   . PHE C 76  ? 0.3992 0.6388 0.4548 -0.1523 0.0462  0.0206  377 PHE C N   
7346  C CA  . PHE C 76  ? 0.3974 0.6091 0.4376 -0.1646 0.0415  0.0223  377 PHE C CA  
7347  C C   . PHE C 76  ? 0.4527 0.6741 0.4891 -0.1846 0.0422  0.0267  377 PHE C C   
7348  O O   . PHE C 76  ? 0.4807 0.7344 0.5300 -0.1912 0.0429  0.0276  377 PHE C O   
7349  C CB  . PHE C 76  ? 0.3789 0.5845 0.4207 -0.1627 0.0352  0.0197  377 PHE C CB  
7350  C CG  . PHE C 76  ? 0.4169 0.5887 0.4409 -0.1719 0.0306  0.0203  377 PHE C CG  
7351  C CD1 . PHE C 76  ? 0.3906 0.5315 0.4042 -0.1622 0.0293  0.0182  377 PHE C CD1 
7352  C CD2 . PHE C 76  ? 0.4646 0.6357 0.4822 -0.1902 0.0276  0.0229  377 PHE C CD2 
7353  C CE1 . PHE C 76  ? 0.4795 0.5893 0.4766 -0.1691 0.0254  0.0183  377 PHE C CE1 
7354  C CE2 . PHE C 76  ? 0.5269 0.6645 0.5265 -0.1980 0.0233  0.0230  377 PHE C CE2 
7355  C CZ  . PHE C 76  ? 0.4692 0.5762 0.4586 -0.1868 0.0224  0.0206  377 PHE C CZ  
7356  N N   . GLY C 77  ? 0.4383 0.6315 0.4567 -0.1944 0.0418  0.0295  378 GLY C N   
7357  C CA  . GLY C 77  ? 0.5101 0.7077 0.5217 -0.2146 0.0425  0.0341  378 GLY C CA  
7358  C C   . GLY C 77  ? 0.4916 0.7115 0.5079 -0.2178 0.0496  0.0369  378 GLY C C   
7359  O O   . GLY C 77  ? 0.5849 0.8086 0.5945 -0.2353 0.0509  0.0412  378 GLY C O   
7360  N N   . SER C 78  ? 0.4841 0.7181 0.5106 -0.2019 0.0543  0.0346  379 SER C N   
7361  C CA  . SER C 78  ? 0.5005 0.7572 0.5315 -0.2037 0.0616  0.0366  379 SER C CA  
7362  C C   . SER C 78  ? 0.5604 0.7908 0.5717 -0.2120 0.0635  0.0407  379 SER C C   
7363  O O   . SER C 78  ? 0.4998 0.6937 0.4949 -0.2125 0.0594  0.0414  379 SER C O   
7364  C CB  . SER C 78  ? 0.3957 0.6681 0.4392 -0.1837 0.0658  0.0326  379 SER C CB  
7365  O OG  . SER C 78  ? 0.3902 0.6321 0.4245 -0.1707 0.0640  0.0304  379 SER C OG  
7366  N N   . LYS C 79  ? 0.5446 0.7946 0.5572 -0.2181 0.0701  0.0434  380 LYS C N   
7367  C CA  . LYS C 79  ? 0.5292 0.7565 0.5231 -0.2250 0.0724  0.0475  380 LYS C CA  
7368  C C   . LYS C 79  ? 0.4753 0.6745 0.4608 -0.2086 0.0714  0.0454  380 LYS C C   
7369  O O   . LYS C 79  ? 0.4800 0.6447 0.4473 -0.2117 0.0681  0.0478  380 LYS C O   
7370  C CB  . LYS C 79  ? 0.6597 0.9167 0.6583 -0.2316 0.0805  0.0500  380 LYS C CB  
7371  C CG  . LYS C 79  ? 0.8271 1.0631 0.8052 -0.2420 0.0831  0.0553  380 LYS C CG  
7372  C CD  . LYS C 79  ? 0.9629 1.2233 0.9458 -0.2382 0.0906  0.0551  380 LYS C CD  
7373  C CE  . LYS C 79  ? 0.9930 1.2819 0.9849 -0.2471 0.0918  0.0556  380 LYS C CE  
7374  N NZ  . LYS C 79  ? 1.0324 1.3022 1.0061 -0.2649 0.0892  0.0608  380 LYS C NZ  
7375  N N   . ALA C 80  ? 0.3551 0.5685 0.3535 -0.1909 0.0738  0.0407  381 ALA C N   
7376  C CA  . ALA C 80  ? 0.4428 0.6324 0.4345 -0.1756 0.0727  0.0384  381 ALA C CA  
7377  C C   . ALA C 80  ? 0.4848 0.6435 0.4692 -0.1721 0.0654  0.0372  381 ALA C C   
7378  O O   . ALA C 80  ? 0.5391 0.6689 0.5106 -0.1674 0.0632  0.0378  381 ALA C O   
7379  C CB  . ALA C 80  ? 0.4469 0.6578 0.4538 -0.1583 0.0762  0.0333  381 ALA C CB  
7380  N N   . HIS C 81  ? 0.3878 0.5531 0.3806 -0.1739 0.0616  0.0352  382 HIS C N   
7381  C CA  . HIS C 81  ? 0.3661 0.5030 0.3514 -0.1713 0.0551  0.0338  382 HIS C CA  
7382  C C   . HIS C 81  ? 0.4105 0.5161 0.3753 -0.1836 0.0522  0.0380  382 HIS C C   
7383  O O   . HIS C 81  ? 0.4091 0.4849 0.3625 -0.1770 0.0493  0.0377  382 HIS C O   
7384  C CB  . HIS C 81  ? 0.3417 0.4931 0.3381 -0.1738 0.0517  0.0315  382 HIS C CB  
7385  C CG  . HIS C 81  ? 0.3442 0.4689 0.3336 -0.1707 0.0455  0.0293  382 HIS C CG  
7386  N ND1 . HIS C 81  ? 0.3753 0.5058 0.3697 -0.1752 0.0414  0.0277  382 HIS C ND1 
7387  C CD2 . HIS C 81  ? 0.3687 0.4618 0.3464 -0.1631 0.0431  0.0283  382 HIS C CD2 
7388  C CE1 . HIS C 81  ? 0.3471 0.4498 0.3324 -0.1706 0.0369  0.0257  382 HIS C CE1 
7389  N NE2 . HIS C 81  ? 0.3937 0.4743 0.3696 -0.1629 0.0380  0.0259  382 HIS C NE2 
7390  N N   . MET C 82  ? 0.3967 0.5089 0.3564 -0.2015 0.0530  0.0422  383 MET C N   
7391  C CA  . MET C 82  ? 0.4648 0.5454 0.4032 -0.2143 0.0499  0.0465  383 MET C CA  
7392  C C   . MET C 82  ? 0.4965 0.5574 0.4213 -0.2104 0.0518  0.0494  383 MET C C   
7393  O O   . MET C 82  ? 0.5253 0.5516 0.4334 -0.2095 0.0478  0.0508  383 MET C O   
7394  C CB  . MET C 82  ? 0.4648 0.5588 0.4007 -0.2356 0.0506  0.0505  383 MET C CB  
7395  C CG  . MET C 82  ? 0.5843 0.6931 0.5305 -0.2418 0.0470  0.0482  383 MET C CG  
7396  S SD  . MET C 82  ? 0.7217 0.7924 0.6553 -0.2396 0.0388  0.0455  383 MET C SD  
7397  C CE  . MET C 82  ? 0.6696 0.7563 0.6231 -0.2179 0.0384  0.0388  383 MET C CE  
7398  N N   . GLU C 83  ? 0.4817 0.5638 0.4128 -0.2073 0.0577  0.0502  384 GLU C N   
7399  C CA  . GLU C 83  ? 0.5706 0.6347 0.4881 -0.2039 0.0592  0.0530  384 GLU C CA  
7400  C C   . GLU C 83  ? 0.5151 0.5601 0.4319 -0.1857 0.0563  0.0495  384 GLU C C   
7401  O O   . GLU C 83  ? 0.5999 0.6166 0.5012 -0.1835 0.0537  0.0520  384 GLU C O   
7402  C CB  . GLU C 83  ? 0.5768 0.6690 0.5007 -0.2050 0.0666  0.0542  384 GLU C CB  
7403  C CG  . GLU C 83  ? 0.7469 0.8419 0.6595 -0.2247 0.0693  0.0603  384 GLU C CG  
7404  C CD  . GLU C 83  ? 0.8379 0.9723 0.7631 -0.2287 0.0772  0.0604  384 GLU C CD  
7405  O OE1 . GLU C 83  ? 0.8754 1.0287 0.8131 -0.2144 0.0811  0.0563  384 GLU C OE1 
7406  O OE2 . GLU C 83  ? 0.8939 1.0403 0.8161 -0.2466 0.0795  0.0645  384 GLU C OE2 
7407  N N   . ARG C 84  ? 0.4703 0.5306 0.4036 -0.1726 0.0564  0.0440  385 ARG C N   
7408  C CA  . ARG C 84  ? 0.4383 0.4817 0.3717 -0.1566 0.0535  0.0406  385 ARG C CA  
7409  C C   . ARG C 84  ? 0.4507 0.4620 0.3719 -0.1579 0.0474  0.0411  385 ARG C C   
7410  O O   . ARG C 84  ? 0.4529 0.4405 0.3643 -0.1503 0.0449  0.0416  385 ARG C O   
7411  C CB  . ARG C 84  ? 0.3896 0.4544 0.3417 -0.1445 0.0546  0.0349  385 ARG C CB  
7412  C CG  . ARG C 84  ? 0.3776 0.4282 0.3308 -0.1287 0.0522  0.0313  385 ARG C CG  
7413  C CD  . ARG C 84  ? 0.3762 0.4169 0.3212 -0.1229 0.0536  0.0329  385 ARG C CD  
7414  N NE  . ARG C 84  ? 0.3740 0.4027 0.3208 -0.1088 0.0509  0.0295  385 ARG C NE  
7415  C CZ  . ARG C 84  ? 0.4471 0.4574 0.3843 -0.1035 0.0491  0.0308  385 ARG C CZ  
7416  N NH1 . ARG C 84  ? 0.5245 0.5242 0.4483 -0.1106 0.0494  0.0357  385 ARG C NH1 
7417  N NH2 . ARG C 84  ? 0.3730 0.3757 0.3138 -0.0914 0.0468  0.0276  385 ARG C NH2 
7418  N N   . LEU C 85  ? 0.4785 0.4891 0.3998 -0.1673 0.0449  0.0409  386 LEU C N   
7419  C CA  . LEU C 85  ? 0.5060 0.4854 0.4143 -0.1692 0.0394  0.0410  386 LEU C CA  
7420  C C   . LEU C 85  ? 0.6255 0.5764 0.5127 -0.1761 0.0377  0.0462  386 LEU C C   
7421  O O   . LEU C 85  ? 0.5970 0.5195 0.4731 -0.1689 0.0340  0.0461  386 LEU C O   
7422  C CB  . LEU C 85  ? 0.5864 0.5717 0.4970 -0.1808 0.0372  0.0402  386 LEU C CB  
7423  C CG  . LEU C 85  ? 0.6138 0.5896 0.5271 -0.1753 0.0330  0.0357  386 LEU C CG  
7424  C CD1 . LEU C 85  ? 0.5132 0.4888 0.4353 -0.1564 0.0332  0.0313  386 LEU C CD1 
7425  C CD2 . LEU C 85  ? 0.6130 0.6150 0.5387 -0.1834 0.0331  0.0342  386 LEU C CD2 
7426  N N   . GLU C 86  ? 0.6334 0.5918 0.5145 -0.1899 0.0405  0.0511  387 GLU C N   
7427  C CA  . GLU C 86  ? 0.6822 0.6129 0.5417 -0.1972 0.0389  0.0567  387 GLU C CA  
7428  C C   . GLU C 86  ? 0.6329 0.5536 0.4888 -0.1835 0.0391  0.0572  387 GLU C C   
7429  O O   . GLU C 86  ? 0.5561 0.4457 0.3964 -0.1797 0.0349  0.0592  387 GLU C O   
7430  C CB  . GLU C 86  ? 0.7773 0.7215 0.6319 -0.2154 0.0425  0.0619  387 GLU C CB  
7431  C CG  . GLU C 86  ? 1.0598 0.9710 0.8891 -0.2274 0.0396  0.0680  387 GLU C CG  
7432  C CD  . GLU C 86  ? 1.2630 1.1377 1.0790 -0.2241 0.0329  0.0668  387 GLU C CD  
7433  O OE1 . GLU C 86  ? 1.2903 1.1638 1.1078 -0.2312 0.0306  0.0646  387 GLU C OE1 
7434  O OE2 . GLU C 86  ? 1.3065 1.1540 1.1105 -0.2141 0.0298  0.0679  387 GLU C OE2 
7435  N N   . GLU C 87  ? 0.5877 0.5342 0.4575 -0.1754 0.0435  0.0552  388 GLU C N   
7436  C CA  . GLU C 87  ? 0.5685 0.5078 0.4355 -0.1628 0.0435  0.0553  388 GLU C CA  
7437  C C   . GLU C 87  ? 0.5707 0.4909 0.4383 -0.1483 0.0387  0.0518  388 GLU C C   
7438  O O   . GLU C 87  ? 0.5384 0.4368 0.3946 -0.1420 0.0357  0.0539  388 GLU C O   
7439  C CB  . GLU C 87  ? 0.5611 0.5322 0.4437 -0.1566 0.0492  0.0525  388 GLU C CB  
7440  C CG  . GLU C 87  ? 0.6415 0.6081 0.5221 -0.1444 0.0493  0.0521  388 GLU C CG  
7441  C CD  . GLU C 87  ? 0.7674 0.7635 0.6624 -0.1379 0.0548  0.0486  388 GLU C CD  
7442  O OE1 . GLU C 87  ? 0.7770 0.7936 0.6879 -0.1348 0.0567  0.0442  388 GLU C OE1 
7443  O OE2 . GLU C 87  ? 0.8723 0.8701 0.7617 -0.1358 0.0570  0.0502  388 GLU C OE2 
7444  N N   . VAL C 88  ? 0.4350 0.3638 0.3156 -0.1428 0.0380  0.0466  389 VAL C N   
7445  C CA  . VAL C 88  ? 0.4811 0.3946 0.3633 -0.1293 0.0342  0.0429  389 VAL C CA  
7446  C C   . VAL C 88  ? 0.5629 0.4423 0.4270 -0.1320 0.0293  0.0454  389 VAL C C   
7447  O O   . VAL C 88  ? 0.5950 0.4559 0.4530 -0.1215 0.0263  0.0454  389 VAL C O   
7448  C CB  . VAL C 88  ? 0.4903 0.4192 0.3883 -0.1249 0.0346  0.0372  389 VAL C CB  
7449  C CG1 . VAL C 88  ? 0.4965 0.4055 0.3923 -0.1146 0.0306  0.0340  389 VAL C CG1 
7450  C CG2 . VAL C 88  ? 0.4827 0.4400 0.3977 -0.1168 0.0385  0.0340  389 VAL C CG2 
7451  N N   . ASN C 89  ? 0.5963 0.4669 0.4513 -0.1459 0.0282  0.0475  390 ASN C N   
7452  C CA  . ASN C 89  ? 0.5792 0.4146 0.4149 -0.1490 0.0235  0.0497  390 ASN C CA  
7453  C C   . ASN C 89  ? 0.6083 0.4231 0.4270 -0.1492 0.0218  0.0554  390 ASN C C   
7454  O O   . ASN C 89  ? 0.6164 0.4030 0.4228 -0.1418 0.0176  0.0561  390 ASN C O   
7455  C CB  . ASN C 89  ? 0.6282 0.4590 0.4566 -0.1658 0.0226  0.0509  390 ASN C CB  
7456  C CG  . ASN C 89  ? 0.8266 0.6727 0.6691 -0.1648 0.0227  0.0452  390 ASN C CG  
7457  O OD1 . ASN C 89  ? 0.8083 0.6548 0.6596 -0.1511 0.0219  0.0403  390 ASN C OD1 
7458  N ND2 . ASN C 89  ? 0.8714 0.7308 0.7159 -0.1800 0.0236  0.0461  390 ASN C ND2 
7459  N N   . LYS C 90  ? 0.5739 0.4027 0.3917 -0.1568 0.0252  0.0595  391 LYS C N   
7460  C CA  . LYS C 90  ? 0.7342 0.5460 0.5364 -0.1564 0.0238  0.0651  391 LYS C CA  
7461  C C   . LYS C 90  ? 0.7032 0.5099 0.5092 -0.1381 0.0216  0.0631  391 LYS C C   
7462  O O   . LYS C 90  ? 0.7576 0.5376 0.5488 -0.1329 0.0171  0.0662  391 LYS C O   
7463  C CB  . LYS C 90  ? 0.8073 0.6407 0.6107 -0.1663 0.0289  0.0687  391 LYS C CB  
7464  C CG  . LYS C 90  ? 1.0078 0.8418 0.8018 -0.1868 0.0307  0.0730  391 LYS C CG  
7465  C CD  . LYS C 90  ? 1.0914 0.9537 0.8908 -0.1948 0.0370  0.0753  391 LYS C CD  
7466  C CE  . LYS C 90  ? 1.1611 1.0301 0.9547 -0.2159 0.0395  0.0790  391 LYS C CE  
7467  N NZ  . LYS C 90  ? 1.1532 1.0615 0.9618 -0.2214 0.0468  0.0783  391 LYS C NZ  
7468  N N   . GLU C 91  ? 0.5555 0.3882 0.3812 -0.1283 0.0245  0.0583  392 GLU C N   
7469  C CA  . GLU C 91  ? 0.5468 0.3780 0.3777 -0.1119 0.0225  0.0561  392 GLU C CA  
7470  C C   . GLU C 91  ? 0.5888 0.3982 0.4166 -0.1021 0.0177  0.0537  392 GLU C C   
7471  O O   . GLU C 91  ? 0.6796 0.4725 0.5002 -0.0925 0.0139  0.0553  392 GLU C O   
7472  C CB  . GLU C 91  ? 0.5625 0.4244 0.4142 -0.1048 0.0265  0.0510  392 GLU C CB  
7473  C CG  . GLU C 91  ? 0.6388 0.5176 0.4921 -0.1063 0.0300  0.0529  392 GLU C CG  
7474  C CD  . GLU C 91  ? 0.7168 0.6226 0.5887 -0.0987 0.0337  0.0475  392 GLU C CD  
7475  O OE1 . GLU C 91  ? 0.7984 0.7040 0.6773 -0.0863 0.0317  0.0442  392 GLU C OE1 
7476  O OE2 . GLU C 91  ? 0.8502 0.7776 0.7296 -0.1051 0.0386  0.0466  392 GLU C OE2 
7477  N N   . ILE C 92  ? 0.6114 0.4217 0.4451 -0.1038 0.0180  0.0496  393 ILE C N   
7478  C CA  . ILE C 92  ? 0.6783 0.4671 0.5076 -0.0950 0.0141  0.0470  393 ILE C CA  
7479  C C   . ILE C 92  ? 0.7453 0.5001 0.5518 -0.0982 0.0098  0.0520  393 ILE C C   
7480  O O   . ILE C 92  ? 0.7808 0.5170 0.5810 -0.0864 0.0060  0.0521  393 ILE C O   
7481  C CB  . ILE C 92  ? 0.5641 0.3586 0.4009 -0.0986 0.0152  0.0421  393 ILE C CB  
7482  C CG1 . ILE C 92  ? 0.5593 0.3855 0.4180 -0.0934 0.0190  0.0373  393 ILE C CG1 
7483  C CG2 . ILE C 92  ? 0.5792 0.3485 0.4082 -0.0906 0.0116  0.0394  393 ILE C CG2 
7484  C CD1 . ILE C 92  ? 0.5258 0.3613 0.3921 -0.0985 0.0201  0.0333  393 ILE C CD1 
7485  N N   . ASP C 93  ? 0.7569 0.5031 0.5502 -0.1141 0.0101  0.0564  394 ASP C N   
7486  C CA  . ASP C 93  ? 0.8501 0.5611 0.6191 -0.1188 0.0058  0.0615  394 ASP C CA  
7487  C C   . ASP C 93  ? 0.8233 0.5229 0.5837 -0.1099 0.0029  0.0660  394 ASP C C   
7488  O O   . ASP C 93  ? 0.8900 0.5606 0.6361 -0.1023 -0.0019 0.0676  394 ASP C O   
7489  C CB  . ASP C 93  ? 1.0164 0.7246 0.7737 -0.1394 0.0072  0.0660  394 ASP C CB  
7490  C CG  . ASP C 93  ? 1.1756 0.8491 0.9119 -0.1472 0.0033  0.0676  394 ASP C CG  
7491  O OD1 . ASP C 93  ? 1.2422 0.9184 0.9816 -0.1546 0.0040  0.0641  394 ASP C OD1 
7492  O OD2 . ASP C 93  ? 1.2512 0.8937 0.9670 -0.1458 -0.0008 0.0722  394 ASP C OD2 
7493  N N   . THR C 94  ? 0.7533 0.4750 0.5215 -0.1103 0.0057  0.0678  395 THR C N   
7494  C CA  . THR C 94  ? 0.8268 0.5384 0.5854 -0.1038 0.0027  0.0726  395 THR C CA  
7495  C C   . THR C 94  ? 0.8847 0.6048 0.6563 -0.0852 0.0008  0.0690  395 THR C C   
7496  O O   . THR C 94  ? 0.9678 0.6694 0.7295 -0.0757 -0.0042 0.0719  395 THR C O   
7497  C CB  . THR C 94  ? 0.9239 0.6532 0.6817 -0.1141 0.0064  0.0767  395 THR C CB  
7498  O OG1 . THR C 94  ? 0.9289 0.6931 0.7088 -0.1116 0.0116  0.0717  395 THR C OG1 
7499  C CG2 . THR C 94  ? 0.9852 0.7064 0.7289 -0.1336 0.0083  0.0812  395 THR C CG2 
7500  N N   . THR C 95  ? 0.8267 0.5744 0.6200 -0.0798 0.0044  0.0630  396 THR C N   
7501  C CA  . THR C 95  ? 0.7341 0.4935 0.5403 -0.0643 0.0032  0.0598  396 THR C CA  
7502  C C   . THR C 95  ? 0.7199 0.4788 0.5368 -0.0535 0.0024  0.0537  396 THR C C   
7503  O O   . THR C 95  ? 0.7636 0.5315 0.5911 -0.0408 0.0012  0.0511  396 THR C O   
7504  C CB  . THR C 95  ? 0.6791 0.4701 0.5008 -0.0653 0.0078  0.0576  396 THR C CB  
7505  O OG1 . THR C 95  ? 0.6933 0.5032 0.5306 -0.0674 0.0120  0.0520  396 THR C OG1 
7506  C CG2 . THR C 95  ? 0.5988 0.3940 0.4110 -0.0775 0.0101  0.0628  396 THR C CG2 
7507  N N   . SER C 96  ? 0.6874 0.4366 0.5015 -0.0587 0.0031  0.0514  397 SER C N   
7508  C CA  . SER C 96  ? 0.6988 0.4476 0.5218 -0.0503 0.0032  0.0454  397 SER C CA  
7509  C C   . SER C 96  ? 0.6803 0.4595 0.5250 -0.0472 0.0073  0.0399  397 SER C C   
7510  O O   . SER C 96  ? 0.6918 0.4742 0.5456 -0.0386 0.0075  0.0349  397 SER C O   
7511  C CB  . SER C 96  ? 0.8085 0.5406 0.6276 -0.0350 -0.0011 0.0449  397 SER C CB  
7512  O OG  . SER C 96  ? 0.9271 0.6268 0.7246 -0.0369 -0.0052 0.0491  397 SER C OG  
7513  N N   . THR C 97  ? 0.6400 0.4409 0.4922 -0.0538 0.0106  0.0408  398 THR C N   
7514  C CA  . THR C 97  ? 0.5431 0.3713 0.4141 -0.0515 0.0145  0.0359  398 THR C CA  
7515  C C   . THR C 97  ? 0.4991 0.3443 0.3723 -0.0630 0.0183  0.0378  398 THR C C   
7516  O O   . THR C 97  ? 0.5179 0.3540 0.3785 -0.0731 0.0181  0.0426  398 THR C O   
7517  C CB  . THR C 97  ? 0.5347 0.3738 0.4158 -0.0390 0.0137  0.0340  398 THR C CB  
7518  O OG1 . THR C 97  ? 0.6053 0.4674 0.5030 -0.0369 0.0172  0.0291  398 THR C OG1 
7519  C CG2 . THR C 97  ? 0.4477 0.2896 0.3236 -0.0397 0.0129  0.0384  398 THR C CG2 
7520  N N   . TYR C 98  ? 0.4530 0.3228 0.3416 -0.0614 0.0219  0.0341  399 TYR C N   
7521  C CA  . TYR C 98  ? 0.5380 0.4261 0.4296 -0.0699 0.0259  0.0355  399 TYR C CA  
7522  C C   . TYR C 98  ? 0.4770 0.3872 0.3830 -0.0625 0.0285  0.0317  399 TYR C C   
7523  O O   . TYR C 98  ? 0.4551 0.3665 0.3687 -0.0523 0.0272  0.0282  399 TYR C O   
7524  C CB  . TYR C 98  ? 0.5086 0.4027 0.4015 -0.0813 0.0280  0.0351  399 TYR C CB  
7525  C CG  . TYR C 98  ? 0.4761 0.3822 0.3825 -0.0780 0.0291  0.0297  399 TYR C CG  
7526  C CD1 . TYR C 98  ? 0.4346 0.3661 0.3540 -0.0797 0.0329  0.0273  399 TYR C CD1 
7527  C CD2 . TYR C 98  ? 0.4527 0.3444 0.3579 -0.0730 0.0263  0.0270  399 TYR C CD2 
7528  C CE1 . TYR C 98  ? 0.4628 0.4042 0.3934 -0.0766 0.0334  0.0228  399 TYR C CE1 
7529  C CE2 . TYR C 98  ? 0.4405 0.3425 0.3566 -0.0705 0.0272  0.0223  399 TYR C CE2 
7530  C CZ  . TYR C 98  ? 0.4406 0.3672 0.3692 -0.0725 0.0304  0.0204  399 TYR C CZ  
7531  O OH  . TYR C 98  ? 0.4727 0.4086 0.4111 -0.0698 0.0308  0.0162  399 TYR C OH  
7532  N N   . GLN C 99  ? 0.3639 0.2913 0.2729 -0.0677 0.0324  0.0324  400 GLN C N   
7533  C CA  . GLN C 99  ? 0.4494 0.3961 0.3697 -0.0614 0.0351  0.0289  400 GLN C CA  
7534  C C   . GLN C 99  ? 0.4291 0.3960 0.3604 -0.0652 0.0393  0.0260  400 GLN C C   
7535  O O   . GLN C 99  ? 0.4209 0.3940 0.3496 -0.0750 0.0417  0.0283  400 GLN C O   
7536  C CB  . GLN C 99  ? 0.4861 0.4361 0.3999 -0.0621 0.0363  0.0317  400 GLN C CB  
7537  C CG  . GLN C 99  ? 0.5387 0.4711 0.4425 -0.0572 0.0317  0.0346  400 GLN C CG  
7538  C CD  . GLN C 99  ? 0.5879 0.5193 0.4998 -0.0457 0.0288  0.0309  400 GLN C CD  
7539  O OE1 . GLN C 99  ? 0.6005 0.5464 0.5228 -0.0407 0.0308  0.0268  400 GLN C OE1 
7540  N NE2 . GLN C 99  ? 0.5465 0.4605 0.4532 -0.0413 0.0242  0.0324  400 GLN C NE2 
7541  N N   . LEU C 100 ? 0.3653 0.3428 0.3084 -0.0575 0.0400  0.0212  401 LEU C N   
7542  C CA  . LEU C 100 ? 0.3249 0.3223 0.2787 -0.0590 0.0436  0.0184  401 LEU C CA  
7543  C C   . LEU C 100 ? 0.3759 0.3892 0.3309 -0.0598 0.0478  0.0186  401 LEU C C   
7544  O O   . LEU C 100 ? 0.3679 0.3795 0.3197 -0.0547 0.0479  0.0185  401 LEU C O   
7545  C CB  . LEU C 100 ? 0.2888 0.2908 0.2530 -0.0501 0.0428  0.0136  401 LEU C CB  
7546  C CG  . LEU C 100 ? 0.3824 0.3713 0.3463 -0.0491 0.0395  0.0126  401 LEU C CG  
7547  C CD1 . LEU C 100 ? 0.3384 0.3315 0.3113 -0.0403 0.0391  0.0081  401 LEU C CD1 
7548  C CD2 . LEU C 100 ? 0.3249 0.3166 0.2888 -0.0582 0.0398  0.0135  401 LEU C CD2 
7549  N N   . LYS C 101 ? 0.3618 0.3915 0.3215 -0.0660 0.0514  0.0188  402 LYS C N   
7550  C CA  . LYS C 101 ? 0.3241 0.3730 0.2884 -0.0641 0.0563  0.0173  402 LYS C CA  
7551  C C   . LYS C 101 ? 0.3582 0.4138 0.3318 -0.0530 0.0565  0.0121  402 LYS C C   
7552  O O   . LYS C 101 ? 0.3601 0.4112 0.3392 -0.0489 0.0537  0.0099  402 LYS C O   
7553  C CB  . LYS C 101 ? 0.3524 0.4200 0.3218 -0.0724 0.0600  0.0182  402 LYS C CB  
7554  C CG  . LYS C 101 ? 0.4607 0.5217 0.4201 -0.0853 0.0600  0.0236  402 LYS C CG  
7555  C CD  . LYS C 101 ? 0.5584 0.6113 0.5054 -0.0868 0.0612  0.0267  402 LYS C CD  
7556  C CE  . LYS C 101 ? 0.7046 0.7485 0.6393 -0.1002 0.0610  0.0326  402 LYS C CE  
7557  N NZ  . LYS C 101 ? 0.7639 0.8300 0.7037 -0.1101 0.0659  0.0337  402 LYS C NZ  
7558  N N   . ASP C 102 ? 0.3620 0.4279 0.3364 -0.0484 0.0600  0.0102  403 ASP C N   
7559  C CA  . ASP C 102 ? 0.3576 0.4277 0.3384 -0.0381 0.0603  0.0054  403 ASP C CA  
7560  C C   . ASP C 102 ? 0.3644 0.4463 0.3566 -0.0359 0.0606  0.0028  403 ASP C C   
7561  O O   . ASP C 102 ? 0.3178 0.3951 0.3144 -0.0294 0.0583  -0.0001 403 ASP C O   
7562  C CB  . ASP C 102 ? 0.3938 0.4731 0.3720 -0.0344 0.0645  0.0036  403 ASP C CB  
7563  C CG  . ASP C 102 ? 0.6128 0.6802 0.5790 -0.0357 0.0636  0.0058  403 ASP C CG  
7564  O OD1 . ASP C 102 ? 0.6078 0.6599 0.5684 -0.0382 0.0593  0.0087  403 ASP C OD1 
7565  O OD2 . ASP C 102 ? 0.6632 0.7367 0.6250 -0.0338 0.0671  0.0045  403 ASP C OD2 
7566  N N   . THR C 103 ? 0.3195 0.4176 0.3165 -0.0413 0.0636  0.0039  404 THR C N   
7567  C CA  . THR C 103 ? 0.3195 0.4303 0.3274 -0.0397 0.0634  0.0019  404 THR C CA  
7568  C C   . THR C 103 ? 0.3411 0.4390 0.3496 -0.0417 0.0584  0.0024  404 THR C C   
7569  O O   . THR C 103 ? 0.3558 0.4552 0.3707 -0.0362 0.0566  -0.0003 404 THR C O   
7570  C CB  . THR C 103 ? 0.3225 0.4534 0.3351 -0.0474 0.0668  0.0039  404 THR C CB  
7571  O OG1 . THR C 103 ? 0.3721 0.4942 0.3761 -0.0588 0.0661  0.0084  404 THR C OG1 
7572  C CG2 . THR C 103 ? 0.3226 0.4698 0.3366 -0.0434 0.0726  0.0023  404 THR C CG2 
7573  N N   . GLU C 104 ? 0.3260 0.4102 0.3267 -0.0495 0.0562  0.0058  405 GLU C N   
7574  C CA  . GLU C 104 ? 0.3508 0.4212 0.3504 -0.0513 0.0518  0.0059  405 GLU C CA  
7575  C C   . GLU C 104 ? 0.3809 0.4381 0.3798 -0.0422 0.0493  0.0033  405 GLU C C   
7576  O O   . GLU C 104 ? 0.3415 0.3945 0.3438 -0.0396 0.0469  0.0014  405 GLU C O   
7577  C CB  . GLU C 104 ? 0.3714 0.4276 0.3607 -0.0609 0.0501  0.0101  405 GLU C CB  
7578  C CG  . GLU C 104 ? 0.3441 0.4118 0.3327 -0.0723 0.0522  0.0132  405 GLU C CG  
7579  C CD  . GLU C 104 ? 0.3844 0.4352 0.3596 -0.0814 0.0510  0.0178  405 GLU C CD  
7580  O OE1 . GLU C 104 ? 0.3509 0.4080 0.3235 -0.0926 0.0523  0.0208  405 GLU C OE1 
7581  O OE2 . GLU C 104 ? 0.3978 0.4291 0.3649 -0.0774 0.0485  0.0184  405 GLU C OE2 
7582  N N   . LEU C 105 ? 0.2904 0.3417 0.2845 -0.0378 0.0499  0.0033  406 LEU C N   
7583  C CA  . LEU C 105 ? 0.3317 0.3729 0.3258 -0.0299 0.0477  0.0009  406 LEU C CA  
7584  C C   . LEU C 105 ? 0.3054 0.3557 0.3075 -0.0232 0.0485  -0.0030 406 LEU C C   
7585  O O   . LEU C 105 ? 0.2880 0.3317 0.2922 -0.0194 0.0462  -0.0049 406 LEU C O   
7586  C CB  . LEU C 105 ? 0.3151 0.3509 0.3029 -0.0273 0.0480  0.0016  406 LEU C CB  
7587  C CG  . LEU C 105 ? 0.3338 0.3598 0.3211 -0.0205 0.0454  -0.0004 406 LEU C CG  
7588  C CD1 . LEU C 105 ? 0.3347 0.3464 0.3188 -0.0218 0.0418  0.0013  406 LEU C CD1 
7589  C CD2 . LEU C 105 ? 0.3148 0.3400 0.2969 -0.0180 0.0459  -0.0003 406 LEU C CD2 
7590  N N   . ILE C 106 ? 0.3002 0.3653 0.3062 -0.0215 0.0517  -0.0042 407 ILE C N   
7591  C CA  . ILE C 106 ? 0.2751 0.3474 0.2873 -0.0142 0.0522  -0.0077 407 ILE C CA  
7592  C C   . ILE C 106 ? 0.2735 0.3493 0.2918 -0.0155 0.0502  -0.0081 407 ILE C C   
7593  O O   . ILE C 106 ? 0.2377 0.3082 0.2578 -0.0108 0.0482  -0.0102 407 ILE C O   
7594  C CB  . ILE C 106 ? 0.2367 0.3242 0.2511 -0.0113 0.0564  -0.0089 407 ILE C CB  
7595  C CG1 . ILE C 106 ? 0.3224 0.4045 0.3290 -0.0097 0.0582  -0.0091 407 ILE C CG1 
7596  C CG2 . ILE C 106 ? 0.2644 0.3588 0.2849 -0.0036 0.0565  -0.0122 407 ILE C CG2 
7597  C CD1 . ILE C 106 ? 0.3691 0.4655 0.3760 -0.0075 0.0630  -0.0103 407 ILE C CD1 
7598  N N   . TYR C 107 ? 0.3412 0.4261 0.3620 -0.0226 0.0507  -0.0059 408 TYR C N   
7599  C CA  . TYR C 107 ? 0.3125 0.4002 0.3377 -0.0256 0.0482  -0.0059 408 TYR C CA  
7600  C C   . TYR C 107 ? 0.3247 0.3943 0.3454 -0.0259 0.0447  -0.0062 408 TYR C C   
7601  O O   . TYR C 107 ? 0.3135 0.3815 0.3370 -0.0232 0.0426  -0.0080 408 TYR C O   
7602  C CB  . TYR C 107 ? 0.2479 0.3453 0.2742 -0.0356 0.0488  -0.0030 408 TYR C CB  
7603  C CG  . TYR C 107 ? 0.3067 0.4039 0.3351 -0.0409 0.0455  -0.0026 408 TYR C CG  
7604  C CD1 . TYR C 107 ? 0.2689 0.3837 0.3062 -0.0402 0.0450  -0.0035 408 TYR C CD1 
7605  C CD2 . TYR C 107 ? 0.3337 0.4131 0.3547 -0.0464 0.0426  -0.0015 408 TYR C CD2 
7606  C CE1 . TYR C 107 ? 0.2828 0.3977 0.3214 -0.0455 0.0414  -0.0032 408 TYR C CE1 
7607  C CE2 . TYR C 107 ? 0.2903 0.3681 0.3117 -0.0514 0.0395  -0.0017 408 TYR C CE2 
7608  C CZ  . TYR C 107 ? 0.3677 0.4636 0.3979 -0.0515 0.0388  -0.0024 408 TYR C CZ  
7609  O OH  . TYR C 107 ? 0.3975 0.4925 0.4275 -0.0571 0.0353  -0.0025 408 TYR C OH  
7610  N N   . GLY C 108 ? 0.3193 0.3753 0.3328 -0.0291 0.0441  -0.0044 409 GLY C N   
7611  C CA  . GLY C 108 ? 0.2948 0.3343 0.3040 -0.0288 0.0413  -0.0049 409 GLY C CA  
7612  C C   . GLY C 108 ? 0.3152 0.3505 0.3262 -0.0205 0.0407  -0.0078 409 GLY C C   
7613  O O   . GLY C 108 ? 0.2907 0.3208 0.3025 -0.0192 0.0389  -0.0093 409 GLY C O   
7614  N N   . ALA C 109 ? 0.2437 0.2811 0.2548 -0.0156 0.0422  -0.0086 410 ALA C N   
7615  C CA  . ALA C 109 ? 0.2609 0.2937 0.2728 -0.0090 0.0416  -0.0111 410 ALA C CA  
7616  C C   . ALA C 109 ? 0.2514 0.2905 0.2680 -0.0058 0.0413  -0.0132 410 ALA C C   
7617  O O   . ALA C 109 ? 0.2573 0.2901 0.2738 -0.0033 0.0399  -0.0148 410 ALA C O   
7618  C CB  . ALA C 109 ? 0.2662 0.2998 0.2760 -0.0054 0.0430  -0.0117 410 ALA C CB  
7619  N N   . LYS C 110 ? 0.2585 0.3106 0.2791 -0.0056 0.0427  -0.0132 411 LYS C N   
7620  C CA  . LYS C 110 ? 0.2286 0.2873 0.2536 -0.0019 0.0419  -0.0148 411 LYS C CA  
7621  C C   . LYS C 110 ? 0.2703 0.3263 0.2961 -0.0056 0.0393  -0.0145 411 LYS C C   
7622  O O   . LYS C 110 ? 0.2580 0.3109 0.2841 -0.0024 0.0377  -0.0159 411 LYS C O   
7623  C CB  . LYS C 110 ? 0.2742 0.3496 0.3043 -0.0005 0.0439  -0.0147 411 LYS C CB  
7624  C CG  . LYS C 110 ? 0.2831 0.3605 0.3113 0.0051  0.0467  -0.0161 411 LYS C CG  
7625  C CD  . LYS C 110 ? 0.2164 0.3117 0.2500 0.0073  0.0492  -0.0163 411 LYS C CD  
7626  C CE  . LYS C 110 ? 0.3361 0.4317 0.3662 0.0135  0.0523  -0.0183 411 LYS C CE  
7627  N NZ  . LYS C 110 ? 0.3086 0.4221 0.3441 0.0178  0.0552  -0.0192 411 LYS C NZ  
7628  N N   . HIS C 111 ? 0.3240 0.3798 0.3488 -0.0128 0.0388  -0.0126 412 HIS C N   
7629  C CA  . HIS C 111 ? 0.3369 0.3895 0.3612 -0.0167 0.0361  -0.0126 412 HIS C CA  
7630  C C   . HIS C 111 ? 0.3166 0.3529 0.3356 -0.0157 0.0350  -0.0137 412 HIS C C   
7631  O O   . HIS C 111 ? 0.3081 0.3409 0.3262 -0.0157 0.0331  -0.0149 412 HIS C O   
7632  C CB  . HIS C 111 ? 0.2881 0.3454 0.3121 -0.0256 0.0357  -0.0103 412 HIS C CB  
7633  C CG  . HIS C 111 ? 0.2997 0.3766 0.3311 -0.0270 0.0359  -0.0097 412 HIS C CG  
7634  N ND1 . HIS C 111 ? 0.2873 0.3778 0.3234 -0.0238 0.0388  -0.0094 412 HIS C ND1 
7635  C CD2 . HIS C 111 ? 0.3068 0.3929 0.3419 -0.0304 0.0335  -0.0095 412 HIS C CD2 
7636  C CE1 . HIS C 111 ? 0.2843 0.3927 0.3276 -0.0247 0.0384  -0.0091 412 HIS C CE1 
7637  N NE2 . HIS C 111 ? 0.3174 0.4239 0.3606 -0.0290 0.0349  -0.0089 412 HIS C NE2 
7638  N N   . ALA C 112 ? 0.3257 0.3530 0.3411 -0.0141 0.0360  -0.0136 413 ALA C N   
7639  C CA  . ALA C 112 ? 0.3358 0.3508 0.3478 -0.0117 0.0353  -0.0150 413 ALA C CA  
7640  C C   . ALA C 112 ? 0.3493 0.3654 0.3632 -0.0065 0.0352  -0.0171 413 ALA C C   
7641  O O   . ALA C 112 ? 0.3614 0.3710 0.3732 -0.0060 0.0344  -0.0185 413 ALA C O   
7642  C CB  . ALA C 112 ? 0.2495 0.2574 0.2588 -0.0100 0.0361  -0.0143 413 ALA C CB  
7643  N N   . TRP C 113 ? 0.2836 0.3070 0.3003 -0.0028 0.0362  -0.0174 414 TRP C N   
7644  C CA  . TRP C 113 ? 0.2875 0.3106 0.3044 0.0016  0.0357  -0.0191 414 TRP C CA  
7645  C C   . TRP C 113 ? 0.2733 0.3008 0.2915 0.0006  0.0338  -0.0192 414 TRP C C   
7646  O O   . TRP C 113 ? 0.3047 0.3268 0.3205 0.0015  0.0327  -0.0202 414 TRP C O   
7647  C CB  . TRP C 113 ? 0.2434 0.2713 0.2613 0.0062  0.0370  -0.0196 414 TRP C CB  
7648  C CG  . TRP C 113 ? 0.2195 0.2437 0.2354 0.0107  0.0364  -0.0212 414 TRP C CG  
7649  C CD1 . TRP C 113 ? 0.2894 0.3066 0.3027 0.0107  0.0351  -0.0219 414 TRP C CD1 
7650  C CD2 . TRP C 113 ? 0.3952 0.4212 0.4101 0.0157  0.0370  -0.0221 414 TRP C CD2 
7651  N NE1 . TRP C 113 ? 0.2833 0.2973 0.2937 0.0148  0.0348  -0.0229 414 TRP C NE1 
7652  C CE2 . TRP C 113 ? 0.3772 0.3958 0.3884 0.0183  0.0358  -0.0231 414 TRP C CE2 
7653  C CE3 . TRP C 113 ? 0.2787 0.3110 0.2945 0.0183  0.0387  -0.0223 414 TRP C CE3 
7654  C CZ2 . TRP C 113 ? 0.3340 0.3496 0.3416 0.0235  0.0358  -0.0243 414 TRP C CZ2 
7655  C CZ3 . TRP C 113 ? 0.2836 0.3137 0.2963 0.0241  0.0391  -0.0239 414 TRP C CZ3 
7656  C CH2 . TRP C 113 ? 0.3067 0.3276 0.3150 0.0267  0.0374  -0.0248 414 TRP C CH2 
7657  N N   . ARG C 114 ? 0.2419 0.2804 0.2639 -0.0015 0.0334  -0.0180 415 ARG C N   
7658  C CA  . ARG C 114 ? 0.2804 0.3254 0.3045 -0.0028 0.0310  -0.0177 415 ARG C CA  
7659  C C   . ARG C 114 ? 0.3143 0.3500 0.3340 -0.0074 0.0293  -0.0181 415 ARG C C   
7660  O O   . ARG C 114 ? 0.2896 0.3251 0.3080 -0.0070 0.0270  -0.0187 415 ARG C O   
7661  C CB  . ARG C 114 ? 0.2654 0.3252 0.2950 -0.0062 0.0311  -0.0161 415 ARG C CB  
7662  C CG  . ARG C 114 ? 0.2373 0.3087 0.2710 -0.0064 0.0283  -0.0158 415 ARG C CG  
7663  C CD  . ARG C 114 ? 0.2647 0.3518 0.3042 -0.0121 0.0284  -0.0140 415 ARG C CD  
7664  N NE  . ARG C 114 ? 0.2124 0.3152 0.2582 -0.0104 0.0259  -0.0136 415 ARG C NE  
7665  C CZ  . ARG C 114 ? 0.2891 0.4103 0.3419 -0.0144 0.0258  -0.0121 415 ARG C CZ  
7666  N NH1 . ARG C 114 ? 0.2127 0.3495 0.2720 -0.0119 0.0230  -0.0117 415 ARG C NH1 
7667  N NH2 . ARG C 114 ? 0.2420 0.3664 0.2952 -0.0210 0.0283  -0.0108 415 ARG C NH2 
7668  N N   . ASN C 115 ? 0.2597 0.2865 0.2758 -0.0111 0.0302  -0.0180 416 ASN C N   
7669  C CA  . ASN C 115 ? 0.2850 0.3015 0.2956 -0.0149 0.0290  -0.0188 416 ASN C CA  
7670  C C   . ASN C 115 ? 0.3257 0.3314 0.3324 -0.0112 0.0300  -0.0207 416 ASN C C   
7671  O O   . ASN C 115 ? 0.3023 0.2990 0.3039 -0.0133 0.0296  -0.0219 416 ASN C O   
7672  C CB  . ASN C 115 ? 0.2640 0.2751 0.2716 -0.0204 0.0293  -0.0177 416 ASN C CB  
7673  C CG  . ASN C 115 ? 0.2935 0.3155 0.3042 -0.0263 0.0283  -0.0156 416 ASN C CG  
7674  O OD1 . ASN C 115 ? 0.2793 0.3130 0.2944 -0.0268 0.0267  -0.0154 416 ASN C OD1 
7675  N ND2 . ASN C 115 ? 0.2590 0.2775 0.2672 -0.0308 0.0291  -0.0140 416 ASN C ND2 
7676  N N   . ALA C 116 ? 0.2184 0.2248 0.2268 -0.0061 0.0314  -0.0211 417 ALA C N   
7677  C CA  . ALA C 116 ? 0.2883 0.2863 0.2936 -0.0036 0.0327  -0.0227 417 ALA C CA  
7678  C C   . ALA C 116 ? 0.3237 0.3193 0.3256 -0.0035 0.0315  -0.0238 417 ALA C C   
7679  O O   . ALA C 116 ? 0.2873 0.2856 0.2895 -0.0008 0.0309  -0.0236 417 ALA C O   
7680  C CB  . ALA C 116 ? 0.2142 0.2136 0.2216 0.0004  0.0342  -0.0228 417 ALA C CB  
7681  N N   . SER C 117 ? 0.2808 0.2701 0.2781 -0.0065 0.0311  -0.0248 418 SER C N   
7682  C CA  A SER C 117 ? 0.2565 0.2436 0.2494 -0.0073 0.0297  -0.0257 418 SER C CA  
7683  C CA  B SER C 117 ? 0.2631 0.2500 0.2559 -0.0073 0.0297  -0.0257 418 SER C CA  
7684  C C   . SER C 117 ? 0.2934 0.2775 0.2842 -0.0041 0.0311  -0.0264 418 SER C C   
7685  O O   . SER C 117 ? 0.4080 0.3915 0.3953 -0.0039 0.0296  -0.0263 418 SER C O   
7686  C CB  A SER C 117 ? 0.2776 0.2566 0.2644 -0.0110 0.0295  -0.0272 418 SER C CB  
7687  C CB  B SER C 117 ? 0.2768 0.2554 0.2634 -0.0109 0.0296  -0.0273 418 SER C CB  
7688  O OG  A SER C 117 ? 0.2810 0.2529 0.2660 -0.0091 0.0325  -0.0287 418 SER C OG  
7689  O OG  B SER C 117 ? 0.2838 0.2632 0.2706 -0.0152 0.0280  -0.0265 418 SER C OG  
7690  N N   . ARG C 118 ? 0.3151 0.2973 0.3075 -0.0020 0.0338  -0.0270 419 ARG C N   
7691  C CA  . ARG C 118 ? 0.2809 0.2604 0.2709 -0.0005 0.0354  -0.0276 419 ARG C CA  
7692  C C   . ARG C 118 ? 0.3381 0.3204 0.3297 0.0019  0.0347  -0.0265 419 ARG C C   
7693  O O   . ARG C 118 ? 0.3226 0.3017 0.3114 0.0022  0.0358  -0.0268 419 ARG C O   
7694  C CB  . ARG C 118 ? 0.2601 0.2376 0.2513 0.0002  0.0385  -0.0290 419 ARG C CB  
7695  C CG  . ARG C 118 ? 0.3112 0.2837 0.2987 -0.0010 0.0397  -0.0308 419 ARG C CG  
7696  C CD  . ARG C 118 ? 0.2593 0.2316 0.2489 0.0011  0.0428  -0.0321 419 ARG C CD  
7697  N NE  . ARG C 118 ? 0.3398 0.3067 0.3247 0.0012  0.0448  -0.0344 419 ARG C NE  
7698  C CZ  . ARG C 118 ? 0.3808 0.3479 0.3675 0.0041  0.0476  -0.0360 419 ARG C CZ  
7699  N NH1 . ARG C 118 ? 0.4281 0.4011 0.4215 0.0064  0.0480  -0.0350 419 ARG C NH1 
7700  N NH2 . ARG C 118 ? 0.3250 0.2869 0.3067 0.0050  0.0497  -0.0385 419 ARG C NH2 
7701  N N   . CYS C 119 ? 0.2862 0.2740 0.2817 0.0033  0.0332  -0.0253 420 CYS C N   
7702  C CA  . CYS C 119 ? 0.2534 0.2427 0.2496 0.0065  0.0329  -0.0247 420 CYS C CA  
7703  C C   . CYS C 119 ? 0.2555 0.2455 0.2493 0.0087  0.0302  -0.0238 420 CYS C C   
7704  O O   . CYS C 119 ? 0.2458 0.2424 0.2425 0.0090  0.0283  -0.0231 420 CYS C O   
7705  C CB  . CYS C 119 ? 0.2369 0.2320 0.2384 0.0076  0.0335  -0.0242 420 CYS C CB  
7706  S SG  . CYS C 119 ? 0.2755 0.2718 0.2765 0.0122  0.0333  -0.0240 420 CYS C SG  
7707  N N   . VAL C 120 ? 0.2296 0.2130 0.2177 0.0102  0.0299  -0.0238 421 VAL C N   
7708  C CA  . VAL C 120 ? 0.3053 0.2873 0.2897 0.0136  0.0270  -0.0228 421 VAL C CA  
7709  C C   . VAL C 120 ? 0.3376 0.3236 0.3248 0.0189  0.0264  -0.0225 421 VAL C C   
7710  O O   . VAL C 120 ? 0.2952 0.2826 0.2811 0.0233  0.0238  -0.0217 421 VAL C O   
7711  C CB  . VAL C 120 ? 0.3632 0.3340 0.3384 0.0126  0.0269  -0.0226 421 VAL C CB  
7712  C CG1 . VAL C 120 ? 0.3209 0.2856 0.2934 0.0130  0.0287  -0.0231 421 VAL C CG1 
7713  C CG2 . VAL C 120 ? 0.3700 0.3375 0.3396 0.0157  0.0232  -0.0211 421 VAL C CG2 
7714  N N   . GLY C 121 ? 0.3612 0.3498 0.3521 0.0192  0.0286  -0.0233 422 GLY C N   
7715  C CA  . GLY C 121 ? 0.2827 0.2740 0.2746 0.0245  0.0286  -0.0235 422 GLY C CA  
7716  C C   . GLY C 121 ? 0.3123 0.3171 0.3122 0.0259  0.0288  -0.0231 422 GLY C C   
7717  O O   . GLY C 121 ? 0.3108 0.3195 0.3125 0.0296  0.0300  -0.0237 422 GLY C O   
7718  N N   . ARG C 122 ? 0.2728 0.2849 0.2771 0.0226  0.0277  -0.0222 423 ARG C N   
7719  C CA  . ARG C 122 ? 0.2587 0.2836 0.2703 0.0213  0.0283  -0.0216 423 ARG C CA  
7720  C C   . ARG C 122 ? 0.3320 0.3685 0.3480 0.0266  0.0271  -0.0212 423 ARG C C   
7721  O O   . ARG C 122 ? 0.3125 0.3615 0.3351 0.0256  0.0282  -0.0207 423 ARG C O   
7722  C CB  . ARG C 122 ? 0.2166 0.2437 0.2299 0.0150  0.0272  -0.0209 423 ARG C CB  
7723  C CG  . ARG C 122 ? 0.2258 0.2463 0.2378 0.0103  0.0293  -0.0214 423 ARG C CG  
7724  C CD  . ARG C 122 ? 0.2481 0.2687 0.2599 0.0048  0.0281  -0.0211 423 ARG C CD  
7725  N NE  . ARG C 122 ? 0.2976 0.3104 0.3039 0.0039  0.0267  -0.0218 423 ARG C NE  
7726  C CZ  . ARG C 122 ? 0.2786 0.2900 0.2826 -0.0004 0.0252  -0.0219 423 ARG C CZ  
7727  N NH1 . ARG C 122 ? 0.2232 0.2399 0.2300 -0.0048 0.0245  -0.0212 423 ARG C NH1 
7728  N NH2 . ARG C 122 ? 0.2678 0.2717 0.2657 -0.0011 0.0243  -0.0227 423 ARG C NH2 
7729  N N   . ILE C 123 ? 0.2262 0.2593 0.2387 0.0326  0.0249  -0.0212 424 ILE C N   
7730  C CA  . ILE C 123 ? 0.2334 0.2783 0.2505 0.0394  0.0240  -0.0210 424 ILE C CA  
7731  C C   . ILE C 123 ? 0.2893 0.3387 0.3087 0.0427  0.0276  -0.0222 424 ILE C C   
7732  O O   . ILE C 123 ? 0.3445 0.4081 0.3701 0.0470  0.0283  -0.0222 424 ILE C O   
7733  C CB  . ILE C 123 ? 0.2540 0.2911 0.2650 0.0466  0.0209  -0.0208 424 ILE C CB  
7734  C CG1 . ILE C 123 ? 0.2760 0.3282 0.2933 0.0544  0.0191  -0.0203 424 ILE C CG1 
7735  C CG2 . ILE C 123 ? 0.2447 0.2654 0.2465 0.0501  0.0224  -0.0222 424 ILE C CG2 
7736  C CD1 . ILE C 123 ? 0.3825 0.4279 0.3939 0.0618  0.0150  -0.0195 424 ILE C CD1 
7737  N N   . GLN C 124 ? 0.2991 0.3376 0.3137 0.0404  0.0300  -0.0233 425 GLN C N   
7738  C CA  . GLN C 124 ? 0.3098 0.3500 0.3243 0.0425  0.0333  -0.0246 425 GLN C CA  
7739  C C   . GLN C 124 ? 0.3546 0.4039 0.3746 0.0363  0.0357  -0.0239 425 GLN C C   
7740  O O   . GLN C 124 ? 0.3060 0.3565 0.3252 0.0370  0.0385  -0.0247 425 GLN C O   
7741  C CB  . GLN C 124 ? 0.3102 0.3332 0.3155 0.0426  0.0340  -0.0260 425 GLN C CB  
7742  C CG  . GLN C 124 ? 0.4261 0.4375 0.4234 0.0491  0.0321  -0.0269 425 GLN C CG  
7743  C CD  . GLN C 124 ? 0.5204 0.5346 0.5162 0.0578  0.0334  -0.0286 425 GLN C CD  
7744  O OE1 . GLN C 124 ? 0.5216 0.5426 0.5200 0.0580  0.0364  -0.0296 425 GLN C OE1 
7745  N NE2 . GLN C 124 ? 0.5248 0.5329 0.5157 0.0654  0.0312  -0.0289 425 GLN C NE2 
7746  N N   . TRP C 125 ? 0.2848 0.3394 0.3091 0.0299  0.0345  -0.0222 426 TRP C N   
7747  C CA  . TRP C 125 ? 0.2908 0.3473 0.3169 0.0230  0.0362  -0.0213 426 TRP C CA  
7748  C C   . TRP C 125 ? 0.3493 0.4182 0.3794 0.0234  0.0391  -0.0210 426 TRP C C   
7749  O O   . TRP C 125 ? 0.3413 0.4075 0.3695 0.0202  0.0412  -0.0207 426 TRP C O   
7750  C CB  . TRP C 125 ? 0.2724 0.3311 0.3009 0.0165  0.0342  -0.0198 426 TRP C CB  
7751  C CG  . TRP C 125 ? 0.3018 0.3768 0.3371 0.0155  0.0331  -0.0187 426 TRP C CG  
7752  C CD1 . TRP C 125 ? 0.3444 0.4259 0.3823 0.0186  0.0302  -0.0185 426 TRP C CD1 
7753  C CD2 . TRP C 125 ? 0.2305 0.3182 0.2709 0.0106  0.0347  -0.0173 426 TRP C CD2 
7754  N NE1 . TRP C 125 ? 0.2652 0.3643 0.3105 0.0161  0.0298  -0.0172 426 TRP C NE1 
7755  C CE2 . TRP C 125 ? 0.2472 0.3506 0.2941 0.0107  0.0328  -0.0165 426 TRP C CE2 
7756  C CE3 . TRP C 125 ? 0.2396 0.3272 0.2792 0.0058  0.0374  -0.0164 426 TRP C CE3 
7757  C CZ2 . TRP C 125 ? 0.2173 0.3372 0.2705 0.0054  0.0338  -0.0149 426 TRP C CZ2 
7758  C CZ3 . TRP C 125 ? 0.2472 0.3492 0.2916 0.0007  0.0385  -0.0148 426 TRP C CZ3 
7759  C CH2 . TRP C 125 ? 0.2978 0.4163 0.3494 0.0001  0.0369  -0.0141 426 TRP C CH2 
7760  N N   . SER C 126 ? 0.2891 0.3723 0.3247 0.0273  0.0393  -0.0210 427 SER C N   
7761  C CA  . SER C 126 ? 0.2933 0.3901 0.3329 0.0265  0.0427  -0.0206 427 SER C CA  
7762  C C   . SER C 126 ? 0.3909 0.4840 0.4260 0.0328  0.0457  -0.0228 427 SER C C   
7763  O O   . SER C 126 ? 0.3368 0.4398 0.3735 0.0324  0.0491  -0.0227 427 SER C O   
7764  C CB  . SER C 126 ? 0.2629 0.3798 0.3113 0.0282  0.0423  -0.0199 427 SER C CB  
7765  O OG  . SER C 126 ? 0.3537 0.4718 0.4022 0.0384  0.0413  -0.0216 427 SER C OG  
7766  N N   . LYS C 127 ? 0.3600 0.4387 0.3884 0.0381  0.0446  -0.0246 428 LYS C N   
7767  C CA  . LYS C 127 ? 0.4447 0.5165 0.4665 0.0433  0.0470  -0.0269 428 LYS C CA  
7768  C C   . LYS C 127 ? 0.6158 0.6727 0.6310 0.0381  0.0466  -0.0269 428 LYS C C   
7769  O O   . LYS C 127 ? 0.7905 0.8333 0.7995 0.0394  0.0449  -0.0280 428 LYS C O   
7770  C CB  . LYS C 127 ? 0.5213 0.5867 0.5391 0.0526  0.0457  -0.0290 428 LYS C CB  
7771  C CG  . LYS C 127 ? 0.7385 0.7953 0.7478 0.0587  0.0480  -0.0319 428 LYS C CG  
7772  C CD  . LYS C 127 ? 0.8154 0.8619 0.8187 0.0677  0.0461  -0.0338 428 LYS C CD  
7773  C CE  . LYS C 127 ? 0.8576 0.8932 0.8506 0.0736  0.0483  -0.0371 428 LYS C CE  
7774  N NZ  . LYS C 127 ? 0.8642 0.8847 0.8484 0.0816  0.0459  -0.0387 428 LYS C NZ  
7775  N N   . LEU C 128 ? 0.4806 0.5415 0.4973 0.0318  0.0480  -0.0253 429 LEU C N   
7776  C CA  . LEU C 128 ? 0.3275 0.3772 0.3395 0.0269  0.0473  -0.0247 429 LEU C CA  
7777  C C   . LEU C 128 ? 0.2899 0.3422 0.2986 0.0258  0.0501  -0.0248 429 LEU C C   
7778  O O   . LEU C 128 ? 0.3131 0.3771 0.3253 0.0236  0.0523  -0.0234 429 LEU C O   
7779  C CB  . LEU C 128 ? 0.2446 0.2936 0.2600 0.0202  0.0455  -0.0223 429 LEU C CB  
7780  C CG  . LEU C 128 ? 0.2665 0.3061 0.2783 0.0159  0.0448  -0.0213 429 LEU C CG  
7781  C CD1 . LEU C 128 ? 0.2557 0.2837 0.2631 0.0178  0.0433  -0.0230 429 LEU C CD1 
7782  C CD2 . LEU C 128 ? 0.2146 0.2539 0.2291 0.0101  0.0435  -0.0190 429 LEU C CD2 
7783  N N   . GLN C 129 ? 0.2501 0.2920 0.2517 0.0269  0.0499  -0.0262 430 GLN C N   
7784  C CA  . GLN C 129 ? 0.2856 0.3284 0.2823 0.0256  0.0521  -0.0263 430 GLN C CA  
7785  C C   . GLN C 129 ? 0.3236 0.3629 0.3202 0.0189  0.0505  -0.0235 430 GLN C C   
7786  O O   . GLN C 129 ? 0.3893 0.4194 0.3845 0.0174  0.0478  -0.0234 430 GLN C O   
7787  C CB  . GLN C 129 ? 0.3502 0.3830 0.3380 0.0296  0.0523  -0.0294 430 GLN C CB  
7788  C CG  . GLN C 129 ? 0.3761 0.4104 0.3577 0.0288  0.0547  -0.0300 430 GLN C CG  
7789  C CD  . GLN C 129 ? 0.4988 0.5473 0.4834 0.0310  0.0589  -0.0300 430 GLN C CD  
7790  O OE1 . GLN C 129 ? 0.6544 0.7093 0.6385 0.0268  0.0608  -0.0281 430 GLN C OE1 
7791  N NE2 . GLN C 129 ? 0.4539 0.5080 0.4416 0.0378  0.0603  -0.0321 430 GLN C NE2 
7792  N N   . VAL C 130 ? 0.2725 0.3192 0.2703 0.0149  0.0521  -0.0212 431 VAL C N   
7793  C CA  . VAL C 130 ? 0.2705 0.3131 0.2675 0.0091  0.0503  -0.0181 431 VAL C CA  
7794  C C   . VAL C 130 ? 0.3578 0.3976 0.3474 0.0079  0.0510  -0.0176 431 VAL C C   
7795  O O   . VAL C 130 ? 0.3553 0.4021 0.3423 0.0077  0.0542  -0.0176 431 VAL C O   
7796  C CB  . VAL C 130 ? 0.2859 0.3361 0.2875 0.0043  0.0510  -0.0153 431 VAL C CB  
7797  C CG1 . VAL C 130 ? 0.2474 0.2908 0.2457 -0.0013 0.0493  -0.0120 431 VAL C CG1 
7798  C CG2 . VAL C 130 ? 0.3241 0.3763 0.3323 0.0052  0.0496  -0.0160 431 VAL C CG2 
7799  N N   . PHE C 131 ? 0.3241 0.3544 0.3101 0.0071  0.0481  -0.0172 432 PHE C N   
7800  C CA  . PHE C 131 ? 0.2967 0.3236 0.2752 0.0055  0.0476  -0.0164 432 PHE C CA  
7801  C C   . PHE C 131 ? 0.2773 0.3017 0.2552 0.0010  0.0457  -0.0122 432 PHE C C   
7802  O O   . PHE C 131 ? 0.3452 0.3643 0.3261 0.0006  0.0427  -0.0111 432 PHE C O   
7803  C CB  . PHE C 131 ? 0.2824 0.3017 0.2571 0.0075  0.0451  -0.0186 432 PHE C CB  
7804  C CG  . PHE C 131 ? 0.3018 0.3203 0.2736 0.0117  0.0469  -0.0226 432 PHE C CG  
7805  C CD1 . PHE C 131 ? 0.3777 0.3996 0.3437 0.0135  0.0502  -0.0242 432 PHE C CD1 
7806  C CD2 . PHE C 131 ? 0.3552 0.3690 0.3292 0.0141  0.0455  -0.0247 432 PHE C CD2 
7807  C CE1 . PHE C 131 ? 0.3879 0.4074 0.3500 0.0185  0.0520  -0.0282 432 PHE C CE1 
7808  C CE2 . PHE C 131 ? 0.3338 0.3443 0.3034 0.0183  0.0469  -0.0283 432 PHE C CE2 
7809  C CZ  . PHE C 131 ? 0.3697 0.3825 0.3331 0.0209  0.0500  -0.0301 432 PHE C CZ  
7810  N N   . ASP C 132 ? 0.3000 0.3279 0.2736 -0.0023 0.0477  -0.0099 433 ASP C N   
7811  C CA  . ASP C 132 ? 0.2529 0.2765 0.2237 -0.0070 0.0459  -0.0056 433 ASP C CA  
7812  C C   . ASP C 132 ? 0.3220 0.3382 0.2861 -0.0066 0.0426  -0.0044 433 ASP C C   
7813  O O   . ASP C 132 ? 0.3669 0.3841 0.3237 -0.0072 0.0437  -0.0045 433 ASP C O   
7814  C CB  . ASP C 132 ? 0.3547 0.3852 0.3226 -0.0116 0.0495  -0.0033 433 ASP C CB  
7815  C CG  . ASP C 132 ? 0.3671 0.3909 0.3306 -0.0172 0.0475  0.0015  433 ASP C CG  
7816  O OD1 . ASP C 132 ? 0.3854 0.4143 0.3464 -0.0226 0.0503  0.0038  433 ASP C OD1 
7817  O OD2 . ASP C 132 ? 0.4099 0.4234 0.3720 -0.0163 0.0433  0.0030  433 ASP C OD2 
7818  N N   . ALA C 133 ? 0.3187 0.3282 0.2849 -0.0055 0.0385  -0.0033 434 ALA C N   
7819  C CA  . ALA C 133 ? 0.3585 0.3625 0.3193 -0.0050 0.0347  -0.0017 434 ALA C CA  
7820  C C   . ALA C 133 ? 0.3490 0.3460 0.3067 -0.0069 0.0318  0.0030  434 ALA C C   
7821  O O   . ALA C 133 ? 0.3027 0.2950 0.2595 -0.0048 0.0275  0.0044  434 ALA C O   
7822  C CB  . ALA C 133 ? 0.3394 0.3427 0.3050 -0.0015 0.0319  -0.0043 434 ALA C CB  
7823  N N   . ARG C 134 ? 0.2867 0.2829 0.2421 -0.0109 0.0339  0.0055  435 ARG C N   
7824  C CA  . ARG C 134 ? 0.3683 0.3547 0.3189 -0.0129 0.0310  0.0099  435 ARG C CA  
7825  C C   . ARG C 134 ? 0.3531 0.3343 0.2929 -0.0143 0.0286  0.0136  435 ARG C C   
7826  O O   . ARG C 134 ? 0.3564 0.3275 0.2910 -0.0147 0.0252  0.0176  435 ARG C O   
7827  C CB  . ARG C 134 ? 0.3189 0.3047 0.2692 -0.0181 0.0337  0.0115  435 ARG C CB  
7828  C CG  . ARG C 134 ? 0.3365 0.3240 0.2961 -0.0166 0.0344  0.0088  435 ARG C CG  
7829  C CD  . ARG C 134 ? 0.3613 0.3500 0.3201 -0.0228 0.0369  0.0103  435 ARG C CD  
7830  N NE  . ARG C 134 ? 0.2974 0.2987 0.2566 -0.0259 0.0412  0.0096  435 ARG C NE  
7831  C CZ  . ARG C 134 ? 0.3292 0.3355 0.2872 -0.0327 0.0439  0.0114  435 ARG C CZ  
7832  N NH1 . ARG C 134 ? 0.3319 0.3297 0.2870 -0.0378 0.0423  0.0141  435 ARG C NH1 
7833  N NH2 . ARG C 134 ? 0.3142 0.3340 0.2734 -0.0343 0.0482  0.0104  435 ARG C NH2 
7834  N N   . ASP C 135 ? 0.2970 0.2836 0.2325 -0.0147 0.0299  0.0124  436 ASP C N   
7835  C CA  . ASP C 135 ? 0.3219 0.3036 0.2465 -0.0159 0.0269  0.0157  436 ASP C CA  
7836  C C   . ASP C 135 ? 0.3516 0.3317 0.2778 -0.0110 0.0215  0.0151  436 ASP C C   
7837  O O   . ASP C 135 ? 0.3605 0.3370 0.2781 -0.0114 0.0179  0.0179  436 ASP C O   
7838  C CB  . ASP C 135 ? 0.3415 0.3294 0.2588 -0.0191 0.0310  0.0147  436 ASP C CB  
7839  C CG  . ASP C 135 ? 0.4618 0.4573 0.3835 -0.0157 0.0330  0.0091  436 ASP C CG  
7840  O OD1 . ASP C 135 ? 0.4873 0.4871 0.4025 -0.0171 0.0364  0.0074  436 ASP C OD1 
7841  O OD2 . ASP C 135 ? 0.5744 0.5707 0.5049 -0.0118 0.0312  0.0062  436 ASP C OD2 
7842  N N   . CYS C 136 ? 0.4011 0.3847 0.3377 -0.0069 0.0207  0.0117  437 CYS C N   
7843  C CA  . CYS C 136 ? 0.3672 0.3523 0.3068 -0.0031 0.0159  0.0108  437 CYS C CA  
7844  C C   . CYS C 136 ? 0.3568 0.3350 0.2950 -0.0003 0.0105  0.0151  437 CYS C C   
7845  O O   . CYS C 136 ? 0.3910 0.3627 0.3300 0.0003  0.0107  0.0172  437 CYS C O   
7846  C CB  . CYS C 136 ? 0.3713 0.3620 0.3222 -0.0004 0.0171  0.0063  437 CYS C CB  
7847  S SG  . CYS C 136 ? 0.3736 0.3696 0.3292 0.0023  0.0126  0.0041  437 CYS C SG  
7848  N N   . THR C 137 ? 0.3446 0.3241 0.2802 0.0016  0.0053  0.0165  438 THR C N   
7849  C CA  . THR C 137 ? 0.3377 0.3114 0.2717 0.0057  -0.0004 0.0208  438 THR C CA  
7850  C C   . THR C 137 ? 0.3127 0.2942 0.2550 0.0105  -0.0053 0.0196  438 THR C C   
7851  O O   . THR C 137 ? 0.3632 0.3418 0.3071 0.0157  -0.0099 0.0226  438 THR C O   
7852  C CB  . THR C 137 ? 0.3463 0.3128 0.2661 0.0032  -0.0034 0.0258  438 THR C CB  
7853  O OG1 . THR C 137 ? 0.4004 0.3733 0.3163 0.0018  -0.0058 0.0247  438 THR C OG1 
7854  C CG2 . THR C 137 ? 0.3792 0.3396 0.2899 -0.0030 0.0017  0.0274  438 THR C CG2 
7855  N N   . THR C 138 ? 0.3257 0.3168 0.2728 0.0090  -0.0046 0.0155  439 THR C N   
7856  C CA  . THR C 138 ? 0.3340 0.3343 0.2885 0.0120  -0.0094 0.0146  439 THR C CA  
7857  C C   . THR C 138 ? 0.3213 0.3296 0.2858 0.0110  -0.0061 0.0094  439 THR C C   
7858  O O   . THR C 138 ? 0.3114 0.3181 0.2748 0.0079  -0.0009 0.0063  439 THR C O   
7859  C CB  . THR C 138 ? 0.3721 0.3754 0.3187 0.0095  -0.0141 0.0159  439 THR C CB  
7860  O OG1 . THR C 138 ? 0.3296 0.3336 0.2708 0.0040  -0.0104 0.0122  439 THR C OG1 
7861  C CG2 . THR C 138 ? 0.3368 0.3311 0.2713 0.0098  -0.0174 0.0214  439 THR C CG2 
7862  N N   . ALA C 139 ? 0.3237 0.3414 0.2976 0.0138  -0.0095 0.0086  440 ALA C N   
7863  C CA  . ALA C 139 ? 0.3137 0.3391 0.2959 0.0119  -0.0070 0.0041  440 ALA C CA  
7864  C C   . ALA C 139 ? 0.3520 0.3777 0.3274 0.0058  -0.0061 0.0012  440 ALA C C   
7865  O O   . ALA C 139 ? 0.3211 0.3465 0.2984 0.0034  -0.0020 -0.0026 440 ALA C O   
7866  C CB  . ALA C 139 ? 0.3342 0.3716 0.3275 0.0151  -0.0109 0.0041  440 ALA C CB  
7867  N N   . HIS C 140 ? 0.3547 0.3797 0.3210 0.0034  -0.0100 0.0028  441 HIS C N   
7868  C CA  . HIS C 140 ? 0.2943 0.3172 0.2518 -0.0021 -0.0088 -0.0004 441 HIS C CA  
7869  C C   . HIS C 140 ? 0.2864 0.3009 0.2380 -0.0030 -0.0022 -0.0023 441 HIS C C   
7870  O O   . HIS C 140 ? 0.2843 0.2971 0.2339 -0.0055 0.0011  -0.0064 441 HIS C O   
7871  C CB  . HIS C 140 ? 0.3528 0.3751 0.2995 -0.0045 -0.0140 0.0019  441 HIS C CB  
7872  C CG  . HIS C 140 ? 0.3791 0.4116 0.3301 -0.0059 -0.0206 0.0021  441 HIS C CG  
7873  N ND1 . HIS C 140 ? 0.4278 0.4688 0.3880 -0.0014 -0.0257 0.0056  441 HIS C ND1 
7874  C CD2 . HIS C 140 ? 0.3831 0.4191 0.3306 -0.0115 -0.0231 -0.0008 441 HIS C CD2 
7875  C CE1 . HIS C 140 ? 0.3895 0.4412 0.3530 -0.0042 -0.0310 0.0050  441 HIS C CE1 
7876  N NE2 . HIS C 140 ? 0.4219 0.4702 0.3773 -0.0110 -0.0297 0.0012  441 HIS C NE2 
7877  N N   . GLY C 141 ? 0.2959 0.3052 0.2444 -0.0011 -0.0004 0.0008  442 GLY C N   
7878  C CA  . GLY C 141 ? 0.2874 0.2916 0.2320 -0.0021 0.0058  -0.0007 442 GLY C CA  
7879  C C   . GLY C 141 ? 0.3302 0.3358 0.2841 -0.0008 0.0100  -0.0038 442 GLY C C   
7880  O O   . GLY C 141 ? 0.3262 0.3304 0.2778 -0.0019 0.0143  -0.0070 442 GLY C O   
7881  N N   . MET C 142 ? 0.3049 0.3133 0.2689 0.0021  0.0087  -0.0028 443 MET C N   
7882  C CA  . MET C 142 ? 0.2592 0.2690 0.2315 0.0031  0.0122  -0.0057 443 MET C CA  
7883  C C   . MET C 142 ? 0.2569 0.2689 0.2294 0.0008  0.0127  -0.0097 443 MET C C   
7884  O O   . MET C 142 ? 0.2716 0.2813 0.2443 0.0005  0.0166  -0.0125 443 MET C O   
7885  C CB  . MET C 142 ? 0.2874 0.3001 0.2694 0.0067  0.0104  -0.0043 443 MET C CB  
7886  C CG  . MET C 142 ? 0.3045 0.3121 0.2853 0.0094  0.0096  -0.0005 443 MET C CG  
7887  S SD  . MET C 142 ? 0.3367 0.3471 0.3275 0.0150  0.0073  0.0005  443 MET C SD  
7888  C CE  . MET C 142 ? 0.2457 0.2565 0.2435 0.0147  0.0127  -0.0034 443 MET C CE  
7889  N N   . PHE C 143 ? 0.2605 0.2766 0.2324 -0.0010 0.0084  -0.0099 444 PHE C N   
7890  C CA  . PHE C 143 ? 0.2615 0.2778 0.2313 -0.0046 0.0084  -0.0136 444 PHE C CA  
7891  C C   . PHE C 143 ? 0.3944 0.4029 0.3535 -0.0061 0.0117  -0.0163 444 PHE C C   
7892  O O   . PHE C 143 ? 0.3355 0.3403 0.2936 -0.0067 0.0145  -0.0196 444 PHE C O   
7893  C CB  . PHE C 143 ? 0.2669 0.2892 0.2361 -0.0074 0.0026  -0.0129 444 PHE C CB  
7894  C CG  . PHE C 143 ? 0.3896 0.4101 0.3535 -0.0127 0.0019  -0.0165 444 PHE C CG  
7895  C CD1 . PHE C 143 ? 0.3684 0.3840 0.3200 -0.0162 -0.0001 -0.0177 444 PHE C CD1 
7896  C CD2 . PHE C 143 ? 0.3521 0.3744 0.3219 -0.0146 0.0032  -0.0187 444 PHE C CD2 
7897  C CE1 . PHE C 143 ? 0.4140 0.4255 0.3589 -0.0215 -0.0010 -0.0212 444 PHE C CE1 
7898  C CE2 . PHE C 143 ? 0.3241 0.3426 0.2874 -0.0203 0.0023  -0.0218 444 PHE C CE2 
7899  C CZ  . PHE C 143 ? 0.3760 0.3886 0.3267 -0.0237 0.0001  -0.0232 444 PHE C CZ  
7900  N N   . ASN C 144 ? 0.3856 0.3915 0.3360 -0.0063 0.0114  -0.0148 445 ASN C N   
7901  C CA  . ASN C 144 ? 0.3388 0.3384 0.2788 -0.0068 0.0152  -0.0176 445 ASN C CA  
7902  C C   . ASN C 144 ? 0.3403 0.3387 0.2844 -0.0038 0.0207  -0.0188 445 ASN C C   
7903  O O   . ASN C 144 ? 0.3036 0.2980 0.2445 -0.0031 0.0237  -0.0224 445 ASN C O   
7904  C CB  . ASN C 144 ? 0.4247 0.4231 0.3551 -0.0077 0.0143  -0.0153 445 ASN C CB  
7905  C CG  . ASN C 144 ? 0.4933 0.4863 0.4122 -0.0080 0.0184  -0.0185 445 ASN C CG  
7906  O OD1 . ASN C 144 ? 0.5943 0.5875 0.5100 -0.0068 0.0223  -0.0174 445 ASN C OD1 
7907  N ND2 . ASN C 144 ? 0.4318 0.4199 0.3438 -0.0097 0.0178  -0.0226 445 ASN C ND2 
7908  N N   . TYR C 145 ? 0.3031 0.3045 0.2540 -0.0019 0.0219  -0.0157 446 TYR C N   
7909  C CA  . TYR C 145 ? 0.3712 0.3729 0.3266 0.0002  0.0265  -0.0166 446 TYR C CA  
7910  C C   . TYR C 145 ? 0.3111 0.3120 0.2724 0.0012  0.0271  -0.0194 446 TYR C C   
7911  O O   . TYR C 145 ? 0.3011 0.3004 0.2619 0.0029  0.0305  -0.0218 446 TYR C O   
7912  C CB  . TYR C 145 ? 0.2858 0.2895 0.2469 0.0009  0.0266  -0.0128 446 TYR C CB  
7913  C CG  . TYR C 145 ? 0.3248 0.3284 0.2798 -0.0002 0.0289  -0.0105 446 TYR C CG  
7914  C CD1 . TYR C 145 ? 0.3146 0.3165 0.2651 -0.0017 0.0261  -0.0065 446 TYR C CD1 
7915  C CD2 . TYR C 145 ? 0.3035 0.3093 0.2572 0.0002  0.0338  -0.0122 446 TYR C CD2 
7916  C CE1 . TYR C 145 ? 0.3070 0.3084 0.2508 -0.0039 0.0285  -0.0041 446 TYR C CE1 
7917  C CE2 . TYR C 145 ? 0.3314 0.3390 0.2801 -0.0017 0.0364  -0.0101 446 TYR C CE2 
7918  C CZ  . TYR C 145 ? 0.3033 0.3083 0.2465 -0.0042 0.0339  -0.0060 446 TYR C CZ  
7919  O OH  . TYR C 145 ? 0.3805 0.3871 0.3177 -0.0071 0.0369  -0.0037 446 TYR C OH  
7920  N N   . ILE C 146 ? 0.2605 0.2633 0.2270 0.0001  0.0238  -0.0190 447 ILE C N   
7921  C CA  . ILE C 146 ? 0.3125 0.3146 0.2840 0.0002  0.0246  -0.0212 447 ILE C CA  
7922  C C   . ILE C 146 ? 0.3438 0.3400 0.3075 -0.0014 0.0249  -0.0247 447 ILE C C   
7923  O O   . ILE C 146 ? 0.2656 0.2576 0.2289 -0.0002 0.0272  -0.0269 447 ILE C O   
7924  C CB  . ILE C 146 ? 0.3293 0.3367 0.3090 -0.0006 0.0216  -0.0198 447 ILE C CB  
7925  C CG1 . ILE C 146 ? 0.3476 0.3577 0.3342 0.0023  0.0222  -0.0170 447 ILE C CG1 
7926  C CG2 . ILE C 146 ? 0.3281 0.3348 0.3110 -0.0020 0.0223  -0.0221 447 ILE C CG2 
7927  C CD1 . ILE C 146 ? 0.3706 0.3865 0.3649 0.0031  0.0194  -0.0155 447 ILE C CD1 
7928  N N   . CYS C 147 ? 0.3651 0.3594 0.3209 -0.0042 0.0222  -0.0254 448 CYS C N   
7929  C CA  . CYS C 147 ? 0.2732 0.2590 0.2189 -0.0061 0.0224  -0.0291 448 CYS C CA  
7930  C C   . CYS C 147 ? 0.3047 0.2849 0.2446 -0.0019 0.0269  -0.0314 448 CYS C C   
7931  O O   . CYS C 147 ? 0.3216 0.2944 0.2576 -0.0007 0.0284  -0.0342 448 CYS C O   
7932  C CB  . CYS C 147 ? 0.3241 0.3085 0.2609 -0.0100 0.0188  -0.0295 448 CYS C CB  
7933  S SG  . CYS C 147 ? 0.4164 0.4081 0.3593 -0.0154 0.0130  -0.0279 448 CYS C SG  
7934  N N   . ASN C 148 ? 0.2767 0.2605 0.2156 0.0004  0.0290  -0.0300 449 ASN C N   
7935  C CA  . ASN C 148 ? 0.3391 0.3211 0.2742 0.0047  0.0337  -0.0320 449 ASN C CA  
7936  C C   . ASN C 148 ? 0.3100 0.2936 0.2533 0.0080  0.0360  -0.0321 449 ASN C C   
7937  O O   . ASN C 148 ? 0.3373 0.3166 0.2771 0.0119  0.0385  -0.0349 449 ASN C O   
7938  C CB  . ASN C 148 ? 0.2802 0.2682 0.2143 0.0053  0.0357  -0.0297 449 ASN C CB  
7939  C CG  . ASN C 148 ? 0.3825 0.3678 0.3057 0.0024  0.0338  -0.0299 449 ASN C CG  
7940  O OD1 . ASN C 148 ? 0.3750 0.3533 0.2901 0.0006  0.0316  -0.0325 449 ASN C OD1 
7941  N ND2 . ASN C 148 ? 0.2924 0.2825 0.2142 0.0016  0.0346  -0.0270 449 ASN C ND2 
7942  N N   . HIS C 149 ? 0.2941 0.2836 0.2479 0.0071  0.0349  -0.0292 450 HIS C N   
7943  C CA  . HIS C 149 ? 0.2869 0.2776 0.2481 0.0093  0.0364  -0.0292 450 HIS C CA  
7944  C C   . HIS C 149 ? 0.2955 0.2782 0.2534 0.0092  0.0354  -0.0318 450 HIS C C   
7945  O O   . HIS C 149 ? 0.2763 0.2555 0.2329 0.0127  0.0373  -0.0335 450 HIS C O   
7946  C CB  . HIS C 149 ? 0.2548 0.2512 0.2256 0.0077  0.0350  -0.0259 450 HIS C CB  
7947  C CG  . HIS C 149 ? 0.3283 0.3256 0.3059 0.0092  0.0360  -0.0259 450 HIS C CG  
7948  N ND1 . HIS C 149 ? 0.2927 0.2948 0.2771 0.0093  0.0367  -0.0236 450 HIS C ND1 
7949  C CD2 . HIS C 149 ? 0.2929 0.2859 0.2703 0.0101  0.0362  -0.0277 450 HIS C CD2 
7950  C CE1 . HIS C 149 ? 0.2712 0.2728 0.2596 0.0104  0.0372  -0.0243 450 HIS C CE1 
7951  N NE2 . HIS C 149 ? 0.2722 0.2684 0.2565 0.0110  0.0370  -0.0266 450 HIS C NE2 
7952  N N   . VAL C 150 ? 0.2784 0.2585 0.2347 0.0049  0.0323  -0.0318 451 VAL C N   
7953  C CA  . VAL C 150 ? 0.2644 0.2364 0.2168 0.0031  0.0313  -0.0339 451 VAL C CA  
7954  C C   . VAL C 150 ? 0.3132 0.2741 0.2536 0.0056  0.0325  -0.0372 451 VAL C C   
7955  O O   . VAL C 150 ? 0.3175 0.2708 0.2548 0.0079  0.0333  -0.0387 451 VAL C O   
7956  C CB  . VAL C 150 ? 0.3156 0.2888 0.2685 -0.0030 0.0277  -0.0333 451 VAL C CB  
7957  C CG1 . VAL C 150 ? 0.2938 0.2567 0.2391 -0.0063 0.0267  -0.0356 451 VAL C CG1 
7958  C CG2 . VAL C 150 ? 0.2746 0.2577 0.2398 -0.0038 0.0271  -0.0305 451 VAL C CG2 
7959  N N   . LYS C 151 ? 0.2877 0.2467 0.2202 0.0056  0.0325  -0.0385 452 LYS C N   
7960  C CA  . LYS C 151 ? 0.3010 0.2483 0.2207 0.0087  0.0339  -0.0423 452 LYS C CA  
7961  C C   . LYS C 151 ? 0.3193 0.2678 0.2407 0.0165  0.0378  -0.0432 452 LYS C C   
7962  O O   . LYS C 151 ? 0.3480 0.2860 0.2623 0.0205  0.0386  -0.0459 452 LYS C O   
7963  C CB  . LYS C 151 ? 0.3090 0.2553 0.2197 0.0073  0.0336  -0.0435 452 LYS C CB  
7964  C CG  . LYS C 151 ? 0.3274 0.2592 0.2223 0.0097  0.0347  -0.0481 452 LYS C CG  
7965  C CD  . LYS C 151 ? 0.3809 0.3121 0.2665 0.0067  0.0337  -0.0490 452 LYS C CD  
7966  C CE  . LYS C 151 ? 0.4948 0.4094 0.3624 0.0077  0.0340  -0.0540 452 LYS C CE  
7967  N NZ  . LYS C 151 ? 0.4659 0.3788 0.3231 0.0032  0.0322  -0.0550 452 LYS C NZ  
7968  N N   . TYR C 152 ? 0.3010 0.2623 0.2317 0.0187  0.0400  -0.0410 453 TYR C N   
7969  C CA  . TYR C 152 ? 0.3392 0.3052 0.2733 0.0255  0.0436  -0.0415 453 TYR C CA  
7970  C C   . TYR C 152 ? 0.3209 0.2849 0.2604 0.0275  0.0428  -0.0410 453 TYR C C   
7971  O O   . TYR C 152 ? 0.3477 0.3076 0.2843 0.0336  0.0442  -0.0429 453 TYR C O   
7972  C CB  . TYR C 152 ? 0.3428 0.3234 0.2857 0.0253  0.0457  -0.0387 453 TYR C CB  
7973  C CG  . TYR C 152 ? 0.3665 0.3552 0.3154 0.0311  0.0489  -0.0388 453 TYR C CG  
7974  C CD1 . TYR C 152 ? 0.4854 0.4777 0.4301 0.0365  0.0527  -0.0410 453 TYR C CD1 
7975  C CD2 . TYR C 152 ? 0.3629 0.3564 0.3216 0.0313  0.0481  -0.0368 453 TYR C CD2 
7976  C CE1 . TYR C 152 ? 0.4612 0.4635 0.4126 0.0419  0.0554  -0.0411 453 TYR C CE1 
7977  C CE2 . TYR C 152 ? 0.3494 0.3516 0.3139 0.0362  0.0504  -0.0368 453 TYR C CE2 
7978  C CZ  . TYR C 152 ? 0.3646 0.3719 0.3259 0.0416  0.0540  -0.0388 453 TYR C CZ  
7979  O OH  . TYR C 152 ? 0.4582 0.4769 0.4264 0.0467  0.0562  -0.0388 453 TYR C OH  
7980  N N   . ALA C 153 ? 0.2964 0.2641 0.2439 0.0228  0.0407  -0.0383 454 ALA C N   
7981  C CA  . ALA C 153 ? 0.3134 0.2800 0.2658 0.0239  0.0401  -0.0374 454 ALA C CA  
7982  C C   . ALA C 153 ? 0.3781 0.3298 0.3206 0.0242  0.0386  -0.0396 454 ALA C C   
7983  O O   . ALA C 153 ? 0.4043 0.3515 0.3456 0.0288  0.0389  -0.0402 454 ALA C O   
7984  C CB  . ALA C 153 ? 0.2557 0.2287 0.2172 0.0187  0.0385  -0.0345 454 ALA C CB  
7985  N N   . THR C 154 ? 0.3697 0.3130 0.3043 0.0193  0.0367  -0.0408 455 THR C N   
7986  C CA  . THR C 154 ? 0.3005 0.2279 0.2243 0.0176  0.0349  -0.0426 455 THR C CA  
7987  C C   . THR C 154 ? 0.3695 0.2851 0.2818 0.0249  0.0363  -0.0458 455 THR C C   
7988  O O   . THR C 154 ? 0.4297 0.3344 0.3364 0.0281  0.0357  -0.0465 455 THR C O   
7989  C CB  . THR C 154 ? 0.3624 0.2856 0.2808 0.0095  0.0324  -0.0430 455 THR C CB  
7990  O OG1 . THR C 154 ? 0.3558 0.2906 0.2857 0.0041  0.0312  -0.0401 455 THR C OG1 
7991  C CG2 . THR C 154 ? 0.3226 0.2276 0.2276 0.0065  0.0305  -0.0450 455 THR C CG2 
7992  N N   . ASN C 155 ? 0.3640 0.2809 0.2718 0.0279  0.0380  -0.0479 456 ASN C N   
7993  C CA  . ASN C 155 ? 0.3347 0.2436 0.2333 0.0368  0.0403  -0.0512 456 ASN C CA  
7994  C C   . ASN C 155 ? 0.4278 0.3144 0.3112 0.0375  0.0382  -0.0536 456 ASN C C   
7995  O O   . ASN C 155 ? 0.4408 0.3196 0.3195 0.0458  0.0390  -0.0550 456 ASN C O   
7996  C CB  . ASN C 155 ? 0.3254 0.2468 0.2347 0.0447  0.0427  -0.0499 456 ASN C CB  
7997  C CG  . ASN C 155 ? 0.4624 0.3812 0.3652 0.0551  0.0457  -0.0533 456 ASN C CG  
7998  O OD1 . ASN C 155 ? 0.4571 0.3705 0.3502 0.0563  0.0473  -0.0563 456 ASN C OD1 
7999  N ND2 . ASN C 155 ? 0.4212 0.3442 0.3291 0.0629  0.0465  -0.0529 456 ASN C ND2 
8000  N N   . LYS C 156 ? 0.3733 0.2496 0.2488 0.0285  0.0353  -0.0539 457 LYS C N   
8001  C CA  . LYS C 156 ? 0.3824 0.2354 0.2413 0.0267  0.0330  -0.0561 457 LYS C CA  
8002  C C   . LYS C 156 ? 0.3909 0.2370 0.2504 0.0288  0.0319  -0.0543 457 LYS C C   
8003  O O   . LYS C 156 ? 0.4839 0.3100 0.3291 0.0325  0.0309  -0.0562 457 LYS C O   
8004  C CB  . LYS C 156 ? 0.5063 0.3440 0.3490 0.0339  0.0344  -0.0608 457 LYS C CB  
8005  C CG  . LYS C 156 ? 0.5324 0.3737 0.3709 0.0306  0.0351  -0.0629 457 LYS C CG  
8006  C CD  . LYS C 156 ? 0.7941 0.6141 0.6115 0.0346  0.0356  -0.0681 457 LYS C CD  
8007  C CE  . LYS C 156 ? 0.9529 0.7730 0.7689 0.0490  0.0398  -0.0707 457 LYS C CE  
8008  N NZ  . LYS C 156 ? 1.0550 0.8727 0.8606 0.0531  0.0427  -0.0750 457 LYS C NZ  
8009  N N   . GLY C 157 ? 0.4246 0.2858 0.2992 0.0265  0.0319  -0.0506 458 GLY C N   
8010  C CA  . GLY C 157 ? 0.4164 0.2729 0.2920 0.0276  0.0308  -0.0485 458 GLY C CA  
8011  C C   . GLY C 157 ? 0.4638 0.3303 0.3485 0.0377  0.0325  -0.0476 458 GLY C C   
8012  O O   . GLY C 157 ? 0.4034 0.2717 0.2930 0.0377  0.0315  -0.0451 458 GLY C O   
8013  N N   . ASN C 158 ? 0.3979 0.2717 0.2849 0.0458  0.0350  -0.0495 459 ASN C N   
8014  C CA  . ASN C 158 ? 0.4358 0.3226 0.3330 0.0549  0.0366  -0.0485 459 ASN C CA  
8015  C C   . ASN C 158 ? 0.3997 0.3091 0.3138 0.0507  0.0380  -0.0459 459 ASN C C   
8016  O O   . ASN C 158 ? 0.4066 0.3290 0.3266 0.0532  0.0407  -0.0465 459 ASN C O   
8017  C CB  . ASN C 158 ? 0.4931 0.3778 0.3844 0.0658  0.0390  -0.0519 459 ASN C CB  
8018  C CG  . ASN C 158 ? 0.5772 0.4757 0.4786 0.0755  0.0402  -0.0509 459 ASN C CG  
8019  O OD1 . ASN C 158 ? 0.5789 0.4847 0.4893 0.0741  0.0386  -0.0477 459 ASN C OD1 
8020  N ND2 . ASN C 158 ? 0.5453 0.4480 0.4452 0.0854  0.0431  -0.0537 459 ASN C ND2 
8021  N N   . LEU C 159 ? 0.3453 0.2587 0.2663 0.0443  0.0364  -0.0429 460 LEU C N   
8022  C CA  . LEU C 159 ? 0.3446 0.2748 0.2787 0.0387  0.0372  -0.0407 460 LEU C CA  
8023  C C   . LEU C 159 ? 0.3557 0.3027 0.3010 0.0439  0.0392  -0.0397 460 LEU C C   
8024  O O   . LEU C 159 ? 0.3330 0.2820 0.2799 0.0505  0.0392  -0.0395 460 LEU C O   
8025  C CB  . LEU C 159 ? 0.3426 0.2730 0.2810 0.0318  0.0354  -0.0382 460 LEU C CB  
8026  C CG  . LEU C 159 ? 0.5102 0.4254 0.4382 0.0256  0.0334  -0.0387 460 LEU C CG  
8027  C CD1 . LEU C 159 ? 0.4736 0.3935 0.4080 0.0186  0.0327  -0.0363 460 LEU C CD1 
8028  C CD2 . LEU C 159 ? 0.4225 0.3330 0.3439 0.0217  0.0332  -0.0406 460 LEU C CD2 
8029  N N   . ARG C 160 ? 0.3154 0.2748 0.2682 0.0404  0.0407  -0.0387 461 ARG C N   
8030  C CA  . ARG C 160 ? 0.2744 0.2502 0.2373 0.0428  0.0427  -0.0374 461 ARG C CA  
8031  C C   . ARG C 160 ? 0.3268 0.3112 0.2987 0.0359  0.0422  -0.0346 461 ARG C C   
8032  O O   . ARG C 160 ? 0.3080 0.2897 0.2784 0.0305  0.0415  -0.0342 461 ARG C O   
8033  C CB  . ARG C 160 ? 0.2963 0.2770 0.2566 0.0459  0.0457  -0.0392 461 ARG C CB  
8034  C CG  . ARG C 160 ? 0.3420 0.3132 0.2922 0.0537  0.0466  -0.0426 461 ARG C CG  
8035  C CD  . ARG C 160 ? 0.3737 0.3512 0.3215 0.0567  0.0502  -0.0446 461 ARG C CD  
8036  N NE  . ARG C 160 ? 0.3990 0.3687 0.3387 0.0511  0.0499  -0.0456 461 ARG C NE  
8037  C CZ  . ARG C 160 ? 0.4830 0.4509 0.4146 0.0537  0.0524  -0.0483 461 ARG C CZ  
8038  N NH1 . ARG C 160 ? 0.3805 0.3547 0.3119 0.0621  0.0559  -0.0504 461 ARG C NH1 
8039  N NH2 . ARG C 160 ? 0.3412 0.3017 0.2648 0.0480  0.0513  -0.0490 461 ARG C NH2 
8040  N N   . SER C 161 ? 0.3098 0.3042 0.2904 0.0361  0.0423  -0.0327 462 SER C N   
8041  C CA  A SER C 161 ? 0.3030 0.3032 0.2905 0.0301  0.0417  -0.0303 462 SER C CA  
8042  C CA  B SER C 161 ? 0.3029 0.3030 0.2904 0.0301  0.0417  -0.0303 462 SER C CA  
8043  C C   . SER C 161 ? 0.3037 0.3112 0.2934 0.0277  0.0434  -0.0294 462 SER C C   
8044  O O   . SER C 161 ? 0.2984 0.3131 0.2885 0.0305  0.0456  -0.0299 462 SER C O   
8045  C CB  A SER C 161 ? 0.2769 0.2842 0.2714 0.0305  0.0410  -0.0287 462 SER C CB  
8046  C CB  B SER C 161 ? 0.2768 0.2841 0.2712 0.0305  0.0410  -0.0288 462 SER C CB  
8047  O OG  A SER C 161 ? 0.2626 0.2822 0.2621 0.0329  0.0427  -0.0283 462 SER C OG  
8048  O OG  B SER C 161 ? 0.2970 0.2968 0.2882 0.0329  0.0393  -0.0293 462 SER C OG  
8049  N N   . ALA C 162 ? 0.2348 0.2410 0.2257 0.0226  0.0423  -0.0280 463 ALA C N   
8050  C CA  . ALA C 162 ? 0.2631 0.2743 0.2544 0.0202  0.0433  -0.0267 463 ALA C CA  
8051  C C   . ALA C 162 ? 0.3101 0.3211 0.3052 0.0157  0.0417  -0.0245 463 ALA C C   
8052  O O   . ALA C 162 ? 0.2948 0.3014 0.2911 0.0146  0.0402  -0.0246 463 ALA C O   
8053  C CB  . ALA C 162 ? 0.2431 0.2493 0.2265 0.0208  0.0437  -0.0284 463 ALA C CB  
8054  N N   . ILE C 163 ? 0.3334 0.3490 0.3297 0.0134  0.0423  -0.0224 464 ILE C N   
8055  C CA  . ILE C 163 ? 0.3261 0.3400 0.3243 0.0101  0.0407  -0.0201 464 ILE C CA  
8056  C C   . ILE C 163 ? 0.2880 0.3025 0.2822 0.0084  0.0407  -0.0186 464 ILE C C   
8057  O O   . ILE C 163 ? 0.2719 0.2908 0.2637 0.0085  0.0429  -0.0185 464 ILE C O   
8058  C CB  . ILE C 163 ? 0.2150 0.2314 0.2179 0.0082  0.0408  -0.0185 464 ILE C CB  
8059  C CG1 . ILE C 163 ? 0.2229 0.2350 0.2263 0.0060  0.0390  -0.0166 464 ILE C CG1 
8060  C CG2 . ILE C 163 ? 0.2280 0.2521 0.2316 0.0070  0.0428  -0.0174 464 ILE C CG2 
8061  C CD1 . ILE C 163 ? 0.2714 0.2822 0.2777 0.0043  0.0387  -0.0158 464 ILE C CD1 
8062  N N   . THR C 164 ? 0.2860 0.2968 0.2794 0.0071  0.0384  -0.0173 465 THR C N   
8063  C CA  . THR C 164 ? 0.3417 0.3521 0.3306 0.0055  0.0376  -0.0152 465 THR C CA  
8064  C C   . THR C 164 ? 0.3607 0.3686 0.3516 0.0039  0.0359  -0.0122 465 THR C C   
8065  O O   . THR C 164 ? 0.3231 0.3285 0.3176 0.0050  0.0341  -0.0123 465 THR C O   
8066  C CB  . THR C 164 ? 0.3405 0.3484 0.3254 0.0058  0.0354  -0.0162 465 THR C CB  
8067  O OG1 . THR C 164 ? 0.3779 0.3855 0.3587 0.0071  0.0371  -0.0191 465 THR C OG1 
8068  C CG2 . THR C 164 ? 0.3170 0.3242 0.2970 0.0041  0.0337  -0.0134 465 THR C CG2 
8069  N N   . ILE C 165 ? 0.2606 0.2689 0.2485 0.0014  0.0367  -0.0095 466 ILE C N   
8070  C CA  . ILE C 165 ? 0.2696 0.2730 0.2575 -0.0003 0.0352  -0.0066 466 ILE C CA  
8071  C C   . ILE C 165 ? 0.3581 0.3571 0.3398 -0.0011 0.0329  -0.0035 466 ILE C C   
8072  O O   . ILE C 165 ? 0.2936 0.2940 0.2696 -0.0036 0.0340  -0.0019 466 ILE C O   
8073  C CB  . ILE C 165 ? 0.3240 0.3295 0.3125 -0.0037 0.0374  -0.0056 466 ILE C CB  
8074  C CG1 . ILE C 165 ? 0.3178 0.3276 0.3125 -0.0024 0.0388  -0.0085 466 ILE C CG1 
8075  C CG2 . ILE C 165 ? 0.3319 0.3293 0.3179 -0.0061 0.0356  -0.0027 466 ILE C CG2 
8076  C CD1 . ILE C 165 ? 0.2664 0.2829 0.2628 -0.0056 0.0411  -0.0080 466 ILE C CD1 
8077  N N   . PHE C 166 ? 0.3656 0.3598 0.3484 0.0014  0.0297  -0.0027 467 PHE C N   
8078  C CA  . PHE C 166 ? 0.3141 0.3038 0.2916 0.0019  0.0264  0.0005  467 PHE C CA  
8079  C C   . PHE C 166 ? 0.3637 0.3446 0.3367 0.0002  0.0255  0.0040  467 PHE C C   
8080  O O   . PHE C 166 ? 0.3303 0.3092 0.3051 -0.0016 0.0273  0.0036  467 PHE C O   
8081  C CB  . PHE C 166 ? 0.2519 0.2429 0.2339 0.0061  0.0232  -0.0005 467 PHE C CB  
8082  C CG  . PHE C 166 ? 0.3101 0.3076 0.2932 0.0062  0.0233  -0.0032 467 PHE C CG  
8083  C CD1 . PHE C 166 ? 0.2727 0.2711 0.2490 0.0044  0.0224  -0.0024 467 PHE C CD1 
8084  C CD2 . PHE C 166 ? 0.3955 0.3970 0.3849 0.0073  0.0243  -0.0066 467 PHE C CD2 
8085  C CE1 . PHE C 166 ? 0.3371 0.3394 0.3125 0.0040  0.0222  -0.0051 467 PHE C CE1 
8086  C CE2 . PHE C 166 ? 0.3871 0.3923 0.3757 0.0065  0.0241  -0.0091 467 PHE C CE2 
8087  C CZ  . PHE C 166 ? 0.2737 0.2789 0.2552 0.0048  0.0230  -0.0085 467 PHE C CZ  
8088  N N   . PRO C 167 ? 0.3506 0.3252 0.3166 0.0003  0.0225  0.0077  468 PRO C N   
8089  C CA  . PRO C 167 ? 0.3529 0.3166 0.3120 -0.0023 0.0217  0.0115  468 PRO C CA  
8090  C C   . PRO C 167 ? 0.3357 0.2923 0.2981 0.0003  0.0211  0.0106  468 PRO C C   
8091  O O   . PRO C 167 ? 0.3350 0.2936 0.3039 0.0059  0.0198  0.0084  468 PRO C O   
8092  C CB  . PRO C 167 ? 0.3245 0.2818 0.2756 -0.0007 0.0175  0.0155  468 PRO C CB  
8093  C CG  . PRO C 167 ? 0.2928 0.2597 0.2444 -0.0005 0.0176  0.0141  468 PRO C CG  
8094  C CD  . PRO C 167 ? 0.3044 0.2806 0.2667 0.0020  0.0195  0.0090  468 PRO C CD  
8095  N N   . GLN C 168 ? 0.3481 0.2965 0.3053 -0.0042 0.0221  0.0123  469 GLN C N   
8096  C CA  . GLN C 168 ? 0.3481 0.2880 0.3062 -0.0027 0.0217  0.0112  469 GLN C CA  
8097  C C   . GLN C 168 ? 0.4128 0.3404 0.3666 0.0034  0.0177  0.0131  469 GLN C C   
8098  O O   . GLN C 168 ? 0.3613 0.2854 0.3097 0.0053  0.0147  0.0164  469 GLN C O   
8099  C CB  . GLN C 168 ? 0.3668 0.3004 0.3191 -0.0104 0.0233  0.0127  469 GLN C CB  
8100  C CG  . GLN C 168 ? 0.4175 0.3400 0.3576 -0.0150 0.0216  0.0178  469 GLN C CG  
8101  C CD  . GLN C 168 ? 0.4219 0.3465 0.3580 -0.0250 0.0244  0.0194  469 GLN C CD  
8102  O OE1 . GLN C 168 ? 0.4561 0.3960 0.3987 -0.0278 0.0278  0.0175  469 GLN C OE1 
8103  N NE2 . GLN C 168 ? 0.4152 0.3247 0.3405 -0.0305 0.0230  0.0228  469 GLN C NE2 
8104  N N   . ARG C 169 ? 0.3651 0.2860 0.3207 0.0069  0.0176  0.0110  470 ARG C N   
8105  C CA  . ARG C 169 ? 0.3736 0.2821 0.3250 0.0139  0.0142  0.0123  470 ARG C CA  
8106  C C   . ARG C 169 ? 0.4132 0.3039 0.3504 0.0103  0.0119  0.0171  470 ARG C C   
8107  O O   . ARG C 169 ? 0.4143 0.3000 0.3454 0.0017  0.0136  0.0183  470 ARG C O   
8108  C CB  . ARG C 169 ? 0.4019 0.3068 0.3572 0.0178  0.0156  0.0084  470 ARG C CB  
8109  C CG  . ARG C 169 ? 0.5184 0.4097 0.4691 0.0262  0.0128  0.0089  470 ARG C CG  
8110  C CD  . ARG C 169 ? 0.5524 0.4448 0.5090 0.0309  0.0151  0.0040  470 ARG C CD  
8111  N NE  . ARG C 169 ? 0.4772 0.3890 0.4471 0.0342  0.0167  0.0010  470 ARG C NE  
8112  C CZ  . ARG C 169 ? 0.7007 0.6181 0.6772 0.0367  0.0195  -0.0033 470 ARG C CZ  
8113  N NH1 . ARG C 169 ? 0.7347 0.6399 0.7056 0.0366  0.0209  -0.0054 470 ARG C NH1 
8114  N NH2 . ARG C 169 ? 0.6358 0.5703 0.6233 0.0385  0.0209  -0.0056 470 ARG C NH2 
8115  N N   . THR C 170 ? 0.4184 0.2997 0.3500 0.0167  0.0077  0.0200  471 THR C N   
8116  C CA  . THR C 170 ? 0.4356 0.2969 0.3517 0.0137  0.0049  0.0250  471 THR C CA  
8117  C C   . THR C 170 ? 0.5035 0.3464 0.4137 0.0212  0.0025  0.0247  471 THR C C   
8118  O O   . THR C 170 ? 0.5468 0.3782 0.4520 0.0178  0.0041  0.0230  471 THR C O   
8119  C CB  . THR C 170 ? 0.4709 0.3328 0.3814 0.0142  0.0016  0.0297  471 THR C CB  
8120  O OG1 . THR C 170 ? 0.5684 0.4388 0.4868 0.0245  -0.0014 0.0288  471 THR C OG1 
8121  C CG2 . THR C 170 ? 0.4496 0.3263 0.3626 0.0057  0.0047  0.0299  471 THR C CG2 
8122  N N   . ASP C 171 ? 0.5619 0.4016 0.4719 0.0317  -0.0016 0.0261  472 ASP C N   
8123  C CA  . ASP C 171 ? 0.5749 0.3985 0.4803 0.0412  -0.0037 0.0252  472 ASP C CA  
8124  C C   . ASP C 171 ? 0.6533 0.4911 0.5734 0.0500  -0.0016 0.0196  472 ASP C C   
8125  O O   . ASP C 171 ? 0.7381 0.5660 0.6565 0.0598  -0.0029 0.0181  472 ASP C O   
8126  C CB  . ASP C 171 ? 0.6257 0.4368 0.5219 0.0489  -0.0096 0.0302  472 ASP C CB  
8127  C CG  . ASP C 171 ? 0.7338 0.5650 0.6404 0.0539  -0.0121 0.0313  472 ASP C CG  
8128  O OD1 . ASP C 171 ? 0.7069 0.5604 0.6285 0.0535  -0.0092 0.0274  472 ASP C OD1 
8129  O OD2 . ASP C 171 ? 0.7954 0.6191 0.6941 0.0579  -0.0173 0.0362  472 ASP C OD2 
8130  N N   . GLY C 172 ? 0.6113 0.4715 0.5452 0.0469  0.0017  0.0164  473 GLY C N   
8131  C CA  . GLY C 172 ? 0.4816 0.3571 0.4293 0.0541  0.0037  0.0116  473 GLY C CA  
8132  C C   . GLY C 172 ? 0.5118 0.4003 0.4679 0.0633  0.0004  0.0125  473 GLY C C   
8133  O O   . GLY C 172 ? 0.5483 0.4526 0.5171 0.0683  0.0022  0.0088  473 GLY C O   
8134  N N   . LYS C 173 ? 0.5799 0.4629 0.5293 0.0651  -0.0045 0.0175  474 LYS C N   
8135  C CA  . LYS C 173 ? 0.5095 0.4052 0.4662 0.0734  -0.0086 0.0190  474 LYS C CA  
8136  C C   . LYS C 173 ? 0.4846 0.3947 0.4443 0.0667  -0.0098 0.0209  474 LYS C C   
8137  O O   . LYS C 173 ? 0.5331 0.4547 0.4981 0.0716  -0.0139 0.0225  474 LYS C O   
8138  C CB  . LYS C 173 ? 0.5653 0.4433 0.5114 0.0825  -0.0141 0.0232  474 LYS C CB  
8139  C CG  . LYS C 173 ? 0.7138 0.5767 0.6563 0.0908  -0.0129 0.0205  474 LYS C CG  
8140  C CD  . LYS C 173 ? 0.8247 0.6609 0.7504 0.0969  -0.0178 0.0250  474 LYS C CD  
8141  C CE  . LYS C 173 ? 0.9142 0.7305 0.8325 0.1023  -0.0156 0.0218  474 LYS C CE  
8142  N NZ  . LYS C 173 ? 0.8843 0.6727 0.7857 0.1106  -0.0207 0.0256  474 LYS C NZ  
8143  N N   . HIS C 174 ? 0.4549 0.3651 0.4114 0.0557  -0.0065 0.0207  475 HIS C N   
8144  C CA  . HIS C 174 ? 0.4275 0.3500 0.3855 0.0490  -0.0067 0.0217  475 HIS C CA  
8145  C C   . HIS C 174 ? 0.4373 0.3718 0.4031 0.0421  -0.0012 0.0173  475 HIS C C   
8146  O O   . HIS C 174 ? 0.4288 0.3664 0.3914 0.0344  0.0005  0.0179  475 HIS C O   
8147  C CB  . HIS C 174 ? 0.4849 0.3942 0.4282 0.0429  -0.0086 0.0268  475 HIS C CB  
8148  C CG  . HIS C 174 ? 0.5909 0.4867 0.5247 0.0496  -0.0146 0.0318  475 HIS C CG  
8149  N ND1 . HIS C 174 ? 0.6560 0.5326 0.5821 0.0548  -0.0159 0.0330  475 HIS C ND1 
8150  C CD2 . HIS C 174 ? 0.5822 0.4797 0.5120 0.0525  -0.0201 0.0358  475 HIS C CD2 
8151  C CE1 . HIS C 174 ? 0.6536 0.5203 0.5714 0.0610  -0.0219 0.0378  475 HIS C CE1 
8152  N NE2 . HIS C 174 ? 0.6269 0.5066 0.5470 0.0596  -0.0247 0.0397  475 HIS C NE2 
8153  N N   . ASP C 175 ? 0.4280 0.3687 0.4033 0.0452  0.0017  0.0129  476 ASP C N   
8154  C CA  . ASP C 175 ? 0.4285 0.3786 0.4102 0.0394  0.0066  0.0089  476 ASP C CA  
8155  C C   . ASP C 175 ? 0.3925 0.3582 0.3798 0.0362  0.0063  0.0081  476 ASP C C   
8156  O O   . ASP C 175 ? 0.3325 0.3073 0.3246 0.0403  0.0031  0.0086  476 ASP C O   
8157  C CB  . ASP C 175 ? 0.4066 0.3611 0.3969 0.0440  0.0092  0.0046  476 ASP C CB  
8158  C CG  . ASP C 175 ? 0.4098 0.3486 0.3937 0.0448  0.0109  0.0039  476 ASP C CG  
8159  O OD1 . ASP C 175 ? 0.4558 0.3798 0.4288 0.0417  0.0096  0.0070  476 ASP C OD1 
8160  O OD2 . ASP C 175 ? 0.4662 0.4072 0.4555 0.0481  0.0134  0.0002  476 ASP C OD2 
8161  N N   . PHE C 176 ? 0.3026 0.2711 0.2889 0.0291  0.0097  0.0067  477 PHE C N   
8162  C CA  . PHE C 176 ? 0.3033 0.2850 0.2953 0.0263  0.0107  0.0043  477 PHE C CA  
8163  C C   . PHE C 176 ? 0.3691 0.3574 0.3700 0.0272  0.0139  0.0000  477 PHE C C   
8164  O O   . PHE C 176 ? 0.3381 0.3208 0.3386 0.0262  0.0168  -0.0014 477 PHE C O   
8165  C CB  . PHE C 176 ? 0.2666 0.2477 0.2528 0.0194  0.0130  0.0045  477 PHE C CB  
8166  C CG  . PHE C 176 ? 0.2763 0.2539 0.2535 0.0176  0.0103  0.0083  477 PHE C CG  
8167  C CD1 . PHE C 176 ? 0.2959 0.2616 0.2646 0.0176  0.0086  0.0123  477 PHE C CD1 
8168  C CD2 . PHE C 176 ? 0.2921 0.2771 0.2680 0.0153  0.0094  0.0078  477 PHE C CD2 
8169  C CE1 . PHE C 176 ? 0.3411 0.3031 0.3003 0.0153  0.0062  0.0162  477 PHE C CE1 
8170  C CE2 . PHE C 176 ? 0.3959 0.3775 0.3624 0.0133  0.0070  0.0112  477 PHE C CE2 
8171  C CZ  . PHE C 176 ? 0.4117 0.3821 0.3699 0.0133  0.0054  0.0155  477 PHE C CZ  
8172  N N   . ARG C 177 ? 0.2566 0.2566 0.2648 0.0284  0.0131  -0.0018 478 ARG C N   
8173  C CA  . ARG C 177 ? 0.3182 0.3250 0.3340 0.0285  0.0160  -0.0055 478 ARG C CA  
8174  C C   . ARG C 177 ? 0.3404 0.3578 0.3595 0.0249  0.0157  -0.0071 478 ARG C C   
8175  O O   . ARG C 177 ? 0.3121 0.3353 0.3316 0.0252  0.0121  -0.0057 478 ARG C O   
8176  C CB  . ARG C 177 ? 0.3439 0.3542 0.3663 0.0352  0.0155  -0.0062 478 ARG C CB  
8177  C CG  . ARG C 177 ? 0.3600 0.3579 0.3784 0.0395  0.0160  -0.0054 478 ARG C CG  
8178  C CD  . ARG C 177 ? 0.3200 0.3108 0.3357 0.0357  0.0201  -0.0076 478 ARG C CD  
8179  N NE  . ARG C 177 ? 0.3547 0.3539 0.3771 0.0349  0.0233  -0.0113 478 ARG C NE  
8180  C CZ  . ARG C 177 ? 0.4263 0.4265 0.4525 0.0394  0.0251  -0.0135 478 ARG C CZ  
8181  N NH1 . ARG C 177 ? 0.3480 0.3410 0.3722 0.0459  0.0239  -0.0127 478 ARG C NH1 
8182  N NH2 . ARG C 177 ? 0.3573 0.3649 0.3884 0.0376  0.0282  -0.0165 478 ARG C NH2 
8183  N N   . VAL C 178 ? 0.3307 0.3493 0.3509 0.0212  0.0190  -0.0100 479 VAL C N   
8184  C CA  . VAL C 178 ? 0.3352 0.3626 0.3591 0.0182  0.0190  -0.0121 479 VAL C CA  
8185  C C   . VAL C 178 ? 0.3175 0.3523 0.3498 0.0209  0.0201  -0.0136 479 VAL C C   
8186  O O   . VAL C 178 ? 0.3320 0.3630 0.3653 0.0222  0.0233  -0.0150 479 VAL C O   
8187  C CB  . VAL C 178 ? 0.3334 0.3572 0.3533 0.0136  0.0219  -0.0142 479 VAL C CB  
8188  C CG1 . VAL C 178 ? 0.2844 0.3145 0.3057 0.0098  0.0214  -0.0161 479 VAL C CG1 
8189  C CG2 . VAL C 178 ? 0.3210 0.3384 0.3330 0.0119  0.0217  -0.0129 479 VAL C CG2 
8190  N N   . TRP C 179 ? 0.3500 0.3961 0.3881 0.0218  0.0176  -0.0133 480 TRP C N   
8191  C CA  . TRP C 179 ? 0.3292 0.3844 0.3759 0.0246  0.0193  -0.0149 480 TRP C CA  
8192  C C   . TRP C 179 ? 0.3171 0.3756 0.3653 0.0191  0.0227  -0.0176 480 TRP C C   
8193  O O   . TRP C 179 ? 0.3316 0.3938 0.3844 0.0208  0.0257  -0.0193 480 TRP C O   
8194  C CB  . TRP C 179 ? 0.2215 0.2903 0.2755 0.0277  0.0155  -0.0135 480 TRP C CB  
8195  C CG  . TRP C 179 ? 0.2377 0.3027 0.2912 0.0356  0.0126  -0.0109 480 TRP C CG  
8196  C CD1 . TRP C 179 ? 0.2592 0.3099 0.3041 0.0371  0.0115  -0.0087 480 TRP C CD1 
8197  C CD2 . TRP C 179 ? 0.2322 0.3076 0.2938 0.0432  0.0104  -0.0100 480 TRP C CD2 
8198  N NE1 . TRP C 179 ? 0.2675 0.3167 0.3131 0.0448  0.0085  -0.0063 480 TRP C NE1 
8199  C CE2 . TRP C 179 ? 0.2448 0.3091 0.3009 0.0494  0.0077  -0.0072 480 TRP C CE2 
8200  C CE3 . TRP C 179 ? 0.2953 0.3889 0.3683 0.0454  0.0105  -0.0113 480 TRP C CE3 
8201  C CZ2 . TRP C 179 ? 0.2721 0.3411 0.3329 0.0588  0.0048  -0.0056 480 TRP C CZ2 
8202  C CZ3 . TRP C 179 ? 0.2671 0.3682 0.3464 0.0549  0.0080  -0.0099 480 TRP C CZ3 
8203  C CH2 . TRP C 179 ? 0.2751 0.3633 0.3481 0.0620  0.0050  -0.0072 480 TRP C CH2 
8204  N N   . ASN C 180 ? 0.3495 0.4053 0.3925 0.0129  0.0223  -0.0182 481 ASN C N   
8205  C CA  . ASN C 180 ? 0.2568 0.3116 0.2984 0.0076  0.0252  -0.0205 481 ASN C CA  
8206  C C   . ASN C 180 ? 0.3028 0.3483 0.3416 0.0093  0.0289  -0.0215 481 ASN C C   
8207  O O   . ASN C 180 ? 0.2631 0.2999 0.2977 0.0116  0.0289  -0.0207 481 ASN C O   
8208  C CB  . ASN C 180 ? 0.2135 0.2628 0.2474 0.0020  0.0238  -0.0209 481 ASN C CB  
8209  C CG  . ASN C 180 ? 0.2535 0.3102 0.2880 -0.0001 0.0196  -0.0198 481 ASN C CG  
8210  O OD1 . ASN C 180 ? 0.2306 0.2881 0.2651 0.0033  0.0168  -0.0178 481 ASN C OD1 
8211  N ND2 . ASN C 180 ? 0.2856 0.3476 0.3202 -0.0064 0.0188  -0.0210 481 ASN C ND2 
8212  N N   . SER C 181 ? 0.2521 0.2998 0.2927 0.0072  0.0319  -0.0233 482 SER C N   
8213  C CA  . SER C 181 ? 0.2778 0.3165 0.3147 0.0081  0.0349  -0.0243 482 SER C CA  
8214  C C   . SER C 181 ? 0.2698 0.2990 0.2990 0.0047  0.0347  -0.0245 482 SER C C   
8215  O O   . SER C 181 ? 0.3377 0.3593 0.3634 0.0064  0.0354  -0.0242 482 SER C O   
8216  C CB  . SER C 181 ? 0.2629 0.3064 0.3029 0.0070  0.0382  -0.0260 482 SER C CB  
8217  O OG  . SER C 181 ? 0.2588 0.3078 0.2988 0.0010  0.0383  -0.0266 482 SER C OG  
8218  N N   . GLN C 182 ? 0.2210 0.2507 0.2472 0.0001  0.0336  -0.0249 483 GLN C N   
8219  C CA  . GLN C 182 ? 0.2663 0.2871 0.2846 -0.0018 0.0330  -0.0252 483 GLN C CA  
8220  C C   . GLN C 182 ? 0.2881 0.3106 0.3040 -0.0041 0.0301  -0.0248 483 GLN C C   
8221  O O   . GLN C 182 ? 0.3336 0.3647 0.3536 -0.0063 0.0285  -0.0245 483 GLN C O   
8222  C CB  . GLN C 182 ? 0.2887 0.3035 0.3017 -0.0055 0.0345  -0.0265 483 GLN C CB  
8223  C CG  . GLN C 182 ? 0.4282 0.4400 0.4414 -0.0041 0.0370  -0.0269 483 GLN C CG  
8224  C CD  . GLN C 182 ? 0.4712 0.4796 0.4798 -0.0089 0.0381  -0.0277 483 GLN C CD  
8225  O OE1 . GLN C 182 ? 0.3763 0.3764 0.3772 -0.0114 0.0371  -0.0281 483 GLN C OE1 
8226  N NE2 . GLN C 182 ? 0.3514 0.3655 0.3639 -0.0102 0.0402  -0.0280 483 GLN C NE2 
8227  N N   . LEU C 183 ? 0.2930 0.3080 0.3021 -0.0037 0.0295  -0.0250 484 LEU C N   
8228  C CA  . LEU C 183 ? 0.3663 0.3816 0.3713 -0.0057 0.0268  -0.0249 484 LEU C CA  
8229  C C   . LEU C 183 ? 0.3884 0.4039 0.3902 -0.0118 0.0255  -0.0261 484 LEU C C   
8230  O O   . LEU C 183 ? 0.3304 0.3514 0.3326 -0.0147 0.0226  -0.0258 484 LEU C O   
8231  C CB  . LEU C 183 ? 0.2587 0.2656 0.2559 -0.0040 0.0273  -0.0254 484 LEU C CB  
8232  C CG  . LEU C 183 ? 0.2248 0.2321 0.2242 0.0004  0.0284  -0.0238 484 LEU C CG  
8233  C CD1 . LEU C 183 ? 0.2499 0.2514 0.2420 0.0016  0.0295  -0.0246 484 LEU C CD1 
8234  C CD2 . LEU C 183 ? 0.2767 0.2902 0.2801 0.0015  0.0262  -0.0216 484 LEU C CD2 
8235  N N   . ILE C 184 ? 0.2320 0.2409 0.2298 -0.0142 0.0273  -0.0274 485 ILE C N   
8236  C CA  . ILE C 184 ? 0.2803 0.2870 0.2732 -0.0211 0.0262  -0.0285 485 ILE C CA  
8237  C C   . ILE C 184 ? 0.3204 0.3318 0.3184 -0.0233 0.0284  -0.0283 485 ILE C C   
8238  O O   . ILE C 184 ? 0.2902 0.2954 0.2864 -0.0211 0.0308  -0.0285 485 ILE C O   
8239  C CB  . ILE C 184 ? 0.3004 0.2914 0.2804 -0.0223 0.0262  -0.0302 485 ILE C CB  
8240  C CG1 . ILE C 184 ? 0.3807 0.3678 0.3553 -0.0197 0.0247  -0.0307 485 ILE C CG1 
8241  C CG2 . ILE C 184 ? 0.2603 0.2465 0.2335 -0.0305 0.0250  -0.0311 485 ILE C CG2 
8242  C CD1 . ILE C 184 ? 0.4648 0.4366 0.4266 -0.0191 0.0251  -0.0328 485 ILE C CD1 
8243  N N   . ARG C 185 ? 0.2735 0.2973 0.2781 -0.0275 0.0276  -0.0279 486 ARG C N   
8244  C CA  . ARG C 185 ? 0.3385 0.3684 0.3471 -0.0313 0.0299  -0.0279 486 ARG C CA  
8245  C C   . ARG C 185 ? 0.3657 0.4045 0.3754 -0.0396 0.0278  -0.0279 486 ARG C C   
8246  O O   . ARG C 185 ? 0.3337 0.3764 0.3434 -0.0412 0.0243  -0.0277 486 ARG C O   
8247  C CB  . ARG C 185 ? 0.2610 0.3026 0.2809 -0.0258 0.0322  -0.0273 486 ARG C CB  
8248  C CG  . ARG C 185 ? 0.2791 0.3136 0.2988 -0.0183 0.0338  -0.0272 486 ARG C CG  
8249  C CD  . ARG C 185 ? 0.2880 0.3304 0.3155 -0.0147 0.0367  -0.0273 486 ARG C CD  
8250  N NE  . ARG C 185 ? 0.4152 0.4569 0.4405 -0.0190 0.0396  -0.0280 486 ARG C NE  
8251  C CZ  . ARG C 185 ? 0.4659 0.5119 0.4952 -0.0166 0.0429  -0.0286 486 ARG C CZ  
8252  N NH1 . ARG C 185 ? 0.3068 0.3572 0.3423 -0.0097 0.0435  -0.0287 486 ARG C NH1 
8253  N NH2 . ARG C 185 ? 0.3797 0.4245 0.4055 -0.0213 0.0456  -0.0292 486 ARG C NH2 
8254  N N   . TYR C 186 ? 0.2439 0.2868 0.2544 -0.0455 0.0300  -0.0280 487 TYR C N   
8255  C CA  . TYR C 186 ? 0.2574 0.3106 0.2696 -0.0549 0.0284  -0.0278 487 TYR C CA  
8256  C C   . TYR C 186 ? 0.2978 0.3744 0.3256 -0.0532 0.0295  -0.0272 487 TYR C C   
8257  O O   . TYR C 186 ? 0.3174 0.3992 0.3518 -0.0474 0.0332  -0.0272 487 TYR C O   
8258  C CB  . TYR C 186 ? 0.2605 0.3036 0.2626 -0.0638 0.0300  -0.0282 487 TYR C CB  
8259  C CG  . TYR C 186 ? 0.3454 0.3646 0.3310 -0.0652 0.0285  -0.0289 487 TYR C CG  
8260  C CD1 . TYR C 186 ? 0.3108 0.3143 0.2876 -0.0635 0.0308  -0.0290 487 TYR C CD1 
8261  C CD2 . TYR C 186 ? 0.3444 0.3563 0.3225 -0.0678 0.0245  -0.0297 487 TYR C CD2 
8262  C CE1 . TYR C 186 ? 0.4242 0.4059 0.3858 -0.0636 0.0292  -0.0298 487 TYR C CE1 
8263  C CE2 . TYR C 186 ? 0.3126 0.3019 0.2748 -0.0682 0.0234  -0.0309 487 TYR C CE2 
8264  C CZ  . TYR C 186 ? 0.3467 0.3212 0.3011 -0.0657 0.0257  -0.0309 487 TYR C CZ  
8265  O OH  . TYR C 186 ? 0.3608 0.3130 0.2995 -0.0647 0.0245  -0.0321 487 TYR C OH  
8266  N N   . ALA C 187 ? 0.3254 0.4164 0.3588 -0.0582 0.0263  -0.0267 488 ALA C N   
8267  C CA  . ALA C 187 ? 0.3147 0.4303 0.3637 -0.0562 0.0269  -0.0260 488 ALA C CA  
8268  C C   . ALA C 187 ? 0.3406 0.4655 0.3934 -0.0615 0.0316  -0.0264 488 ALA C C   
8269  O O   . ALA C 187 ? 0.3050 0.4182 0.3474 -0.0696 0.0333  -0.0267 488 ALA C O   
8270  C CB  . ALA C 187 ? 0.3191 0.4489 0.3726 -0.0616 0.0217  -0.0252 488 ALA C CB  
8271  N N   . GLY C 188 ? 0.2791 0.4250 0.3463 -0.0565 0.0338  -0.0263 489 GLY C N   
8272  C CA  . GLY C 188 ? 0.3298 0.4899 0.4027 -0.0615 0.0387  -0.0267 489 GLY C CA  
8273  C C   . GLY C 188 ? 0.3676 0.5572 0.4568 -0.0613 0.0375  -0.0263 489 GLY C C   
8274  O O   . GLY C 188 ? 0.2884 0.4869 0.3865 -0.0518 0.0349  -0.0258 489 GLY C O   
8275  N N   . TYR C 189 ? 0.4094 0.6144 0.5020 -0.0723 0.0393  -0.0261 490 TYR C N   
8276  C CA  . TYR C 189 ? 0.3193 0.5557 0.4283 -0.0735 0.0383  -0.0256 490 TYR C CA  
8277  C C   . TYR C 189 ? 0.3908 0.6455 0.5077 -0.0765 0.0452  -0.0264 490 TYR C C   
8278  O O   . TYR C 189 ? 0.3867 0.6371 0.4955 -0.0891 0.0478  -0.0263 490 TYR C O   
8279  C CB  . TYR C 189 ? 0.2739 0.5158 0.3804 -0.0866 0.0326  -0.0244 490 TYR C CB  
8280  C CG  . TYR C 189 ? 0.3024 0.5225 0.3968 -0.0862 0.0264  -0.0240 490 TYR C CG  
8281  C CD1 . TYR C 189 ? 0.2532 0.4453 0.3289 -0.0935 0.0260  -0.0245 490 TYR C CD1 
8282  C CD2 . TYR C 189 ? 0.3264 0.5537 0.4275 -0.0783 0.0211  -0.0232 490 TYR C CD2 
8283  C CE1 . TYR C 189 ? 0.3341 0.5072 0.3987 -0.0926 0.0209  -0.0245 490 TYR C CE1 
8284  C CE2 . TYR C 189 ? 0.3119 0.5200 0.4014 -0.0783 0.0159  -0.0230 490 TYR C CE2 
8285  C CZ  . TYR C 189 ? 0.3376 0.5193 0.4092 -0.0854 0.0161  -0.0238 490 TYR C CZ  
8286  O OH  . TYR C 189 ? 0.3559 0.5192 0.4158 -0.0847 0.0115  -0.0240 490 TYR C OH  
8287  N N   . LYS C 190 ? 0.4314 0.7055 0.5630 -0.0650 0.0482  -0.0272 491 LYS C N   
8288  C CA  . LYS C 190 ? 0.3860 0.6832 0.5274 -0.0675 0.0548  -0.0282 491 LYS C CA  
8289  C C   . LYS C 190 ? 0.3975 0.7228 0.5492 -0.0792 0.0527  -0.0270 491 LYS C C   
8290  O O   . LYS C 190 ? 0.4120 0.7528 0.5739 -0.0763 0.0469  -0.0260 491 LYS C O   
8291  C CB  . LYS C 190 ? 0.3510 0.6616 0.5052 -0.0508 0.0584  -0.0299 491 LYS C CB  
8292  C CG  . LYS C 190 ? 0.5532 0.8714 0.7089 -0.0504 0.0675  -0.0319 491 LYS C CG  
8293  C CD  . LYS C 190 ? 0.6907 0.9772 0.8295 -0.0486 0.0706  -0.0329 491 LYS C CD  
8294  C CE  . LYS C 190 ? 0.7685 1.0587 0.9038 -0.0538 0.0790  -0.0344 491 LYS C CE  
8295  N NZ  . LYS C 190 ? 0.8207 1.1364 0.9703 -0.0444 0.0852  -0.0367 491 LYS C NZ  
8296  N N   . GLN C 191 ? 0.2561 0.5876 0.4043 -0.0933 0.0570  -0.0269 492 GLN C N   
8297  C CA  . GLN C 191 ? 0.3581 0.7184 0.5163 -0.1063 0.0558  -0.0257 492 GLN C CA  
8298  C C   . GLN C 191 ? 0.3811 0.7782 0.5598 -0.0999 0.0615  -0.0268 492 GLN C C   
8299  O O   . GLN C 191 ? 0.3293 0.7255 0.5100 -0.0891 0.0681  -0.0288 492 GLN C O   
8300  C CB  . GLN C 191 ? 0.4789 0.8275 0.6223 -0.1258 0.0577  -0.0248 492 GLN C CB  
8301  C CG  . GLN C 191 ? 0.5514 0.8607 0.6726 -0.1308 0.0534  -0.0242 492 GLN C CG  
8302  C CD  . GLN C 191 ? 0.6459 0.9517 0.7640 -0.1370 0.0447  -0.0231 492 GLN C CD  
8303  O OE1 . GLN C 191 ? 0.6033 0.9328 0.7363 -0.1331 0.0406  -0.0227 492 GLN C OE1 
8304  N NE2 . GLN C 191 ? 0.8022 1.0779 0.9000 -0.1466 0.0416  -0.0226 492 GLN C NE2 
8305  N N   . PRO C 192 ? 0.3609 0.7915 0.5550 -0.1059 0.0590  -0.0258 493 PRO C N   
8306  C CA  . PRO C 192 ? 0.3106 0.7795 0.5251 -0.1005 0.0650  -0.0270 493 PRO C CA  
8307  C C   . PRO C 192 ? 0.3741 0.8437 0.5838 -0.1063 0.0752  -0.0284 493 PRO C C   
8308  O O   . PRO C 192 ? 0.2680 0.7548 0.4886 -0.0947 0.0821  -0.0306 493 PRO C O   
8309  C CB  . PRO C 192 ? 0.2606 0.7620 0.4881 -0.1128 0.0601  -0.0251 493 PRO C CB  
8310  C CG  . PRO C 192 ? 0.2906 0.7718 0.5090 -0.1150 0.0497  -0.0234 493 PRO C CG  
8311  C CD  . PRO C 192 ? 0.2402 0.6762 0.4347 -0.1165 0.0501  -0.0237 493 PRO C CD  
8312  N N   . ASP C 193 ? 0.2828 0.7320 0.4748 -0.1234 0.0763  -0.0272 494 ASP C N   
8313  C CA  . ASP C 193 ? 0.3338 0.7847 0.5200 -0.1315 0.0855  -0.0279 494 ASP C CA  
8314  C C   . ASP C 193 ? 0.3198 0.7416 0.4931 -0.1202 0.0903  -0.0298 494 ASP C C   
8315  O O   . ASP C 193 ? 0.3587 0.7752 0.5230 -0.1269 0.0974  -0.0302 494 ASP C O   
8316  C CB  . ASP C 193 ? 0.3071 0.7479 0.4785 -0.1551 0.0842  -0.0255 494 ASP C CB  
8317  C CG  . ASP C 193 ? 0.4059 0.8007 0.5528 -0.1590 0.0795  -0.0245 494 ASP C CG  
8318  O OD1 . ASP C 193 ? 0.4243 0.8037 0.5550 -0.1763 0.0798  -0.0228 494 ASP C OD1 
8319  O OD2 . ASP C 193 ? 0.4404 0.8143 0.5836 -0.1449 0.0756  -0.0253 494 ASP C OD2 
8320  N N   . GLY C 194 ? 0.3128 0.7167 0.4849 -0.1038 0.0866  -0.0308 495 GLY C N   
8321  C CA  . GLY C 194 ? 0.3548 0.7316 0.5152 -0.0933 0.0901  -0.0326 495 GLY C CA  
8322  C C   . GLY C 194 ? 0.4092 0.7462 0.5471 -0.0997 0.0866  -0.0312 495 GLY C C   
8323  O O   . GLY C 194 ? 0.4218 0.7350 0.5508 -0.0896 0.0873  -0.0324 495 GLY C O   
8324  N N   . SER C 195 ? 0.3773 0.7066 0.5058 -0.1162 0.0828  -0.0289 496 SER C N   
8325  C CA  . SER C 195 ? 0.4012 0.6925 0.5086 -0.1208 0.0788  -0.0277 496 SER C CA  
8326  C C   . SER C 195 ? 0.4225 0.6994 0.5299 -0.1096 0.0715  -0.0278 496 SER C C   
8327  O O   . SER C 195 ? 0.4084 0.7041 0.5308 -0.1014 0.0685  -0.0282 496 SER C O   
8328  C CB  . SER C 195 ? 0.3771 0.6625 0.4731 -0.1409 0.0763  -0.0254 496 SER C CB  
8329  O OG  . SER C 195 ? 0.3800 0.6773 0.4833 -0.1454 0.0695  -0.0245 496 SER C OG  
8330  N N   . THR C 196 ? 0.4116 0.6550 0.5018 -0.1091 0.0688  -0.0274 497 THR C N   
8331  C CA  . THR C 196 ? 0.4335 0.6608 0.5213 -0.0998 0.0625  -0.0274 497 THR C CA  
8332  C C   . THR C 196 ? 0.4699 0.6739 0.5414 -0.1104 0.0571  -0.0261 497 THR C C   
8333  O O   . THR C 196 ? 0.5462 0.7312 0.6023 -0.1190 0.0588  -0.0254 497 THR C O   
8334  C CB  . THR C 196 ? 0.5004 0.7097 0.5839 -0.0858 0.0645  -0.0288 497 THR C CB  
8335  O OG1 . THR C 196 ? 0.5009 0.7302 0.5984 -0.0752 0.0692  -0.0304 497 THR C OG1 
8336  C CG2 . THR C 196 ? 0.5474 0.7401 0.6275 -0.0776 0.0583  -0.0285 497 THR C CG2 
8337  N N   . LEU C 197 ? 0.3678 0.5728 0.4419 -0.1098 0.0506  -0.0256 498 LEU C N   
8338  C CA  . LEU C 197 ? 0.3104 0.4915 0.3684 -0.1174 0.0453  -0.0249 498 LEU C CA  
8339  C C   . LEU C 197 ? 0.3379 0.4968 0.3895 -0.1048 0.0428  -0.0256 498 LEU C C   
8340  O O   . LEU C 197 ? 0.3793 0.5473 0.4419 -0.0928 0.0418  -0.0260 498 LEU C O   
8341  C CB  . LEU C 197 ? 0.3766 0.5722 0.4395 -0.1260 0.0396  -0.0242 498 LEU C CB  
8342  C CG  . LEU C 197 ? 0.4439 0.6147 0.4895 -0.1336 0.0337  -0.0240 498 LEU C CG  
8343  C CD1 . LEU C 197 ? 0.4231 0.5700 0.4495 -0.1447 0.0357  -0.0237 498 LEU C CD1 
8344  C CD2 . LEU C 197 ? 0.3752 0.5631 0.4263 -0.1427 0.0278  -0.0235 498 LEU C CD2 
8345  N N   . GLY C 198 ? 0.3185 0.4486 0.3523 -0.1075 0.0420  -0.0256 499 GLY C N   
8346  C CA  . GLY C 198 ? 0.2685 0.3788 0.2964 -0.0962 0.0402  -0.0262 499 GLY C CA  
8347  C C   . GLY C 198 ? 0.3497 0.4577 0.3808 -0.0858 0.0449  -0.0268 499 GLY C C   
8348  O O   . GLY C 198 ? 0.3854 0.4984 0.4169 -0.0888 0.0498  -0.0268 499 GLY C O   
8349  N N   . ASP C 199 ? 0.3020 0.4026 0.3347 -0.0740 0.0435  -0.0273 500 ASP C N   
8350  C CA  . ASP C 199 ? 0.3340 0.4287 0.3674 -0.0644 0.0470  -0.0279 500 ASP C CA  
8351  C C   . ASP C 199 ? 0.3379 0.4542 0.3867 -0.0574 0.0502  -0.0286 500 ASP C C   
8352  O O   . ASP C 199 ? 0.3574 0.4838 0.4159 -0.0502 0.0479  -0.0286 500 ASP C O   
8353  C CB  . ASP C 199 ? 0.3972 0.4751 0.4253 -0.0559 0.0440  -0.0281 500 ASP C CB  
8354  C CG  . ASP C 199 ? 0.4032 0.4714 0.4290 -0.0481 0.0469  -0.0286 500 ASP C CG  
8355  O OD1 . ASP C 199 ? 0.3738 0.4515 0.4054 -0.0461 0.0510  -0.0292 500 ASP C OD1 
8356  O OD2 . ASP C 199 ? 0.3381 0.3897 0.3561 -0.0441 0.0452  -0.0285 500 ASP C OD2 
8357  N N   . PRO C 200 ? 0.3337 0.4562 0.3840 -0.0585 0.0556  -0.0293 501 PRO C N   
8358  C CA  . PRO C 200 ? 0.3224 0.4649 0.3865 -0.0509 0.0593  -0.0305 501 PRO C CA  
8359  C C   . PRO C 200 ? 0.3163 0.4526 0.3834 -0.0375 0.0586  -0.0313 501 PRO C C   
8360  O O   . PRO C 200 ? 0.3177 0.4694 0.3965 -0.0297 0.0596  -0.0321 501 PRO C O   
8361  C CB  . PRO C 200 ? 0.3164 0.4600 0.3765 -0.0553 0.0655  -0.0312 501 PRO C CB  
8362  C CG  . PRO C 200 ? 0.3432 0.4751 0.3906 -0.0686 0.0644  -0.0297 501 PRO C CG  
8363  C CD  . PRO C 200 ? 0.2673 0.3791 0.3058 -0.0674 0.0586  -0.0289 501 PRO C CD  
8364  N N   . ALA C 201 ? 0.3469 0.4613 0.4035 -0.0347 0.0570  -0.0311 502 ALA C N   
8365  C CA  . ALA C 201 ? 0.3830 0.4906 0.4413 -0.0236 0.0562  -0.0316 502 ALA C CA  
8366  C C   . ALA C 201 ? 0.3301 0.4437 0.3954 -0.0185 0.0517  -0.0307 502 ALA C C   
8367  O O   . ALA C 201 ? 0.3476 0.4587 0.4159 -0.0093 0.0511  -0.0309 502 ALA C O   
8368  C CB  . ALA C 201 ? 0.3715 0.4565 0.4176 -0.0231 0.0551  -0.0313 502 ALA C CB  
8369  N N   . ASN C 202 ? 0.2585 0.3785 0.3253 -0.0247 0.0481  -0.0296 503 ASN C N   
8370  C CA  . ASN C 202 ? 0.2917 0.4144 0.3623 -0.0209 0.0431  -0.0284 503 ASN C CA  
8371  C C   . ASN C 202 ? 0.2977 0.4442 0.3813 -0.0207 0.0417  -0.0279 503 ASN C C   
8372  O O   . ASN C 202 ? 0.3101 0.4609 0.3966 -0.0191 0.0368  -0.0266 503 ASN C O   
8373  C CB  . ASN C 202 ? 0.2381 0.3467 0.2982 -0.0273 0.0393  -0.0276 503 ASN C CB  
8374  C CG  . ASN C 202 ? 0.2896 0.3770 0.3391 -0.0244 0.0398  -0.0278 503 ASN C CG  
8375  O OD1 . ASN C 202 ? 0.3680 0.4513 0.4190 -0.0165 0.0409  -0.0280 503 ASN C OD1 
8376  N ND2 . ASN C 202 ? 0.2962 0.3700 0.3347 -0.0306 0.0388  -0.0278 503 ASN C ND2 
8377  N N   . VAL C 203 ? 0.2599 0.4226 0.3511 -0.0220 0.0459  -0.0289 504 VAL C N   
8378  C CA  . VAL C 203 ? 0.2701 0.4590 0.3751 -0.0220 0.0450  -0.0286 504 VAL C CA  
8379  C C   . VAL C 203 ? 0.3566 0.5518 0.4700 -0.0096 0.0420  -0.0279 504 VAL C C   
8380  O O   . VAL C 203 ? 0.2887 0.4963 0.4087 -0.0096 0.0370  -0.0264 504 VAL C O   
8381  C CB  . VAL C 203 ? 0.3267 0.5320 0.4384 -0.0242 0.0514  -0.0301 504 VAL C CB  
8382  C CG1 . VAL C 203 ? 0.3035 0.5383 0.4322 -0.0196 0.0512  -0.0301 504 VAL C CG1 
8383  C CG2 . VAL C 203 ? 0.2813 0.4839 0.3852 -0.0391 0.0531  -0.0298 504 VAL C CG2 
8384  N N   . GLN C 204 ? 0.3485 0.5341 0.4607 0.0008  0.0445  -0.0289 505 GLN C N   
8385  C CA  . GLN C 204 ? 0.3316 0.5204 0.4499 0.0129  0.0417  -0.0282 505 GLN C CA  
8386  C C   . GLN C 204 ? 0.3225 0.5003 0.4353 0.0127  0.0351  -0.0258 505 GLN C C   
8387  O O   . GLN C 204 ? 0.2426 0.4316 0.3623 0.0168  0.0304  -0.0241 505 GLN C O   
8388  C CB  . GLN C 204 ? 0.4373 0.6133 0.5521 0.0227  0.0454  -0.0298 505 GLN C CB  
8389  C CG  . GLN C 204 ? 0.6643 0.8489 0.7876 0.0359  0.0443  -0.0298 505 GLN C CG  
8390  C CD  . GLN C 204 ? 0.7514 0.9154 0.8668 0.0451  0.0455  -0.0306 505 GLN C CD  
8391  O OE1 . GLN C 204 ? 0.6994 0.8461 0.8048 0.0418  0.0482  -0.0317 505 GLN C OE1 
8392  N NE2 . GLN C 204 ? 0.7674 0.9329 0.8869 0.0566  0.0430  -0.0299 505 GLN C NE2 
8393  N N   . PHE C 205 ? 0.2581 0.4145 0.3584 0.0084  0.0347  -0.0256 506 PHE C N   
8394  C CA  . PHE C 205 ? 0.2640 0.4096 0.3579 0.0080  0.0292  -0.0236 506 PHE C CA  
8395  C C   . PHE C 205 ? 0.2790 0.4360 0.3750 0.0000  0.0249  -0.0225 506 PHE C C   
8396  O O   . PHE C 205 ? 0.2359 0.3951 0.3326 0.0022  0.0196  -0.0206 506 PHE C O   
8397  C CB  . PHE C 205 ? 0.3079 0.4309 0.3888 0.0049  0.0304  -0.0240 506 PHE C CB  
8398  C CG  . PHE C 205 ? 0.3453 0.4577 0.4193 0.0047  0.0258  -0.0222 506 PHE C CG  
8399  C CD1 . PHE C 205 ? 0.3640 0.4691 0.4366 0.0126  0.0240  -0.0208 506 PHE C CD1 
8400  C CD2 . PHE C 205 ? 0.3517 0.4607 0.4194 -0.0036 0.0233  -0.0221 506 PHE C CD2 
8401  C CE1 . PHE C 205 ? 0.3666 0.4626 0.4322 0.0119  0.0201  -0.0190 506 PHE C CE1 
8402  C CE2 . PHE C 205 ? 0.3089 0.4084 0.3694 -0.0036 0.0196  -0.0208 506 PHE C CE2 
8403  C CZ  . PHE C 205 ? 0.2984 0.3923 0.3581 0.0040  0.0182  -0.0192 506 PHE C CZ  
8404  N N   . THR C 206 ? 0.2455 0.4088 0.3413 -0.0100 0.0267  -0.0235 507 THR C N   
8405  C CA  . THR C 206 ? 0.2860 0.4614 0.3839 -0.0187 0.0225  -0.0227 507 THR C CA  
8406  C C   . THR C 206 ? 0.3261 0.5256 0.4383 -0.0136 0.0193  -0.0214 507 THR C C   
8407  O O   . THR C 206 ? 0.3529 0.5582 0.4658 -0.0157 0.0133  -0.0198 507 THR C O   
8408  C CB  . THR C 206 ? 0.2161 0.3949 0.3117 -0.0305 0.0257  -0.0239 507 THR C CB  
8409  O OG1 . THR C 206 ? 0.2760 0.4310 0.3575 -0.0340 0.0279  -0.0248 507 THR C OG1 
8410  C CG2 . THR C 206 ? 0.2213 0.4113 0.3175 -0.0414 0.0211  -0.0231 507 THR C CG2 
8411  N N   . GLU C 207 ? 0.2827 0.4964 0.4060 -0.0061 0.0231  -0.0222 508 GLU C N   
8412  C CA  . GLU C 207 ? 0.2837 0.5217 0.4215 0.0005  0.0201  -0.0210 508 GLU C CA  
8413  C C   . GLU C 207 ? 0.2602 0.4905 0.3961 0.0101  0.0144  -0.0188 508 GLU C C   
8414  O O   . GLU C 207 ? 0.2586 0.5033 0.4008 0.0109  0.0085  -0.0168 508 GLU C O   
8415  C CB  . GLU C 207 ? 0.3655 0.6180 0.5142 0.0083  0.0259  -0.0228 508 GLU C CB  
8416  C CG  . GLU C 207 ? 0.4957 0.7653 0.6501 -0.0013 0.0308  -0.0244 508 GLU C CG  
8417  C CD  . GLU C 207 ? 0.6761 0.9554 0.8380 0.0066  0.0380  -0.0267 508 GLU C CD  
8418  O OE1 . GLU C 207 ? 0.6848 0.9555 0.8466 0.0197  0.0391  -0.0273 508 GLU C OE1 
8419  O OE2 . GLU C 207 ? 0.7514 1.0459 0.9181 -0.0009 0.0428  -0.0280 508 GLU C OE2 
8420  N N   . ILE C 208 ? 0.2547 0.4623 0.3814 0.0166  0.0159  -0.0189 509 ILE C N   
8421  C CA  . ILE C 208 ? 0.2166 0.4141 0.3391 0.0243  0.0108  -0.0164 509 ILE C CA  
8422  C C   . ILE C 208 ? 0.2771 0.4711 0.3928 0.0163  0.0049  -0.0147 509 ILE C C   
8423  O O   . ILE C 208 ? 0.3551 0.5560 0.4732 0.0198  -0.0012 -0.0122 509 ILE C O   
8424  C CB  . ILE C 208 ? 0.3266 0.4995 0.4389 0.0299  0.0138  -0.0169 509 ILE C CB  
8425  C CG1 . ILE C 208 ? 0.3734 0.5491 0.4915 0.0390  0.0189  -0.0188 509 ILE C CG1 
8426  C CG2 . ILE C 208 ? 0.2969 0.4576 0.4025 0.0351  0.0086  -0.0140 509 ILE C CG2 
8427  C CD1 . ILE C 208 ? 0.4084 0.5605 0.5161 0.0425  0.0222  -0.0197 509 ILE C CD1 
8428  N N   . CYS C 209 ? 0.3275 0.5097 0.4334 0.0058  0.0065  -0.0160 510 CYS C N   
8429  C CA  . CYS C 209 ? 0.3620 0.5386 0.4593 -0.0021 0.0014  -0.0150 510 CYS C CA  
8430  C C   . CYS C 209 ? 0.3284 0.5277 0.4343 -0.0069 -0.0037 -0.0139 510 CYS C C   
8431  O O   . CYS C 209 ? 0.3291 0.5303 0.4328 -0.0066 -0.0100 -0.0118 510 CYS C O   
8432  C CB  . CYS C 209 ? 0.2561 0.4170 0.3418 -0.0119 0.0045  -0.0170 510 CYS C CB  
8433  S SG  . CYS C 209 ? 0.3011 0.4357 0.3753 -0.0071 0.0086  -0.0178 510 CYS C SG  
8434  N N   . ILE C 210 ? 0.3392 0.5565 0.4546 -0.0122 -0.0012 -0.0152 511 ILE C N   
8435  C CA  . ILE C 210 ? 0.3349 0.5773 0.4603 -0.0174 -0.0061 -0.0141 511 ILE C CA  
8436  C C   . ILE C 210 ? 0.3168 0.5740 0.4527 -0.0057 -0.0109 -0.0116 511 ILE C C   
8437  O O   . ILE C 210 ? 0.3306 0.5977 0.4679 -0.0079 -0.0181 -0.0096 511 ILE C O   
8438  C CB  . ILE C 210 ? 0.3776 0.6388 0.5128 -0.0241 -0.0015 -0.0158 511 ILE C CB  
8439  C CG1 . ILE C 210 ? 0.3815 0.6272 0.5041 -0.0376 0.0015  -0.0177 511 ILE C CG1 
8440  C CG2 . ILE C 210 ? 0.3449 0.6376 0.4945 -0.0273 -0.0063 -0.0145 511 ILE C CG2 
8441  C CD1 . ILE C 210 ? 0.2544 0.5113 0.3829 -0.0435 0.0078  -0.0193 511 ILE C CD1 
8442  N N   . GLN C 211 ? 0.2813 0.5387 0.4234 0.0071  -0.0075 -0.0117 512 GLN C N   
8443  C CA  . GLN C 211 ? 0.3705 0.6397 0.5216 0.0197  -0.0120 -0.0092 512 GLN C CA  
8444  C C   . GLN C 211 ? 0.3941 0.6476 0.5342 0.0221  -0.0186 -0.0064 512 GLN C C   
8445  O O   . GLN C 211 ? 0.3230 0.5893 0.4685 0.0270  -0.0254 -0.0036 512 GLN C O   
8446  C CB  . GLN C 211 ? 0.3487 0.6146 0.5046 0.0330  -0.0067 -0.0103 512 GLN C CB  
8447  C CG  . GLN C 211 ? 0.5333 0.8113 0.6985 0.0474  -0.0109 -0.0081 512 GLN C CG  
8448  C CD  . GLN C 211 ? 0.8058 1.0716 0.9703 0.0605  -0.0059 -0.0093 512 GLN C CD  
8449  O OE1 . GLN C 211 ? 0.8924 1.1415 1.0495 0.0581  0.0005  -0.0118 512 GLN C OE1 
8450  N NE2 . GLN C 211 ? 0.9043 1.1776 1.0756 0.0746  -0.0091 -0.0076 512 GLN C NE2 
8451  N N   . GLN C 212 ? 0.3606 0.5874 0.4852 0.0188  -0.0167 -0.0069 513 GLN C N   
8452  C CA  . GLN C 212 ? 0.3669 0.5776 0.4794 0.0197  -0.0219 -0.0044 513 GLN C CA  
8453  C C   . GLN C 212 ? 0.4380 0.6523 0.5446 0.0084  -0.0273 -0.0039 513 GLN C C   
8454  O O   . GLN C 212 ? 0.5207 0.7216 0.6157 0.0078  -0.0314 -0.0021 513 GLN C O   
8455  C CB  . GLN C 212 ? 0.3724 0.5553 0.4712 0.0201  -0.0171 -0.0054 513 GLN C CB  
8456  C CG  . GLN C 212 ? 0.3529 0.5277 0.4539 0.0311  -0.0128 -0.0055 513 GLN C CG  
8457  C CD  . GLN C 212 ? 0.4898 0.6715 0.5967 0.0430  -0.0174 -0.0025 513 GLN C CD  
8458  O OE1 . GLN C 212 ? 0.5255 0.7177 0.6428 0.0516  -0.0154 -0.0032 513 GLN C OE1 
8459  N NE2 . GLN C 212 ? 0.4235 0.5989 0.5229 0.0441  -0.0237 0.0008  513 GLN C NE2 
8460  N N   . GLY C 213 ? 0.3650 0.5960 0.4781 -0.0013 -0.0274 -0.0055 514 GLY C N   
8461  C CA  . GLY C 213 ? 0.3282 0.5637 0.4357 -0.0126 -0.0333 -0.0052 514 GLY C CA  
8462  C C   . GLY C 213 ? 0.3731 0.5958 0.4696 -0.0259 -0.0300 -0.0082 514 GLY C C   
8463  O O   . GLY C 213 ? 0.3717 0.5964 0.4621 -0.0364 -0.0347 -0.0085 514 GLY C O   
8464  N N   . TRP C 214 ? 0.4120 0.6210 0.5049 -0.0260 -0.0226 -0.0106 515 TRP C N   
8465  C CA  . TRP C 214 ? 0.3448 0.5400 0.4263 -0.0376 -0.0198 -0.0132 515 TRP C CA  
8466  C C   . TRP C 214 ? 0.3766 0.5905 0.4647 -0.0492 -0.0209 -0.0141 515 TRP C C   
8467  O O   . TRP C 214 ? 0.3813 0.6167 0.4845 -0.0473 -0.0190 -0.0138 515 TRP C O   
8468  C CB  . TRP C 214 ? 0.3792 0.5583 0.4570 -0.0344 -0.0120 -0.0151 515 TRP C CB  
8469  C CG  . TRP C 214 ? 0.3520 0.5133 0.4163 -0.0442 -0.0094 -0.0176 515 TRP C CG  
8470  C CD1 . TRP C 214 ? 0.3502 0.4941 0.3991 -0.0493 -0.0118 -0.0184 515 TRP C CD1 
8471  C CD2 . TRP C 214 ? 0.4002 0.5578 0.4638 -0.0493 -0.0038 -0.0195 515 TRP C CD2 
8472  N NE1 . TRP C 214 ? 0.3827 0.5118 0.4215 -0.0567 -0.0083 -0.0208 515 TRP C NE1 
8473  C CE2 . TRP C 214 ? 0.4167 0.5537 0.4641 -0.0571 -0.0036 -0.0213 515 TRP C CE2 
8474  C CE3 . TRP C 214 ? 0.3679 0.5372 0.4421 -0.0478 0.0011  -0.0200 515 TRP C CE3 
8475  C CZ2 . TRP C 214 ? 0.3539 0.4809 0.3952 -0.0633 0.0008  -0.0231 515 TRP C CZ2 
8476  C CZ3 . TRP C 214 ? 0.3908 0.5508 0.4588 -0.0549 0.0057  -0.0217 515 TRP C CZ3 
8477  C CH2 . TRP C 214 ? 0.3823 0.5210 0.4340 -0.0624 0.0053  -0.0230 515 TRP C CH2 
8478  N N   . LYS C 215 ? 0.3288 0.5341 0.4048 -0.0614 -0.0238 -0.0153 516 LYS C N   
8479  C CA  . LYS C 215 ? 0.3262 0.5457 0.4053 -0.0748 -0.0250 -0.0162 516 LYS C CA  
8480  C C   . LYS C 215 ? 0.3651 0.5678 0.4350 -0.0818 -0.0187 -0.0186 516 LYS C C   
8481  O O   . LYS C 215 ? 0.4783 0.6563 0.5307 -0.0866 -0.0186 -0.0203 516 LYS C O   
8482  C CB  . LYS C 215 ? 0.4499 0.6692 0.5199 -0.0849 -0.0327 -0.0160 516 LYS C CB  
8483  C CG  . LYS C 215 ? 0.6046 0.8418 0.6832 -0.0787 -0.0399 -0.0131 516 LYS C CG  
8484  C CD  . LYS C 215 ? 0.7091 0.9813 0.8090 -0.0787 -0.0417 -0.0115 516 LYS C CD  
8485  C CE  . LYS C 215 ? 0.7532 1.0423 0.8643 -0.0667 -0.0474 -0.0082 516 LYS C CE  
8486  N NZ  . LYS C 215 ? 0.6987 0.9839 0.8167 -0.0502 -0.0426 -0.0074 516 LYS C NZ  
8487  N N   . PRO C 216 ? 0.3972 0.6112 0.4771 -0.0821 -0.0133 -0.0190 517 PRO C N   
8488  C CA  . PRO C 216 ? 0.3959 0.5915 0.4660 -0.0868 -0.0072 -0.0209 517 PRO C CA  
8489  C C   . PRO C 216 ? 0.4386 0.6302 0.4987 -0.1037 -0.0088 -0.0220 517 PRO C C   
8490  O O   . PRO C 216 ? 0.4308 0.6445 0.4992 -0.1127 -0.0119 -0.0212 517 PRO C O   
8491  C CB  . PRO C 216 ? 0.3786 0.5910 0.4638 -0.0810 -0.0013 -0.0207 517 PRO C CB  
8492  C CG  . PRO C 216 ? 0.3914 0.6364 0.4939 -0.0813 -0.0048 -0.0191 517 PRO C CG  
8493  C CD  . PRO C 216 ? 0.4394 0.6841 0.5399 -0.0776 -0.0125 -0.0177 517 PRO C CD  
8494  N N   . PRO C 217 ? 0.4887 0.6522 0.5307 -0.1084 -0.0069 -0.0237 518 PRO C N   
8495  C CA  . PRO C 217 ? 0.4395 0.5959 0.4704 -0.1246 -0.0075 -0.0247 518 PRO C CA  
8496  C C   . PRO C 217 ? 0.4121 0.5847 0.4525 -0.1311 -0.0029 -0.0241 518 PRO C C   
8497  O O   . PRO C 217 ? 0.4917 0.6696 0.5285 -0.1461 -0.0044 -0.0241 518 PRO C O   
8498  C CB  . PRO C 217 ? 0.4241 0.5453 0.4343 -0.1238 -0.0055 -0.0266 518 PRO C CB  
8499  C CG  . PRO C 217 ? 0.4299 0.5429 0.4401 -0.1094 -0.0058 -0.0266 518 PRO C CG  
8500  C CD  . PRO C 217 ? 0.4441 0.5812 0.4746 -0.0992 -0.0043 -0.0248 518 PRO C CD  
8501  N N   . ARG C 218 ? 0.4801 0.6608 0.5319 -0.1207 0.0028  -0.0237 519 ARG C N   
8502  C CA  . ARG C 218 ? 0.4536 0.6473 0.5128 -0.1255 0.0085  -0.0234 519 ARG C CA  
8503  C C   . ARG C 218 ? 0.5395 0.7102 0.5806 -0.1378 0.0107  -0.0242 519 ARG C C   
8504  O O   . ARG C 218 ? 0.6158 0.7952 0.6558 -0.1520 0.0110  -0.0237 519 ARG C O   
8505  C CB  . ARG C 218 ? 0.4816 0.7113 0.5584 -0.1317 0.0069  -0.0222 519 ARG C CB  
8506  C CG  . ARG C 218 ? 0.5112 0.7627 0.6056 -0.1179 0.0046  -0.0213 519 ARG C CG  
8507  C CD  . ARG C 218 ? 0.5638 0.8535 0.6796 -0.1185 0.0059  -0.0203 519 ARG C CD  
8508  N NE  . ARG C 218 ? 0.7403 1.0428 0.8708 -0.1006 0.0073  -0.0200 519 ARG C NE  
8509  C CZ  . ARG C 218 ? 0.8094 1.1179 0.9480 -0.0919 0.0144  -0.0208 519 ARG C CZ  
8510  N NH1 . ARG C 218 ? 0.8068 1.1242 0.9567 -0.0755 0.0149  -0.0206 519 ARG C NH1 
8511  N NH2 . ARG C 218 ? 0.8205 1.1252 0.9546 -0.0997 0.0207  -0.0217 519 ARG C NH2 
8512  N N   . GLY C 219 ? 0.5222 0.6630 0.5484 -0.1320 0.0121  -0.0252 520 GLY C N   
8513  C CA  . GLY C 219 ? 0.4815 0.5977 0.4904 -0.1394 0.0148  -0.0257 520 GLY C CA  
8514  C C   . GLY C 219 ? 0.4753 0.5821 0.4847 -0.1286 0.0206  -0.0259 520 GLY C C   
8515  O O   . GLY C 219 ? 0.4015 0.5215 0.4247 -0.1165 0.0228  -0.0257 520 GLY C O   
8516  N N   . ARG C 220 ? 0.4140 0.4965 0.4070 -0.1331 0.0226  -0.0261 521 ARG C N   
8517  C CA  . ARG C 220 ? 0.3866 0.4609 0.3790 -0.1251 0.0279  -0.0260 521 ARG C CA  
8518  C C   . ARG C 220 ? 0.3651 0.4214 0.3527 -0.1115 0.0275  -0.0269 521 ARG C C   
8519  O O   . ARG C 220 ? 0.3353 0.3904 0.3268 -0.1025 0.0313  -0.0268 521 ARG C O   
8520  C CB  . ARG C 220 ? 0.4013 0.4585 0.3782 -0.1359 0.0301  -0.0253 521 ARG C CB  
8521  C CG  . ARG C 220 ? 0.3950 0.4507 0.3733 -0.1308 0.0359  -0.0248 521 ARG C CG  
8522  C CD  . ARG C 220 ? 0.4761 0.5156 0.4379 -0.1434 0.0372  -0.0236 521 ARG C CD  
8523  N NE  . ARG C 220 ? 0.5316 0.5663 0.4911 -0.1401 0.0423  -0.0228 521 ARG C NE  
8524  C CZ  . ARG C 220 ? 0.5992 0.6098 0.5403 -0.1456 0.0428  -0.0217 521 ARG C CZ  
8525  N NH1 . ARG C 220 ? 0.5450 0.5332 0.4684 -0.1540 0.0388  -0.0214 521 ARG C NH1 
8526  N NH2 . ARG C 220 ? 0.6702 0.6777 0.6093 -0.1426 0.0472  -0.0209 521 ARG C NH2 
8527  N N   . PHE C 221 ? 0.4578 0.5008 0.4369 -0.1100 0.0231  -0.0278 522 PHE C N   
8528  C CA  . PHE C 221 ? 0.3377 0.3645 0.3118 -0.0981 0.0229  -0.0287 522 PHE C CA  
8529  C C   . PHE C 221 ? 0.3774 0.4087 0.3543 -0.0945 0.0185  -0.0293 522 PHE C C   
8530  O O   . PHE C 221 ? 0.3801 0.3935 0.3441 -0.0942 0.0159  -0.0306 522 PHE C O   
8531  C CB  . PHE C 221 ? 0.4285 0.4260 0.3829 -0.0998 0.0228  -0.0295 522 PHE C CB  
8532  C CG  . PHE C 221 ? 0.4548 0.4456 0.4041 -0.1038 0.0264  -0.0285 522 PHE C CG  
8533  C CD1 . PHE C 221 ? 0.4701 0.4524 0.4078 -0.1171 0.0259  -0.0279 522 PHE C CD1 
8534  C CD2 . PHE C 221 ? 0.3773 0.3697 0.3324 -0.0947 0.0302  -0.0280 522 PHE C CD2 
8535  C CE1 . PHE C 221 ? 0.5019 0.4771 0.4335 -0.1211 0.0293  -0.0266 522 PHE C CE1 
8536  C CE2 . PHE C 221 ? 0.4309 0.4166 0.3801 -0.0984 0.0333  -0.0270 522 PHE C CE2 
8537  C CZ  . PHE C 221 ? 0.4936 0.4707 0.4310 -0.1115 0.0329  -0.0261 522 PHE C CZ  
8538  N N   . ASP C 222 ? 0.3211 0.3765 0.3144 -0.0915 0.0178  -0.0284 523 ASP C N   
8539  C CA  . ASP C 222 ? 0.3232 0.3845 0.3202 -0.0871 0.0137  -0.0284 523 ASP C CA  
8540  C C   . ASP C 222 ? 0.3353 0.3906 0.3347 -0.0736 0.0153  -0.0284 523 ASP C C   
8541  O O   . ASP C 222 ? 0.3567 0.4226 0.3676 -0.0664 0.0183  -0.0276 523 ASP C O   
8542  C CB  . ASP C 222 ? 0.3346 0.4245 0.3483 -0.0886 0.0118  -0.0271 523 ASP C CB  
8543  C CG  . ASP C 222 ? 0.3671 0.4674 0.3807 -0.1027 0.0102  -0.0269 523 ASP C CG  
8544  O OD1 . ASP C 222 ? 0.4190 0.5015 0.4169 -0.1123 0.0091  -0.0278 523 ASP C OD1 
8545  O OD2 . ASP C 222 ? 0.3614 0.4880 0.3905 -0.1040 0.0100  -0.0258 523 ASP C OD2 
8546  N N   . VAL C 223 ? 0.2991 0.3378 0.2875 -0.0704 0.0135  -0.0294 524 VAL C N   
8547  C CA  . VAL C 223 ? 0.3228 0.3581 0.3141 -0.0587 0.0148  -0.0291 524 VAL C CA  
8548  C C   . VAL C 223 ? 0.2692 0.3237 0.2741 -0.0539 0.0128  -0.0275 524 VAL C C   
8549  O O   . VAL C 223 ? 0.2905 0.3536 0.2966 -0.0579 0.0086  -0.0270 524 VAL C O   
8550  C CB  . VAL C 223 ? 0.3601 0.3764 0.3373 -0.0566 0.0135  -0.0306 524 VAL C CB  
8551  C CG1 . VAL C 223 ? 0.2956 0.3114 0.2767 -0.0458 0.0149  -0.0300 524 VAL C CG1 
8552  C CG2 . VAL C 223 ? 0.2875 0.2837 0.2509 -0.0596 0.0153  -0.0323 524 VAL C CG2 
8553  N N   . LEU C 224 ? 0.2976 0.3581 0.3119 -0.0454 0.0156  -0.0265 525 LEU C N   
8554  C CA  . LEU C 224 ? 0.2831 0.3602 0.3097 -0.0397 0.0138  -0.0248 525 LEU C CA  
8555  C C   . LEU C 224 ? 0.2407 0.3122 0.2627 -0.0352 0.0105  -0.0240 525 LEU C C   
8556  O O   . LEU C 224 ? 0.2856 0.3412 0.2976 -0.0333 0.0116  -0.0248 525 LEU C O   
8557  C CB  . LEU C 224 ? 0.2461 0.3278 0.2817 -0.0319 0.0178  -0.0243 525 LEU C CB  
8558  C CG  . LEU C 224 ? 0.2738 0.3683 0.3175 -0.0353 0.0207  -0.0247 525 LEU C CG  
8559  C CD1 . LEU C 224 ? 0.2321 0.3217 0.2775 -0.0296 0.0257  -0.0253 525 LEU C CD1 
8560  C CD2 . LEU C 224 ? 0.2538 0.3708 0.3109 -0.0336 0.0182  -0.0235 525 LEU C CD2 
8561  N N   . PRO C 225 ? 0.2393 0.3242 0.2684 -0.0331 0.0066  -0.0222 526 PRO C N   
8562  C CA  . PRO C 225 ? 0.2967 0.3759 0.3210 -0.0285 0.0038  -0.0210 526 PRO C CA  
8563  C C   . PRO C 225 ? 0.2550 0.3286 0.2817 -0.0193 0.0069  -0.0200 526 PRO C C   
8564  O O   . PRO C 225 ? 0.2529 0.3308 0.2873 -0.0156 0.0102  -0.0200 526 PRO C O   
8565  C CB  . PRO C 225 ? 0.2669 0.3637 0.2994 -0.0285 -0.0015 -0.0190 526 PRO C CB  
8566  C CG  . PRO C 225 ? 0.3295 0.4424 0.3757 -0.0272 0.0005  -0.0187 526 PRO C CG  
8567  C CD  . PRO C 225 ? 0.2819 0.3885 0.3244 -0.0337 0.0049  -0.0211 526 PRO C CD  
8568  N N   . LEU C 226 ? 0.2703 0.3339 0.2893 -0.0163 0.0061  -0.0193 527 LEU C N   
8569  C CA  . LEU C 226 ? 0.2918 0.3510 0.3126 -0.0086 0.0081  -0.0178 527 LEU C CA  
8570  C C   . LEU C 226 ? 0.3287 0.3987 0.3574 -0.0035 0.0047  -0.0150 527 LEU C C   
8571  O O   . LEU C 226 ? 0.2891 0.3661 0.3176 -0.0052 -0.0001 -0.0137 527 LEU C O   
8572  C CB  . LEU C 226 ? 0.2364 0.2825 0.2463 -0.0078 0.0087  -0.0177 527 LEU C CB  
8573  C CG  . LEU C 226 ? 0.2838 0.3183 0.2860 -0.0102 0.0124  -0.0204 527 LEU C CG  
8574  C CD1 . LEU C 226 ? 0.2890 0.3138 0.2808 -0.0093 0.0128  -0.0206 527 LEU C CD1 
8575  C CD2 . LEU C 226 ? 0.2585 0.2906 0.2655 -0.0071 0.0167  -0.0209 527 LEU C CD2 
8576  N N   . LEU C 227 ? 0.2947 0.3656 0.3298 0.0030  0.0069  -0.0141 528 LEU C N   
8577  C CA  . LEU C 227 ? 0.2900 0.3682 0.3317 0.0098  0.0040  -0.0115 528 LEU C CA  
8578  C C   . LEU C 227 ? 0.2743 0.3390 0.3099 0.0146  0.0053  -0.0099 528 LEU C C   
8579  O O   . LEU C 227 ? 0.2544 0.3130 0.2908 0.0170  0.0094  -0.0109 528 LEU C O   
8580  C CB  . LEU C 227 ? 0.3128 0.4026 0.3661 0.0135  0.0059  -0.0123 528 LEU C CB  
8581  C CG  . LEU C 227 ? 0.3716 0.4793 0.4352 0.0168  0.0019  -0.0109 528 LEU C CG  
8582  C CD1 . LEU C 227 ? 0.3373 0.4508 0.4100 0.0247  0.0047  -0.0113 528 LEU C CD1 
8583  C CD2 . LEU C 227 ? 0.2698 0.3778 0.3302 0.0196  -0.0043 -0.0076 528 LEU C CD2 
8584  N N   . LEU C 228 ? 0.2844 0.3446 0.3134 0.0153  0.0018  -0.0074 529 LEU C N   
8585  C CA  . LEU C 228 ? 0.2603 0.3069 0.2810 0.0169  0.0034  -0.0059 529 LEU C CA  
8586  C C   . LEU C 228 ? 0.3136 0.3582 0.3338 0.0230  -0.0001 -0.0021 529 LEU C C   
8587  O O   . LEU C 228 ? 0.2674 0.3185 0.2882 0.0243  -0.0053 0.0000  529 LEU C O   
8588  C CB  . LEU C 228 ? 0.3175 0.3578 0.3278 0.0115  0.0033  -0.0062 529 LEU C CB  
8589  C CG  . LEU C 228 ? 0.2910 0.3304 0.2995 0.0062  0.0064  -0.0099 529 LEU C CG  
8590  C CD1 . LEU C 228 ? 0.2677 0.2999 0.2650 0.0026  0.0065  -0.0105 529 LEU C CD1 
8591  C CD2 . LEU C 228 ? 0.2686 0.3038 0.2802 0.0072  0.0114  -0.0118 529 LEU C CD2 
8592  N N   . GLN C 229 ? 0.2962 0.3308 0.3143 0.0265  0.0022  -0.0012 530 GLN C N   
8593  C CA  . GLN C 229 ? 0.2826 0.3116 0.2986 0.0326  -0.0008 0.0023  530 GLN C CA  
8594  C C   . GLN C 229 ? 0.3009 0.3154 0.3055 0.0303  0.0003  0.0045  530 GLN C C   
8595  O O   . GLN C 229 ? 0.3019 0.3097 0.3045 0.0278  0.0047  0.0030  530 GLN C O   
8596  C CB  . GLN C 229 ? 0.3225 0.3516 0.3455 0.0391  0.0010  0.0012  530 GLN C CB  
8597  C CG  . GLN C 229 ? 0.3318 0.3488 0.3493 0.0454  -0.0011 0.0045  530 GLN C CG  
8598  C CD  . GLN C 229 ? 0.3807 0.3963 0.4038 0.0524  0.0009  0.0028  530 GLN C CD  
8599  O OE1 . GLN C 229 ? 0.4082 0.4278 0.4367 0.0510  0.0053  -0.0008 530 GLN C OE1 
8600  N NE2 . GLN C 229 ? 0.4513 0.4604 0.4720 0.0603  -0.0025 0.0055  530 GLN C NE2 
8601  N N   . ALA C 230 ? 0.3067 0.3174 0.3038 0.0306  -0.0039 0.0082  531 ALA C N   
8602  C CA  . ALA C 230 ? 0.3511 0.3491 0.3366 0.0277  -0.0031 0.0110  531 ALA C CA  
8603  C C   . ALA C 230 ? 0.3807 0.3686 0.3614 0.0332  -0.0067 0.0152  531 ALA C C   
8604  O O   . ALA C 230 ? 0.3444 0.3363 0.3270 0.0385  -0.0119 0.0174  531 ALA C O   
8605  C CB  . ALA C 230 ? 0.2852 0.2849 0.2628 0.0225  -0.0047 0.0119  531 ALA C CB  
8606  N N   . ASN C 231 ? 0.3743 0.3488 0.3484 0.0319  -0.0041 0.0164  532 ASN C N   
8607  C CA  . ASN C 231 ? 0.3425 0.3027 0.3075 0.0354  -0.0075 0.0210  532 ASN C CA  
8608  C C   . ASN C 231 ? 0.3683 0.3289 0.3393 0.0453  -0.0109 0.0213  532 ASN C C   
8609  O O   . ASN C 231 ? 0.3888 0.3413 0.3537 0.0506  -0.0159 0.0254  532 ASN C O   
8610  C CB  . ASN C 231 ? 0.4248 0.3818 0.3791 0.0327  -0.0114 0.0254  532 ASN C CB  
8611  C CG  . ASN C 231 ? 0.5496 0.4883 0.4904 0.0322  -0.0131 0.0304  532 ASN C CG  
8612  O OD1 . ASN C 231 ? 0.5197 0.4486 0.4561 0.0282  -0.0092 0.0302  532 ASN C OD1 
8613  N ND2 . ASN C 231 ? 0.5516 0.4850 0.4852 0.0361  -0.0192 0.0350  532 ASN C ND2 
8614  N N   . GLY C 232 ? 0.3953 0.3648 0.3779 0.0484  -0.0081 0.0170  533 GLY C N   
8615  C CA  . GLY C 232 ? 0.4387 0.4106 0.4280 0.0583  -0.0103 0.0166  533 GLY C CA  
8616  C C   . GLY C 232 ? 0.4385 0.4254 0.4352 0.0635  -0.0155 0.0178  533 GLY C C   
8617  O O   . GLY C 232 ? 0.4543 0.4449 0.4571 0.0730  -0.0177 0.0178  533 GLY C O   
8618  N N   . ASN C 233 ? 0.3929 0.3887 0.3887 0.0579  -0.0176 0.0187  534 ASN C N   
8619  C CA  . ASN C 233 ? 0.3490 0.3609 0.3522 0.0613  -0.0229 0.0196  534 ASN C CA  
8620  C C   . ASN C 233 ? 0.3558 0.3865 0.3740 0.0614  -0.0202 0.0150  534 ASN C C   
8621  O O   . ASN C 233 ? 0.3429 0.3733 0.3643 0.0577  -0.0143 0.0112  534 ASN C O   
8622  C CB  . ASN C 233 ? 0.4451 0.4589 0.4406 0.0542  -0.0259 0.0217  534 ASN C CB  
8623  C CG  . ASN C 233 ? 0.4480 0.4447 0.4283 0.0542  -0.0291 0.0269  534 ASN C CG  
8624  O OD1 . ASN C 233 ? 0.4387 0.4278 0.4161 0.0621  -0.0332 0.0304  534 ASN C OD1 
8625  N ND2 . ASN C 233 ? 0.4774 0.4675 0.4474 0.0457  -0.0270 0.0275  534 ASN C ND2 
8626  N N   . ASP C 234 ? 0.3573 0.4050 0.3845 0.0652  -0.0248 0.0155  535 ASP C N   
8627  C CA  . ASP C 234 ? 0.4055 0.4724 0.4465 0.0637  -0.0224 0.0115  535 ASP C CA  
8628  C C   . ASP C 234 ? 0.3798 0.4481 0.4183 0.0522  -0.0189 0.0087  535 ASP C C   
8629  O O   . ASP C 234 ? 0.3394 0.4009 0.3681 0.0463  -0.0204 0.0101  535 ASP C O   
8630  C CB  . ASP C 234 ? 0.3970 0.4841 0.4479 0.0678  -0.0285 0.0130  535 ASP C CB  
8631  C CG  . ASP C 234 ? 0.3945 0.4832 0.4502 0.0811  -0.0316 0.0151  535 ASP C CG  
8632  O OD1 . ASP C 234 ? 0.4200 0.5239 0.4825 0.0859  -0.0378 0.0173  535 ASP C OD1 
8633  O OD2 . ASP C 234 ? 0.4327 0.5072 0.4851 0.0869  -0.0282 0.0145  535 ASP C OD2 
8634  N N   . PRO C 235 ? 0.3550 0.4309 0.4013 0.0491  -0.0139 0.0046  536 PRO C N   
8635  C CA  . PRO C 235 ? 0.3020 0.3771 0.3448 0.0390  -0.0108 0.0019  536 PRO C CA  
8636  C C   . PRO C 235 ? 0.2915 0.3796 0.3361 0.0334  -0.0150 0.0020  536 PRO C C   
8637  O O   . PRO C 235 ? 0.2777 0.3814 0.3309 0.0365  -0.0193 0.0030  536 PRO C O   
8638  C CB  . PRO C 235 ? 0.2670 0.3460 0.3174 0.0385  -0.0048 -0.0020 536 PRO C CB  
8639  C CG  . PRO C 235 ? 0.2477 0.3394 0.3094 0.0469  -0.0061 -0.0018 536 PRO C CG  
8640  C CD  . PRO C 235 ? 0.3443 0.4271 0.4010 0.0550  -0.0104 0.0021  536 PRO C CD  
8641  N N   . GLU C 236 ? 0.2528 0.3348 0.2889 0.0251  -0.0140 0.0007  537 GLU C N   
8642  C CA  . GLU C 236 ? 0.2550 0.3457 0.2894 0.0185  -0.0180 0.0003  537 GLU C CA  
8643  C C   . GLU C 236 ? 0.2572 0.3478 0.2907 0.0102  -0.0140 -0.0037 537 GLU C C   
8644  O O   . GLU C 236 ? 0.3004 0.3794 0.3292 0.0088  -0.0087 -0.0057 537 GLU C O   
8645  C CB  . GLU C 236 ? 0.2994 0.3803 0.3207 0.0166  -0.0216 0.0029  537 GLU C CB  
8646  C CG  . GLU C 236 ? 0.3547 0.4323 0.3742 0.0244  -0.0258 0.0075  537 GLU C CG  
8647  C CD  . GLU C 236 ? 0.4587 0.5227 0.4629 0.0221  -0.0275 0.0101  537 GLU C CD  
8648  O OE1 . GLU C 236 ? 0.4323 0.4953 0.4289 0.0149  -0.0280 0.0086  537 GLU C OE1 
8649  O OE2 . GLU C 236 ? 0.4422 0.4958 0.4412 0.0271  -0.0281 0.0134  537 GLU C OE2 
8650  N N   . LEU C 237 ? 0.2686 0.3720 0.3060 0.0045  -0.0169 -0.0048 538 LEU C N   
8651  C CA  . LEU C 237 ? 0.2561 0.3588 0.2916 -0.0040 -0.0140 -0.0084 538 LEU C CA  
8652  C C   . LEU C 237 ? 0.3585 0.4482 0.3793 -0.0104 -0.0146 -0.0096 538 LEU C C   
8653  O O   . LEU C 237 ? 0.3177 0.4069 0.3319 -0.0115 -0.0194 -0.0080 538 LEU C O   
8654  C CB  . LEU C 237 ? 0.2468 0.3687 0.2919 -0.0087 -0.0170 -0.0090 538 LEU C CB  
8655  C CG  . LEU C 237 ? 0.3420 0.4796 0.4025 -0.0035 -0.0153 -0.0088 538 LEU C CG  
8656  C CD1 . LEU C 237 ? 0.2800 0.4387 0.3493 -0.0092 -0.0193 -0.0088 538 LEU C CD1 
8657  C CD2 . LEU C 237 ? 0.4031 0.5338 0.4647 -0.0042 -0.0080 -0.0115 538 LEU C CD2 
8658  N N   . PHE C 238 ? 0.3684 0.4475 0.3836 -0.0142 -0.0097 -0.0127 539 PHE C N   
8659  C CA  . PHE C 238 ? 0.3467 0.4133 0.3477 -0.0199 -0.0096 -0.0148 539 PHE C CA  
8660  C C   . PHE C 238 ? 0.4204 0.4825 0.4192 -0.0259 -0.0065 -0.0182 539 PHE C C   
8661  O O   . PHE C 238 ? 0.3796 0.4405 0.3837 -0.0238 -0.0020 -0.0191 539 PHE C O   
8662  C CB  . PHE C 238 ? 0.2976 0.3501 0.2899 -0.0157 -0.0064 -0.0145 539 PHE C CB  
8663  C CG  . PHE C 238 ? 0.3675 0.4211 0.3595 -0.0105 -0.0091 -0.0108 539 PHE C CG  
8664  C CD1 . PHE C 238 ? 0.3780 0.4335 0.3779 -0.0037 -0.0077 -0.0085 539 PHE C CD1 
8665  C CD2 . PHE C 238 ? 0.2872 0.3383 0.2694 -0.0126 -0.0131 -0.0095 539 PHE C CD2 
8666  C CE1 . PHE C 238 ? 0.3767 0.4308 0.3746 0.0009  -0.0104 -0.0048 539 PHE C CE1 
8667  C CE2 . PHE C 238 ? 0.3769 0.4277 0.3574 -0.0080 -0.0158 -0.0056 539 PHE C CE2 
8668  C CZ  . PHE C 238 ? 0.4698 0.5216 0.4580 -0.0013 -0.0146 -0.0031 539 PHE C CZ  
8669  N N   . GLN C 239 ? 0.3405 0.3987 0.3299 -0.0336 -0.0090 -0.0201 540 GLN C N   
8670  C CA  . GLN C 239 ? 0.4299 0.4801 0.4138 -0.0399 -0.0065 -0.0233 540 GLN C CA  
8671  C C   . GLN C 239 ? 0.3936 0.4247 0.3645 -0.0378 -0.0027 -0.0255 540 GLN C C   
8672  O O   . GLN C 239 ? 0.4168 0.4401 0.3767 -0.0380 -0.0042 -0.0262 540 GLN C O   
8673  C CB  . GLN C 239 ? 0.5041 0.5580 0.4830 -0.0499 -0.0113 -0.0244 540 GLN C CB  
8674  C CG  . GLN C 239 ? 0.5967 0.6364 0.5643 -0.0573 -0.0094 -0.0278 540 GLN C CG  
8675  C CD  . GLN C 239 ? 0.7025 0.7316 0.6540 -0.0643 -0.0133 -0.0300 540 GLN C CD  
8676  O OE1 . GLN C 239 ? 0.6248 0.6434 0.5660 -0.0607 -0.0133 -0.0307 540 GLN C OE1 
8677  N NE2 . GLN C 239 ? 0.6606 0.6922 0.6091 -0.0749 -0.0166 -0.0310 540 GLN C NE2 
8678  N N   . ILE C 240 ? 0.3092 0.3338 0.2817 -0.0351 0.0022  -0.0266 541 ILE C N   
8679  C CA  . ILE C 240 ? 0.3421 0.3499 0.3029 -0.0332 0.0057  -0.0291 541 ILE C CA  
8680  C C   . ILE C 240 ? 0.4597 0.4564 0.4064 -0.0402 0.0036  -0.0320 541 ILE C C   
8681  O O   . ILE C 240 ? 0.4294 0.4279 0.3763 -0.0475 0.0019  -0.0327 541 ILE C O   
8682  C CB  . ILE C 240 ? 0.3098 0.3134 0.2745 -0.0302 0.0103  -0.0297 541 ILE C CB  
8683  C CG1 . ILE C 240 ? 0.3908 0.4044 0.3685 -0.0240 0.0121  -0.0271 541 ILE C CG1 
8684  C CG2 . ILE C 240 ? 0.3314 0.3197 0.2853 -0.0269 0.0134  -0.0319 541 ILE C CG2 
8685  C CD1 . ILE C 240 ? 0.4099 0.4198 0.3911 -0.0218 0.0162  -0.0277 541 ILE C CD1 
8686  N N   . PRO C 241 ? 0.4381 0.4230 0.3717 -0.0389 0.0039  -0.0340 542 PRO C N   
8687  C CA  . PRO C 241 ? 0.4495 0.4207 0.3674 -0.0453 0.0021  -0.0373 542 PRO C CA  
8688  C C   . PRO C 241 ? 0.4160 0.3759 0.3298 -0.0474 0.0046  -0.0393 542 PRO C C   
8689  O O   . PRO C 241 ? 0.3331 0.2874 0.2483 -0.0408 0.0089  -0.0397 542 PRO C O   
8690  C CB  . PRO C 241 ? 0.4006 0.3611 0.3064 -0.0403 0.0040  -0.0393 542 PRO C CB  
8691  C CG  . PRO C 241 ? 0.3951 0.3681 0.3107 -0.0349 0.0043  -0.0359 542 PRO C CG  
8692  C CD  . PRO C 241 ? 0.3973 0.3803 0.3287 -0.0319 0.0061  -0.0333 542 PRO C CD  
8693  N N   . PRO C 242 ? 0.3676 0.3242 0.2761 -0.0568 0.0016  -0.0404 543 PRO C N   
8694  C CA  . PRO C 242 ? 0.3930 0.3395 0.2982 -0.0597 0.0036  -0.0414 543 PRO C CA  
8695  C C   . PRO C 242 ? 0.4809 0.4059 0.3719 -0.0544 0.0068  -0.0444 543 PRO C C   
8696  O O   . PRO C 242 ? 0.5241 0.4426 0.4157 -0.0519 0.0096  -0.0443 543 PRO C O   
8697  C CB  . PRO C 242 ? 0.5051 0.4510 0.4043 -0.0724 -0.0008 -0.0420 543 PRO C CB  
8698  C CG  . PRO C 242 ? 0.5578 0.5235 0.4669 -0.0748 -0.0048 -0.0399 543 PRO C CG  
8699  C CD  . PRO C 242 ? 0.5297 0.4936 0.4364 -0.0660 -0.0040 -0.0401 543 PRO C CD  
8700  N N   . GLU C 243 ? 0.4707 0.3849 0.3490 -0.0518 0.0065  -0.0469 544 GLU C N   
8701  C CA  . GLU C 243 ? 0.4682 0.3633 0.3336 -0.0451 0.0097  -0.0501 544 GLU C CA  
8702  C C   . GLU C 243 ? 0.4559 0.3572 0.3317 -0.0341 0.0143  -0.0487 544 GLU C C   
8703  O O   . GLU C 243 ? 0.4768 0.3653 0.3452 -0.0277 0.0172  -0.0507 544 GLU C O   
8704  C CB  . GLU C 243 ? 0.4844 0.3680 0.3337 -0.0445 0.0088  -0.0535 544 GLU C CB  
8705  C CG  . GLU C 243 ? 0.5145 0.4116 0.3703 -0.0395 0.0095  -0.0522 544 GLU C CG  
8706  C CD  . GLU C 243 ? 0.5525 0.4627 0.4124 -0.0473 0.0044  -0.0502 544 GLU C CD  
8707  O OE1 . GLU C 243 ? 0.5512 0.4661 0.4148 -0.0560 0.0009  -0.0490 544 GLU C OE1 
8708  O OE2 . GLU C 243 ? 0.6386 0.5547 0.4977 -0.0450 0.0040  -0.0497 544 GLU C OE2 
8709  N N   . LEU C 244 ? 0.3937 0.3140 0.2858 -0.0317 0.0149  -0.0454 545 LEU C N   
8710  C CA  . LEU C 244 ? 0.4187 0.3449 0.3205 -0.0230 0.0189  -0.0440 545 LEU C CA  
8711  C C   . LEU C 244 ? 0.4028 0.3328 0.3142 -0.0235 0.0199  -0.0421 545 LEU C C   
8712  O O   . LEU C 244 ? 0.3844 0.3177 0.3027 -0.0169 0.0228  -0.0411 545 LEU C O   
8713  C CB  . LEU C 244 ? 0.3736 0.3155 0.2862 -0.0198 0.0192  -0.0414 545 LEU C CB  
8714  C CG  . LEU C 244 ? 0.4282 0.3691 0.3325 -0.0192 0.0185  -0.0425 545 LEU C CG  
8715  C CD1 . LEU C 244 ? 0.4383 0.3938 0.3538 -0.0162 0.0189  -0.0390 545 LEU C CD1 
8716  C CD2 . LEU C 244 ? 0.4207 0.3487 0.3127 -0.0135 0.0218  -0.0460 545 LEU C CD2 
8717  N N   . VAL C 245 ? 0.3422 0.2724 0.2539 -0.0315 0.0176  -0.0415 546 VAL C N   
8718  C CA  . VAL C 245 ? 0.3787 0.3137 0.2991 -0.0328 0.0188  -0.0397 546 VAL C CA  
8719  C C   . VAL C 245 ? 0.4197 0.3358 0.3272 -0.0345 0.0192  -0.0414 546 VAL C C   
8720  O O   . VAL C 245 ? 0.3947 0.3023 0.2929 -0.0430 0.0169  -0.0423 546 VAL C O   
8721  C CB  . VAL C 245 ? 0.4474 0.3971 0.3776 -0.0403 0.0166  -0.0377 546 VAL C CB  
8722  C CG1 . VAL C 245 ? 0.4217 0.3751 0.3589 -0.0419 0.0185  -0.0362 546 VAL C CG1 
8723  C CG2 . VAL C 245 ? 0.3417 0.3085 0.2841 -0.0369 0.0158  -0.0357 546 VAL C CG2 
8724  N N   . LEU C 246 ? 0.3839 0.2932 0.2901 -0.0267 0.0218  -0.0417 547 LEU C N   
8725  C CA  . LEU C 246 ? 0.4164 0.3065 0.3096 -0.0267 0.0220  -0.0430 547 LEU C CA  
8726  C C   . LEU C 246 ? 0.3982 0.2909 0.2960 -0.0323 0.0221  -0.0408 547 LEU C C   
8727  O O   . LEU C 246 ? 0.3510 0.2568 0.2618 -0.0295 0.0239  -0.0387 547 LEU C O   
8728  C CB  . LEU C 246 ? 0.3950 0.2790 0.2861 -0.0155 0.0244  -0.0440 547 LEU C CB  
8729  C CG  . LEU C 246 ? 0.4831 0.3467 0.3608 -0.0132 0.0242  -0.0450 547 LEU C CG  
8730  C CD1 . LEU C 246 ? 0.5225 0.3665 0.3818 -0.0187 0.0219  -0.0477 547 LEU C CD1 
8731  C CD2 . LEU C 246 ? 0.5322 0.3938 0.4100 -0.0011 0.0264  -0.0460 547 LEU C CD2 
8732  N N   . GLU C 247 ? 0.4037 0.2836 0.2899 -0.0409 0.0202  -0.0412 548 GLU C N   
8733  C CA  . GLU C 247 ? 0.4065 0.2872 0.2945 -0.0473 0.0206  -0.0391 548 GLU C CA  
8734  C C   . GLU C 247 ? 0.4837 0.3398 0.3543 -0.0477 0.0201  -0.0397 548 GLU C C   
8735  O O   . GLU C 247 ? 0.4594 0.2967 0.3148 -0.0455 0.0187  -0.0421 548 GLU C O   
8736  C CB  . GLU C 247 ? 0.4655 0.3567 0.3572 -0.0595 0.0189  -0.0383 548 GLU C CB  
8737  C CG  . GLU C 247 ? 0.4535 0.3689 0.3623 -0.0584 0.0188  -0.0374 548 GLU C CG  
8738  C CD  . GLU C 247 ? 0.5296 0.4578 0.4432 -0.0696 0.0168  -0.0365 548 GLU C CD  
8739  O OE1 . GLU C 247 ? 0.5761 0.4968 0.4795 -0.0771 0.0137  -0.0379 548 GLU C OE1 
8740  O OE2 . GLU C 247 ? 0.5218 0.4681 0.4494 -0.0711 0.0183  -0.0346 548 GLU C OE2 
8741  N N   . VAL C 248 ? 0.4789 0.3345 0.3509 -0.0502 0.0212  -0.0375 549 VAL C N   
8742  C CA  . VAL C 248 ? 0.4359 0.2684 0.2915 -0.0507 0.0205  -0.0372 549 VAL C CA  
8743  C C   . VAL C 248 ? 0.4066 0.2378 0.2581 -0.0643 0.0201  -0.0353 549 VAL C C   
8744  O O   . VAL C 248 ? 0.4448 0.2932 0.3091 -0.0673 0.0221  -0.0331 549 VAL C O   
8745  C CB  . VAL C 248 ? 0.4366 0.2687 0.2961 -0.0403 0.0222  -0.0358 549 VAL C CB  
8746  C CG1 . VAL C 248 ? 0.4717 0.2785 0.3129 -0.0405 0.0208  -0.0351 549 VAL C CG1 
8747  C CG2 . VAL C 248 ? 0.4274 0.2652 0.2934 -0.0277 0.0230  -0.0375 549 VAL C CG2 
8748  N N   . PRO C 249 ? 0.4705 0.2821 0.3043 -0.0732 0.0177  -0.0360 550 PRO C N   
8749  C CA  . PRO C 249 ? 0.4882 0.2971 0.3166 -0.0868 0.0175  -0.0338 550 PRO C CA  
8750  C C   . PRO C 249 ? 0.5090 0.3050 0.3300 -0.0838 0.0186  -0.0315 550 PRO C C   
8751  O O   . PRO C 249 ? 0.5081 0.2840 0.3174 -0.0746 0.0175  -0.0321 550 PRO C O   
8752  C CB  . PRO C 249 ? 0.5356 0.3234 0.3444 -0.0966 0.0141  -0.0355 550 PRO C CB  
8753  C CG  . PRO C 249 ? 0.5866 0.3560 0.3846 -0.0848 0.0128  -0.0385 550 PRO C CG  
8754  C CD  . PRO C 249 ? 0.4840 0.2734 0.3005 -0.0713 0.0151  -0.0390 550 PRO C CD  
8755  N N   . ILE C 250 ? 0.4484 0.2569 0.2766 -0.0909 0.0208  -0.0288 551 ILE C N   
8756  C CA  . ILE C 250 ? 0.5158 0.3157 0.3392 -0.0875 0.0220  -0.0264 551 ILE C CA  
8757  C C   . ILE C 250 ? 0.5355 0.3106 0.3369 -0.0985 0.0204  -0.0247 551 ILE C C   
8758  O O   . ILE C 250 ? 0.5533 0.3334 0.3531 -0.1130 0.0209  -0.0235 551 ILE C O   
8759  C CB  . ILE C 250 ? 0.4747 0.3004 0.3165 -0.0877 0.0258  -0.0247 551 ILE C CB  
8760  C CG1 . ILE C 250 ? 0.4004 0.2485 0.2624 -0.0776 0.0271  -0.0263 551 ILE C CG1 
8761  C CG2 . ILE C 250 ? 0.4835 0.2987 0.3185 -0.0838 0.0266  -0.0223 551 ILE C CG2 
8762  C CD1 . ILE C 250 ? 0.3900 0.2292 0.2504 -0.0635 0.0258  -0.0277 551 ILE C CD1 
8763  N N   . ARG C 251 ? 0.4877 0.2360 0.2719 -0.0916 0.0182  -0.0243 552 ARG C N   
8764  C CA  . ARG C 251 ? 0.5699 0.2905 0.3309 -0.1002 0.0163  -0.0221 552 ARG C CA  
8765  C C   . ARG C 251 ? 0.5211 0.2315 0.2770 -0.0910 0.0163  -0.0196 552 ARG C C   
8766  O O   . ARG C 251 ? 0.5591 0.2828 0.3287 -0.0780 0.0173  -0.0201 552 ARG C O   
8767  C CB  . ARG C 251 ? 0.6065 0.2977 0.3460 -0.1014 0.0125  -0.0243 552 ARG C CB  
8768  C CG  . ARG C 251 ? 0.6309 0.3098 0.3667 -0.0841 0.0108  -0.0271 552 ARG C CG  
8769  C CD  . ARG C 251 ? 0.6236 0.3249 0.3776 -0.0771 0.0120  -0.0305 552 ARG C CD  
8770  N NE  . ARG C 251 ? 0.7131 0.3972 0.4573 -0.0645 0.0103  -0.0338 552 ARG C NE  
8771  C CZ  . ARG C 251 ? 0.7013 0.3999 0.4577 -0.0552 0.0113  -0.0367 552 ARG C CZ  
8772  N NH1 . ARG C 251 ? 0.6547 0.3366 0.4005 -0.0440 0.0102  -0.0398 552 ARG C NH1 
8773  N NH2 . ARG C 251 ? 0.5819 0.3111 0.3605 -0.0568 0.0136  -0.0366 552 ARG C NH2 
8774  N N   . HIS C 252 ? 0.5471 0.2337 0.2826 -0.0984 0.0148  -0.0167 553 HIS C N   
8775  C CA  . HIS C 252 ? 0.6145 0.2906 0.3431 -0.0917 0.0142  -0.0137 553 HIS C CA  
8776  C C   . HIS C 252 ? 0.6896 0.3273 0.3915 -0.0871 0.0096  -0.0130 553 HIS C C   
8777  O O   . HIS C 252 ? 0.6469 0.2623 0.3301 -0.0971 0.0076  -0.0132 553 HIS C O   
8778  C CB  . HIS C 252 ? 0.5543 0.2385 0.2827 -0.1050 0.0170  -0.0100 553 HIS C CB  
8779  C CG  . HIS C 252 ? 0.5955 0.2746 0.3198 -0.0989 0.0169  -0.0068 553 HIS C CG  
8780  N ND1 . HIS C 252 ? 0.6416 0.2887 0.3419 -0.0972 0.0132  -0.0040 553 HIS C ND1 
8781  C CD2 . HIS C 252 ? 0.5879 0.2891 0.3279 -0.0947 0.0198  -0.0059 553 HIS C CD2 
8782  C CE1 . HIS C 252 ? 0.6494 0.3002 0.3513 -0.0922 0.0136  -0.0013 553 HIS C CE1 
8783  N NE2 . HIS C 252 ? 0.5927 0.2760 0.3183 -0.0908 0.0176  -0.0026 553 HIS C NE2 
8784  N N   . PRO C 253 ? 0.6464 0.2751 0.3454 -0.0720 0.0076  -0.0122 554 PRO C N   
8785  C CA  . PRO C 253 ? 0.6646 0.2565 0.3383 -0.0652 0.0030  -0.0118 554 PRO C CA  
8786  C C   . PRO C 253 ? 0.7734 0.3372 0.4219 -0.0779 0.0010  -0.0077 554 PRO C C   
8787  O O   . PRO C 253 ? 0.8096 0.3393 0.4338 -0.0773 -0.0028 -0.0077 554 PRO C O   
8788  C CB  . PRO C 253 ? 0.7292 0.3255 0.4101 -0.0468 0.0017  -0.0112 554 PRO C CB  
8789  C CG  . PRO C 253 ? 0.7060 0.3335 0.4080 -0.0495 0.0052  -0.0094 554 PRO C CG  
8790  C CD  . PRO C 253 ? 0.6246 0.2761 0.3426 -0.0606 0.0092  -0.0116 554 PRO C CD  
8791  N N   . LYS C 254 ? 0.7963 0.3722 0.4487 -0.0896 0.0036  -0.0042 555 LYS C N   
8792  C CA  . LYS C 254 ? 0.8643 0.4143 0.4922 -0.1024 0.0021  0.0003  555 LYS C CA  
8793  C C   . LYS C 254 ? 0.8672 0.4249 0.4942 -0.1241 0.0051  0.0010  555 LYS C C   
8794  O O   . LYS C 254 ? 0.8497 0.3797 0.4524 -0.1368 0.0030  0.0032  555 LYS C O   
8795  C CB  . LYS C 254 ? 1.0345 0.5879 0.6626 -0.0988 0.0023  0.0045  555 LYS C CB  
8796  C CG  . LYS C 254 ? 1.1814 0.7283 0.8102 -0.0781 -0.0013 0.0045  555 LYS C CG  
8797  C CD  . LYS C 254 ? 1.3425 0.8503 0.9458 -0.0704 -0.0068 0.0044  555 LYS C CD  
8798  C CE  . LYS C 254 ? 1.4119 0.9202 1.0213 -0.0480 -0.0099 0.0031  555 LYS C CE  
8799  N NZ  . LYS C 254 ? 1.4116 0.9404 1.0345 -0.0424 -0.0093 0.0059  555 LYS C NZ  
8800  N N   . PHE C 255 ? 0.7756 0.3703 0.4281 -0.1289 0.0098  -0.0007 556 PHE C N   
8801  C CA  . PHE C 255 ? 0.7465 0.3547 0.4016 -0.1490 0.0131  0.0002  556 PHE C CA  
8802  C C   . PHE C 255 ? 0.7402 0.3508 0.3982 -0.1541 0.0121  -0.0037 556 PHE C C   
8803  O O   . PHE C 255 ? 0.6577 0.2945 0.3380 -0.1475 0.0137  -0.0071 556 PHE C O   
8804  C CB  . PHE C 255 ? 0.7681 0.4149 0.4486 -0.1506 0.0187  0.0005  556 PHE C CB  
8805  C CG  . PHE C 255 ? 0.7401 0.3842 0.4162 -0.1474 0.0198  0.0042  556 PHE C CG  
8806  C CD1 . PHE C 255 ? 0.7608 0.4330 0.4585 -0.1389 0.0232  0.0035  556 PHE C CD1 
8807  C CD2 . PHE C 255 ? 0.7602 0.3719 0.4088 -0.1532 0.0170  0.0084  556 PHE C CD2 
8808  C CE1 . PHE C 255 ? 0.7256 0.3948 0.4179 -0.1365 0.0239  0.0068  556 PHE C CE1 
8809  C CE2 . PHE C 255 ? 0.8277 0.4366 0.4711 -0.1505 0.0176  0.0120  556 PHE C CE2 
8810  C CZ  . PHE C 255 ? 0.7387 0.3768 0.4041 -0.1422 0.0211  0.0111  556 PHE C CZ  
8811  N N   . GLU C 256 ? 0.7850 0.3664 0.4185 -0.1662 0.0090  -0.0030 557 GLU C N   
8812  C CA  . GLU C 256 ? 0.8033 0.3829 0.4355 -0.1722 0.0073  -0.0066 557 GLU C CA  
8813  C C   . GLU C 256 ? 0.7699 0.3886 0.4262 -0.1834 0.0111  -0.0077 557 GLU C C   
8814  O O   . GLU C 256 ? 0.7953 0.4263 0.4621 -0.1823 0.0104  -0.0114 557 GLU C O   
8815  C CB  . GLU C 256 ? 0.8746 0.4146 0.4741 -0.1860 0.0033  -0.0052 557 GLU C CB  
8816  C CG  . GLU C 256 ? 1.1902 0.7132 0.7793 -0.1858 -0.0003 -0.0096 557 GLU C CG  
8817  C CD  . GLU C 256 ? 1.4592 0.9911 1.0465 -0.2067 -0.0005 -0.0097 557 GLU C CD  
8818  O OE1 . GLU C 256 ? 1.5102 1.0631 1.1134 -0.2096 0.0001  -0.0133 557 GLU C OE1 
8819  O OE2 . GLU C 256 ? 1.5515 1.0734 1.1229 -0.2189 -0.0015 -0.0060 557 GLU C OE2 
8820  N N   . TRP C 257 ? 0.7454 0.3841 0.4104 -0.1936 0.0152  -0.0046 558 TRP C N   
8821  C CA  . TRP C 257 ? 0.7475 0.4240 0.4349 -0.2044 0.0191  -0.0053 558 TRP C CA  
8822  C C   . TRP C 257 ? 0.6493 0.3603 0.3669 -0.1899 0.0218  -0.0081 558 TRP C C   
8823  O O   . TRP C 257 ? 0.6995 0.4415 0.4366 -0.1959 0.0242  -0.0094 558 TRP C O   
8824  C CB  . TRP C 257 ? 0.7545 0.4416 0.4409 -0.2191 0.0233  -0.0012 558 TRP C CB  
8825  C CG  . TRP C 257 ? 0.6713 0.3546 0.3562 -0.2095 0.0254  0.0014  558 TRP C CG  
8826  C CD1 . TRP C 257 ? 0.6984 0.3491 0.3580 -0.2111 0.0234  0.0051  558 TRP C CD1 
8827  C CD2 . TRP C 257 ? 0.6873 0.3989 0.3955 -0.1970 0.0294  0.0006  558 TRP C CD2 
8828  N NE1 . TRP C 257 ? 0.6891 0.3474 0.3554 -0.2005 0.0257  0.0066  558 TRP C NE1 
8829  C CE2 . TRP C 257 ? 0.7093 0.4046 0.4050 -0.1921 0.0295  0.0038  558 TRP C CE2 
8830  C CE3 . TRP C 257 ? 0.7081 0.4560 0.4453 -0.1897 0.0325  -0.0024 558 TRP C CE3 
8831  C CZ2 . TRP C 257 ? 0.7017 0.4162 0.4130 -0.1809 0.0327  0.0038  558 TRP C CZ2 
8832  C CZ3 . TRP C 257 ? 0.7660 0.5314 0.5180 -0.1782 0.0358  -0.0024 558 TRP C CZ3 
8833  C CH2 . TRP C 257 ? 0.7194 0.4682 0.4584 -0.1743 0.0359  0.0005  558 TRP C CH2 
8834  N N   . PHE C 258 ? 0.6330 0.3398 0.3547 -0.1714 0.0214  -0.0089 559 PHE C N   
8835  C CA  . PHE C 258 ? 0.6210 0.3598 0.3703 -0.1590 0.0242  -0.0110 559 PHE C CA  
8836  C C   . PHE C 258 ? 0.6587 0.4124 0.4207 -0.1577 0.0230  -0.0147 559 PHE C C   
8837  O O   . PHE C 258 ? 0.5380 0.3239 0.3228 -0.1575 0.0258  -0.0157 559 PHE C O   
8838  C CB  . PHE C 258 ? 0.5966 0.3263 0.3462 -0.1404 0.0233  -0.0112 559 PHE C CB  
8839  C CG  . PHE C 258 ? 0.5877 0.3481 0.3623 -0.1305 0.0269  -0.0120 559 PHE C CG  
8840  C CD1 . PHE C 258 ? 0.5880 0.3559 0.3655 -0.1302 0.0300  -0.0096 559 PHE C CD1 
8841  C CD2 . PHE C 258 ? 0.5237 0.3043 0.3173 -0.1221 0.0272  -0.0152 559 PHE C CD2 
8842  C CE1 . PHE C 258 ? 0.5735 0.3673 0.3722 -0.1214 0.0332  -0.0106 559 PHE C CE1 
8843  C CE2 . PHE C 258 ? 0.5703 0.3765 0.3850 -0.1136 0.0303  -0.0159 559 PHE C CE2 
8844  C CZ  . PHE C 258 ? 0.5974 0.4100 0.4146 -0.1132 0.0333  -0.0138 559 PHE C CZ  
8845  N N   . LYS C 259 ? 0.6550 0.3845 0.4013 -0.1572 0.0187  -0.0166 560 LYS C N   
8846  C CA  . LYS C 259 ? 0.6367 0.3781 0.3923 -0.1569 0.0171  -0.0200 560 LYS C CA  
8847  C C   . LYS C 259 ? 0.6372 0.4019 0.4026 -0.1737 0.0183  -0.0196 560 LYS C C   
8848  O O   . LYS C 259 ? 0.6188 0.4058 0.4004 -0.1725 0.0180  -0.0217 560 LYS C O   
8849  C CB  . LYS C 259 ? 0.6549 0.3629 0.3880 -0.1552 0.0124  -0.0223 560 LYS C CB  
8850  C CG  . LYS C 259 ? 0.7142 0.3928 0.4205 -0.1712 0.0099  -0.0206 560 LYS C CG  
8851  C CD  . LYS C 259 ? 0.7308 0.3820 0.4178 -0.1715 0.0053  -0.0240 560 LYS C CD  
8852  C CE  . LYS C 259 ? 0.7913 0.4050 0.4471 -0.1844 0.0022  -0.0222 560 LYS C CE  
8853  N NZ  . LYS C 259 ? 0.9112 0.4998 0.5523 -0.1752 0.0020  -0.0196 560 LYS C NZ  
8854  N N   . ASP C 260 ? 0.6646 0.4254 0.4205 -0.1893 0.0195  -0.0165 561 ASP C N   
8855  C CA  . ASP C 260 ? 0.7829 0.5686 0.5489 -0.2060 0.0209  -0.0158 561 ASP C CA  
8856  C C   . ASP C 260 ? 0.7324 0.5594 0.5280 -0.2013 0.0255  -0.0158 561 ASP C C   
8857  O O   . ASP C 260 ? 0.7223 0.5760 0.5317 -0.2110 0.0264  -0.0160 561 ASP C O   
8858  C CB  . ASP C 260 ? 0.8914 0.6639 0.6399 -0.2243 0.0217  -0.0123 561 ASP C CB  
8859  C CG  . ASP C 260 ? 1.0358 0.7678 0.7536 -0.2329 0.0167  -0.0122 561 ASP C CG  
8860  O OD1 . ASP C 260 ? 0.9584 0.6780 0.6707 -0.2281 0.0126  -0.0154 561 ASP C OD1 
8861  O OD2 . ASP C 260 ? 1.1564 0.8682 0.8548 -0.2446 0.0169  -0.0089 561 ASP C OD2 
8862  N N   . LEU C 261 ? 0.6514 0.4842 0.4565 -0.1868 0.0285  -0.0155 562 LEU C N   
8863  C CA  . LEU C 261 ? 0.6662 0.5352 0.4980 -0.1805 0.0326  -0.0161 562 LEU C CA  
8864  C C   . LEU C 261 ? 0.5931 0.4800 0.4415 -0.1730 0.0306  -0.0190 562 LEU C C   
8865  O O   . LEU C 261 ? 0.5953 0.5131 0.4657 -0.1694 0.0334  -0.0195 562 LEU C O   
8866  C CB  . LEU C 261 ? 0.5837 0.4512 0.4195 -0.1667 0.0355  -0.0155 562 LEU C CB  
8867  C CG  . LEU C 261 ? 0.5992 0.4491 0.4183 -0.1728 0.0373  -0.0123 562 LEU C CG  
8868  C CD1 . LEU C 261 ? 0.5177 0.3616 0.3379 -0.1580 0.0384  -0.0120 562 LEU C CD1 
8869  C CD2 . LEU C 261 ? 0.6020 0.4741 0.4282 -0.1866 0.0421  -0.0105 562 LEU C CD2 
8870  N N   . GLY C 262 ? 0.5507 0.4186 0.3884 -0.1701 0.0260  -0.0209 563 GLY C N   
8871  C CA  . GLY C 262 ? 0.5577 0.4407 0.4087 -0.1638 0.0238  -0.0235 563 GLY C CA  
8872  C C   . GLY C 262 ? 0.5568 0.4517 0.4236 -0.1459 0.0255  -0.0246 563 GLY C C   
8873  O O   . GLY C 262 ? 0.5802 0.4952 0.4627 -0.1411 0.0249  -0.0259 563 GLY C O   
8874  N N   . LEU C 263 ? 0.5063 0.3892 0.3690 -0.1363 0.0274  -0.0239 564 LEU C N   
8875  C CA  . LEU C 263 ? 0.3945 0.2898 0.2723 -0.1210 0.0292  -0.0247 564 LEU C CA  
8876  C C   . LEU C 263 ? 0.4251 0.3076 0.2987 -0.1102 0.0262  -0.0269 564 LEU C C   
8877  O O   . LEU C 263 ? 0.4693 0.3257 0.3246 -0.1102 0.0235  -0.0276 564 LEU C O   
8878  C CB  . LEU C 263 ? 0.5277 0.4171 0.4033 -0.1155 0.0321  -0.0230 564 LEU C CB  
8879  C CG  . LEU C 263 ? 0.5439 0.4464 0.4231 -0.1255 0.0360  -0.0210 564 LEU C CG  
8880  C CD1 . LEU C 263 ? 0.4866 0.3783 0.3591 -0.1208 0.0381  -0.0193 564 LEU C CD1 
8881  C CD2 . LEU C 263 ? 0.5188 0.4547 0.4211 -0.1243 0.0389  -0.0217 564 LEU C CD2 
8882  N N   . LYS C 264 ? 0.4512 0.3517 0.3413 -0.1007 0.0268  -0.0280 565 LYS C N   
8883  C CA  . LYS C 264 ? 0.4347 0.3261 0.3228 -0.0891 0.0251  -0.0298 565 LYS C CA  
8884  C C   . LYS C 264 ? 0.4671 0.3766 0.3727 -0.0780 0.0276  -0.0296 565 LYS C C   
8885  O O   . LYS C 264 ? 0.4490 0.3774 0.3677 -0.0794 0.0302  -0.0285 565 LYS C O   
8886  C CB  . LYS C 264 ? 0.4583 0.3491 0.3435 -0.0924 0.0219  -0.0318 565 LYS C CB  
8887  C CG  . LYS C 264 ? 0.4313 0.3494 0.3338 -0.0960 0.0218  -0.0316 565 LYS C CG  
8888  C CD  . LYS C 264 ? 0.5041 0.4208 0.4037 -0.0961 0.0182  -0.0335 565 LYS C CD  
8889  C CE  . LYS C 264 ? 0.5780 0.5106 0.4829 -0.1080 0.0159  -0.0332 565 LYS C CE  
8890  N NZ  . LYS C 264 ? 0.6752 0.6065 0.5768 -0.1074 0.0121  -0.0351 565 LYS C NZ  
8891  N N   . TRP C 265 ? 0.3930 0.2965 0.2983 -0.0670 0.0269  -0.0309 566 TRP C N   
8892  C CA  . TRP C 265 ? 0.3963 0.3163 0.3173 -0.0576 0.0286  -0.0308 566 TRP C CA  
8893  C C   . TRP C 265 ? 0.4532 0.3689 0.3729 -0.0497 0.0270  -0.0325 566 TRP C C   
8894  O O   . TRP C 265 ? 0.4809 0.3794 0.3869 -0.0497 0.0251  -0.0340 566 TRP C O   
8895  C CB  . TRP C 265 ? 0.3165 0.2354 0.2397 -0.0519 0.0310  -0.0295 566 TRP C CB  
8896  C CG  . TRP C 265 ? 0.3505 0.2887 0.2903 -0.0463 0.0331  -0.0292 566 TRP C CG  
8897  C CD1 . TRP C 265 ? 0.3250 0.2664 0.2710 -0.0365 0.0335  -0.0295 566 TRP C CD1 
8898  C CD2 . TRP C 265 ? 0.2963 0.2530 0.2480 -0.0501 0.0352  -0.0285 566 TRP C CD2 
8899  N NE1 . TRP C 265 ? 0.2950 0.2533 0.2546 -0.0345 0.0355  -0.0290 566 TRP C NE1 
8900  C CE2 . TRP C 265 ? 0.2722 0.2400 0.2356 -0.0419 0.0366  -0.0286 566 TRP C CE2 
8901  C CE3 . TRP C 265 ? 0.3594 0.3246 0.3129 -0.0597 0.0362  -0.0280 566 TRP C CE3 
8902  C CZ2 . TRP C 265 ? 0.2785 0.2638 0.2544 -0.0420 0.0389  -0.0283 566 TRP C CZ2 
8903  C CZ3 . TRP C 265 ? 0.3295 0.3148 0.2968 -0.0596 0.0387  -0.0277 566 TRP C CZ3 
8904  C CH2 . TRP C 265 ? 0.2930 0.2873 0.2710 -0.0502 0.0400  -0.0280 566 TRP C CH2 
8905  N N   . TYR C 266 ? 0.3786 0.3096 0.3117 -0.0431 0.0280  -0.0324 567 TYR C N   
8906  C CA  . TYR C 266 ? 0.3588 0.2881 0.2915 -0.0362 0.0271  -0.0337 567 TYR C CA  
8907  C C   . TYR C 266 ? 0.3758 0.2978 0.3066 -0.0268 0.0284  -0.0338 567 TYR C C   
8908  O O   . TYR C 266 ? 0.3504 0.2743 0.2849 -0.0248 0.0299  -0.0325 567 TYR C O   
8909  C CB  . TYR C 266 ? 0.3271 0.2752 0.2737 -0.0344 0.0271  -0.0331 567 TYR C CB  
8910  C CG  . TYR C 266 ? 0.3257 0.2882 0.2856 -0.0323 0.0293  -0.0315 567 TYR C CG  
8911  C CD1 . TYR C 266 ? 0.3870 0.3516 0.3522 -0.0243 0.0310  -0.0311 567 TYR C CD1 
8912  C CD2 . TYR C 266 ? 0.3248 0.2991 0.2917 -0.0383 0.0299  -0.0306 567 TYR C CD2 
8913  C CE1 . TYR C 266 ? 0.3431 0.3187 0.3186 -0.0224 0.0329  -0.0300 567 TYR C CE1 
8914  C CE2 . TYR C 266 ? 0.3046 0.2911 0.2827 -0.0354 0.0323  -0.0297 567 TYR C CE2 
8915  C CZ  . TYR C 266 ? 0.3222 0.3080 0.3037 -0.0275 0.0336  -0.0294 567 TYR C CZ  
8916  O OH  . TYR C 266 ? 0.3426 0.3382 0.3333 -0.0248 0.0358  -0.0288 567 TYR C OH  
8917  N N   . GLY C 267 ? 0.3429 0.2575 0.2679 -0.0210 0.0278  -0.0354 568 GLY C N   
8918  C CA  . GLY C 267 ? 0.3344 0.2438 0.2580 -0.0120 0.0289  -0.0356 568 GLY C CA  
8919  C C   . GLY C 267 ? 0.3099 0.2344 0.2468 -0.0060 0.0305  -0.0346 568 GLY C C   
8920  O O   . GLY C 267 ? 0.4038 0.3277 0.3422 0.0000  0.0314  -0.0341 568 GLY C O   
8921  N N   . LEU C 268 ? 0.2962 0.2339 0.2423 -0.0076 0.0307  -0.0341 569 LEU C N   
8922  C CA  . LEU C 268 ? 0.3349 0.2840 0.2908 -0.0021 0.0320  -0.0333 569 LEU C CA  
8923  C C   . LEU C 268 ? 0.3629 0.3239 0.3301 -0.0037 0.0328  -0.0314 569 LEU C C   
8924  O O   . LEU C 268 ? 0.3767 0.3457 0.3491 -0.0074 0.0322  -0.0309 569 LEU C O   
8925  C CB  . LEU C 268 ? 0.3548 0.3080 0.3107 -0.0014 0.0315  -0.0340 569 LEU C CB  
8926  C CG  . LEU C 268 ? 0.3351 0.2980 0.2988 0.0035  0.0330  -0.0329 569 LEU C CG  
8927  C CD1 . LEU C 268 ? 0.3319 0.2909 0.2926 0.0100  0.0345  -0.0338 569 LEU C CD1 
8928  C CD2 . LEU C 268 ? 0.3208 0.2884 0.2843 0.0027  0.0323  -0.0330 569 LEU C CD2 
8929  N N   . PRO C 269 ? 0.3332 0.2959 0.3042 -0.0007 0.0340  -0.0306 570 PRO C N   
8930  C CA  . PRO C 269 ? 0.2474 0.2201 0.2280 -0.0014 0.0350  -0.0293 570 PRO C CA  
8931  C C   . PRO C 269 ? 0.2724 0.2529 0.2596 0.0021  0.0353  -0.0286 570 PRO C C   
8932  O O   . PRO C 269 ? 0.3165 0.2967 0.3035 0.0060  0.0358  -0.0285 570 PRO C O   
8933  C CB  . PRO C 269 ? 0.2476 0.2163 0.2267 -0.0001 0.0357  -0.0289 570 PRO C CB  
8934  C CG  . PRO C 269 ? 0.2761 0.2374 0.2490 0.0047  0.0351  -0.0295 570 PRO C CG  
8935  C CD  . PRO C 269 ? 0.2814 0.2368 0.2476 0.0041  0.0342  -0.0309 570 PRO C CD  
8936  N N   . ALA C 270 ? 0.2852 0.2731 0.2779 0.0005  0.0349  -0.0279 571 ALA C N   
8937  C CA  . ALA C 270 ? 0.2837 0.2768 0.2801 0.0029  0.0347  -0.0269 571 ALA C CA  
8938  C C   . ALA C 270 ? 0.3434 0.3433 0.3472 0.0029  0.0348  -0.0257 571 ALA C C   
8939  O O   . ALA C 270 ? 0.3247 0.3293 0.3313 0.0012  0.0336  -0.0254 571 ALA C O   
8940  C CB  . ALA C 270 ? 0.2805 0.2728 0.2727 0.0017  0.0332  -0.0273 571 ALA C CB  
8941  N N   . VAL C 271 ? 0.2748 0.2751 0.2815 0.0049  0.0359  -0.0251 572 VAL C N   
8942  C CA  . VAL C 271 ? 0.2660 0.2701 0.2782 0.0057  0.0363  -0.0245 572 VAL C CA  
8943  C C   . VAL C 271 ? 0.2241 0.2305 0.2381 0.0073  0.0350  -0.0229 572 VAL C C   
8944  O O   . VAL C 271 ? 0.2539 0.2585 0.2658 0.0080  0.0350  -0.0219 572 VAL C O   
8945  C CB  . VAL C 271 ? 0.2492 0.2507 0.2617 0.0066  0.0377  -0.0247 572 VAL C CB  
8946  C CG1 . VAL C 271 ? 0.2579 0.2610 0.2742 0.0083  0.0380  -0.0242 572 VAL C CG1 
8947  C CG2 . VAL C 271 ? 0.2329 0.2319 0.2430 0.0047  0.0387  -0.0260 572 VAL C CG2 
8948  N N   . SER C 272 ? 0.2158 0.2267 0.2337 0.0081  0.0340  -0.0223 573 SER C N   
8949  C CA  . SER C 272 ? 0.3098 0.3219 0.3279 0.0097  0.0321  -0.0204 573 SER C CA  
8950  C C   . SER C 272 ? 0.2791 0.2923 0.3012 0.0130  0.0317  -0.0194 573 SER C C   
8951  O O   . SER C 272 ? 0.3052 0.3186 0.3271 0.0149  0.0296  -0.0175 573 SER C O   
8952  C CB  . SER C 272 ? 0.2806 0.2969 0.2981 0.0079  0.0299  -0.0202 573 SER C CB  
8953  O OG  . SER C 272 ? 0.2366 0.2591 0.2583 0.0066  0.0296  -0.0212 573 SER C OG  
8954  N N   . ASN C 273 ? 0.2360 0.2486 0.2604 0.0142  0.0336  -0.0208 574 ASN C N   
8955  C CA  . ASN C 273 ? 0.2133 0.2258 0.2405 0.0184  0.0335  -0.0204 574 ASN C CA  
8956  C C   . ASN C 273 ? 0.2998 0.3033 0.3234 0.0192  0.0346  -0.0204 574 ASN C C   
8957  O O   . ASN C 273 ? 0.2947 0.2953 0.3188 0.0229  0.0350  -0.0207 574 ASN C O   
8958  C CB  . ASN C 273 ? 0.2577 0.2779 0.2905 0.0197  0.0350  -0.0222 574 ASN C CB  
8959  C CG  . ASN C 273 ? 0.3411 0.3600 0.3727 0.0169  0.0380  -0.0243 574 ASN C CG  
8960  O OD1 . ASN C 273 ? 0.2804 0.2929 0.3073 0.0145  0.0385  -0.0245 574 ASN C OD1 
8961  N ND2 . ASN C 273 ? 0.3104 0.3361 0.3461 0.0174  0.0400  -0.0259 574 ASN C ND2 
8962  N N   . MET C 274 ? 0.2361 0.2352 0.2557 0.0161  0.0350  -0.0201 575 MET C N   
8963  C CA  . MET C 274 ? 0.2456 0.2370 0.2615 0.0156  0.0357  -0.0200 575 MET C CA  
8964  C C   . MET C 274 ? 0.2995 0.2857 0.3117 0.0151  0.0340  -0.0174 575 MET C C   
8965  O O   . MET C 274 ? 0.3465 0.3350 0.3583 0.0152  0.0324  -0.0156 575 MET C O   
8966  C CB  . MET C 274 ? 0.2500 0.2415 0.2645 0.0122  0.0370  -0.0212 575 MET C CB  
8967  C CG  . MET C 274 ? 0.2872 0.2804 0.3031 0.0124  0.0387  -0.0236 575 MET C CG  
8968  S SD  . MET C 274 ? 0.3193 0.3111 0.3323 0.0093  0.0393  -0.0244 575 MET C SD  
8969  C CE  . MET C 274 ? 0.2602 0.2447 0.2697 0.0087  0.0395  -0.0248 575 MET C CE  
8970  N N   . LEU C 275 ? 0.2993 0.2775 0.3074 0.0140  0.0341  -0.0172 576 LEU C N   
8971  C CA  . LEU C 275 ? 0.2695 0.2406 0.2724 0.0124  0.0326  -0.0145 576 LEU C CA  
8972  C C   . LEU C 275 ? 0.3426 0.3135 0.3431 0.0069  0.0334  -0.0141 576 LEU C C   
8973  O O   . LEU C 275 ? 0.3449 0.3147 0.3453 0.0054  0.0343  -0.0159 576 LEU C O   
8974  C CB  . LEU C 275 ? 0.3430 0.3032 0.3418 0.0155  0.0318  -0.0143 576 LEU C CB  
8975  C CG  . LEU C 275 ? 0.4410 0.3908 0.4323 0.0139  0.0298  -0.0110 576 LEU C CG  
8976  C CD1 . LEU C 275 ? 0.3864 0.3276 0.3751 0.0204  0.0280  -0.0104 576 LEU C CD1 
8977  C CD2 . LEU C 275 ? 0.3567 0.2986 0.3421 0.0080  0.0301  -0.0108 576 LEU C CD2 
8978  N N   . LEU C 276 ? 0.3010 0.2742 0.2998 0.0040  0.0329  -0.0118 577 LEU C N   
8979  C CA  . LEU C 276 ? 0.2815 0.2578 0.2793 -0.0012 0.0337  -0.0111 577 LEU C CA  
8980  C C   . LEU C 276 ? 0.3715 0.3386 0.3627 -0.0053 0.0327  -0.0086 577 LEU C C   
8981  O O   . LEU C 276 ? 0.3186 0.2811 0.3057 -0.0053 0.0315  -0.0060 577 LEU C O   
8982  C CB  . LEU C 276 ? 0.3067 0.2924 0.3065 -0.0019 0.0346  -0.0104 577 LEU C CB  
8983  C CG  . LEU C 276 ? 0.2713 0.2620 0.2700 -0.0070 0.0356  -0.0089 577 LEU C CG  
8984  C CD1 . LEU C 276 ? 0.2716 0.2662 0.2734 -0.0086 0.0361  -0.0107 577 LEU C CD1 
8985  C CD2 . LEU C 276 ? 0.3154 0.3148 0.3151 -0.0065 0.0369  -0.0085 577 LEU C CD2 
8986  N N   . GLU C 277 ? 0.3034 0.2668 0.2924 -0.0092 0.0327  -0.0092 578 GLU C N   
8987  C CA  . GLU C 277 ? 0.2656 0.2181 0.2468 -0.0143 0.0315  -0.0071 578 GLU C CA  
8988  C C   . GLU C 277 ? 0.3363 0.2972 0.3182 -0.0218 0.0321  -0.0057 578 GLU C C   
8989  O O   . GLU C 277 ? 0.3052 0.2745 0.2917 -0.0232 0.0327  -0.0075 578 GLU C O   
8990  C CB  . GLU C 277 ? 0.3708 0.3110 0.3474 -0.0136 0.0307  -0.0091 578 GLU C CB  
8991  C CG  . GLU C 277 ? 0.6091 0.5346 0.5755 -0.0190 0.0290  -0.0071 578 GLU C CG  
8992  C CD  . GLU C 277 ? 0.8403 0.7674 0.8048 -0.0273 0.0288  -0.0074 578 GLU C CD  
8993  O OE1 . GLU C 277 ? 0.9052 0.8388 0.8742 -0.0266 0.0294  -0.0103 578 GLU C OE1 
8994  O OE2 . GLU C 277 ? 0.8558 0.7780 0.8140 -0.0349 0.0279  -0.0047 578 GLU C OE2 
8995  N N   . ILE C 278 ? 0.2981 0.2577 0.2755 -0.0265 0.0320  -0.0024 579 ILE C N   
8996  C CA  . ILE C 278 ? 0.3632 0.3328 0.3416 -0.0342 0.0331  -0.0007 579 ILE C CA  
8997  C C   . ILE C 278 ? 0.4662 0.4234 0.4344 -0.0417 0.0318  0.0027  579 ILE C C   
8998  O O   . ILE C 278 ? 0.3918 0.3412 0.3539 -0.0413 0.0313  0.0054  579 ILE C O   
8999  C CB  . ILE C 278 ? 0.3773 0.3613 0.3606 -0.0328 0.0353  0.0001  579 ILE C CB  
9000  C CG1 . ILE C 278 ? 0.3223 0.3154 0.3136 -0.0254 0.0362  -0.0031 579 ILE C CG1 
9001  C CG2 . ILE C 278 ? 0.2984 0.2946 0.2834 -0.0405 0.0369  0.0018  579 ILE C CG2 
9002  C CD1 . ILE C 278 ? 0.3187 0.3211 0.3121 -0.0227 0.0381  -0.0028 579 ILE C CD1 
9003  N N   . GLY C 279 ? 0.3395 0.2946 0.3050 -0.0492 0.0310  0.0028  580 GLY C N   
9004  C CA  . GLY C 279 ? 0.3877 0.3305 0.3423 -0.0583 0.0297  0.0061  580 GLY C CA  
9005  C C   . GLY C 279 ? 0.4855 0.4049 0.4290 -0.0549 0.0275  0.0070  580 GLY C C   
9006  O O   . GLY C 279 ? 0.5189 0.4270 0.4523 -0.0599 0.0265  0.0108  580 GLY C O   
9007  N N   . GLY C 280 ? 0.4045 0.3167 0.3493 -0.0461 0.0267  0.0038  581 GLY C N   
9008  C CA  . GLY C 280 ? 0.4171 0.3091 0.3529 -0.0405 0.0248  0.0042  581 GLY C CA  
9009  C C   . GLY C 280 ? 0.4273 0.3211 0.3652 -0.0329 0.0247  0.0058  581 GLY C C   
9010  O O   . GLY C 280 ? 0.4559 0.3355 0.3882 -0.0263 0.0228  0.0061  581 GLY C O   
9011  N N   . LEU C 281 ? 0.3859 0.2968 0.3313 -0.0333 0.0264  0.0068  582 LEU C N   
9012  C CA  . LEU C 281 ? 0.4360 0.3501 0.3836 -0.0264 0.0261  0.0079  582 LEU C CA  
9013  C C   . LEU C 281 ? 0.4125 0.3355 0.3702 -0.0178 0.0268  0.0039  582 LEU C C   
9014  O O   . LEU C 281 ? 0.3653 0.2989 0.3304 -0.0183 0.0286  0.0009  582 LEU C O   
9015  C CB  . LEU C 281 ? 0.3383 0.2657 0.2879 -0.0309 0.0278  0.0102  582 LEU C CB  
9016  C CG  . LEU C 281 ? 0.3987 0.3195 0.3384 -0.0407 0.0277  0.0145  582 LEU C CG  
9017  C CD1 . LEU C 281 ? 0.4709 0.4071 0.4131 -0.0445 0.0303  0.0163  582 LEU C CD1 
9018  C CD2 . LEU C 281 ? 0.3689 0.2681 0.2960 -0.0391 0.0244  0.0177  582 LEU C CD2 
9019  N N   . GLU C 282 ? 0.3815 0.3005 0.3394 -0.0101 0.0252  0.0041  583 GLU C N   
9020  C CA  . GLU C 282 ? 0.3800 0.3065 0.3467 -0.0025 0.0258  0.0005  583 GLU C CA  
9021  C C   . GLU C 282 ? 0.4106 0.3490 0.3827 0.0004  0.0257  0.0011  583 GLU C C   
9022  O O   . GLU C 282 ? 0.3701 0.3044 0.3383 0.0030  0.0235  0.0038  583 GLU C O   
9023  C CB  . GLU C 282 ? 0.4329 0.3471 0.3965 0.0045  0.0241  -0.0004 583 GLU C CB  
9024  C CG  . GLU C 282 ? 0.5323 0.4329 0.4892 0.0019  0.0242  -0.0017 583 GLU C CG  
9025  C CD  . GLU C 282 ? 0.5758 0.4645 0.5295 0.0102  0.0231  -0.0034 583 GLU C CD  
9026  O OE1 . GLU C 282 ? 0.6412 0.5242 0.5922 0.0161  0.0209  -0.0013 583 GLU C OE1 
9027  O OE2 . GLU C 282 ? 0.6451 0.5305 0.5988 0.0113  0.0246  -0.0070 583 GLU C OE2 
9028  N N   . PHE C 283 ? 0.3720 0.3239 0.3519 0.0001  0.0278  -0.0014 584 PHE C N   
9029  C CA  . PHE C 283 ? 0.3236 0.2857 0.3076 0.0024  0.0279  -0.0015 584 PHE C CA  
9030  C C   . PHE C 283 ? 0.3255 0.2920 0.3162 0.0083  0.0276  -0.0044 584 PHE C C   
9031  O O   . PHE C 283 ? 0.3290 0.3022 0.3251 0.0083  0.0295  -0.0073 584 PHE C O   
9032  C CB  . PHE C 283 ? 0.2701 0.2426 0.2565 -0.0017 0.0304  -0.0023 584 PHE C CB  
9033  C CG  . PHE C 283 ? 0.3565 0.3279 0.3372 -0.0078 0.0311  0.0006  584 PHE C CG  
9034  C CD1 . PHE C 283 ? 0.3123 0.2828 0.2921 -0.0130 0.0323  0.0007  584 PHE C CD1 
9035  C CD2 . PHE C 283 ? 0.3188 0.2900 0.2942 -0.0091 0.0305  0.0034  584 PHE C CD2 
9036  C CE1 . PHE C 283 ? 0.3041 0.2750 0.2789 -0.0198 0.0332  0.0036  584 PHE C CE1 
9037  C CE2 . PHE C 283 ? 0.3108 0.2815 0.2804 -0.0155 0.0317  0.0063  584 PHE C CE2 
9038  C CZ  . PHE C 283 ? 0.3057 0.2769 0.2754 -0.0210 0.0331  0.0064  584 PHE C CZ  
9039  N N   . SER C 284 ? 0.3700 0.3331 0.3602 0.0132  0.0252  -0.0033 585 SER C N   
9040  C CA  . SER C 284 ? 0.3869 0.3553 0.3840 0.0186  0.0250  -0.0058 585 SER C CA  
9041  C C   . SER C 284 ? 0.3491 0.3297 0.3517 0.0183  0.0253  -0.0072 585 SER C C   
9042  O O   . SER C 284 ? 0.3112 0.2981 0.3200 0.0209  0.0259  -0.0096 585 SER C O   
9043  C CB  . SER C 284 ? 0.3847 0.3475 0.3802 0.0247  0.0221  -0.0041 585 SER C CB  
9044  O OG  . SER C 284 ? 0.4038 0.3641 0.3941 0.0240  0.0193  -0.0004 585 SER C OG  
9045  N N   . ALA C 285 ? 0.3023 0.2860 0.3022 0.0150  0.0251  -0.0059 586 ALA C N   
9046  C CA  . ALA C 285 ? 0.2549 0.2476 0.2579 0.0141  0.0254  -0.0076 586 ALA C CA  
9047  C C   . ALA C 285 ? 0.3065 0.3007 0.3072 0.0101  0.0280  -0.0085 586 ALA C C   
9048  O O   . ALA C 285 ? 0.3222 0.3149 0.3178 0.0077  0.0282  -0.0065 586 ALA C O   
9049  C CB  . ALA C 285 ? 0.3237 0.3191 0.3248 0.0152  0.0222  -0.0057 586 ALA C CB  
9050  N N   . CYS C 286 ? 0.2339 0.2313 0.2382 0.0097  0.0300  -0.0113 587 CYS C N   
9051  C CA  . CYS C 286 ? 0.2821 0.2814 0.2851 0.0073  0.0323  -0.0122 587 CYS C CA  
9052  C C   . CYS C 286 ? 0.3644 0.3670 0.3698 0.0079  0.0334  -0.0151 587 CYS C C   
9053  O O   . CYS C 286 ? 0.3837 0.3864 0.3907 0.0076  0.0349  -0.0164 587 CYS C O   
9054  C CB  . CYS C 286 ? 0.3352 0.3313 0.3381 0.0056  0.0334  -0.0116 587 CYS C CB  
9055  S SG  . CYS C 286 ? 0.3539 0.3470 0.3606 0.0074  0.0337  -0.0137 587 CYS C SG  
9056  N N   . PRO C 287 ? 0.3749 0.3795 0.3799 0.0083  0.0323  -0.0161 588 PRO C N   
9057  C CA  . PRO C 287 ? 0.2861 0.2915 0.2919 0.0081  0.0331  -0.0187 588 PRO C CA  
9058  C C   . PRO C 287 ? 0.2826 0.2873 0.2860 0.0081  0.0350  -0.0199 588 PRO C C   
9059  O O   . PRO C 287 ? 0.2996 0.3055 0.3000 0.0081  0.0358  -0.0194 588 PRO C O   
9060  C CB  . PRO C 287 ? 0.3123 0.3192 0.3160 0.0072  0.0312  -0.0191 588 PRO C CB  
9061  C CG  . PRO C 287 ? 0.3440 0.3510 0.3442 0.0072  0.0301  -0.0169 588 PRO C CG  
9062  C CD  . PRO C 287 ? 0.3245 0.3300 0.3269 0.0082  0.0301  -0.0147 588 PRO C CD  
9063  N N   . PHE C 288 ? 0.2503 0.2538 0.2550 0.0085  0.0359  -0.0214 589 PHE C N   
9064  C CA  . PHE C 288 ? 0.2168 0.2201 0.2199 0.0097  0.0372  -0.0225 589 PHE C CA  
9065  C C   . PHE C 288 ? 0.2673 0.2666 0.2680 0.0100  0.0371  -0.0244 589 PHE C C   
9066  O O   . PHE C 288 ? 0.2551 0.2530 0.2569 0.0084  0.0365  -0.0247 589 PHE C O   
9067  C CB  . PHE C 288 ? 0.2560 0.2611 0.2622 0.0095  0.0379  -0.0216 589 PHE C CB  
9068  C CG  . PHE C 288 ? 0.3449 0.3477 0.3535 0.0088  0.0375  -0.0218 589 PHE C CG  
9069  C CD1 . PHE C 288 ? 0.3044 0.3050 0.3122 0.0092  0.0377  -0.0232 589 PHE C CD1 
9070  C CD2 . PHE C 288 ? 0.3252 0.3270 0.3356 0.0080  0.0371  -0.0207 589 PHE C CD2 
9071  C CE1 . PHE C 288 ? 0.2970 0.2956 0.3060 0.0083  0.0378  -0.0236 589 PHE C CE1 
9072  C CE2 . PHE C 288 ? 0.3763 0.3757 0.3880 0.0079  0.0373  -0.0214 589 PHE C CE2 
9073  C CZ  . PHE C 288 ? 0.2851 0.2835 0.2963 0.0079  0.0378  -0.0229 589 PHE C CZ  
9074  N N   . SER C 289 ? 0.2873 0.2846 0.2842 0.0121  0.0377  -0.0256 590 SER C N   
9075  C CA  . SER C 289 ? 0.2670 0.2576 0.2589 0.0123  0.0372  -0.0273 590 SER C CA  
9076  C C   . SER C 289 ? 0.2572 0.2460 0.2469 0.0161  0.0378  -0.0280 590 SER C C   
9077  O O   . SER C 289 ? 0.2446 0.2388 0.2361 0.0188  0.0388  -0.0278 590 SER C O   
9078  C CB  . SER C 289 ? 0.2362 0.2229 0.2223 0.0111  0.0365  -0.0284 590 SER C CB  
9079  O OG  . SER C 289 ? 0.3292 0.3165 0.3119 0.0141  0.0375  -0.0292 590 SER C OG  
9080  N N   . GLY C 290 ? 0.2849 0.2668 0.2708 0.0162  0.0370  -0.0287 591 GLY C N   
9081  C CA  . GLY C 290 ? 0.2414 0.2199 0.2238 0.0208  0.0369  -0.0294 591 GLY C CA  
9082  C C   . GLY C 290 ? 0.2801 0.2460 0.2530 0.0208  0.0359  -0.0307 591 GLY C C   
9083  O O   . GLY C 290 ? 0.3479 0.3085 0.3152 0.0197  0.0358  -0.0320 591 GLY C O   
9084  N N   . TRP C 291 ? 0.3109 0.2708 0.2806 0.0214  0.0348  -0.0303 592 TRP C N   
9085  C CA  . TRP C 291 ? 0.3098 0.2559 0.2693 0.0195  0.0337  -0.0310 592 TRP C CA  
9086  C C   . TRP C 291 ? 0.2685 0.2125 0.2280 0.0158  0.0331  -0.0296 592 TRP C C   
9087  O O   . TRP C 291 ? 0.3057 0.2574 0.2718 0.0162  0.0333  -0.0284 592 TRP C O   
9088  C CB  . TRP C 291 ? 0.3042 0.2402 0.2548 0.0260  0.0328  -0.0322 592 TRP C CB  
9089  C CG  . TRP C 291 ? 0.3599 0.3007 0.3140 0.0322  0.0322  -0.0313 592 TRP C CG  
9090  C CD1 . TRP C 291 ? 0.4132 0.3502 0.3654 0.0328  0.0305  -0.0298 592 TRP C CD1 
9091  C CD2 . TRP C 291 ? 0.3602 0.3118 0.3204 0.0385  0.0332  -0.0318 592 TRP C CD2 
9092  N NE1 . TRP C 291 ? 0.3592 0.3045 0.3164 0.0393  0.0299  -0.0293 592 TRP C NE1 
9093  C CE2 . TRP C 291 ? 0.3854 0.3404 0.3481 0.0428  0.0317  -0.0305 592 TRP C CE2 
9094  C CE3 . TRP C 291 ? 0.4290 0.3885 0.3925 0.0407  0.0353  -0.0330 592 TRP C CE3 
9095  C CZ2 . TRP C 291 ? 0.4200 0.3877 0.3896 0.0489  0.0322  -0.0304 592 TRP C CZ2 
9096  C CZ3 . TRP C 291 ? 0.3916 0.3630 0.3614 0.0465  0.0363  -0.0330 592 TRP C CZ3 
9097  C CH2 . TRP C 291 ? 0.4119 0.3881 0.3853 0.0506  0.0347  -0.0317 592 TRP C CH2 
9098  N N   . TYR C 292 ? 0.3707 0.3036 0.3216 0.0115  0.0324  -0.0297 593 TYR C N   
9099  C CA  . TYR C 292 ? 0.3820 0.3135 0.3321 0.0064  0.0325  -0.0284 593 TYR C CA  
9100  C C   . TYR C 292 ? 0.2941 0.2182 0.2384 0.0096  0.0311  -0.0273 593 TYR C C   
9101  O O   . TYR C 292 ? 0.3232 0.2374 0.2598 0.0146  0.0294  -0.0275 593 TYR C O   
9102  C CB  . TYR C 292 ? 0.3108 0.2342 0.2536 -0.0007 0.0325  -0.0287 593 TYR C CB  
9103  C CG  . TYR C 292 ? 0.3968 0.3314 0.3476 -0.0064 0.0339  -0.0289 593 TYR C CG  
9104  C CD1 . TYR C 292 ? 0.3030 0.2378 0.2527 -0.0095 0.0334  -0.0299 593 TYR C CD1 
9105  C CD2 . TYR C 292 ? 0.3420 0.2867 0.3009 -0.0084 0.0356  -0.0281 593 TYR C CD2 
9106  C CE1 . TYR C 292 ? 0.3297 0.2760 0.2872 -0.0141 0.0341  -0.0298 593 TYR C CE1 
9107  C CE2 . TYR C 292 ? 0.3224 0.2778 0.2888 -0.0123 0.0368  -0.0283 593 TYR C CE2 
9108  C CZ  . TYR C 292 ? 0.3490 0.3059 0.3152 -0.0150 0.0359  -0.0289 593 TYR C CZ  
9109  O OH  . TYR C 292 ? 0.3391 0.3082 0.3137 -0.0182 0.0367  -0.0289 593 TYR C OH  
9110  N N   . MET C 293 ? 0.2731 0.2018 0.2208 0.0071  0.0317  -0.0261 594 MET C N   
9111  C CA  . MET C 293 ? 0.2873 0.2067 0.2268 0.0069  0.0302  -0.0247 594 MET C CA  
9112  C C   . MET C 293 ? 0.3423 0.2533 0.2739 -0.0010 0.0311  -0.0243 594 MET C C   
9113  O O   . MET C 293 ? 0.3336 0.2527 0.2709 -0.0065 0.0334  -0.0248 594 MET C O   
9114  C CB  . MET C 293 ? 0.2747 0.2030 0.2204 0.0073  0.0305  -0.0239 594 MET C CB  
9115  C CG  . MET C 293 ? 0.3111 0.2303 0.2478 0.0077  0.0284  -0.0222 594 MET C CG  
9116  S SD  . MET C 293 ? 0.3486 0.2788 0.2925 0.0092  0.0278  -0.0216 594 MET C SD  
9117  C CE  . MET C 293 ? 0.3472 0.2827 0.2944 0.0016  0.0317  -0.0225 594 MET C CE  
9118  N N   . GLY C 294 ? 0.3842 0.2790 0.3023 -0.0015 0.0292  -0.0233 595 GLY C N   
9119  C CA  . GLY C 294 ? 0.3956 0.2809 0.3044 -0.0101 0.0298  -0.0228 595 GLY C CA  
9120  C C   . GLY C 294 ? 0.4170 0.3112 0.3301 -0.0175 0.0327  -0.0222 595 GLY C C   
9121  O O   . GLY C 294 ? 0.3457 0.2416 0.2582 -0.0253 0.0344  -0.0225 595 GLY C O   
9122  N N   . THR C 295 ? 0.3672 0.2676 0.2843 -0.0155 0.0332  -0.0215 596 THR C N   
9123  C CA  . THR C 295 ? 0.3639 0.2716 0.2833 -0.0219 0.0364  -0.0213 596 THR C CA  
9124  C C   . THR C 295 ? 0.3292 0.2533 0.2621 -0.0235 0.0394  -0.0231 596 THR C C   
9125  O O   . THR C 295 ? 0.3103 0.2413 0.2455 -0.0293 0.0424  -0.0233 596 THR C O   
9126  C CB  . THR C 295 ? 0.3028 0.2123 0.2221 -0.0191 0.0361  -0.0206 596 THR C CB  
9127  O OG1 . THR C 295 ? 0.3103 0.2280 0.2392 -0.0119 0.0349  -0.0214 596 THR C OG1 
9128  C CG2 . THR C 295 ? 0.3193 0.2127 0.2240 -0.0188 0.0332  -0.0183 596 THR C CG2 
9129  N N   . GLU C 296 ? 0.3298 0.2609 0.2716 -0.0182 0.0386  -0.0242 597 GLU C N   
9130  C CA  . GLU C 296 ? 0.3239 0.2689 0.2771 -0.0196 0.0408  -0.0255 597 GLU C CA  
9131  C C   . GLU C 296 ? 0.3788 0.3245 0.3300 -0.0269 0.0418  -0.0256 597 GLU C C   
9132  O O   . GLU C 296 ? 0.3171 0.2743 0.2750 -0.0306 0.0444  -0.0261 597 GLU C O   
9133  C CB  . GLU C 296 ? 0.3643 0.3141 0.3246 -0.0137 0.0394  -0.0263 597 GLU C CB  
9134  C CG  . GLU C 296 ? 0.3269 0.2789 0.2908 -0.0076 0.0385  -0.0261 597 GLU C CG  
9135  C CD  . GLU C 296 ? 0.3051 0.2623 0.2753 -0.0031 0.0376  -0.0267 597 GLU C CD  
9136  O OE1 . GLU C 296 ? 0.2907 0.2571 0.2690 -0.0034 0.0388  -0.0272 597 GLU C OE1 
9137  O OE2 . GLU C 296 ? 0.3135 0.2654 0.2801 0.0009  0.0357  -0.0265 597 GLU C OE2 
9138  N N   . ILE C 297 ? 0.3042 0.2373 0.2453 -0.0292 0.0396  -0.0252 598 ILE C N   
9139  C CA  . ILE C 297 ? 0.4084 0.3407 0.3461 -0.0373 0.0398  -0.0252 598 ILE C CA  
9140  C C   . ILE C 297 ? 0.3823 0.3082 0.3106 -0.0451 0.0413  -0.0238 598 ILE C C   
9141  O O   . ILE C 297 ? 0.3917 0.3281 0.3242 -0.0521 0.0439  -0.0238 598 ILE C O   
9142  C CB  . ILE C 297 ? 0.3766 0.2959 0.3056 -0.0367 0.0367  -0.0257 598 ILE C CB  
9143  C CG1 . ILE C 297 ? 0.3441 0.2696 0.2811 -0.0291 0.0357  -0.0271 598 ILE C CG1 
9144  C CG2 . ILE C 297 ? 0.3409 0.2579 0.2645 -0.0467 0.0365  -0.0258 598 ILE C CG2 
9145  C CD1 . ILE C 297 ? 0.3021 0.2133 0.2291 -0.0263 0.0331  -0.0279 598 ILE C CD1 
9146  N N   . GLY C 298 ? 0.3169 0.2259 0.2323 -0.0439 0.0394  -0.0225 599 GLY C N   
9147  C CA  . GLY C 298 ? 0.4450 0.3441 0.3482 -0.0520 0.0403  -0.0206 599 GLY C CA  
9148  C C   . GLY C 298 ? 0.4737 0.3845 0.3819 -0.0549 0.0441  -0.0202 599 GLY C C   
9149  O O   . GLY C 298 ? 0.4676 0.3798 0.3713 -0.0642 0.0466  -0.0193 599 GLY C O   
9150  N N   . VAL C 299 ? 0.3983 0.3176 0.3151 -0.0476 0.0449  -0.0211 600 VAL C N   
9151  C CA  . VAL C 299 ? 0.3610 0.2896 0.2809 -0.0497 0.0488  -0.0212 600 VAL C CA  
9152  C C   . VAL C 299 ? 0.3541 0.3031 0.2892 -0.0499 0.0523  -0.0232 600 VAL C C   
9153  O O   . VAL C 299 ? 0.3591 0.3174 0.2960 -0.0563 0.0562  -0.0234 600 VAL C O   
9154  C CB  . VAL C 299 ? 0.3873 0.3123 0.3059 -0.0426 0.0475  -0.0210 600 VAL C CB  
9155  C CG1 . VAL C 299 ? 0.4578 0.3899 0.3768 -0.0452 0.0514  -0.0215 600 VAL C CG1 
9156  C CG2 . VAL C 299 ? 0.3560 0.2616 0.2601 -0.0410 0.0433  -0.0188 600 VAL C CG2 
9157  N N   . ARG C 300 ? 0.3486 0.3051 0.2947 -0.0428 0.0511  -0.0247 601 ARG C N   
9158  C CA  . ARG C 300 ? 0.3171 0.2914 0.2768 -0.0411 0.0541  -0.0264 601 ARG C CA  
9159  C C   . ARG C 300 ? 0.3748 0.3589 0.3408 -0.0456 0.0543  -0.0267 601 ARG C C   
9160  O O   . ARG C 300 ? 0.3717 0.3688 0.3431 -0.0502 0.0577  -0.0272 601 ARG C O   
9161  C CB  . ARG C 300 ? 0.2925 0.2697 0.2600 -0.0321 0.0527  -0.0275 601 ARG C CB  
9162  C CG  . ARG C 300 ? 0.3032 0.2718 0.2649 -0.0282 0.0518  -0.0272 601 ARG C CG  
9163  C CD  . ARG C 300 ? 0.2672 0.2388 0.2264 -0.0303 0.0555  -0.0279 601 ARG C CD  
9164  N NE  . ARG C 300 ? 0.2652 0.2515 0.2346 -0.0299 0.0595  -0.0298 601 ARG C NE  
9165  C CZ  . ARG C 300 ? 0.2660 0.2585 0.2438 -0.0237 0.0598  -0.0314 601 ARG C CZ  
9166  N NH1 . ARG C 300 ? 0.2869 0.2730 0.2642 -0.0189 0.0567  -0.0312 601 ARG C NH1 
9167  N NH2 . ARG C 300 ? 0.2853 0.2904 0.2717 -0.0224 0.0631  -0.0331 601 ARG C NH2 
9168  N N   . ASP C 301 ? 0.3621 0.3409 0.3273 -0.0445 0.0507  -0.0265 602 ASP C N   
9169  C CA  . ASP C 301 ? 0.3646 0.3525 0.3352 -0.0491 0.0501  -0.0267 602 ASP C CA  
9170  C C   . ASP C 301 ? 0.3061 0.2937 0.2701 -0.0601 0.0515  -0.0258 602 ASP C C   
9171  O O   . ASP C 301 ? 0.3871 0.3906 0.3591 -0.0651 0.0533  -0.0261 602 ASP C O   
9172  C CB  . ASP C 301 ? 0.3294 0.3087 0.2970 -0.0465 0.0460  -0.0268 602 ASP C CB  
9173  C CG  . ASP C 301 ? 0.3486 0.3305 0.3234 -0.0369 0.0449  -0.0275 602 ASP C CG  
9174  O OD1 . ASP C 301 ? 0.3932 0.3874 0.3783 -0.0332 0.0467  -0.0281 602 ASP C OD1 
9175  O OD2 . ASP C 301 ? 0.3818 0.3532 0.3514 -0.0331 0.0423  -0.0275 602 ASP C OD2 
9176  N N   . TYR C 302 ? 0.3530 0.3232 0.3023 -0.0643 0.0507  -0.0244 603 TYR C N   
9177  C CA  . TYR C 302 ? 0.3356 0.3029 0.2765 -0.0761 0.0517  -0.0232 603 TYR C CA  
9178  C C   . TYR C 302 ? 0.4119 0.3877 0.3530 -0.0811 0.0565  -0.0227 603 TYR C C   
9179  O O   . TYR C 302 ? 0.4212 0.4061 0.3627 -0.0911 0.0588  -0.0221 603 TYR C O   
9180  C CB  . TYR C 302 ? 0.3659 0.3080 0.2884 -0.0789 0.0482  -0.0217 603 TYR C CB  
9181  C CG  . TYR C 302 ? 0.3294 0.2638 0.2490 -0.0789 0.0441  -0.0225 603 TYR C CG  
9182  C CD1 . TYR C 302 ? 0.3456 0.2559 0.2487 -0.0790 0.0407  -0.0218 603 TYR C CD1 
9183  C CD2 . TYR C 302 ? 0.4072 0.3577 0.3395 -0.0782 0.0437  -0.0239 603 TYR C CD2 
9184  C CE1 . TYR C 302 ? 0.4942 0.3963 0.3930 -0.0786 0.0373  -0.0230 603 TYR C CE1 
9185  C CE2 . TYR C 302 ? 0.4221 0.3649 0.3503 -0.0784 0.0399  -0.0248 603 TYR C CE2 
9186  C CZ  . TYR C 302 ? 0.4715 0.3900 0.3828 -0.0787 0.0370  -0.0245 603 TYR C CZ  
9187  O OH  . TYR C 302 ? 0.4919 0.4016 0.3976 -0.0787 0.0337  -0.0258 603 TYR C OH  
9188  N N   . CYS C 303 ? 0.4173 0.3915 0.3580 -0.0750 0.0584  -0.0229 604 CYS C N   
9189  C CA  . CYS C 303 ? 0.4084 0.3863 0.3450 -0.0804 0.0630  -0.0223 604 CYS C CA  
9190  C C   . CYS C 303 ? 0.3741 0.3697 0.3229 -0.0747 0.0675  -0.0245 604 CYS C C   
9191  O O   . CYS C 303 ? 0.3777 0.3785 0.3235 -0.0792 0.0721  -0.0244 604 CYS C O   
9192  C CB  . CYS C 303 ? 0.3623 0.3186 0.2819 -0.0806 0.0614  -0.0204 604 CYS C CB  
9193  S SG  . CYS C 303 ? 0.4441 0.3755 0.3456 -0.0867 0.0563  -0.0178 604 CYS C SG  
9194  N N   . ASP C 304 ? 0.3338 0.3372 0.2945 -0.0652 0.0666  -0.0263 605 ASP C N   
9195  C CA  . ASP C 304 ? 0.3442 0.3648 0.3163 -0.0606 0.0710  -0.0285 605 ASP C CA  
9196  C C   . ASP C 304 ? 0.3970 0.4366 0.3764 -0.0677 0.0750  -0.0288 605 ASP C C   
9197  O O   . ASP C 304 ? 0.3725 0.4168 0.3548 -0.0731 0.0729  -0.0280 605 ASP C O   
9198  C CB  . ASP C 304 ? 0.3016 0.3278 0.2853 -0.0504 0.0689  -0.0301 605 ASP C CB  
9199  C CG  . ASP C 304 ? 0.4009 0.4147 0.3804 -0.0427 0.0670  -0.0305 605 ASP C CG  
9200  O OD1 . ASP C 304 ? 0.4229 0.4233 0.3907 -0.0445 0.0664  -0.0295 605 ASP C OD1 
9201  O OD2 . ASP C 304 ? 0.4061 0.4240 0.3941 -0.0351 0.0657  -0.0317 605 ASP C OD2 
9202  N N   . ASN C 305 ? 0.3585 0.4092 0.3402 -0.0682 0.0808  -0.0302 606 ASN C N   
9203  C CA  . ASN C 305 ? 0.3641 0.4365 0.3543 -0.0744 0.0854  -0.0307 606 ASN C CA  
9204  C C   . ASN C 305 ? 0.3796 0.4703 0.3867 -0.0696 0.0840  -0.0319 606 ASN C C   
9205  O O   . ASN C 305 ? 0.4091 0.5153 0.4228 -0.0767 0.0847  -0.0312 606 ASN C O   
9206  C CB  . ASN C 305 ? 0.3918 0.4737 0.3824 -0.0730 0.0924  -0.0327 606 ASN C CB  
9207  C CG  . ASN C 305 ? 0.6270 0.6946 0.6003 -0.0812 0.0944  -0.0310 606 ASN C CG  
9208  O OD1 . ASN C 305 ? 0.6868 0.7467 0.6508 -0.0919 0.0929  -0.0282 606 ASN C OD1 
9209  N ND2 . ASN C 305 ? 0.6497 0.7121 0.6173 -0.0765 0.0975  -0.0326 606 ASN C ND2 
9210  N N   . SER C 306 ? 0.3577 0.4467 0.3713 -0.0582 0.0818  -0.0333 607 SER C N   
9211  C CA  . SER C 306 ? 0.4265 0.5308 0.4549 -0.0524 0.0799  -0.0340 607 SER C CA  
9212  C C   . SER C 306 ? 0.4308 0.5265 0.4580 -0.0536 0.0733  -0.0323 607 SER C C   
9213  O O   . SER C 306 ? 0.3467 0.4525 0.3846 -0.0485 0.0708  -0.0326 607 SER C O   
9214  C CB  . SER C 306 ? 0.4752 0.5809 0.5099 -0.0395 0.0809  -0.0363 607 SER C CB  
9215  O OG  . SER C 306 ? 0.6759 0.7604 0.7015 -0.0353 0.0776  -0.0359 607 SER C OG  
9216  N N   . ARG C 307 ? 0.3664 0.4432 0.3803 -0.0598 0.0704  -0.0306 608 ARG C N   
9217  C CA  . ARG C 307 ? 0.2581 0.3259 0.2693 -0.0611 0.0647  -0.0294 608 ARG C CA  
9218  C C   . ARG C 307 ? 0.3184 0.3861 0.3236 -0.0739 0.0638  -0.0279 608 ARG C C   
9219  O O   . ARG C 307 ? 0.3758 0.4617 0.3877 -0.0804 0.0667  -0.0279 608 ARG C O   
9220  C CB  . ARG C 307 ? 0.3044 0.3494 0.3048 -0.0564 0.0615  -0.0289 608 ARG C CB  
9221  C CG  . ARG C 307 ? 0.3713 0.4157 0.3770 -0.0451 0.0618  -0.0302 608 ARG C CG  
9222  C CD  . ARG C 307 ? 0.4389 0.4941 0.4566 -0.0385 0.0597  -0.0308 608 ARG C CD  
9223  N NE  . ARG C 307 ? 0.3941 0.4421 0.4091 -0.0397 0.0549  -0.0298 608 ARG C NE  
9224  C CZ  . ARG C 307 ? 0.4334 0.4654 0.4408 -0.0366 0.0520  -0.0293 608 ARG C CZ  
9225  N NH1 . ARG C 307 ? 0.3109 0.3333 0.3136 -0.0324 0.0530  -0.0295 608 ARG C NH1 
9226  N NH2 . ARG C 307 ? 0.3973 0.4237 0.4019 -0.0377 0.0482  -0.0288 608 ARG C NH2 
9227  N N   . TYR C 308 ? 0.3247 0.3725 0.3170 -0.0779 0.0598  -0.0267 609 TYR C N   
9228  C CA  . TYR C 308 ? 0.3427 0.3885 0.3279 -0.0907 0.0586  -0.0254 609 TYR C CA  
9229  C C   . TYR C 308 ? 0.4088 0.4529 0.3855 -0.1001 0.0628  -0.0243 609 TYR C C   
9230  O O   . TYR C 308 ? 0.4087 0.4580 0.3826 -0.1123 0.0632  -0.0232 609 TYR C O   
9231  C CB  . TYR C 308 ? 0.3669 0.3898 0.3389 -0.0919 0.0533  -0.0247 609 TYR C CB  
9232  C CG  . TYR C 308 ? 0.3780 0.4069 0.3573 -0.0889 0.0492  -0.0256 609 TYR C CG  
9233  C CD1 . TYR C 308 ? 0.3327 0.3622 0.3190 -0.0770 0.0477  -0.0265 609 TYR C CD1 
9234  C CD2 . TYR C 308 ? 0.3506 0.3851 0.3294 -0.0987 0.0468  -0.0252 609 TYR C CD2 
9235  C CE1 . TYR C 308 ? 0.3443 0.3788 0.3360 -0.0746 0.0440  -0.0270 609 TYR C CE1 
9236  C CE2 . TYR C 308 ? 0.3766 0.4164 0.3610 -0.0963 0.0428  -0.0259 609 TYR C CE2 
9237  C CZ  . TYR C 308 ? 0.4038 0.4434 0.3944 -0.0840 0.0415  -0.0268 609 TYR C CZ  
9238  O OH  . TYR C 308 ? 0.3769 0.4213 0.3718 -0.0821 0.0375  -0.0272 609 TYR C OH  
9239  N N   . ASN C 309 ? 0.3703 0.4075 0.3424 -0.0956 0.0658  -0.0244 610 ASN C N   
9240  C CA  . ASN C 309 ? 0.3774 0.4174 0.3436 -0.1031 0.0709  -0.0236 610 ASN C CA  
9241  C C   . ASN C 309 ? 0.3627 0.3896 0.3134 -0.1174 0.0698  -0.0211 610 ASN C C   
9242  O O   . ASN C 309 ? 0.4376 0.4780 0.3899 -0.1285 0.0729  -0.0203 610 ASN C O   
9243  C CB  . ASN C 309 ? 0.4258 0.4953 0.4083 -0.1032 0.0763  -0.0251 610 ASN C CB  
9244  C CG  . ASN C 309 ? 0.4236 0.4982 0.4008 -0.1099 0.0826  -0.0247 610 ASN C CG  
9245  O OD1 . ASN C 309 ? 0.3627 0.4198 0.3266 -0.1096 0.0834  -0.0239 610 ASN C OD1 
9246  N ND2 . ASN C 309 ? 0.3700 0.4693 0.3574 -0.1164 0.0871  -0.0252 610 ASN C ND2 
9247  N N   . ILE C 310 ? 0.3895 0.3894 0.3244 -0.1171 0.0652  -0.0197 611 ILE C N   
9248  C CA  . ILE C 310 ? 0.3998 0.3830 0.3180 -0.1300 0.0630  -0.0174 611 ILE C CA  
9249  C C   . ILE C 310 ? 0.4655 0.4311 0.3661 -0.1355 0.0648  -0.0150 611 ILE C C   
9250  O O   . ILE C 310 ? 0.4658 0.4142 0.3498 -0.1465 0.0629  -0.0128 611 ILE C O   
9251  C CB  . ILE C 310 ? 0.4323 0.3948 0.3419 -0.1271 0.0565  -0.0175 611 ILE C CB  
9252  C CG1 . ILE C 310 ? 0.4542 0.3949 0.3540 -0.1163 0.0542  -0.0172 611 ILE C CG1 
9253  C CG2 . ILE C 310 ? 0.4430 0.4213 0.3684 -0.1215 0.0544  -0.0196 611 ILE C CG2 
9254  C CD1 . ILE C 310 ? 0.4078 0.3248 0.2952 -0.1139 0.0485  -0.0170 611 ILE C CD1 
9255  N N   . LEU C 311 ? 0.3849 0.3527 0.2868 -0.1285 0.0679  -0.0154 612 LEU C N   
9256  C CA  . LEU C 311 ? 0.4014 0.3511 0.2852 -0.1331 0.0689  -0.0129 612 LEU C CA  
9257  C C   . LEU C 311 ? 0.4057 0.3562 0.2797 -0.1499 0.0719  -0.0105 612 LEU C C   
9258  O O   . LEU C 311 ? 0.4385 0.3649 0.2921 -0.1573 0.0695  -0.0075 612 LEU C O   
9259  C CB  . LEU C 311 ? 0.3866 0.3445 0.2755 -0.1250 0.0729  -0.0141 612 LEU C CB  
9260  C CG  . LEU C 311 ? 0.3916 0.3390 0.2818 -0.1107 0.0690  -0.0152 612 LEU C CG  
9261  C CD1 . LEU C 311 ? 0.5063 0.4627 0.4011 -0.1044 0.0729  -0.0167 612 LEU C CD1 
9262  C CD2 . LEU C 311 ? 0.3930 0.3111 0.2637 -0.1109 0.0636  -0.0124 612 LEU C CD2 
9263  N N   . GLU C 312 ? 0.4583 0.4365 0.3461 -0.1561 0.0771  -0.0117 613 GLU C N   
9264  C CA  . GLU C 312 ? 0.5608 0.5428 0.4399 -0.1729 0.0809  -0.0093 613 GLU C CA  
9265  C C   . GLU C 312 ? 0.5480 0.5144 0.4148 -0.1851 0.0762  -0.0072 613 GLU C C   
9266  O O   . GLU C 312 ? 0.5670 0.5161 0.4144 -0.1978 0.0762  -0.0039 613 GLU C O   
9267  C CB  . GLU C 312 ? 0.6254 0.6440 0.5242 -0.1760 0.0878  -0.0113 613 GLU C CB  
9268  C CG  . GLU C 312 ? 0.8297 0.8573 0.7221 -0.1945 0.0921  -0.0089 613 GLU C CG  
9269  C CD  . GLU C 312 ? 0.9161 0.9823 0.8289 -0.1961 0.0995  -0.0111 613 GLU C CD  
9270  O OE1 . GLU C 312 ? 0.9452 1.0281 0.8749 -0.1819 0.1015  -0.0144 613 GLU C OE1 
9271  O OE2 . GLU C 312 ? 0.8938 0.9736 0.8055 -0.2116 0.1033  -0.0094 613 GLU C OE2 
9272  N N   . GLU C 313 ? 0.5387 0.5095 0.4150 -0.1820 0.0719  -0.0089 614 GLU C N   
9273  C CA  . GLU C 313 ? 0.5588 0.5121 0.4215 -0.1932 0.0670  -0.0073 614 GLU C CA  
9274  C C   . GLU C 313 ? 0.5424 0.4566 0.3810 -0.1908 0.0620  -0.0053 614 GLU C C   
9275  O O   . GLU C 313 ? 0.6213 0.5143 0.4399 -0.2035 0.0601  -0.0026 614 GLU C O   
9276  C CB  . GLU C 313 ? 0.5666 0.5310 0.4431 -0.1891 0.0631  -0.0098 614 GLU C CB  
9277  C CG  . GLU C 313 ? 0.6768 0.6250 0.5391 -0.2025 0.0583  -0.0086 614 GLU C CG  
9278  C CD  . GLU C 313 ? 0.9057 0.8645 0.7799 -0.1997 0.0542  -0.0110 614 GLU C CD  
9279  O OE1 . GLU C 313 ? 0.9502 0.8993 0.8142 -0.2117 0.0504  -0.0105 614 GLU C OE1 
9280  O OE2 . GLU C 313 ? 0.8809 0.8565 0.7733 -0.1858 0.0545  -0.0134 614 GLU C OE2 
9281  N N   . VAL C 314 ? 0.4590 0.3630 0.2989 -0.1746 0.0598  -0.0065 615 VAL C N   
9282  C CA  . VAL C 314 ? 0.4885 0.3574 0.3071 -0.1703 0.0548  -0.0047 615 VAL C CA  
9283  C C   . VAL C 314 ? 0.5811 0.4345 0.3811 -0.1779 0.0568  -0.0011 615 VAL C C   
9284  O O   . VAL C 314 ? 0.5827 0.4064 0.3598 -0.1840 0.0532  0.0016  615 VAL C O   
9285  C CB  . VAL C 314 ? 0.5439 0.4101 0.3704 -0.1515 0.0523  -0.0068 615 VAL C CB  
9286  C CG1 . VAL C 314 ? 0.4695 0.3027 0.2752 -0.1458 0.0479  -0.0047 615 VAL C CG1 
9287  C CG2 . VAL C 314 ? 0.5312 0.4063 0.3709 -0.1453 0.0495  -0.0098 615 VAL C CG2 
9288  N N   . ALA C 315 ? 0.5473 0.4191 0.3557 -0.1773 0.0625  -0.0011 616 ALA C N   
9289  C CA  . ALA C 315 ? 0.5366 0.3950 0.3271 -0.1849 0.0647  0.0024  616 ALA C CA  
9290  C C   . ALA C 315 ? 0.6152 0.4691 0.3925 -0.2049 0.0663  0.0052  616 ALA C C   
9291  O O   . ALA C 315 ? 0.6025 0.4294 0.3557 -0.2128 0.0645  0.0090  616 ALA C O   
9292  C CB  . ALA C 315 ? 0.4839 0.3650 0.2865 -0.1804 0.0711  0.0011  616 ALA C CB  
9293  N N   . LYS C 316 ? 0.6311 0.5109 0.4235 -0.2136 0.0694  0.0036  617 LYS C N   
9294  C CA  . LYS C 316 ? 0.7327 0.6100 0.5137 -0.2340 0.0704  0.0062  617 LYS C CA  
9295  C C   . LYS C 316 ? 0.7256 0.5648 0.4823 -0.2390 0.0631  0.0084  617 LYS C C   
9296  O O   . LYS C 316 ? 0.6835 0.4992 0.4164 -0.2513 0.0625  0.0124  617 LYS C O   
9297  C CB  . LYS C 316 ? 0.7819 0.6933 0.5849 -0.2404 0.0729  0.0038  617 LYS C CB  
9298  C CG  . LYS C 316 ? 0.8588 0.8074 0.6796 -0.2446 0.0814  0.0029  617 LYS C CG  
9299  C CD  . LYS C 316 ? 0.9327 0.9147 0.7776 -0.2462 0.0821  0.0001  617 LYS C CD  
9300  C CE  . LYS C 316 ? 0.9467 0.9650 0.8057 -0.2563 0.0903  0.0000  617 LYS C CE  
9301  N NZ  . LYS C 316 ? 0.8811 0.9157 0.7508 -0.2445 0.0968  -0.0018 617 LYS C NZ  
9302  N N   . LYS C 317 ? 0.6825 0.5137 0.4435 -0.2291 0.0576  0.0059  618 LYS C N   
9303  C CA  . LYS C 317 ? 0.6991 0.4933 0.4367 -0.2322 0.0508  0.0073  618 LYS C CA  
9304  C C   . LYS C 317 ? 0.6971 0.4573 0.4121 -0.2255 0.0479  0.0102  618 LYS C C   
9305  O O   . LYS C 317 ? 0.6781 0.4044 0.3676 -0.2325 0.0435  0.0128  618 LYS C O   
9306  C CB  . LYS C 317 ? 0.7306 0.5245 0.4780 -0.2211 0.0461  0.0034  618 LYS C CB  
9307  C CG  . LYS C 317 ? 0.8311 0.6553 0.5980 -0.2286 0.0476  0.0010  618 LYS C CG  
9308  C CD  . LYS C 317 ? 0.9120 0.7198 0.6714 -0.2298 0.0415  -0.0008 618 LYS C CD  
9309  C CE  . LYS C 317 ? 1.0393 0.8779 0.8176 -0.2378 0.0422  -0.0030 618 LYS C CE  
9310  N NZ  . LYS C 317 ? 1.0674 0.9171 0.8420 -0.2596 0.0449  -0.0006 618 LYS C NZ  
9311  N N   . MET C 318 ? 0.6872 0.4547 0.4099 -0.2124 0.0499  0.0100  619 MET C N   
9312  C CA  . MET C 318 ? 0.7498 0.4879 0.4515 -0.2068 0.0470  0.0132  619 MET C CA  
9313  C C   . MET C 318 ? 0.7152 0.4459 0.3996 -0.2219 0.0505  0.0177  619 MET C C   
9314  O O   . MET C 318 ? 0.7321 0.4367 0.3964 -0.2190 0.0478  0.0211  619 MET C O   
9315  C CB  . MET C 318 ? 0.6604 0.4090 0.3761 -0.1878 0.0472  0.0113  619 MET C CB  
9316  C CG  . MET C 318 ? 0.5803 0.3260 0.3056 -0.1722 0.0425  0.0079  619 MET C CG  
9317  S SD  . MET C 318 ? 0.6310 0.3926 0.3746 -0.1521 0.0429  0.0056  619 MET C SD  
9318  C CE  . MET C 318 ? 0.5811 0.3133 0.3002 -0.1489 0.0397  0.0102  619 MET C CE  
9319  N N   . ASN C 319 ? 0.7266 0.4803 0.4183 -0.2379 0.0563  0.0180  620 ASN C N   
9320  C CA  A ASN C 319 ? 0.7786 0.5296 0.4553 -0.2538 0.0608  0.0222  620 ASN C CA  
9321  C CA  B ASN C 319 ? 0.7785 0.5297 0.4553 -0.2538 0.0609  0.0222  620 ASN C CA  
9322  C C   . ASN C 319 ? 0.7893 0.5465 0.4676 -0.2450 0.0643  0.0229  620 ASN C C   
9323  O O   . ASN C 319 ? 0.8671 0.6055 0.5239 -0.2519 0.0647  0.0273  620 ASN C O   
9324  C CB  A ASN C 319 ? 0.8276 0.5371 0.4708 -0.2657 0.0558  0.0270  620 ASN C CB  
9325  C CB  B ASN C 319 ? 0.8277 0.5378 0.4712 -0.2661 0.0559  0.0269  620 ASN C CB  
9326  C CG  A ASN C 319 ? 0.8736 0.5765 0.5141 -0.2735 0.0515  0.0253  620 ASN C CG  
9327  C CG  B ASN C 319 ? 0.8493 0.5647 0.4825 -0.2802 0.0590  0.0293  620 ASN C CG  
9328  O OD1 A ASN C 319 ? 0.9043 0.6365 0.5620 -0.2823 0.0548  0.0230  620 ASN C OD1 
9329  O OD1 B ASN C 319 ? 0.8448 0.5947 0.4951 -0.2881 0.0656  0.0277  620 ASN C OD1 
9330  N ND2 A ASN C 319 ? 0.9030 0.5686 0.5222 -0.2689 0.0438  0.0261  620 ASN C ND2 
9331  N ND2 B ASN C 319 ? 0.9183 0.6006 0.5242 -0.2821 0.0540  0.0326  620 ASN C ND2 
9332  N N   . LEU C 320 ? 0.7280 0.5107 0.4306 -0.2302 0.0665  0.0188  621 LEU C N   
9333  C CA  . LEU C 320 ? 0.7065 0.4951 0.4110 -0.2214 0.0693  0.0189  621 LEU C CA  
9334  C C   . LEU C 320 ? 0.7735 0.5882 0.4838 -0.2330 0.0785  0.0191  621 LEU C C   
9335  O O   . LEU C 320 ? 0.7126 0.5538 0.4381 -0.2418 0.0833  0.0172  621 LEU C O   
9336  C CB  . LEU C 320 ? 0.6503 0.4543 0.3769 -0.2017 0.0681  0.0144  621 LEU C CB  
9337  C CG  . LEU C 320 ? 0.6466 0.4264 0.3676 -0.1886 0.0596  0.0141  621 LEU C CG  
9338  C CD1 . LEU C 320 ? 0.5590 0.3546 0.3004 -0.1703 0.0590  0.0102  621 LEU C CD1 
9339  C CD2 . LEU C 320 ? 0.6993 0.4430 0.3918 -0.1891 0.0546  0.0189  621 LEU C CD2 
9340  N N   . ASP C 321 ? 0.8736 0.6813 0.5715 -0.2329 0.0808  0.0213  622 ASP C N   
9341  C CA  . ASP C 321 ? 0.8109 0.6447 0.5152 -0.2408 0.0902  0.0207  622 ASP C CA  
9342  C C   . ASP C 321 ? 0.6671 0.5334 0.4001 -0.2271 0.0942  0.0149  622 ASP C C   
9343  O O   . ASP C 321 ? 0.6661 0.5286 0.4022 -0.2124 0.0921  0.0133  622 ASP C O   
9344  C CB  . ASP C 321 ? 0.8668 0.6820 0.5482 -0.2438 0.0911  0.0246  622 ASP C CB  
9345  C CG  . ASP C 321 ? 0.9703 0.8132 0.6590 -0.2491 0.1013  0.0231  622 ASP C CG  
9346  O OD1 . ASP C 321 ? 1.0158 0.8535 0.6966 -0.2429 0.1023  0.0234  622 ASP C OD1 
9347  O OD2 . ASP C 321 ? 0.9400 0.8107 0.6424 -0.2590 0.1081  0.0214  622 ASP C OD2 
9348  N N   . MET C 322 ? 0.6375 0.5353 0.3912 -0.2318 0.0996  0.0120  623 MET C N   
9349  C CA  . MET C 322 ? 0.6569 0.5846 0.4377 -0.2187 0.1030  0.0065  623 MET C CA  
9350  C C   . MET C 322 ? 0.6466 0.6032 0.4366 -0.2221 0.1132  0.0045  623 MET C C   
9351  O O   . MET C 322 ? 0.7208 0.7052 0.5339 -0.2131 0.1170  -0.0001 623 MET C O   
9352  C CB  . MET C 322 ? 0.6108 0.5543 0.4107 -0.2179 0.1009  0.0041  623 MET C CB  
9353  C CG  . MET C 322 ? 0.6852 0.6009 0.4750 -0.2161 0.0916  0.0058  623 MET C CG  
9354  S SD  . MET C 322 ? 0.7285 0.6642 0.5391 -0.2172 0.0896  0.0030  623 MET C SD  
9355  C CE  . MET C 322 ? 0.6004 0.5723 0.4414 -0.2016 0.0945  -0.0024 623 MET C CE  
9356  N N   . ARG C 323 ? 0.6206 0.5705 0.3923 -0.2346 0.1176  0.0078  624 ARG C N   
9357  C CA  . ARG C 323 ? 0.7495 0.7275 0.5286 -0.2389 0.1281  0.0057  624 ARG C CA  
9358  C C   . ARG C 323 ? 0.7437 0.7229 0.5236 -0.2253 0.1307  0.0027  624 ARG C C   
9359  O O   . ARG C 323 ? 0.8308 0.8363 0.6216 -0.2242 0.1395  -0.0006 624 ARG C O   
9360  C CB  . ARG C 323 ? 0.8096 0.7815 0.5707 -0.2562 0.1306  0.0097  624 ARG C CB  
9361  C CG  . ARG C 323 ? 0.8594 0.8399 0.6257 -0.2687 0.1282  0.0108  624 ARG C CG  
9362  C CD  . ARG C 323 ? 0.9914 0.9603 0.7383 -0.2828 0.1277  0.0143  624 ARG C CD  
9363  N NE  . ARG C 323 ? 1.1203 1.0478 0.8382 -0.2840 0.1214  0.0188  624 ARG C NE  
9364  C CZ  . ARG C 323 ? 1.3231 1.2380 1.0259 -0.2815 0.1230  0.0201  624 ARG C CZ  
9365  N NH1 . ARG C 323 ? 1.3968 1.3365 1.1098 -0.2781 0.1311  0.0170  624 ARG C NH1 
9366  N NH2 . ARG C 323 ? 1.3740 1.2512 1.0510 -0.2818 0.1162  0.0245  624 ARG C NH2 
9367  N N   . LYS C 324 ? 0.6331 0.5852 0.4016 -0.2150 0.1234  0.0038  625 LYS C N   
9368  C CA  . LYS C 324 ? 0.6788 0.6315 0.4482 -0.2022 0.1248  0.0008  625 LYS C CA  
9369  C C   . LYS C 324 ? 0.6703 0.6076 0.4443 -0.1865 0.1157  -0.0004 625 LYS C C   
9370  O O   . LYS C 324 ? 0.6770 0.5944 0.4448 -0.1866 0.1079  0.0025  625 LYS C O   
9371  C CB  . LYS C 324 ? 0.7976 0.7329 0.5416 -0.2092 0.1268  0.0041  625 LYS C CB  
9372  C CG  . LYS C 324 ? 0.9777 0.8775 0.6967 -0.2157 0.1186  0.0105  625 LYS C CG  
9373  C CD  . LYS C 324 ? 1.1143 1.0042 0.8092 -0.2322 0.1230  0.0152  625 LYS C CD  
9374  C CE  . LYS C 324 ? 1.1738 1.0257 0.8428 -0.2377 0.1141  0.0217  625 LYS C CE  
9375  N NZ  . LYS C 324 ? 1.0644 0.8950 0.7290 -0.2218 0.1049  0.0218  625 LYS C NZ  
9376  N N   . THR C 325 ? 0.5628 0.5093 0.3472 -0.1733 0.1171  -0.0047 626 THR C N   
9377  C CA  . THR C 325 ? 0.6310 0.5681 0.4230 -0.1586 0.1094  -0.0063 626 THR C CA  
9378  C C   . THR C 325 ? 0.5421 0.4481 0.3135 -0.1564 0.1014  -0.0023 626 THR C C   
9379  O O   . THR C 325 ? 0.5601 0.4531 0.3337 -0.1485 0.0935  -0.0016 626 THR C O   
9380  C CB  . THR C 325 ? 0.7029 0.6570 0.5097 -0.1464 0.1131  -0.0119 626 THR C CB  
9381  O OG1 . THR C 325 ? 0.7210 0.6712 0.5139 -0.1478 0.1172  -0.0122 626 THR C OG1 
9382  C CG2 . THR C 325 ? 0.6599 0.6449 0.4887 -0.1460 0.1202  -0.0159 626 THR C CG2 
9383  N N   . SER C 326 ? 0.5539 0.4481 0.3049 -0.1630 0.1033  0.0004  627 SER C N   
9384  C CA  . SER C 326 ? 0.5806 0.4476 0.3124 -0.1593 0.0957  0.0040  627 SER C CA  
9385  C C   . SER C 326 ? 0.6034 0.4453 0.3203 -0.1645 0.0885  0.0094  627 SER C C   
9386  O O   . SER C 326 ? 0.6237 0.4425 0.3266 -0.1592 0.0808  0.0125  627 SER C O   
9387  C CB  . SER C 326 ? 0.5457 0.4083 0.2595 -0.1649 0.1000  0.0052  627 SER C CB  
9388  O OG  . SER C 326 ? 0.6989 0.5637 0.4015 -0.1805 0.1063  0.0079  627 SER C OG  
9389  N N   . SER C 327 ? 0.5772 0.4228 0.2967 -0.1743 0.0904  0.0106  628 SER C N   
9390  C CA  . SER C 327 ? 0.6874 0.5085 0.3952 -0.1765 0.0827  0.0146  628 SER C CA  
9391  C C   . SER C 327 ? 0.6002 0.4179 0.3211 -0.1617 0.0756  0.0124  628 SER C C   
9392  O O   . SER C 327 ? 0.6370 0.4315 0.3469 -0.1598 0.0683  0.0153  628 SER C O   
9393  C CB  . SER C 327 ? 0.7039 0.5302 0.4119 -0.1910 0.0862  0.0158  628 SER C CB  
9394  O OG  . SER C 327 ? 0.6774 0.5284 0.4107 -0.1871 0.0885  0.0113  628 SER C OG  
9395  N N   . LEU C 328 ? 0.5227 0.3621 0.2657 -0.1511 0.0776  0.0073  629 LEU C N   
9396  C CA  . LEU C 328 ? 0.5554 0.3952 0.3126 -0.1377 0.0718  0.0050  629 LEU C CA  
9397  C C   . LEU C 328 ? 0.5467 0.3831 0.3083 -0.1406 0.0692  0.0054  629 LEU C C   
9398  O O   . LEU C 328 ? 0.4934 0.3179 0.2561 -0.1321 0.0627  0.0055  629 LEU C O   
9399  C CB  . LEU C 328 ? 0.5303 0.3493 0.2763 -0.1278 0.0640  0.0071  629 LEU C CB  
9400  C CG  . LEU C 328 ? 0.5795 0.4008 0.3200 -0.1249 0.0656  0.0067  629 LEU C CG  
9401  C CD1 . LEU C 328 ? 0.5056 0.3143 0.2429 -0.1128 0.0575  0.0076  629 LEU C CD1 
9402  C CD2 . LEU C 328 ? 0.5106 0.3592 0.2700 -0.1227 0.0729  0.0014  629 LEU C CD2 
9403  N N   . TRP C 329 ? 0.5829 0.4307 0.3470 -0.1530 0.0745  0.0054  630 TRP C N   
9404  C CA  . TRP C 329 ? 0.6000 0.4461 0.3684 -0.1570 0.0721  0.0054  630 TRP C CA  
9405  C C   . TRP C 329 ? 0.5735 0.4341 0.3641 -0.1447 0.0702  0.0012  630 TRP C C   
9406  O O   . TRP C 329 ? 0.5578 0.4072 0.3480 -0.1416 0.0648  0.0014  630 TRP C O   
9407  C CB  . TRP C 329 ? 0.5424 0.4034 0.3123 -0.1729 0.0784  0.0059  630 TRP C CB  
9408  C CG  . TRP C 329 ? 0.5431 0.4388 0.3344 -0.1728 0.0864  0.0019  630 TRP C CG  
9409  C CD1 . TRP C 329 ? 0.5768 0.4865 0.3678 -0.1764 0.0936  0.0013  630 TRP C CD1 
9410  C CD2 . TRP C 329 ? 0.4641 0.3845 0.2791 -0.1686 0.0879  -0.0019 630 TRP C CD2 
9411  N NE1 . TRP C 329 ? 0.5220 0.4635 0.3356 -0.1739 0.0996  -0.0029 630 TRP C NE1 
9412  C CE2 . TRP C 329 ? 0.4534 0.4018 0.2821 -0.1690 0.0960  -0.0047 630 TRP C CE2 
9413  C CE3 . TRP C 329 ? 0.4725 0.3936 0.2978 -0.1644 0.0832  -0.0032 630 TRP C CE3 
9414  C CZ2 . TRP C 329 ? 0.4663 0.4430 0.3188 -0.1646 0.0990  -0.0085 630 TRP C CZ2 
9415  C CZ3 . TRP C 329 ? 0.5287 0.4778 0.3772 -0.1609 0.0860  -0.0068 630 TRP C CZ3 
9416  C CH2 . TRP C 329 ? 0.4222 0.3988 0.2843 -0.1607 0.0937  -0.0093 630 TRP C CH2 
9417  N N   . LYS C 330 ? 0.4745 0.3585 0.2832 -0.1375 0.0744  -0.0025 631 LYS C N   
9418  C CA  . LYS C 330 ? 0.4578 0.3540 0.2861 -0.1260 0.0723  -0.0061 631 LYS C CA  
9419  C C   . LYS C 330 ? 0.5538 0.4315 0.3774 -0.1146 0.0650  -0.0055 631 LYS C C   
9420  O O   . LYS C 330 ? 0.4815 0.3570 0.3119 -0.1091 0.0611  -0.0065 631 LYS C O   
9421  C CB  . LYS C 330 ? 0.4238 0.3449 0.2697 -0.1198 0.0778  -0.0100 631 LYS C CB  
9422  C CG  . LYS C 330 ? 0.5238 0.4693 0.3808 -0.1279 0.0849  -0.0116 631 LYS C CG  
9423  C CD  . LYS C 330 ? 0.5193 0.4871 0.3936 -0.1191 0.0896  -0.0158 631 LYS C CD  
9424  C CE  . LYS C 330 ? 0.5314 0.5262 0.4200 -0.1247 0.0960  -0.0177 631 LYS C CE  
9425  N NZ  . LYS C 330 ? 0.4399 0.4541 0.3445 -0.1142 0.1001  -0.0221 631 LYS C NZ  
9426  N N   . ASP C 331 ? 0.4365 0.3022 0.2488 -0.1108 0.0633  -0.0039 632 ASP C N   
9427  C CA  . ASP C 331 ? 0.4769 0.3273 0.2852 -0.0997 0.0564  -0.0031 632 ASP C CA  
9428  C C   . ASP C 331 ? 0.4960 0.3238 0.2911 -0.1012 0.0508  -0.0004 632 ASP C C   
9429  O O   . ASP C 331 ? 0.4744 0.2969 0.2741 -0.0919 0.0460  -0.0012 632 ASP C O   
9430  C CB  . ASP C 331 ? 0.5557 0.3973 0.3522 -0.0972 0.0552  -0.0014 632 ASP C CB  
9431  C CG  . ASP C 331 ? 0.5159 0.3763 0.3202 -0.0984 0.0617  -0.0041 632 ASP C CG  
9432  O OD1 . ASP C 331 ? 0.4951 0.3638 0.2973 -0.1084 0.0678  -0.0041 632 ASP C OD1 
9433  O OD2 . ASP C 331 ? 0.5052 0.3723 0.3176 -0.0894 0.0607  -0.0063 632 ASP C OD2 
9434  N N   . GLN C 332 ? 0.5101 0.3238 0.2878 -0.1130 0.0514  0.0029  633 GLN C N   
9435  C CA  . GLN C 332 ? 0.5695 0.3580 0.3313 -0.1152 0.0461  0.0056  633 GLN C CA  
9436  C C   . GLN C 332 ? 0.5147 0.3095 0.2877 -0.1150 0.0455  0.0030  633 GLN C C   
9437  O O   . GLN C 332 ? 0.5463 0.3270 0.3161 -0.1075 0.0402  0.0028  633 GLN C O   
9438  C CB  . GLN C 332 ? 0.6117 0.3847 0.3523 -0.1299 0.0476  0.0097  633 GLN C CB  
9439  C CG  . GLN C 332 ? 0.7873 0.5283 0.5034 -0.1277 0.0413  0.0141  633 GLN C CG  
9440  C CD  . GLN C 332 ? 0.8557 0.5823 0.5499 -0.1424 0.0433  0.0185  633 GLN C CD  
9441  O OE1 . GLN C 332 ? 0.7185 0.4610 0.4166 -0.1547 0.0500  0.0181  633 GLN C OE1 
9442  N NE2 . GLN C 332 ? 1.0706 0.7675 0.7414 -0.1411 0.0377  0.0229  633 GLN C NE2 
9443  N N   . ALA C 333 ? 0.4990 0.3157 0.2853 -0.1229 0.0509  0.0010  634 ALA C N   
9444  C CA  . ALA C 333 ? 0.5417 0.3659 0.3386 -0.1238 0.0502  -0.0013 634 ALA C CA  
9445  C C   . ALA C 333 ? 0.4979 0.3321 0.3116 -0.1092 0.0480  -0.0046 634 ALA C C   
9446  O O   . ALA C 333 ? 0.5286 0.3558 0.3432 -0.1054 0.0444  -0.0057 634 ALA C O   
9447  C CB  . ALA C 333 ? 0.5375 0.3860 0.3461 -0.1349 0.0563  -0.0026 634 ALA C CB  
9448  N N   . LEU C 334 ? 0.4778 0.3275 0.3038 -0.1015 0.0503  -0.0062 635 LEU C N   
9449  C CA  . LEU C 334 ? 0.4159 0.2750 0.2570 -0.0885 0.0484  -0.0089 635 LEU C CA  
9450  C C   . LEU C 334 ? 0.5145 0.3534 0.3467 -0.0796 0.0421  -0.0080 635 LEU C C   
9451  O O   . LEU C 334 ? 0.4961 0.3377 0.3368 -0.0727 0.0399  -0.0099 635 LEU C O   
9452  C CB  . LEU C 334 ? 0.3919 0.2649 0.2419 -0.0830 0.0513  -0.0101 635 LEU C CB  
9453  C CG  . LEU C 334 ? 0.4770 0.3595 0.3417 -0.0707 0.0495  -0.0126 635 LEU C CG  
9454  C CD1 . LEU C 334 ? 0.4056 0.3052 0.2869 -0.0697 0.0512  -0.0153 635 LEU C CD1 
9455  C CD2 . LEU C 334 ? 0.3891 0.2803 0.2577 -0.0669 0.0518  -0.0136 635 LEU C CD2 
9456  N N   . VAL C 335 ? 0.4311 0.2500 0.2458 -0.0794 0.0392  -0.0049 636 VAL C N   
9457  C CA  . VAL C 335 ? 0.5265 0.3269 0.3327 -0.0696 0.0331  -0.0040 636 VAL C CA  
9458  C C   . VAL C 335 ? 0.5272 0.3133 0.3260 -0.0717 0.0307  -0.0043 636 VAL C C   
9459  O O   . VAL C 335 ? 0.4624 0.2461 0.2657 -0.0623 0.0277  -0.0060 636 VAL C O   
9460  C CB  . VAL C 335 ? 0.5786 0.3600 0.3665 -0.0690 0.0301  -0.0002 636 VAL C CB  
9461  C CG1 . VAL C 335 ? 0.5303 0.2922 0.3087 -0.0587 0.0237  0.0008  636 VAL C CG1 
9462  C CG2 . VAL C 335 ? 0.5000 0.2952 0.2953 -0.0652 0.0316  -0.0004 636 VAL C CG2 
9463  N N   . GLU C 336 ? 0.4918 0.2685 0.2787 -0.0846 0.0320  -0.0027 637 GLU C N   
9464  C CA  . GLU C 336 ? 0.5634 0.3238 0.3404 -0.0880 0.0294  -0.0031 637 GLU C CA  
9465  C C   . GLU C 336 ? 0.5603 0.3383 0.3549 -0.0854 0.0305  -0.0069 637 GLU C C   
9466  O O   . GLU C 336 ? 0.5313 0.2978 0.3220 -0.0803 0.0272  -0.0083 637 GLU C O   
9467  C CB  . GLU C 336 ? 0.5371 0.2868 0.2990 -0.1045 0.0309  -0.0006 637 GLU C CB  
9468  C CG  . GLU C 336 ? 0.5732 0.3041 0.3157 -0.1080 0.0298  0.0036  637 GLU C CG  
9469  C CD  . GLU C 336 ? 0.6699 0.3688 0.3923 -0.1001 0.0233  0.0056  637 GLU C CD  
9470  O OE1 . GLU C 336 ? 0.6565 0.3465 0.3787 -0.0931 0.0202  0.0034  637 GLU C OE1 
9471  O OE2 . GLU C 336 ? 0.7258 0.4079 0.4320 -0.1006 0.0214  0.0093  637 GLU C OE2 
9472  N N   . ILE C 337 ? 0.5152 0.3204 0.3284 -0.0885 0.0350  -0.0086 638 ILE C N   
9473  C CA  . ILE C 337 ? 0.4712 0.2939 0.3013 -0.0857 0.0358  -0.0118 638 ILE C CA  
9474  C C   . ILE C 337 ? 0.5132 0.3359 0.3503 -0.0710 0.0331  -0.0135 638 ILE C C   
9475  O O   . ILE C 337 ? 0.4381 0.2597 0.2782 -0.0673 0.0313  -0.0156 638 ILE C O   
9476  C CB  . ILE C 337 ? 0.4173 0.2687 0.2656 -0.0897 0.0410  -0.0130 638 ILE C CB  
9477  C CG1 . ILE C 337 ? 0.4483 0.3027 0.2909 -0.1050 0.0440  -0.0115 638 ILE C CG1 
9478  C CG2 . ILE C 337 ? 0.4006 0.2708 0.2673 -0.0847 0.0413  -0.0160 638 ILE C CG2 
9479  C CD1 . ILE C 337 ? 0.5079 0.3894 0.3664 -0.1079 0.0496  -0.0124 638 ILE C CD1 
9480  N N   . ASN C 338 ? 0.5003 0.3243 0.3395 -0.0629 0.0327  -0.0127 639 ASN C N   
9481  C CA  . ASN C 338 ? 0.4975 0.3245 0.3447 -0.0497 0.0304  -0.0142 639 ASN C CA  
9482  C C   . ASN C 338 ? 0.4800 0.2841 0.3128 -0.0434 0.0259  -0.0137 639 ASN C C   
9483  O O   . ASN C 338 ? 0.4852 0.2913 0.3238 -0.0342 0.0243  -0.0157 639 ASN C O   
9484  C CB  . ASN C 338 ? 0.4434 0.2804 0.2977 -0.0440 0.0312  -0.0136 639 ASN C CB  
9485  C CG  . ASN C 338 ? 0.4343 0.2953 0.3064 -0.0451 0.0353  -0.0155 639 ASN C CG  
9486  O OD1 . ASN C 338 ? 0.3989 0.2716 0.2840 -0.0383 0.0352  -0.0175 639 ASN C OD1 
9487  N ND2 . ASN C 338 ? 0.4122 0.2808 0.2848 -0.0538 0.0390  -0.0150 639 ASN C ND2 
9488  N N   . ILE C 339 ? 0.4869 0.2686 0.3001 -0.0480 0.0238  -0.0111 640 ILE C N   
9489  C CA  . ILE C 339 ? 0.4765 0.2334 0.2736 -0.0427 0.0195  -0.0108 640 ILE C CA  
9490  C C   . ILE C 339 ? 0.5370 0.2909 0.3336 -0.0458 0.0195  -0.0135 640 ILE C C   
9491  O O   . ILE C 339 ? 0.5202 0.2665 0.3150 -0.0366 0.0173  -0.0155 640 ILE C O   
9492  C CB  . ILE C 339 ? 0.4862 0.2176 0.2604 -0.0488 0.0172  -0.0072 640 ILE C CB  
9493  C CG1 . ILE C 339 ? 0.4868 0.2178 0.2591 -0.0426 0.0157  -0.0045 640 ILE C CG1 
9494  C CG2 . ILE C 339 ? 0.5122 0.2149 0.2672 -0.0458 0.0131  -0.0072 640 ILE C CG2 
9495  C CD1 . ILE C 339 ? 0.5149 0.2215 0.2642 -0.0491 0.0135  -0.0003 640 ILE C CD1 
9496  N N   . ALA C 340 ? 0.5056 0.2669 0.3044 -0.0588 0.0222  -0.0138 641 ALA C N   
9497  C CA  . ALA C 340 ? 0.5731 0.3319 0.3705 -0.0635 0.0218  -0.0162 641 ALA C CA  
9498  C C   . ALA C 340 ? 0.5835 0.3607 0.3987 -0.0542 0.0225  -0.0194 641 ALA C C   
9499  O O   . ALA C 340 ? 0.5228 0.2904 0.3331 -0.0495 0.0205  -0.0217 641 ALA C O   
9500  C CB  . ALA C 340 ? 0.5410 0.3092 0.3401 -0.0795 0.0244  -0.0156 641 ALA C CB  
9501  N N   . VAL C 341 ? 0.4371 0.2395 0.2716 -0.0518 0.0254  -0.0197 642 VAL C N   
9502  C CA  . VAL C 341 ? 0.4782 0.2979 0.3290 -0.0437 0.0261  -0.0222 642 VAL C CA  
9503  C C   . VAL C 341 ? 0.4989 0.3082 0.3457 -0.0307 0.0236  -0.0233 642 VAL C C   
9504  O O   . VAL C 341 ? 0.4756 0.2846 0.3237 -0.0265 0.0229  -0.0257 642 VAL C O   
9505  C CB  . VAL C 341 ? 0.4438 0.2882 0.3131 -0.0424 0.0292  -0.0219 642 VAL C CB  
9506  C CG1 . VAL C 341 ? 0.3702 0.2290 0.2540 -0.0331 0.0295  -0.0239 642 VAL C CG1 
9507  C CG2 . VAL C 341 ? 0.4213 0.2794 0.2970 -0.0539 0.0320  -0.0218 642 VAL C CG2 
9508  N N   . LEU C 342 ? 0.4239 0.2248 0.2651 -0.0242 0.0221  -0.0215 643 LEU C N   
9509  C CA  . LEU C 342 ? 0.4441 0.2389 0.2837 -0.0108 0.0198  -0.0224 643 LEU C CA  
9510  C C   . LEU C 342 ? 0.4756 0.2462 0.2977 -0.0088 0.0173  -0.0237 643 LEU C C   
9511  O O   . LEU C 342 ? 0.4377 0.2082 0.2614 -0.0005 0.0170  -0.0264 643 LEU C O   
9512  C CB  . LEU C 342 ? 0.4165 0.2086 0.2540 -0.0045 0.0181  -0.0199 643 LEU C CB  
9513  C CG  . LEU C 342 ? 0.4227 0.2386 0.2778 -0.0043 0.0203  -0.0194 643 LEU C CG  
9514  C CD1 . LEU C 342 ? 0.4425 0.2533 0.2916 -0.0034 0.0187  -0.0164 643 LEU C CD1 
9515  C CD2 . LEU C 342 ? 0.4223 0.2540 0.2918 0.0051  0.0208  -0.0214 643 LEU C CD2 
9516  N N   . TYR C 343 ? 0.4795 0.2282 0.2833 -0.0162 0.0156  -0.0220 644 TYR C N   
9517  C CA  . TYR C 343 ? 0.5506 0.2725 0.3347 -0.0155 0.0130  -0.0233 644 TYR C CA  
9518  C C   . TYR C 343 ? 0.5763 0.3022 0.3632 -0.0192 0.0141  -0.0268 644 TYR C C   
9519  O O   . TYR C 343 ? 0.5342 0.2469 0.3125 -0.0120 0.0127  -0.0295 644 TYR C O   
9520  C CB  . TYR C 343 ? 0.5525 0.2522 0.3171 -0.0268 0.0114  -0.0204 644 TYR C CB  
9521  C CG  . TYR C 343 ? 0.5924 0.2621 0.3344 -0.0297 0.0088  -0.0217 644 TYR C CG  
9522  C CD1 . TYR C 343 ? 0.6340 0.2801 0.3609 -0.0176 0.0055  -0.0223 644 TYR C CD1 
9523  C CD2 . TYR C 343 ? 0.6404 0.3049 0.3754 -0.0448 0.0093  -0.0222 644 TYR C CD2 
9524  C CE1 . TYR C 343 ? 0.6834 0.2988 0.3873 -0.0199 0.0029  -0.0237 644 TYR C CE1 
9525  C CE2 . TYR C 343 ? 0.7277 0.3624 0.4400 -0.0486 0.0065  -0.0234 644 TYR C CE2 
9526  C CZ  . TYR C 343 ? 0.7184 0.3273 0.4143 -0.0359 0.0034  -0.0243 644 TYR C CZ  
9527  O OH  . TYR C 343 ? 0.8117 0.3879 0.4829 -0.0389 0.0005  -0.0258 644 TYR C OH  
9528  N N   . SER C 344 ? 0.5295 0.2735 0.3278 -0.0301 0.0165  -0.0268 645 SER C N   
9529  C CA  . SER C 344 ? 0.5375 0.2854 0.3375 -0.0351 0.0169  -0.0297 645 SER C CA  
9530  C C   . SER C 344 ? 0.4912 0.2524 0.3033 -0.0236 0.0178  -0.0325 645 SER C C   
9531  O O   . SER C 344 ? 0.4897 0.2403 0.2936 -0.0206 0.0168  -0.0354 645 SER C O   
9532  C CB  . SER C 344 ? 0.4905 0.2576 0.3017 -0.0484 0.0189  -0.0286 645 SER C CB  
9533  O OG  . SER C 344 ? 0.5446 0.2977 0.3420 -0.0604 0.0182  -0.0263 645 SER C OG  
9534  N N   . PHE C 345 ? 0.4935 0.2770 0.3239 -0.0173 0.0198  -0.0316 646 PHE C N   
9535  C CA  . PHE C 345 ? 0.4587 0.2555 0.3005 -0.0071 0.0209  -0.0339 646 PHE C CA  
9536  C C   . PHE C 345 ? 0.5723 0.3527 0.4032 0.0051  0.0194  -0.0354 646 PHE C C   
9537  O O   . PHE C 345 ? 0.5140 0.2930 0.3432 0.0107  0.0198  -0.0384 646 PHE C O   
9538  C CB  . PHE C 345 ? 0.3825 0.2035 0.2439 -0.0035 0.0230  -0.0323 646 PHE C CB  
9539  C CG  . PHE C 345 ? 0.3637 0.2053 0.2395 -0.0109 0.0250  -0.0322 646 PHE C CG  
9540  C CD1 . PHE C 345 ? 0.4287 0.2718 0.3036 -0.0225 0.0253  -0.0309 646 PHE C CD1 
9541  C CD2 . PHE C 345 ? 0.4015 0.2616 0.2920 -0.0061 0.0265  -0.0331 646 PHE C CD2 
9542  C CE1 . PHE C 345 ? 0.4235 0.2867 0.3125 -0.0279 0.0271  -0.0308 646 PHE C CE1 
9543  C CE2 . PHE C 345 ? 0.3461 0.2239 0.2492 -0.0118 0.0280  -0.0328 646 PHE C CE2 
9544  C CZ  . PHE C 345 ? 0.4244 0.3042 0.3272 -0.0221 0.0282  -0.0318 646 PHE C CZ  
9545  N N   . GLN C 346 ? 0.4988 0.2669 0.3217 0.0098  0.0176  -0.0334 647 GLN C N   
9546  C CA  . GLN C 346 ? 0.5722 0.3258 0.3853 0.0230  0.0160  -0.0348 647 GLN C CA  
9547  C C   . GLN C 346 ? 0.5650 0.2929 0.3581 0.0222  0.0146  -0.0375 647 GLN C C   
9548  O O   . GLN C 346 ? 0.6209 0.3434 0.4099 0.0327  0.0148  -0.0406 647 GLN C O   
9549  C CB  . GLN C 346 ? 0.5678 0.3124 0.3752 0.0278  0.0136  -0.0316 647 GLN C CB  
9550  C CG  . GLN C 346 ? 0.5942 0.3634 0.4206 0.0325  0.0146  -0.0297 647 GLN C CG  
9551  C CD  . GLN C 346 ? 0.7005 0.4622 0.5211 0.0334  0.0120  -0.0260 647 GLN C CD  
9552  O OE1 . GLN C 346 ? 0.7610 0.4985 0.5631 0.0306  0.0095  -0.0245 647 GLN C OE1 
9553  N NE2 . GLN C 346 ? 0.6493 0.4308 0.4846 0.0368  0.0124  -0.0245 647 GLN C NE2 
9554  N N   . SER C 347 ? 0.5586 0.2709 0.3387 0.0093  0.0133  -0.0367 648 SER C N   
9555  C CA  . SER C 347 ? 0.5947 0.2805 0.3538 0.0066  0.0115  -0.0393 648 SER C CA  
9556  C C   . SER C 347 ? 0.6546 0.3497 0.4187 0.0059  0.0132  -0.0433 648 SER C C   
9557  O O   . SER C 347 ? 0.5993 0.2762 0.3489 0.0111  0.0124  -0.0468 648 SER C O   
9558  C CB  . SER C 347 ? 0.6115 0.2810 0.3566 -0.0092 0.0098  -0.0371 648 SER C CB  
9559  O OG  . SER C 347 ? 0.6285 0.2829 0.3634 -0.0078 0.0078  -0.0336 648 SER C OG  
9560  N N   . ASP C 348 ? 0.5735 0.2958 0.3568 0.0000  0.0154  -0.0428 649 ASP C N   
9561  C CA  . ASP C 348 ? 0.5518 0.2844 0.3404 -0.0003 0.0168  -0.0460 649 ASP C CA  
9562  C C   . ASP C 348 ? 0.5616 0.3105 0.3631 0.0134  0.0192  -0.0475 649 ASP C C   
9563  O O   . ASP C 348 ? 0.4912 0.2513 0.2986 0.0138  0.0207  -0.0498 649 ASP C O   
9564  C CB  . ASP C 348 ? 0.4923 0.2450 0.2939 -0.0132 0.0174  -0.0447 649 ASP C CB  
9565  C CG  . ASP C 348 ? 0.5766 0.3147 0.3648 -0.0281 0.0152  -0.0440 649 ASP C CG  
9566  O OD1 . ASP C 348 ? 0.5863 0.2963 0.3535 -0.0288 0.0130  -0.0447 649 ASP C OD1 
9567  O OD2 . ASP C 348 ? 0.6204 0.3750 0.4188 -0.0391 0.0155  -0.0427 649 ASP C OD2 
9568  N N   . LYS C 349 ? 0.5494 0.3005 0.3551 0.0241  0.0194  -0.0461 650 LYS C N   
9569  C CA  . LYS C 349 ? 0.5325 0.2999 0.3504 0.0369  0.0217  -0.0473 650 LYS C CA  
9570  C C   . LYS C 349 ? 0.5293 0.3255 0.3678 0.0331  0.0242  -0.0465 650 LYS C C   
9571  O O   . LYS C 349 ? 0.5235 0.3309 0.3681 0.0381  0.0264  -0.0486 650 LYS C O   
9572  C CB  . LYS C 349 ? 0.6527 0.4064 0.4581 0.0462  0.0223  -0.0517 650 LYS C CB  
9573  C CG  . LYS C 349 ? 0.7649 0.4877 0.5484 0.0517  0.0197  -0.0527 650 LYS C CG  
9574  C CD  . LYS C 349 ? 0.8823 0.5920 0.6535 0.0626  0.0208  -0.0577 650 LYS C CD  
9575  C CE  . LYS C 349 ? 1.0296 0.7212 0.7892 0.0768  0.0192  -0.0580 650 LYS C CE  
9576  N NZ  . LYS C 349 ? 1.1368 0.8226 0.8892 0.0910  0.0214  -0.0630 650 LYS C NZ  
9577  N N   . VAL C 350 ? 0.4203 0.2277 0.2686 0.0241  0.0240  -0.0434 651 VAL C N   
9578  C CA  . VAL C 350 ? 0.3994 0.2324 0.2668 0.0212  0.0259  -0.0421 651 VAL C CA  
9579  C C   . VAL C 350 ? 0.4861 0.3308 0.3646 0.0262  0.0264  -0.0395 651 VAL C C   
9580  O O   . VAL C 350 ? 0.4067 0.2441 0.2813 0.0236  0.0249  -0.0373 651 VAL C O   
9581  C CB  . VAL C 350 ? 0.4467 0.2845 0.3170 0.0081  0.0255  -0.0409 651 VAL C CB  
9582  C CG1 . VAL C 350 ? 0.4088 0.2716 0.2982 0.0064  0.0273  -0.0393 651 VAL C CG1 
9583  C CG2 . VAL C 350 ? 0.3857 0.2117 0.2440 0.0020  0.0243  -0.0433 651 VAL C CG2 
9584  N N   . THR C 351 ? 0.4026 0.2648 0.2939 0.0329  0.0282  -0.0396 652 THR C N   
9585  C CA  . THR C 351 ? 0.3713 0.2454 0.2731 0.0373  0.0283  -0.0374 652 THR C CA  
9586  C C   . THR C 351 ? 0.4379 0.3161 0.3445 0.0289  0.0277  -0.0347 652 THR C C   
9587  O O   . THR C 351 ? 0.3886 0.2747 0.3011 0.0210  0.0287  -0.0343 652 THR C O   
9588  C CB  . THR C 351 ? 0.4088 0.3039 0.3251 0.0414  0.0306  -0.0376 652 THR C CB  
9589  O OG1 . THR C 351 ? 0.4503 0.3433 0.3622 0.0485  0.0319  -0.0404 652 THR C OG1 
9590  C CG2 . THR C 351 ? 0.3133 0.2193 0.2386 0.0463  0.0301  -0.0355 652 THR C CG2 
9591  N N   . ILE C 352 ? 0.3737 0.2469 0.2776 0.0312  0.0261  -0.0328 653 ILE C N   
9592  C CA  . ILE C 352 ? 0.3845 0.2623 0.2926 0.0245  0.0260  -0.0303 653 ILE C CA  
9593  C C   . ILE C 352 ? 0.4082 0.2861 0.3165 0.0309  0.0242  -0.0286 653 ILE C C   
9594  O O   . ILE C 352 ? 0.4424 0.3120 0.3442 0.0395  0.0224  -0.0290 653 ILE C O   
9595  C CB  . ILE C 352 ? 0.3756 0.2391 0.2724 0.0151  0.0253  -0.0297 653 ILE C CB  
9596  C CG1 . ILE C 352 ? 0.3820 0.2556 0.2861 0.0073  0.0266  -0.0278 653 ILE C CG1 
9597  C CG2 . ILE C 352 ? 0.3858 0.2270 0.2657 0.0181  0.0226  -0.0290 653 ILE C CG2 
9598  C CD1 . ILE C 352 ? 0.3357 0.2024 0.2331 -0.0036 0.0270  -0.0275 653 ILE C CD1 
9599  N N   . VAL C 353 ? 0.3324 0.2201 0.2481 0.0273  0.0244  -0.0267 654 VAL C N   
9600  C CA  . VAL C 353 ? 0.3675 0.2565 0.2835 0.0322  0.0223  -0.0248 654 VAL C CA  
9601  C C   . VAL C 353 ? 0.3342 0.2172 0.2449 0.0247  0.0218  -0.0228 654 VAL C C   
9602  O O   . VAL C 353 ? 0.3269 0.2168 0.2427 0.0169  0.0242  -0.0229 654 VAL C O   
9603  C CB  . VAL C 353 ? 0.3929 0.3022 0.3239 0.0360  0.0230  -0.0248 654 VAL C CB  
9604  C CG1 . VAL C 353 ? 0.3188 0.2405 0.2597 0.0284  0.0253  -0.0247 654 VAL C CG1 
9605  C CG2 . VAL C 353 ? 0.4139 0.3251 0.3449 0.0423  0.0199  -0.0231 654 VAL C CG2 
9606  N N   . ASP C 354 ? 0.3386 0.2085 0.2382 0.0273  0.0188  -0.0209 655 ASP C N   
9607  C CA  . ASP C 354 ? 0.4159 0.2805 0.3095 0.0202  0.0186  -0.0188 655 ASP C CA  
9608  C C   . ASP C 354 ? 0.4703 0.3502 0.3742 0.0207  0.0186  -0.0180 655 ASP C C   
9609  O O   . ASP C 354 ? 0.3737 0.2652 0.2867 0.0273  0.0175  -0.0183 655 ASP C O   
9610  C CB  . ASP C 354 ? 0.4138 0.2569 0.2898 0.0219  0.0152  -0.0167 655 ASP C CB  
9611  C CG  . ASP C 354 ? 0.5239 0.3669 0.3993 0.0327  0.0112  -0.0154 655 ASP C CG  
9612  O OD1 . ASP C 354 ? 0.6298 0.4665 0.5019 0.0416  0.0095  -0.0164 655 ASP C OD1 
9613  O OD2 . ASP C 354 ? 0.5538 0.4035 0.4319 0.0326  0.0097  -0.0136 655 ASP C OD2 
9614  N N   . HIS C 355 ? 0.4045 0.2845 0.3062 0.0130  0.0199  -0.0169 656 HIS C N   
9615  C CA  . HIS C 355 ? 0.3937 0.2870 0.3040 0.0125  0.0203  -0.0167 656 HIS C CA  
9616  C C   . HIS C 355 ? 0.3856 0.2779 0.2931 0.0191  0.0158  -0.0149 656 HIS C C   
9617  O O   . HIS C 355 ? 0.4339 0.3395 0.3507 0.0209  0.0152  -0.0151 656 HIS C O   
9618  C CB  . HIS C 355 ? 0.3650 0.2579 0.2722 0.0035  0.0231  -0.0164 656 HIS C CB  
9619  C CG  . HIS C 355 ? 0.3366 0.2128 0.2278 -0.0007 0.0220  -0.0142 656 HIS C CG  
9620  N ND1 . HIS C 355 ? 0.3991 0.2630 0.2813 -0.0049 0.0228  -0.0140 656 HIS C ND1 
9621  C CD2 . HIS C 355 ? 0.3631 0.2324 0.2447 -0.0026 0.0204  -0.0121 656 HIS C CD2 
9622  C CE1 . HIS C 355 ? 0.4566 0.3063 0.3242 -0.0092 0.0216  -0.0116 656 HIS C CE1 
9623  N NE2 . HIS C 355 ? 0.3912 0.2438 0.2580 -0.0076 0.0202  -0.0103 656 HIS C NE2 
9624  N N   . HIS C 356 ? 0.4077 0.2846 0.3025 0.0229  0.0124  -0.0130 657 HIS C N   
9625  C CA  . HIS C 356 ? 0.3813 0.2592 0.2745 0.0301  0.0075  -0.0111 657 HIS C CA  
9626  C C   . HIS C 356 ? 0.4196 0.3106 0.3245 0.0392  0.0064  -0.0123 657 HIS C C   
9627  O O   . HIS C 356 ? 0.4143 0.3198 0.3283 0.0418  0.0046  -0.0120 657 HIS C O   
9628  C CB  . HIS C 356 ? 0.4230 0.2797 0.2986 0.0327  0.0038  -0.0085 657 HIS C CB  
9629  C CG  . HIS C 356 ? 0.4737 0.3177 0.3368 0.0228  0.0052  -0.0070 657 HIS C CG  
9630  N ND1 . HIS C 356 ? 0.4637 0.3109 0.3247 0.0178  0.0050  -0.0055 657 HIS C ND1 
9631  C CD2 . HIS C 356 ? 0.4542 0.2832 0.3063 0.0163  0.0073  -0.0068 657 HIS C CD2 
9632  C CE1 . HIS C 356 ? 0.5045 0.3398 0.3538 0.0089  0.0072  -0.0045 657 HIS C CE1 
9633  N NE2 . HIS C 356 ? 0.5330 0.3576 0.3772 0.0075  0.0086  -0.0051 657 HIS C NE2 
9634  N N   . SER C 357 ? 0.4441 0.3310 0.3489 0.0433  0.0076  -0.0140 658 SER C N   
9635  C CA  A SER C 357 ? 0.3741 0.2746 0.2900 0.0515  0.0076  -0.0154 658 SER C CA  
9636  C CA  B SER C 357 ? 0.3746 0.2752 0.2905 0.0516  0.0075  -0.0154 658 SER C CA  
9637  C C   . SER C 357 ? 0.3126 0.2336 0.2442 0.0474  0.0105  -0.0168 658 SER C C   
9638  O O   . SER C 357 ? 0.3608 0.2974 0.3024 0.0516  0.0091  -0.0166 658 SER C O   
9639  C CB  A SER C 357 ? 0.3557 0.2468 0.2670 0.0555  0.0092  -0.0175 658 SER C CB  
9640  C CB  B SER C 357 ? 0.3615 0.2525 0.2727 0.0557  0.0091  -0.0175 658 SER C CB  
9641  O OG  A SER C 357 ? 0.3841 0.2892 0.3058 0.0636  0.0097  -0.0190 658 SER C OG  
9642  O OG  B SER C 357 ? 0.4123 0.2814 0.3070 0.0592  0.0062  -0.0162 658 SER C OG  
9643  N N   . ALA C 358 ? 0.3171 0.2385 0.2507 0.0389  0.0143  -0.0179 659 ALA C N   
9644  C CA  . ALA C 358 ? 0.3109 0.2489 0.2577 0.0356  0.0169  -0.0192 659 ALA C CA  
9645  C C   . ALA C 358 ? 0.3907 0.3384 0.3424 0.0336  0.0152  -0.0180 659 ALA C C   
9646  O O   . ALA C 358 ? 0.3287 0.2911 0.2909 0.0345  0.0153  -0.0184 659 ALA C O   
9647  C CB  . ALA C 358 ? 0.2956 0.2312 0.2428 0.0279  0.0208  -0.0204 659 ALA C CB  
9648  N N   . THR C 359 ? 0.3949 0.3341 0.3380 0.0302  0.0136  -0.0166 660 THR C N   
9649  C CA  . THR C 359 ? 0.2865 0.2336 0.2325 0.0275  0.0118  -0.0158 660 THR C CA  
9650  C C   . THR C 359 ? 0.2900 0.2446 0.2386 0.0343  0.0069  -0.0143 660 THR C C   
9651  O O   . THR C 359 ? 0.2844 0.2524 0.2411 0.0330  0.0056  -0.0143 660 THR C O   
9652  C CB  . THR C 359 ? 0.3241 0.2603 0.2594 0.0217  0.0118  -0.0150 660 THR C CB  
9653  O OG1 . THR C 359 ? 0.3278 0.2493 0.2506 0.0245  0.0091  -0.0130 660 THR C OG1 
9654  C CG2 . THR C 359 ? 0.2894 0.2233 0.2250 0.0147  0.0170  -0.0167 660 THR C CG2 
9655  N N   . GLU C 360 ? 0.3021 0.2482 0.2438 0.0414  0.0039  -0.0130 661 GLU C N   
9656  C CA  . GLU C 360 ? 0.3878 0.3435 0.3337 0.0495  -0.0007 -0.0116 661 GLU C CA  
9657  C C   . GLU C 360 ? 0.4188 0.3934 0.3795 0.0523  0.0011  -0.0131 661 GLU C C   
9658  O O   . GLU C 360 ? 0.3783 0.3691 0.3478 0.0533  -0.0014 -0.0124 661 GLU C O   
9659  C CB  . GLU C 360 ? 0.3954 0.3372 0.3309 0.0582  -0.0036 -0.0103 661 GLU C CB  
9660  C CG  . GLU C 360 ? 0.5310 0.4837 0.4713 0.0684  -0.0086 -0.0089 661 GLU C CG  
9661  C CD  . GLU C 360 ? 0.8422 0.7793 0.7712 0.0786  -0.0118 -0.0077 661 GLU C CD  
9662  O OE1 . GLU C 360 ? 0.9424 0.8582 0.8581 0.0765  -0.0104 -0.0078 661 GLU C OE1 
9663  O OE2 . GLU C 360 ? 0.9212 0.8673 0.8542 0.0889  -0.0158 -0.0067 661 GLU C OE2 
9664  N N   . SER C 361 ? 0.3552 0.3284 0.3184 0.0528  0.0054  -0.0151 662 SER C N   
9665  C CA  . SER C 361 ? 0.3166 0.3070 0.2925 0.0547  0.0076  -0.0165 662 SER C CA  
9666  C C   . SER C 361 ? 0.3657 0.3685 0.3502 0.0465  0.0088  -0.0166 662 SER C C   
9667  O O   . SER C 361 ? 0.3274 0.3474 0.3220 0.0471  0.0081  -0.0163 662 SER C O   
9668  C CB  . SER C 361 ? 0.3511 0.3356 0.3260 0.0558  0.0119  -0.0186 662 SER C CB  
9669  O OG  . SER C 361 ? 0.4313 0.4062 0.3990 0.0649  0.0105  -0.0188 662 SER C OG  
9670  N N   . PHE C 362 ? 0.3307 0.3249 0.3109 0.0386  0.0106  -0.0170 663 PHE C N   
9671  C CA  . PHE C 362 ? 0.2975 0.3004 0.2839 0.0313  0.0119  -0.0175 663 PHE C CA  
9672  C C   . PHE C 362 ? 0.3527 0.3644 0.3411 0.0299  0.0076  -0.0161 663 PHE C C   
9673  O O   . PHE C 362 ? 0.3604 0.3848 0.3567 0.0261  0.0075  -0.0162 663 PHE C O   
9674  C CB  . PHE C 362 ? 0.3379 0.3297 0.3188 0.0245  0.0148  -0.0185 663 PHE C CB  
9675  C CG  . PHE C 362 ? 0.3590 0.3565 0.3441 0.0180  0.0158  -0.0191 663 PHE C CG  
9676  C CD1 . PHE C 362 ? 0.2595 0.2645 0.2522 0.0160  0.0184  -0.0199 663 PHE C CD1 
9677  C CD2 . PHE C 362 ? 0.2751 0.2692 0.2550 0.0137  0.0139  -0.0189 663 PHE C CD2 
9678  C CE1 . PHE C 362 ? 0.2531 0.2608 0.2479 0.0102  0.0189  -0.0204 663 PHE C CE1 
9679  C CE2 . PHE C 362 ? 0.3513 0.3485 0.3334 0.0079  0.0147  -0.0198 663 PHE C CE2 
9680  C CZ  . PHE C 362 ? 0.3821 0.3856 0.3716 0.0062  0.0171  -0.0206 663 PHE C CZ  
9681  N N   . ILE C 363 ? 0.3202 0.3251 0.3008 0.0324  0.0036  -0.0146 664 ILE C N   
9682  C CA  . ILE C 363 ? 0.3777 0.3919 0.3599 0.0316  -0.0014 -0.0130 664 ILE C CA  
9683  C C   . ILE C 363 ? 0.2947 0.3282 0.2885 0.0368  -0.0034 -0.0124 664 ILE C C   
9684  O O   . ILE C 363 ? 0.3515 0.3995 0.3526 0.0326  -0.0053 -0.0120 664 ILE C O   
9685  C CB  . ILE C 363 ? 0.2813 0.2839 0.2519 0.0344  -0.0057 -0.0111 664 ILE C CB  
9686  C CG1 . ILE C 363 ? 0.3999 0.3866 0.3594 0.0274  -0.0035 -0.0118 664 ILE C CG1 
9687  C CG2 . ILE C 363 ? 0.3298 0.3446 0.3031 0.0353  -0.0119 -0.0092 664 ILE C CG2 
9688  C CD1 . ILE C 363 ? 0.4036 0.3943 0.3638 0.0190  -0.0033 -0.0127 664 ILE C CD1 
9689  N N   . LYS C 364 ? 0.3090 0.3432 0.3043 0.0459  -0.0029 -0.0124 665 LYS C N   
9690  C CA  . LYS C 364 ? 0.3829 0.4374 0.3902 0.0516  -0.0038 -0.0121 665 LYS C CA  
9691  C C   . LYS C 364 ? 0.3480 0.4152 0.3651 0.0453  0.0003  -0.0133 665 LYS C C   
9692  O O   . LYS C 364 ? 0.2976 0.3839 0.3245 0.0430  -0.0013 -0.0126 665 LYS C O   
9693  C CB  . LYS C 364 ? 0.4242 0.4747 0.4296 0.0632  -0.0031 -0.0125 665 LYS C CB  
9694  C CG  . LYS C 364 ? 0.4763 0.5149 0.4717 0.0705  -0.0081 -0.0107 665 LYS C CG  
9695  C CD  . LYS C 364 ? 0.6703 0.7013 0.6616 0.0822  -0.0075 -0.0115 665 LYS C CD  
9696  C CE  . LYS C 364 ? 0.8168 0.8392 0.7993 0.0910  -0.0137 -0.0091 665 LYS C CE  
9697  N NZ  . LYS C 364 ? 0.8837 0.8941 0.8593 0.1029  -0.0133 -0.0100 665 LYS C NZ  
9698  N N   . HIS C 365 ? 0.3088 0.3656 0.3232 0.0416  0.0052  -0.0150 666 HIS C N   
9699  C CA  . HIS C 365 ? 0.3010 0.3665 0.3226 0.0350  0.0088  -0.0158 666 HIS C CA  
9700  C C   . HIS C 365 ? 0.3526 0.4226 0.3754 0.0256  0.0068  -0.0151 666 HIS C C   
9701  O O   . HIS C 365 ? 0.2310 0.3162 0.2620 0.0213  0.0067  -0.0146 666 HIS C O   
9702  C CB  . HIS C 365 ? 0.2743 0.3257 0.2910 0.0327  0.0134  -0.0174 666 HIS C CB  
9703  C CG  . HIS C 365 ? 0.3094 0.3652 0.3306 0.0253  0.0165  -0.0178 666 HIS C CG  
9704  N ND1 . HIS C 365 ? 0.2590 0.3289 0.2883 0.0252  0.0186  -0.0177 666 HIS C ND1 
9705  C CD2 . HIS C 365 ? 0.2794 0.3265 0.2972 0.0180  0.0179  -0.0183 666 HIS C CD2 
9706  C CE1 . HIS C 365 ? 0.2795 0.3478 0.3094 0.0178  0.0208  -0.0178 666 HIS C CE1 
9707  N NE2 . HIS C 365 ? 0.2819 0.3366 0.3052 0.0138  0.0203  -0.0183 666 HIS C NE2 
9708  N N   . MET C 366 ? 0.2971 0.3535 0.3110 0.0219  0.0052  -0.0152 667 MET C N   
9709  C CA  . MET C 366 ? 0.2886 0.3462 0.3014 0.0129  0.0035  -0.0151 667 MET C CA  
9710  C C   . MET C 366 ? 0.3128 0.3880 0.3321 0.0121  -0.0014 -0.0135 667 MET C C   
9711  O O   . MET C 366 ? 0.2988 0.3840 0.3232 0.0049  -0.0017 -0.0133 667 MET C O   
9712  C CB  . MET C 366 ? 0.3144 0.3550 0.3158 0.0104  0.0028  -0.0157 667 MET C CB  
9713  C CG  . MET C 366 ? 0.3870 0.4238 0.3848 0.0013  0.0027  -0.0166 667 MET C CG  
9714  S SD  . MET C 366 ? 0.4262 0.4453 0.4100 0.0002  0.0018  -0.0172 667 MET C SD  
9715  C CE  . MET C 366 ? 0.4548 0.4734 0.4341 -0.0093 -0.0007 -0.0182 667 MET C CE  
9716  N N   . GLU C 367 ? 0.3050 0.3846 0.3242 0.0195  -0.0054 -0.0121 668 GLU C N   
9717  C CA  . GLU C 367 ? 0.4021 0.5008 0.4285 0.0195  -0.0107 -0.0104 668 GLU C CA  
9718  C C   . GLU C 367 ? 0.3630 0.4830 0.4028 0.0199  -0.0087 -0.0102 668 GLU C C   
9719  O O   . GLU C 367 ? 0.3088 0.4451 0.3555 0.0134  -0.0111 -0.0093 668 GLU C O   
9720  C CB  . GLU C 367 ? 0.4160 0.5146 0.4394 0.0291  -0.0155 -0.0087 668 GLU C CB  
9721  C CG  . GLU C 367 ? 0.4557 0.5346 0.4649 0.0274  -0.0180 -0.0084 668 GLU C CG  
9722  C CD  . GLU C 367 ? 0.5888 0.6656 0.5933 0.0368  -0.0234 -0.0062 668 GLU C CD  
9723  O OE1 . GLU C 367 ? 0.5959 0.6807 0.6063 0.0470  -0.0237 -0.0056 668 GLU C OE1 
9724  O OE2 . GLU C 367 ? 0.6001 0.6665 0.5941 0.0344  -0.0273 -0.0051 668 GLU C OE2 
9725  N N   . ASN C 368 ? 0.3218 0.4421 0.3649 0.0268  -0.0043 -0.0110 669 ASN C N   
9726  C CA  . ASN C 368 ? 0.3277 0.4681 0.3827 0.0270  -0.0016 -0.0110 669 ASN C CA  
9727  C C   . ASN C 368 ? 0.3036 0.4455 0.3602 0.0148  0.0010  -0.0112 669 ASN C C   
9728  O O   . ASN C 368 ? 0.2887 0.4499 0.3541 0.0096  0.0005  -0.0102 669 ASN C O   
9729  C CB  . ASN C 368 ? 0.3508 0.4873 0.4061 0.0363  0.0031  -0.0123 669 ASN C CB  
9730  C CG  . ASN C 368 ? 0.3842 0.5409 0.4506 0.0366  0.0067  -0.0125 669 ASN C CG  
9731  O OD1 . ASN C 368 ? 0.3618 0.5411 0.4382 0.0388  0.0046  -0.0114 669 ASN C OD1 
9732  N ND2 . ASN C 368 ? 0.3767 0.5266 0.4415 0.0343  0.0122  -0.0138 669 ASN C ND2 
9733  N N   . GLU C 369 ? 0.2835 0.4050 0.3310 0.0101  0.0037  -0.0125 670 GLU C N   
9734  C CA  . GLU C 369 ? 0.2875 0.4060 0.3341 -0.0006 0.0058  -0.0127 670 GLU C CA  
9735  C C   . GLU C 369 ? 0.3117 0.4358 0.3578 -0.0100 0.0014  -0.0118 670 GLU C C   
9736  O O   . GLU C 369 ? 0.2923 0.4256 0.3424 -0.0185 0.0018  -0.0111 670 GLU C O   
9737  C CB  . GLU C 369 ? 0.2438 0.3393 0.2806 -0.0019 0.0089  -0.0143 670 GLU C CB  
9738  C CG  . GLU C 369 ? 0.2579 0.3487 0.2952 0.0045  0.0135  -0.0152 670 GLU C CG  
9739  C CD  . GLU C 369 ? 0.2906 0.3893 0.3332 0.0006  0.0171  -0.0148 670 GLU C CD  
9740  O OE1 . GLU C 369 ? 0.2847 0.3715 0.3227 -0.0035 0.0198  -0.0154 670 GLU C OE1 
9741  O OE2 . GLU C 369 ? 0.3277 0.4450 0.3786 0.0015  0.0171  -0.0138 670 GLU C OE2 
9742  N N   . TYR C 370 ? 0.3011 0.4184 0.3410 -0.0096 -0.0030 -0.0118 671 TYR C N   
9743  C CA  . TYR C 370 ? 0.2995 0.4232 0.3386 -0.0185 -0.0079 -0.0110 671 TYR C CA  
9744  C C   . TYR C 370 ? 0.2987 0.4498 0.3504 -0.0198 -0.0105 -0.0091 671 TYR C C   
9745  O O   . TYR C 370 ? 0.3422 0.5019 0.3962 -0.0304 -0.0119 -0.0085 671 TYR C O   
9746  C CB  . TYR C 370 ? 0.3648 0.4785 0.3949 -0.0167 -0.0126 -0.0111 671 TYR C CB  
9747  C CG  . TYR C 370 ? 0.3363 0.4263 0.3534 -0.0215 -0.0107 -0.0131 671 TYR C CG  
9748  C CD1 . TYR C 370 ? 0.3259 0.3996 0.3376 -0.0161 -0.0062 -0.0145 671 TYR C CD1 
9749  C CD2 . TYR C 370 ? 0.3314 0.4158 0.3416 -0.0315 -0.0133 -0.0139 671 TYR C CD2 
9750  C CE1 . TYR C 370 ? 0.3354 0.3902 0.3366 -0.0199 -0.0041 -0.0164 671 TYR C CE1 
9751  C CE2 . TYR C 370 ? 0.3766 0.4396 0.3747 -0.0348 -0.0110 -0.0162 671 TYR C CE2 
9752  C CZ  . TYR C 370 ? 0.4232 0.4726 0.4175 -0.0286 -0.0063 -0.0174 671 TYR C CZ  
9753  O OH  . TYR C 370 ? 0.4573 0.4880 0.4408 -0.0312 -0.0037 -0.0197 671 TYR C OH  
9754  N N   . ARG C 371 ? 0.3644 0.5295 0.4243 -0.0091 -0.0109 -0.0083 672 ARG C N   
9755  C CA  . ARG C 371 ? 0.3862 0.5805 0.4596 -0.0088 -0.0134 -0.0066 672 ARG C CA  
9756  C C   . ARG C 371 ? 0.4123 0.6192 0.4935 -0.0149 -0.0085 -0.0064 672 ARG C C   
9757  O O   . ARG C 371 ? 0.5133 0.7390 0.6016 -0.0238 -0.0104 -0.0050 672 ARG C O   
9758  C CB  . ARG C 371 ? 0.5177 0.7221 0.5969 0.0060  -0.0146 -0.0060 672 ARG C CB  
9759  C CG  . ARG C 371 ? 0.7289 0.9401 0.8079 0.0095  -0.0224 -0.0044 672 ARG C CG  
9760  C CD  . ARG C 371 ? 0.8711 1.0605 0.9388 0.0192  -0.0239 -0.0048 672 ARG C CD  
9761  N NE  . ARG C 371 ? 0.9290 1.1147 0.9899 0.0172  -0.0311 -0.0034 672 ARG C NE  
9762  C CZ  . ARG C 371 ? 0.9120 1.0793 0.9615 0.0235  -0.0336 -0.0031 672 ARG C CZ  
9763  N NH1 . ARG C 371 ? 0.9514 1.1023 0.9953 0.0319  -0.0295 -0.0041 672 ARG C NH1 
9764  N NH2 . ARG C 371 ? 0.8169 0.9818 0.8597 0.0208  -0.0403 -0.0017 672 ARG C NH2 
9765  N N   . CYS C 372 ? 0.3480 0.5452 0.4276 -0.0109 -0.0023 -0.0076 673 CYS C N   
9766  C CA  A CYS C 372 ? 0.4065 0.6163 0.4930 -0.0155 0.0025  -0.0071 673 CYS C CA  
9767  C CA  B CYS C 372 ? 0.4003 0.6102 0.4869 -0.0156 0.0025  -0.0071 673 CYS C CA  
9768  C C   . CYS C 372 ? 0.3992 0.5939 0.4779 -0.0280 0.0047  -0.0072 673 CYS C C   
9769  O O   . CYS C 372 ? 0.4753 0.6818 0.5586 -0.0363 0.0067  -0.0060 673 CYS C O   
9770  C CB  A CYS C 372 ? 0.3996 0.6091 0.4885 -0.0043 0.0080  -0.0083 673 CYS C CB  
9771  C CB  B CYS C 372 ? 0.4059 0.6158 0.4950 -0.0042 0.0078  -0.0082 673 CYS C CB  
9772  S SG  A CYS C 372 ? 0.3643 0.5424 0.4406 -0.0017 0.0126  -0.0103 673 CYS C SG  
9773  S SG  B CYS C 372 ? 0.4940 0.7138 0.5882 0.0125  0.0051  -0.0086 673 CYS C SG  
9774  N N   . ARG C 373 ? 0.3249 0.4940 0.3916 -0.0294 0.0043  -0.0085 674 ARG C N   
9775  C CA  . ARG C 373 ? 0.2300 0.3821 0.2883 -0.0389 0.0064  -0.0089 674 ARG C CA  
9776  C C   . ARG C 373 ? 0.3439 0.4840 0.3932 -0.0481 0.0021  -0.0092 674 ARG C C   
9777  O O   . ARG C 373 ? 0.3419 0.4699 0.3843 -0.0572 0.0032  -0.0093 674 ARG C O   
9778  C CB  . ARG C 373 ? 0.2384 0.3694 0.2896 -0.0324 0.0106  -0.0105 674 ARG C CB  
9779  C CG  . ARG C 373 ? 0.2887 0.4083 0.3351 -0.0384 0.0143  -0.0104 674 ARG C CG  
9780  C CD  . ARG C 373 ? 0.2881 0.3874 0.3275 -0.0319 0.0172  -0.0121 674 ARG C CD  
9781  N NE  . ARG C 373 ? 0.3441 0.4327 0.3789 -0.0364 0.0203  -0.0117 674 ARG C NE  
9782  C CZ  . ARG C 373 ? 0.3256 0.3964 0.3539 -0.0334 0.0223  -0.0129 674 ARG C CZ  
9783  N NH1 . ARG C 373 ? 0.2869 0.3486 0.3123 -0.0268 0.0220  -0.0147 674 ARG C NH1 
9784  N NH2 . ARG C 373 ? 0.3292 0.3917 0.3536 -0.0371 0.0245  -0.0121 674 ARG C NH2 
9785  N N   . GLY C 374 ? 0.2599 0.4019 0.3080 -0.0460 -0.0028 -0.0095 675 GLY C N   
9786  C CA  . GLY C 374 ? 0.3215 0.4504 0.3594 -0.0545 -0.0066 -0.0103 675 GLY C CA  
9787  C C   . GLY C 374 ? 0.4063 0.5094 0.4320 -0.0508 -0.0053 -0.0126 675 GLY C C   
9788  O O   . GLY C 374 ? 0.3124 0.4015 0.3276 -0.0576 -0.0074 -0.0139 675 GLY C O   
9789  N N   . GLY C 375 ? 0.3541 0.4505 0.3802 -0.0408 -0.0017 -0.0133 676 GLY C N   
9790  C CA  . GLY C 375 ? 0.3280 0.4028 0.3438 -0.0375 -0.0002 -0.0154 676 GLY C CA  
9791  C C   . GLY C 375 ? 0.3754 0.4438 0.3926 -0.0293 0.0049  -0.0159 676 GLY C C   
9792  O O   . GLY C 375 ? 0.3863 0.4653 0.4115 -0.0261 0.0073  -0.0150 676 GLY C O   
9793  N N   . CYS C 376 ? 0.3711 0.4226 0.3802 -0.0264 0.0064  -0.0176 677 CYS C N   
9794  C CA  . CYS C 376 ? 0.3549 0.3990 0.3641 -0.0196 0.0106  -0.0183 677 CYS C CA  
9795  C C   . CYS C 376 ? 0.3527 0.3784 0.3522 -0.0207 0.0126  -0.0204 677 CYS C C   
9796  O O   . CYS C 376 ? 0.3828 0.4019 0.3762 -0.0191 0.0113  -0.0212 677 CYS C O   
9797  C CB  . CYS C 376 ? 0.3210 0.3704 0.3329 -0.0110 0.0097  -0.0177 677 CYS C CB  
9798  S SG  . CYS C 376 ? 0.3644 0.4032 0.3746 -0.0041 0.0144  -0.0187 677 CYS C SG  
9799  N N   . PRO C 377 ? 0.2798 0.2971 0.2772 -0.0233 0.0155  -0.0213 678 PRO C N   
9800  C CA  . PRO C 377 ? 0.2664 0.2678 0.2555 -0.0232 0.0177  -0.0235 678 PRO C CA  
9801  C C   . PRO C 377 ? 0.3367 0.3349 0.3256 -0.0165 0.0199  -0.0240 678 PRO C C   
9802  O O   . PRO C 377 ? 0.2801 0.2832 0.2745 -0.0122 0.0215  -0.0232 678 PRO C O   
9803  C CB  . PRO C 377 ? 0.3200 0.3156 0.3090 -0.0254 0.0203  -0.0238 678 PRO C CB  
9804  C CG  . PRO C 377 ? 0.3834 0.3916 0.3813 -0.0243 0.0208  -0.0215 678 PRO C CG  
9805  C CD  . PRO C 377 ? 0.3362 0.3583 0.3385 -0.0257 0.0173  -0.0202 678 PRO C CD  
9806  N N   . ALA C 378 ? 0.3090 0.2987 0.2906 -0.0163 0.0200  -0.0255 679 ALA C N   
9807  C CA  . ALA C 378 ? 0.3153 0.3019 0.2954 -0.0114 0.0217  -0.0256 679 ALA C CA  
9808  C C   . ALA C 378 ? 0.3114 0.2869 0.2835 -0.0125 0.0242  -0.0279 679 ALA C C   
9809  O O   . ALA C 378 ? 0.2999 0.2704 0.2652 -0.0161 0.0229  -0.0291 679 ALA C O   
9810  C CB  . ALA C 378 ? 0.3799 0.3715 0.3595 -0.0090 0.0183  -0.0240 679 ALA C CB  
9811  N N   . ASP C 379 ? 0.3052 0.2777 0.2782 -0.0095 0.0278  -0.0286 680 ASP C N   
9812  C CA  . ASP C 379 ? 0.3373 0.3019 0.3044 -0.0099 0.0312  -0.0308 680 ASP C CA  
9813  C C   . ASP C 379 ? 0.3288 0.2916 0.2912 -0.0090 0.0314  -0.0303 680 ASP C C   
9814  O O   . ASP C 379 ? 0.3145 0.2787 0.2796 -0.0067 0.0329  -0.0295 680 ASP C O   
9815  C CB  . ASP C 379 ? 0.3221 0.2864 0.2939 -0.0076 0.0349  -0.0317 680 ASP C CB  
9816  C CG  . ASP C 379 ? 0.3603 0.3190 0.3275 -0.0071 0.0388  -0.0343 680 ASP C CG  
9817  O OD1 . ASP C 379 ? 0.3052 0.2632 0.2755 -0.0051 0.0412  -0.0354 680 ASP C OD1 
9818  O OD2 . ASP C 379 ? 0.3747 0.3299 0.3349 -0.0085 0.0394  -0.0352 680 ASP C OD2 
9819  N N   . TRP C 380 ? 0.2729 0.2315 0.2270 -0.0114 0.0296  -0.0306 681 TRP C N   
9820  C CA  . TRP C 380 ? 0.2701 0.2256 0.2177 -0.0112 0.0289  -0.0295 681 TRP C CA  
9821  C C   . TRP C 380 ? 0.2700 0.2226 0.2163 -0.0107 0.0338  -0.0304 681 TRP C C   
9822  O O   . TRP C 380 ? 0.2844 0.2357 0.2290 -0.0100 0.0337  -0.0288 681 TRP C O   
9823  C CB  . TRP C 380 ? 0.2904 0.2408 0.2279 -0.0146 0.0267  -0.0301 681 TRP C CB  
9824  C CG  . TRP C 380 ? 0.2888 0.2353 0.2178 -0.0148 0.0246  -0.0282 681 TRP C CG  
9825  C CD1 . TRP C 380 ? 0.3061 0.2544 0.2330 -0.0141 0.0188  -0.0257 681 TRP C CD1 
9826  C CD2 . TRP C 380 ? 0.2955 0.2353 0.2162 -0.0161 0.0279  -0.0285 681 TRP C CD2 
9827  N NE1 . TRP C 380 ? 0.3148 0.2561 0.2314 -0.0145 0.0180  -0.0242 681 TRP C NE1 
9828  C CE2 . TRP C 380 ? 0.3645 0.3003 0.2769 -0.0163 0.0237  -0.0259 681 TRP C CE2 
9829  C CE3 . TRP C 380 ? 0.3250 0.2628 0.2447 -0.0171 0.0340  -0.0305 681 TRP C CE3 
9830  C CZ2 . TRP C 380 ? 0.3250 0.2531 0.2268 -0.0183 0.0255  -0.0250 681 TRP C CZ2 
9831  C CZ3 . TRP C 380 ? 0.3044 0.2368 0.2147 -0.0194 0.0361  -0.0299 681 TRP C CZ3 
9832  C CH2 . TRP C 380 ? 0.3137 0.2404 0.2146 -0.0204 0.0319  -0.0271 681 TRP C CH2 
9833  N N   . VAL C 381 ? 0.2758 0.2271 0.2224 -0.0113 0.0379  -0.0330 682 VAL C N   
9834  C CA  . VAL C 381 ? 0.2703 0.2219 0.2170 -0.0111 0.0428  -0.0341 682 VAL C CA  
9835  C C   . VAL C 381 ? 0.3252 0.2816 0.2797 -0.0092 0.0432  -0.0325 682 VAL C C   
9836  O O   . VAL C 381 ? 0.3087 0.2653 0.2618 -0.0103 0.0455  -0.0321 682 VAL C O   
9837  C CB  . VAL C 381 ? 0.2809 0.2321 0.2286 -0.0103 0.0468  -0.0374 682 VAL C CB  
9838  C CG1 . VAL C 381 ? 0.2702 0.2255 0.2211 -0.0093 0.0518  -0.0384 682 VAL C CG1 
9839  C CG2 . VAL C 381 ? 0.3288 0.2729 0.2658 -0.0126 0.0471  -0.0396 682 VAL C CG2 
9840  N N   . TRP C 382 ? 0.3199 0.2802 0.2818 -0.0069 0.0409  -0.0316 683 TRP C N   
9841  C CA  . TRP C 382 ? 0.3148 0.2788 0.2826 -0.0052 0.0409  -0.0303 683 TRP C CA  
9842  C C   . TRP C 382 ? 0.3059 0.2685 0.2717 -0.0041 0.0373  -0.0280 683 TRP C C   
9843  O O   . TRP C 382 ? 0.3361 0.2976 0.3017 -0.0037 0.0376  -0.0271 683 TRP C O   
9844  C CB  . TRP C 382 ? 0.2518 0.2206 0.2281 -0.0031 0.0411  -0.0305 683 TRP C CB  
9845  C CG  . TRP C 382 ? 0.2963 0.2671 0.2759 -0.0024 0.0447  -0.0323 683 TRP C CG  
9846  C CD1 . TRP C 382 ? 0.3212 0.2899 0.2981 -0.0026 0.0474  -0.0345 683 TRP C CD1 
9847  C CD2 . TRP C 382 ? 0.2675 0.2433 0.2537 -0.0009 0.0460  -0.0320 683 TRP C CD2 
9848  N NE1 . TRP C 382 ? 0.3104 0.2834 0.2927 -0.0005 0.0503  -0.0356 683 TRP C NE1 
9849  C CE2 . TRP C 382 ? 0.4193 0.3971 0.4075 0.0003  0.0491  -0.0339 683 TRP C CE2 
9850  C CE3 . TRP C 382 ? 0.3072 0.2860 0.2973 -0.0001 0.0446  -0.0305 683 TRP C CE3 
9851  C CZ2 . TRP C 382 ? 0.3830 0.3669 0.3779 0.0021  0.0504  -0.0339 683 TRP C CZ2 
9852  C CZ3 . TRP C 382 ? 0.3588 0.3425 0.3544 0.0008  0.0459  -0.0307 683 TRP C CZ3 
9853  C CH2 . TRP C 382 ? 0.2896 0.2764 0.2880 0.0019  0.0485  -0.0322 683 TRP C CH2 
9854  N N   . ILE C 383 ? 0.3333 0.2960 0.2976 -0.0036 0.0337  -0.0271 684 ILE C N   
9855  C CA  . ILE C 383 ? 0.2620 0.2248 0.2255 -0.0009 0.0302  -0.0250 684 ILE C CA  
9856  C C   . ILE C 383 ? 0.2896 0.2442 0.2436 -0.0016 0.0296  -0.0239 684 ILE C C   
9857  O O   . ILE C 383 ? 0.3173 0.2689 0.2698 0.0010  0.0282  -0.0225 684 ILE C O   
9858  C CB  . ILE C 383 ? 0.3173 0.2847 0.2822 -0.0003 0.0262  -0.0242 684 ILE C CB  
9859  C CG1 . ILE C 383 ? 0.3135 0.2885 0.2873 -0.0003 0.0267  -0.0248 684 ILE C CG1 
9860  C CG2 . ILE C 383 ? 0.2742 0.2423 0.2378 0.0036  0.0224  -0.0221 684 ILE C CG2 
9861  C CD1 . ILE C 383 ? 0.3544 0.3335 0.3346 0.0029  0.0278  -0.0243 684 ILE C CD1 
9862  N N   . VAL C 384 ? 0.2778 0.2276 0.2243 -0.0050 0.0307  -0.0244 685 VAL C N   
9863  C CA  . VAL C 384 ? 0.3006 0.2416 0.2364 -0.0065 0.0300  -0.0228 685 VAL C CA  
9864  C C   . VAL C 384 ? 0.2972 0.2355 0.2324 -0.0084 0.0335  -0.0229 685 VAL C C   
9865  O O   . VAL C 384 ? 0.3146 0.2575 0.2544 -0.0106 0.0377  -0.0248 685 VAL C O   
9866  C CB  . VAL C 384 ? 0.2880 0.2248 0.2148 -0.0104 0.0307  -0.0233 685 VAL C CB  
9867  C CG1 . VAL C 384 ? 0.3008 0.2276 0.2151 -0.0128 0.0303  -0.0213 685 VAL C CG1 
9868  C CG2 . VAL C 384 ? 0.2906 0.2297 0.2168 -0.0094 0.0264  -0.0230 685 VAL C CG2 
9869  N N   . PRO C 385 ? 0.3299 0.2608 0.2593 -0.0076 0.0316  -0.0210 686 PRO C N   
9870  C CA  . PRO C 385 ? 0.3878 0.3160 0.3165 -0.0103 0.0343  -0.0212 686 PRO C CA  
9871  C C   . PRO C 385 ? 0.3932 0.3199 0.3164 -0.0167 0.0384  -0.0216 686 PRO C C   
9872  O O   . PRO C 385 ? 0.3819 0.3047 0.2971 -0.0190 0.0384  -0.0211 686 PRO C O   
9873  C CB  . PRO C 385 ? 0.3764 0.2935 0.2967 -0.0079 0.0306  -0.0189 686 PRO C CB  
9874  C CG  . PRO C 385 ? 0.4585 0.3782 0.3817 -0.0015 0.0264  -0.0183 686 PRO C CG  
9875  C CD  . PRO C 385 ? 0.3647 0.2903 0.2896 -0.0030 0.0265  -0.0189 686 PRO C CD  
9876  N N   . PRO C 386 ? 0.3964 0.3269 0.3233 -0.0201 0.0418  -0.0226 687 PRO C N   
9877  C CA  . PRO C 386 ? 0.3535 0.2864 0.2773 -0.0263 0.0465  -0.0232 687 PRO C CA  
9878  C C   . PRO C 386 ? 0.3817 0.3029 0.2911 -0.0319 0.0462  -0.0209 687 PRO C C   
9879  O O   . PRO C 386 ? 0.4142 0.3379 0.3204 -0.0382 0.0504  -0.0212 687 PRO C O   
9880  C CB  . PRO C 386 ? 0.3694 0.3119 0.3032 -0.0276 0.0492  -0.0246 687 PRO C CB  
9881  C CG  . PRO C 386 ? 0.2856 0.2227 0.2197 -0.0249 0.0454  -0.0235 687 PRO C CG  
9882  C CD  . PRO C 386 ? 0.3154 0.2496 0.2497 -0.0185 0.0417  -0.0230 687 PRO C CD  
9883  N N   . MET C 387 ? 0.3717 0.2803 0.2722 -0.0299 0.0415  -0.0185 688 MET C N   
9884  C CA  . MET C 387 ? 0.4326 0.3272 0.3170 -0.0348 0.0406  -0.0158 688 MET C CA  
9885  C C   . MET C 387 ? 0.4857 0.3708 0.3627 -0.0292 0.0349  -0.0138 688 MET C C   
9886  O O   . MET C 387 ? 0.4298 0.3186 0.3143 -0.0219 0.0317  -0.0143 688 MET C O   
9887  C CB  . MET C 387 ? 0.4201 0.3052 0.2980 -0.0391 0.0401  -0.0144 688 MET C CB  
9888  C CG  . MET C 387 ? 0.3614 0.2375 0.2380 -0.0325 0.0352  -0.0136 688 MET C CG  
9889  S SD  . MET C 387 ? 0.5683 0.4299 0.4344 -0.0382 0.0345  -0.0124 688 MET C SD  
9890  C CE  . MET C 387 ? 0.5891 0.4298 0.4330 -0.0431 0.0324  -0.0085 688 MET C CE  
9891  N N   . SER C 388 ? 0.3974 0.2709 0.2595 -0.0328 0.0338  -0.0113 689 SER C N   
9892  C CA  . SER C 388 ? 0.4653 0.3281 0.3181 -0.0276 0.0277  -0.0087 689 SER C CA  
9893  C C   . SER C 388 ? 0.4261 0.2996 0.2887 -0.0211 0.0252  -0.0100 689 SER C C   
9894  O O   . SER C 388 ? 0.4167 0.2882 0.2800 -0.0140 0.0199  -0.0087 689 SER C O   
9895  C CB  . SER C 388 ? 0.4515 0.3021 0.2994 -0.0232 0.0235  -0.0069 689 SER C CB  
9896  O OG  . SER C 388 ? 0.5581 0.3969 0.3950 -0.0306 0.0255  -0.0055 689 SER C OG  
9897  N N   . GLY C 389 ? 0.4400 0.3250 0.3098 -0.0236 0.0290  -0.0127 690 GLY C N   
9898  C CA  . GLY C 389 ? 0.3771 0.2727 0.2572 -0.0188 0.0272  -0.0144 690 GLY C CA  
9899  C C   . GLY C 389 ? 0.4834 0.3749 0.3576 -0.0146 0.0208  -0.0121 690 GLY C C   
9900  O O   . GLY C 389 ? 0.4483 0.3455 0.3306 -0.0085 0.0170  -0.0120 690 GLY C O   
9901  N N   . SER C 390 ? 0.3608 0.2431 0.2207 -0.0181 0.0194  -0.0102 691 SER C N   
9902  C CA  . SER C 390 ? 0.3675 0.2484 0.2226 -0.0145 0.0129  -0.0083 691 SER C CA  
9903  C C   . SER C 390 ? 0.3773 0.2493 0.2270 -0.0083 0.0068  -0.0047 691 SER C C   
9904  O O   . SER C 390 ? 0.4507 0.3240 0.2989 -0.0037 0.0007  -0.0029 691 SER C O   
9905  C CB  . SER C 390 ? 0.4308 0.3054 0.2719 -0.0202 0.0131  -0.0075 691 SER C CB  
9906  O OG  . SER C 390 ? 0.4444 0.3041 0.2700 -0.0233 0.0128  -0.0044 691 SER C OG  
9907  N N   . ILE C 391 ? 0.4424 0.3053 0.2887 -0.0077 0.0079  -0.0037 692 ILE C N   
9908  C CA  . ILE C 391 ? 0.4264 0.2813 0.2690 0.0003  0.0020  -0.0010 692 ILE C CA  
9909  C C   . ILE C 391 ? 0.3944 0.2618 0.2534 0.0076  0.0015  -0.0030 692 ILE C C   
9910  O O   . ILE C 391 ? 0.4342 0.2978 0.2925 0.0157  -0.0028 -0.0015 692 ILE C O   
9911  C CB  . ILE C 391 ? 0.5089 0.3442 0.3363 -0.0022 0.0023  0.0014  692 ILE C CB  
9912  C CG1 . ILE C 391 ? 0.6021 0.4384 0.4354 -0.0059 0.0078  -0.0010 692 ILE C CG1 
9913  C CG2 . ILE C 391 ? 0.4492 0.2728 0.2591 -0.0104 0.0028  0.0038  692 ILE C CG2 
9914  C CD1 . ILE C 391 ? 0.6691 0.4854 0.4878 -0.0074 0.0069  0.0013  692 ILE C CD1 
9915  N N   . THR C 392 ? 0.4011 0.2834 0.2743 0.0053  0.0058  -0.0064 693 THR C N   
9916  C CA  . THR C 392 ? 0.4536 0.3490 0.3418 0.0116  0.0049  -0.0079 693 THR C CA  
9917  C C   . THR C 392 ? 0.4302 0.3385 0.3253 0.0131  0.0018  -0.0081 693 THR C C   
9918  O O   . THR C 392 ? 0.4495 0.3588 0.3411 0.0076  0.0024  -0.0085 693 THR C O   
9919  C CB  . THR C 392 ? 0.3936 0.2968 0.2928 0.0087  0.0108  -0.0110 693 THR C CB  
9920  O OG1 . THR C 392 ? 0.4033 0.3143 0.3068 0.0029  0.0141  -0.0130 693 THR C OG1 
9921  C CG2 . THR C 392 ? 0.4097 0.3018 0.3023 0.0055  0.0139  -0.0110 693 THR C CG2 
9922  N N   . PRO C 393 ? 0.4182 0.3369 0.3229 0.0201  -0.0016 -0.0078 694 PRO C N   
9923  C CA  . PRO C 393 ? 0.3397 0.2712 0.2503 0.0206  -0.0055 -0.0075 694 PRO C CA  
9924  C C   . PRO C 393 ? 0.3725 0.3141 0.2915 0.0142  -0.0018 -0.0103 694 PRO C C   
9925  O O   . PRO C 393 ? 0.3666 0.3129 0.2846 0.0108  -0.0042 -0.0104 694 PRO C O   
9926  C CB  . PRO C 393 ? 0.3542 0.2959 0.2742 0.0297  -0.0090 -0.0067 694 PRO C CB  
9927  C CG  . PRO C 393 ? 0.3436 0.2810 0.2665 0.0324  -0.0046 -0.0082 694 PRO C CG  
9928  C CD  . PRO C 393 ? 0.3758 0.2946 0.2849 0.0279  -0.0023 -0.0077 694 PRO C CD  
9929  N N   . VAL C 394 ? 0.3613 0.3050 0.2872 0.0123  0.0038  -0.0127 695 VAL C N   
9930  C CA  . VAL C 394 ? 0.3201 0.2717 0.2533 0.0072  0.0070  -0.0152 695 VAL C CA  
9931  C C   . VAL C 394 ? 0.3319 0.2768 0.2558 0.0007  0.0086  -0.0162 695 VAL C C   
9932  O O   . VAL C 394 ? 0.2973 0.2471 0.2239 -0.0030 0.0092  -0.0180 695 VAL C O   
9933  C CB  . VAL C 394 ? 0.3004 0.2538 0.2410 0.0069  0.0123  -0.0172 695 VAL C CB  
9934  C CG1 . VAL C 394 ? 0.2823 0.2455 0.2336 0.0125  0.0113  -0.0169 695 VAL C CG1 
9935  C CG2 . VAL C 394 ? 0.2892 0.2311 0.2223 0.0055  0.0156  -0.0172 695 VAL C CG2 
9936  N N   . PHE C 395 ? 0.3114 0.2444 0.2235 -0.0010 0.0094  -0.0151 696 PHE C N   
9937  C CA  . PHE C 395 ? 0.3628 0.2898 0.2652 -0.0070 0.0116  -0.0162 696 PHE C CA  
9938  C C   . PHE C 395 ? 0.4115 0.3410 0.3098 -0.0085 0.0068  -0.0158 696 PHE C C   
9939  O O   . PHE C 395 ? 0.3433 0.2722 0.2380 -0.0133 0.0088  -0.0181 696 PHE C O   
9940  C CB  . PHE C 395 ? 0.3314 0.2456 0.2208 -0.0089 0.0127  -0.0144 696 PHE C CB  
9941  C CG  . PHE C 395 ? 0.3404 0.2489 0.2189 -0.0151 0.0155  -0.0154 696 PHE C CG  
9942  C CD1 . PHE C 395 ? 0.3739 0.2824 0.2530 -0.0193 0.0225  -0.0179 696 PHE C CD1 
9943  C CD2 . PHE C 395 ? 0.3808 0.2845 0.2480 -0.0166 0.0111  -0.0138 696 PHE C CD2 
9944  C CE1 . PHE C 395 ? 0.3734 0.2776 0.2422 -0.0246 0.0258  -0.0192 696 PHE C CE1 
9945  C CE2 . PHE C 395 ? 0.4096 0.3076 0.2654 -0.0225 0.0142  -0.0150 696 PHE C CE2 
9946  C CZ  . PHE C 395 ? 0.3805 0.2789 0.2372 -0.0263 0.0218  -0.0179 696 PHE C CZ  
9947  N N   . HIS C 396 ? 0.3861 0.3183 0.2843 -0.0042 0.0003  -0.0130 697 HIS C N   
9948  C CA  . HIS C 396 ? 0.3789 0.3143 0.2728 -0.0055 -0.0055 -0.0120 697 HIS C CA  
9949  C C   . HIS C 396 ? 0.3837 0.3336 0.2899 -0.0057 -0.0076 -0.0132 697 HIS C C   
9950  O O   . HIS C 396 ? 0.3450 0.2999 0.2492 -0.0075 -0.0130 -0.0124 697 HIS C O   
9951  C CB  . HIS C 396 ? 0.3596 0.2910 0.2467 -0.0003 -0.0119 -0.0080 697 HIS C CB  
9952  C CG  . HIS C 396 ? 0.4230 0.3384 0.2969 -0.0007 -0.0099 -0.0063 697 HIS C CG  
9953  N ND1 . HIS C 396 ? 0.4242 0.3287 0.2825 -0.0060 -0.0100 -0.0055 697 HIS C ND1 
9954  C CD2 . HIS C 396 ? 0.4420 0.3499 0.3150 0.0022  -0.0074 -0.0055 697 HIS C CD2 
9955  C CE1 . HIS C 396 ? 0.4807 0.3721 0.3293 -0.0064 -0.0077 -0.0039 697 HIS C CE1 
9956  N NE2 . HIS C 396 ? 0.4807 0.3735 0.3379 -0.0016 -0.0063 -0.0039 697 HIS C NE2 
9957  N N   . GLN C 397 ? 0.4055 0.3621 0.3237 -0.0044 -0.0038 -0.0149 698 GLN C N   
9958  C CA  . GLN C 397 ? 0.3040 0.2743 0.2342 -0.0049 -0.0052 -0.0156 698 GLN C CA  
9959  C C   . GLN C 397 ? 0.3216 0.2901 0.2514 -0.0116 -0.0015 -0.0189 698 GLN C C   
9960  O O   . GLN C 397 ? 0.3813 0.3449 0.3123 -0.0122 0.0044  -0.0209 698 GLN C O   
9961  C CB  . GLN C 397 ? 0.2946 0.2722 0.2368 0.0004  -0.0031 -0.0154 698 GLN C CB  
9962  C CG  . GLN C 397 ? 0.3516 0.3435 0.3056 -0.0009 -0.0039 -0.0160 698 GLN C CG  
9963  C CD  . GLN C 397 ? 0.3681 0.3717 0.3248 -0.0001 -0.0107 -0.0139 698 GLN C CD  
9964  O OE1 . GLN C 397 ? 0.3620 0.3691 0.3196 0.0067  -0.0142 -0.0116 698 GLN C OE1 
9965  N NE2 . GLN C 397 ? 0.3635 0.3729 0.3210 -0.0068 -0.0129 -0.0147 698 GLN C NE2 
9966  N N   . GLU C 398 ? 0.3063 0.2785 0.2340 -0.0164 -0.0051 -0.0195 699 GLU C N   
9967  C CA  . GLU C 398 ? 0.3051 0.2752 0.2330 -0.0220 -0.0021 -0.0226 699 GLU C CA  
9968  C C   . GLU C 398 ? 0.3089 0.2881 0.2500 -0.0207 0.0000  -0.0228 699 GLU C C   
9969  O O   . GLU C 398 ? 0.2904 0.2816 0.2408 -0.0176 -0.0029 -0.0206 699 GLU C O   
9970  C CB  . GLU C 398 ? 0.3147 0.2859 0.2365 -0.0283 -0.0070 -0.0231 699 GLU C CB  
9971  C CG  . GLU C 398 ? 0.3684 0.3281 0.2744 -0.0311 -0.0080 -0.0239 699 GLU C CG  
9972  C CD  . GLU C 398 ? 0.4320 0.3931 0.3314 -0.0376 -0.0138 -0.0244 699 GLU C CD  
9973  O OE1 . GLU C 398 ? 0.4709 0.4220 0.3560 -0.0410 -0.0145 -0.0256 699 GLU C OE1 
9974  O OE2 . GLU C 398 ? 0.4375 0.4102 0.3456 -0.0399 -0.0175 -0.0236 699 GLU C OE2 
9975  N N   . MET C 399 ? 0.3393 0.3125 0.2807 -0.0227 0.0051  -0.0253 700 MET C N   
9976  C CA  . MET C 399 ? 0.3319 0.3113 0.2839 -0.0220 0.0075  -0.0255 700 MET C CA  
9977  C C   . MET C 399 ? 0.3754 0.3484 0.3238 -0.0275 0.0092  -0.0280 700 MET C C   
9978  O O   . MET C 399 ? 0.5043 0.4661 0.4427 -0.0298 0.0109  -0.0305 700 MET C O   
9979  C CB  . MET C 399 ? 0.3048 0.2817 0.2608 -0.0169 0.0124  -0.0256 700 MET C CB  
9980  C CG  . MET C 399 ? 0.3640 0.3436 0.3214 -0.0115 0.0111  -0.0234 700 MET C CG  
9981  S SD  . MET C 399 ? 0.3544 0.3274 0.3124 -0.0080 0.0169  -0.0242 700 MET C SD  
9982  C CE  . MET C 399 ? 0.3149 0.2865 0.2696 -0.0029 0.0141  -0.0215 700 MET C CE  
9983  N N   . LEU C 400 ? 0.3050 0.2844 0.2607 -0.0296 0.0087  -0.0275 701 LEU C N   
9984  C CA  . LEU C 400 ? 0.2853 0.2568 0.2374 -0.0344 0.0104  -0.0296 701 LEU C CA  
9985  C C   . LEU C 400 ? 0.3524 0.3227 0.3107 -0.0308 0.0150  -0.0297 701 LEU C C   
9986  O O   . LEU C 400 ? 0.3328 0.3134 0.3007 -0.0279 0.0151  -0.0276 701 LEU C O   
9987  C CB  . LEU C 400 ? 0.3344 0.3128 0.2882 -0.0414 0.0059  -0.0285 701 LEU C CB  
9988  C CG  . LEU C 400 ? 0.3125 0.2915 0.2589 -0.0468 0.0006  -0.0287 701 LEU C CG  
9989  C CD1 . LEU C 400 ? 0.3891 0.3796 0.3406 -0.0538 -0.0039 -0.0270 701 LEU C CD1 
9990  C CD2 . LEU C 400 ? 0.3299 0.2911 0.2616 -0.0500 0.0020  -0.0323 701 LEU C CD2 
9991  N N   . ASN C 401 ? 0.4086 0.3667 0.3611 -0.0304 0.0187  -0.0323 702 ASN C N   
9992  C CA  . ASN C 401 ? 0.4447 0.4012 0.4024 -0.0268 0.0226  -0.0324 702 ASN C CA  
9993  C C   . ASN C 401 ? 0.3995 0.3489 0.3542 -0.0310 0.0224  -0.0330 702 ASN C C   
9994  O O   . ASN C 401 ? 0.3636 0.3014 0.3084 -0.0342 0.0221  -0.0354 702 ASN C O   
9995  C CB  . ASN C 401 ? 0.3437 0.2933 0.2985 -0.0219 0.0271  -0.0345 702 ASN C CB  
9996  C CG  . ASN C 401 ? 0.4346 0.3871 0.3971 -0.0175 0.0301  -0.0337 702 ASN C CG  
9997  O OD1 . ASN C 401 ? 0.3735 0.3336 0.3432 -0.0174 0.0289  -0.0314 702 ASN C OD1 
9998  N ND2 . ASN C 401 ? 0.4053 0.3529 0.3666 -0.0138 0.0341  -0.0357 702 ASN C ND2 
9999  N N   . TYR C 402 ? 0.3710 0.3264 0.3330 -0.0312 0.0224  -0.0308 703 TYR C N   
10000 C CA  . TYR C 402 ? 0.3352 0.2825 0.2937 -0.0352 0.0223  -0.0308 703 TYR C CA  
10001 C C   . TYR C 402 ? 0.3612 0.3145 0.3279 -0.0323 0.0240  -0.0285 703 TYR C C   
10002 O O   . TYR C 402 ? 0.3117 0.2767 0.2868 -0.0285 0.0246  -0.0270 703 TYR C O   
10003 C CB  . TYR C 402 ? 0.3055 0.2546 0.2606 -0.0441 0.0180  -0.0299 703 TYR C CB  
10004 C CG  . TYR C 402 ? 0.3635 0.3313 0.3278 -0.0458 0.0151  -0.0272 703 TYR C CG  
10005 C CD1 . TYR C 402 ? 0.3674 0.3471 0.3406 -0.0468 0.0152  -0.0244 703 TYR C CD1 
10006 C CD2 . TYR C 402 ? 0.3898 0.3636 0.3534 -0.0459 0.0124  -0.0275 703 TYR C CD2 
10007 C CE1 . TYR C 402 ? 0.2928 0.2910 0.2749 -0.0472 0.0129  -0.0223 703 TYR C CE1 
10008 C CE2 . TYR C 402 ? 0.3619 0.3533 0.3343 -0.0460 0.0095  -0.0250 703 TYR C CE2 
10009 C CZ  . TYR C 402 ? 0.3339 0.3379 0.3159 -0.0463 0.0099  -0.0226 703 TYR C CZ  
10010 O OH  . TYR C 402 ? 0.3584 0.3812 0.3496 -0.0454 0.0074  -0.0204 703 TYR C OH  
10011 N N   . ARG C 403 ? 0.3761 0.3199 0.3391 -0.0339 0.0247  -0.0283 704 ARG C N   
10012 C CA  . ARG C 403 ? 0.3986 0.3449 0.3671 -0.0304 0.0266  -0.0264 704 ARG C CA  
10013 C C   . ARG C 403 ? 0.3860 0.3382 0.3567 -0.0369 0.0248  -0.0234 704 ARG C C   
10014 O O   . ARG C 403 ? 0.3882 0.3309 0.3514 -0.0434 0.0232  -0.0231 704 ARG C O   
10015 C CB  . ARG C 403 ? 0.5690 0.5005 0.5317 -0.0263 0.0287  -0.0279 704 ARG C CB  
10016 C CG  . ARG C 403 ? 0.8100 0.7452 0.7789 -0.0207 0.0306  -0.0264 704 ARG C CG  
10017 C CD  . ARG C 403 ? 0.9617 0.8823 0.9244 -0.0169 0.0317  -0.0274 704 ARG C CD  
10018 N NE  . ARG C 403 ? 1.0979 1.0188 1.0631 -0.0156 0.0316  -0.0245 704 ARG C NE  
10019 C CZ  . ARG C 403 ? 1.1498 1.0681 1.1121 -0.0215 0.0298  -0.0217 704 ARG C CZ  
10020 N NH1 . ARG C 403 ? 1.2450 1.1615 1.2027 -0.0296 0.0279  -0.0214 704 ARG C NH1 
10021 N NH2 . ARG C 403 ? 1.0548 0.9728 1.0183 -0.0199 0.0299  -0.0190 704 ARG C NH2 
10022 N N   . LEU C 404 ? 0.3136 0.2812 0.2937 -0.0355 0.0251  -0.0213 705 LEU C N   
10023 C CA  . LEU C 404 ? 0.3465 0.3221 0.3297 -0.0409 0.0245  -0.0183 705 LEU C CA  
10024 C C   . LEU C 404 ? 0.3200 0.2944 0.3053 -0.0370 0.0268  -0.0168 705 LEU C C   
10025 O O   . LEU C 404 ? 0.3262 0.3006 0.3145 -0.0297 0.0286  -0.0177 705 LEU C O   
10026 C CB  . LEU C 404 ? 0.3226 0.3178 0.3148 -0.0417 0.0234  -0.0171 705 LEU C CB  
10027 C CG  . LEU C 404 ? 0.3574 0.3574 0.3489 -0.0452 0.0203  -0.0181 705 LEU C CG  
10028 C CD1 . LEU C 404 ? 0.3460 0.3663 0.3477 -0.0428 0.0195  -0.0168 705 LEU C CD1 
10029 C CD2 . LEU C 404 ? 0.3283 0.3235 0.3134 -0.0556 0.0177  -0.0174 705 LEU C CD2 
10030 N N   . THR C 405 ? 0.3349 0.3081 0.3180 -0.0427 0.0265  -0.0143 706 THR C N   
10031 C CA  A THR C 405 ? 0.3549 0.3283 0.3394 -0.0400 0.0283  -0.0123 706 THR C CA  
10032 C CA  B THR C 405 ? 0.3506 0.3238 0.3348 -0.0402 0.0283  -0.0122 706 THR C CA  
10033 C C   . THR C 405 ? 0.2998 0.2905 0.2910 -0.0433 0.0291  -0.0099 706 THR C C   
10034 O O   . THR C 405 ? 0.3064 0.3063 0.2995 -0.0500 0.0279  -0.0090 706 THR C O   
10035 C CB  A THR C 405 ? 0.3633 0.3189 0.3377 -0.0430 0.0277  -0.0110 706 THR C CB  
10036 C CB  B THR C 405 ? 0.3711 0.3270 0.3452 -0.0440 0.0276  -0.0107 706 THR C CB  
10037 O OG1 A THR C 405 ? 0.3589 0.3137 0.3340 -0.0392 0.0290  -0.0091 706 THR C OG1 
10038 O OG1 B THR C 405 ? 0.4007 0.3553 0.3699 -0.0544 0.0257  -0.0093 706 THR C OG1 
10039 C CG2 A THR C 405 ? 0.4131 0.3667 0.3820 -0.0540 0.0260  -0.0090 706 THR C CG2 
10040 C CG2 B THR C 405 ? 0.4027 0.3417 0.3701 -0.0391 0.0273  -0.0134 706 THR C CG2 
10041 N N   . PRO C 406 ? 0.3448 0.3416 0.3401 -0.0386 0.0312  -0.0090 707 PRO C N   
10042 C CA  . PRO C 406 ? 0.3587 0.3494 0.3537 -0.0311 0.0324  -0.0096 707 PRO C CA  
10043 C C   . PRO C 406 ? 0.3383 0.3274 0.3358 -0.0245 0.0325  -0.0126 707 PRO C C   
10044 O O   . PRO C 406 ? 0.2713 0.2675 0.2722 -0.0243 0.0319  -0.0140 707 PRO C O   
10045 C CB  . PRO C 406 ? 0.3297 0.3335 0.3300 -0.0294 0.0344  -0.0083 707 PRO C CB  
10046 C CG  . PRO C 406 ? 0.3357 0.3476 0.3361 -0.0374 0.0346  -0.0059 707 PRO C CG  
10047 C CD  . PRO C 406 ? 0.3097 0.3226 0.3103 -0.0419 0.0325  -0.0069 707 PRO C CD  
10048 N N   . SER C 407 ? 0.3594 0.3395 0.3548 -0.0195 0.0329  -0.0134 708 SER C N   
10049 C CA  . SER C 407 ? 0.3611 0.3391 0.3578 -0.0144 0.0333  -0.0162 708 SER C CA  
10050 C C   . SER C 407 ? 0.2783 0.2553 0.2769 -0.0085 0.0343  -0.0165 708 SER C C   
10051 O O   . SER C 407 ? 0.3491 0.3221 0.3456 -0.0080 0.0341  -0.0148 708 SER C O   
10052 C CB  . SER C 407 ? 0.5225 0.4885 0.5131 -0.0157 0.0325  -0.0179 708 SER C CB  
10053 O OG  . SER C 407 ? 0.6620 0.6160 0.6469 -0.0151 0.0322  -0.0170 708 SER C OG  
10054 N N   . PHE C 408 ? 0.2973 0.2779 0.2991 -0.0047 0.0351  -0.0185 709 PHE C N   
10055 C CA  . PHE C 408 ? 0.2911 0.2706 0.2945 0.0001  0.0359  -0.0192 709 PHE C CA  
10056 C C   . PHE C 408 ? 0.3161 0.2876 0.3168 0.0021  0.0363  -0.0211 709 PHE C C   
10057 O O   . PHE C 408 ? 0.3411 0.3106 0.3401 0.0010  0.0366  -0.0228 709 PHE C O   
10058 C CB  . PHE C 408 ? 0.2622 0.2491 0.2695 0.0022  0.0366  -0.0203 709 PHE C CB  
10059 C CG  . PHE C 408 ? 0.2747 0.2684 0.2837 0.0019  0.0366  -0.0190 709 PHE C CG  
10060 C CD1 . PHE C 408 ? 0.2284 0.2280 0.2387 0.0012  0.0367  -0.0193 709 PHE C CD1 
10061 C CD2 . PHE C 408 ? 0.3130 0.3072 0.3218 0.0028  0.0365  -0.0176 709 PHE C CD2 
10062 C CE1 . PHE C 408 ? 0.2826 0.2888 0.2943 0.0019  0.0372  -0.0186 709 PHE C CE1 
10063 C CE2 . PHE C 408 ? 0.2956 0.2958 0.3050 0.0025  0.0370  -0.0168 709 PHE C CE2 
10064 C CZ  . PHE C 408 ? 0.2538 0.2599 0.2646 0.0023  0.0376  -0.0175 709 PHE C CZ  
10065 N N   . GLU C 409 ? 0.3730 0.3402 0.3733 0.0055  0.0362  -0.0207 710 GLU C N   
10066 C CA  . GLU C 409 ? 0.3882 0.3479 0.3859 0.0088  0.0369  -0.0226 710 GLU C CA  
10067 C C   . GLU C 409 ? 0.4254 0.3908 0.4281 0.0140  0.0379  -0.0234 710 GLU C C   
10068 O O   . GLU C 409 ? 0.3205 0.2921 0.3270 0.0150  0.0371  -0.0219 710 GLU C O   
10069 C CB  . GLU C 409 ? 0.4646 0.4122 0.4558 0.0088  0.0355  -0.0213 710 GLU C CB  
10070 C CG  . GLU C 409 ? 0.4972 0.4394 0.4829 0.0020  0.0343  -0.0201 710 GLU C CG  
10071 C CD  . GLU C 409 ? 0.6328 0.5713 0.6150 -0.0006 0.0348  -0.0227 710 GLU C CD  
10072 O OE1 . GLU C 409 ? 0.6770 0.6128 0.6585 0.0034  0.0363  -0.0255 710 GLU C OE1 
10073 O OE2 . GLU C 409 ? 0.6762 0.6154 0.6563 -0.0068 0.0336  -0.0219 710 GLU C OE2 
10074 N N   . TYR C 410 ? 0.3276 0.2913 0.3302 0.0171  0.0397  -0.0260 711 TYR C N   
10075 C CA  . TYR C 410 ? 0.3405 0.3100 0.3482 0.0225  0.0406  -0.0267 711 TYR C CA  
10076 C C   . TYR C 410 ? 0.3950 0.3585 0.4011 0.0270  0.0389  -0.0252 711 TYR C C   
10077 O O   . TYR C 410 ? 0.3325 0.2839 0.3316 0.0265  0.0377  -0.0244 711 TYR C O   
10078 C CB  . TYR C 410 ? 0.3341 0.3042 0.3418 0.0248  0.0436  -0.0300 711 TYR C CB  
10079 C CG  . TYR C 410 ? 0.5610 0.5372 0.5698 0.0209  0.0452  -0.0312 711 TYR C CG  
10080 C CD1 . TYR C 410 ? 0.7033 0.6740 0.7066 0.0187  0.0466  -0.0332 711 TYR C CD1 
10081 C CD2 . TYR C 410 ? 0.6042 0.5901 0.6181 0.0192  0.0451  -0.0303 711 TYR C CD2 
10082 C CE1 . TYR C 410 ? 0.6710 0.6461 0.6742 0.0153  0.0477  -0.0339 711 TYR C CE1 
10083 C CE2 . TYR C 410 ? 0.7019 0.6909 0.7152 0.0157  0.0463  -0.0311 711 TYR C CE2 
10084 C CZ  . TYR C 410 ? 0.6106 0.5943 0.6186 0.0139  0.0475  -0.0327 711 TYR C CZ  
10085 O OH  . TYR C 410 ? 0.5179 0.5037 0.5242 0.0106  0.0483  -0.0331 711 TYR C OH  
10086 N N   . GLN C 411 ? 0.3767 0.3485 0.3888 0.0313  0.0384  -0.0246 712 GLN C N   
10087 C CA  . GLN C 411 ? 0.3490 0.3164 0.3602 0.0371  0.0364  -0.0231 712 GLN C CA  
10088 C C   . GLN C 411 ? 0.3305 0.3095 0.3498 0.0431  0.0374  -0.0245 712 GLN C C   
10089 O O   . GLN C 411 ? 0.3322 0.3232 0.3575 0.0409  0.0392  -0.0258 712 GLN C O   
10090 C CB  . GLN C 411 ? 0.3751 0.3419 0.3850 0.0348  0.0331  -0.0193 712 GLN C CB  
10091 C CG  . GLN C 411 ? 0.2571 0.2370 0.2731 0.0319  0.0327  -0.0186 712 GLN C CG  
10092 C CD  . GLN C 411 ? 0.4054 0.3841 0.4187 0.0299  0.0298  -0.0151 712 GLN C CD  
10093 O OE1 . GLN C 411 ? 0.3765 0.3469 0.3852 0.0324  0.0276  -0.0128 712 GLN C OE1 
10094 N NE2 . GLN C 411 ? 0.3271 0.3127 0.3419 0.0254  0.0299  -0.0148 712 GLN C NE2 
10095 N N   . PRO C 412 ? 0.3832 0.3590 0.4024 0.0508  0.0362  -0.0241 713 PRO C N   
10096 C CA  . PRO C 412 ? 0.4081 0.3982 0.4366 0.0570  0.0372  -0.0254 713 PRO C CA  
10097 C C   . PRO C 412 ? 0.4192 0.4246 0.4554 0.0539  0.0352  -0.0235 713 PRO C C   
10098 O O   . PRO C 412 ? 0.3862 0.3888 0.4197 0.0500  0.0322  -0.0206 713 PRO C O   
10099 C CB  . PRO C 412 ? 0.4982 0.4801 0.5240 0.0664  0.0350  -0.0245 713 PRO C CB  
10100 C CG  . PRO C 412 ? 0.4555 0.4158 0.4687 0.0646  0.0343  -0.0241 713 PRO C CG  
10101 C CD  . PRO C 412 ? 0.4285 0.3877 0.4390 0.0543  0.0338  -0.0224 713 PRO C CD  
10102 N N   . ASP C 413 ? 0.3668 0.3883 0.4121 0.0551  0.0371  -0.0252 714 ASP C N   
10103 C CA  . ASP C 413 ? 0.4308 0.4670 0.4832 0.0524  0.0348  -0.0235 714 ASP C CA  
10104 C C   . ASP C 413 ? 0.4625 0.4995 0.5162 0.0584  0.0301  -0.0206 714 ASP C C   
10105 O O   . ASP C 413 ? 0.3849 0.4203 0.4397 0.0672  0.0297  -0.0208 714 ASP C O   
10106 C CB  . ASP C 413 ? 0.4621 0.5161 0.5238 0.0521  0.0377  -0.0258 714 ASP C CB  
10107 C CG  . ASP C 413 ? 0.6292 0.6830 0.6887 0.0444  0.0414  -0.0279 714 ASP C CG  
10108 O OD1 . ASP C 413 ? 0.6436 0.6885 0.6969 0.0383  0.0405  -0.0269 714 ASP C OD1 
10109 O OD2 . ASP C 413 ? 0.7082 0.7708 0.7718 0.0447  0.0453  -0.0304 714 ASP C OD2 
10110 N N   . PRO C 414 ? 0.3843 0.4234 0.4371 0.0543  0.0263  -0.0178 715 PRO C N   
10111 C CA  . PRO C 414 ? 0.3388 0.3757 0.3903 0.0595  0.0213  -0.0144 715 PRO C CA  
10112 C C   . PRO C 414 ? 0.3779 0.4294 0.4390 0.0676  0.0196  -0.0144 715 PRO C C   
10113 O O   . PRO C 414 ? 0.4115 0.4578 0.4707 0.0755  0.0163  -0.0122 715 PRO C O   
10114 C CB  . PRO C 414 ? 0.2602 0.2994 0.3093 0.0522  0.0184  -0.0122 715 PRO C CB  
10115 C CG  . PRO C 414 ? 0.2481 0.2902 0.2975 0.0441  0.0218  -0.0145 715 PRO C CG  
10116 C CD  . PRO C 414 ? 0.3565 0.4017 0.4100 0.0454  0.0264  -0.0178 715 PRO C CD  
10117 N N   . TRP C 415 ? 0.4104 0.4803 0.4816 0.0658  0.0217  -0.0165 716 TRP C N   
10118 C CA  . TRP C 415 ? 0.4350 0.5224 0.5170 0.0735  0.0202  -0.0165 716 TRP C CA  
10119 C C   . TRP C 415 ? 0.4509 0.5348 0.5341 0.0843  0.0230  -0.0186 716 TRP C C   
10120 O O   . TRP C 415 ? 0.5062 0.6022 0.5974 0.0935  0.0212  -0.0182 716 TRP C O   
10121 C CB  . TRP C 415 ? 0.3955 0.5048 0.4879 0.0675  0.0218  -0.0181 716 TRP C CB  
10122 C CG  . TRP C 415 ? 0.3642 0.4722 0.4554 0.0611  0.0278  -0.0214 716 TRP C CG  
10123 C CD1 . TRP C 415 ? 0.3607 0.4743 0.4561 0.0645  0.0331  -0.0245 716 TRP C CD1 
10124 C CD2 . TRP C 415 ? 0.4254 0.5257 0.5100 0.0504  0.0291  -0.0217 716 TRP C CD2 
10125 N NE1 . TRP C 415 ? 0.3768 0.4862 0.4681 0.0560  0.0373  -0.0265 716 TRP C NE1 
10126 C CE2 . TRP C 415 ? 0.4098 0.5109 0.4946 0.0477  0.0348  -0.0248 716 TRP C CE2 
10127 C CE3 . TRP C 415 ? 0.3221 0.4147 0.4000 0.0435  0.0261  -0.0198 716 TRP C CE3 
10128 C CZ2 . TRP C 415 ? 0.3914 0.4854 0.4701 0.0386  0.0369  -0.0257 716 TRP C CZ2 
10129 C CZ3 . TRP C 415 ? 0.4003 0.4863 0.4726 0.0351  0.0286  -0.0211 716 TRP C CZ3 
10130 C CH2 . TRP C 415 ? 0.4614 0.5479 0.5342 0.0329  0.0337  -0.0238 716 TRP C CH2 
10131 N N   . ASN C 416 ? 0.4902 0.5582 0.5655 0.0838  0.0272  -0.0209 717 ASN C N   
10132 C CA  . ASN C 416 ? 0.5332 0.5947 0.6073 0.0944  0.0296  -0.0231 717 ASN C CA  
10133 C C   . ASN C 416 ? 0.5234 0.5647 0.5875 0.1015  0.0256  -0.0205 717 ASN C C   
10134 O O   . ASN C 416 ? 0.5826 0.6187 0.6456 0.1125  0.0261  -0.0218 717 ASN C O   
10135 C CB  . ASN C 416 ? 0.4896 0.5421 0.5582 0.0908  0.0357  -0.0270 717 ASN C CB  
10136 C CG  . ASN C 416 ? 0.4576 0.5281 0.5344 0.0842  0.0399  -0.0294 717 ASN C CG  
10137 O OD1 . ASN C 416 ? 0.4489 0.5410 0.5374 0.0861  0.0401  -0.0296 717 ASN C OD1 
10138 N ND2 . ASN C 416 ? 0.4205 0.4826 0.4910 0.0758  0.0431  -0.0309 717 ASN C ND2 
10139 N N   . THR C 417 ? 0.4869 0.5160 0.5427 0.0956  0.0217  -0.0170 718 THR C N   
10140 C CA  . THR C 417 ? 0.5080 0.5163 0.5526 0.1006  0.0179  -0.0141 718 THR C CA  
10141 C C   . THR C 417 ? 0.4485 0.4593 0.4929 0.1017  0.0114  -0.0092 718 THR C C   
10142 O O   . THR C 417 ? 0.4818 0.4774 0.5177 0.1082  0.0076  -0.0064 718 THR C O   
10143 C CB  . THR C 417 ? 0.5029 0.4900 0.5345 0.0924  0.0194  -0.0140 718 THR C CB  
10144 O OG1 . THR C 417 ? 0.4211 0.4140 0.4534 0.0813  0.0190  -0.0126 718 THR C OG1 
10145 C CG2 . THR C 417 ? 0.4358 0.4184 0.4659 0.0920  0.0252  -0.0187 718 THR C CG2 
10146 N N   . HIS C 418 ? 0.4279 0.4560 0.4797 0.0955  0.0097  -0.0080 719 HIS C N   
10147 C CA  . HIS C 418 ? 0.4067 0.4357 0.4562 0.0952  0.0033  -0.0034 719 HIS C CA  
10148 C C   . HIS C 418 ? 0.4481 0.4853 0.5035 0.1076  -0.0012 -0.0016 719 HIS C C   
10149 O O   . HIS C 418 ? 0.4747 0.5309 0.5427 0.1133  0.0003  -0.0040 719 HIS C O   
10150 C CB  . HIS C 418 ? 0.4307 0.4755 0.4858 0.0854  0.0026  -0.0031 719 HIS C CB  
10151 C CG  . HIS C 418 ? 0.4441 0.4910 0.4965 0.0849  -0.0040 0.0013  719 HIS C CG  
10152 N ND1 . HIS C 418 ? 0.3893 0.4184 0.4286 0.0817  -0.0066 0.0048  719 HIS C ND1 
10153 C CD2 . HIS C 418 ? 0.3787 0.4436 0.4393 0.0871  -0.0087 0.0030  719 HIS C CD2 
10154 C CE1 . HIS C 418 ? 0.4477 0.4828 0.4863 0.0820  -0.0125 0.0083  719 HIS C CE1 
10155 N NE2 . HIS C 418 ? 0.3993 0.4561 0.4509 0.0852  -0.0142 0.0073  719 HIS C NE2 
10156 N N   . VAL C 419 ? 0.5005 0.5238 0.5464 0.1117  -0.0067 0.0029  720 VAL C N   
10157 C CA  . VAL C 419 ? 0.6200 0.6490 0.6698 0.1242  -0.0122 0.0054  720 VAL C CA  
10158 C C   . VAL C 419 ? 0.4765 0.5200 0.5301 0.1201  -0.0182 0.0091  720 VAL C C   
10159 O O   . VAL C 419 ? 0.5648 0.5956 0.6071 0.1148  -0.0219 0.0130  720 VAL C O   
10160 C CB  . VAL C 419 ? 0.6956 0.6973 0.7307 0.1323  -0.0149 0.0082  720 VAL C CB  
10161 C CG1 . VAL C 419 ? 0.5955 0.6006 0.6315 0.1438  -0.0225 0.0125  720 VAL C CG1 
10162 C CG2 . VAL C 419 ? 0.7170 0.7084 0.7506 0.1392  -0.0094 0.0037  720 VAL C CG2 
10163 N N   . TRP C 420 ? 0.3948 0.4657 0.4640 0.1219  -0.0189 0.0077  721 TRP C N   
10164 C CA  . TRP C 420 ? 0.5302 0.6178 0.6042 0.1163  -0.0243 0.0103  721 TRP C CA  
10165 C C   . TRP C 420 ? 0.6767 0.7582 0.7443 0.1236  -0.0327 0.0159  721 TRP C C   
10166 O O   . TRP C 420 ? 0.6682 0.7472 0.7371 0.1371  -0.0354 0.0172  721 TRP C O   
10167 C CB  . TRP C 420 ? 0.5100 0.6286 0.6024 0.1169  -0.0233 0.0076  721 TRP C CB  
10168 C CG  . TRP C 420 ? 0.4463 0.5707 0.5424 0.1058  -0.0164 0.0032  721 TRP C CG  
10169 C CD1 . TRP C 420 ? 0.3628 0.4860 0.4621 0.1069  -0.0090 -0.0011 721 TRP C CD1 
10170 C CD2 . TRP C 420 ? 0.3228 0.4526 0.4177 0.0920  -0.0163 0.0028  721 TRP C CD2 
10171 N NE1 . TRP C 420 ? 0.3149 0.4428 0.4154 0.0946  -0.0047 -0.0038 721 TRP C NE1 
10172 C CE2 . TRP C 420 ? 0.3681 0.4997 0.4659 0.0856  -0.0089 -0.0016 721 TRP C CE2 
10173 C CE3 . TRP C 420 ? 0.4161 0.5486 0.5068 0.0846  -0.0217 0.0056  721 TRP C CE3 
10174 C CZ2 . TRP C 420 ? 0.4983 0.6332 0.5948 0.0727  -0.0071 -0.0030 721 TRP C CZ2 
10175 C CZ3 . TRP C 420 ? 0.4666 0.6023 0.5559 0.0718  -0.0195 0.0036  721 TRP C CZ3 
10176 C CH2 . TRP C 420 ? 0.5051 0.6416 0.5972 0.0662  -0.0124 -0.0006 721 TRP C CH2 
10177 N N   . LYS C 421 ? 0.7416 0.8205 0.8017 0.1149  -0.0369 0.0191  722 LYS C N   
10178 C CA  . LYS C 421 ? 0.7783 0.8499 0.8296 0.1192  -0.0452 0.0249  722 LYS C CA  
10179 C C   . LYS C 421 ? 0.8917 0.9889 0.9540 0.1211  -0.0522 0.0268  722 LYS C C   
10180 O O   . LYS C 421 ? 0.9335 1.0319 0.9955 0.1317  -0.0592 0.0308  722 LYS C O   
10181 C CB  . LYS C 421 ? 0.7747 0.8272 0.8092 0.1081  -0.0455 0.0274  722 LYS C CB  
10182 C CG  . LYS C 421 ? 0.8559 0.8838 0.8787 0.1044  -0.0394 0.0261  722 LYS C CG  
10183 C CD  . LYS C 421 ? 0.9154 0.9268 0.9219 0.0948  -0.0405 0.0295  722 LYS C CD  
10184 C CE  . LYS C 421 ? 0.8675 0.8580 0.8638 0.0893  -0.0343 0.0282  722 LYS C CE  
10185 N NZ  . LYS C 421 ? 0.8753 0.8460 0.8642 0.0980  -0.0346 0.0297  722 LYS C NZ  
10202 N N   . PHE D 4   ? 0.9958 0.7340 0.7640 0.1176  -0.0244 0.0152  305 PHE D N   
10203 C CA  . PHE D 4   ? 0.9276 0.6916 0.7097 0.1304  -0.0304 0.0157  305 PHE D CA  
10204 C C   . PHE D 4   ? 0.8241 0.6037 0.6161 0.1186  -0.0307 0.0179  305 PHE D C   
10205 O O   . PHE D 4   ? 0.8569 0.6235 0.6340 0.1206  -0.0349 0.0215  305 PHE D O   
10206 C CB  . PHE D 4   ? 1.0870 0.8278 0.8454 0.1491  -0.0370 0.0180  305 PHE D CB  
10207 C CG  . PHE D 4   ? 1.2950 0.9907 1.0214 0.1509  -0.0354 0.0186  305 PHE D CG  
10208 C CD1 . PHE D 4   ? 1.3964 1.0549 1.0929 0.1446  -0.0364 0.0230  305 PHE D CD1 
10209 C CD2 . PHE D 4   ? 1.3182 1.0069 1.0424 0.1575  -0.0327 0.0148  305 PHE D CD2 
10210 C CE1 . PHE D 4   ? 1.4484 1.0625 1.1126 0.1443  -0.0350 0.0237  305 PHE D CE1 
10211 C CE2 . PHE D 4   ? 1.4031 1.0468 1.0948 0.1578  -0.0313 0.0152  305 PHE D CE2 
10212 C CZ  . PHE D 4   ? 1.4709 1.0767 1.1322 0.1507  -0.0326 0.0197  305 PHE D CZ  
10213 N N   . LEU D 5   ? 0.6518 0.4574 0.4673 0.1066  -0.0262 0.0157  306 LEU D N   
10214 C CA  . LEU D 5   ? 0.5864 0.4061 0.4113 0.0951  -0.0254 0.0170  306 LEU D CA  
10215 C C   . LEU D 5   ? 0.5436 0.3994 0.3926 0.0994  -0.0287 0.0152  306 LEU D C   
10216 O O   . LEU D 5   ? 0.6188 0.4945 0.4838 0.1053  -0.0286 0.0123  306 LEU D O   
10217 C CB  . LEU D 5   ? 0.5404 0.3606 0.3714 0.0779  -0.0177 0.0161  306 LEU D CB  
10218 C CG  . LEU D 5   ? 0.6363 0.4241 0.4448 0.0706  -0.0139 0.0177  306 LEU D CG  
10219 C CD1 . LEU D 5   ? 0.5913 0.3869 0.4105 0.0556  -0.0067 0.0161  306 LEU D CD1 
10220 C CD2 . LEU D 5   ? 0.5851 0.3503 0.3712 0.0673  -0.0156 0.0219  306 LEU D CD2 
10221 N N   . LYS D 6   ? 0.4599 0.3238 0.3103 0.0955  -0.0316 0.0170  307 LYS D N   
10222 C CA  . LYS D 6   ? 0.4973 0.3936 0.3676 0.0971  -0.0353 0.0155  307 LYS D CA  
10223 C C   . LYS D 6   ? 0.4832 0.3911 0.3652 0.0818  -0.0305 0.0144  307 LYS D C   
10224 O O   . LYS D 6   ? 0.5072 0.3991 0.3787 0.0725  -0.0268 0.0159  307 LYS D O   
10225 C CB  . LYS D 6   ? 0.5897 0.4875 0.4514 0.1055  -0.0437 0.0181  307 LYS D CB  
10226 C CG  . LYS D 6   ? 0.6979 0.5896 0.5502 0.1240  -0.0497 0.0191  307 LYS D CG  
10227 C CD  . LYS D 6   ? 0.7437 0.6406 0.5889 0.1321  -0.0588 0.0219  307 LYS D CD  
10228 C CE  . LYS D 6   ? 0.8051 0.6949 0.6391 0.1528  -0.0652 0.0234  307 LYS D CE  
10229 N NZ  . LYS D 6   ? 0.8335 0.7491 0.6868 0.1631  -0.0648 0.0199  307 LYS D NZ  
10230 N N   . VAL D 7   ? 0.4040 0.3393 0.3067 0.0795  -0.0303 0.0117  308 VAL D N   
10231 C CA  . VAL D 7   ? 0.4201 0.3662 0.3320 0.0671  -0.0273 0.0107  308 VAL D CA  
10232 C C   . VAL D 7   ? 0.4529 0.4215 0.3737 0.0682  -0.0335 0.0102  308 VAL D C   
10233 O O   . VAL D 7   ? 0.4722 0.4591 0.4022 0.0767  -0.0380 0.0093  308 VAL D O   
10234 C CB  . VAL D 7   ? 0.4216 0.3767 0.3477 0.0602  -0.0207 0.0081  308 VAL D CB  
10235 C CG1 . VAL D 7   ? 0.5511 0.4857 0.4683 0.0576  -0.0150 0.0086  308 VAL D CG1 
10236 C CG2 . VAL D 7   ? 0.3520 0.3292 0.2938 0.0660  -0.0223 0.0058  308 VAL D CG2 
10237 N N   . LYS D 8   ? 0.4307 0.3982 0.3478 0.0595  -0.0339 0.0106  309 LYS D N   
10238 C CA  . LYS D 8   ? 0.3735 0.3594 0.2955 0.0580  -0.0402 0.0101  309 LYS D CA  
10239 C C   . LYS D 8   ? 0.3346 0.3303 0.2659 0.0459  -0.0365 0.0078  309 LYS D C   
10240 O O   . LYS D 8   ? 0.3426 0.3246 0.2697 0.0390  -0.0300 0.0075  309 LYS D O   
10241 C CB  . LYS D 8   ? 0.4398 0.4122 0.3441 0.0586  -0.0452 0.0127  309 LYS D CB  
10242 C CG  . LYS D 8   ? 0.4366 0.4253 0.3431 0.0540  -0.0517 0.0122  309 LYS D CG  
10243 C CD  . LYS D 8   ? 0.6064 0.5805 0.4937 0.0566  -0.0573 0.0150  309 LYS D CD  
10244 C CE  . LYS D 8   ? 0.6529 0.6433 0.5408 0.0516  -0.0648 0.0145  309 LYS D CE  
10245 N NZ  . LYS D 8   ? 0.6126 0.5867 0.4798 0.0530  -0.0699 0.0172  309 LYS D NZ  
10246 N N   . ASN D 9   ? 0.3213 0.3409 0.2646 0.0435  -0.0406 0.0063  310 ASN D N   
10247 C CA  . ASN D 9   ? 0.3598 0.3859 0.3072 0.0313  -0.0389 0.0044  310 ASN D CA  
10248 C C   . ASN D 9   ? 0.3574 0.3814 0.2936 0.0265  -0.0448 0.0050  310 ASN D C   
10249 O O   . ASN D 9   ? 0.4033 0.4426 0.3412 0.0303  -0.0526 0.0057  310 ASN D O   
10250 C CB  . ASN D 9   ? 0.4707 0.5229 0.4355 0.0286  -0.0396 0.0024  310 ASN D CB  
10251 C CG  . ASN D 9   ? 0.5096 0.5634 0.4753 0.0152  -0.0374 0.0006  310 ASN D CG  
10252 O OD1 . ASN D 9   ? 0.5222 0.5768 0.4808 0.0080  -0.0417 0.0004  310 ASN D OD1 
10253 N ND2 . ASN D 9   ? 0.4841 0.5359 0.4561 0.0117  -0.0309 -0.0006 310 ASN D ND2 
10254 N N   . TRP D 10  ? 0.3289 0.3349 0.2534 0.0187  -0.0410 0.0046  311 TRP D N   
10255 C CA  . TRP D 10  ? 0.4205 0.4189 0.3302 0.0146  -0.0459 0.0051  311 TRP D CA  
10256 C C   . TRP D 10  ? 0.4862 0.4995 0.3987 0.0047  -0.0507 0.0031  311 TRP D C   
10257 O O   . TRP D 10  ? 0.4525 0.4646 0.3540 0.0011  -0.0567 0.0034  311 TRP D O   
10258 C CB  . TRP D 10  ? 0.3632 0.3357 0.2574 0.0113  -0.0394 0.0052  311 TRP D CB  
10259 C CG  . TRP D 10  ? 0.4109 0.3691 0.2981 0.0193  -0.0369 0.0078  311 TRP D CG  
10260 C CD1 . TRP D 10  ? 0.3549 0.3079 0.2476 0.0229  -0.0306 0.0083  311 TRP D CD1 
10261 C CD2 . TRP D 10  ? 0.4666 0.4134 0.3384 0.0239  -0.0413 0.0105  311 TRP D CD2 
10262 N NE1 . TRP D 10  ? 0.4063 0.3439 0.2871 0.0285  -0.0305 0.0110  311 TRP D NE1 
10263 C CE2 . TRP D 10  ? 0.4354 0.3683 0.3029 0.0295  -0.0369 0.0125  311 TRP D CE2 
10264 C CE3 . TRP D 10  ? 0.4555 0.4013 0.3152 0.0230  -0.0488 0.0114  311 TRP D CE3 
10265 C CZ2 . TRP D 10  ? 0.5207 0.4372 0.3712 0.0343  -0.0395 0.0157  311 TRP D CZ2 
10266 C CZ3 . TRP D 10  ? 0.5503 0.4809 0.3939 0.0288  -0.0516 0.0146  311 TRP D CZ3 
10267 C CH2 . TRP D 10  ? 0.6480 0.5633 0.4866 0.0343  -0.0468 0.0168  311 TRP D CH2 
10268 N N   . GLU D 11  ? 0.4306 0.4576 0.3563 -0.0006 -0.0483 0.0012  312 GLU D N   
10269 C CA  . GLU D 11  ? 0.3823 0.4250 0.3108 -0.0116 -0.0530 -0.0005 312 GLU D CA  
10270 C C   . GLU D 11  ? 0.4119 0.4861 0.3543 -0.0078 -0.0608 0.0002  312 GLU D C   
10271 O O   . GLU D 11  ? 0.4332 0.5206 0.3729 -0.0140 -0.0685 0.0000  312 GLU D O   
10272 C CB  . GLU D 11  ? 0.3806 0.4219 0.3147 -0.0196 -0.0466 -0.0024 312 GLU D CB  
10273 C CG  . GLU D 11  ? 0.5855 0.6330 0.5159 -0.0341 -0.0497 -0.0043 312 GLU D CG  
10274 C CD  . GLU D 11  ? 0.6881 0.7348 0.6241 -0.0408 -0.0438 -0.0057 312 GLU D CD  
10275 O OE1 . GLU D 11  ? 0.6036 0.6431 0.5454 -0.0339 -0.0370 -0.0053 312 GLU D OE1 
10276 O OE2 . GLU D 11  ? 0.7811 0.8340 0.7146 -0.0537 -0.0462 -0.0070 312 GLU D OE2 
10277 N N   . THR D 12  ? 0.3832 0.4701 0.3397 0.0029  -0.0592 0.0009  313 THR D N   
10278 C CA  . THR D 12  ? 0.3403 0.4601 0.3119 0.0083  -0.0654 0.0012  313 THR D CA  
10279 C C   . THR D 12  ? 0.3996 0.5212 0.3685 0.0237  -0.0709 0.0036  313 THR D C   
10280 O O   . THR D 12  ? 0.3872 0.5370 0.3666 0.0298  -0.0776 0.0041  313 THR D O   
10281 C CB  . THR D 12  ? 0.4514 0.5860 0.4400 0.0107  -0.0598 0.0000  313 THR D CB  
10282 O OG1 . THR D 12  ? 0.4959 0.6118 0.4824 0.0220  -0.0542 0.0008  313 THR D OG1 
10283 C CG2 . THR D 12  ? 0.4644 0.5944 0.4534 -0.0042 -0.0544 -0.0020 313 THR D CG2 
10284 N N   . GLU D 13  ? 0.4142 0.5068 0.3688 0.0303  -0.0682 0.0053  314 GLU D N   
10285 C CA  . GLU D 13  ? 0.4371 0.5226 0.3845 0.0453  -0.0722 0.0080  314 GLU D CA  
10286 C C   . GLU D 13  ? 0.4728 0.5694 0.4322 0.0589  -0.0706 0.0080  314 GLU D C   
10287 O O   . GLU D 13  ? 0.4255 0.5183 0.3792 0.0731  -0.0747 0.0101  314 GLU D O   
10288 C CB  . GLU D 13  ? 0.5869 0.6856 0.5290 0.0475  -0.0831 0.0096  314 GLU D CB  
10289 C CG  . GLU D 13  ? 0.7022 0.7921 0.6321 0.0327  -0.0852 0.0089  314 GLU D CG  
10290 C CD  . GLU D 13  ? 0.8351 0.9233 0.7511 0.0364  -0.0948 0.0113  314 GLU D CD  
10291 O OE1 . GLU D 13  ? 0.8843 0.9485 0.7851 0.0451  -0.0945 0.0139  314 GLU D OE1 
10292 O OE2 . GLU D 13  ? 0.8709 0.9816 0.7904 0.0297  -0.1027 0.0108  314 GLU D OE2 
10293 N N   . VAL D 14  ? 0.4728 0.5809 0.4467 0.0553  -0.0647 0.0057  315 VAL D N   
10294 C CA  . VAL D 14  ? 0.4613 0.5746 0.4437 0.0679  -0.0618 0.0053  315 VAL D CA  
10295 C C   . VAL D 14  ? 0.4261 0.5051 0.3936 0.0743  -0.0570 0.0068  315 VAL D C   
10296 O O   . VAL D 14  ? 0.4040 0.4612 0.3636 0.0652  -0.0512 0.0067  315 VAL D O   
10297 C CB  . VAL D 14  ? 0.4980 0.6286 0.4969 0.0608  -0.0559 0.0026  315 VAL D CB  
10298 C CG1 . VAL D 14  ? 0.4569 0.5828 0.4599 0.0718  -0.0506 0.0018  315 VAL D CG1 
10299 C CG2 . VAL D 14  ? 0.5158 0.6847 0.5300 0.0570  -0.0611 0.0015  315 VAL D CG2 
10300 N N   . VAL D 15  ? 0.3978 0.4715 0.3600 0.0900  -0.0597 0.0082  316 VAL D N   
10301 C CA  . VAL D 15  ? 0.4422 0.4834 0.3892 0.0960  -0.0554 0.0095  316 VAL D CA  
10302 C C   . VAL D 15  ? 0.4377 0.4832 0.3929 0.1045  -0.0512 0.0076  316 VAL D C   
10303 O O   . VAL D 15  ? 0.4351 0.5037 0.4005 0.1155  -0.0546 0.0066  316 VAL D O   
10304 C CB  . VAL D 15  ? 0.4260 0.4494 0.3542 0.1072  -0.0618 0.0128  316 VAL D CB  
10305 C CG1 . VAL D 15  ? 0.4748 0.4615 0.3846 0.1097  -0.0567 0.0143  316 VAL D CG1 
10306 C CG2 . VAL D 15  ? 0.4257 0.4483 0.3457 0.0997  -0.0671 0.0146  316 VAL D CG2 
10307 N N   . LEU D 16  ? 0.3645 0.3889 0.3148 0.0997  -0.0437 0.0069  317 LEU D N   
10308 C CA  . LEU D 16  ? 0.4398 0.4615 0.3933 0.1065  -0.0392 0.0050  317 LEU D CA  
10309 C C   . LEU D 16  ? 0.5012 0.4872 0.4332 0.1121  -0.0377 0.0067  317 LEU D C   
10310 O O   . LEU D 16  ? 0.5034 0.4673 0.4218 0.1045  -0.0366 0.0089  317 LEU D O   
10311 C CB  . LEU D 16  ? 0.3617 0.3900 0.3274 0.0943  -0.0320 0.0026  317 LEU D CB  
10312 C CG  . LEU D 16  ? 0.4130 0.4719 0.3967 0.0858  -0.0328 0.0010  317 LEU D CG  
10313 C CD1 . LEU D 16  ? 0.3815 0.4415 0.3732 0.0743  -0.0259 -0.0008 317 LEU D CD1 
10314 C CD2 . LEU D 16  ? 0.3964 0.4855 0.3930 0.0962  -0.0368 -0.0002 317 LEU D CD2 
10315 N N   . THR D 17  ? 0.4325 0.4123 0.3603 0.1249  -0.0373 0.0057  318 THR D N   
10316 C CA  . THR D 17  ? 0.4715 0.4152 0.3757 0.1313  -0.0366 0.0073  318 THR D CA  
10317 C C   . THR D 17  ? 0.4696 0.4017 0.3731 0.1276  -0.0296 0.0048  318 THR D C   
10318 O O   . THR D 17  ? 0.4869 0.4339 0.4008 0.1348  -0.0281 0.0019  318 THR D O   
10319 C CB  . THR D 17  ? 0.5642 0.5039 0.4578 0.1515  -0.0430 0.0084  318 THR D CB  
10320 O OG1 . THR D 17  ? 0.5727 0.5311 0.4710 0.1549  -0.0503 0.0104  318 THR D OG1 
10321 C CG2 . THR D 17  ? 0.6117 0.5076 0.4754 0.1560  -0.0430 0.0108  318 THR D CG2 
10322 N N   . ASP D 18  ? 0.3924 0.2989 0.2833 0.1162  -0.0254 0.0060  319 ASP D N   
10323 C CA  . ASP D 18  ? 0.4252 0.3225 0.3162 0.1091  -0.0189 0.0038  319 ASP D CA  
10324 C C   . ASP D 18  ? 0.5024 0.3658 0.3690 0.1165  -0.0188 0.0041  319 ASP D C   
10325 O O   . ASP D 18  ? 0.5308 0.3666 0.3763 0.1147  -0.0202 0.0072  319 ASP D O   
10326 C CB  . ASP D 18  ? 0.4273 0.3211 0.3207 0.0913  -0.0143 0.0048  319 ASP D CB  
10327 C CG  . ASP D 18  ? 0.4063 0.3002 0.3056 0.0833  -0.0084 0.0024  319 ASP D CG  
10328 O OD1 . ASP D 18  ? 0.4987 0.3704 0.3834 0.0846  -0.0066 0.0018  319 ASP D OD1 
10329 O OD2 . ASP D 18  ? 0.4491 0.3643 0.3663 0.0755  -0.0058 0.0011  319 ASP D OD2 
10330 N N   . THR D 19  ? 0.4650 0.3292 0.3329 0.1244  -0.0169 0.0010  320 THR D N   
10331 C CA  . THR D 19  ? 0.5087 0.3384 0.3529 0.1280  -0.0152 0.0003  320 THR D CA  
10332 C C   . THR D 19  ? 0.5314 0.3593 0.3798 0.1163  -0.0091 -0.0024 320 THR D C   
10333 O O   . THR D 19  ? 0.5524 0.3495 0.3797 0.1133  -0.0072 -0.0028 320 THR D O   
10334 C CB  . THR D 19  ? 0.5145 0.3402 0.3505 0.1497  -0.0184 -0.0014 320 THR D CB  
10335 O OG1 . THR D 19  ? 0.5339 0.3968 0.3951 0.1558  -0.0174 -0.0046 320 THR D OG1 
10336 C CG2 . THR D 19  ? 0.5362 0.3539 0.3601 0.1626  -0.0253 0.0020  320 THR D CG2 
10337 N N   . LEU D 20  ? 0.4361 0.2952 0.3095 0.1091  -0.0063 -0.0042 321 LEU D N   
10338 C CA  . LEU D 20  ? 0.4781 0.3375 0.3560 0.0985  -0.0011 -0.0066 321 LEU D CA  
10339 C C   . LEU D 20  ? 0.5559 0.3936 0.4213 0.0827  0.0014  -0.0046 321 LEU D C   
10340 O O   . LEU D 20  ? 0.5034 0.3277 0.3607 0.0761  0.0044  -0.0063 321 LEU D O   
10341 C CB  . LEU D 20  ? 0.3898 0.2850 0.2951 0.0929  0.0009  -0.0080 321 LEU D CB  
10342 C CG  . LEU D 20  ? 0.4375 0.3376 0.3496 0.0840  0.0056  -0.0105 321 LEU D CG  
10343 C CD1 . LEU D 20  ? 0.5103 0.3997 0.4125 0.0943  0.0068  -0.0139 321 LEU D CD1 
10344 C CD2 . LEU D 20  ? 0.3019 0.2344 0.2381 0.0791  0.0069  -0.0111 321 LEU D CD2 
10345 N N   . HIS D 21  ? 0.4450 0.2800 0.3080 0.0760  0.0002  -0.0012 322 HIS D N   
10346 C CA  . HIS D 21  ? 0.4530 0.2722 0.3059 0.0604  0.0032  0.0008  322 HIS D CA  
10347 C C   . HIS D 21  ? 0.5597 0.3424 0.3846 0.0589  0.0035  0.0011  322 HIS D C   
10348 O O   . HIS D 21  ? 0.5175 0.2891 0.3347 0.0442  0.0066  0.0019  322 HIS D O   
10349 C CB  . HIS D 21  ? 0.4639 0.2841 0.3157 0.0560  0.0019  0.0044  322 HIS D CB  
10350 C CG  . HIS D 21  ? 0.4637 0.2615 0.2949 0.0660  -0.0027 0.0068  322 HIS D CG  
10351 N ND1 . HIS D 21  ? 0.5977 0.3622 0.4023 0.0611  -0.0025 0.0092  322 HIS D ND1 
10352 C CD2 . HIS D 21  ? 0.4814 0.2848 0.3134 0.0811  -0.0078 0.0070  322 HIS D CD2 
10353 C CE1 . HIS D 21  ? 0.6202 0.3686 0.4090 0.0734  -0.0075 0.0112  322 HIS D CE1 
10354 N NE2 . HIS D 21  ? 0.6184 0.3913 0.4243 0.0863  -0.0110 0.0099  322 HIS D NE2 
10355 N N   . LEU D 22  ? 0.5687 0.3322 0.3772 0.0737  0.0003  0.0003  323 LEU D N   
10356 C CA  . LEU D 22  ? 0.6434 0.3677 0.4218 0.0725  0.0006  0.0002  323 LEU D CA  
10357 C C   . LEU D 22  ? 0.6844 0.4064 0.4631 0.0641  0.0043  -0.0033 323 LEU D C   
10358 O O   . LEU D 22  ? 0.8054 0.4964 0.5599 0.0557  0.0054  -0.0032 323 LEU D O   
10359 C CB  . LEU D 22  ? 0.7090 0.4135 0.4695 0.0931  -0.0037 -0.0003 323 LEU D CB  
10360 C CG  . LEU D 22  ? 0.7965 0.4963 0.5500 0.1021  -0.0086 0.0035  323 LEU D CG  
10361 C CD1 . LEU D 22  ? 0.8733 0.5528 0.6079 0.1241  -0.0129 0.0029  323 LEU D CD1 
10362 C CD2 . LEU D 22  ? 0.7875 0.4622 0.5213 0.0875  -0.0080 0.0077  323 LEU D CD2 
10363 N N   . LYS D 23  ? 0.5813 0.3342 0.3849 0.0653  0.0062  -0.0061 324 LYS D N   
10364 C CA  . LYS D 23  ? 0.6001 0.3546 0.4060 0.0568  0.0095  -0.0092 324 LYS D CA  
10365 C C   . LYS D 23  ? 0.6194 0.3899 0.4387 0.0378  0.0124  -0.0078 324 LYS D C   
10366 O O   . LYS D 23  ? 0.6857 0.4665 0.5131 0.0309  0.0146  -0.0101 324 LYS D O   
10367 C CB  . LYS D 23  ? 0.5006 0.2799 0.3251 0.0679  0.0102  -0.0129 324 LYS D CB  
10368 C CG  . LYS D 23  ? 0.7087 0.4742 0.5201 0.0873  0.0084  -0.0154 324 LYS D CG  
10369 C CD  . LYS D 23  ? 0.7931 0.5210 0.5752 0.0866  0.0094  -0.0177 324 LYS D CD  
10370 C CE  . LYS D 23  ? 0.8629 0.5960 0.6467 0.0982  0.0113  -0.0227 324 LYS D CE  
10371 N NZ  . LYS D 23  ? 0.8984 0.5893 0.6482 0.1040  0.0115  -0.0253 324 LYS D NZ  
10372 N N   . SER D 24  ? 0.5021 0.2766 0.3241 0.0301  0.0124  -0.0042 325 SER D N   
10373 C CA  . SER D 24  ? 0.5773 0.3701 0.4131 0.0141  0.0154  -0.0029 325 SER D CA  
10374 C C   . SER D 24  ? 0.6803 0.4544 0.4997 -0.0007 0.0172  -0.0032 325 SER D C   
10375 O O   . SER D 24  ? 0.6898 0.4312 0.4824 -0.0029 0.0163  -0.0025 325 SER D O   
10376 C CB  . SER D 24  ? 0.6492 0.4486 0.4890 0.0104  0.0154  0.0008  325 SER D CB  
10377 O OG  . SER D 24  ? 0.7820 0.5955 0.6309 -0.0045 0.0188  0.0021  325 SER D OG  
10378 N N   . THR D 25  ? 0.7247 0.5190 0.5588 -0.0112 0.0195  -0.0041 326 THR D N   
10379 C CA  . THR D 25  ? 0.8300 0.6113 0.6507 -0.0262 0.0207  -0.0047 326 THR D CA  
10380 C C   . THR D 25  ? 0.8181 0.6105 0.6429 -0.0428 0.0230  -0.0016 326 THR D C   
10381 O O   . THR D 25  ? 0.9715 0.7423 0.7755 -0.0550 0.0236  -0.0001 326 THR D O   
10382 C CB  . THR D 25  ? 0.8693 0.6646 0.7008 -0.0268 0.0211  -0.0081 326 THR D CB  
10383 O OG1 . THR D 25  ? 0.8045 0.6113 0.6484 -0.0104 0.0203  -0.0103 326 THR D OG1 
10384 C CG2 . THR D 25  ? 0.9594 0.7250 0.7654 -0.0331 0.0206  -0.0106 326 THR D CG2 
10385 N N   . LEU D 26  ? 0.6154 0.4404 0.4654 -0.0434 0.0246  -0.0005 327 LEU D N   
10386 C CA  . LEU D 26  ? 0.6522 0.4947 0.5103 -0.0577 0.0274  0.0019  327 LEU D CA  
10387 C C   . LEU D 26  ? 0.6622 0.5089 0.5225 -0.0567 0.0290  0.0051  327 LEU D C   
10388 O O   . LEU D 26  ? 0.5574 0.4041 0.4218 -0.0440 0.0276  0.0052  327 LEU D O   
10389 C CB  . LEU D 26  ? 0.7094 0.5847 0.5922 -0.0583 0.0283  0.0009  327 LEU D CB  
10390 C CG  . LEU D 26  ? 0.7355 0.6059 0.6144 -0.0602 0.0266  -0.0023 327 LEU D CG  
10391 C CD1 . LEU D 26  ? 0.7432 0.6370 0.6432 -0.0513 0.0261  -0.0040 327 LEU D CD1 
10392 C CD2 . LEU D 26  ? 0.6607 0.5327 0.5330 -0.0783 0.0273  -0.0018 327 LEU D CD2 
10393 N N   . GLU D 27  ? 0.6010 0.4521 0.4577 -0.0709 0.0319  0.0075  328 GLU D N   
10394 C CA  . GLU D 27  ? 0.5375 0.3954 0.3967 -0.0714 0.0344  0.0104  328 GLU D CA  
10395 C C   . GLU D 27  ? 0.4930 0.3804 0.3775 -0.0619 0.0354  0.0100  328 GLU D C   
10396 O O   . GLU D 27  ? 0.4838 0.3940 0.3860 -0.0617 0.0358  0.0086  328 GLU D O   
10397 C CB  . GLU D 27  ? 0.6074 0.4702 0.4606 -0.0896 0.0383  0.0127  328 GLU D CB  
10398 C CG  . GLU D 27  ? 0.5749 0.4033 0.3978 -0.1012 0.0376  0.0138  328 GLU D CG  
10399 C CD  . GLU D 27  ? 0.6532 0.4885 0.4699 -0.1214 0.0418  0.0164  328 GLU D CD  
10400 O OE1 . GLU D 27  ? 0.7138 0.5194 0.5034 -0.1329 0.0417  0.0179  328 GLU D OE1 
10401 O OE2 . GLU D 27  ? 0.6121 0.4823 0.4500 -0.1259 0.0452  0.0170  328 GLU D OE2 
10402 N N   . THR D 28  ? 0.4652 0.3504 0.3496 -0.0538 0.0353  0.0112  329 THR D N   
10403 C CA  . THR D 28  ? 0.3981 0.3075 0.3025 -0.0464 0.0365  0.0110  329 THR D CA  
10404 C C   . THR D 28  ? 0.3526 0.2821 0.2650 -0.0547 0.0415  0.0126  329 THR D C   
10405 O O   . THR D 28  ? 0.3954 0.3468 0.3249 -0.0498 0.0430  0.0121  329 THR D O   
10406 C CB  . THR D 28  ? 0.5370 0.4368 0.4369 -0.0360 0.0344  0.0115  329 THR D CB  
10407 O OG1 . THR D 28  ? 0.4215 0.3059 0.3043 -0.0418 0.0360  0.0142  329 THR D OG1 
10408 C CG2 . THR D 28  ? 0.4534 0.3382 0.3477 -0.0259 0.0294  0.0098  329 THR D CG2 
10409 N N   . GLY D 29  ? 0.3856 0.3078 0.2852 -0.0671 0.0443  0.0146  330 GLY D N   
10410 C CA  . GLY D 29  ? 0.4322 0.3726 0.3369 -0.0743 0.0497  0.0165  330 GLY D CA  
10411 C C   . GLY D 29  ? 0.5462 0.4728 0.4370 -0.0742 0.0516  0.0186  330 GLY D C   
10412 O O   . GLY D 29  ? 0.5100 0.4446 0.3974 -0.0839 0.0566  0.0206  330 GLY D O   
10413 N N   . CYS D 30  ? 0.5248 0.4321 0.4072 -0.0638 0.0476  0.0184  331 CYS D N   
10414 C CA  . CYS D 30  ? 0.4584 0.3506 0.3258 -0.0630 0.0484  0.0205  331 CYS D CA  
10415 C C   . CYS D 30  ? 0.5171 0.3815 0.3591 -0.0732 0.0481  0.0229  331 CYS D C   
10416 O O   . CYS D 30  ? 0.4936 0.3447 0.3274 -0.0779 0.0458  0.0223  331 CYS D O   
10417 C CB  . CYS D 30  ? 0.4037 0.2866 0.2709 -0.0484 0.0433  0.0196  331 CYS D CB  
10418 S SG  . CYS D 30  ? 0.4509 0.3602 0.3428 -0.0377 0.0432  0.0169  331 CYS D SG  
10419 N N   . THR D 31  ? 0.4676 0.3213 0.2949 -0.0770 0.0504  0.0255  332 THR D N   
10420 C CA  . THR D 31  ? 0.5071 0.3280 0.3056 -0.0840 0.0492  0.0283  332 THR D CA  
10421 C C   . THR D 31  ? 0.5220 0.3271 0.3083 -0.0746 0.0467  0.0299  332 THR D C   
10422 O O   . THR D 31  ? 0.5507 0.3716 0.3509 -0.0649 0.0465  0.0287  332 THR D O   
10423 C CB  . THR D 31  ? 0.5681 0.3910 0.3564 -0.1033 0.0556  0.0308  332 THR D CB  
10424 O OG1 . THR D 31  ? 0.5962 0.4343 0.3881 -0.1047 0.0610  0.0322  332 THR D OG1 
10425 C CG2 . THR D 31  ? 0.5403 0.3878 0.3450 -0.1131 0.0583  0.0292  332 THR D CG2 
10426 N N   . GLU D 32  ? 0.5883 0.3604 0.3465 -0.0780 0.0446  0.0327  333 GLU D N   
10427 C CA  . GLU D 32  ? 0.6457 0.4016 0.3883 -0.0719 0.0426  0.0352  333 GLU D CA  
10428 C C   . GLU D 32  ? 0.6110 0.3864 0.3599 -0.0771 0.0490  0.0361  333 GLU D C   
10429 O O   . GLU D 32  ? 0.6378 0.4098 0.3824 -0.0692 0.0472  0.0368  333 GLU D O   
10430 C CB  . GLU D 32  ? 0.7544 0.4702 0.4621 -0.0780 0.0405  0.0388  333 GLU D CB  
10431 C CG  . GLU D 32  ? 1.0297 0.7194 0.7254 -0.0670 0.0330  0.0381  333 GLU D CG  
10432 C CD  . GLU D 32  ? 1.2460 0.9357 0.9460 -0.0731 0.0335  0.0357  333 GLU D CD  
10433 O OE1 . GLU D 32  ? 1.2698 0.9828 0.9846 -0.0858 0.0390  0.0346  333 GLU D OE1 
10434 O OE2 . GLU D 32  ? 1.3312 0.9977 1.0190 -0.0645 0.0282  0.0348  333 GLU D OE2 
10435 N N   . TYR D 33  ? 0.5678 0.3648 0.3266 -0.0899 0.0564  0.0359  334 TYR D N   
10436 C CA  . TYR D 33  ? 0.5648 0.3798 0.3271 -0.0952 0.0637  0.0368  334 TYR D CA  
10437 C C   . TYR D 33  ? 0.5887 0.4405 0.3804 -0.0889 0.0673  0.0336  334 TYR D C   
10438 O O   . TYR D 33  ? 0.5645 0.4290 0.3587 -0.0880 0.0723  0.0336  334 TYR D O   
10439 C CB  . TYR D 33  ? 0.6058 0.4198 0.3551 -0.1150 0.0705  0.0396  334 TYR D CB  
10440 C CG  . TYR D 33  ? 0.7658 0.5397 0.4809 -0.1223 0.0679  0.0434  334 TYR D CG  
10441 C CD1 . TYR D 33  ? 0.9538 0.7113 0.6486 -0.1227 0.0692  0.0464  334 TYR D CD1 
10442 C CD2 . TYR D 33  ? 0.8460 0.5957 0.5465 -0.1281 0.0639  0.0441  334 TYR D CD2 
10443 C CE1 . TYR D 33  ? 1.0620 0.7803 0.7232 -0.1287 0.0665  0.0503  334 TYR D CE1 
10444 C CE2 . TYR D 33  ? 0.9935 0.7022 0.6593 -0.1338 0.0613  0.0477  334 TYR D CE2 
10445 C CZ  . TYR D 33  ? 1.1072 0.8004 0.7536 -0.1340 0.0625  0.0510  334 TYR D CZ  
10446 O OH  . TYR D 33  ? 1.2647 0.9150 0.8743 -0.1391 0.0597  0.0551  334 TYR D OH  
10447 N N   . ILE D 34  ? 0.4810 0.3485 0.2928 -0.0844 0.0650  0.0308  335 ILE D N   
10448 C CA  . ILE D 34  ? 0.4537 0.3535 0.2909 -0.0782 0.0683  0.0281  335 ILE D CA  
10449 C C   . ILE D 34  ? 0.5377 0.4399 0.3894 -0.0661 0.0618  0.0253  335 ILE D C   
10450 O O   . ILE D 34  ? 0.5194 0.4126 0.3700 -0.0676 0.0578  0.0249  335 ILE D O   
10451 C CB  . ILE D 34  ? 0.6080 0.5347 0.4575 -0.0895 0.0749  0.0281  335 ILE D CB  
10452 C CG1 . ILE D 34  ? 0.8147 0.7404 0.6491 -0.1038 0.0818  0.0312  335 ILE D CG1 
10453 C CG2 . ILE D 34  ? 0.4605 0.4184 0.3334 -0.0807 0.0783  0.0257  335 ILE D CG2 
10454 C CD1 . ILE D 34  ? 0.9378 0.8613 0.7643 -0.1217 0.0834  0.0331  335 ILE D CD1 
10455 N N   . CYS D 35  ? 0.4467 0.3597 0.3101 -0.0547 0.0610  0.0232  336 CYS D N   
10456 C CA  . CYS D 35  ? 0.3766 0.2944 0.2542 -0.0446 0.0557  0.0206  336 CYS D CA  
10457 C C   . CYS D 35  ? 0.3927 0.3380 0.2914 -0.0429 0.0592  0.0187  336 CYS D C   
10458 O O   . CYS D 35  ? 0.3554 0.3153 0.2591 -0.0415 0.0645  0.0184  336 CYS D O   
10459 C CB  . CYS D 35  ? 0.4202 0.3291 0.2949 -0.0337 0.0510  0.0197  336 CYS D CB  
10460 S SG  . CYS D 35  ? 0.4169 0.3370 0.3106 -0.0233 0.0459  0.0165  336 CYS D SG  
10461 N N   . MET D 36  ? 0.3158 0.2676 0.2255 -0.0424 0.0564  0.0174  337 MET D N   
10462 C CA  . MET D 36  ? 0.3249 0.3014 0.2535 -0.0404 0.0588  0.0160  337 MET D CA  
10463 C C   . MET D 36  ? 0.3140 0.2925 0.2531 -0.0296 0.0543  0.0137  337 MET D C   
10464 O O   . MET D 36  ? 0.3292 0.3232 0.2820 -0.0278 0.0543  0.0127  337 MET D O   
10465 C CB  . MET D 36  ? 0.3941 0.3789 0.3266 -0.0503 0.0595  0.0165  337 MET D CB  
10466 C CG  . MET D 36  ? 0.5269 0.5125 0.4492 -0.0632 0.0645  0.0189  337 MET D CG  
10467 S SD  . MET D 36  ? 0.6706 0.6818 0.6046 -0.0751 0.0674  0.0193  337 MET D SD  
10468 C CE  . MET D 36  ? 0.6763 0.6829 0.5935 -0.0916 0.0731  0.0223  337 MET D CE  
10469 N N   . GLY D 37  ? 0.3608 0.3250 0.2932 -0.0230 0.0505  0.0132  338 GLY D N   
10470 C CA  . GLY D 37  ? 0.3032 0.2688 0.2440 -0.0147 0.0461  0.0112  338 GLY D CA  
10471 C C   . GLY D 37  ? 0.3402 0.3220 0.2936 -0.0099 0.0483  0.0098  338 GLY D C   
10472 O O   . GLY D 37  ? 0.3241 0.3091 0.2856 -0.0057 0.0451  0.0084  338 GLY D O   
10473 N N   . SER D 38  ? 0.2828 0.2744 0.2371 -0.0100 0.0539  0.0101  339 SER D N   
10474 C CA  . SER D 38  ? 0.3304 0.3349 0.2941 -0.0035 0.0560  0.0089  339 SER D CA  
10475 C C   . SER D 38  ? 0.3703 0.3954 0.3454 -0.0056 0.0595  0.0095  339 SER D C   
10476 O O   . SER D 38  ? 0.3364 0.3732 0.3184 0.0009  0.0618  0.0089  339 SER D O   
10477 C CB  . SER D 38  ? 0.2857 0.2869 0.2419 0.0014  0.0595  0.0082  339 SER D CB  
10478 O OG  . SER D 38  ? 0.3589 0.3663 0.3107 -0.0026 0.0655  0.0094  339 SER D OG  
10479 N N   . ILE D 39  ? 0.3442 0.3733 0.3201 -0.0145 0.0598  0.0108  340 ILE D N   
10480 C CA  . ILE D 39  ? 0.3122 0.3624 0.2994 -0.0181 0.0618  0.0115  340 ILE D CA  
10481 C C   . ILE D 39  ? 0.2994 0.3511 0.2950 -0.0151 0.0569  0.0105  340 ILE D C   
10482 O O   . ILE D 39  ? 0.3120 0.3490 0.3034 -0.0165 0.0524  0.0099  340 ILE D O   
10483 C CB  . ILE D 39  ? 0.4163 0.4681 0.3987 -0.0310 0.0634  0.0131  340 ILE D CB  
10484 C CG1 . ILE D 39  ? 0.4771 0.5239 0.4484 -0.0348 0.0682  0.0143  340 ILE D CG1 
10485 C CG2 . ILE D 39  ? 0.3689 0.4459 0.3636 -0.0361 0.0652  0.0138  340 ILE D CG2 
10486 C CD1 . ILE D 39  ? 0.4365 0.5051 0.4144 -0.0311 0.0749  0.0144  340 ILE D CD1 
10487 N N   . MET D 40  ? 0.2910 0.3608 0.2978 -0.0102 0.0579  0.0104  341 MET D N   
10488 C CA  . MET D 40  ? 0.3609 0.4320 0.3745 -0.0072 0.0535  0.0097  341 MET D CA  
10489 C C   . MET D 40  ? 0.3794 0.4493 0.3932 -0.0166 0.0506  0.0098  341 MET D C   
10490 O O   . MET D 40  ? 0.3244 0.3826 0.3363 -0.0160 0.0465  0.0088  341 MET D O   
10491 C CB  . MET D 40  ? 0.4874 0.5785 0.5113 -0.0004 0.0551  0.0102  341 MET D CB  
10492 C CG  . MET D 40  ? 0.6857 0.7767 0.7146 0.0038  0.0507  0.0098  341 MET D CG  
10493 S SD  . MET D 40  ? 0.7284 0.8011 0.7510 0.0137  0.0489  0.0085  341 MET D SD  
10494 C CE  . MET D 40  ? 0.5473 0.6260 0.5677 0.0233  0.0542  0.0088  341 MET D CE  
10495 N N   . HIS D 41  ? 0.3768 0.4594 0.3922 -0.0257 0.0528  0.0110  342 HIS D N   
10496 C CA  A HIS D 41  ? 0.4578 0.5374 0.4703 -0.0364 0.0503  0.0110  342 HIS D CA  
10497 C CA  B HIS D 41  ? 0.4592 0.5389 0.4717 -0.0364 0.0503  0.0110  342 HIS D CA  
10498 C C   . HIS D 41  ? 0.4163 0.4879 0.4177 -0.0471 0.0530  0.0121  342 HIS D C   
10499 O O   . HIS D 41  ? 0.3787 0.4669 0.3827 -0.0561 0.0560  0.0135  342 HIS D O   
10500 C CB  A HIS D 41  ? 0.4809 0.5843 0.5047 -0.0398 0.0497  0.0116  342 HIS D CB  
10501 C CB  B HIS D 41  ? 0.4797 0.5834 0.5039 -0.0393 0.0497  0.0116  342 HIS D CB  
10502 C CG  A HIS D 41  ? 0.4652 0.5820 0.5001 -0.0281 0.0489  0.0115  342 HIS D CG  
10503 C CG  B HIS D 41  ? 0.5057 0.6039 0.5266 -0.0481 0.0457  0.0108  342 HIS D CG  
10504 N ND1 A HIS D 41  ? 0.5619 0.6714 0.5981 -0.0230 0.0448  0.0105  342 HIS D ND1 
10505 N ND1 B HIS D 41  ? 0.5099 0.5836 0.5208 -0.0481 0.0425  0.0093  342 HIS D ND1 
10506 C CD2 A HIS D 41  ? 0.5174 0.6536 0.5608 -0.0203 0.0519  0.0124  342 HIS D CD2 
10507 C CD2 B HIS D 41  ? 0.5110 0.6254 0.5366 -0.0570 0.0445  0.0113  342 HIS D CD2 
10508 C CE1 A HIS D 41  ? 0.5244 0.6460 0.5683 -0.0132 0.0449  0.0111  342 HIS D CE1 
10509 C CE1 B HIS D 41  ? 0.4804 0.5531 0.4886 -0.0562 0.0398  0.0085  342 HIS D CE1 
10510 N NE2 A HIS D 41  ? 0.4752 0.6126 0.5234 -0.0106 0.0491  0.0122  342 HIS D NE2 
10511 N NE2 B HIS D 41  ? 0.4988 0.5956 0.5156 -0.0624 0.0407  0.0098  342 HIS D NE2 
10512 N N   . PRO D 42  ? 0.4497 0.4965 0.4379 -0.0467 0.0518  0.0118  343 PRO D N   
10513 C CA  . PRO D 42  ? 0.4871 0.5240 0.4622 -0.0560 0.0545  0.0134  343 PRO D CA  
10514 C C   . PRO D 42  ? 0.5719 0.6024 0.5382 -0.0700 0.0535  0.0139  343 PRO D C   
10515 O O   . PRO D 42  ? 0.5154 0.5455 0.4731 -0.0811 0.0568  0.0157  343 PRO D O   
10516 C CB  . PRO D 42  ? 0.4745 0.4861 0.4377 -0.0494 0.0523  0.0130  343 PRO D CB  
10517 C CG  . PRO D 42  ? 0.4685 0.4743 0.4365 -0.0413 0.0475  0.0110  343 PRO D CG  
10518 C CD  . PRO D 42  ? 0.5404 0.5689 0.5247 -0.0376 0.0479  0.0104  343 PRO D CD  
10519 N N   . SER D 43  ? 0.5382 0.5628 0.5047 -0.0708 0.0493  0.0124  344 SER D N   
10520 C CA  . SER D 43  ? 0.5773 0.5876 0.5302 -0.0836 0.0476  0.0124  344 SER D CA  
10521 C C   . SER D 43  ? 0.5337 0.5603 0.4958 -0.0888 0.0456  0.0114  344 SER D C   
10522 O O   . SER D 43  ? 0.4498 0.4855 0.4237 -0.0794 0.0433  0.0101  344 SER D O   
10523 C CB  . SER D 43  ? 0.5418 0.5185 0.4779 -0.0791 0.0439  0.0112  344 SER D CB  
10524 O OG  . SER D 43  ? 0.6016 0.5598 0.5208 -0.0909 0.0425  0.0110  344 SER D OG  
10525 N N   . GLN D 44  ? 0.5198 0.5495 0.4752 -0.1048 0.0462  0.0122  345 GLN D N   
10526 C CA  . GLN D 44  ? 0.6444 0.6840 0.6034 -0.1123 0.0433  0.0111  345 GLN D CA  
10527 C C   . GLN D 44  ? 0.7020 0.7092 0.6396 -0.1195 0.0399  0.0094  345 GLN D C   
10528 O O   . GLN D 44  ? 0.6665 0.6768 0.6014 -0.1296 0.0375  0.0084  345 GLN D O   
10529 C CB  . GLN D 44  ? 0.6726 0.7422 0.6397 -0.1263 0.0458  0.0130  345 GLN D CB  
10530 C CG  . GLN D 44  ? 0.7241 0.8266 0.7114 -0.1178 0.0496  0.0145  345 GLN D CG  
10531 C CD  . GLN D 44  ? 0.7498 0.8840 0.7448 -0.1314 0.0529  0.0165  345 GLN D CD  
10532 O OE1 . GLN D 44  ? 0.8055 0.9422 0.7954 -0.1384 0.0578  0.0182  345 GLN D OE1 
10533 N NE2 . GLN D 44  ? 0.7518 0.9120 0.7591 -0.1354 0.0503  0.0164  345 GLN D NE2 
10534 N N   . HIS D 45  ? 0.6735 0.6492 0.5948 -0.1140 0.0395  0.0091  346 HIS D N   
10535 C CA  . HIS D 45  ? 0.6928 0.6340 0.5911 -0.1177 0.0365  0.0073  346 HIS D CA  
10536 C C   . HIS D 45  ? 0.6756 0.6163 0.5791 -0.1096 0.0330  0.0042  346 HIS D C   
10537 O O   . HIS D 45  ? 0.7252 0.6668 0.6378 -0.0941 0.0321  0.0031  346 HIS D O   
10538 C CB  . HIS D 45  ? 0.6461 0.5569 0.5280 -0.1093 0.0365  0.0078  346 HIS D CB  
10539 C CG  . HIS D 45  ? 0.7037 0.5759 0.5573 -0.1142 0.0341  0.0066  346 HIS D CG  
10540 N ND1 . HIS D 45  ? 0.7215 0.5639 0.5591 -0.1031 0.0326  0.0064  346 HIS D ND1 
10541 C CD2 . HIS D 45  ? 0.7229 0.5800 0.5594 -0.1287 0.0329  0.0056  346 HIS D CD2 
10542 C CE1 . HIS D 45  ? 0.7783 0.5874 0.5896 -0.1091 0.0307  0.0053  346 HIS D CE1 
10543 N NE2 . HIS D 45  ? 0.7287 0.5446 0.5379 -0.1253 0.0310  0.0047  346 HIS D NE2 
10544 N N   . ALA D 46  ? 0.7650 0.7051 0.6625 -0.1211 0.0310  0.0029  347 ALA D N   
10545 C CA  . ALA D 46  ? 0.7111 0.6479 0.6096 -0.1156 0.0278  -0.0002 347 ALA D CA  
10546 C C   . ALA D 46  ? 0.7284 0.6262 0.5989 -0.1191 0.0259  -0.0027 347 ALA D C   
10547 O O   . ALA D 46  ? 0.7064 0.5823 0.5561 -0.1307 0.0265  -0.0018 347 ALA D O   
10548 C CB  . ALA D 46  ? 0.6582 0.6238 0.5700 -0.1249 0.0264  -0.0002 347 ALA D CB  
10549 N N   . ARG D 47  ? 0.7974 0.6854 0.6658 -0.1089 0.0239  -0.0059 348 ARG D N   
10550 C CA  . ARG D 47  ? 0.8469 0.6961 0.6877 -0.1085 0.0225  -0.0087 348 ARG D CA  
10551 C C   . ARG D 47  ? 0.8163 0.6542 0.6399 -0.1259 0.0206  -0.0104 348 ARG D C   
10552 O O   . ARG D 47  ? 0.8392 0.6408 0.6339 -0.1318 0.0199  -0.0118 348 ARG D O   
10553 C CB  . ARG D 47  ? 0.8219 0.6654 0.6662 -0.0897 0.0217  -0.0116 348 ARG D CB  
10554 C CG  . ARG D 47  ? 0.8325 0.6632 0.6744 -0.0747 0.0225  -0.0109 348 ARG D CG  
10555 C CD  . ARG D 47  ? 0.8776 0.7242 0.7377 -0.0574 0.0225  -0.0123 348 ARG D CD  
10556 N NE  . ARG D 47  ? 0.9801 0.8194 0.8345 -0.0526 0.0217  -0.0162 348 ARG D NE  
10557 C CZ  . ARG D 47  ? 0.9891 0.7987 0.8220 -0.0455 0.0212  -0.0191 348 ARG D CZ  
10558 N NH1 . ARG D 47  ? 1.0165 0.8000 0.8311 -0.0422 0.0209  -0.0182 348 ARG D NH1 
10559 N NH2 . ARG D 47  ? 0.7756 0.5811 0.6041 -0.0408 0.0211  -0.0230 348 ARG D NH2 
10560 N N   . ARG D 48  ? 0.7895 0.6568 0.6288 -0.1347 0.0195  -0.0102 349 ARG D N   
10561 C CA  . ARG D 48  ? 0.8698 0.7326 0.6956 -0.1530 0.0171  -0.0116 349 ARG D CA  
10562 C C   . ARG D 48  ? 0.8538 0.7542 0.6978 -0.1676 0.0172  -0.0084 349 ARG D C   
10563 O O   . ARG D 48  ? 0.8662 0.7996 0.7367 -0.1594 0.0186  -0.0060 349 ARG D O   
10564 C CB  . ARG D 48  ? 0.8212 0.6821 0.6461 -0.1474 0.0146  -0.0155 349 ARG D CB  
10565 C CG  . ARG D 48  ? 0.7304 0.6262 0.5848 -0.1349 0.0145  -0.0148 349 ARG D CG  
10566 C CD  . ARG D 48  ? 0.8260 0.7513 0.6921 -0.1472 0.0117  -0.0141 349 ARG D CD  
10567 N NE  . ARG D 48  ? 0.9309 0.8448 0.7848 -0.1497 0.0088  -0.0178 349 ARG D NE  
10568 C CZ  . ARG D 48  ? 1.1462 1.0738 0.9990 -0.1646 0.0052  -0.0180 349 ARG D CZ  
10569 N NH1 . ARG D 48  ? 1.2292 1.1844 1.0937 -0.1780 0.0043  -0.0147 349 ARG D NH1 
10570 N NH2 . ARG D 48  ? 1.1977 1.1127 1.0376 -0.1661 0.0027  -0.0217 349 ARG D NH2 
10571 N N   . PRO D 49  ? 0.9203 0.8173 0.7500 -0.1892 0.0156  -0.0084 350 PRO D N   
10572 C CA  . PRO D 49  ? 0.9874 0.9218 0.8336 -0.2041 0.0162  -0.0050 350 PRO D CA  
10573 C C   . PRO D 49  ? 1.1832 1.1609 1.0569 -0.2013 0.0139  -0.0044 350 PRO D C   
10574 O O   . PRO D 49  ? 1.0876 1.0670 0.9688 -0.1876 0.0120  -0.0064 350 PRO D O   
10575 C CB  . PRO D 49  ? 0.8759 0.7904 0.6953 -0.2294 0.0145  -0.0056 350 PRO D CB  
10576 C CG  . PRO D 49  ? 0.9203 0.7812 0.7067 -0.2255 0.0139  -0.0089 350 PRO D CG  
10577 C CD  . PRO D 49  ? 0.9698 0.8274 0.7659 -0.2017 0.0134  -0.0114 350 PRO D CD  
10578 N N   . GLU D 50  ? 1.4749 1.4881 1.3626 -0.2147 0.0141  -0.0016 351 GLU D N   
10579 C CA  . GLU D 50  ? 1.4550 1.5142 1.3695 -0.2129 0.0119  -0.0001 351 GLU D CA  
10580 C C   . GLU D 50  ? 1.3342 1.3920 1.2475 -0.2095 0.0068  -0.0028 351 GLU D C   
10581 O O   . GLU D 50  ? 1.3176 1.3841 1.2454 -0.1912 0.0063  -0.0031 351 GLU D O   
10582 C CB  . GLU D 50  ? 1.5744 1.6646 1.4942 -0.2346 0.0115  0.0024  351 GLU D CB  
10583 C CG  . GLU D 50  ? 1.6178 1.7149 1.5392 -0.2410 0.0170  0.0053  351 GLU D CG  
10584 C CD  . GLU D 50  ? 1.5865 1.7339 1.5393 -0.2335 0.0196  0.0086  351 GLU D CD  
10585 O OE1 . GLU D 50  ? 1.5558 1.7364 1.5275 -0.2290 0.0161  0.0090  351 GLU D OE1 
10586 O OE2 . GLU D 50  ? 1.5805 1.7335 1.5378 -0.2314 0.0250  0.0108  351 GLU D OE2 
10587 N N   . ASP D 51  ? 1.2522 1.2986 1.1470 -0.2280 0.0030  -0.0048 352 ASP D N   
10588 C CA  . ASP D 51  ? 1.2410 1.2919 1.1348 -0.2285 -0.0023 -0.0071 352 ASP D CA  
10589 C C   . ASP D 51  ? 1.2270 1.2302 1.0935 -0.2245 -0.0029 -0.0117 352 ASP D C   
10590 O O   . ASP D 51  ? 1.2926 1.2650 1.1480 -0.2139 0.0008  -0.0128 352 ASP D O   
10591 C CB  . ASP D 51  ? 1.3109 1.3859 1.2035 -0.2524 -0.0067 -0.0063 352 ASP D CB  
10592 C CG  . ASP D 51  ? 1.3254 1.4545 1.2495 -0.2482 -0.0090 -0.0030 352 ASP D CG  
10593 O OD1 . ASP D 51  ? 1.3532 1.5147 1.2873 -0.2629 -0.0093 -0.0003 352 ASP D OD1 
10594 O OD2 . ASP D 51  ? 1.2785 1.4177 1.2165 -0.2298 -0.0103 -0.0030 352 ASP D OD2 
10595 N N   . VAL D 52  ? 1.1300 1.1276 0.9850 -0.2322 -0.0076 -0.0145 353 VAL D N   
10596 C CA  . VAL D 52  ? 1.0307 0.9840 0.8578 -0.2292 -0.0081 -0.0194 353 VAL D CA  
10597 C C   . VAL D 52  ? 1.0180 0.9290 0.8156 -0.2384 -0.0057 -0.0209 353 VAL D C   
10598 O O   . VAL D 52  ? 0.9417 0.8478 0.7243 -0.2610 -0.0072 -0.0204 353 VAL D O   
10599 C CB  . VAL D 52  ? 0.8747 0.8298 0.6911 -0.2412 -0.0139 -0.0221 353 VAL D CB  
10600 C CG1 . VAL D 52  ? 0.8489 0.8349 0.6711 -0.2645 -0.0180 -0.0197 353 VAL D CG1 
10601 C CG2 . VAL D 52  ? 0.8768 0.7802 0.6557 -0.2455 -0.0141 -0.0276 353 VAL D CG2 
10602 N N   . ALA D 53  ? 0.9742 0.8553 0.7631 -0.2211 -0.0019 -0.0224 354 ALA D N   
10603 C CA  . ALA D 53  ? 0.8799 0.7187 0.6404 -0.2258 0.0004  -0.0233 354 ALA D CA  
10604 C C   . ALA D 53  ? 0.8609 0.6597 0.5841 -0.2401 -0.0023 -0.0277 354 ALA D C   
10605 O O   . ALA D 53  ? 0.7735 0.5676 0.4906 -0.2378 -0.0049 -0.0313 354 ALA D O   
10606 C CB  . ALA D 53  ? 0.8472 0.6660 0.6081 -0.2014 0.0043  -0.0240 354 ALA D CB  
10607 N N   . THR D 54  ? 0.8624 0.6307 0.5585 -0.2559 -0.0018 -0.0274 355 THR D N   
10608 C CA  . THR D 54  ? 0.8862 0.6047 0.5408 -0.2636 -0.0033 -0.0315 355 THR D CA  
10609 C C   . THR D 54  ? 0.8368 0.5172 0.4762 -0.2399 -0.0009 -0.0355 355 THR D C   
10610 O O   . THR D 54  ? 0.7142 0.4074 0.3748 -0.2182 0.0022  -0.0340 355 THR D O   
10611 C CB  . THR D 54  ? 0.8682 0.5681 0.5005 -0.2764 -0.0019 -0.0277 355 THR D CB  
10612 O OG1 . THR D 54  ? 0.8156 0.5099 0.4535 -0.2682 0.0017  -0.0252 355 THR D OG1 
10613 C CG2 . THR D 54  ? 0.7348 0.4737 0.3795 -0.2972 -0.0040 -0.0239 355 THR D CG2 
10614 N N   . LYS D 55  ? 0.8196 0.4583 0.4243 -0.2403 -0.0017 -0.0394 356 LYS D N   
10615 C CA  . LYS D 55  ? 0.8280 0.4297 0.4155 -0.2177 0.0006  -0.0441 356 LYS D CA  
10616 C C   . LYS D 55  ? 0.7379 0.3183 0.3198 -0.2049 0.0038  -0.0421 356 LYS D C   
10617 O O   . LYS D 55  ? 0.7393 0.3256 0.3362 -0.1800 0.0064  -0.0423 356 LYS D O   
10618 C CB  . LYS D 55  ? 0.9622 0.5265 0.5142 -0.2186 0.0000  -0.0464 356 LYS D CB  
10619 C CG  . LYS D 55  ? 1.0176 0.5462 0.5519 -0.1937 0.0028  -0.0506 356 LYS D CG  
10620 C CD  . LYS D 55  ? 1.1380 0.6379 0.6432 -0.1938 0.0022  -0.0535 356 LYS D CD  
10621 C CE  . LYS D 55  ? 1.1592 0.6360 0.6553 -0.1664 0.0054  -0.0583 356 LYS D CE  
10622 N NZ  . LYS D 55  ? 1.1951 0.6361 0.6573 -0.1649 0.0056  -0.0603 356 LYS D NZ  
10623 N N   . ASP D 56  ? 0.7771 0.3445 0.3436 -0.2165 0.0042  -0.0373 357 ASP D N   
10624 C CA  . ASP D 56  ? 0.8688 0.4135 0.4264 -0.2047 0.0067  -0.0349 357 ASP D CA  
10625 C C   . ASP D 56  ? 0.8405 0.4200 0.4332 -0.1986 0.0084  -0.0320 357 ASP D C   
10626 O O   . ASP D 56  ? 0.8187 0.3846 0.4088 -0.1852 0.0104  -0.0299 357 ASP D O   
10627 C CB  . ASP D 56  ? 0.9619 0.4844 0.4919 -0.2196 0.0066  -0.0306 357 ASP D CB  
10628 C CG  . ASP D 56  ? 1.1048 0.6633 0.6499 -0.2448 0.0057  -0.0267 357 ASP D CG  
10629 O OD1 . ASP D 56  ? 1.1854 0.7298 0.7088 -0.2587 0.0057  -0.0236 357 ASP D OD1 
10630 O OD2 . ASP D 56  ? 1.1896 0.7919 0.7679 -0.2500 0.0049  -0.0266 357 ASP D OD2 
10631 N N   . GLN D 57  ? 0.7026 0.3341 0.3315 -0.2036 0.0079  -0.0302 358 GLN D N   
10632 C CA  . GLN D 57  ? 0.7162 0.3895 0.3835 -0.1910 0.0101  -0.0262 358 GLN D CA  
10633 C C   . GLN D 57  ? 0.7466 0.4366 0.4356 -0.1663 0.0109  -0.0283 358 GLN D C   
10634 O O   . GLN D 57  ? 0.6968 0.3960 0.4019 -0.1485 0.0131  -0.0266 358 GLN D O   
10635 C CB  . GLN D 57  ? 0.7993 0.5198 0.4933 -0.2084 0.0093  -0.0227 358 GLN D CB  
10636 C CG  . GLN D 57  ? 0.8810 0.5939 0.5597 -0.2326 0.0095  -0.0196 358 GLN D CG  
10637 C CD  . GLN D 57  ? 0.9048 0.6629 0.6048 -0.2525 0.0080  -0.0173 358 GLN D CD  
10638 O OE1 . GLN D 57  ? 0.8959 0.6846 0.6165 -0.2497 0.0057  -0.0185 358 GLN D OE1 
10639 N NE2 . GLN D 57  ? 0.9341 0.6986 0.6295 -0.2711 0.0092  -0.0137 358 GLN D NE2 
10640 N N   . LEU D 58  ? 0.7038 0.3980 0.3926 -0.1659 0.0092  -0.0321 359 LEU D N   
10641 C CA  . LEU D 58  ? 0.6367 0.3503 0.3471 -0.1448 0.0104  -0.0337 359 LEU D CA  
10642 C C   . LEU D 58  ? 0.6190 0.2968 0.3087 -0.1255 0.0122  -0.0378 359 LEU D C   
10643 O O   . LEU D 58  ? 0.6029 0.2929 0.3099 -0.1053 0.0143  -0.0375 359 LEU D O   
10644 C CB  . LEU D 58  ? 0.6397 0.3764 0.3603 -0.1518 0.0080  -0.0356 359 LEU D CB  
10645 C CG  . LEU D 58  ? 0.6570 0.4163 0.4001 -0.1327 0.0093  -0.0369 359 LEU D CG  
10646 C CD1 . LEU D 58  ? 0.6036 0.3961 0.3795 -0.1215 0.0112  -0.0324 359 LEU D CD1 
10647 C CD2 . LEU D 58  ? 0.6336 0.4128 0.3832 -0.1407 0.0065  -0.0384 359 LEU D CD2 
10648 N N   . PHE D 59  ? 0.7015 0.3356 0.3539 -0.1310 0.0113  -0.0416 360 PHE D N   
10649 C CA  . PHE D 59  ? 0.7444 0.3465 0.3773 -0.1103 0.0132  -0.0460 360 PHE D CA  
10650 C C   . PHE D 59  ? 0.6556 0.2505 0.2920 -0.0917 0.0152  -0.0438 360 PHE D C   
10651 O O   . PHE D 59  ? 0.6748 0.2761 0.3212 -0.0697 0.0172  -0.0457 360 PHE D O   
10652 C CB  . PHE D 59  ? 0.7550 0.3054 0.3423 -0.1187 0.0120  -0.0505 360 PHE D CB  
10653 C CG  . PHE D 59  ? 0.8417 0.3608 0.4090 -0.0952 0.0144  -0.0554 360 PHE D CG  
10654 C CD1 . PHE D 59  ? 0.8322 0.3639 0.4077 -0.0831 0.0160  -0.0597 360 PHE D CD1 
10655 C CD2 . PHE D 59  ? 0.8292 0.3099 0.3716 -0.0835 0.0152  -0.0554 360 PHE D CD2 
10656 C CE1 . PHE D 59  ? 0.8688 0.3765 0.4282 -0.0603 0.0188  -0.0643 360 PHE D CE1 
10657 C CE2 . PHE D 59  ? 0.9196 0.3774 0.4469 -0.0593 0.0174  -0.0593 360 PHE D CE2 
10658 C CZ  . PHE D 59  ? 0.9926 0.4633 0.5278 -0.0478 0.0195  -0.0644 360 PHE D CZ  
10659 N N   . PRO D 60  ? 0.7364 0.3190 0.3647 -0.0992 0.0147  -0.0398 361 PRO D N   
10660 C CA  . PRO D 60  ? 0.6948 0.2713 0.3263 -0.0802 0.0160  -0.0377 361 PRO D CA  
10661 C C   . PRO D 60  ? 0.6718 0.2942 0.3442 -0.0657 0.0174  -0.0357 361 PRO D C   
10662 O O   . PRO D 60  ? 0.6602 0.2812 0.3370 -0.0446 0.0184  -0.0363 361 PRO D O   
10663 C CB  . PRO D 60  ? 0.7265 0.2885 0.3452 -0.0960 0.0152  -0.0331 361 PRO D CB  
10664 C CG  . PRO D 60  ? 0.8485 0.3873 0.4404 -0.1201 0.0136  -0.0346 361 PRO D CG  
10665 C CD  . PRO D 60  ? 0.7403 0.3099 0.3517 -0.1251 0.0130  -0.0373 361 PRO D CD  
10666 N N   . LEU D 61  ? 0.6747 0.3378 0.3764 -0.0765 0.0172  -0.0334 362 LEU D N   
10667 C CA  . LEU D 61  ? 0.6225 0.3263 0.3602 -0.0640 0.0185  -0.0317 362 LEU D CA  
10668 C C   . LEU D 61  ? 0.6727 0.3834 0.4165 -0.0492 0.0196  -0.0359 362 LEU D C   
10669 O O   . LEU D 61  ? 0.6137 0.3402 0.3744 -0.0321 0.0210  -0.0357 362 LEU D O   
10670 C CB  . LEU D 61  ? 0.5693 0.3112 0.3330 -0.0785 0.0179  -0.0284 362 LEU D CB  
10671 C CG  . LEU D 61  ? 0.6738 0.4129 0.4319 -0.0955 0.0175  -0.0244 362 LEU D CG  
10672 C CD1 . LEU D 61  ? 0.5373 0.3155 0.3199 -0.1090 0.0170  -0.0218 362 LEU D CD1 
10673 C CD2 . LEU D 61  ? 0.6949 0.4298 0.4558 -0.0858 0.0187  -0.0213 362 LEU D CD2 
10674 N N   . ALA D 62  ? 0.6663 0.3659 0.3958 -0.0564 0.0190  -0.0396 363 ALA D N   
10675 C CA  . ALA D 62  ? 0.6939 0.3986 0.4265 -0.0432 0.0207  -0.0439 363 ALA D CA  
10676 C C   . ALA D 62  ? 0.7072 0.3857 0.4228 -0.0228 0.0226  -0.0469 363 ALA D C   
10677 O O   . ALA D 62  ? 0.6047 0.3013 0.3364 -0.0057 0.0248  -0.0480 363 ALA D O   
10678 C CB  . ALA D 62  ? 0.6580 0.3519 0.3742 -0.0561 0.0195  -0.0474 363 ALA D CB  
10679 N N   . LYS D 63  ? 0.6747 0.3106 0.3569 -0.0245 0.0217  -0.0481 364 LYS D N   
10680 C CA  . LYS D 63  ? 0.7222 0.3301 0.3849 -0.0036 0.0231  -0.0509 364 LYS D CA  
10681 C C   . LYS D 63  ? 0.7132 0.3430 0.3987 0.0125  0.0236  -0.0476 364 LYS D C   
10682 O O   . LYS D 63  ? 0.6769 0.3133 0.3680 0.0331  0.0254  -0.0499 364 LYS D O   
10683 C CB  . LYS D 63  ? 0.7653 0.3211 0.3864 -0.0099 0.0215  -0.0517 364 LYS D CB  
10684 C CG  . LYS D 63  ? 0.9158 0.4389 0.5133 0.0135  0.0225  -0.0545 364 LYS D CG  
10685 C CD  . LYS D 63  ? 1.0127 0.4781 0.5635 0.0070  0.0209  -0.0558 364 LYS D CD  
10686 C CE  . LYS D 63  ? 1.0117 0.4557 0.5460 0.0324  0.0213  -0.0558 364 LYS D CE  
10687 N NZ  . LYS D 63  ? 0.8915 0.3512 0.4438 0.0483  0.0208  -0.0529 364 LYS D NZ  
10688 N N   . GLU D 64  ? 0.6400 0.2837 0.3395 0.0029  0.0220  -0.0423 365 GLU D N   
10689 C CA  . GLU D 64  ? 0.7466 0.4122 0.4678 0.0157  0.0219  -0.0389 365 GLU D CA  
10690 C C   . GLU D 64  ? 0.6948 0.4015 0.4481 0.0257  0.0237  -0.0398 365 GLU D C   
10691 O O   . GLU D 64  ? 0.6257 0.3424 0.3878 0.0438  0.0244  -0.0403 365 GLU D O   
10692 C CB  . GLU D 64  ? 0.7714 0.4472 0.5024 0.0007  0.0204  -0.0335 365 GLU D CB  
10693 C CG  . GLU D 64  ? 1.0032 0.7108 0.7628 0.0091  0.0204  -0.0299 365 GLU D CG  
10694 C CD  . GLU D 64  ? 1.2867 1.0082 1.0577 -0.0070 0.0198  -0.0251 365 GLU D CD  
10695 O OE1 . GLU D 64  ? 1.3641 1.0821 1.1346 -0.0038 0.0190  -0.0218 365 GLU D OE1 
10696 O OE2 . GLU D 64  ? 1.3615 1.0982 1.1413 -0.0226 0.0202  -0.0247 365 GLU D OE2 
10697 N N   . PHE D 65  ? 0.5195 0.2511 0.2900 0.0136  0.0243  -0.0397 366 PHE D N   
10698 C CA  . PHE D 65  ? 0.5489 0.3164 0.3469 0.0214  0.0261  -0.0402 366 PHE D CA  
10699 C C   . PHE D 65  ? 0.5413 0.3025 0.3308 0.0368  0.0287  -0.0453 366 PHE D C   
10700 O O   . PHE D 65  ? 0.5028 0.2850 0.3083 0.0512  0.0303  -0.0457 366 PHE D O   
10701 C CB  . PHE D 65  ? 0.5670 0.3583 0.3811 0.0063  0.0259  -0.0390 366 PHE D CB  
10702 C CG  . PHE D 65  ? 0.5857 0.4072 0.4218 0.0134  0.0279  -0.0399 366 PHE D CG  
10703 C CD1 . PHE D 65  ? 0.5273 0.3749 0.3868 0.0208  0.0284  -0.0372 366 PHE D CD1 
10704 C CD2 . PHE D 65  ? 0.5130 0.3354 0.3443 0.0124  0.0294  -0.0435 366 PHE D CD2 
10705 C CE1 . PHE D 65  ? 0.5135 0.3875 0.3913 0.0259  0.0303  -0.0378 366 PHE D CE1 
10706 C CE2 . PHE D 65  ? 0.5598 0.4093 0.4099 0.0181  0.0316  -0.0440 366 PHE D CE2 
10707 C CZ  . PHE D 65  ? 0.5150 0.3900 0.3881 0.0245  0.0321  -0.0411 366 PHE D CZ  
10708 N N   . ILE D 66  ? 0.5778 0.3114 0.3418 0.0335  0.0292  -0.0493 367 ILE D N   
10709 C CA  . ILE D 66  ? 0.6556 0.3828 0.4100 0.0487  0.0324  -0.0547 367 ILE D CA  
10710 C C   . ILE D 66  ? 0.6508 0.3650 0.3963 0.0697  0.0330  -0.0556 367 ILE D C   
10711 O O   . ILE D 66  ? 0.5804 0.3146 0.3386 0.0862  0.0356  -0.0575 367 ILE D O   
10712 C CB  . ILE D 66  ? 0.6152 0.3108 0.3400 0.0404  0.0326  -0.0591 367 ILE D CB  
10713 C CG1 . ILE D 66  ? 0.6638 0.3764 0.3992 0.0197  0.0312  -0.0578 367 ILE D CG1 
10714 C CG2 . ILE D 66  ? 0.5955 0.2842 0.3091 0.0573  0.0367  -0.0651 367 ILE D CG2 
10715 C CD1 . ILE D 66  ? 0.6090 0.3583 0.3696 0.0225  0.0336  -0.0582 367 ILE D CD1 
10716 N N   . ASP D 67  ? 0.6865 0.3691 0.4109 0.0691  0.0303  -0.0539 368 ASP D N   
10717 C CA  . ASP D 67  ? 0.7300 0.4016 0.4471 0.0890  0.0297  -0.0535 368 ASP D CA  
10718 C C   . ASP D 67  ? 0.6505 0.3650 0.4021 0.0982  0.0298  -0.0507 368 ASP D C   
10719 O O   . ASP D 67  ? 0.6111 0.3383 0.3689 0.1177  0.0314  -0.0528 368 ASP D O   
10720 C CB  . ASP D 67  ? 0.8032 0.4397 0.4970 0.0826  0.0262  -0.0503 368 ASP D CB  
10721 C CG  . ASP D 67  ? 0.8889 0.4742 0.5407 0.0789  0.0260  -0.0538 368 ASP D CG  
10722 O OD1 . ASP D 67  ? 0.8621 0.4377 0.5017 0.0841  0.0286  -0.0591 368 ASP D OD1 
10723 O OD2 . ASP D 67  ? 0.8867 0.4403 0.5161 0.0698  0.0234  -0.0511 368 ASP D OD2 
10724 N N   . GLN D 68  ? 0.5870 0.3253 0.3610 0.0840  0.0281  -0.0460 369 GLN D N   
10725 C CA  . GLN D 68  ? 0.5714 0.3482 0.3762 0.0899  0.0278  -0.0432 369 GLN D CA  
10726 C C   . GLN D 68  ? 0.6529 0.4605 0.4764 0.0977  0.0313  -0.0462 369 GLN D C   
10727 O O   . GLN D 68  ? 0.6544 0.4820 0.4903 0.1128  0.0319  -0.0466 369 GLN D O   
10728 C CB  . GLN D 68  ? 0.6171 0.4108 0.4394 0.0720  0.0262  -0.0385 369 GLN D CB  
10729 C CG  . GLN D 68  ? 0.6577 0.4868 0.5086 0.0754  0.0255  -0.0355 369 GLN D CG  
10730 C CD  . GLN D 68  ? 0.7472 0.5928 0.6143 0.0584  0.0248  -0.0316 369 GLN D CD  
10731 O OE1 . GLN D 68  ? 0.6738 0.5495 0.5642 0.0570  0.0253  -0.0302 369 GLN D OE1 
10732 N NE2 . GLN D 68  ? 0.8332 0.6589 0.6870 0.0455  0.0236  -0.0298 369 GLN D NE2 
10733 N N   . TYR D 69  ? 0.6186 0.4318 0.4443 0.0868  0.0335  -0.0481 370 TYR D N   
10734 C CA  . TYR D 69  ? 0.6073 0.4483 0.4487 0.0925  0.0372  -0.0507 370 TYR D CA  
10735 C C   . TYR D 69  ? 0.5691 0.4022 0.3980 0.1127  0.0402  -0.0556 370 TYR D C   
10736 O O   . TYR D 69  ? 0.5285 0.3907 0.3746 0.1239  0.0427  -0.0565 370 TYR D O   
10737 C CB  . TYR D 69  ? 0.5805 0.4232 0.4211 0.0778  0.0386  -0.0520 370 TYR D CB  
10738 C CG  . TYR D 69  ? 0.5508 0.4148 0.4003 0.0844  0.0431  -0.0554 370 TYR D CG  
10739 C CD1 . TYR D 69  ? 0.4738 0.3749 0.3502 0.0846  0.0444  -0.0533 370 TYR D CD1 
10740 C CD2 . TYR D 69  ? 0.5412 0.3869 0.3702 0.0902  0.0462  -0.0608 370 TYR D CD2 
10741 C CE1 . TYR D 69  ? 0.5145 0.4355 0.3981 0.0893  0.0489  -0.0561 370 TYR D CE1 
10742 C CE2 . TYR D 69  ? 0.5951 0.4612 0.4316 0.0960  0.0510  -0.0639 370 TYR D CE2 
10743 C CZ  . TYR D 69  ? 0.5841 0.4885 0.4484 0.0952  0.0524  -0.0614 370 TYR D CZ  
10744 O OH  . TYR D 69  ? 0.5970 0.5221 0.4680 0.0996  0.0575  -0.0642 370 TYR D OH  
10745 N N   . TYR D 70  ? 0.5293 0.3233 0.3272 0.1176  0.0402  -0.0588 371 TYR D N   
10746 C CA  . TYR D 70  ? 0.6116 0.3975 0.3963 0.1389  0.0434  -0.0637 371 TYR D CA  
10747 C C   . TYR D 70  ? 0.5617 0.3541 0.3511 0.1575  0.0417  -0.0622 371 TYR D C   
10748 O O   . TYR D 70  ? 0.6061 0.4157 0.4012 0.1762  0.0446  -0.0651 371 TYR D O   
10749 C CB  . TYR D 70  ? 0.6480 0.3872 0.3951 0.1396  0.0441  -0.0681 371 TYR D CB  
10750 C CG  . TYR D 70  ? 0.6154 0.3594 0.3606 0.1314  0.0479  -0.0720 371 TYR D CG  
10751 C CD1 . TYR D 70  ? 0.5847 0.3234 0.3284 0.1087  0.0461  -0.0705 371 TYR D CD1 
10752 C CD2 . TYR D 70  ? 0.6561 0.4143 0.4033 0.1464  0.0533  -0.0768 371 TYR D CD2 
10753 C CE1 . TYR D 70  ? 0.6285 0.3726 0.3704 0.1012  0.0489  -0.0738 371 TYR D CE1 
10754 C CE2 . TYR D 70  ? 0.5875 0.3507 0.3325 0.1386  0.0569  -0.0801 371 TYR D CE2 
10755 C CZ  . TYR D 70  ? 0.6022 0.3573 0.3440 0.1159  0.0543  -0.0785 371 TYR D CZ  
10756 O OH  . TYR D 70  ? 0.6672 0.4267 0.4056 0.1083  0.0572  -0.0817 371 TYR D OH  
10757 N N   . SER D 71  ? 0.6200 0.4008 0.4073 0.1530  0.0368  -0.0576 372 SER D N   
10758 C CA  . SER D 71  ? 0.6960 0.4888 0.4918 0.1688  0.0342  -0.0552 372 SER D CA  
10759 C C   . SER D 71  ? 0.6482 0.4927 0.4800 0.1704  0.0353  -0.0538 372 SER D C   
10760 O O   . SER D 71  ? 0.5786 0.4435 0.4194 0.1885  0.0357  -0.0548 372 SER D O   
10761 C CB  . SER D 71  ? 0.7442 0.5175 0.5326 0.1601  0.0290  -0.0501 372 SER D CB  
10762 O OG  . SER D 71  ? 0.8612 0.5848 0.6134 0.1615  0.0275  -0.0510 372 SER D OG  
10763 N N   . SER D 72  ? 0.6171 0.4831 0.4687 0.1515  0.0358  -0.0515 373 SER D N   
10764 C CA  . SER D 72  ? 0.5927 0.5038 0.4758 0.1497  0.0366  -0.0498 373 SER D CA  
10765 C C   . SER D 72  ? 0.6360 0.5718 0.5274 0.1625  0.0415  -0.0540 373 SER D C   
10766 O O   . SER D 72  ? 0.6242 0.5949 0.5364 0.1695  0.0417  -0.0532 373 SER D O   
10767 C CB  . SER D 72  ? 0.5477 0.4709 0.4450 0.1279  0.0366  -0.0471 373 SER D CB  
10768 O OG  . SER D 72  ? 0.5795 0.5038 0.4741 0.1219  0.0407  -0.0502 373 SER D OG  
10769 N N   . ILE D 73  ? 0.5484 0.4680 0.4236 0.1649  0.0457  -0.0586 374 ILE D N   
10770 C CA  . ILE D 73  ? 0.5603 0.5024 0.4414 0.1774  0.0513  -0.0630 374 ILE D CA  
10771 C C   . ILE D 73  ? 0.5976 0.5216 0.4588 0.2018  0.0525  -0.0670 374 ILE D C   
10772 O O   . ILE D 73  ? 0.6535 0.5862 0.5114 0.2141  0.0580  -0.0718 374 ILE D O   
10773 C CB  . ILE D 73  ? 0.5933 0.5342 0.4708 0.1655  0.0559  -0.0658 374 ILE D CB  
10774 C CG1 . ILE D 73  ? 0.5736 0.4680 0.4184 0.1642  0.0559  -0.0690 374 ILE D CG1 
10775 C CG2 . ILE D 73  ? 0.5176 0.4758 0.4139 0.1433  0.0542  -0.0614 374 ILE D CG2 
10776 C CD1 . ILE D 73  ? 0.5529 0.4444 0.3908 0.1549  0.0602  -0.0724 374 ILE D CD1 
10777 N N   . LYS D 74  ? 0.6975 0.5960 0.5443 0.2099  0.0475  -0.0650 375 LYS D N   
10778 C CA  . LYS D 74  ? 0.7698 0.6532 0.5997 0.2327  0.0467  -0.0669 375 LYS D CA  
10779 C C   . LYS D 74  ? 0.6907 0.5409 0.4930 0.2352  0.0497  -0.0708 375 LYS D C   
10780 O O   . LYS D 74  ? 0.6434 0.4975 0.4408 0.2496  0.0510  -0.0723 375 LYS D O   
10781 C CB  . LYS D 74  ? 0.8520 0.7827 0.7076 0.2451  0.0473  -0.0660 375 LYS D CB  
10782 C CG  . LYS D 74  ? 0.9244 0.8910 0.8080 0.2406  0.0444  -0.0622 375 LYS D CG  
10783 C CD  . LYS D 74  ? 1.0227 1.0426 0.9354 0.2437  0.0471  -0.0624 375 LYS D CD  
10784 C CE  . LYS D 74  ? 1.0883 1.1412 1.0261 0.2386  0.0430  -0.0583 375 LYS D CE  
10785 N NZ  . LYS D 74  ? 1.0861 1.1151 1.0122 0.2448  0.0358  -0.0548 375 LYS D NZ  
10786 N N   . ARG D 75  ? 0.7158 0.5329 0.4990 0.2207  0.0504  -0.0726 376 ARG D N   
10787 C CA  . ARG D 75  ? 0.7147 0.4980 0.4700 0.2192  0.0528  -0.0764 376 ARG D CA  
10788 C C   . ARG D 75  ? 0.7939 0.5257 0.5180 0.2092  0.0485  -0.0750 376 ARG D C   
10789 O O   . ARG D 75  ? 0.7500 0.4528 0.4524 0.1980  0.0498  -0.0778 376 ARG D O   
10790 C CB  . ARG D 75  ? 0.6714 0.4689 0.4335 0.2081  0.0585  -0.0804 376 ARG D CB  
10791 C CG  . ARG D 75  ? 0.6556 0.5038 0.4471 0.2155  0.0633  -0.0814 376 ARG D CG  
10792 C CD  . ARG D 75  ? 0.8590 0.7142 0.6480 0.2349  0.0642  -0.0822 376 ARG D CD  
10793 N NE  . ARG D 75  ? 1.0813 0.9526 0.8729 0.2373  0.0707  -0.0865 376 ARG D NE  
10794 C CZ  . ARG D 75  ? 1.1331 1.0514 0.9517 0.2410  0.0748  -0.0867 376 ARG D CZ  
10795 N NH1 . ARG D 75  ? 1.1639 1.0928 0.9815 0.2423  0.0811  -0.0906 376 ARG D NH1 
10796 N NH2 . ARG D 75  ? 1.0732 1.0275 0.9188 0.2424  0.0726  -0.0829 376 ARG D NH2 
10797 N N   . PHE D 76  ? 0.7899 0.5105 0.5109 0.2116  0.0432  -0.0705 377 PHE D N   
10798 C CA  . PHE D 76  ? 0.8486 0.5215 0.5397 0.2005  0.0392  -0.0685 377 PHE D CA  
10799 C C   . PHE D 76  ? 0.9261 0.5628 0.5849 0.2077  0.0391  -0.0701 377 PHE D C   
10800 O O   . PHE D 76  ? 0.8601 0.5013 0.5162 0.2270  0.0387  -0.0697 377 PHE D O   
10801 C CB  . PHE D 76  ? 0.9171 0.5863 0.6107 0.2028  0.0338  -0.0631 377 PHE D CB  
10802 C CG  . PHE D 76  ? 0.9992 0.6230 0.6644 0.1878  0.0302  -0.0605 377 PHE D CG  
10803 C CD1 . PHE D 76  ? 1.0582 0.6437 0.6914 0.1931  0.0275  -0.0590 377 PHE D CD1 
10804 C CD2 . PHE D 76  ? 1.0266 0.6474 0.6965 0.1671  0.0296  -0.0593 377 PHE D CD2 
10805 C CE1 . PHE D 76  ? 1.0942 0.6394 0.7005 0.1773  0.0245  -0.0563 377 PHE D CE1 
10806 C CE2 . PHE D 76  ? 1.0051 0.5863 0.6490 0.1515  0.0266  -0.0569 377 PHE D CE2 
10807 C CZ  . PHE D 76  ? 1.0089 0.5533 0.6215 0.1558  0.0240  -0.0551 377 PHE D CZ  
10808 N N   . GLY D 77  ? 0.9727 0.5747 0.6067 0.1917  0.0393  -0.0718 378 GLY D N   
10809 C CA  . GLY D 77  ? 0.9204 0.4860 0.5216 0.1962  0.0394  -0.0734 378 GLY D CA  
10810 C C   . GLY D 77  ? 0.9000 0.4799 0.5041 0.2064  0.0446  -0.0785 378 GLY D C   
10811 O O   . GLY D 77  ? 0.9383 0.4883 0.5146 0.2120  0.0451  -0.0801 378 GLY D O   
10812 N N   . SER D 78  ? 0.8243 0.4483 0.4598 0.2088  0.0488  -0.0808 379 SER D N   
10813 C CA  . SER D 78  ? 0.7553 0.3954 0.3947 0.2164  0.0544  -0.0856 379 SER D CA  
10814 C C   . SER D 78  ? 0.8208 0.4301 0.4357 0.2005  0.0557  -0.0891 379 SER D C   
10815 O O   . SER D 78  ? 0.7827 0.3674 0.3845 0.1810  0.0526  -0.0879 379 SER D O   
10816 C CB  . SER D 78  ? 0.7147 0.4074 0.3914 0.2169  0.0585  -0.0867 379 SER D CB  
10817 O OG  . SER D 78  ? 0.7446 0.4406 0.4285 0.1964  0.0586  -0.0870 379 SER D OG  
10818 N N   . LYS D 79  ? 0.7811 0.3941 0.3906 0.2082  0.0604  -0.0934 380 LYS D N   
10819 C CA  . LYS D 79  ? 0.9084 0.4968 0.4966 0.1933  0.0619  -0.0971 380 LYS D CA  
10820 C C   . LYS D 79  ? 0.8907 0.4931 0.4928 0.1714  0.0618  -0.0975 380 LYS D C   
10821 O O   . LYS D 79  ? 0.9413 0.5152 0.5244 0.1520  0.0586  -0.0973 380 LYS D O   
10822 C CB  . LYS D 79  ? 0.9426 0.5415 0.5288 0.2058  0.0678  -0.1019 380 LYS D CB  
10823 C CG  . LYS D 79  ? 1.0787 0.6451 0.6364 0.1932  0.0687  -0.1057 380 LYS D CG  
10824 C CD  . LYS D 79  ? 1.1293 0.7049 0.6836 0.2066  0.0749  -0.1106 380 LYS D CD  
10825 C CE  . LYS D 79  ? 1.1249 0.6930 0.6697 0.2313  0.0756  -0.1101 380 LYS D CE  
10826 N NZ  . LYS D 79  ? 1.0731 0.5880 0.5797 0.2313  0.0709  -0.1082 380 LYS D NZ  
10827 N N   . ALA D 80  ? 0.8318 0.4788 0.4665 0.1735  0.0650  -0.0977 381 ALA D N   
10828 C CA  . ALA D 80  ? 0.7796 0.4404 0.4261 0.1541  0.0650  -0.0979 381 ALA D CA  
10829 C C   . ALA D 80  ? 0.8058 0.4479 0.4474 0.1392  0.0592  -0.0941 381 ALA D C   
10830 O O   . ALA D 80  ? 0.7618 0.3969 0.3997 0.1173  0.0566  -0.0933 381 ALA D O   
10831 C CB  . ALA D 80  ? 0.7116 0.4232 0.3930 0.1602  0.0694  -0.0977 381 ALA D CB  
10832 N N   . HIS D 81  ? 0.8507 0.4902 0.4964 0.1490  0.0562  -0.0903 382 HIS D N   
10833 C CA  . HIS D 81  ? 0.8101 0.4321 0.4510 0.1353  0.0510  -0.0863 382 HIS D CA  
10834 C C   . HIS D 81  ? 0.8392 0.4157 0.4463 0.1193  0.0475  -0.0863 382 HIS D C   
10835 O O   . HIS D 81  ? 0.7766 0.3457 0.3808 0.0972  0.0446  -0.0850 382 HIS D O   
10836 C CB  . HIS D 81  ? 0.7763 0.4027 0.4253 0.1505  0.0485  -0.0821 382 HIS D CB  
10837 C CG  . HIS D 81  ? 0.8382 0.4502 0.4847 0.1368  0.0433  -0.0771 382 HIS D CG  
10838 N ND1 . HIS D 81  ? 0.8953 0.5034 0.5430 0.1481  0.0404  -0.0735 382 HIS D ND1 
10839 C CD2 . HIS D 81  ? 0.8355 0.4417 0.4818 0.1114  0.0400  -0.0740 382 HIS D CD2 
10840 C CE1 . HIS D 81  ? 0.8936 0.4915 0.5400 0.1303  0.0362  -0.0687 382 HIS D CE1 
10841 N NE2 . HIS D 81  ? 0.8717 0.4696 0.5181 0.1078  0.0360  -0.0688 382 HIS D NE2 
10842 N N   . MET D 82  ? 0.7732 0.3218 0.3557 0.1292  0.0473  -0.0870 383 MET D N   
10843 C CA  . MET D 82  ? 0.8545 0.3592 0.4031 0.1141  0.0439  -0.0862 383 MET D CA  
10844 C C   . MET D 82  ? 0.9211 0.4229 0.4627 0.0951  0.0447  -0.0898 383 MET D C   
10845 O O   . MET D 82  ? 0.9508 0.4330 0.4782 0.0726  0.0410  -0.0883 383 MET D O   
10846 C CB  . MET D 82  ? 0.8973 0.3721 0.4191 0.1306  0.0440  -0.0862 383 MET D CB  
10847 C CG  . MET D 82  ? 0.9297 0.4047 0.4545 0.1487  0.0421  -0.0822 383 MET D CG  
10848 S SD  . MET D 82  ? 1.0922 0.5631 0.6229 0.1327  0.0370  -0.0764 383 MET D SD  
10849 C CE  . MET D 82  ? 1.0878 0.5072 0.5776 0.1092  0.0334  -0.0746 383 MET D CE  
10850 N N   . GLU D 83  ? 0.9011 0.4242 0.4527 0.1032  0.0494  -0.0942 384 GLU D N   
10851 C CA  . GLU D 83  ? 0.9544 0.4793 0.5017 0.0855  0.0499  -0.0974 384 GLU D CA  
10852 C C   . GLU D 83  ? 0.8879 0.4313 0.4523 0.0654  0.0473  -0.0957 384 GLU D C   
10853 O O   . GLU D 83  ? 0.8959 0.4275 0.4488 0.0430  0.0439  -0.0957 384 GLU D O   
10854 C CB  . GLU D 83  ? 0.9986 0.5487 0.5573 0.0984  0.0560  -0.1020 384 GLU D CB  
10855 C CG  . GLU D 83  ? 1.1958 0.7289 0.7368 0.1171  0.0590  -0.1044 384 GLU D CG  
10856 C CD  . GLU D 83  ? 1.2754 0.8353 0.8280 0.1275  0.0654  -0.1089 384 GLU D CD  
10857 O OE1 . GLU D 83  ? 1.3047 0.8917 0.8747 0.1175  0.0672  -0.1101 384 GLU D OE1 
10858 O OE2 . GLU D 83  ? 1.2941 0.8479 0.8374 0.1454  0.0688  -0.1111 384 GLU D OE2 
10859 N N   . ARG D 84  ? 0.8024 0.3807 0.3988 0.0721  0.0480  -0.0924 385 ARG D N   
10860 C CA  . ARG D 84  ? 0.7693 0.3808 0.3958 0.0525  0.0441  -0.0861 385 ARG D CA  
10861 C C   . ARG D 84  ? 0.7870 0.3735 0.3987 0.0337  0.0386  -0.0827 385 ARG D C   
10862 O O   . ARG D 84  ? 0.8112 0.4059 0.4275 0.0119  0.0352  -0.0806 385 ARG D O   
10863 C CB  . ARG D 84  ? 0.7603 0.4142 0.4248 0.0634  0.0452  -0.0815 385 ARG D CB  
10864 C CG  . ARG D 84  ? 0.6546 0.3452 0.3509 0.0464  0.0423  -0.0757 385 ARG D CG  
10865 C CD  . ARG D 84  ? 0.6674 0.3815 0.3750 0.0387  0.0439  -0.0770 385 ARG D CD  
10866 N NE  . ARG D 84  ? 0.6698 0.4148 0.4048 0.0237  0.0405  -0.0710 385 ARG D NE  
10867 C CZ  . ARG D 84  ? 0.7250 0.4708 0.4580 0.0045  0.0367  -0.0695 385 ARG D CZ  
10868 N NH1 . ARG D 84  ? 0.8074 0.5254 0.5122 -0.0041 0.0357  -0.0737 385 ARG D NH1 
10869 N NH2 . ARG D 84  ? 0.5804 0.3556 0.3392 -0.0058 0.0339  -0.0640 385 ARG D NH2 
10870 N N   . LEU D 85  ? 0.7916 0.3471 0.3838 0.0418  0.0376  -0.0823 386 LEU D N   
10871 C CA  . LEU D 85  ? 0.7807 0.3081 0.3540 0.0233  0.0330  -0.0794 386 LEU D CA  
10872 C C   . LEU D 85  ? 0.8339 0.3307 0.3763 0.0043  0.0312  -0.0830 386 LEU D C   
10873 O O   . LEU D 85  ? 0.8070 0.3073 0.3509 -0.0197 0.0273  -0.0800 386 LEU D O   
10874 C CB  . LEU D 85  ? 0.8694 0.3641 0.4219 0.0372  0.0325  -0.0783 386 LEU D CB  
10875 C CG  . LEU D 85  ? 0.8351 0.3586 0.4165 0.0518  0.0329  -0.0743 386 LEU D CG  
10876 C CD1 . LEU D 85  ? 0.8581 0.3509 0.4191 0.0647  0.0314  -0.0719 386 LEU D CD1 
10877 C CD2 . LEU D 85  ? 0.7857 0.3439 0.3982 0.0330  0.0301  -0.0679 386 LEU D CD2 
10878 N N   . GLU D 86  ? 0.8946 0.3746 0.4188 0.0144  0.0334  -0.0861 387 GLU D N   
10879 C CA  . GLU D 86  ? 0.9394 0.3984 0.4401 -0.0029 0.0313  -0.0873 387 GLU D CA  
10880 C C   . GLU D 86  ? 0.8959 0.3816 0.4116 -0.0206 0.0301  -0.0894 387 GLU D C   
10881 O O   . GLU D 86  ? 0.8522 0.3314 0.3581 -0.0442 0.0259  -0.0880 387 GLU D O   
10882 C CB  . GLU D 86  ? 1.0470 0.4858 0.5275 0.0141  0.0346  -0.0907 387 GLU D CB  
10883 C CG  . GLU D 86  ? 1.2341 0.6367 0.6887 0.0259  0.0341  -0.0883 387 GLU D CG  
10884 C CD  . GLU D 86  ? 1.3864 0.7539 0.8110 0.0040  0.0297  -0.0850 387 GLU D CD  
10885 O OE1 . GLU D 86  ? 1.3839 0.7439 0.8067 -0.0047 0.0268  -0.0802 387 GLU D OE1 
10886 O OE2 . GLU D 86  ? 1.4664 0.8146 0.8689 -0.0052 0.0293  -0.0870 387 GLU D OE2 
10887 N N   . GLU D 87  ? 0.8336 0.3518 0.3733 -0.0094 0.0337  -0.0920 388 GLU D N   
10888 C CA  . GLU D 87  ? 0.7791 0.3340 0.3422 -0.0239 0.0320  -0.0903 388 GLU D CA  
10889 C C   . GLU D 87  ? 0.8018 0.3813 0.3878 -0.0434 0.0268  -0.0833 388 GLU D C   
10890 O O   . GLU D 87  ? 0.7864 0.3721 0.3709 -0.0645 0.0226  -0.0823 388 GLU D O   
10891 C CB  . GLU D 87  ? 0.7613 0.3548 0.3543 -0.0065 0.0368  -0.0903 388 GLU D CB  
10892 C CG  . GLU D 87  ? 0.8961 0.5249 0.5105 -0.0180 0.0356  -0.0888 388 GLU D CG  
10893 C CD  . GLU D 87  ? 1.0320 0.6916 0.6685 -0.0010 0.0412  -0.0896 388 GLU D CD  
10894 O OE1 . GLU D 87  ? 0.9071 0.5771 0.5574 0.0166  0.0446  -0.0887 388 GLU D OE1 
10895 O OE2 . GLU D 87  ? 1.0914 0.7649 0.7305 -0.0059 0.0420  -0.0911 388 GLU D OE2 
10896 N N   . VAL D 88  ? 0.7279 0.3226 0.3349 -0.0363 0.0270  -0.0784 389 VAL D N   
10897 C CA  . VAL D 88  ? 0.7075 0.3255 0.3357 -0.0529 0.0229  -0.0720 389 VAL D CA  
10898 C C   . VAL D 88  ? 0.7150 0.3010 0.3145 -0.0742 0.0189  -0.0720 389 VAL D C   
10899 O O   . VAL D 88  ? 0.6848 0.2888 0.2937 -0.0950 0.0149  -0.0689 389 VAL D O   
10900 C CB  . VAL D 88  ? 0.7297 0.3643 0.3807 -0.0399 0.0244  -0.0675 389 VAL D CB  
10901 C CG1 . VAL D 88  ? 0.6670 0.3190 0.3342 -0.0565 0.0208  -0.0614 389 VAL D CG1 
10902 C CG2 . VAL D 88  ? 0.6781 0.3500 0.3599 -0.0238 0.0277  -0.0670 389 VAL D CG2 
10903 N N   . ASN D 89  ? 0.7240 0.2619 0.2867 -0.0694 0.0198  -0.0756 390 ASN D N   
10904 C CA  . ASN D 89  ? 0.8348 0.3350 0.3636 -0.0903 0.0162  -0.0762 390 ASN D CA  
10905 C C   . ASN D 89  ? 0.9330 0.4395 0.4557 -0.1107 0.0129  -0.0772 390 ASN D C   
10906 O O   . ASN D 89  ? 0.8542 0.3686 0.3780 -0.1341 0.0087  -0.0735 390 ASN D O   
10907 C CB  . ASN D 89  ? 0.9631 0.4229 0.4626 -0.0755 0.0182  -0.0760 390 ASN D CB  
10908 C CG  . ASN D 89  ? 1.2807 0.7146 0.7595 -0.0898 0.0154  -0.0707 390 ASN D CG  
10909 O OD1 . ASN D 89  ? 1.2830 0.7192 0.7566 -0.1145 0.0121  -0.0683 390 ASN D OD1 
10910 N ND2 . ASN D 89  ? 1.4602 0.8713 0.9269 -0.0743 0.0168  -0.0685 390 ASN D ND2 
10911 N N   . LYS D 90  ? 0.8405 0.3455 0.3570 -0.1021 0.0148  -0.0818 391 LYS D N   
10912 C CA  . LYS D 90  ? 0.8278 0.3370 0.3366 -0.1209 0.0113  -0.0824 391 LYS D CA  
10913 C C   . LYS D 90  ? 0.8115 0.3647 0.3495 -0.1337 0.0080  -0.0816 391 LYS D C   
10914 O O   . LYS D 90  ? 0.8855 0.4490 0.4224 -0.1555 0.0030  -0.0798 391 LYS D O   
10915 C CB  . LYS D 90  ? 1.0392 0.5316 0.5306 -0.1081 0.0144  -0.0873 391 LYS D CB  
10916 C CG  . LYS D 90  ? 1.1807 0.6979 0.6916 -0.0900 0.0186  -0.0915 391 LYS D CG  
10917 C CD  . LYS D 90  ? 1.2693 0.7864 0.7705 -0.0901 0.0195  -0.0955 391 LYS D CD  
10918 C CE  . LYS D 90  ? 1.1981 0.7527 0.7250 -0.0831 0.0217  -0.0975 391 LYS D CE  
10919 N NZ  . LYS D 90  ? 1.0321 0.6287 0.5916 -0.0997 0.0163  -0.0905 391 LYS D NZ  
10920 N N   . GLU D 91  ? 0.8042 0.3959 0.3792 -0.1173 0.0109  -0.0783 392 GLU D N   
10921 C CA  . GLU D 91  ? 0.7571 0.3989 0.3690 -0.1252 0.0081  -0.0731 392 GLU D CA  
10922 C C   . GLU D 91  ? 0.7598 0.4146 0.3810 -0.1447 0.0036  -0.0678 392 GLU D C   
10923 O O   . GLU D 91  ? 0.7492 0.4283 0.3804 -0.1621 -0.0011 -0.0655 392 GLU D O   
10924 C CB  . GLU D 91  ? 0.6935 0.3683 0.3397 -0.1046 0.0121  -0.0703 392 GLU D CB  
10925 C CG  . GLU D 91  ? 0.7208 0.4059 0.3716 -0.0913 0.0155  -0.0736 392 GLU D CG  
10926 C CD  . GLU D 91  ? 0.8764 0.5986 0.5631 -0.0762 0.0186  -0.0698 392 GLU D CD  
10927 O OE1 . GLU D 91  ? 0.9624 0.7196 0.6754 -0.0832 0.0158  -0.0649 392 GLU D OE1 
10928 O OE2 . GLU D 91  ? 0.9671 0.6835 0.6551 -0.0574 0.0236  -0.0715 392 GLU D OE2 
10929 N N   . ILE D 92  ? 0.7861 0.4268 0.4044 -0.1415 0.0052  -0.0656 393 ILE D N   
10930 C CA  . ILE D 92  ? 0.7991 0.4506 0.4241 -0.1602 0.0020  -0.0607 393 ILE D CA  
10931 C C   . ILE D 92  ? 0.8301 0.4548 0.4226 -0.1851 -0.0023 -0.0630 393 ILE D C   
10932 O O   . ILE D 92  ? 0.8294 0.4789 0.4323 -0.2057 -0.0067 -0.0599 393 ILE D O   
10933 C CB  . ILE D 92  ? 0.7708 0.4093 0.3966 -0.1504 0.0049  -0.0580 393 ILE D CB  
10934 C CG1 . ILE D 92  ? 0.7030 0.3768 0.3657 -0.1301 0.0080  -0.0548 393 ILE D CG1 
10935 C CG2 . ILE D 92  ? 0.8432 0.4833 0.4666 -0.1718 0.0023  -0.0537 393 ILE D CG2 
10936 C CD1 . ILE D 92  ? 0.7157 0.3767 0.3788 -0.1162 0.0110  -0.0529 393 ILE D CD1 
10937 N N   . ASP D 93  ? 0.8793 0.4560 0.4334 -0.1825 -0.0011 -0.0681 394 ASP D N   
10938 C CA  . ASP D 93  ? 0.9887 0.5481 0.5190 -0.2004 -0.0039 -0.0662 394 ASP D CA  
10939 C C   . ASP D 93  ? 1.0207 0.6094 0.5614 -0.2156 -0.0084 -0.0664 394 ASP D C   
10940 O O   . ASP D 93  ? 1.1247 0.7200 0.6599 -0.2367 -0.0121 -0.0628 394 ASP D O   
10941 C CB  . ASP D 93  ? 1.1311 0.6441 0.6269 -0.1877 -0.0008 -0.0693 394 ASP D CB  
10942 C CG  . ASP D 93  ? 1.2656 0.7449 0.7417 -0.1815 0.0016  -0.0668 394 ASP D CG  
10943 O OD1 . ASP D 93  ? 1.2679 0.7535 0.7471 -0.1963 -0.0001 -0.0618 394 ASP D OD1 
10944 O OD2 . ASP D 93  ? 1.3503 0.7987 0.8079 -0.1613 0.0051  -0.0694 394 ASP D OD2 
10945 N N   . THR D 94  ? 0.8732 0.4806 0.4282 -0.2051 -0.0083 -0.0703 395 THR D N   
10946 C CA  . THR D 94  ? 0.9544 0.5851 0.5151 -0.2169 -0.0128 -0.0705 395 THR D CA  
10947 C C   . THR D 94  ? 0.9779 0.6605 0.5752 -0.2221 -0.0165 -0.0676 395 THR D C   
10948 O O   . THR D 94  ? 1.0204 0.7268 0.6240 -0.2354 -0.0217 -0.0664 395 THR D O   
10949 C CB  . THR D 94  ? 0.9537 0.5666 0.4993 -0.2024 -0.0101 -0.0763 395 THR D CB  
10950 O OG1 . THR D 94  ? 1.0652 0.6837 0.6241 -0.1800 -0.0052 -0.0793 395 THR D OG1 
10951 C CG2 . THR D 94  ? 0.9886 0.5535 0.4981 -0.1991 -0.0073 -0.0780 395 THR D CG2 
10952 N N   . THR D 95  ? 0.8757 0.5832 0.5040 -0.2070 -0.0130 -0.0631 396 THR D N   
10953 C CA  . THR D 95  ? 0.7639 0.5245 0.4325 -0.2058 -0.0151 -0.0572 396 THR D CA  
10954 C C   . THR D 95  ? 0.7519 0.5336 0.4433 -0.2069 -0.0140 -0.0515 396 THR D C   
10955 O O   . THR D 95  ? 0.8242 0.6485 0.5487 -0.2037 -0.0151 -0.0467 396 THR D O   
10956 C CB  . THR D 95  ? 0.7046 0.4825 0.3932 -0.1831 -0.0115 -0.0573 396 THR D CB  
10957 O OG1 . THR D 95  ? 0.7495 0.5198 0.4466 -0.1640 -0.0055 -0.0567 396 THR D OG1 
10958 C CG2 . THR D 95  ? 0.6951 0.4493 0.3595 -0.1793 -0.0109 -0.0634 396 THR D CG2 
10959 N N   . SER D 96  ? 0.6666 0.4183 0.3401 -0.2102 -0.0118 -0.0520 397 SER D N   
10960 C CA  . SER D 96  ? 0.7037 0.4724 0.3960 -0.2113 -0.0102 -0.0467 397 SER D CA  
10961 C C   . SER D 96  ? 0.7134 0.5005 0.4334 -0.1871 -0.0057 -0.0443 397 SER D C   
10962 O O   . SER D 96  ? 0.7124 0.5129 0.4486 -0.1846 -0.0038 -0.0402 397 SER D O   
10963 C CB  . SER D 96  ? 0.7405 0.5501 0.4530 -0.2304 -0.0147 -0.0421 397 SER D CB  
10964 O OG  . SER D 96  ? 0.8044 0.5950 0.4908 -0.2556 -0.0180 -0.0432 397 SER D OG  
10965 N N   . THR D 97  ? 0.6833 0.4710 0.4078 -0.1700 -0.0037 -0.0468 398 THR D N   
10966 C CA  . THR D 97  ? 0.6197 0.4229 0.3680 -0.1484 0.0005  -0.0449 398 THR D CA  
10967 C C   . THR D 97  ? 0.5502 0.3295 0.2842 -0.1316 0.0041  -0.0499 398 THR D C   
10968 O O   . THR D 97  ? 0.5971 0.3431 0.3006 -0.1354 0.0039  -0.0549 398 THR D O   
10969 C CB  . THR D 97  ? 0.5393 0.3891 0.3217 -0.1464 -0.0012 -0.0404 398 THR D CB  
10970 O OG1 . THR D 97  ? 0.5498 0.4131 0.3538 -0.1280 0.0028  -0.0381 398 THR D OG1 
10971 C CG2 . THR D 97  ? 0.5499 0.4083 0.3306 -0.1474 -0.0037 -0.0425 398 THR D CG2 
10972 N N   . TYR D 98  ? 0.5647 0.3603 0.3194 -0.1128 0.0077  -0.0488 399 TYR D N   
10973 C CA  . TYR D 98  ? 0.6310 0.4118 0.3764 -0.0964 0.0116  -0.0533 399 TYR D CA  
10974 C C   . TYR D 98  ? 0.5653 0.3798 0.3407 -0.0833 0.0137  -0.0508 399 TYR D C   
10975 O O   . TYR D 98  ? 0.4893 0.3319 0.2897 -0.0847 0.0126  -0.0457 399 TYR D O   
10976 C CB  . TYR D 98  ? 0.6039 0.3506 0.3297 -0.0847 0.0150  -0.0562 399 TYR D CB  
10977 C CG  . TYR D 98  ? 0.5837 0.3431 0.3296 -0.0731 0.0172  -0.0523 399 TYR D CG  
10978 C CD1 . TYR D 98  ? 0.4981 0.2644 0.2548 -0.0531 0.0212  -0.0533 399 TYR D CD1 
10979 C CD2 . TYR D 98  ? 0.5024 0.2681 0.2560 -0.0828 0.0152  -0.0478 399 TYR D CD2 
10980 C CE1 . TYR D 98  ? 0.5323 0.3101 0.3061 -0.0434 0.0225  -0.0500 399 TYR D CE1 
10981 C CE2 . TYR D 98  ? 0.5687 0.3446 0.3387 -0.0725 0.0170  -0.0445 399 TYR D CE2 
10982 C CZ  . TYR D 98  ? 0.5833 0.3645 0.3629 -0.0530 0.0203  -0.0456 399 TYR D CZ  
10983 O OH  . TYR D 98  ? 0.6219 0.4136 0.4171 -0.0436 0.0215  -0.0424 399 TYR D OH  
10984 N N   . GLN D 99  ? 0.5456 0.3561 0.3169 -0.0709 0.0172  -0.0544 400 GLN D N   
10985 C CA  . GLN D 99  ? 0.5122 0.3524 0.3077 -0.0610 0.0193  -0.0523 400 GLN D CA  
10986 C C   . GLN D 99  ? 0.5452 0.3822 0.3451 -0.0424 0.0246  -0.0539 400 GLN D C   
10987 O O   . GLN D 99  ? 0.5328 0.3451 0.3124 -0.0339 0.0277  -0.0588 400 GLN D O   
10988 C CB  . GLN D 99  ? 0.5047 0.3495 0.2939 -0.0642 0.0188  -0.0547 400 GLN D CB  
10989 C CG  . GLN D 99  ? 0.5659 0.4175 0.3516 -0.0824 0.0126  -0.0530 400 GLN D CG  
10990 C CD  . GLN D 99  ? 0.6234 0.5064 0.4356 -0.0882 0.0090  -0.0465 400 GLN D CD  
10991 O OE1 . GLN D 99  ? 0.6144 0.5202 0.4486 -0.0794 0.0106  -0.0431 400 GLN D OE1 
10992 N NE2 . GLN D 99  ? 0.6303 0.5141 0.4392 -0.1032 0.0044  -0.0447 400 GLN D NE2 
10993 N N   . LEU D 100 ? 0.5029 0.3652 0.3285 -0.0358 0.0256  -0.0497 401 LEU D N   
10994 C CA  . LEU D 100 ? 0.5173 0.3828 0.3503 -0.0192 0.0302  -0.0508 401 LEU D CA  
10995 C C   . LEU D 100 ? 0.4854 0.3585 0.3179 -0.0112 0.0341  -0.0539 401 LEU D C   
10996 O O   . LEU D 100 ? 0.4980 0.3868 0.3373 -0.0173 0.0333  -0.0527 401 LEU D O   
10997 C CB  . LEU D 100 ? 0.4520 0.3426 0.3113 -0.0165 0.0298  -0.0455 401 LEU D CB  
10998 C CG  . LEU D 100 ? 0.4525 0.3386 0.3141 -0.0233 0.0268  -0.0421 401 LEU D CG  
10999 C CD1 . LEU D 100 ? 0.3828 0.2934 0.2692 -0.0197 0.0268  -0.0375 401 LEU D CD1 
11000 C CD2 . LEU D 100 ? 0.4661 0.3234 0.3084 -0.0176 0.0277  -0.0448 401 LEU D CD2 
11001 N N   . LYS D 101 ? 0.4475 0.3102 0.2717 0.0030  0.0385  -0.0579 402 LYS D N   
11002 C CA  . LYS D 101 ? 0.4095 0.2875 0.2398 0.0126  0.0435  -0.0601 402 LYS D CA  
11003 C C   . LYS D 101 ? 0.4184 0.3289 0.2771 0.0139  0.0440  -0.0553 402 LYS D C   
11004 O O   . LYS D 101 ? 0.3933 0.3110 0.2654 0.0132  0.0416  -0.0514 402 LYS D O   
11005 C CB  . LYS D 101 ? 0.5010 0.3649 0.3189 0.0293  0.0481  -0.0651 402 LYS D CB  
11006 C CG  . LYS D 101 ? 0.6018 0.4296 0.3877 0.0297  0.0483  -0.0704 402 LYS D CG  
11007 C CD  . LYS D 101 ? 0.6440 0.4692 0.4181 0.0218  0.0491  -0.0733 402 LYS D CD  
11008 C CE  . LYS D 101 ? 0.8788 0.6677 0.6186 0.0257  0.0510  -0.0801 402 LYS D CE  
11009 N NZ  . LYS D 101 ? 0.9321 0.6944 0.6518 0.0094  0.0453  -0.0801 402 LYS D NZ  
11010 N N   . ASP D 102 ? 0.4222 0.3505 0.2880 0.0154  0.0472  -0.0557 403 ASP D N   
11011 C CA  . ASP D 102 ? 0.4276 0.3838 0.3167 0.0156  0.0479  -0.0513 403 ASP D CA  
11012 C C   . ASP D 102 ? 0.4161 0.3809 0.3175 0.0259  0.0494  -0.0506 403 ASP D C   
11013 O O   . ASP D 102 ? 0.3513 0.3296 0.2691 0.0231  0.0472  -0.0461 403 ASP D O   
11014 C CB  . ASP D 102 ? 0.5359 0.5064 0.4263 0.0165  0.0523  -0.0527 403 ASP D CB  
11015 C CG  . ASP D 102 ? 0.7238 0.6881 0.6029 0.0061  0.0502  -0.0527 403 ASP D CG  
11016 O OD1 . ASP D 102 ? 0.8078 0.7560 0.6766 -0.0013 0.0456  -0.0527 403 ASP D OD1 
11017 O OD2 . ASP D 102 ? 0.7714 0.7475 0.6516 0.0045  0.0531  -0.0526 403 ASP D OD2 
11018 N N   . THR D 103 ? 0.4287 0.3861 0.3215 0.0387  0.0531  -0.0550 404 THR D N   
11019 C CA  . THR D 103 ? 0.4538 0.4190 0.3565 0.0498  0.0539  -0.0545 404 THR D CA  
11020 C C   . THR D 103 ? 0.4167 0.3691 0.3197 0.0465  0.0488  -0.0514 404 THR D C   
11021 O O   . THR D 103 ? 0.4266 0.3924 0.3447 0.0487  0.0475  -0.0482 404 THR D O   
11022 C CB  . THR D 103 ? 0.5099 0.4650 0.3992 0.0655  0.0581  -0.0601 404 THR D CB  
11023 O OG1 . THR D 103 ? 0.5691 0.4904 0.4332 0.0647  0.0566  -0.0633 404 THR D OG1 
11024 C CG2 . THR D 103 ? 0.5358 0.5082 0.4269 0.0701  0.0642  -0.0633 404 THR D CG2 
11025 N N   . GLU D 104 ? 0.4058 0.3323 0.2911 0.0404  0.0461  -0.0524 405 GLU D N   
11026 C CA  . GLU D 104 ? 0.4298 0.3436 0.3134 0.0357  0.0418  -0.0494 405 GLU D CA  
11027 C C   . GLU D 104 ? 0.4120 0.3440 0.3139 0.0244  0.0388  -0.0440 405 GLU D C   
11028 O O   . GLU D 104 ? 0.3729 0.3093 0.2844 0.0246  0.0369  -0.0408 405 GLU D O   
11029 C CB  . GLU D 104 ? 0.4467 0.3288 0.3052 0.0295  0.0399  -0.0519 405 GLU D CB  
11030 C CG  . GLU D 104 ? 0.5144 0.3726 0.3503 0.0418  0.0429  -0.0575 405 GLU D CG  
11031 C CD  . GLU D 104 ? 0.5343 0.3597 0.3424 0.0332  0.0412  -0.0605 405 GLU D CD  
11032 O OE1 . GLU D 104 ? 0.5623 0.3608 0.3471 0.0428  0.0430  -0.0650 405 GLU D OE1 
11033 O OE2 . GLU D 104 ? 0.5657 0.3919 0.3742 0.0169  0.0379  -0.0583 405 GLU D OE2 
11034 N N   . LEU D 105 ? 0.3836 0.3252 0.2890 0.0152  0.0384  -0.0431 406 LEU D N   
11035 C CA  . LEU D 105 ? 0.3740 0.3330 0.2956 0.0065  0.0358  -0.0381 406 LEU D CA  
11036 C C   . LEU D 105 ? 0.3899 0.3687 0.3296 0.0124  0.0372  -0.0357 406 LEU D C   
11037 O O   . LEU D 105 ? 0.3892 0.3743 0.3395 0.0099  0.0350  -0.0320 406 LEU D O   
11038 C CB  . LEU D 105 ? 0.3985 0.3648 0.3193 -0.0014 0.0352  -0.0377 406 LEU D CB  
11039 C CG  . LEU D 105 ? 0.3451 0.3271 0.2798 -0.0092 0.0321  -0.0325 406 LEU D CG  
11040 C CD1 . LEU D 105 ? 0.5078 0.4828 0.4403 -0.0169 0.0281  -0.0305 406 LEU D CD1 
11041 C CD2 . LEU D 105 ? 0.3761 0.3659 0.3092 -0.0142 0.0318  -0.0321 406 LEU D CD2 
11042 N N   . ILE D 106 ? 0.3465 0.3358 0.2894 0.0197  0.0410  -0.0378 407 ILE D N   
11043 C CA  . ILE D 106 ? 0.2842 0.2936 0.2436 0.0233  0.0421  -0.0356 407 ILE D CA  
11044 C C   . ILE D 106 ? 0.3774 0.3834 0.3399 0.0301  0.0407  -0.0351 407 ILE D C   
11045 O O   . ILE D 106 ? 0.3855 0.3999 0.3592 0.0276  0.0387  -0.0316 407 ILE D O   
11046 C CB  . ILE D 106 ? 0.3176 0.3411 0.2792 0.0288  0.0469  -0.0383 407 ILE D CB  
11047 C CG1 . ILE D 106 ? 0.3096 0.3376 0.2688 0.0205  0.0479  -0.0377 407 ILE D CG1 
11048 C CG2 . ILE D 106 ? 0.2633 0.3074 0.2406 0.0325  0.0479  -0.0365 407 ILE D CG2 
11049 C CD1 . ILE D 106 ? 0.3346 0.3726 0.2911 0.0250  0.0534  -0.0411 407 ILE D CD1 
11050 N N   . TYR D 107 ? 0.3836 0.3753 0.3343 0.0392  0.0417  -0.0385 408 TYR D N   
11051 C CA  . TYR D 107 ? 0.3980 0.3826 0.3480 0.0465  0.0398  -0.0379 408 TYR D CA  
11052 C C   . TYR D 107 ? 0.3473 0.3236 0.2984 0.0377  0.0360  -0.0341 408 TYR D C   
11053 O O   . TYR D 107 ? 0.3484 0.3316 0.3087 0.0391  0.0343  -0.0314 408 TYR D O   
11054 C CB  . TYR D 107 ? 0.4068 0.3692 0.3378 0.0566  0.0409  -0.0421 408 TYR D CB  
11055 C CG  . TYR D 107 ? 0.3868 0.3359 0.3125 0.0635  0.0382  -0.0410 408 TYR D CG  
11056 C CD1 . TYR D 107 ? 0.3535 0.3162 0.2880 0.0755  0.0383  -0.0409 408 TYR D CD1 
11057 C CD2 . TYR D 107 ? 0.4730 0.3971 0.3846 0.0570  0.0354  -0.0398 408 TYR D CD2 
11058 C CE1 . TYR D 107 ? 0.3781 0.3279 0.3064 0.0822  0.0354  -0.0396 408 TYR D CE1 
11059 C CE2 . TYR D 107 ? 0.5180 0.4283 0.4229 0.0626  0.0330  -0.0384 408 TYR D CE2 
11060 C CZ  . TYR D 107 ? 0.5141 0.4365 0.4270 0.0757  0.0328  -0.0382 408 TYR D CZ  
11061 O OH  . TYR D 107 ? 0.6090 0.5167 0.5138 0.0818  0.0299  -0.0365 408 TYR D OH  
11062 N N   . GLY D 108 ? 0.3452 0.3078 0.2866 0.0283  0.0346  -0.0339 409 GLY D N   
11063 C CA  . GLY D 108 ? 0.3261 0.2822 0.2676 0.0200  0.0316  -0.0306 409 GLY D CA  
11064 C C   . GLY D 108 ? 0.4182 0.3941 0.3774 0.0148  0.0306  -0.0265 409 GLY D C   
11065 O O   . GLY D 108 ? 0.2987 0.2751 0.2627 0.0138  0.0291  -0.0238 409 GLY D O   
11066 N N   . ALA D 109 ? 0.2903 0.2808 0.2574 0.0115  0.0316  -0.0260 410 ALA D N   
11067 C CA  . ALA D 109 ? 0.2927 0.2986 0.2735 0.0076  0.0307  -0.0222 410 ALA D CA  
11068 C C   . ALA D 109 ? 0.2773 0.2925 0.2674 0.0135  0.0312  -0.0213 410 ALA D C   
11069 O O   . ALA D 109 ? 0.3327 0.3511 0.3292 0.0117  0.0297  -0.0185 410 ALA D O   
11070 C CB  . ALA D 109 ? 0.2361 0.2524 0.2201 0.0037  0.0316  -0.0218 410 ALA D CB  
11071 N N   . LYS D 110 ? 0.2681 0.2890 0.2590 0.0206  0.0333  -0.0238 411 LYS D N   
11072 C CA  . LYS D 110 ? 0.3299 0.3620 0.3297 0.0257  0.0331  -0.0231 411 LYS D CA  
11073 C C   . LYS D 110 ? 0.3395 0.3610 0.3361 0.0292  0.0307  -0.0222 411 LYS D C   
11074 O O   . LYS D 110 ? 0.2693 0.2972 0.2730 0.0286  0.0292  -0.0199 411 LYS D O   
11075 C CB  . LYS D 110 ? 0.2622 0.3049 0.2635 0.0335  0.0358  -0.0262 411 LYS D CB  
11076 C CG  . LYS D 110 ? 0.2605 0.3175 0.2666 0.0289  0.0386  -0.0265 411 LYS D CG  
11077 C CD  . LYS D 110 ? 0.2115 0.2828 0.2202 0.0364  0.0420  -0.0296 411 LYS D CD  
11078 C CE  . LYS D 110 ? 0.2548 0.3400 0.2669 0.0301  0.0453  -0.0295 411 LYS D CE  
11079 N NZ  . LYS D 110 ? 0.3113 0.4155 0.3283 0.0369  0.0491  -0.0324 411 LYS D NZ  
11080 N N   . HIS D 111 ? 0.3187 0.3220 0.3025 0.0320  0.0303  -0.0238 412 HIS D N   
11081 C CA  . HIS D 111 ? 0.2864 0.2778 0.2650 0.0351  0.0281  -0.0226 412 HIS D CA  
11082 C C   . HIS D 111 ? 0.3401 0.3273 0.3198 0.0260  0.0266  -0.0193 412 HIS D C   
11083 O O   . HIS D 111 ? 0.3004 0.2857 0.2812 0.0272  0.0251  -0.0174 412 HIS D O   
11084 C CB  . HIS D 111 ? 0.3403 0.3103 0.3018 0.0415  0.0282  -0.0253 412 HIS D CB  
11085 C CG  . HIS D 111 ? 0.3392 0.3143 0.3007 0.0550  0.0288  -0.0277 412 HIS D CG  
11086 N ND1 . HIS D 111 ? 0.3345 0.3247 0.3017 0.0597  0.0316  -0.0304 412 HIS D ND1 
11087 C CD2 . HIS D 111 ? 0.3374 0.3085 0.2958 0.0650  0.0268  -0.0274 412 HIS D CD2 
11088 C CE1 . HIS D 111 ? 0.3901 0.3870 0.3585 0.0725  0.0316  -0.0319 412 HIS D CE1 
11089 N NE2 . HIS D 111 ? 0.3844 0.3695 0.3473 0.0763  0.0284  -0.0301 412 HIS D NE2 
11090 N N   . ALA D 112 ? 0.2800 0.2672 0.2595 0.0174  0.0270  -0.0187 413 ALA D N   
11091 C CA  . ALA D 112 ? 0.2684 0.2576 0.2519 0.0099  0.0261  -0.0155 413 ALA D CA  
11092 C C   . ALA D 112 ? 0.2875 0.2905 0.2830 0.0111  0.0259  -0.0133 413 ALA D C   
11093 O O   . ALA D 112 ? 0.2528 0.2542 0.2494 0.0099  0.0251  -0.0111 413 ALA D O   
11094 C CB  . ALA D 112 ? 0.2783 0.2709 0.2621 0.0019  0.0262  -0.0150 413 ALA D CB  
11095 N N   . TRP D 113 ? 0.2725 0.2880 0.2754 0.0128  0.0267  -0.0138 414 TRP D N   
11096 C CA  . TRP D 113 ? 0.2596 0.2855 0.2710 0.0130  0.0263  -0.0120 414 TRP D CA  
11097 C C   . TRP D 113 ? 0.2618 0.2870 0.2732 0.0186  0.0250  -0.0123 414 TRP D C   
11098 O O   . TRP D 113 ? 0.2526 0.2780 0.2660 0.0176  0.0238  -0.0104 414 TRP D O   
11099 C CB  . TRP D 113 ? 0.2048 0.2429 0.2217 0.0120  0.0275  -0.0126 414 TRP D CB  
11100 C CG  . TRP D 113 ? 0.1998 0.2462 0.2228 0.0101  0.0270  -0.0108 414 TRP D CG  
11101 C CD1 . TRP D 113 ? 0.2314 0.2748 0.2551 0.0092  0.0257  -0.0089 414 TRP D CD1 
11102 C CD2 . TRP D 113 ? 0.1885 0.2458 0.2155 0.0077  0.0280  -0.0108 414 TRP D CD2 
11103 N NE1 . TRP D 113 ? 0.2245 0.2746 0.2513 0.0065  0.0254  -0.0080 414 TRP D NE1 
11104 C CE2 . TRP D 113 ? 0.2472 0.3059 0.2760 0.0049  0.0268  -0.0090 414 TRP D CE2 
11105 C CE3 . TRP D 113 ? 0.2187 0.2838 0.2463 0.0068  0.0301  -0.0123 414 TRP D CE3 
11106 C CZ2 . TRP D 113 ? 0.1944 0.2611 0.2251 0.0002  0.0273  -0.0084 414 TRP D CZ2 
11107 C CZ3 . TRP D 113 ? 0.2843 0.3595 0.3150 0.0023  0.0309  -0.0116 414 TRP D CZ3 
11108 C CH2 . TRP D 113 ? 0.2835 0.3588 0.3152 -0.0014 0.0293  -0.0096 414 TRP D CH2 
11109 N N   . ARG D 114 ? 0.3325 0.3566 0.3408 0.0254  0.0250  -0.0147 415 ARG D N   
11110 C CA  . ARG D 114 ? 0.3091 0.3336 0.3170 0.0323  0.0231  -0.0148 415 ARG D CA  
11111 C C   . ARG D 114 ? 0.3245 0.3341 0.3248 0.0317  0.0214  -0.0130 415 ARG D C   
11112 O O   . ARG D 114 ? 0.2966 0.3076 0.2978 0.0343  0.0193  -0.0118 415 ARG D O   
11113 C CB  . ARG D 114 ? 0.2869 0.3105 0.2904 0.0416  0.0236  -0.0178 415 ARG D CB  
11114 C CG  . ARG D 114 ? 0.2918 0.3219 0.2972 0.0507  0.0213  -0.0180 415 ARG D CG  
11115 C CD  . ARG D 114 ? 0.2888 0.3126 0.2861 0.0623  0.0218  -0.0209 415 ARG D CD  
11116 N NE  . ARG D 114 ? 0.2802 0.3178 0.2827 0.0724  0.0196  -0.0212 415 ARG D NE  
11117 C CZ  . ARG D 114 ? 0.3177 0.3584 0.3171 0.0851  0.0200  -0.0238 415 ARG D CZ  
11118 N NH1 . ARG D 114 ? 0.2892 0.3468 0.2954 0.0942  0.0174  -0.0237 415 ARG D NH1 
11119 N NH2 . ARG D 114 ? 0.3080 0.3360 0.2974 0.0891  0.0230  -0.0266 415 ARG D NH2 
11120 N N   . ASN D 115 ? 0.2906 0.2863 0.2827 0.0272  0.0222  -0.0127 416 ASN D N   
11121 C CA  . ASN D 115 ? 0.3293 0.3102 0.3123 0.0251  0.0213  -0.0109 416 ASN D CA  
11122 C C   . ASN D 115 ? 0.3385 0.3240 0.3265 0.0178  0.0219  -0.0083 416 ASN D C   
11123 O O   . ASN D 115 ? 0.3244 0.3000 0.3057 0.0149  0.0218  -0.0067 416 ASN D O   
11124 C CB  . ASN D 115 ? 0.2577 0.2212 0.2276 0.0225  0.0220  -0.0121 416 ASN D CB  
11125 C CG  . ASN D 115 ? 0.2878 0.2409 0.2480 0.0316  0.0215  -0.0148 416 ASN D CG  
11126 O OD1 . ASN D 115 ? 0.3383 0.2964 0.3009 0.0409  0.0202  -0.0153 416 ASN D OD1 
11127 N ND2 . ASN D 115 ? 0.3599 0.2986 0.3083 0.0293  0.0225  -0.0167 416 ASN D ND2 
11128 N N   . ALA D 116 ? 0.2524 0.2518 0.2507 0.0151  0.0228  -0.0079 417 ALA D N   
11129 C CA  . ALA D 116 ? 0.2915 0.2947 0.2935 0.0099  0.0237  -0.0056 417 ALA D CA  
11130 C C   . ALA D 116 ? 0.2355 0.2382 0.2375 0.0118  0.0227  -0.0044 417 ALA D C   
11131 O O   . ALA D 116 ? 0.2473 0.2578 0.2545 0.0133  0.0218  -0.0045 417 ALA D O   
11132 C CB  . ALA D 116 ? 0.2049 0.2192 0.2146 0.0076  0.0246  -0.0055 417 ALA D CB  
11133 N N   . SER D 117 ? 0.2750 0.2681 0.2699 0.0108  0.0228  -0.0031 418 SER D N   
11134 C CA  A SER D 117 ? 0.2678 0.2583 0.2601 0.0130  0.0214  -0.0021 418 SER D CA  
11135 C CA  B SER D 117 ? 0.2701 0.2604 0.2623 0.0128  0.0215  -0.0021 418 SER D CA  
11136 C C   . SER D 117 ? 0.2942 0.2923 0.2919 0.0111  0.0223  -0.0013 418 SER D C   
11137 O O   . SER D 117 ? 0.3344 0.3329 0.3312 0.0128  0.0206  -0.0011 418 SER D O   
11138 C CB  A SER D 117 ? 0.2819 0.2594 0.2638 0.0111  0.0219  -0.0007 418 SER D CB  
11139 C CB  B SER D 117 ? 0.2740 0.2517 0.2560 0.0105  0.0222  -0.0006 418 SER D CB  
11140 O OG  A SER D 117 ? 0.2637 0.2438 0.2467 0.0051  0.0250  0.0006  418 SER D OG  
11141 O OG  B SER D 117 ? 0.2893 0.2551 0.2624 0.0116  0.0214  -0.0013 418 SER D OG  
11142 N N   . ARG D 118 ? 0.2427 0.2459 0.2445 0.0080  0.0247  -0.0007 419 ARG D N   
11143 C CA  . ARG D 118 ? 0.2719 0.2788 0.2759 0.0076  0.0258  0.0000  419 ARG D CA  
11144 C C   . ARG D 118 ? 0.3424 0.3546 0.3505 0.0080  0.0247  -0.0007 419 ARG D C   
11145 O O   . ARG D 118 ? 0.2553 0.2670 0.2623 0.0077  0.0254  -0.0001 419 ARG D O   
11146 C CB  . ARG D 118 ? 0.2399 0.2507 0.2458 0.0057  0.0287  0.0012  419 ARG D CB  
11147 C CG  . ARG D 118 ? 0.2744 0.2815 0.2756 0.0034  0.0305  0.0022  419 ARG D CG  
11148 C CD  . ARG D 118 ? 0.2640 0.2802 0.2693 0.0011  0.0333  0.0033  419 ARG D CD  
11149 N NE  . ARG D 118 ? 0.3184 0.3338 0.3195 -0.0016 0.0360  0.0045  419 ARG D NE  
11150 C CZ  . ARG D 118 ? 0.3799 0.4061 0.3846 -0.0045 0.0388  0.0056  419 ARG D CZ  
11151 N NH1 . ARG D 118 ? 0.3377 0.3755 0.3500 -0.0042 0.0386  0.0057  419 ARG D NH1 
11152 N NH2 . ARG D 118 ? 0.3585 0.3852 0.3590 -0.0079 0.0418  0.0067  419 ARG D NH2 
11153 N N   . CYS D 119 ? 0.2613 0.2779 0.2727 0.0085  0.0232  -0.0020 420 CYS D N   
11154 C CA  . CYS D 119 ? 0.2130 0.2359 0.2280 0.0071  0.0229  -0.0025 420 CYS D CA  
11155 C C   . CYS D 119 ? 0.1785 0.2049 0.1936 0.0071  0.0205  -0.0033 420 CYS D C   
11156 O O   . CYS D 119 ? 0.2130 0.2434 0.2299 0.0100  0.0189  -0.0044 420 CYS D O   
11157 C CB  . CYS D 119 ? 0.2295 0.2576 0.2481 0.0069  0.0235  -0.0035 420 CYS D CB  
11158 S SG  . CYS D 119 ? 0.2706 0.3069 0.2922 0.0042  0.0234  -0.0040 420 CYS D SG  
11159 N N   . VAL D 120 ? 0.2554 0.2804 0.2679 0.0040  0.0200  -0.0028 421 VAL D N   
11160 C CA  . VAL D 120 ? 0.2570 0.2871 0.2694 0.0017  0.0173  -0.0035 421 VAL D CA  
11161 C C   . VAL D 120 ? 0.2841 0.3263 0.3021 -0.0011 0.0171  -0.0044 421 VAL D C   
11162 O O   . VAL D 120 ? 0.2451 0.2970 0.2655 -0.0031 0.0148  -0.0051 421 VAL D O   
11163 C CB  . VAL D 120 ? 0.2830 0.3040 0.2873 -0.0022 0.0170  -0.0028 421 VAL D CB  
11164 C CG1 . VAL D 120 ? 0.2621 0.2791 0.2632 -0.0060 0.0186  -0.0022 421 VAL D CG1 
11165 C CG2 . VAL D 120 ? 0.3173 0.3424 0.3196 -0.0055 0.0134  -0.0035 421 VAL D CG2 
11166 N N   . GLY D 121 ? 0.3029 0.3464 0.3231 -0.0015 0.0194  -0.0043 422 GLY D N   
11167 C CA  . GLY D 121 ? 0.3137 0.3684 0.3379 -0.0049 0.0200  -0.0051 422 GLY D CA  
11168 C C   . GLY D 121 ? 0.3421 0.4082 0.3729 -0.0001 0.0204  -0.0069 422 GLY D C   
11169 O O   . GLY D 121 ? 0.2610 0.3372 0.2952 -0.0022 0.0219  -0.0078 422 GLY D O   
11170 N N   . ARG D 122 ? 0.3001 0.3636 0.3311 0.0065  0.0193  -0.0076 423 ARG D N   
11171 C CA  . ARG D 122 ? 0.2639 0.3322 0.2975 0.0126  0.0202  -0.0094 423 ARG D CA  
11172 C C   . ARG D 122 ? 0.3254 0.4114 0.3653 0.0153  0.0194  -0.0111 423 ARG D C   
11173 O O   . ARG D 122 ? 0.2488 0.3390 0.2899 0.0218  0.0206  -0.0130 423 ARG D O   
11174 C CB  . ARG D 122 ? 0.2426 0.2989 0.2712 0.0186  0.0192  -0.0094 423 ARG D CB  
11175 C CG  . ARG D 122 ? 0.2595 0.3025 0.2831 0.0164  0.0208  -0.0084 423 ARG D CG  
11176 C CD  . ARG D 122 ? 0.2350 0.2662 0.2521 0.0204  0.0198  -0.0082 423 ARG D CD  
11177 N NE  . ARG D 122 ? 0.2652 0.2923 0.2799 0.0196  0.0181  -0.0066 423 ARG D NE  
11178 C CZ  . ARG D 122 ? 0.2989 0.3164 0.3069 0.0230  0.0166  -0.0060 423 ARG D CZ  
11179 N NH1 . ARG D 122 ? 0.2431 0.2526 0.2454 0.0276  0.0164  -0.0069 423 ARG D NH1 
11180 N NH2 . ARG D 122 ? 0.2469 0.2606 0.2518 0.0216  0.0154  -0.0045 423 ARG D NH2 
11181 N N   . ILE D 123 ? 0.2074 0.3048 0.2508 0.0107  0.0176  -0.0106 424 ILE D N   
11182 C CA  . ILE D 123 ? 0.2543 0.3738 0.3056 0.0126  0.0173  -0.0122 424 ILE D CA  
11183 C C   . ILE D 123 ? 0.3191 0.4471 0.3733 0.0108  0.0214  -0.0135 424 ILE D C   
11184 O O   . ILE D 123 ? 0.1925 0.3376 0.2528 0.0160  0.0227  -0.0155 424 ILE D O   
11185 C CB  . ILE D 123 ? 0.2925 0.4245 0.3467 0.0049  0.0145  -0.0114 424 ILE D CB  
11186 C CG1 . ILE D 123 ? 0.2831 0.4415 0.3469 0.0095  0.0130  -0.0130 424 ILE D CG1 
11187 C CG2 . ILE D 123 ? 0.2665 0.3971 0.3180 -0.0075 0.0165  -0.0104 424 ILE D CG2 
11188 C CD1 . ILE D 123 ? 0.3547 0.5270 0.4214 0.0021  0.0090  -0.0122 424 ILE D CD1 
11189 N N   . GLN D 124 ? 0.2324 0.3484 0.2817 0.0049  0.0236  -0.0124 425 GLN D N   
11190 C CA  . GLN D 124 ? 0.3511 0.4718 0.4006 0.0020  0.0273  -0.0132 425 GLN D CA  
11191 C C   . GLN D 124 ? 0.3075 0.4204 0.3542 0.0095  0.0293  -0.0149 425 GLN D C   
11192 O O   . GLN D 124 ? 0.2778 0.3936 0.3234 0.0076  0.0324  -0.0157 425 GLN D O   
11193 C CB  . GLN D 124 ? 0.3310 0.4402 0.3742 -0.0074 0.0280  -0.0108 425 GLN D CB  
11194 C CG  . GLN D 124 ? 0.3879 0.5016 0.4301 -0.0170 0.0267  -0.0094 425 GLN D CG  
11195 C CD  . GLN D 124 ? 0.5056 0.6388 0.5519 -0.0232 0.0289  -0.0102 425 GLN D CD  
11196 O OE1 . GLN D 124 ? 0.5234 0.6604 0.5697 -0.0229 0.0323  -0.0109 425 GLN D OE1 
11197 N NE2 . GLN D 124 ? 0.4574 0.6040 0.5068 -0.0297 0.0272  -0.0101 425 GLN D NE2 
11198 N N   . TRP D 125 ? 0.2689 0.3707 0.3125 0.0171  0.0276  -0.0154 426 TRP D N   
11199 C CA  . TRP D 125 ? 0.2013 0.2884 0.2382 0.0205  0.0289  -0.0163 426 TRP D CA  
11200 C C   . TRP D 125 ? 0.2454 0.3387 0.2815 0.0241  0.0321  -0.0191 426 TRP D C   
11201 O O   . TRP D 125 ? 0.3686 0.4522 0.3989 0.0224  0.0336  -0.0196 426 TRP D O   
11202 C CB  . TRP D 125 ? 0.2585 0.3328 0.2904 0.0274  0.0267  -0.0165 426 TRP D CB  
11203 C CG  . TRP D 125 ? 0.2601 0.3418 0.2931 0.0376  0.0261  -0.0187 426 TRP D CG  
11204 C CD1 . TRP D 125 ? 0.2841 0.3775 0.3225 0.0412  0.0235  -0.0183 426 TRP D CD1 
11205 C CD2 . TRP D 125 ? 0.2392 0.3167 0.2666 0.0464  0.0279  -0.0216 426 TRP D CD2 
11206 N NE1 . TRP D 125 ? 0.3044 0.4031 0.3421 0.0528  0.0235  -0.0206 426 TRP D NE1 
11207 C CE2 . TRP D 125 ? 0.2782 0.3660 0.3084 0.0566  0.0264  -0.0228 426 TRP D CE2 
11208 C CE3 . TRP D 125 ? 0.2958 0.3614 0.3150 0.0468  0.0304  -0.0235 426 TRP D CE3 
11209 C CZ2 . TRP D 125 ? 0.2569 0.3422 0.2814 0.0687  0.0278  -0.0258 426 TRP D CZ2 
11210 C CZ3 . TRP D 125 ? 0.3361 0.3976 0.3485 0.0574  0.0318  -0.0268 426 TRP D CZ3 
11211 C CH2 . TRP D 125 ? 0.3206 0.3914 0.3355 0.0689  0.0307  -0.0279 426 TRP D CH2 
11212 N N   . SER D 126 ? 0.2901 0.4002 0.3317 0.0297  0.0333  -0.0211 427 SER D N   
11213 C CA  . SER D 126 ? 0.4002 0.5154 0.4396 0.0348  0.0370  -0.0242 427 SER D CA  
11214 C C   . SER D 126 ? 0.3592 0.4852 0.4009 0.0262  0.0404  -0.0240 427 SER D C   
11215 O O   . SER D 126 ? 0.3362 0.4640 0.3742 0.0287  0.0439  -0.0264 427 SER D O   
11216 C CB  . SER D 126 ? 0.3562 0.4870 0.4004 0.0461  0.0374  -0.0267 427 SER D CB  
11217 O OG  . SER D 126 ? 0.3715 0.5272 0.4272 0.0420  0.0373  -0.0259 427 SER D OG  
11218 N N   . LYS D 127 ? 0.3317 0.4626 0.3771 0.0161  0.0393  -0.0211 428 LYS D N   
11219 C CA  . LYS D 127 ? 0.3906 0.5277 0.4351 0.0066  0.0420  -0.0201 428 LYS D CA  
11220 C C   . LYS D 127 ? 0.5698 0.6870 0.6064 0.0012  0.0407  -0.0176 428 LYS D C   
11221 O O   . LYS D 127 ? 0.7994 0.9105 0.8346 -0.0055 0.0388  -0.0146 428 LYS D O   
11222 C CB  . LYS D 127 ? 0.3540 0.5072 0.4049 -0.0014 0.0415  -0.0184 428 LYS D CB  
11223 C CG  . LYS D 127 ? 0.6833 0.8401 0.7307 -0.0133 0.0441  -0.0167 428 LYS D CG  
11224 C CD  . LYS D 127 ? 0.7504 0.9194 0.8016 -0.0230 0.0429  -0.0150 428 LYS D CD  
11225 C CE  . LYS D 127 ? 0.7864 0.9598 0.8323 -0.0356 0.0460  -0.0134 428 LYS D CE  
11226 N NZ  . LYS D 127 ? 0.8028 1.0023 0.8559 -0.0433 0.0474  -0.0138 428 LYS D NZ  
11227 N N   . LEU D 128 ? 0.3768 0.4835 0.4072 0.0049  0.0416  -0.0191 429 LEU D N   
11228 C CA  . LEU D 128 ? 0.1947 0.2853 0.2185 0.0013  0.0398  -0.0171 429 LEU D CA  
11229 C C   . LEU D 128 ? 0.2573 0.3467 0.2745 -0.0002 0.0424  -0.0184 429 LEU D C   
11230 O O   . LEU D 128 ? 0.2852 0.3758 0.2998 0.0054  0.0446  -0.0219 429 LEU D O   
11231 C CB  . LEU D 128 ? 0.1811 0.2583 0.2024 0.0061  0.0372  -0.0175 429 LEU D CB  
11232 C CG  . LEU D 128 ? 0.2044 0.2694 0.2197 0.0024  0.0356  -0.0158 429 LEU D CG  
11233 C CD1 . LEU D 128 ? 0.1773 0.2411 0.1944 -0.0027 0.0338  -0.0119 429 LEU D CD1 
11234 C CD2 . LEU D 128 ? 0.2204 0.2735 0.2317 0.0054  0.0338  -0.0167 429 LEU D CD2 
11235 N N   . GLN D 129 ? 0.2508 0.3366 0.2638 -0.0071 0.0421  -0.0158 430 GLN D N   
11236 C CA  . GLN D 129 ? 0.2588 0.3425 0.2641 -0.0091 0.0440  -0.0167 430 GLN D CA  
11237 C C   . GLN D 129 ? 0.2382 0.3084 0.2378 -0.0080 0.0410  -0.0166 430 GLN D C   
11238 O O   . GLN D 129 ? 0.3457 0.4097 0.3460 -0.0099 0.0376  -0.0136 430 GLN D O   
11239 C CB  . GLN D 129 ? 0.2682 0.3536 0.2695 -0.0171 0.0447  -0.0136 430 GLN D CB  
11240 C CG  . GLN D 129 ? 0.3892 0.4730 0.3813 -0.0197 0.0468  -0.0143 430 GLN D CG  
11241 C CD  . GLN D 129 ? 0.4567 0.5516 0.4492 -0.0164 0.0519  -0.0187 430 GLN D CD  
11242 O OE1 . GLN D 129 ? 0.5174 0.6262 0.5175 -0.0147 0.0545  -0.0201 430 GLN D OE1 
11243 N NE2 . GLN D 129 ? 0.6305 0.7200 0.6142 -0.0151 0.0532  -0.0209 430 GLN D NE2 
11244 N N   . VAL D 130 ? 0.2743 0.3404 0.2678 -0.0049 0.0423  -0.0201 431 VAL D N   
11245 C CA  . VAL D 130 ? 0.2800 0.3338 0.2670 -0.0055 0.0394  -0.0204 431 VAL D CA  
11246 C C   . VAL D 130 ? 0.3127 0.3640 0.2905 -0.0099 0.0395  -0.0204 431 VAL D C   
11247 O O   . VAL D 130 ? 0.3671 0.4200 0.3389 -0.0088 0.0430  -0.0235 431 VAL D O   
11248 C CB  . VAL D 130 ? 0.2618 0.3076 0.2447 0.0005  0.0400  -0.0244 431 VAL D CB  
11249 C CG1 . VAL D 130 ? 0.3141 0.3466 0.2881 -0.0029 0.0369  -0.0248 431 VAL D CG1 
11250 C CG2 . VAL D 130 ? 0.2445 0.2921 0.2355 0.0052  0.0392  -0.0238 431 VAL D CG2 
11251 N N   . PHE D 131 ? 0.3244 0.3726 0.3008 -0.0144 0.0355  -0.0170 432 PHE D N   
11252 C CA  . PHE D 131 ? 0.3346 0.3801 0.3017 -0.0187 0.0343  -0.0165 432 PHE D CA  
11253 C C   . PHE D 131 ? 0.2862 0.3239 0.2476 -0.0202 0.0310  -0.0181 432 PHE D C   
11254 O O   . PHE D 131 ? 0.3379 0.3754 0.3039 -0.0215 0.0273  -0.0159 432 PHE D O   
11255 C CB  . PHE D 131 ? 0.2730 0.3210 0.2410 -0.0219 0.0315  -0.0113 432 PHE D CB  
11256 C CG  . PHE D 131 ? 0.3245 0.3771 0.2944 -0.0227 0.0346  -0.0097 432 PHE D CG  
11257 C CD1 . PHE D 131 ? 0.3016 0.3578 0.2660 -0.0246 0.0390  -0.0115 432 PHE D CD1 
11258 C CD2 . PHE D 131 ? 0.2922 0.3454 0.2683 -0.0223 0.0334  -0.0065 432 PHE D CD2 
11259 C CE1 . PHE D 131 ? 0.3972 0.4589 0.3628 -0.0275 0.0419  -0.0099 432 PHE D CE1 
11260 C CE2 . PHE D 131 ? 0.3540 0.4100 0.3299 -0.0250 0.0360  -0.0050 432 PHE D CE2 
11261 C CZ  . PHE D 131 ? 0.3453 0.4062 0.3163 -0.0284 0.0402  -0.0065 432 PHE D CZ  
11262 N N   . ASP D 132 ? 0.3215 0.3528 0.2720 -0.0206 0.0327  -0.0221 433 ASP D N   
11263 C CA  . ASP D 132 ? 0.3646 0.3860 0.3061 -0.0240 0.0297  -0.0242 433 ASP D CA  
11264 C C   . ASP D 132 ? 0.4209 0.4453 0.3581 -0.0304 0.0252  -0.0213 433 ASP D C   
11265 O O   . ASP D 132 ? 0.3870 0.4115 0.3161 -0.0321 0.0262  -0.0217 433 ASP D O   
11266 C CB  . ASP D 132 ? 0.3648 0.3754 0.2935 -0.0213 0.0335  -0.0300 433 ASP D CB  
11267 C CG  . ASP D 132 ? 0.4033 0.3996 0.3185 -0.0262 0.0304  -0.0327 433 ASP D CG  
11268 O OD1 . ASP D 132 ? 0.4787 0.4622 0.3808 -0.0231 0.0334  -0.0377 433 ASP D OD1 
11269 O OD2 . ASP D 132 ? 0.3631 0.3608 0.2799 -0.0330 0.0253  -0.0300 433 ASP D OD2 
11270 N N   . ALA D 133 ? 0.4170 0.4455 0.3599 -0.0336 0.0204  -0.0182 434 ALA D N   
11271 C CA  . ALA D 133 ? 0.3184 0.3524 0.2584 -0.0387 0.0152  -0.0152 434 ALA D CA  
11272 C C   . ALA D 133 ? 0.3414 0.3719 0.2749 -0.0456 0.0112  -0.0170 434 ALA D C   
11273 O O   . ALA D 133 ? 0.3019 0.3419 0.2382 -0.0499 0.0059  -0.0139 434 ALA D O   
11274 C CB  . ALA D 133 ? 0.2605 0.3057 0.2121 -0.0362 0.0125  -0.0096 434 ALA D CB  
11275 N N   . ARG D 134 ? 0.2899 0.3066 0.2137 -0.0468 0.0136  -0.0219 435 ARG D N   
11276 C CA  . ARG D 134 ? 0.3296 0.3397 0.2445 -0.0553 0.0099  -0.0238 435 ARG D CA  
11277 C C   . ARG D 134 ? 0.3383 0.3472 0.2401 -0.0626 0.0061  -0.0248 435 ARG D C   
11278 O O   . ARG D 134 ? 0.3648 0.3701 0.2586 -0.0719 0.0021  -0.0260 435 ARG D O   
11279 C CB  . ARG D 134 ? 0.3505 0.3416 0.2554 -0.0538 0.0136  -0.0287 435 ARG D CB  
11280 C CG  . ARG D 134 ? 0.3414 0.3338 0.2582 -0.0480 0.0158  -0.0274 435 ARG D CG  
11281 C CD  . ARG D 134 ? 0.3686 0.3407 0.2734 -0.0444 0.0193  -0.0321 435 ARG D CD  
11282 N NE  . ARG D 134 ? 0.3637 0.3308 0.2628 -0.0360 0.0241  -0.0355 435 ARG D NE  
11283 C CZ  . ARG D 134 ? 0.4059 0.3548 0.2911 -0.0307 0.0274  -0.0404 435 ARG D CZ  
11284 N NH1 . ARG D 134 ? 0.4365 0.3667 0.3097 -0.0337 0.0261  -0.0423 435 ARG D NH1 
11285 N NH2 . ARG D 134 ? 0.3729 0.3219 0.2549 -0.0223 0.0322  -0.0434 435 ARG D NH2 
11286 N N   . ASP D 135 ? 0.3208 0.3328 0.2194 -0.0599 0.0070  -0.0241 436 ASP D N   
11287 C CA  . ASP D 135 ? 0.3574 0.3692 0.2433 -0.0667 0.0028  -0.0244 436 ASP D CA  
11288 C C   . ASP D 135 ? 0.4284 0.4590 0.3238 -0.0688 -0.0037 -0.0184 436 ASP D C   
11289 O O   . ASP D 135 ? 0.4372 0.4708 0.3235 -0.0743 -0.0085 -0.0177 436 ASP D O   
11290 C CB  . ASP D 135 ? 0.3598 0.3639 0.2344 -0.0630 0.0075  -0.0269 436 ASP D CB  
11291 C CG  . ASP D 135 ? 0.5145 0.5292 0.3995 -0.0565 0.0098  -0.0226 436 ASP D CG  
11292 O OD1 . ASP D 135 ? 0.4804 0.4921 0.3568 -0.0550 0.0132  -0.0235 436 ASP D OD1 
11293 O OD2 . ASP D 135 ? 0.5270 0.5522 0.4275 -0.0533 0.0084  -0.0183 436 ASP D OD2 
11294 N N   . CYS D 136 ? 0.3784 0.4212 0.2909 -0.0637 -0.0040 -0.0141 437 CYS D N   
11295 C CA  . CYS D 136 ? 0.3514 0.4117 0.2731 -0.0624 -0.0096 -0.0083 437 CYS D CA  
11296 C C   . CYS D 136 ? 0.4312 0.5033 0.3538 -0.0711 -0.0164 -0.0076 437 CYS D C   
11297 O O   . CYS D 136 ? 0.4462 0.5154 0.3689 -0.0772 -0.0161 -0.0102 437 CYS D O   
11298 C CB  . CYS D 136 ? 0.3258 0.3931 0.2635 -0.0541 -0.0072 -0.0048 437 CYS D CB  
11299 S SG  . CYS D 136 ? 0.3907 0.4756 0.3378 -0.0485 -0.0127 0.0022  437 CYS D SG  
11300 N N   . THR D 137 ? 0.3686 0.4543 0.2908 -0.0722 -0.0229 -0.0038 438 THR D N   
11301 C CA  . THR D 137 ? 0.3160 0.4176 0.2402 -0.0811 -0.0300 -0.0028 438 THR D CA  
11302 C C   . THR D 137 ? 0.3116 0.4387 0.2505 -0.0758 -0.0356 0.0034  438 THR D C   
11303 O O   . THR D 137 ? 0.3723 0.5181 0.3173 -0.0826 -0.0409 0.0044  438 THR D O   
11304 C CB  . THR D 137 ? 0.4229 0.5188 0.3290 -0.0905 -0.0345 -0.0053 438 THR D CB  
11305 O OG1 . THR D 137 ? 0.4478 0.5479 0.3496 -0.0850 -0.0376 -0.0017 438 THR D OG1 
11306 C CG2 . THR D 137 ? 0.4030 0.4723 0.2920 -0.0943 -0.0286 -0.0119 438 THR D CG2 
11307 N N   . THR D 138 ? 0.3264 0.4551 0.2701 -0.0640 -0.0347 0.0075  439 THR D N   
11308 C CA  . THR D 138 ? 0.2756 0.4263 0.2302 -0.0566 -0.0403 0.0133  439 THR D CA  
11309 C C   . THR D 138 ? 0.2635 0.4113 0.2277 -0.0441 -0.0357 0.0161  439 THR D C   
11310 O O   . THR D 138 ? 0.2866 0.4154 0.2467 -0.0412 -0.0292 0.0142  439 THR D O   
11311 C CB  . THR D 138 ? 0.3284 0.4821 0.2726 -0.0543 -0.0466 0.0167  439 THR D CB  
11312 O OG1 . THR D 138 ? 0.3387 0.4724 0.2735 -0.0475 -0.0421 0.0174  439 THR D OG1 
11313 C CG2 . THR D 138 ? 0.3027 0.4551 0.2338 -0.0674 -0.0509 0.0134  439 THR D CG2 
11314 N N   . ALA D 139 ? 0.3436 0.5112 0.3199 -0.0363 -0.0392 0.0206  440 ALA D N   
11315 C CA  . ALA D 139 ? 0.3543 0.5175 0.3370 -0.0238 -0.0354 0.0233  440 ALA D CA  
11316 C C   . ALA D 139 ? 0.3000 0.4434 0.2697 -0.0173 -0.0341 0.0253  440 ALA D C   
11317 O O   . ALA D 139 ? 0.2542 0.3831 0.2235 -0.0119 -0.0286 0.0253  440 ALA D O   
11318 C CB  . ALA D 139 ? 0.3574 0.5455 0.3529 -0.0149 -0.0397 0.0278  440 ALA D CB  
11319 N N   . HIS D 140 ? 0.3218 0.4640 0.2796 -0.0189 -0.0391 0.0270  441 HIS D N   
11320 C CA  . HIS D 140 ? 0.3170 0.4390 0.2597 -0.0149 -0.0375 0.0289  441 HIS D CA  
11321 C C   . HIS D 140 ? 0.2794 0.3818 0.2161 -0.0212 -0.0296 0.0242  441 HIS D C   
11322 O O   . HIS D 140 ? 0.3500 0.4375 0.2822 -0.0171 -0.0250 0.0252  441 HIS D O   
11323 C CB  . HIS D 140 ? 0.2980 0.4221 0.2275 -0.0171 -0.0444 0.0312  441 HIS D CB  
11324 C CG  . HIS D 140 ? 0.3258 0.4618 0.2556 -0.0059 -0.0518 0.0376  441 HIS D CG  
11325 N ND1 . HIS D 140 ? 0.4057 0.5692 0.3473 -0.0042 -0.0585 0.0393  441 HIS D ND1 
11326 C CD2 . HIS D 140 ? 0.4023 0.5263 0.3206 0.0042  -0.0536 0.0428  441 HIS D CD2 
11327 C CE1 . HIS D 140 ? 0.4360 0.6056 0.3747 0.0084  -0.0644 0.0453  441 HIS D CE1 
11328 N NE2 . HIS D 140 ? 0.4503 0.5940 0.3736 0.0138  -0.0616 0.0475  441 HIS D NE2 
11329 N N   . GLY D 141 ? 0.2787 0.3806 0.2139 -0.0313 -0.0282 0.0191  442 GLY D N   
11330 C CA  . GLY D 141 ? 0.3232 0.4093 0.2545 -0.0352 -0.0204 0.0143  442 GLY D CA  
11331 C C   . GLY D 141 ? 0.3109 0.3947 0.2541 -0.0308 -0.0150 0.0135  442 GLY D C   
11332 O O   . GLY D 141 ? 0.3052 0.3769 0.2458 -0.0295 -0.0092 0.0122  442 GLY D O   
11333 N N   . MET D 142 ? 0.3054 0.4022 0.2617 -0.0290 -0.0169 0.0143  443 MET D N   
11334 C CA  . MET D 142 ? 0.2711 0.3660 0.2379 -0.0244 -0.0122 0.0139  443 MET D CA  
11335 C C   . MET D 142 ? 0.3029 0.3896 0.2673 -0.0159 -0.0107 0.0177  443 MET D C   
11336 O O   . MET D 142 ? 0.3077 0.3841 0.2730 -0.0147 -0.0054 0.0164  443 MET D O   
11337 C CB  . MET D 142 ? 0.3271 0.4390 0.3071 -0.0236 -0.0147 0.0148  443 MET D CB  
11338 C CG  . MET D 142 ? 0.3076 0.4246 0.2890 -0.0336 -0.0153 0.0111  443 MET D CG  
11339 S SD  . MET D 142 ? 0.3282 0.4684 0.3254 -0.0338 -0.0177 0.0129  443 MET D SD  
11340 C CE  . MET D 142 ? 0.2348 0.3671 0.2403 -0.0266 -0.0111 0.0126  443 MET D CE  
11341 N N   . PHE D 143 ? 0.3824 0.4729 0.3424 -0.0102 -0.0157 0.0224  444 PHE D N   
11342 C CA  . PHE D 143 ? 0.3303 0.4084 0.2833 -0.0025 -0.0147 0.0262  444 PHE D CA  
11343 C C   . PHE D 143 ? 0.4090 0.4694 0.3499 -0.0074 -0.0102 0.0249  444 PHE D C   
11344 O O   . PHE D 143 ? 0.3698 0.4185 0.3087 -0.0058 -0.0060 0.0252  444 PHE D O   
11345 C CB  . PHE D 143 ? 0.2938 0.3771 0.2409 0.0049  -0.0216 0.0316  444 PHE D CB  
11346 C CG  . PHE D 143 ? 0.3772 0.4424 0.3114 0.0121  -0.0212 0.0357  444 PHE D CG  
11347 C CD1 . PHE D 143 ? 0.3805 0.4331 0.2973 0.0104  -0.0231 0.0382  444 PHE D CD1 
11348 C CD2 . PHE D 143 ? 0.3741 0.4324 0.3110 0.0197  -0.0186 0.0370  444 PHE D CD2 
11349 C CE1 . PHE D 143 ? 0.3935 0.4260 0.2952 0.0158  -0.0228 0.0423  444 PHE D CE1 
11350 C CE2 . PHE D 143 ? 0.3332 0.3710 0.2549 0.0255  -0.0185 0.0408  444 PHE D CE2 
11351 C CZ  . PHE D 143 ? 0.3894 0.4137 0.2931 0.0232  -0.0205 0.0436  444 PHE D CZ  
11352 N N   . ASN D 144 ? 0.3094 0.3683 0.2414 -0.0141 -0.0109 0.0232  445 ASN D N   
11353 C CA  . ASN D 144 ? 0.2891 0.3346 0.2101 -0.0193 -0.0058 0.0216  445 ASN D CA  
11354 C C   . ASN D 144 ? 0.2657 0.3091 0.1949 -0.0220 0.0011  0.0171  445 ASN D C   
11355 O O   . ASN D 144 ? 0.2873 0.3218 0.2130 -0.0227 0.0056  0.0174  445 ASN D O   
11356 C CB  . ASN D 144 ? 0.3399 0.3862 0.2509 -0.0257 -0.0074 0.0196  445 ASN D CB  
11357 C CG  . ASN D 144 ? 0.4861 0.5208 0.3846 -0.0307 -0.0019 0.0182  445 ASN D CG  
11358 O OD1 . ASN D 144 ? 0.5498 0.5746 0.4410 -0.0296 0.0001  0.0214  445 ASN D OD1 
11359 N ND2 . ASN D 144 ? 0.4887 0.5240 0.3834 -0.0366 0.0009  0.0133  445 ASN D ND2 
11360 N N   . TYR D 145 ? 0.2555 0.3069 0.1945 -0.0240 0.0017  0.0130  446 TYR D N   
11361 C CA  . TYR D 145 ? 0.4171 0.4668 0.3635 -0.0251 0.0075  0.0090  446 TYR D CA  
11362 C C   . TYR D 145 ? 0.3605 0.4082 0.3143 -0.0203 0.0091  0.0110  446 TYR D C   
11363 O O   . TYR D 145 ? 0.2396 0.2829 0.1946 -0.0213 0.0139  0.0093  446 TYR D O   
11364 C CB  . TYR D 145 ? 0.2781 0.3337 0.2312 -0.0274 0.0069  0.0051  446 TYR D CB  
11365 C CG  . TYR D 145 ? 0.2759 0.3273 0.2204 -0.0326 0.0088  0.0005  446 TYR D CG  
11366 C CD1 . TYR D 145 ? 0.2770 0.3307 0.2153 -0.0371 0.0045  -0.0005 446 TYR D CD1 
11367 C CD2 . TYR D 145 ? 0.2991 0.3447 0.2410 -0.0328 0.0149  -0.0031 446 TYR D CD2 
11368 C CE1 . TYR D 145 ? 0.2957 0.3426 0.2234 -0.0417 0.0065  -0.0052 446 TYR D CE1 
11369 C CE2 . TYR D 145 ? 0.3065 0.3473 0.2392 -0.0359 0.0173  -0.0077 446 TYR D CE2 
11370 C CZ  . TYR D 145 ? 0.3261 0.3657 0.2507 -0.0403 0.0132  -0.0089 446 TYR D CZ  
11371 O OH  . TYR D 145 ? 0.3733 0.4052 0.2862 -0.0429 0.0159  -0.0139 446 TYR D OH  
11372 N N   . ILE D 146 ? 0.3100 0.3618 0.2683 -0.0150 0.0052  0.0145  447 ILE D N   
11373 C CA  . ILE D 146 ? 0.3028 0.3513 0.2666 -0.0102 0.0068  0.0159  447 ILE D CA  
11374 C C   . ILE D 146 ? 0.3184 0.3535 0.2711 -0.0095 0.0082  0.0188  447 ILE D C   
11375 O O   . ILE D 146 ? 0.3435 0.3722 0.2971 -0.0100 0.0117  0.0183  447 ILE D O   
11376 C CB  . ILE D 146 ? 0.3239 0.3817 0.2953 -0.0038 0.0030  0.0184  447 ILE D CB  
11377 C CG1 . ILE D 146 ? 0.3074 0.3768 0.2897 -0.0070 0.0031  0.0151  447 ILE D CG1 
11378 C CG2 . ILE D 146 ? 0.3195 0.3705 0.2920 0.0027  0.0044  0.0205  447 ILE D CG2 
11379 C CD1 . ILE D 146 ? 0.2249 0.3092 0.2153 -0.0032 -0.0008 0.0172  447 ILE D CD1 
11380 N N   . CYS D 147 ? 0.2833 0.3131 0.2237 -0.0094 0.0053  0.0220  448 CYS D N   
11381 C CA  . CYS D 147 ? 0.3005 0.3145 0.2267 -0.0106 0.0068  0.0250  448 CYS D CA  
11382 C C   . CYS D 147 ? 0.2858 0.2973 0.2103 -0.0190 0.0127  0.0218  448 CYS D C   
11383 O O   . CYS D 147 ? 0.3602 0.3623 0.2797 -0.0217 0.0155  0.0227  448 CYS D O   
11384 C CB  . CYS D 147 ? 0.4082 0.4163 0.3197 -0.0095 0.0025  0.0290  448 CYS D CB  
11385 S SG  . CYS D 147 ? 0.4712 0.4797 0.3809 0.0027  -0.0045 0.0342  448 CYS D SG  
11386 N N   . ASN D 148 ? 0.2975 0.3174 0.2247 -0.0235 0.0145  0.0181  449 ASN D N   
11387 C CA  . ASN D 148 ? 0.2898 0.3111 0.2170 -0.0298 0.0205  0.0146  449 ASN D CA  
11388 C C   . ASN D 148 ? 0.2871 0.3129 0.2269 -0.0289 0.0235  0.0120  449 ASN D C   
11389 O O   . ASN D 148 ? 0.3070 0.3315 0.2458 -0.0330 0.0274  0.0115  449 ASN D O   
11390 C CB  . ASN D 148 ? 0.2617 0.2901 0.1884 -0.0325 0.0218  0.0107  449 ASN D CB  
11391 C CG  . ASN D 148 ? 0.3161 0.3393 0.2278 -0.0349 0.0192  0.0132  449 ASN D CG  
11392 O OD1 . ASN D 148 ? 0.3569 0.3705 0.2576 -0.0353 0.0176  0.0179  449 ASN D OD1 
11393 N ND2 . ASN D 148 ? 0.3230 0.3506 0.2324 -0.0364 0.0185  0.0102  449 ASN D ND2 
11394 N N   . HIS D 149 ? 0.2402 0.2717 0.1911 -0.0241 0.0215  0.0106  450 HIS D N   
11395 C CA  . HIS D 149 ? 0.2750 0.3094 0.2365 -0.0225 0.0236  0.0087  450 HIS D CA  
11396 C C   . HIS D 149 ? 0.2425 0.2678 0.1999 -0.0223 0.0236  0.0119  450 HIS D C   
11397 O O   . HIS D 149 ? 0.2768 0.3020 0.2352 -0.0262 0.0269  0.0107  450 HIS D O   
11398 C CB  . HIS D 149 ? 0.2172 0.2573 0.1883 -0.0181 0.0210  0.0076  450 HIS D CB  
11399 C CG  . HIS D 149 ? 0.3274 0.3692 0.3080 -0.0160 0.0226  0.0060  450 HIS D CG  
11400 N ND1 . HIS D 149 ? 0.2752 0.3221 0.2635 -0.0149 0.0229  0.0029  450 HIS D ND1 
11401 C CD2 . HIS D 149 ? 0.2744 0.3119 0.2563 -0.0150 0.0235  0.0072  450 HIS D CD2 
11402 C CE1 . HIS D 149 ? 0.3172 0.3638 0.3116 -0.0129 0.0240  0.0024  450 HIS D CE1 
11403 N NE2 . HIS D 149 ? 0.2669 0.3085 0.2580 -0.0130 0.0244  0.0049  450 HIS D NE2 
11404 N N   . VAL D 150 ? 0.2719 0.2893 0.2231 -0.0180 0.0199  0.0159  451 VAL D N   
11405 C CA  . VAL D 150 ? 0.2789 0.2834 0.2229 -0.0168 0.0197  0.0187  451 VAL D CA  
11406 C C   . VAL D 150 ? 0.4507 0.4460 0.3826 -0.0250 0.0225  0.0197  451 VAL D C   
11407 O O   . VAL D 150 ? 0.2648 0.2537 0.1942 -0.0287 0.0243  0.0197  451 VAL D O   
11408 C CB  . VAL D 150 ? 0.3274 0.3244 0.2646 -0.0086 0.0152  0.0229  451 VAL D CB  
11409 C CG1 . VAL D 150 ? 0.2828 0.2603 0.2060 -0.0075 0.0151  0.0261  451 VAL D CG1 
11410 C CG2 . VAL D 150 ? 0.2936 0.3021 0.2444 -0.0015 0.0134  0.0219  451 VAL D CG2 
11411 N N   . LYS D 151 ? 0.4204 0.4153 0.3437 -0.0292 0.0229  0.0205  452 LYS D N   
11412 C CA  . LYS D 151 ? 0.3419 0.3288 0.2526 -0.0385 0.0260  0.0217  452 LYS D CA  
11413 C C   . LYS D 151 ? 0.3161 0.3168 0.2369 -0.0452 0.0311  0.0176  452 LYS D C   
11414 O O   . LYS D 151 ? 0.2804 0.2771 0.1963 -0.0525 0.0335  0.0181  452 LYS D O   
11415 C CB  . LYS D 151 ? 0.3909 0.3741 0.2888 -0.0413 0.0254  0.0237  452 LYS D CB  
11416 C CG  . LYS D 151 ? 0.3439 0.3163 0.2253 -0.0516 0.0286  0.0260  452 LYS D CG  
11417 C CD  . LYS D 151 ? 0.4375 0.4043 0.3043 -0.0534 0.0274  0.0285  452 LYS D CD  
11418 C CE  . LYS D 151 ? 0.5082 0.4584 0.3536 -0.0635 0.0296  0.0322  452 LYS D CE  
11419 N NZ  . LYS D 151 ? 0.5415 0.4827 0.3700 -0.0639 0.0274  0.0355  452 LYS D NZ  
11420 N N   . TYR D 152 ? 0.2951 0.3118 0.2289 -0.0428 0.0327  0.0134  453 TYR D N   
11421 C CA  . TYR D 152 ? 0.3364 0.3677 0.2806 -0.0462 0.0372  0.0093  453 TYR D CA  
11422 C C   . TYR D 152 ? 0.2650 0.2969 0.2172 -0.0453 0.0367  0.0088  453 TYR D C   
11423 O O   . TYR D 152 ? 0.3436 0.3806 0.2967 -0.0519 0.0393  0.0082  453 TYR D O   
11424 C CB  . TYR D 152 ? 0.2699 0.3135 0.2241 -0.0413 0.0382  0.0049  453 TYR D CB  
11425 C CG  . TYR D 152 ? 0.3118 0.3703 0.2769 -0.0417 0.0423  0.0008  453 TYR D CG  
11426 C CD1 . TYR D 152 ? 0.3719 0.4412 0.3355 -0.0464 0.0473  -0.0012 453 TYR D CD1 
11427 C CD2 . TYR D 152 ? 0.3049 0.3676 0.2815 -0.0368 0.0412  -0.0010 453 TYR D CD2 
11428 C CE1 . TYR D 152 ? 0.3908 0.4764 0.3649 -0.0452 0.0509  -0.0049 453 TYR D CE1 
11429 C CE2 . TYR D 152 ? 0.3098 0.3866 0.2957 -0.0360 0.0443  -0.0044 453 TYR D CE2 
11430 C CZ  . TYR D 152 ? 0.3657 0.4547 0.3509 -0.0396 0.0491  -0.0064 453 TYR D CZ  
11431 O OH  . TYR D 152 ? 0.4406 0.5464 0.4358 -0.0372 0.0521  -0.0098 453 TYR D OH  
11432 N N   . ALA D 153 ? 0.3276 0.3560 0.2857 -0.0377 0.0333  0.0090  454 ALA D N   
11433 C CA  . ALA D 153 ? 0.2877 0.3166 0.2531 -0.0360 0.0328  0.0082  454 ALA D CA  
11434 C C   . ALA D 153 ? 0.3116 0.3270 0.2659 -0.0414 0.0323  0.0111  454 ALA D C   
11435 O O   . ALA D 153 ? 0.3499 0.3683 0.3073 -0.0454 0.0333  0.0100  454 ALA D O   
11436 C CB  . ALA D 153 ? 0.2189 0.2459 0.1907 -0.0273 0.0297  0.0082  454 ALA D CB  
11437 N N   . THR D 154 ? 0.3635 0.3626 0.3029 -0.0415 0.0305  0.0150  455 THR D N   
11438 C CA  . THR D 154 ? 0.3888 0.3697 0.3133 -0.0466 0.0299  0.0178  455 THR D CA  
11439 C C   . THR D 154 ? 0.3999 0.3838 0.3185 -0.0597 0.0333  0.0176  455 THR D C   
11440 O O   . THR D 154 ? 0.3303 0.3118 0.2468 -0.0664 0.0339  0.0172  455 THR D O   
11441 C CB  . THR D 154 ? 0.3597 0.3205 0.2676 -0.0419 0.0269  0.0222  455 THR D CB  
11442 O OG1 . THR D 154 ? 0.3266 0.2884 0.2418 -0.0297 0.0239  0.0223  455 THR D OG1 
11443 C CG2 . THR D 154 ? 0.3672 0.3037 0.2546 -0.0475 0.0264  0.0252  455 THR D CG2 
11444 N N   . ASN D 155 ? 0.3881 0.3781 0.3032 -0.0644 0.0356  0.0178  456 ASN D N   
11445 C CA  . ASN D 155 ? 0.3862 0.3855 0.2986 -0.0772 0.0398  0.0171  456 ASN D CA  
11446 C C   . ASN D 155 ? 0.4087 0.3893 0.3035 -0.0880 0.0394  0.0201  456 ASN D C   
11447 O O   . ASN D 155 ? 0.3941 0.3842 0.2918 -0.0980 0.0415  0.0187  456 ASN D O   
11448 C CB  . ASN D 155 ? 0.3837 0.4095 0.3164 -0.0772 0.0425  0.0124  456 ASN D CB  
11449 C CG  . ASN D 155 ? 0.4202 0.4629 0.3536 -0.0889 0.0474  0.0112  456 ASN D CG  
11450 O OD1 . ASN D 155 ? 0.3881 0.4281 0.3106 -0.0952 0.0499  0.0128  456 ASN D OD1 
11451 N ND2 . ASN D 155 ? 0.3479 0.4093 0.2940 -0.0920 0.0488  0.0085  456 ASN D ND2 
11452 N N   . LYS D 156 ? 0.3537 0.3069 0.2292 -0.0854 0.0364  0.0242  457 LYS D N   
11453 C CA  . LYS D 156 ? 0.3886 0.3163 0.2412 -0.0951 0.0357  0.0275  457 LYS D CA  
11454 C C   . LYS D 156 ? 0.4338 0.3598 0.2899 -0.0980 0.0348  0.0257  457 LYS D C   
11455 O O   . LYS D 156 ? 0.4713 0.3854 0.3128 -0.1112 0.0355  0.0268  457 LYS D O   
11456 C CB  . LYS D 156 ? 0.4925 0.4214 0.3329 -0.1116 0.0395  0.0289  457 LYS D CB  
11457 C CG  . LYS D 156 ? 0.5357 0.4630 0.3685 -0.1102 0.0405  0.0310  457 LYS D CG  
11458 C CD  . LYS D 156 ? 0.6618 0.5949 0.4847 -0.1276 0.0455  0.0319  457 LYS D CD  
11459 C CE  . LYS D 156 ? 0.8114 0.7404 0.6235 -0.1270 0.0465  0.0342  457 LYS D CE  
11460 N NZ  . LYS D 156 ? 0.8796 0.7734 0.6668 -0.1216 0.0416  0.0396  457 LYS D NZ  
11461 N N   . GLY D 157 ? 0.3922 0.3295 0.2663 -0.0866 0.0333  0.0230  458 GLY D N   
11462 C CA  . GLY D 157 ? 0.3953 0.3297 0.2718 -0.0876 0.0320  0.0213  458 GLY D CA  
11463 C C   . GLY D 157 ? 0.4053 0.3692 0.3032 -0.0913 0.0337  0.0173  458 GLY D C   
11464 O O   . GLY D 157 ? 0.3935 0.3587 0.2972 -0.0894 0.0321  0.0155  458 GLY D O   
11465 N N   . ASN D 158 ? 0.3404 0.3281 0.2495 -0.0958 0.0369  0.0157  459 ASN D N   
11466 C CA  . ASN D 158 ? 0.3833 0.4012 0.3136 -0.0963 0.0385  0.0118  459 ASN D CA  
11467 C C   . ASN D 158 ? 0.4229 0.4518 0.3695 -0.0811 0.0380  0.0096  459 ASN D C   
11468 O O   . ASN D 158 ? 0.3718 0.4161 0.3268 -0.0782 0.0405  0.0080  459 ASN D O   
11469 C CB  . ASN D 158 ? 0.3638 0.4017 0.2962 -0.1083 0.0428  0.0112  459 ASN D CB  
11470 C CG  . ASN D 158 ? 0.4621 0.5326 0.4153 -0.1084 0.0443  0.0073  459 ASN D CG  
11471 O OD1 . ASN D 158 ? 0.4195 0.4939 0.3815 -0.1038 0.0416  0.0058  459 ASN D OD1 
11472 N ND2 . ASN D 158 ? 0.4503 0.5447 0.4110 -0.1130 0.0488  0.0059  459 ASN D ND2 
11473 N N   . LEU D 159 ? 0.2578 0.2770 0.2070 -0.0718 0.0350  0.0094  460 LEU D N   
11474 C CA  . LEU D 159 ? 0.3371 0.3599 0.2964 -0.0588 0.0340  0.0083  460 LEU D CA  
11475 C C   . LEU D 159 ? 0.3258 0.3730 0.3025 -0.0554 0.0359  0.0046  460 LEU D C   
11476 O O   . LEU D 159 ? 0.3374 0.3996 0.3218 -0.0594 0.0368  0.0027  460 LEU D O   
11477 C CB  . LEU D 159 ? 0.3125 0.3232 0.2718 -0.0507 0.0311  0.0087  460 LEU D CB  
11478 C CG  . LEU D 159 ? 0.5275 0.5124 0.4685 -0.0511 0.0292  0.0120  460 LEU D CG  
11479 C CD1 . LEU D 159 ? 0.5529 0.5297 0.4960 -0.0404 0.0272  0.0120  460 LEU D CD1 
11480 C CD2 . LEU D 159 ? 0.4739 0.4484 0.4034 -0.0510 0.0293  0.0149  460 LEU D CD2 
11481 N N   . ARG D 160 ? 0.2994 0.3499 0.2811 -0.0477 0.0363  0.0036  461 ARG D N   
11482 C CA  . ARG D 160 ? 0.2061 0.2748 0.2004 -0.0431 0.0382  0.0000  461 ARG D CA  
11483 C C   . ARG D 160 ? 0.2944 0.3583 0.2933 -0.0333 0.0361  -0.0008 461 ARG D C   
11484 O O   . ARG D 160 ? 0.2765 0.3289 0.2693 -0.0310 0.0344  0.0013  461 ARG D O   
11485 C CB  . ARG D 160 ? 0.2546 0.3320 0.2466 -0.0465 0.0417  -0.0008 461 ARG D CB  
11486 C CG  . ARG D 160 ? 0.3535 0.4401 0.3421 -0.0575 0.0447  -0.0003 461 ARG D CG  
11487 C CD  . ARG D 160 ? 0.3038 0.4000 0.2898 -0.0602 0.0490  -0.0014 461 ARG D CD  
11488 N NE  . ARG D 160 ? 0.3235 0.4022 0.2954 -0.0621 0.0482  0.0016  461 ARG D NE  
11489 C CZ  . ARG D 160 ? 0.3920 0.4734 0.3560 -0.0674 0.0516  0.0020  461 ARG D CZ  
11490 N NH1 . ARG D 160 ? 0.3195 0.4216 0.2893 -0.0713 0.0567  -0.0007 461 ARG D NH1 
11491 N NH2 . ARG D 160 ? 0.2877 0.3520 0.2378 -0.0684 0.0500  0.0051  461 ARG D NH2 
11492 N N   . SER D 161 ? 0.2534 0.3260 0.2622 -0.0278 0.0359  -0.0035 462 SER D N   
11493 C CA  . SER D 161 ? 0.2818 0.3490 0.2936 -0.0203 0.0341  -0.0042 462 SER D CA  
11494 C C   . SER D 161 ? 0.2754 0.3431 0.2854 -0.0180 0.0352  -0.0055 462 SER D C   
11495 O O   . SER D 161 ? 0.2523 0.3285 0.2626 -0.0187 0.0379  -0.0077 462 SER D O   
11496 C CB  . SER D 161 ? 0.2204 0.2942 0.2403 -0.0155 0.0337  -0.0066 462 SER D CB  
11497 O OG  . SER D 161 ? 0.3660 0.4390 0.3866 -0.0182 0.0322  -0.0054 462 SER D OG  
11498 N N   . ALA D 162 ? 0.2357 0.2951 0.2434 -0.0154 0.0330  -0.0044 463 ALA D N   
11499 C CA  . ALA D 162 ? 0.1997 0.2585 0.2037 -0.0148 0.0332  -0.0055 463 ALA D CA  
11500 C C   . ALA D 162 ? 0.2641 0.3178 0.2691 -0.0118 0.0305  -0.0052 463 ALA D C   
11501 O O   . ALA D 162 ? 0.2113 0.2618 0.2185 -0.0105 0.0286  -0.0031 463 ALA D O   
11502 C CB  . ALA D 162 ? 0.1937 0.2495 0.1896 -0.0192 0.0332  -0.0030 463 ALA D CB  
11503 N N   . ILE D 163 ? 0.2507 0.3038 0.2530 -0.0114 0.0306  -0.0074 464 ILE D N   
11504 C CA  . ILE D 163 ? 0.2461 0.2957 0.2478 -0.0112 0.0279  -0.0071 464 ILE D CA  
11505 C C   . ILE D 163 ? 0.2985 0.3472 0.2930 -0.0140 0.0273  -0.0079 464 ILE D C   
11506 O O   . ILE D 163 ? 0.2404 0.2891 0.2303 -0.0143 0.0298  -0.0105 464 ILE D O   
11507 C CB  . ILE D 163 ? 0.2208 0.2670 0.2244 -0.0087 0.0282  -0.0096 464 ILE D CB  
11508 C CG1 . ILE D 163 ? 0.1879 0.2313 0.1902 -0.0110 0.0256  -0.0089 464 ILE D CG1 
11509 C CG2 . ILE D 163 ? 0.2107 0.2551 0.2100 -0.0066 0.0308  -0.0137 464 ILE D CG2 
11510 C CD1 . ILE D 163 ? 0.2205 0.2581 0.2231 -0.0098 0.0257  -0.0103 464 ILE D CD1 
11511 N N   . THR D 164 ? 0.2468 0.2961 0.2402 -0.0158 0.0239  -0.0056 465 THR D N   
11512 C CA  . THR D 164 ? 0.2486 0.2974 0.2346 -0.0191 0.0222  -0.0063 465 THR D CA  
11513 C C   . THR D 164 ? 0.3029 0.3511 0.2890 -0.0216 0.0197  -0.0073 465 THR D C   
11514 O O   . THR D 164 ? 0.3197 0.3727 0.3120 -0.0213 0.0176  -0.0049 465 THR D O   
11515 C CB  . THR D 164 ? 0.2221 0.2737 0.2052 -0.0199 0.0195  -0.0023 465 THR D CB  
11516 O OG1 . THR D 164 ? 0.2899 0.3395 0.2700 -0.0196 0.0221  -0.0014 465 THR D OG1 
11517 C CG2 . THR D 164 ? 0.2569 0.3090 0.2322 -0.0238 0.0169  -0.0030 465 THR D CG2 
11518 N N   . ILE D 165 ? 0.2978 0.3398 0.2757 -0.0244 0.0201  -0.0109 466 ILE D N   
11519 C CA  . ILE D 165 ? 0.3418 0.3794 0.3169 -0.0283 0.0184  -0.0126 466 ILE D CA  
11520 C C   . ILE D 165 ? 0.2757 0.3139 0.2425 -0.0349 0.0150  -0.0129 466 ILE D C   
11521 O O   . ILE D 165 ? 0.2962 0.3273 0.2523 -0.0364 0.0159  -0.0159 466 ILE D O   
11522 C CB  . ILE D 165 ? 0.3836 0.4088 0.3527 -0.0260 0.0216  -0.0168 466 ILE D CB  
11523 C CG1 . ILE D 165 ? 0.3071 0.3341 0.2849 -0.0195 0.0242  -0.0161 466 ILE D CG1 
11524 C CG2 . ILE D 165 ? 0.3558 0.3728 0.3189 -0.0315 0.0196  -0.0180 466 ILE D CG2 
11525 C CD1 . ILE D 165 ? 0.2745 0.2915 0.2470 -0.0145 0.0271  -0.0200 466 ILE D CD1 
11526 N N   . PHE D 166 ? 0.3062 0.3542 0.2780 -0.0389 0.0110  -0.0101 467 PHE D N   
11527 C CA  . PHE D 166 ? 0.3121 0.3653 0.2783 -0.0459 0.0065  -0.0097 467 PHE D CA  
11528 C C   . PHE D 166 ? 0.3720 0.4162 0.3291 -0.0542 0.0055  -0.0130 467 PHE D C   
11529 O O   . PHE D 166 ? 0.3599 0.3938 0.3156 -0.0535 0.0083  -0.0149 467 PHE D O   
11530 C CB  . PHE D 166 ? 0.2807 0.3521 0.2579 -0.0451 0.0026  -0.0048 467 PHE D CB  
11531 C CG  . PHE D 166 ? 0.3246 0.4003 0.3049 -0.0379 0.0025  -0.0015 467 PHE D CG  
11532 C CD1 . PHE D 166 ? 0.2905 0.3648 0.2622 -0.0387 0.0007  -0.0011 467 PHE D CD1 
11533 C CD2 . PHE D 166 ? 0.3367 0.4153 0.3260 -0.0308 0.0044  0.0012  467 PHE D CD2 
11534 C CE1 . PHE D 166 ? 0.3147 0.3898 0.2864 -0.0330 0.0006  0.0023  467 PHE D CE1 
11535 C CE2 . PHE D 166 ? 0.3697 0.4483 0.3585 -0.0250 0.0042  0.0042  467 PHE D CE2 
11536 C CZ  . PHE D 166 ? 0.2422 0.3187 0.2219 -0.0262 0.0023  0.0049  467 PHE D CZ  
11537 N N   . PRO D 167 ? 0.3993 0.4454 0.3480 -0.0627 0.0014  -0.0137 468 PRO D N   
11538 C CA  . PRO D 167 ? 0.3948 0.4287 0.3309 -0.0726 0.0003  -0.0171 468 PRO D CA  
11539 C C   . PRO D 167 ? 0.4012 0.4366 0.3432 -0.0760 0.0008  -0.0161 468 PRO D C   
11540 O O   . PRO D 167 ? 0.3695 0.4236 0.3262 -0.0750 -0.0004 -0.0122 468 PRO D O   
11541 C CB  . PRO D 167 ? 0.4286 0.4729 0.3599 -0.0820 -0.0056 -0.0163 468 PRO D CB  
11542 C CG  . PRO D 167 ? 0.3957 0.4456 0.3282 -0.0753 -0.0060 -0.0147 468 PRO D CG  
11543 C CD  . PRO D 167 ? 0.3998 0.4556 0.3464 -0.0639 -0.0025 -0.0118 468 PRO D CD  
11544 N N   . GLN D 168 ? 0.3579 0.3720 0.2864 -0.0797 0.0029  -0.0198 469 GLN D N   
11545 C CA  . GLN D 168 ? 0.3807 0.3916 0.3106 -0.0840 0.0037  -0.0191 469 GLN D CA  
11546 C C   . GLN D 168 ? 0.4461 0.4709 0.3768 -0.0981 -0.0008 -0.0172 469 GLN D C   
11547 O O   . GLN D 168 ? 0.3934 0.4251 0.3192 -0.1056 -0.0050 -0.0176 469 GLN D O   
11548 C CB  . GLN D 168 ? 0.3189 0.2998 0.2301 -0.0842 0.0065  -0.0234 469 GLN D CB  
11549 C CG  . GLN D 168 ? 0.4125 0.3761 0.3020 -0.0948 0.0041  -0.0272 469 GLN D CG  
11550 C CD  . GLN D 168 ? 0.4619 0.3952 0.3320 -0.0882 0.0076  -0.0322 469 GLN D CD  
11551 O OE1 . GLN D 168 ? 0.4795 0.4121 0.3545 -0.0748 0.0112  -0.0332 469 GLN D OE1 
11552 N NE2 . GLN D 168 ? 0.4593 0.3673 0.3064 -0.0974 0.0067  -0.0355 469 GLN D NE2 
11553 N N   . ARG D 169 ? 0.3708 0.4012 0.3078 -0.1020 0.0001  -0.0152 470 ARG D N   
11554 C CA  . ARG D 169 ? 0.4328 0.4786 0.3711 -0.1166 -0.0034 -0.0135 470 ARG D CA  
11555 C C   . ARG D 169 ? 0.4257 0.4499 0.3406 -0.1311 -0.0056 -0.0173 470 ARG D C   
11556 O O   . ARG D 169 ? 0.4818 0.4747 0.3785 -0.1295 -0.0030 -0.0209 470 ARG D O   
11557 C CB  . ARG D 169 ? 0.5596 0.6130 0.5072 -0.1178 -0.0008 -0.0109 470 ARG D CB  
11558 C CG  . ARG D 169 ? 0.6743 0.7386 0.6192 -0.1354 -0.0031 -0.0098 470 ARG D CG  
11559 C CD  . ARG D 169 ? 0.7292 0.8072 0.6869 -0.1343 0.0002  -0.0066 470 ARG D CD  
11560 N NE  . ARG D 169 ? 0.6405 0.7469 0.6207 -0.1217 0.0005  -0.0032 470 ARG D NE  
11561 C CZ  . ARG D 169 ? 0.7615 0.8745 0.7532 -0.1125 0.0044  -0.0011 470 ARG D CZ  
11562 N NH1 . ARG D 169 ? 0.7995 0.8940 0.7832 -0.1145 0.0081  -0.0018 470 ARG D NH1 
11563 N NH2 . ARG D 169 ? 0.8100 0.9458 0.8191 -0.1009 0.0044  0.0017  470 ARG D NH2 
11564 N N   . THR D 170 ? 0.5080 0.5485 0.4222 -0.1448 -0.0106 -0.0165 471 THR D N   
11565 C CA  . THR D 170 ? 0.5289 0.5482 0.4188 -0.1612 -0.0132 -0.0201 471 THR D CA  
11566 C C   . THR D 170 ? 0.5740 0.6035 0.4639 -0.1782 -0.0145 -0.0182 471 THR D C   
11567 O O   . THR D 170 ? 0.7172 0.7245 0.5950 -0.1826 -0.0113 -0.0191 471 THR D O   
11568 C CB  . THR D 170 ? 0.5599 0.5862 0.4439 -0.1666 -0.0185 -0.0214 471 THR D CB  
11569 O OG1 . THR D 170 ? 0.5489 0.6156 0.4545 -0.1681 -0.0228 -0.0169 471 THR D OG1 
11570 C CG2 . THR D 170 ? 0.4925 0.5037 0.3716 -0.1517 -0.0163 -0.0239 471 THR D CG2 
11571 N N   . ASP D 171 ? 0.6655 0.7300 0.5690 -0.1876 -0.0191 -0.0152 472 ASP D N   
11572 C CA  . ASP D 171 ? 0.7086 0.7900 0.6146 -0.2052 -0.0203 -0.0131 472 ASP D CA  
11573 C C   . ASP D 171 ? 0.6938 0.8112 0.6277 -0.1977 -0.0181 -0.0082 472 ASP D C   
11574 O O   . ASP D 171 ? 0.7701 0.9088 0.7099 -0.2113 -0.0186 -0.0060 472 ASP D O   
11575 C CB  . ASP D 171 ? 0.7182 0.8162 0.6185 -0.2239 -0.0273 -0.0135 472 ASP D CB  
11576 C CG  . ASP D 171 ? 0.7639 0.8969 0.6838 -0.2152 -0.0321 -0.0109 472 ASP D CG  
11577 O OD1 . ASP D 171 ? 0.7207 0.8660 0.6590 -0.1955 -0.0296 -0.0085 472 ASP D OD1 
11578 O OD2 . ASP D 171 ? 0.7423 0.8893 0.6576 -0.2284 -0.0386 -0.0113 472 ASP D OD2 
11579 N N   . GLY D 172 ? 0.6266 0.7513 0.5768 -0.1769 -0.0154 -0.0066 473 GLY D N   
11580 C CA  . GLY D 172 ? 0.5723 0.7291 0.5469 -0.1680 -0.0133 -0.0023 473 GLY D CA  
11581 C C   . GLY D 172 ? 0.5857 0.7841 0.5791 -0.1664 -0.0182 0.0010  473 GLY D C   
11582 O O   . GLY D 172 ? 0.6012 0.8253 0.6146 -0.1547 -0.0165 0.0044  473 GLY D O   
11583 N N   . LYS D 173 ? 0.5904 0.7957 0.5769 -0.1772 -0.0245 0.0000  474 LYS D N   
11584 C CA  . LYS D 173 ? 0.6622 0.9066 0.6650 -0.1747 -0.0303 0.0032  474 LYS D CA  
11585 C C   . LYS D 173 ? 0.7030 0.9405 0.7048 -0.1601 -0.0330 0.0031  474 LYS D C   
11586 O O   . LYS D 173 ? 0.6750 0.9415 0.6888 -0.1549 -0.0381 0.0061  474 LYS D O   
11587 C CB  . LYS D 173 ? 0.7212 0.9826 0.7178 -0.1976 -0.0364 0.0027  474 LYS D CB  
11588 C CG  . LYS D 173 ? 0.7752 1.0458 0.7718 -0.2150 -0.0338 0.0032  474 LYS D CG  
11589 C CD  . LYS D 173 ? 0.8082 1.1000 0.7997 -0.2393 -0.0404 0.0031  474 LYS D CD  
11590 C CE  . LYS D 173 ? 0.7854 1.0768 0.7713 -0.2523 -0.0357 0.0041  474 LYS D CE  
11591 N NZ  . LYS D 173 ? 0.7424 1.0544 0.7241 -0.2663 -0.0396 0.0057  474 LYS D NZ  
11592 N N   . HIS D 174 ? 0.6761 0.8767 0.6637 -0.1530 -0.0296 0.0000  475 HIS D N   
11593 C CA  . HIS D 174 ? 0.5757 0.7668 0.5595 -0.1412 -0.0313 -0.0005 475 HIS D CA  
11594 C C   . HIS D 174 ? 0.4624 0.6363 0.4500 -0.1234 -0.0252 -0.0004 475 HIS D C   
11595 O O   . HIS D 174 ? 0.4414 0.5926 0.4184 -0.1170 -0.0238 -0.0026 475 HIS D O   
11596 C CB  . HIS D 174 ? 0.6265 0.7910 0.5867 -0.1518 -0.0337 -0.0050 475 HIS D CB  
11597 C CG  . HIS D 174 ? 0.7272 0.9081 0.6817 -0.1699 -0.0408 -0.0052 475 HIS D CG  
11598 N ND1 . HIS D 174 ? 0.7316 0.9208 0.6841 -0.1877 -0.0418 -0.0054 475 HIS D ND1 
11599 C CD2 . HIS D 174 ? 0.6505 0.8414 0.6000 -0.1740 -0.0477 -0.0050 475 HIS D CD2 
11600 C CE1 . HIS D 174 ? 0.6858 0.8906 0.6330 -0.2026 -0.0491 -0.0056 475 HIS D CE1 
11601 N NE2 . HIS D 174 ? 0.7219 0.9280 0.6672 -0.1942 -0.0530 -0.0053 475 HIS D NE2 
11602 N N   . ASP D 175 ? 0.4225 0.6075 0.4245 -0.1159 -0.0213 0.0021  476 ASP D N   
11603 C CA  . ASP D 175 ? 0.3658 0.5340 0.3704 -0.1011 -0.0157 0.0020  476 ASP D CA  
11604 C C   . ASP D 175 ? 0.3279 0.4988 0.3368 -0.0869 -0.0169 0.0039  476 ASP D C   
11605 O O   . ASP D 175 ? 0.3802 0.5749 0.3981 -0.0830 -0.0212 0.0073  476 ASP D O   
11606 C CB  . ASP D 175 ? 0.4265 0.6073 0.4448 -0.0964 -0.0117 0.0044  476 ASP D CB  
11607 C CG  . ASP D 175 ? 0.4375 0.6062 0.4484 -0.1082 -0.0085 0.0024  476 ASP D CG  
11608 O OD1 . ASP D 175 ? 0.4281 0.5783 0.4225 -0.1205 -0.0099 -0.0008 476 ASP D OD1 
11609 O OD2 . ASP D 175 ? 0.4620 0.6378 0.4818 -0.1051 -0.0047 0.0040  476 ASP D OD2 
11610 N N   . PHE D 176 ? 0.2908 0.4373 0.2923 -0.0792 -0.0131 0.0019  477 PHE D N   
11611 C CA  . PHE D 176 ? 0.2984 0.4447 0.3047 -0.0652 -0.0123 0.0042  477 PHE D CA  
11612 C C   . PHE D 176 ? 0.2793 0.4298 0.2972 -0.0558 -0.0082 0.0062  477 PHE D C   
11613 O O   . PHE D 176 ? 0.3164 0.4548 0.3331 -0.0574 -0.0040 0.0043  477 PHE D O   
11614 C CB  . PHE D 176 ? 0.2662 0.3873 0.2598 -0.0626 -0.0097 0.0010  477 PHE D CB  
11615 C CG  . PHE D 176 ? 0.2968 0.4141 0.2781 -0.0690 -0.0136 -0.0006 477 PHE D CG  
11616 C CD1 . PHE D 176 ? 0.2878 0.3994 0.2585 -0.0820 -0.0156 -0.0038 477 PHE D CD1 
11617 C CD2 . PHE D 176 ? 0.3065 0.4242 0.2850 -0.0628 -0.0154 0.0011  477 PHE D CD2 
11618 C CE1 . PHE D 176 ? 0.3683 0.4753 0.3259 -0.0884 -0.0194 -0.0056 477 PHE D CE1 
11619 C CE2 . PHE D 176 ? 0.3657 0.4796 0.3316 -0.0688 -0.0190 -0.0004 477 PHE D CE2 
11620 C CZ  . PHE D 176 ? 0.3751 0.4839 0.3308 -0.0815 -0.0210 -0.0039 477 PHE D CZ  
11621 N N   . ARG D 177 ? 0.2435 0.4100 0.2710 -0.0458 -0.0097 0.0101  478 ARG D N   
11622 C CA  . ARG D 177 ? 0.3540 0.5229 0.3904 -0.0361 -0.0058 0.0119  478 ARG D CA  
11623 C C   . ARG D 177 ? 0.3099 0.4766 0.3466 -0.0230 -0.0064 0.0147  478 ARG D C   
11624 O O   . ARG D 177 ? 0.3319 0.5103 0.3688 -0.0195 -0.0110 0.0173  478 ARG D O   
11625 C CB  . ARG D 177 ? 0.2821 0.4766 0.3307 -0.0376 -0.0062 0.0139  478 ARG D CB  
11626 C CG  . ARG D 177 ? 0.3494 0.5446 0.3968 -0.0513 -0.0047 0.0116  478 ARG D CG  
11627 C CD  . ARG D 177 ? 0.3836 0.5548 0.4255 -0.0509 0.0007  0.0092  478 ARG D CD  
11628 N NE  . ARG D 177 ? 0.3645 0.5376 0.4140 -0.0396 0.0045  0.0109  478 ARG D NE  
11629 C CZ  . ARG D 177 ? 0.3912 0.5769 0.4483 -0.0401 0.0073  0.0120  478 ARG D CZ  
11630 N NH1 . ARG D 177 ? 0.2893 0.4883 0.3481 -0.0522 0.0068  0.0118  478 ARG D NH1 
11631 N NH2 . ARG D 177 ? 0.3754 0.5595 0.4369 -0.0292 0.0107  0.0132  478 ARG D NH2 
11632 N N   . VAL D 178 ? 0.2551 0.4062 0.2903 -0.0162 -0.0021 0.0143  479 VAL D N   
11633 C CA  . VAL D 178 ? 0.2751 0.4239 0.3103 -0.0039 -0.0020 0.0174  479 VAL D CA  
11634 C C   . VAL D 178 ? 0.3081 0.4717 0.3534 0.0025  -0.0004 0.0192  479 VAL D C   
11635 O O   . VAL D 178 ? 0.3003 0.4598 0.3486 0.0009  0.0037  0.0175  479 VAL D O   
11636 C CB  . VAL D 178 ? 0.2257 0.3510 0.2533 -0.0013 0.0018  0.0160  479 VAL D CB  
11637 C CG1 . VAL D 178 ? 0.2296 0.3495 0.2544 0.0100  0.0018  0.0191  479 VAL D CG1 
11638 C CG2 . VAL D 178 ? 0.2534 0.3672 0.2717 -0.0074 0.0010  0.0140  479 VAL D CG2 
11639 N N   . TRP D 179 ? 0.2699 0.4523 0.3202 0.0100  -0.0038 0.0225  480 TRP D N   
11640 C CA  . TRP D 179 ? 0.1891 0.3889 0.2496 0.0168  -0.0018 0.0239  480 TRP D CA  
11641 C C   . TRP D 179 ? 0.2713 0.4544 0.3276 0.0280  0.0023  0.0244  480 TRP D C   
11642 O O   . TRP D 179 ? 0.2938 0.4841 0.3563 0.0316  0.0060  0.0242  480 TRP D O   
11643 C CB  . TRP D 179 ? 0.2414 0.4688 0.3091 0.0233  -0.0066 0.0273  480 TRP D CB  
11644 C CG  . TRP D 179 ? 0.2368 0.4872 0.3114 0.0106  -0.0101 0.0268  480 TRP D CG  
11645 C CD1 . TRP D 179 ? 0.2730 0.5147 0.3419 -0.0042 -0.0115 0.0241  480 TRP D CD1 
11646 C CD2 . TRP D 179 ? 0.2635 0.5496 0.3510 0.0110  -0.0127 0.0288  480 TRP D CD2 
11647 N NE1 . TRP D 179 ? 0.2710 0.5385 0.3468 -0.0143 -0.0151 0.0243  480 TRP D NE1 
11648 C CE2 . TRP D 179 ? 0.1867 0.4837 0.2751 -0.0058 -0.0160 0.0273  480 TRP D CE2 
11649 C CE3 . TRP D 179 ? 0.2692 0.5799 0.3671 0.0242  -0.0124 0.0317  480 TRP D CE3 
11650 C CZ2 . TRP D 179 ? 0.1998 0.5329 0.3000 -0.0117 -0.0192 0.0287  480 TRP D CZ2 
11651 C CZ3 . TRP D 179 ? 0.2901 0.6392 0.4013 0.0200  -0.0153 0.0331  480 TRP D CZ3 
11652 C CH2 . TRP D 179 ? 0.2463 0.6071 0.3589 0.0013  -0.0189 0.0317  480 TRP D CH2 
11653 N N   . ASN D 180 ? 0.2466 0.4073 0.2916 0.0324  0.0019  0.0249  481 ASN D N   
11654 C CA  . ASN D 180 ? 0.2509 0.3921 0.2893 0.0401  0.0056  0.0249  481 ASN D CA  
11655 C C   . ASN D 180 ? 0.3660 0.4985 0.4064 0.0327  0.0102  0.0216  481 ASN D C   
11656 O O   . ASN D 180 ? 0.3453 0.4739 0.3858 0.0220  0.0104  0.0191  481 ASN D O   
11657 C CB  . ASN D 180 ? 0.2403 0.3585 0.2648 0.0420  0.0044  0.0258  481 ASN D CB  
11658 C CG  . ASN D 180 ? 0.3261 0.4500 0.3460 0.0479  -0.0009 0.0292  481 ASN D CG  
11659 O OD1 . ASN D 180 ? 0.3273 0.4644 0.3507 0.0418  -0.0045 0.0293  481 ASN D OD1 
11660 N ND2 . ASN D 180 ? 0.3565 0.4690 0.3668 0.0601  -0.0016 0.0321  481 ASN D ND2 
11661 N N   . SER D 181 ? 0.2337 0.3617 0.2741 0.0392  0.0139  0.0215  482 SER D N   
11662 C CA  . SER D 181 ? 0.3031 0.4207 0.3435 0.0331  0.0178  0.0187  482 SER D CA  
11663 C C   . SER D 181 ? 0.2858 0.3802 0.3165 0.0299  0.0181  0.0173  482 SER D C   
11664 O O   . SER D 181 ? 0.2411 0.3295 0.2723 0.0220  0.0194  0.0148  482 SER D O   
11665 C CB  . SER D 181 ? 0.2253 0.3447 0.2673 0.0407  0.0215  0.0188  482 SER D CB  
11666 O OG  . SER D 181 ? 0.2787 0.3844 0.3111 0.0517  0.0216  0.0203  482 SER D OG  
11667 N N   . GLN D 182 ? 0.2674 0.3490 0.2886 0.0360  0.0169  0.0190  483 GLN D N   
11668 C CA  . GLN D 182 ? 0.2551 0.3182 0.2669 0.0315  0.0169  0.0182  483 GLN D CA  
11669 C C   . GLN D 182 ? 0.3240 0.3833 0.3280 0.0340  0.0136  0.0208  483 GLN D C   
11670 O O   . GLN D 182 ? 0.2896 0.3540 0.2919 0.0429  0.0114  0.0236  483 GLN D O   
11671 C CB  . GLN D 182 ? 0.3019 0.3470 0.3054 0.0341  0.0194  0.0177  483 GLN D CB  
11672 C CG  . GLN D 182 ? 0.3274 0.3735 0.3365 0.0308  0.0224  0.0152  483 GLN D CG  
11673 C CD  . GLN D 182 ? 0.4666 0.5089 0.4728 0.0388  0.0246  0.0156  483 GLN D CD  
11674 O OE1 . GLN D 182 ? 0.5769 0.6314 0.5909 0.0403  0.0264  0.0151  483 GLN D OE1 
11675 N NE2 . GLN D 182 ? 0.4114 0.4355 0.4047 0.0433  0.0247  0.0165  483 GLN D NE2 
11676 N N   . LEU D 183 ? 0.2394 0.2903 0.2381 0.0267  0.0132  0.0199  484 LEU D N   
11677 C CA  . LEU D 183 ? 0.2681 0.3157 0.2585 0.0273  0.0101  0.0223  484 LEU D CA  
11678 C C   . LEU D 183 ? 0.3543 0.3874 0.3320 0.0363  0.0090  0.0257  484 LEU D C   
11679 O O   . LEU D 183 ? 0.3344 0.3696 0.3071 0.0424  0.0054  0.0288  484 LEU D O   
11680 C CB  . LEU D 183 ? 0.2343 0.2740 0.2198 0.0180  0.0112  0.0205  484 LEU D CB  
11681 C CG  . LEU D 183 ? 0.2544 0.3046 0.2483 0.0102  0.0120  0.0171  484 LEU D CG  
11682 C CD1 . LEU D 183 ? 0.2767 0.3194 0.2643 0.0033  0.0136  0.0155  484 LEU D CD1 
11683 C CD2 . LEU D 183 ? 0.2128 0.2781 0.2120 0.0099  0.0088  0.0176  484 LEU D CD2 
11684 N N   . ILE D 184 ? 0.2492 0.2662 0.2198 0.0373  0.0116  0.0252  485 ILE D N   
11685 C CA  . ILE D 184 ? 0.3144 0.3116 0.2688 0.0453  0.0110  0.0280  485 ILE D CA  
11686 C C   . ILE D 184 ? 0.3899 0.3863 0.3464 0.0534  0.0132  0.0272  485 ILE D C   
11687 O O   . ILE D 184 ? 0.3125 0.3060 0.2724 0.0484  0.0161  0.0245  485 ILE D O   
11688 C CB  . ILE D 184 ? 0.3412 0.3160 0.2805 0.0372  0.0122  0.0280  485 ILE D CB  
11689 C CG1 . ILE D 184 ? 0.3766 0.3534 0.3128 0.0300  0.0105  0.0289  485 ILE D CG1 
11690 C CG2 . ILE D 184 ? 0.3347 0.2844 0.2538 0.0444  0.0116  0.0307  485 ILE D CG2 
11691 C CD1 . ILE D 184 ? 0.3607 0.3283 0.2914 0.0179  0.0131  0.0273  485 ILE D CD1 
11692 N N   . ARG D 185 ? 0.3435 0.3444 0.2986 0.0665  0.0117  0.0296  486 ARG D N   
11693 C CA  . ARG D 185 ? 0.3668 0.3653 0.3209 0.0766  0.0141  0.0291  486 ARG D CA  
11694 C C   . ARG D 185 ? 0.4492 0.4377 0.3897 0.0921  0.0119  0.0326  486 ARG D C   
11695 O O   . ARG D 185 ? 0.4003 0.3901 0.3364 0.0951  0.0079  0.0356  486 ARG D O   
11696 C CB  . ARG D 185 ? 0.3001 0.3270 0.2743 0.0778  0.0158  0.0275  486 ARG D CB  
11697 C CG  . ARG D 185 ? 0.3170 0.3521 0.3030 0.0643  0.0179  0.0241  486 ARG D CG  
11698 C CD  . ARG D 185 ? 0.3865 0.4412 0.3861 0.0659  0.0206  0.0227  486 ARG D CD  
11699 N NE  . ARG D 185 ? 0.4038 0.4467 0.3965 0.0728  0.0241  0.0218  486 ARG D NE  
11700 C CZ  . ARG D 185 ? 0.3747 0.4294 0.3757 0.0738  0.0275  0.0203  486 ARG D CZ  
11701 N NH1 . ARG D 185 ? 0.2618 0.3397 0.2781 0.0675  0.0278  0.0196  486 ARG D NH1 
11702 N NH2 . ARG D 185 ? 0.3540 0.3957 0.3462 0.0804  0.0306  0.0194  486 ARG D NH2 
11703 N N   . TYR D 186 ? 0.3748 0.3526 0.3074 0.1028  0.0144  0.0323  487 TYR D N   
11704 C CA  . TYR D 186 ? 0.4260 0.3909 0.3430 0.1200  0.0127  0.0353  487 TYR D CA  
11705 C C   . TYR D 186 ? 0.4139 0.4094 0.3467 0.1338  0.0130  0.0359  487 TYR D C   
11706 O O   . TYR D 186 ? 0.4232 0.4386 0.3718 0.1317  0.0165  0.0334  487 TYR D O   
11707 C CB  . TYR D 186 ? 0.3633 0.2932 0.2574 0.1244  0.0154  0.0344  487 TYR D CB  
11708 C CG  . TYR D 186 ? 0.4619 0.3618 0.3383 0.1106  0.0148  0.0343  487 TYR D CG  
11709 C CD1 . TYR D 186 ? 0.4500 0.3374 0.3232 0.0988  0.0178  0.0310  487 TYR D CD1 
11710 C CD2 . TYR D 186 ? 0.4570 0.3434 0.3201 0.1084  0.0110  0.0376  487 TYR D CD2 
11711 C CE1 . TYR D 186 ? 0.4423 0.3063 0.3004 0.0850  0.0172  0.0310  487 TYR D CE1 
11712 C CE2 . TYR D 186 ? 0.4583 0.3197 0.3053 0.0945  0.0109  0.0377  487 TYR D CE2 
11713 C CZ  . TYR D 186 ? 0.4706 0.3223 0.3159 0.0825  0.0141  0.0344  487 TYR D CZ  
11714 O OH  . TYR D 186 ? 0.4809 0.3114 0.3112 0.0677  0.0140  0.0345  487 TYR D OH  
11715 N N   . ALA D 187 ? 0.4480 0.4478 0.3757 0.1478  0.0091  0.0396  488 ALA D N   
11716 C CA  . ALA D 187 ? 0.4182 0.4500 0.3607 0.1624  0.0090  0.0406  488 ALA D CA  
11717 C C   . ALA D 187 ? 0.4575 0.4824 0.3942 0.1758  0.0142  0.0388  488 ALA D C   
11718 O O   . ALA D 187 ? 0.4589 0.4484 0.3745 0.1776  0.0166  0.0377  488 ALA D O   
11719 C CB  . ALA D 187 ? 0.4016 0.4373 0.3373 0.1766  0.0031  0.0452  488 ALA D CB  
11720 N N   . GLY D 188 ? 0.3986 0.4587 0.3538 0.1849  0.0160  0.0386  489 GLY D N   
11721 C CA  . GLY D 188 ? 0.4005 0.4606 0.3519 0.2005  0.0212  0.0371  489 GLY D CA  
11722 C C   . GLY D 188 ? 0.4395 0.5321 0.4013 0.2201  0.0196  0.0397  489 GLY D C   
11723 O O   . GLY D 188 ? 0.4746 0.6040 0.4572 0.2155  0.0162  0.0413  489 GLY D O   
11724 N N   . TYR D 189 ? 0.4196 0.4997 0.3666 0.2421  0.0219  0.0401  490 TYR D N   
11725 C CA  . TYR D 189 ? 0.5499 0.6588 0.5039 0.2639  0.0199  0.0429  490 TYR D CA  
11726 C C   . TYR D 189 ? 0.5987 0.7157 0.5529 0.2723  0.0267  0.0396  490 TYR D C   
11727 O O   . TYR D 189 ? 0.6918 0.7725 0.6241 0.2771  0.0309  0.0373  490 TYR D O   
11728 C CB  . TYR D 189 ? 0.5225 0.6004 0.4507 0.2761  0.0142  0.0462  490 TYR D CB  
11729 C CG  . TYR D 189 ? 0.5514 0.6108 0.4722 0.2647  0.0077  0.0493  490 TYR D CG  
11730 C CD1 . TYR D 189 ? 0.5330 0.5429 0.4281 0.2547  0.0080  0.0485  490 TYR D CD1 
11731 C CD2 . TYR D 189 ? 0.5916 0.6828 0.5299 0.2589  0.0015  0.0521  490 TYR D CD2 
11732 C CE1 . TYR D 189 ? 0.5964 0.5904 0.4843 0.2399  0.0030  0.0506  490 TYR D CE1 
11733 C CE2 . TYR D 189 ? 0.6324 0.7056 0.5622 0.2446  -0.0037 0.0540  490 TYR D CE2 
11734 C CZ  . TYR D 189 ? 0.6196 0.6449 0.5246 0.2355  -0.0027 0.0532  490 TYR D CZ  
11735 O OH  . TYR D 189 ? 0.5779 0.5883 0.4752 0.2211  -0.0072 0.0551  490 TYR D OH  
11736 N N   . LYS D 190 ? 0.6200 0.7837 0.5976 0.2729  0.0277  0.0395  491 LYS D N   
11737 C CA  . LYS D 190 ? 0.7108 0.8851 0.6872 0.2840  0.0332  0.0374  491 LYS D CA  
11738 C C   . LYS D 190 ? 0.7175 0.8699 0.6705 0.3041  0.0307  0.0389  491 LYS D C   
11739 O O   . LYS D 190 ? 0.7247 0.8902 0.6800 0.3105  0.0246  0.0421  491 LYS D O   
11740 C CB  . LYS D 190 ? 0.7372 0.9675 0.7434 0.2787  0.0342  0.0374  491 LYS D CB  
11741 C CG  . LYS D 190 ? 0.7512 1.0035 0.7788 0.2584  0.0377  0.0355  491 LYS D CG  
11742 C CD  . LYS D 190 ? 0.8714 1.1469 0.9089 0.2578  0.0450  0.0329  491 LYS D CD  
11743 C CE  . LYS D 190 ? 0.9622 1.2002 0.9778 0.2661  0.0511  0.0299  491 LYS D CE  
11744 N NZ  . LYS D 190 ? 1.0024 1.2081 1.0095 0.2545  0.0526  0.0282  491 LYS D NZ  
11745 N N   . GLN D 191 ? 0.8091 0.9272 0.7384 0.3137  0.0352  0.0367  492 GLN D N   
11746 C CA  . GLN D 191 ? 0.8831 0.9764 0.7867 0.3330  0.0336  0.0377  492 GLN D CA  
11747 C C   . GLN D 191 ? 0.9169 1.0464 0.8313 0.3472  0.0361  0.0375  492 GLN D C   
11748 O O   . GLN D 191 ? 0.8694 1.0364 0.8072 0.3412  0.0403  0.0360  492 GLN D O   
11749 C CB  . GLN D 191 ? 0.8933 0.9323 0.7643 0.3358  0.0373  0.0351  492 GLN D CB  
11750 C CG  . GLN D 191 ? 0.8672 0.8636 0.7205 0.3242  0.0341  0.0357  492 GLN D CG  
11751 C CD  . GLN D 191 ? 0.9035 0.8798 0.7401 0.3305  0.0270  0.0395  492 GLN D CD  
11752 O OE1 . GLN D 191 ? 0.8754 0.8823 0.7297 0.3310  0.0219  0.0426  492 GLN D OE1 
11753 N NE2 . GLN D 191 ? 0.9802 0.9039 0.7810 0.3344  0.0264  0.0392  492 GLN D NE2 
11754 N N   . PRO D 192 ? 0.9863 1.1055 0.8832 0.3660  0.0334  0.0392  493 PRO D N   
11755 C CA  . PRO D 192 ? 0.9215 1.0733 0.8262 0.3817  0.0362  0.0389  493 PRO D CA  
11756 C C   . PRO D 192 ? 0.9319 1.0822 0.8343 0.3838  0.0446  0.0353  493 PRO D C   
11757 O O   . PRO D 192 ? 0.8320 1.0259 0.7574 0.3833  0.0482  0.0345  493 PRO D O   
11758 C CB  . PRO D 192 ? 0.9109 1.0353 0.7878 0.4021  0.0323  0.0409  493 PRO D CB  
11759 C CG  . PRO D 192 ? 0.9069 1.0077 0.7754 0.3942  0.0253  0.0435  493 PRO D CG  
11760 C CD  . PRO D 192 ? 0.9495 1.0332 0.8218 0.3732  0.0271  0.0419  493 PRO D CD  
11761 N N   . ASP D 193 ? 0.9014 1.0021 0.7754 0.3850  0.0477  0.0330  494 ASP D N   
11762 C CA  . ASP D 193 ? 0.8337 0.9293 0.7018 0.3886  0.0553  0.0295  494 ASP D CA  
11763 C C   . ASP D 193 ? 0.8233 0.9440 0.7166 0.3698  0.0599  0.0273  494 ASP D C   
11764 O O   . ASP D 193 ? 0.8275 0.9559 0.7225 0.3717  0.0665  0.0247  494 ASP D O   
11765 C CB  . ASP D 193 ? 0.9099 0.9435 0.7388 0.3934  0.0568  0.0277  494 ASP D CB  
11766 C CG  . ASP D 193 ? 0.9804 0.9782 0.7992 0.3763  0.0538  0.0276  494 ASP D CG  
11767 O OD1 . ASP D 193 ? 1.0128 0.9585 0.7978 0.3783  0.0532  0.0268  494 ASP D OD1 
11768 O OD2 . ASP D 193 ? 0.9747 0.9960 0.8183 0.3603  0.0521  0.0283  494 ASP D OD2 
11769 N N   . GLY D 194 ? 0.8068 0.9401 0.7185 0.3519  0.0567  0.0283  495 GLY D N   
11770 C CA  . GLY D 194 ? 0.6667 0.8224 0.6010 0.3335  0.0608  0.0264  495 GLY D CA  
11771 C C   . GLY D 194 ? 0.7188 0.8392 0.6434 0.3184  0.0612  0.0247  495 GLY D C   
11772 O O   . GLY D 194 ? 0.7265 0.8654 0.6704 0.3019  0.0635  0.0235  495 GLY D O   
11773 N N   . SER D 195 ? 0.7221 0.7922 0.6167 0.3229  0.0591  0.0246  496 SER D N   
11774 C CA  . SER D 195 ? 0.7380 0.7735 0.6220 0.3085  0.0587  0.0232  496 SER D CA  
11775 C C   . SER D 195 ? 0.6987 0.7463 0.5979 0.2977  0.0527  0.0261  496 SER D C   
11776 O O   . SER D 195 ? 0.6455 0.7289 0.5638 0.3000  0.0489  0.0289  496 SER D O   
11777 C CB  . SER D 195 ? 0.7928 0.7709 0.6380 0.3155  0.0581  0.0223  496 SER D CB  
11778 O OG  . SER D 195 ? 0.8274 0.7904 0.6575 0.3262  0.0523  0.0255  496 SER D OG  
11779 N N   . THR D 196 ? 0.6320 0.6498 0.5222 0.2853  0.0515  0.0255  497 THR D N   
11780 C CA  . THR D 196 ? 0.6046 0.6313 0.5080 0.2742  0.0464  0.0280  497 THR D CA  
11781 C C   . THR D 196 ? 0.5913 0.5682 0.4666 0.2729  0.0421  0.0293  497 THR D C   
11782 O O   . THR D 196 ? 0.6270 0.5638 0.4794 0.2693  0.0447  0.0268  497 THR D O   
11783 C CB  . THR D 196 ? 0.5564 0.6037 0.4821 0.2570  0.0497  0.0261  497 THR D CB  
11784 O OG1 . THR D 196 ? 0.5597 0.6549 0.5116 0.2555  0.0529  0.0255  497 THR D OG1 
11785 C CG2 . THR D 196 ? 0.5573 0.6077 0.4924 0.2387  0.0431  0.0283  497 THR D CG2 
11786 N N   . LEU D 197 ? 0.6337 0.6128 0.5095 0.2745  0.0355  0.0334  498 LEU D N   
11787 C CA  . LEU D 197 ? 0.6442 0.5794 0.4950 0.2704  0.0308  0.0355  498 LEU D CA  
11788 C C   . LEU D 197 ? 0.5990 0.5447 0.4663 0.2442  0.0279  0.0357  498 LEU D C   
11789 O O   . LEU D 197 ? 0.5181 0.5052 0.4130 0.2380  0.0260  0.0367  498 LEU D O   
11790 C CB  . LEU D 197 ? 0.6711 0.6005 0.5093 0.2826  0.0249  0.0393  498 LEU D CB  
11791 C CG  . LEU D 197 ? 0.7174 0.6048 0.5308 0.2762  0.0196  0.0424  498 LEU D CG  
11792 C CD1 . LEU D 197 ? 0.8418 0.6756 0.6208 0.2733  0.0223  0.0399  498 LEU D CD1 
11793 C CD2 . LEU D 197 ? 0.7136 0.6034 0.5196 0.2873  0.0134  0.0464  498 LEU D CD2 
11794 N N   . GLY D 198 ? 0.5435 0.4525 0.3933 0.2280  0.0276  0.0343  499 GLY D N   
11795 C CA  . GLY D 198 ? 0.4851 0.4034 0.3494 0.2035  0.0255  0.0339  499 GLY D CA  
11796 C C   . GLY D 198 ? 0.4888 0.4285 0.3737 0.1900  0.0300  0.0300  499 GLY D C   
11797 O O   . GLY D 198 ? 0.5519 0.4841 0.4314 0.1943  0.0350  0.0271  499 GLY D O   
11798 N N   . ASP D 199 ? 0.4366 0.4018 0.3436 0.1736  0.0282  0.0300  500 ASP D N   
11799 C CA  . ASP D 199 ? 0.3669 0.3503 0.2919 0.1595  0.0317  0.0268  500 ASP D CA  
11800 C C   . ASP D 199 ? 0.4039 0.4282 0.3517 0.1666  0.0344  0.0266  500 ASP D C   
11801 O O   . ASP D 199 ? 0.3769 0.4310 0.3422 0.1648  0.0314  0.0285  500 ASP D O   
11802 C CB  . ASP D 199 ? 0.3751 0.3640 0.3106 0.1395  0.0287  0.0267  500 ASP D CB  
11803 C CG  . ASP D 199 ? 0.4543 0.4500 0.4009 0.1250  0.0319  0.0233  500 ASP D CG  
11804 O OD1 . ASP D 199 ? 0.5035 0.5100 0.4558 0.1296  0.0362  0.0215  500 ASP D OD1 
11805 O OD2 . ASP D 199 ? 0.4185 0.4090 0.3673 0.1096  0.0302  0.0226  500 ASP D OD2 
11806 N N   . PRO D 200 ? 0.4700 0.4981 0.4184 0.1726  0.0402  0.0241  501 PRO D N   
11807 C CA  . PRO D 200 ? 0.3640 0.4336 0.3342 0.1781  0.0434  0.0240  501 PRO D CA  
11808 C C   . PRO D 200 ? 0.3575 0.4566 0.3511 0.1599  0.0426  0.0237  501 PRO D C   
11809 O O   . PRO D 200 ? 0.4139 0.5502 0.4262 0.1620  0.0429  0.0248  501 PRO D O   
11810 C CB  . PRO D 200 ? 0.3584 0.4183 0.3200 0.1851  0.0503  0.0209  501 PRO D CB  
11811 C CG  . PRO D 200 ? 0.4264 0.4398 0.3579 0.1925  0.0496  0.0204  501 PRO D CG  
11812 C CD  . PRO D 200 ? 0.3691 0.3633 0.2955 0.1766  0.0440  0.0215  501 PRO D CD  
11813 N N   . ALA D 201 ? 0.3239 0.4075 0.3160 0.1422  0.0415  0.0222  502 ALA D N   
11814 C CA  . ALA D 201 ? 0.3921 0.4983 0.4027 0.1256  0.0404  0.0218  502 ALA D CA  
11815 C C   . ALA D 201 ? 0.4946 0.6225 0.5163 0.1243  0.0352  0.0245  502 ALA D C   
11816 O O   . ALA D 201 ? 0.4065 0.5624 0.4451 0.1151  0.0347  0.0246  502 ALA D O   
11817 C CB  . ALA D 201 ? 0.3648 0.4476 0.3692 0.1098  0.0395  0.0199  502 ALA D CB  
11818 N N   . ASN D 202 ? 0.4661 0.5804 0.4769 0.1329  0.0309  0.0268  503 ASN D N   
11819 C CA  . ASN D 202 ? 0.3872 0.5179 0.4057 0.1304  0.0252  0.0294  503 ASN D CA  
11820 C C   . ASN D 202 ? 0.4419 0.5977 0.4664 0.1471  0.0233  0.0323  503 ASN D C   
11821 O O   . ASN D 202 ? 0.3810 0.5468 0.4078 0.1484  0.0177  0.0349  503 ASN D O   
11822 C CB  . ASN D 202 ? 0.2992 0.3993 0.3017 0.1262  0.0212  0.0304  503 ASN D CB  
11823 C CG  . ASN D 202 ? 0.2888 0.3723 0.2895 0.1090  0.0225  0.0277  503 ASN D CG  
11824 O OD1 . ASN D 202 ? 0.3974 0.4969 0.4116 0.0981  0.0242  0.0257  503 ASN D OD1 
11825 N ND2 . ASN D 202 ? 0.2960 0.3476 0.2792 0.1066  0.0218  0.0275  503 ASN D ND2 
11826 N N   . VAL D 203 ? 0.3774 0.5456 0.4046 0.1602  0.0280  0.0317  504 VAL D N   
11827 C CA  . VAL D 203 ? 0.4168 0.6117 0.4503 0.1785  0.0265  0.0344  504 VAL D CA  
11828 C C   . VAL D 203 ? 0.4005 0.6380 0.4564 0.1699  0.0228  0.0359  504 VAL D C   
11829 O O   . VAL D 203 ? 0.4941 0.7459 0.5523 0.1778  0.0169  0.0391  504 VAL D O   
11830 C CB  . VAL D 203 ? 0.3921 0.5954 0.4257 0.1933  0.0335  0.0329  504 VAL D CB  
11831 C CG1 . VAL D 203 ? 0.3139 0.5587 0.3618 0.2095  0.0327  0.0353  504 VAL D CG1 
11832 C CG2 . VAL D 203 ? 0.3840 0.5428 0.3907 0.2061  0.0354  0.0320  504 VAL D CG2 
11833 N N   . GLN D 204 ? 0.3445 0.6012 0.4153 0.1529  0.0256  0.0338  505 GLN D N   
11834 C CA  . GLN D 204 ? 0.3114 0.6070 0.4015 0.1423  0.0221  0.0350  505 GLN D CA  
11835 C C   . GLN D 204 ? 0.3387 0.6244 0.4251 0.1322  0.0148  0.0363  505 GLN D C   
11836 O O   . GLN D 204 ? 0.3038 0.6146 0.3982 0.1340  0.0091  0.0389  505 GLN D O   
11837 C CB  . GLN D 204 ? 0.2575 0.5686 0.3597 0.1246  0.0269  0.0325  505 GLN D CB  
11838 C CG  . GLN D 204 ? 0.3852 0.7370 0.5057 0.1126  0.0237  0.0336  505 GLN D CG  
11839 C CD  . GLN D 204 ? 0.4459 0.8042 0.5733 0.0917  0.0274  0.0312  505 GLN D CD  
11840 O OE1 . GLN D 204 ? 0.5247 0.8522 0.6423 0.0826  0.0299  0.0289  505 GLN D OE1 
11841 N NE2 . GLN D 204 ? 0.4631 0.8619 0.6067 0.0837  0.0277  0.0320  505 GLN D NE2 
11842 N N   . PHE D 205 ? 0.3197 0.5706 0.3939 0.1213  0.0148  0.0346  506 PHE D N   
11843 C CA  . PHE D 205 ? 0.3477 0.5881 0.4168 0.1125  0.0087  0.0356  506 PHE D CA  
11844 C C   . PHE D 205 ? 0.3601 0.5939 0.4189 0.1284  0.0035  0.0392  506 PHE D C   
11845 O O   . PHE D 205 ? 0.3132 0.5606 0.3750 0.1262  -0.0027 0.0414  506 PHE D O   
11846 C CB  . PHE D 205 ? 0.3253 0.5306 0.3829 0.1002  0.0105  0.0330  506 PHE D CB  
11847 C CG  . PHE D 205 ? 0.4024 0.5983 0.4552 0.0901  0.0054  0.0335  506 PHE D CG  
11848 C CD1 . PHE D 205 ? 0.3872 0.6019 0.4504 0.0756  0.0031  0.0325  506 PHE D CD1 
11849 C CD2 . PHE D 205 ? 0.3657 0.5333 0.4018 0.0948  0.0031  0.0349  506 PHE D CD2 
11850 C CE1 . PHE D 205 ? 0.3243 0.5298 0.3816 0.0669  -0.0013 0.0326  506 PHE D CE1 
11851 C CE2 . PHE D 205 ? 0.4306 0.5907 0.4617 0.0854  -0.0010 0.0353  506 PHE D CE2 
11852 C CZ  . PHE D 205 ? 0.3473 0.5265 0.3892 0.0720  -0.0031 0.0340  506 PHE D CZ  
11853 N N   . THR D 206 ? 0.2570 0.4686 0.3016 0.1447  0.0057  0.0399  507 THR D N   
11854 C CA  . THR D 206 ? 0.3272 0.5285 0.3586 0.1615  0.0009  0.0437  507 THR D CA  
11855 C C   . THR D 206 ? 0.3753 0.6181 0.4213 0.1727  -0.0034 0.0467  507 THR D C   
11856 O O   . THR D 206 ? 0.4103 0.6570 0.4524 0.1768  -0.0103 0.0499  507 THR D O   
11857 C CB  . THR D 206 ? 0.3416 0.5114 0.3538 0.1774  0.0047  0.0435  507 THR D CB  
11858 O OG1 . THR D 206 ? 0.3725 0.5058 0.3714 0.1650  0.0077  0.0409  507 THR D OG1 
11859 C CG2 . THR D 206 ? 0.3261 0.4805 0.3207 0.1962  -0.0003 0.0477  507 THR D CG2 
11860 N N   . GLU D 207 ? 0.3220 0.5981 0.3849 0.1771  0.0006  0.0456  508 GLU D N   
11861 C CA  . GLU D 207 ? 0.3440 0.6650 0.4228 0.1876  -0.0032 0.0484  508 GLU D CA  
11862 C C   . GLU D 207 ? 0.2885 0.6347 0.3800 0.1705  -0.0096 0.0494  508 GLU D C   
11863 O O   . GLU D 207 ? 0.3949 0.7656 0.4914 0.1786  -0.0164 0.0527  508 GLU D O   
11864 C CB  . GLU D 207 ? 0.3841 0.7380 0.4793 0.1929  0.0035  0.0468  508 GLU D CB  
11865 C CG  . GLU D 207 ? 0.5938 0.9237 0.6736 0.2120  0.0092  0.0457  508 GLU D CG  
11866 C CD  . GLU D 207 ? 0.6867 1.0369 0.7766 0.2106  0.0169  0.0427  508 GLU D CD  
11867 O OE1 . GLU D 207 ? 0.5994 0.9756 0.7067 0.1930  0.0192  0.0412  508 GLU D OE1 
11868 O OE2 . GLU D 207 ? 0.6844 1.0225 0.7627 0.2269  0.0206  0.0420  508 GLU D OE2 
11869 N N   . ILE D 208 ? 0.3444 0.6842 0.4397 0.1473  -0.0078 0.0463  509 ILE D N   
11870 C CA  . ILE D 208 ? 0.3504 0.7057 0.4527 0.1300  -0.0138 0.0466  509 ILE D CA  
11871 C C   . ILE D 208 ? 0.3386 0.6710 0.4251 0.1338  -0.0207 0.0492  509 ILE D C   
11872 O O   . ILE D 208 ? 0.3306 0.6848 0.4215 0.1338  -0.0280 0.0519  509 ILE D O   
11873 C CB  . ILE D 208 ? 0.3661 0.7103 0.4706 0.1066  -0.0100 0.0426  509 ILE D CB  
11874 C CG1 . ILE D 208 ? 0.4225 0.7927 0.5424 0.1012  -0.0038 0.0407  509 ILE D CG1 
11875 C CG2 . ILE D 208 ? 0.3230 0.6740 0.4291 0.0896  -0.0161 0.0425  509 ILE D CG2 
11876 C CD1 . ILE D 208 ? 0.3798 0.7326 0.4982 0.0812  0.0007  0.0369  509 ILE D CD1 
11877 N N   . CYS D 209 ? 0.3185 0.6071 0.3856 0.1367  -0.0186 0.0487  510 CYS D N   
11878 C CA  . CYS D 209 ? 0.3248 0.5886 0.3744 0.1395  -0.0243 0.0513  510 CYS D CA  
11879 C C   . CYS D 209 ? 0.3902 0.6674 0.4364 0.1605  -0.0302 0.0561  510 CYS D C   
11880 O O   . CYS D 209 ? 0.4002 0.6850 0.4436 0.1598  -0.0377 0.0590  510 CYS D O   
11881 C CB  . CYS D 209 ? 0.3997 0.6164 0.4290 0.1396  -0.0201 0.0501  510 CYS D CB  
11882 S SG  . CYS D 209 ? 0.3904 0.5909 0.4219 0.1152  -0.0150 0.0450  510 CYS D SG  
11883 N N   . ILE D 210 ? 0.3299 0.6095 0.3750 0.1803  -0.0271 0.0571  511 ILE D N   
11884 C CA  . ILE D 210 ? 0.3910 0.6841 0.4326 0.2035  -0.0325 0.0616  511 ILE D CA  
11885 C C   . ILE D 210 ? 0.3809 0.7266 0.4445 0.2012  -0.0386 0.0634  511 ILE D C   
11886 O O   . ILE D 210 ? 0.4362 0.7895 0.4950 0.2086  -0.0466 0.0672  511 ILE D O   
11887 C CB  . ILE D 210 ? 0.4724 0.7610 0.5101 0.2251  -0.0268 0.0614  511 ILE D CB  
11888 C CG1 . ILE D 210 ? 0.5337 0.7674 0.5465 0.2256  -0.0218 0.0597  511 ILE D CG1 
11889 C CG2 . ILE D 210 ? 0.4196 0.7152 0.4504 0.2445  -0.0307 0.0640  511 ILE D CG2 
11890 C CD1 . ILE D 210 ? 0.5320 0.7548 0.5371 0.2453  -0.0157 0.0588  511 ILE D CD1 
11891 N N   . GLN D 211 ? 0.3612 0.7412 0.4472 0.1885  -0.0349 0.0605  512 GLN D N   
11892 C CA  . GLN D 211 ? 0.3747 0.7990 0.4792 0.1782  -0.0393 0.0607  512 GLN D CA  
11893 C C   . GLN D 211 ? 0.3876 0.8128 0.4885 0.1670  -0.0486 0.0630  512 GLN D C   
11894 O O   . GLN D 211 ? 0.4361 0.8832 0.5406 0.1671  -0.0550 0.0648  512 GLN D O   
11895 C CB  . GLN D 211 ? 0.5445 0.9937 0.6679 0.1602  -0.0333 0.0569  512 GLN D CB  
11896 C CG  . GLN D 211 ? 0.7599 1.2515 0.8997 0.1543  -0.0337 0.0563  512 GLN D CG  
11897 C CD  . GLN D 211 ? 0.9888 1.4917 1.1359 0.1596  -0.0248 0.0540  512 GLN D CD  
11898 O OE1 . GLN D 211 ? 0.9813 1.4590 1.1208 0.1679  -0.0183 0.0526  512 GLN D OE1 
11899 N NE2 . GLN D 211 ? 1.0669 1.6075 1.2277 0.1546  -0.0244 0.0537  512 GLN D NE2 
11900 N N   . GLN D 212 ? 0.3177 0.7039 0.4047 0.1515  -0.0465 0.0605  513 GLN D N   
11901 C CA  . GLN D 212 ? 0.3274 0.7054 0.4071 0.1366  -0.0529 0.0608  513 GLN D CA  
11902 C C   . GLN D 212 ? 0.4616 0.8133 0.5201 0.1498  -0.0588 0.0650  513 GLN D C   
11903 O O   . GLN D 212 ? 0.5053 0.8407 0.5527 0.1381  -0.0628 0.0651  513 GLN D O   
11904 C CB  . GLN D 212 ? 0.4419 0.7921 0.5166 0.1149  -0.0474 0.0561  513 GLN D CB  
11905 C CG  . GLN D 212 ? 0.4417 0.8150 0.5343 0.0994  -0.0424 0.0522  513 GLN D CG  
11906 C CD  . GLN D 212 ? 0.4885 0.9086 0.5980 0.0915  -0.0483 0.0532  513 GLN D CD  
11907 O OE1 . GLN D 212 ? 0.5113 0.9366 0.6171 0.0831  -0.0555 0.0542  513 GLN D OE1 
11908 N NE2 . GLN D 212 ? 0.6203 1.0755 0.7480 0.0936  -0.0452 0.0530  513 GLN D NE2 
11909 N N   . GLY D 213 ? 0.4625 0.8085 0.5134 0.1741  -0.0593 0.0684  514 GLY D N   
11910 C CA  . GLY D 213 ? 0.4530 0.7732 0.4815 0.1882  -0.0653 0.0730  514 GLY D CA  
11911 C C   . GLY D 213 ? 0.4466 0.7119 0.4497 0.1916  -0.0604 0.0727  514 GLY D C   
11912 O O   . GLY D 213 ? 0.5579 0.7964 0.5389 0.2012  -0.0650 0.0766  514 GLY D O   
11913 N N   . TRP D 214 ? 0.4741 0.7217 0.4786 0.1835  -0.0516 0.0683  515 TRP D N   
11914 C CA  . TRP D 214 ? 0.4842 0.6815 0.4645 0.1854  -0.0472 0.0680  515 TRP D CA  
11915 C C   . TRP D 214 ? 0.5840 0.7659 0.5492 0.2115  -0.0475 0.0713  515 TRP D C   
11916 O O   . TRP D 214 ? 0.5390 0.7453 0.5168 0.2258  -0.0454 0.0711  515 TRP D O   
11917 C CB  . TRP D 214 ? 0.4732 0.6581 0.4593 0.1708  -0.0383 0.0626  515 TRP D CB  
11918 C CG  . TRP D 214 ? 0.5479 0.6838 0.5100 0.1687  -0.0345 0.0620  515 TRP D CG  
11919 C CD1 . TRP D 214 ? 0.5120 0.6184 0.4550 0.1605  -0.0368 0.0634  515 TRP D CD1 
11920 C CD2 . TRP D 214 ? 0.5047 0.6163 0.4586 0.1736  -0.0276 0.0598  515 TRP D CD2 
11921 N NE1 . TRP D 214 ? 0.5249 0.5917 0.4491 0.1592  -0.0319 0.0624  515 TRP D NE1 
11922 C CE2 . TRP D 214 ? 0.4743 0.5427 0.4043 0.1672  -0.0265 0.0602  515 TRP D CE2 
11923 C CE3 . TRP D 214 ? 0.4949 0.6173 0.4585 0.1822  -0.0222 0.0576  515 TRP D CE3 
11924 C CZ2 . TRP D 214 ? 0.4805 0.5167 0.3963 0.1682  -0.0209 0.0583  515 TRP D CZ2 
11925 C CZ3 . TRP D 214 ? 0.5514 0.6400 0.4999 0.1842  -0.0164 0.0556  515 TRP D CZ3 
11926 C CH2 . TRP D 214 ? 0.5310 0.5770 0.4559 0.1769  -0.0161 0.0560  515 TRP D CH2 
11927 N N   . LYS D 215 ? 0.5753 0.7161 0.5120 0.2179  -0.0501 0.0746  516 LYS D N   
11928 C CA  . LYS D 215 ? 0.6129 0.7284 0.5283 0.2423  -0.0503 0.0777  516 LYS D CA  
11929 C C   . LYS D 215 ? 0.6421 0.7171 0.5423 0.2382  -0.0421 0.0744  516 LYS D C   
11930 O O   . LYS D 215 ? 0.7292 0.7670 0.6104 0.2250  -0.0409 0.0742  516 LYS D O   
11931 C CB  . LYS D 215 ? 0.6773 0.7677 0.5666 0.2516  -0.0581 0.0836  516 LYS D CB  
11932 C CG  . LYS D 215 ? 0.7887 0.9156 0.6906 0.2511  -0.0671 0.0868  516 LYS D CG  
11933 C CD  . LYS D 215 ? 0.7860 0.9623 0.7150 0.2602  -0.0674 0.0850  516 LYS D CD  
11934 C CE  . LYS D 215 ? 0.8058 1.0133 0.7440 0.2579  -0.0763 0.0875  516 LYS D CE  
11935 N NZ  . LYS D 215 ? 0.7506 1.0102 0.7178 0.2603  -0.0762 0.0853  516 LYS D NZ  
11936 N N   . PRO D 216 ? 0.6032 0.6859 0.5113 0.2482  -0.0363 0.0718  517 PRO D N   
11937 C CA  . PRO D 216 ? 0.6218 0.6688 0.5165 0.2430  -0.0288 0.0683  517 PRO D CA  
11938 C C   . PRO D 216 ? 0.6580 0.6557 0.5166 0.2586  -0.0296 0.0712  517 PRO D C   
11939 O O   . PRO D 216 ? 0.6386 0.6372 0.4889 0.2796  -0.0320 0.0733  517 PRO D O   
11940 C CB  . PRO D 216 ? 0.6519 0.7288 0.5678 0.2502  -0.0230 0.0649  517 PRO D CB  
11941 C CG  . PRO D 216 ? 0.6792 0.7924 0.6063 0.2704  -0.0277 0.0680  517 PRO D CG  
11942 C CD  . PRO D 216 ? 0.6087 0.7365 0.5393 0.2641  -0.0363 0.0719  517 PRO D CD  
11943 N N   . PRO D 217 ? 0.6913 0.6453 0.5279 0.2450  -0.0269 0.0701  518 PRO D N   
11944 C CA  . PRO D 217 ? 0.7552 0.6579 0.5548 0.2579  -0.0264 0.0722  518 PRO D CA  
11945 C C   . PRO D 217 ? 0.7627 0.6597 0.5594 0.2731  -0.0206 0.0689  518 PRO D C   
11946 O O   . PRO D 217 ? 0.7622 0.6246 0.5320 0.2824  -0.0194 0.0681  518 PRO D O   
11947 C CB  . PRO D 217 ? 0.7255 0.5913 0.5084 0.2341  -0.0239 0.0706  518 PRO D CB  
11948 C CG  . PRO D 217 ? 0.6483 0.5464 0.4581 0.2120  -0.0241 0.0686  518 PRO D CG  
11949 C CD  . PRO D 217 ? 0.6380 0.5878 0.4821 0.2175  -0.0238 0.0667  518 PRO D CD  
11950 N N   . ARG D 218 ? 0.6858 0.6173 0.5106 0.2698  -0.0157 0.0650  519 ARG D N   
11951 C CA  . ARG D 218 ? 0.7594 0.6913 0.5847 0.2812  -0.0091 0.0609  519 ARG D CA  
11952 C C   . ARG D 218 ? 0.7423 0.6203 0.5363 0.2776  -0.0049 0.0587  519 ARG D C   
11953 O O   . ARG D 218 ? 0.7979 0.6547 0.5729 0.2891  -0.0020 0.0564  519 ARG D O   
11954 C CB  . ARG D 218 ? 0.8386 0.7886 0.6646 0.3002  -0.0101 0.0608  519 ARG D CB  
11955 C CG  . ARG D 218 ? 0.8853 0.8933 0.7445 0.3022  -0.0135 0.0621  519 ARG D CG  
11956 C CD  . ARG D 218 ? 0.9179 0.9536 0.7861 0.3185  -0.0107 0.0602  519 ARG D CD  
11957 N NE  . ARG D 218 ? 0.9821 1.0648 0.8832 0.3123  -0.0065 0.0575  519 ARG D NE  
11958 C CZ  . ARG D 218 ? 0.9891 1.1209 0.9191 0.3066  -0.0098 0.0587  519 ARG D CZ  
11959 N NH1 . ARG D 218 ? 0.9856 1.1560 0.9423 0.2989  -0.0053 0.0561  519 ARG D NH1 
11960 N NH2 . ARG D 218 ? 0.9606 1.1020 0.8913 0.3073  -0.0176 0.0626  519 ARG D NH2 
11961 N N   . GLY D 219 ? 0.7173 0.5758 0.5070 0.2560  -0.0040 0.0579  520 GLY D N   
11962 C CA  . GLY D 219 ? 0.7098 0.5245 0.4754 0.2474  0.0003  0.0551  520 GLY D CA  
11963 C C   . GLY D 219 ? 0.6907 0.5238 0.4776 0.2330  0.0064  0.0496  520 GLY D C   
11964 O O   . GLY D 219 ? 0.6112 0.4891 0.4302 0.2307  0.0078  0.0480  520 GLY D O   
11965 N N   . ARG D 220 ? 0.7353 0.5317 0.5021 0.2222  0.0097  0.0469  521 ARG D N   
11966 C CA  . ARG D 220 ? 0.7003 0.5086 0.4829 0.2088  0.0151  0.0418  521 ARG D CA  
11967 C C   . ARG D 220 ? 0.6018 0.4251 0.4025 0.1829  0.0144  0.0406  521 ARG D C   
11968 O O   . ARG D 220 ? 0.5444 0.3888 0.3655 0.1725  0.0179  0.0370  521 ARG D O   
11969 C CB  . ARG D 220 ? 0.7197 0.4832 0.4721 0.2095  0.0186  0.0392  521 ARG D CB  
11970 C CG  . ARG D 220 ? 0.6790 0.4549 0.4452 0.2018  0.0241  0.0342  521 ARG D CG  
11971 C CD  . ARG D 220 ? 0.8671 0.5977 0.6013 0.2026  0.0270  0.0315  521 ARG D CD  
11972 N NE  . ARG D 220 ? 0.8892 0.6343 0.6351 0.2039  0.0325  0.0271  521 ARG D NE  
11973 C CZ  . ARG D 220 ? 0.9751 0.6930 0.7041 0.1953  0.0353  0.0235  521 ARG D CZ  
11974 N NH1 . ARG D 220 ? 1.0071 0.6826 0.7071 0.1834  0.0331  0.0237  521 ARG D NH1 
11975 N NH2 . ARG D 220 ? 0.9226 0.6564 0.6632 0.1974  0.0402  0.0197  521 ARG D NH2 
11976 N N   . PHE D 221 ? 0.5745 0.3870 0.3673 0.1730  0.0102  0.0436  522 PHE D N   
11977 C CA  . PHE D 221 ? 0.5647 0.3897 0.3723 0.1498  0.0099  0.0424  522 PHE D CA  
11978 C C   . PHE D 221 ? 0.6008 0.4425 0.4162 0.1482  0.0050  0.0460  522 PHE D C   
11979 O O   . PHE D 221 ? 0.7009 0.5269 0.5051 0.1358  0.0030  0.0477  522 PHE D O   
11980 C CB  . PHE D 221 ? 0.6582 0.4463 0.4431 0.1337  0.0111  0.0412  522 PHE D CB  
11981 C CG  . PHE D 221 ? 0.6675 0.4404 0.4451 0.1325  0.0154  0.0373  522 PHE D CG  
11982 C CD1 . PHE D 221 ? 0.6955 0.4281 0.4410 0.1426  0.0161  0.0375  522 PHE D CD1 
11983 C CD2 . PHE D 221 ? 0.5917 0.3885 0.3923 0.1218  0.0185  0.0333  522 PHE D CD2 
11984 C CE1 . PHE D 221 ? 0.7391 0.4566 0.4761 0.1411  0.0199  0.0336  522 PHE D CE1 
11985 C CE2 . PHE D 221 ? 0.6452 0.4278 0.4379 0.1207  0.0220  0.0298  522 PHE D CE2 
11986 C CZ  . PHE D 221 ? 0.6943 0.4378 0.4555 0.1301  0.0228  0.0298  522 PHE D CZ  
11987 N N   . ASP D 222 ? 0.6048 0.4804 0.4397 0.1604  0.0032  0.0473  523 ASP D N   
11988 C CA  . ASP D 222 ? 0.5655 0.4616 0.4103 0.1586  -0.0019 0.0503  523 ASP D CA  
11989 C C   . ASP D 222 ? 0.5081 0.4325 0.3785 0.1396  -0.0007 0.0474  523 ASP D C   
11990 O O   . ASP D 222 ? 0.4281 0.3825 0.3217 0.1392  0.0016  0.0448  523 ASP D O   
11991 C CB  . ASP D 222 ? 0.5940 0.5170 0.4492 0.1789  -0.0049 0.0528  523 ASP D CB  
11992 C CG  . ASP D 222 ? 0.6681 0.5632 0.4968 0.2008  -0.0064 0.0559  523 ASP D CG  
11993 O OD1 . ASP D 222 ? 0.6980 0.5494 0.4967 0.1986  -0.0067 0.0572  523 ASP D OD1 
11994 O OD2 . ASP D 222 ? 0.6184 0.5355 0.4558 0.2204  -0.0072 0.0570  523 ASP D OD2 
11995 N N   . VAL D 223 ? 0.4845 0.3987 0.3493 0.1239  -0.0019 0.0478  524 VAL D N   
11996 C CA  . VAL D 223 ? 0.4478 0.3875 0.3348 0.1078  -0.0011 0.0451  524 VAL D CA  
11997 C C   . VAL D 223 ? 0.3780 0.3531 0.2844 0.1133  -0.0046 0.0463  524 VAL D C   
11998 O O   . VAL D 223 ? 0.4507 0.4272 0.3502 0.1212  -0.0096 0.0501  524 VAL D O   
11999 C CB  . VAL D 223 ? 0.5106 0.4342 0.3868 0.0921  -0.0016 0.0455  524 VAL D CB  
12000 C CG1 . VAL D 223 ? 0.4231 0.3740 0.3211 0.0787  -0.0011 0.0428  524 VAL D CG1 
12001 C CG2 . VAL D 223 ? 0.4909 0.3851 0.3513 0.0833  0.0022  0.0438  524 VAL D CG2 
12002 N N   . LEU D 224 ? 0.3243 0.3278 0.2540 0.1088  -0.0023 0.0431  525 LEU D N   
12003 C CA  . LEU D 224 ? 0.3679 0.4068 0.3167 0.1116  -0.0053 0.0438  525 LEU D CA  
12004 C C   . LEU D 224 ? 0.3583 0.4041 0.3090 0.1002  -0.0092 0.0445  525 LEU D C   
12005 O O   . LEU D 224 ? 0.3001 0.3309 0.2451 0.0869  -0.0075 0.0428  525 LEU D O   
12006 C CB  . LEU D 224 ? 0.3469 0.4102 0.3170 0.1064  -0.0014 0.0401  525 LEU D CB  
12007 C CG  . LEU D 224 ? 0.4453 0.5122 0.4167 0.1209  0.0016  0.0400  525 LEU D CG  
12008 C CD1 . LEU D 224 ? 0.3381 0.4138 0.3221 0.1134  0.0071  0.0360  525 LEU D CD1 
12009 C CD2 . LEU D 224 ? 0.3844 0.4806 0.3656 0.1345  -0.0020 0.0429  525 LEU D CD2 
12010 N N   . PRO D 225 ? 0.3017 0.3715 0.2605 0.1050  -0.0142 0.0468  526 PRO D N   
12011 C CA  . PRO D 225 ? 0.3119 0.3909 0.2737 0.0930  -0.0177 0.0468  526 PRO D CA  
12012 C C   . PRO D 225 ? 0.3853 0.4809 0.3643 0.0783  -0.0145 0.0422  526 PRO D C   
12013 O O   . PRO D 225 ? 0.3589 0.4661 0.3503 0.0787  -0.0109 0.0399  526 PRO D O   
12014 C CB  . PRO D 225 ? 0.3001 0.4033 0.2668 0.1035  -0.0243 0.0504  526 PRO D CB  
12015 C CG  . PRO D 225 ? 0.3777 0.5008 0.3574 0.1153  -0.0224 0.0502  526 PRO D CG  
12016 C CD  . PRO D 225 ? 0.3314 0.4258 0.2995 0.1206  -0.0167 0.0490  526 PRO D CD  
12017 N N   . LEU D 226 ? 0.2935 0.3878 0.2712 0.0655  -0.0156 0.0408  527 LEU D N   
12018 C CA  . LEU D 226 ? 0.3109 0.4218 0.3029 0.0527  -0.0140 0.0368  527 LEU D CA  
12019 C C   . LEU D 226 ? 0.2930 0.4350 0.2976 0.0536  -0.0187 0.0378  527 LEU D C   
12020 O O   . LEU D 226 ? 0.3587 0.5084 0.3590 0.0590  -0.0245 0.0412  527 LEU D O   
12021 C CB  . LEU D 226 ? 0.3317 0.4304 0.3164 0.0401  -0.0134 0.0347  527 LEU D CB  
12022 C CG  . LEU D 226 ? 0.3489 0.4226 0.3244 0.0360  -0.0083 0.0329  527 LEU D CG  
12023 C CD1 . LEU D 226 ? 0.3043 0.3684 0.2707 0.0260  -0.0081 0.0317  527 LEU D CD1 
12024 C CD2 . LEU D 226 ? 0.2633 0.3391 0.2496 0.0321  -0.0032 0.0291  527 LEU D CD2 
12025 N N   . LEU D 227 ? 0.3239 0.4843 0.3434 0.0479  -0.0165 0.0352  528 LEU D N   
12026 C CA  . LEU D 227 ? 0.3111 0.5029 0.3433 0.0444  -0.0204 0.0355  528 LEU D CA  
12027 C C   . LEU D 227 ? 0.3270 0.5185 0.3617 0.0271  -0.0191 0.0314  528 LEU D C   
12028 O O   . LEU D 227 ? 0.2733 0.4626 0.3136 0.0213  -0.0143 0.0284  528 LEU D O   
12029 C CB  . LEU D 227 ? 0.3378 0.5521 0.3838 0.0519  -0.0185 0.0362  528 LEU D CB  
12030 C CG  . LEU D 227 ? 0.3611 0.6068 0.4160 0.0622  -0.0236 0.0398  528 LEU D CG  
12031 C CD1 . LEU D 227 ? 0.3430 0.6160 0.4148 0.0619  -0.0202 0.0388  528 LEU D CD1 
12032 C CD2 . LEU D 227 ? 0.2585 0.5200 0.3133 0.0556  -0.0311 0.0413  528 LEU D CD2 
12033 N N   . LEU D 228 ? 0.3621 0.5539 0.3906 0.0196  -0.0235 0.0312  529 LEU D N   
12034 C CA  . LEU D 228 ? 0.3384 0.5213 0.3632 0.0048  -0.0220 0.0270  529 LEU D CA  
12035 C C   . LEU D 228 ? 0.3597 0.5652 0.3902 -0.0056 -0.0266 0.0262  529 LEU D C   
12036 O O   . LEU D 228 ? 0.3075 0.5286 0.3376 -0.0038 -0.0330 0.0289  529 LEU D O   
12037 C CB  . LEU D 228 ? 0.2846 0.4453 0.2942 0.0030  -0.0223 0.0266  529 LEU D CB  
12038 C CG  . LEU D 228 ? 0.2694 0.4080 0.2723 0.0108  -0.0179 0.0274  529 LEU D CG  
12039 C CD1 . LEU D 228 ? 0.2343 0.3534 0.2223 0.0077  -0.0176 0.0272  529 LEU D CD1 
12040 C CD2 . LEU D 228 ? 0.2494 0.3807 0.2583 0.0083  -0.0116 0.0242  529 LEU D CD2 
12041 N N   . GLN D 229 ? 0.2755 0.4812 0.3095 -0.0170 -0.0236 0.0225  530 GLN D N   
12042 C CA  . GLN D 229 ? 0.2610 0.4839 0.2978 -0.0302 -0.0272 0.0211  530 GLN D CA  
12043 C C   . GLN D 229 ? 0.2798 0.4809 0.3036 -0.0424 -0.0259 0.0166  530 GLN D C   
12044 O O   . GLN D 229 ? 0.2851 0.4666 0.3054 -0.0442 -0.0203 0.0135  530 GLN D O   
12045 C CB  . GLN D 229 ? 0.2949 0.5351 0.3443 -0.0342 -0.0246 0.0207  530 GLN D CB  
12046 C CG  . GLN D 229 ? 0.3650 0.6155 0.4135 -0.0517 -0.0270 0.0184  530 GLN D CG  
12047 C CD  . GLN D 229 ? 0.3598 0.6276 0.4195 -0.0569 -0.0240 0.0184  530 GLN D CD  
12048 O OE1 . GLN D 229 ? 0.3815 0.6472 0.4476 -0.0481 -0.0189 0.0191  530 GLN D OE1 
12049 N NE2 . GLN D 229 ? 0.5188 0.8038 0.5798 -0.0722 -0.0271 0.0176  530 GLN D NE2 
12050 N N   . ALA D 230 ? 0.3080 0.5125 0.3239 -0.0499 -0.0313 0.0161  531 ALA D N   
12051 C CA  . ALA D 230 ? 0.3381 0.5227 0.3392 -0.0613 -0.0308 0.0116  531 ALA D CA  
12052 C C   . ALA D 230 ? 0.3528 0.5507 0.3527 -0.0766 -0.0350 0.0100  531 ALA D C   
12053 O O   . ALA D 230 ? 0.3158 0.5401 0.3224 -0.0788 -0.0413 0.0129  531 ALA D O   
12054 C CB  . ALA D 230 ? 0.4209 0.5944 0.4094 -0.0586 -0.0334 0.0120  531 ALA D CB  
12055 N N   . ASN D 231 ? 0.3672 0.5467 0.3577 -0.0873 -0.0317 0.0054  532 ASN D N   
12056 C CA  . ASN D 231 ? 0.3753 0.5587 0.3581 -0.1045 -0.0355 0.0030  532 ASN D CA  
12057 C C   . ASN D 231 ? 0.3888 0.6066 0.3866 -0.1102 -0.0394 0.0062  532 ASN D C   
12058 O O   . ASN D 231 ? 0.3858 0.6207 0.3815 -0.1219 -0.0458 0.0065  532 ASN D O   
12059 C CB  . ASN D 231 ? 0.4040 0.5810 0.3718 -0.1103 -0.0406 0.0015  532 ASN D CB  
12060 C CG  . ASN D 231 ? 0.5996 0.7649 0.5512 -0.1285 -0.0426 -0.0030 532 ASN D CG  
12061 O OD1 . ASN D 231 ? 0.6992 0.8458 0.6442 -0.1342 -0.0379 -0.0062 532 ASN D OD1 
12062 N ND2 . ASN D 231 ? 0.5971 0.7719 0.5407 -0.1380 -0.0497 -0.0030 532 ASN D ND2 
12063 N N   . GLY D 232 ? 0.3461 0.5756 0.3591 -0.1022 -0.0355 0.0085  533 GLY D N   
12064 C CA  . GLY D 232 ? 0.3359 0.5993 0.3642 -0.1069 -0.0375 0.0113  533 GLY D CA  
12065 C C   . GLY D 232 ? 0.3621 0.6602 0.4036 -0.0989 -0.0437 0.0159  533 GLY D C   
12066 O O   . GLY D 232 ? 0.3454 0.6764 0.4018 -0.1007 -0.0450 0.0184  533 GLY D O   
12067 N N   . ASN D 233 ? 0.3568 0.6493 0.3927 -0.0897 -0.0474 0.0173  534 ASN D N   
12068 C CA  . ASN D 233 ? 0.4073 0.7305 0.4533 -0.0807 -0.0541 0.0220  534 ASN D CA  
12069 C C   . ASN D 233 ? 0.3318 0.6668 0.3922 -0.0616 -0.0507 0.0257  534 ASN D C   
12070 O O   . ASN D 233 ? 0.2746 0.5903 0.3353 -0.0551 -0.0435 0.0246  534 ASN D O   
12071 C CB  . ASN D 233 ? 0.4492 0.7584 0.4814 -0.0771 -0.0590 0.0225  534 ASN D CB  
12072 C CG  . ASN D 233 ? 0.5193 0.8150 0.5349 -0.0955 -0.0620 0.0183  534 ASN D CG  
12073 O OD1 . ASN D 233 ? 0.5990 0.9126 0.6163 -0.1109 -0.0658 0.0173  534 ASN D OD1 
12074 N ND2 . ASN D 233 ? 0.5031 0.7667 0.5018 -0.0945 -0.0600 0.0157  534 ASN D ND2 
12075 N N   . ASP D 234 ? 0.2986 0.6658 0.3702 -0.0522 -0.0563 0.0301  535 ASP D N   
12076 C CA  . ASP D 234 ? 0.3116 0.6879 0.3938 -0.0318 -0.0537 0.0337  535 ASP D CA  
12077 C C   . ASP D 234 ? 0.2322 0.5705 0.3020 -0.0196 -0.0495 0.0335  535 ASP D C   
12078 O O   . ASP D 234 ? 0.2981 0.6146 0.3533 -0.0221 -0.0518 0.0327  535 ASP D O   
12079 C CB  . ASP D 234 ? 0.4288 0.8397 0.5199 -0.0206 -0.0616 0.0386  535 ASP D CB  
12080 C CG  . ASP D 234 ? 0.4376 0.8938 0.5451 -0.0304 -0.0652 0.0394  535 ASP D CG  
12081 O OD1 . ASP D 234 ? 0.4770 0.9646 0.5909 -0.0258 -0.0733 0.0429  535 ASP D OD1 
12082 O OD2 . ASP D 234 ? 0.4235 0.8846 0.5369 -0.0432 -0.0601 0.0368  535 ASP D OD2 
12083 N N   . PRO D 235 ? 0.3047 0.6343 0.3789 -0.0075 -0.0432 0.0340  536 PRO D N   
12084 C CA  . PRO D 235 ? 0.3246 0.6192 0.3864 0.0022  -0.0395 0.0339  536 PRO D CA  
12085 C C   . PRO D 235 ? 0.3790 0.6732 0.4345 0.0171  -0.0448 0.0384  536 PRO D C   
12086 O O   . PRO D 235 ? 0.3468 0.6694 0.4103 0.0250  -0.0503 0.0420  536 PRO D O   
12087 C CB  . PRO D 235 ? 0.2433 0.5328 0.3121 0.0097  -0.0321 0.0333  536 PRO D CB  
12088 C CG  . PRO D 235 ? 0.2311 0.5585 0.3166 0.0128  -0.0332 0.0352  536 PRO D CG  
12089 C CD  . PRO D 235 ? 0.2218 0.5731 0.3114 -0.0031 -0.0390 0.0346  536 PRO D CD  
12090 N N   . GLU D 236 ? 0.2324 0.4942 0.2725 0.0206  -0.0432 0.0383  537 GLU D N   
12091 C CA  . GLU D 236 ? 0.2459 0.4997 0.2749 0.0330  -0.0479 0.0426  537 GLU D CA  
12092 C C   . GLU D 236 ? 0.3497 0.5745 0.3693 0.0446  -0.0427 0.0435  537 GLU D C   
12093 O O   . GLU D 236 ? 0.3340 0.5372 0.3501 0.0385  -0.0363 0.0402  537 GLU D O   
12094 C CB  . GLU D 236 ? 0.2735 0.5155 0.2886 0.0230  -0.0521 0.0419  537 GLU D CB  
12095 C CG  . GLU D 236 ? 0.3671 0.6351 0.3883 0.0102  -0.0580 0.0407  537 GLU D CG  
12096 C CD  . GLU D 236 ? 0.5143 0.7669 0.5201 -0.0021 -0.0607 0.0386  537 GLU D CD  
12097 O OE1 . GLU D 236 ? 0.5291 0.7586 0.5196 0.0026  -0.0607 0.0400  537 GLU D OE1 
12098 O OE2 . GLU D 236 ? 0.5297 0.7927 0.5374 -0.0171 -0.0625 0.0354  537 GLU D OE2 
12099 N N   . LEU D 237 ? 0.3956 0.6188 0.4092 0.0612  -0.0459 0.0482  538 LEU D N   
12100 C CA  . LEU D 237 ? 0.2791 0.4727 0.2805 0.0720  -0.0417 0.0495  538 LEU D CA  
12101 C C   . LEU D 237 ? 0.3579 0.5200 0.3388 0.0678  -0.0420 0.0501  538 LEU D C   
12102 O O   . LEU D 237 ? 0.3387 0.5026 0.3113 0.0657  -0.0478 0.0522  538 LEU D O   
12103 C CB  . LEU D 237 ? 0.2938 0.4952 0.2940 0.0927  -0.0448 0.0542  538 LEU D CB  
12104 C CG  . LEU D 237 ? 0.3655 0.5935 0.3842 0.1001  -0.0421 0.0534  538 LEU D CG  
12105 C CD1 . LEU D 237 ? 0.3540 0.5957 0.3720 0.1220  -0.0464 0.0582  538 LEU D CD1 
12106 C CD2 . LEU D 237 ? 0.3420 0.5498 0.3603 0.0984  -0.0335 0.0501  538 LEU D CD2 
12107 N N   . PHE D 238 ? 0.3224 0.4565 0.2945 0.0666  -0.0358 0.0486  539 PHE D N   
12108 C CA  . PHE D 238 ? 0.3722 0.4764 0.3244 0.0628  -0.0349 0.0495  539 PHE D CA  
12109 C C   . PHE D 238 ? 0.3684 0.4461 0.3099 0.0699  -0.0302 0.0503  539 PHE D C   
12110 O O   . PHE D 238 ? 0.4004 0.4782 0.3510 0.0693  -0.0250 0.0474  539 PHE D O   
12111 C CB  . PHE D 238 ? 0.3768 0.4753 0.3295 0.0457  -0.0312 0.0448  539 PHE D CB  
12112 C CG  . PHE D 238 ? 0.3502 0.4692 0.3095 0.0368  -0.0353 0.0433  539 PHE D CG  
12113 C CD1 . PHE D 238 ? 0.2963 0.4376 0.2729 0.0308  -0.0347 0.0401  539 PHE D CD1 
12114 C CD2 . PHE D 238 ? 0.3019 0.4163 0.2481 0.0335  -0.0400 0.0451  539 PHE D CD2 
12115 C CE1 . PHE D 238 ? 0.2800 0.4379 0.2601 0.0210  -0.0388 0.0385  539 PHE D CE1 
12116 C CE2 . PHE D 238 ? 0.3122 0.4440 0.2625 0.0245  -0.0441 0.0434  539 PHE D CE2 
12117 C CZ  . PHE D 238 ? 0.2792 0.4323 0.2462 0.0179  -0.0436 0.0400  539 PHE D CZ  
12118 N N   . GLN D 239 ? 0.4686 0.5218 0.3889 0.0757  -0.0322 0.0542  540 GLN D N   
12119 C CA  . GLN D 239 ? 0.4693 0.4925 0.3749 0.0796  -0.0279 0.0549  540 GLN D CA  
12120 C C   . GLN D 239 ? 0.4129 0.4176 0.3112 0.0638  -0.0228 0.0520  540 GLN D C   
12121 O O   . GLN D 239 ? 0.4155 0.4118 0.3023 0.0564  -0.0242 0.0531  540 GLN D O   
12122 C CB  . GLN D 239 ? 0.4372 0.4395 0.3203 0.0932  -0.0324 0.0607  540 GLN D CB  
12123 C CG  . GLN D 239 ? 0.5805 0.5465 0.4433 0.0953  -0.0284 0.0616  540 GLN D CG  
12124 C CD  . GLN D 239 ? 0.7795 0.7161 0.6131 0.1025  -0.0325 0.0673  540 GLN D CD  
12125 O OE1 . GLN D 239 ? 0.9315 0.8568 0.7533 0.1195  -0.0354 0.0708  540 GLN D OE1 
12126 N NE2 . GLN D 239 ? 0.7847 0.7076 0.6049 0.0898  -0.0326 0.0682  540 GLN D NE2 
12127 N N   . ILE D 240 ? 0.4047 0.4044 0.3095 0.0589  -0.0169 0.0484  541 ILE D N   
12128 C CA  . ILE D 240 ? 0.3876 0.3708 0.2852 0.0454  -0.0120 0.0460  541 ILE D CA  
12129 C C   . ILE D 240 ? 0.4444 0.3976 0.3158 0.0462  -0.0127 0.0501  541 ILE D C   
12130 O O   . ILE D 240 ? 0.4567 0.3929 0.3156 0.0572  -0.0140 0.0531  541 ILE D O   
12131 C CB  . ILE D 240 ? 0.4244 0.4066 0.3317 0.0419  -0.0064 0.0421  541 ILE D CB  
12132 C CG1 . ILE D 240 ? 0.4254 0.4346 0.3559 0.0418  -0.0058 0.0387  541 ILE D CG1 
12133 C CG2 . ILE D 240 ? 0.3787 0.3500 0.2814 0.0280  -0.0017 0.0395  541 ILE D CG2 
12134 C CD1 . ILE D 240 ? 0.4574 0.4657 0.3967 0.0398  -0.0010 0.0353  541 ILE D CD1 
12135 N N   . PRO D 241 ? 0.5174 0.4618 0.3779 0.0354  -0.0119 0.0504  542 PRO D N   
12136 C CA  . PRO D 241 ? 0.5472 0.4609 0.3807 0.0335  -0.0119 0.0544  542 PRO D CA  
12137 C C   . PRO D 241 ? 0.5020 0.3955 0.3280 0.0319  -0.0077 0.0535  542 PRO D C   
12138 O O   . PRO D 241 ? 0.4867 0.3872 0.3245 0.0223  -0.0027 0.0492  542 PRO D O   
12139 C CB  . PRO D 241 ? 0.5940 0.5087 0.4234 0.0186  -0.0093 0.0530  542 PRO D CB  
12140 C CG  . PRO D 241 ? 0.5118 0.4549 0.3600 0.0182  -0.0113 0.0503  542 PRO D CG  
12141 C CD  . PRO D 241 ? 0.4829 0.4444 0.3531 0.0247  -0.0110 0.0474  542 PRO D CD  
12142 N N   . PRO D 242 ? 0.5525 0.4204 0.3579 0.0417  -0.0099 0.0576  543 PRO D N   
12143 C CA  . PRO D 242 ? 0.5161 0.3636 0.3131 0.0410  -0.0065 0.0565  543 PRO D CA  
12144 C C   . PRO D 242 ? 0.5712 0.4062 0.3602 0.0226  -0.0015 0.0546  543 PRO D C   
12145 O O   . PRO D 242 ? 0.5534 0.3852 0.3465 0.0177  0.0021  0.0516  543 PRO D O   
12146 C CB  . PRO D 242 ? 0.5909 0.4085 0.3612 0.0550  -0.0104 0.0617  543 PRO D CB  
12147 C CG  . PRO D 242 ? 0.6173 0.4519 0.3931 0.0680  -0.0164 0.0647  543 PRO D CG  
12148 C CD  . PRO D 242 ? 0.5542 0.4103 0.3425 0.0552  -0.0161 0.0632  543 PRO D CD  
12149 N N   . GLU D 243 ? 0.4889 0.3194 0.2672 0.0118  -0.0011 0.0563  544 GLU D N   
12150 C CA  . GLU D 243 ? 0.4877 0.3117 0.2606 -0.0063 0.0041  0.0544  544 GLU D CA  
12151 C C   . GLU D 243 ? 0.4882 0.3425 0.2894 -0.0137 0.0082  0.0485  544 GLU D C   
12152 O O   . GLU D 243 ? 0.5265 0.3805 0.3282 -0.0267 0.0126  0.0462  544 GLU D O   
12153 C CB  . GLU D 243 ? 0.5199 0.3340 0.2746 -0.0161 0.0042  0.0576  544 GLU D CB  
12154 C CG  . GLU D 243 ? 0.5208 0.3613 0.2907 -0.0163 0.0033  0.0563  544 GLU D CG  
12155 C CD  . GLU D 243 ? 0.5482 0.3888 0.3138 -0.0014 -0.0036 0.0601  544 GLU D CD  
12156 O OE1 . GLU D 243 ? 0.5837 0.4094 0.3402 0.0117  -0.0073 0.0630  544 GLU D OE1 
12157 O OE2 . GLU D 243 ? 0.7081 0.5636 0.4784 -0.0025 -0.0054 0.0601  544 GLU D OE2 
12158 N N   . LEU D 244 ? 0.4124 0.2927 0.2363 -0.0059 0.0067  0.0461  545 LEU D N   
12159 C CA  . LEU D 244 ? 0.3960 0.3009 0.2443 -0.0108 0.0102  0.0407  545 LEU D CA  
12160 C C   . LEU D 244 ? 0.4429 0.3482 0.3006 -0.0057 0.0111  0.0385  545 LEU D C   
12161 O O   . LEU D 244 ? 0.3764 0.2973 0.2507 -0.0110 0.0143  0.0343  545 LEU D O   
12162 C CB  . LEU D 244 ? 0.3406 0.2704 0.2067 -0.0066 0.0084  0.0388  545 LEU D CB  
12163 C CG  . LEU D 244 ? 0.5270 0.4604 0.3867 -0.0134 0.0084  0.0394  545 LEU D CG  
12164 C CD1 . LEU D 244 ? 0.5324 0.4901 0.4099 -0.0116 0.0074  0.0363  545 LEU D CD1 
12165 C CD2 . LEU D 244 ? 0.5178 0.4468 0.3708 -0.0276 0.0139  0.0380  545 LEU D CD2 
12166 N N   . VAL D 245 ? 0.4599 0.3485 0.3067 0.0051  0.0085  0.0412  546 VAL D N   
12167 C CA  . VAL D 245 ? 0.4324 0.3218 0.2874 0.0116  0.0094  0.0391  546 VAL D CA  
12168 C C   . VAL D 245 ? 0.4390 0.3023 0.2755 0.0045  0.0115  0.0394  546 VAL D C   
12169 O O   . VAL D 245 ? 0.4978 0.3334 0.3109 0.0094  0.0097  0.0428  546 VAL D O   
12170 C CB  . VAL D 245 ? 0.4604 0.3499 0.3154 0.0289  0.0059  0.0414  546 VAL D CB  
12171 C CG1 . VAL D 245 ? 0.4594 0.3506 0.3226 0.0351  0.0077  0.0388  546 VAL D CG1 
12172 C CG2 . VAL D 245 ? 0.3997 0.3156 0.2713 0.0340  0.0031  0.0415  546 VAL D CG2 
12173 N N   . LEU D 246 ? 0.4235 0.2951 0.2690 -0.0073 0.0149  0.0359  547 LEU D N   
12174 C CA  . LEU D 246 ? 0.4136 0.2641 0.2431 -0.0168 0.0167  0.0357  547 LEU D CA  
12175 C C   . LEU D 246 ? 0.5114 0.3516 0.3391 -0.0076 0.0162  0.0346  547 LEU D C   
12176 O O   . LEU D 246 ? 0.5434 0.4035 0.3915 -0.0020 0.0169  0.0317  547 LEU D O   
12177 C CB  . LEU D 246 ? 0.4314 0.2994 0.2733 -0.0319 0.0201  0.0323  547 LEU D CB  
12178 C CG  . LEU D 246 ? 0.5272 0.3806 0.3565 -0.0448 0.0218  0.0315  547 LEU D CG  
12179 C CD1 . LEU D 246 ? 0.5447 0.3651 0.3428 -0.0509 0.0209  0.0356  547 LEU D CD1 
12180 C CD2 . LEU D 246 ? 0.4693 0.3470 0.3138 -0.0583 0.0249  0.0285  547 LEU D CD2 
12181 N N   . GLU D 247 ? 0.5166 0.3239 0.3178 -0.0056 0.0152  0.0370  548 GLU D N   
12182 C CA  . GLU D 247 ? 0.5313 0.3238 0.3256 0.0041  0.0151  0.0361  548 GLU D CA  
12183 C C   . GLU D 247 ? 0.6077 0.3726 0.3798 -0.0084 0.0162  0.0355  548 GLU D C   
12184 O O   . GLU D 247 ? 0.6105 0.3590 0.3646 -0.0212 0.0162  0.0375  548 GLU D O   
12185 C CB  . GLU D 247 ? 0.5324 0.3086 0.3128 0.0228  0.0124  0.0395  548 GLU D CB  
12186 C CG  . GLU D 247 ? 0.5056 0.3131 0.3104 0.0358  0.0110  0.0395  548 GLU D CG  
12187 C CD  . GLU D 247 ? 0.6098 0.4060 0.4025 0.0548  0.0079  0.0431  548 GLU D CD  
12188 O OE1 . GLU D 247 ? 0.7045 0.4810 0.4768 0.0563  0.0053  0.0472  548 GLU D OE1 
12189 O OE2 . GLU D 247 ? 0.6100 0.4177 0.4132 0.0688  0.0081  0.0421  548 GLU D OE2 
12190 N N   . VAL D 248 ? 0.5735 0.3337 0.3462 -0.0057 0.0171  0.0327  549 VAL D N   
12191 C CA  . VAL D 248 ? 0.5959 0.3317 0.3486 -0.0183 0.0177  0.0315  549 VAL D CA  
12192 C C   . VAL D 248 ? 0.5942 0.2966 0.3227 -0.0053 0.0170  0.0320  549 VAL D C   
12193 O O   . VAL D 248 ? 0.6383 0.3503 0.3784 0.0080  0.0177  0.0299  549 VAL D O   
12194 C CB  . VAL D 248 ? 0.5848 0.3447 0.3583 -0.0284 0.0193  0.0272  549 VAL D CB  
12195 C CG1 . VAL D 248 ? 0.5263 0.2622 0.2781 -0.0435 0.0192  0.0260  549 VAL D CG1 
12196 C CG2 . VAL D 248 ? 0.4931 0.2881 0.2920 -0.0372 0.0203  0.0263  549 VAL D CG2 
12197 N N   . PRO D 249 ? 0.6261 0.2878 0.3194 -0.0084 0.0159  0.0346  550 PRO D N   
12198 C CA  . PRO D 249 ? 0.6659 0.2916 0.3325 0.0030  0.0156  0.0343  550 PRO D CA  
12199 C C   . PRO D 249 ? 0.6392 0.2625 0.3058 -0.0069 0.0170  0.0300  550 PRO D C   
12200 O O   . PRO D 249 ? 0.6712 0.2982 0.3378 -0.0278 0.0171  0.0288  550 PRO D O   
12201 C CB  . PRO D 249 ? 0.6457 0.2266 0.2724 -0.0027 0.0140  0.0383  550 PRO D CB  
12202 C CG  . PRO D 249 ? 0.7086 0.3067 0.3446 -0.0129 0.0133  0.0413  550 PRO D CG  
12203 C CD  . PRO D 249 ? 0.6381 0.2830 0.3122 -0.0231 0.0151  0.0379  550 PRO D CD  
12204 N N   . ILE D 250 ? 0.6696 0.2891 0.3367 0.0079  0.0180  0.0276  551 ILE D N   
12205 C CA  . ILE D 250 ? 0.6215 0.2414 0.2902 -0.0003 0.0191  0.0233  551 ILE D CA  
12206 C C   . ILE D 250 ? 0.6936 0.2632 0.3203 -0.0050 0.0185  0.0229  551 ILE D C   
12207 O O   . ILE D 250 ? 0.7463 0.2845 0.3487 0.0115  0.0187  0.0239  551 ILE D O   
12208 C CB  . ILE D 250 ? 0.6394 0.2830 0.3307 0.0160  0.0211  0.0206  551 ILE D CB  
12209 C CG1 . ILE D 250 ? 0.6070 0.2961 0.3359 0.0209  0.0214  0.0213  551 ILE D CG1 
12210 C CG2 . ILE D 250 ? 0.6236 0.2694 0.3171 0.0055  0.0218  0.0163  551 ILE D CG2 
12211 C CD1 . ILE D 250 ? 0.4990 0.2168 0.2502 0.0029  0.0211  0.0201  551 ILE D CD1 
12212 N N   . ARG D 251 ? 0.7266 0.2884 0.3438 -0.0277 0.0177  0.0214  552 ARG D N   
12213 C CA  . ARG D 251 ? 0.8279 0.3434 0.4056 -0.0365 0.0169  0.0203  552 ARG D CA  
12214 C C   . ARG D 251 ? 0.7939 0.3233 0.3809 -0.0520 0.0166  0.0160  552 ARG D C   
12215 O O   . ARG D 251 ? 0.7025 0.2756 0.3244 -0.0578 0.0167  0.0147  552 ARG D O   
12216 C CB  . ARG D 251 ? 0.8863 0.3698 0.4333 -0.0526 0.0153  0.0238  552 ARG D CB  
12217 C CG  . ARG D 251 ? 0.8173 0.3308 0.3829 -0.0759 0.0148  0.0247  552 ARG D CG  
12218 C CD  . ARG D 251 ? 0.8478 0.3924 0.4392 -0.0682 0.0154  0.0278  552 ARG D CD  
12219 N NE  . ARG D 251 ? 0.8700 0.4307 0.4673 -0.0906 0.0155  0.0292  552 ARG D NE  
12220 C CZ  . ARG D 251 ? 0.7804 0.3770 0.4052 -0.0906 0.0164  0.0307  552 ARG D CZ  
12221 N NH1 . ARG D 251 ? 0.7651 0.3746 0.3924 -0.1114 0.0171  0.0317  552 ARG D NH1 
12222 N NH2 . ARG D 251 ? 0.6549 0.2749 0.3039 -0.0704 0.0168  0.0309  552 ARG D NH2 
12223 N N   . HIS D 252 ? 0.7494 0.2395 0.3029 -0.0581 0.0159  0.0138  553 HIS D N   
12224 C CA  . HIS D 252 ? 0.7345 0.2321 0.2912 -0.0716 0.0149  0.0097  553 HIS D CA  
12225 C C   . HIS D 252 ? 0.8135 0.2893 0.3448 -0.0998 0.0123  0.0098  553 HIS D C   
12226 O O   . HIS D 252 ? 0.7973 0.2393 0.2963 -0.1028 0.0114  0.0109  553 HIS D O   
12227 C CB  . HIS D 252 ? 0.7624 0.2332 0.3002 -0.0561 0.0163  0.0064  553 HIS D CB  
12228 C CG  . HIS D 252 ? 0.7902 0.2771 0.3388 -0.0646 0.0155  0.0022  553 HIS D CG  
12229 N ND1 . HIS D 252 ? 0.8601 0.3275 0.3864 -0.0870 0.0127  0.0000  553 HIS D ND1 
12230 C CD2 . HIS D 252 ? 0.7841 0.3032 0.3612 -0.0539 0.0170  -0.0002 553 HIS D CD2 
12231 C CE1 . HIS D 252 ? 0.8312 0.3191 0.3727 -0.0889 0.0121  -0.0035 553 HIS D CE1 
12232 N NE2 . HIS D 252 ? 0.8038 0.3222 0.3756 -0.0689 0.0148  -0.0036 553 HIS D NE2 
12233 N N   . PRO D 253 ? 0.7166 0.2225 0.2665 -0.1189 0.0105  0.0077  554 PRO D N   
12234 C CA  . PRO D 253 ? 0.7816 0.2754 0.3113 -0.1473 0.0078  0.0077  554 PRO D CA  
12235 C C   . PRO D 253 ? 0.8972 0.3560 0.3902 -0.1504 0.0058  0.0047  554 PRO D C   
12236 O O   . PRO D 253 ? 0.9702 0.4209 0.4439 -0.1697 0.0035  0.0048  554 PRO D O   
12237 C CB  . PRO D 253 ? 0.7929 0.3362 0.3577 -0.1610 0.0062  0.0057  554 PRO D CB  
12238 C CG  . PRO D 253 ? 0.7772 0.3438 0.3683 -0.1394 0.0075  0.0033  554 PRO D CG  
12239 C CD  . PRO D 253 ? 0.6856 0.2426 0.2781 -0.1148 0.0107  0.0056  554 PRO D CD  
12240 N N   . LYS D 254 ? 0.8725 0.3113 0.3546 -0.1323 0.0070  0.0023  555 LYS D N   
12241 C CA  . LYS D 254 ? 0.9625 0.3680 0.4095 -0.1334 0.0058  -0.0002 555 LYS D CA  
12242 C C   . LYS D 254 ? 1.0138 0.3837 0.4349 -0.1092 0.0083  0.0001  555 LYS D C   
12243 O O   . LYS D 254 ? 1.1246 0.4606 0.5091 -0.1123 0.0073  0.0000  555 LYS D O   
12244 C CB  . LYS D 254 ? 1.0298 0.4472 0.4870 -0.1351 0.0050  -0.0039 555 LYS D CB  
12245 C CG  . LYS D 254 ? 1.1511 0.5404 0.5747 -0.1422 0.0032  -0.0062 555 LYS D CG  
12246 C CD  . LYS D 254 ? 1.1994 0.6043 0.6366 -0.1432 0.0022  -0.0097 555 LYS D CD  
12247 C CE  . LYS D 254 ? 1.1837 0.5931 0.6374 -0.1167 0.0063  -0.0114 555 LYS D CE  
12248 N NZ  . LYS D 254 ? 1.1853 0.6146 0.6565 -0.1176 0.0055  -0.0152 555 LYS D NZ  
12249 N N   . PHE D 255 ? 0.9712 0.3495 0.4105 -0.0850 0.0114  0.0007  556 PHE D N   
12250 C CA  . PHE D 255 ? 0.9338 0.2862 0.3538 -0.0589 0.0140  0.0008  556 PHE D CA  
12251 C C   . PHE D 255 ? 0.9633 0.3075 0.3773 -0.0523 0.0139  0.0047  556 PHE D C   
12252 O O   . PHE D 255 ? 0.9162 0.2826 0.3565 -0.0413 0.0152  0.0073  556 PHE D O   
12253 C CB  . PHE D 255 ? 0.9119 0.2826 0.3563 -0.0361 0.0175  -0.0005 556 PHE D CB  
12254 C CG  . PHE D 255 ? 0.9006 0.2754 0.3471 -0.0395 0.0179  -0.0047 556 PHE D CG  
12255 C CD1 . PHE D 255 ? 0.8927 0.2969 0.3711 -0.0322 0.0199  -0.0064 556 PHE D CD1 
12256 C CD2 . PHE D 255 ? 0.9238 0.2721 0.3388 -0.0498 0.0163  -0.0067 556 PHE D CD2 
12257 C CE1 . PHE D 255 ? 0.9099 0.3175 0.3891 -0.0352 0.0201  -0.0105 556 PHE D CE1 
12258 C CE2 . PHE D 255 ? 0.9696 0.3214 0.3856 -0.0528 0.0164  -0.0102 556 PHE D CE2 
12259 C CZ  . PHE D 255 ? 0.8565 0.2383 0.3048 -0.0454 0.0183  -0.0122 556 PHE D CZ  
12260 N N   . GLU D 256 ? 0.9754 0.2867 0.3532 -0.0589 0.0122  0.0051  557 GLU D N   
12261 C CA  . GLU D 256 ? 1.0274 0.3285 0.3965 -0.0536 0.0117  0.0085  557 GLU D CA  
12262 C C   . GLU D 256 ? 0.9946 0.2929 0.3675 -0.0219 0.0141  0.0098  557 GLU D C   
12263 O O   . GLU D 256 ? 0.9837 0.2869 0.3632 -0.0142 0.0137  0.0132  557 GLU D O   
12264 C CB  . GLU D 256 ? 1.1798 0.4429 0.5057 -0.0672 0.0093  0.0082  557 GLU D CB  
12265 C CG  . GLU D 256 ? 1.3556 0.6267 0.6794 -0.0998 0.0067  0.0075  557 GLU D CG  
12266 C CD  . GLU D 256 ? 1.5907 0.8243 0.8704 -0.1145 0.0044  0.0073  557 GLU D CD  
12267 O OE1 . GLU D 256 ? 1.6656 0.8627 0.9128 -0.0991 0.0048  0.0073  557 GLU D OE1 
12268 O OE2 . GLU D 256 ? 1.6472 0.8888 0.9241 -0.1416 0.0022  0.0073  557 GLU D OE2 
12269 N N   . TRP D 257 ? 1.0470 0.3409 0.4174 -0.0036 0.0165  0.0074  558 TRP D N   
12270 C CA  . TRP D 257 ? 1.0132 0.3117 0.3911 0.0268  0.0190  0.0086  558 TRP D CA  
12271 C C   . TRP D 257 ? 0.9939 0.3341 0.4157 0.0361  0.0205  0.0105  558 TRP D C   
12272 O O   . TRP D 257 ? 0.9879 0.3382 0.4199 0.0593  0.0219  0.0125  558 TRP D O   
12273 C CB  . TRP D 257 ? 1.0656 0.3501 0.4283 0.0430  0.0218  0.0054  558 TRP D CB  
12274 C CG  . TRP D 257 ? 1.0371 0.3360 0.4138 0.0334  0.0230  0.0022  558 TRP D CG  
12275 C CD1 . TRP D 257 ? 1.1353 0.4147 0.4898 0.0157  0.0217  -0.0005 558 TRP D CD1 
12276 C CD2 . TRP D 257 ? 0.9939 0.3293 0.4086 0.0408  0.0255  0.0012  558 TRP D CD2 
12277 N NE1 . TRP D 257 ? 1.1089 0.4106 0.4855 0.0120  0.0230  -0.0031 558 TRP D NE1 
12278 C CE2 . TRP D 257 ? 0.9512 0.2863 0.3641 0.0273  0.0255  -0.0024 558 TRP D CE2 
12279 C CE3 . TRP D 257 ? 0.8529 0.2209 0.3016 0.0575  0.0276  0.0029  558 TRP D CE3 
12280 C CZ2 . TRP D 257 ? 0.9680 0.3328 0.4112 0.0300  0.0276  -0.0045 558 TRP D CZ2 
12281 C CZ3 . TRP D 257 ? 0.8879 0.2855 0.3666 0.0597  0.0300  0.0008  558 TRP D CZ3 
12282 C CH2 . TRP D 257 ? 0.9123 0.3073 0.3876 0.0462  0.0301  -0.0031 558 TRP D CH2 
12283 N N   . PHE D 258 ? 0.8820 0.2473 0.3296 0.0188  0.0201  0.0102  559 PHE D N   
12284 C CA  . PHE D 258 ? 0.8528 0.2554 0.3397 0.0284  0.0219  0.0117  559 PHE D CA  
12285 C C   . PHE D 258 ? 0.8848 0.2989 0.3833 0.0366  0.0209  0.0169  559 PHE D C   
12286 O O   . PHE D 258 ? 0.8063 0.2442 0.3286 0.0557  0.0226  0.0186  559 PHE D O   
12287 C CB  . PHE D 258 ? 0.7697 0.1940 0.2782 0.0064  0.0213  0.0106  559 PHE D CB  
12288 C CG  . PHE D 258 ? 0.8628 0.3390 0.4163 0.0166  0.0233  0.0095  559 PHE D CG  
12289 C CD1 . PHE D 258 ? 0.7719 0.2576 0.3333 0.0216  0.0254  0.0053  559 PHE D CD1 
12290 C CD2 . PHE D 258 ? 0.7749 0.2899 0.3612 0.0207  0.0231  0.0125  559 PHE D CD2 
12291 C CE1 . PHE D 258 ? 0.7367 0.2689 0.3374 0.0298  0.0273  0.0044  559 PHE D CE1 
12292 C CE2 . PHE D 258 ? 0.7629 0.3239 0.3882 0.0289  0.0249  0.0114  559 PHE D CE2 
12293 C CZ  . PHE D 258 ? 0.7099 0.2794 0.3424 0.0331  0.0270  0.0074  559 PHE D CZ  
12294 N N   . LYS D 259 ? 0.9019 0.3008 0.3839 0.0221  0.0182  0.0193  560 LYS D N   
12295 C CA  . LYS D 259 ? 0.9695 0.3780 0.4602 0.0291  0.0170  0.0243  560 LYS D CA  
12296 C C   . LYS D 259 ? 0.9960 0.3986 0.4803 0.0585  0.0175  0.0252  560 LYS D C   
12297 O O   . LYS D 259 ? 0.9062 0.3317 0.4115 0.0727  0.0172  0.0288  560 LYS D O   
12298 C CB  . LYS D 259 ? 1.0179 0.4076 0.4873 0.0085  0.0143  0.0260  560 LYS D CB  
12299 C CG  . LYS D 259 ? 1.0933 0.4415 0.5207 0.0063  0.0131  0.0233  560 LYS D CG  
12300 C CD  . LYS D 259 ? 1.1642 0.4956 0.5715 -0.0121 0.0107  0.0254  560 LYS D CD  
12301 C CE  . LYS D 259 ? 1.2293 0.5173 0.5919 -0.0175 0.0093  0.0226  560 LYS D CE  
12302 N NZ  . LYS D 259 ? 1.2543 0.5358 0.6081 -0.0322 0.0097  0.0183  560 LYS D NZ  
12303 N N   . ASP D 260 ? 0.9833 0.3577 0.4391 0.0680  0.0182  0.0220  561 ASP D N   
12304 C CA  . ASP D 260 ? 1.1055 0.4747 0.5530 0.0957  0.0188  0.0227  561 ASP D CA  
12305 C C   . ASP D 260 ? 1.0113 0.4173 0.4922 0.1170  0.0215  0.0229  561 ASP D C   
12306 O O   . ASP D 260 ? 1.0489 0.4627 0.5321 0.1400  0.0216  0.0244  561 ASP D O   
12307 C CB  . ASP D 260 ? 1.2884 0.6206 0.6980 0.1007  0.0196  0.0193  561 ASP D CB  
12308 C CG  . ASP D 260 ? 1.4159 0.7114 0.7906 0.0780  0.0170  0.0186  561 ASP D CG  
12309 O OD1 . ASP D 260 ? 1.4408 0.7352 0.8149 0.0659  0.0144  0.0216  561 ASP D OD1 
12310 O OD2 . ASP D 260 ? 1.4993 0.7683 0.8471 0.0718  0.0176  0.0153  561 ASP D OD2 
12311 N N   . LEU D 261 ? 0.9159 0.3459 0.4225 0.1099  0.0236  0.0211  562 LEU D N   
12312 C CA  . LEU D 261 ? 0.9081 0.3760 0.4482 0.1283  0.0262  0.0212  562 LEU D CA  
12313 C C   . LEU D 261 ? 0.8861 0.3810 0.4496 0.1353  0.0241  0.0263  562 LEU D C   
12314 O O   . LEU D 261 ? 0.8588 0.3870 0.4485 0.1529  0.0256  0.0269  562 LEU D O   
12315 C CB  . LEU D 261 ? 0.8873 0.3733 0.4484 0.1172  0.0287  0.0182  562 LEU D CB  
12316 C CG  . LEU D 261 ? 0.9180 0.3822 0.4592 0.1102  0.0306  0.0130  562 LEU D CG  
12317 C CD1 . LEU D 261 ? 0.7982 0.2863 0.3628 0.0930  0.0315  0.0101  562 LEU D CD1 
12318 C CD2 . LEU D 261 ? 0.9568 0.4227 0.4931 0.1338  0.0342  0.0108  562 LEU D CD2 
12319 N N   . GLY D 262 ? 0.8920 0.3755 0.4470 0.1208  0.0206  0.0300  563 GLY D N   
12320 C CA  . GLY D 262 ? 0.8207 0.3324 0.3974 0.1242  0.0181  0.0345  563 GLY D CA  
12321 C C   . GLY D 262 ? 0.7946 0.3631 0.4183 0.1163  0.0191  0.0329  563 GLY D C   
12322 O O   . GLY D 262 ? 0.7663 0.3672 0.4137 0.1254  0.0178  0.0352  563 GLY D O   
12323 N N   . LEU D 263 ? 0.6992 0.2798 0.3358 0.0997  0.0211  0.0289  564 LEU D N   
12324 C CA  . LEU D 263 ? 0.6428 0.2734 0.3210 0.0919  0.0220  0.0273  564 LEU D CA  
12325 C C   . LEU D 263 ? 0.6560 0.3000 0.3448 0.0732  0.0196  0.0294  564 LEU D C   
12326 O O   . LEU D 263 ? 0.6700 0.2872 0.3367 0.0577  0.0183  0.0304  564 LEU D O   
12327 C CB  . LEU D 263 ? 0.6477 0.2855 0.3343 0.0824  0.0246  0.0226  564 LEU D CB  
12328 C CG  . LEU D 263 ? 0.7394 0.3661 0.4163 0.1003  0.0278  0.0200  564 LEU D CG  
12329 C CD1 . LEU D 263 ? 0.7643 0.3901 0.4424 0.0880  0.0297  0.0155  564 LEU D CD1 
12330 C CD2 . LEU D 263 ? 0.6958 0.3600 0.4004 0.1193  0.0295  0.0207  564 LEU D CD2 
12331 N N   . LYS D 264 ? 0.5887 0.2747 0.3109 0.0742  0.0193  0.0299  565 LYS D N   
12332 C CA  . LYS D 264 ? 0.6327 0.3381 0.3703 0.0562  0.0182  0.0306  565 LYS D CA  
12333 C C   . LYS D 264 ? 0.6048 0.3554 0.3802 0.0560  0.0195  0.0283  565 LYS D C   
12334 O O   . LYS D 264 ? 0.6263 0.3929 0.4148 0.0697  0.0209  0.0272  565 LYS D O   
12335 C CB  . LYS D 264 ? 0.7022 0.4003 0.4301 0.0575  0.0154  0.0352  565 LYS D CB  
12336 C CG  . LYS D 264 ? 0.7102 0.4300 0.4529 0.0763  0.0139  0.0374  565 LYS D CG  
12337 C CD  . LYS D 264 ? 0.7425 0.4551 0.4747 0.0762  0.0104  0.0421  565 LYS D CD  
12338 C CE  . LYS D 264 ? 0.8397 0.5401 0.5579 0.0992  0.0079  0.0457  565 LYS D CE  
12339 N NZ  . LYS D 264 ? 0.8652 0.5627 0.5756 0.1000  0.0039  0.0505  565 LYS D NZ  
12340 N N   . TRP D 265 ? 0.4865 0.2570 0.2780 0.0403  0.0192  0.0277  566 TRP D N   
12341 C CA  . TRP D 265 ? 0.4536 0.2637 0.2778 0.0404  0.0199  0.0262  566 TRP D CA  
12342 C C   . TRP D 265 ? 0.5529 0.3764 0.3856 0.0289  0.0187  0.0274  566 TRP D C   
12343 O O   . TRP D 265 ? 0.5839 0.3890 0.3995 0.0183  0.0180  0.0289  566 TRP D O   
12344 C CB  . TRP D 265 ? 0.3852 0.2087 0.2235 0.0341  0.0220  0.0222  566 TRP D CB  
12345 C CG  . TRP D 265 ? 0.3545 0.2112 0.2203 0.0402  0.0230  0.0209  566 TRP D CG  
12346 C CD1 . TRP D 265 ? 0.3373 0.2201 0.2251 0.0318  0.0232  0.0193  566 TRP D CD1 
12347 C CD2 . TRP D 265 ? 0.4037 0.2704 0.2765 0.0559  0.0240  0.0211  566 TRP D CD2 
12348 N NE1 . TRP D 265 ? 0.3420 0.2477 0.2483 0.0399  0.0241  0.0186  566 TRP D NE1 
12349 C CE2 . TRP D 265 ? 0.3751 0.2735 0.2738 0.0541  0.0248  0.0197  566 TRP D CE2 
12350 C CE3 . TRP D 265 ? 0.4104 0.2626 0.2694 0.0715  0.0246  0.0223  566 TRP D CE3 
12351 C CZ2 . TRP D 265 ? 0.3958 0.3132 0.3075 0.0653  0.0261  0.0196  566 TRP D CZ2 
12352 C CZ3 . TRP D 265 ? 0.3744 0.2483 0.2482 0.0843  0.0261  0.0221  566 TRP D CZ3 
12353 C CH2 . TRP D 265 ? 0.3361 0.2429 0.2362 0.0801  0.0269  0.0208  566 TRP D CH2 
12354 N N   . TYR D 266 ? 0.4743 0.3292 0.3319 0.0308  0.0187  0.0268  567 TYR D N   
12355 C CA  . TYR D 266 ? 0.4544 0.3237 0.3210 0.0210  0.0180  0.0273  567 TYR D CA  
12356 C C   . TYR D 266 ? 0.4128 0.2963 0.2924 0.0074  0.0199  0.0240  567 TYR D C   
12357 O O   . TYR D 266 ? 0.3728 0.2634 0.2616 0.0077  0.0211  0.0212  567 TYR D O   
12358 C CB  . TYR D 266 ? 0.3587 0.2529 0.2431 0.0291  0.0167  0.0281  567 TYR D CB  
12359 C CG  . TYR D 266 ? 0.3705 0.2857 0.2744 0.0360  0.0179  0.0258  567 TYR D CG  
12360 C CD1 . TYR D 266 ? 0.3414 0.2779 0.2646 0.0285  0.0193  0.0228  567 TYR D CD1 
12361 C CD2 . TYR D 266 ? 0.3951 0.3085 0.2969 0.0501  0.0178  0.0267  567 TYR D CD2 
12362 C CE1 . TYR D 266 ? 0.3622 0.3154 0.3006 0.0334  0.0204  0.0209  567 TYR D CE1 
12363 C CE2 . TYR D 266 ? 0.4126 0.3463 0.3317 0.0549  0.0194  0.0246  567 TYR D CE2 
12364 C CZ  . TYR D 266 ? 0.4213 0.3737 0.3579 0.0457  0.0207  0.0219  567 TYR D CZ  
12365 O OH  . TYR D 266 ? 0.4159 0.3863 0.3675 0.0491  0.0223  0.0202  567 TYR D OH  
12366 N N   . GLY D 267 ? 0.3622 0.2507 0.2423 -0.0038 0.0201  0.0243  568 GLY D N   
12367 C CA  . GLY D 267 ? 0.4055 0.3083 0.2967 -0.0161 0.0219  0.0213  568 GLY D CA  
12368 C C   . GLY D 267 ? 0.3876 0.3190 0.3035 -0.0142 0.0227  0.0186  568 GLY D C   
12369 O O   . GLY D 267 ? 0.3926 0.3352 0.3185 -0.0198 0.0238  0.0159  568 GLY D O   
12370 N N   . LEU D 268 ? 0.3542 0.2967 0.2787 -0.0064 0.0218  0.0195  569 LEU D N   
12371 C CA  . LEU D 268 ? 0.3094 0.2753 0.2530 -0.0070 0.0224  0.0171  569 LEU D CA  
12372 C C   . LEU D 268 ? 0.3350 0.3112 0.2908 0.0016  0.0221  0.0160  569 LEU D C   
12373 O O   . LEU D 268 ? 0.3496 0.3277 0.3057 0.0097  0.0206  0.0178  569 LEU D O   
12374 C CB  . LEU D 268 ? 0.2915 0.2632 0.2347 -0.0078 0.0217  0.0185  569 LEU D CB  
12375 C CG  . LEU D 268 ? 0.3245 0.3165 0.2832 -0.0099 0.0226  0.0156  569 LEU D CG  
12376 C CD1 . LEU D 268 ? 0.3545 0.3527 0.3168 -0.0186 0.0252  0.0130  569 LEU D CD1 
12377 C CD2 . LEU D 268 ? 0.2918 0.2890 0.2493 -0.0091 0.0213  0.0168  569 LEU D CD2 
12378 N N   . PRO D 269 ? 0.3348 0.3188 0.3003 0.0001  0.0233  0.0133  570 PRO D N   
12379 C CA  . PRO D 269 ? 0.2936 0.2885 0.2705 0.0064  0.0234  0.0123  570 PRO D CA  
12380 C C   . PRO D 269 ? 0.3052 0.3159 0.2933 0.0046  0.0233  0.0111  570 PRO D C   
12381 O O   . PRO D 269 ? 0.2660 0.2825 0.2588 -0.0007 0.0242  0.0088  570 PRO D O   
12382 C CB  . PRO D 269 ? 0.2134 0.2073 0.1930 0.0041  0.0246  0.0101  570 PRO D CB  
12383 C CG  . PRO D 269 ? 0.2146 0.2080 0.1922 -0.0047 0.0249  0.0089  570 PRO D CG  
12384 C CD  . PRO D 269 ? 0.2873 0.2726 0.2542 -0.0080 0.0245  0.0111  570 PRO D CD  
12385 N N   . ALA D 270 ? 0.2023 0.2200 0.1938 0.0093  0.0220  0.0123  571 ALA D N   
12386 C CA  . ALA D 270 ? 0.1943 0.2239 0.1927 0.0066  0.0213  0.0113  571 ALA D CA  
12387 C C   . ALA D 270 ? 0.2637 0.3045 0.2704 0.0100  0.0206  0.0113  571 ALA D C   
12388 O O   . ALA D 270 ? 0.3084 0.3539 0.3149 0.0149  0.0189  0.0136  571 ALA D O   
12389 C CB  . ALA D 270 ? 0.2023 0.2296 0.1935 0.0057  0.0196  0.0132  571 ALA D CB  
12390 N N   . VAL D 271 ? 0.2721 0.3175 0.2855 0.0075  0.0219  0.0089  572 VAL D N   
12391 C CA  . VAL D 271 ? 0.2880 0.3436 0.3082 0.0087  0.0218  0.0090  572 VAL D CA  
12392 C C   . VAL D 271 ? 0.2467 0.3114 0.2692 0.0049  0.0199  0.0087  572 VAL D C   
12393 O O   . VAL D 271 ? 0.2670 0.3290 0.2878 0.0002  0.0200  0.0066  572 VAL D O   
12394 C CB  . VAL D 271 ? 0.2301 0.2841 0.2534 0.0065  0.0238  0.0069  572 VAL D CB  
12395 C CG1 . VAL D 271 ? 0.1679 0.2325 0.1967 0.0048  0.0238  0.0070  572 VAL D CG1 
12396 C CG2 . VAL D 271 ? 0.2221 0.2680 0.2425 0.0099  0.0253  0.0072  572 VAL D CG2 
12397 N N   . SER D 272 ? 0.2437 0.3202 0.2701 0.0069  0.0183  0.0106  573 SER D N   
12398 C CA  . SER D 272 ? 0.2958 0.3814 0.3231 0.0025  0.0156  0.0105  573 SER D CA  
12399 C C   . SER D 272 ? 0.3011 0.4017 0.3353 -0.0008 0.0149  0.0107  573 SER D C   
12400 O O   . SER D 272 ? 0.2895 0.4001 0.3246 -0.0050 0.0120  0.0110  573 SER D O   
12401 C CB  . SER D 272 ? 0.1873 0.2749 0.2106 0.0067  0.0126  0.0133  573 SER D CB  
12402 O OG  . SER D 272 ? 0.2210 0.3121 0.2454 0.0157  0.0123  0.0162  573 SER D OG  
12403 N N   . ASN D 273 ? 0.2482 0.3511 0.2866 -0.0001 0.0175  0.0104  574 ASN D N   
12404 C CA  . ASN D 273 ? 0.2520 0.3706 0.2965 -0.0047 0.0173  0.0108  574 ASN D CA  
12405 C C   . ASN D 273 ? 0.2440 0.3551 0.2861 -0.0128 0.0193  0.0084  574 ASN D C   
12406 O O   . ASN D 273 ? 0.2466 0.3683 0.2919 -0.0187 0.0197  0.0087  574 ASN D O   
12407 C CB  . ASN D 273 ? 0.2510 0.3820 0.3017 0.0029  0.0189  0.0131  574 ASN D CB  
12408 C CG  . ASN D 273 ? 0.2485 0.3669 0.2968 0.0074  0.0227  0.0124  574 ASN D CG  
12409 O OD1 . ASN D 273 ? 0.3018 0.4031 0.3444 0.0061  0.0236  0.0107  574 ASN D OD1 
12410 N ND2 . ASN D 273 ? 0.3127 0.4410 0.3651 0.0133  0.0250  0.0137  574 ASN D ND2 
12411 N N   . MET D 274 ? 0.1943 0.2879 0.2301 -0.0135 0.0203  0.0062  575 MET D N   
12412 C CA  . MET D 274 ? 0.3113 0.3949 0.3425 -0.0196 0.0217  0.0040  575 MET D CA  
12413 C C   . MET D 274 ? 0.3243 0.4030 0.3490 -0.0271 0.0197  0.0020  575 MET D C   
12414 O O   . MET D 274 ? 0.2844 0.3668 0.3082 -0.0278 0.0174  0.0019  575 MET D O   
12415 C CB  . MET D 274 ? 0.2781 0.3468 0.3059 -0.0151 0.0236  0.0027  575 MET D CB  
12416 C CG  . MET D 274 ? 0.2773 0.3483 0.3088 -0.0096 0.0256  0.0043  575 MET D CG  
12417 S SD  . MET D 274 ? 0.2992 0.3548 0.3263 -0.0060 0.0270  0.0028  575 MET D SD  
12418 C CE  . MET D 274 ? 0.2753 0.3252 0.2984 -0.0108 0.0284  0.0023  575 MET D CE  
12419 N N   . LEU D 275 ? 0.2656 0.3339 0.2836 -0.0330 0.0206  0.0003  576 LEU D N   
12420 C CA  . LEU D 275 ? 0.3464 0.4054 0.3544 -0.0408 0.0191  -0.0021 576 LEU D CA  
12421 C C   . LEU D 275 ? 0.2984 0.3366 0.2971 -0.0374 0.0205  -0.0049 576 LEU D C   
12422 O O   . LEU D 275 ? 0.3248 0.3555 0.3226 -0.0344 0.0223  -0.0047 576 LEU D O   
12423 C CB  . LEU D 275 ? 0.3784 0.4415 0.3835 -0.0517 0.0188  -0.0015 576 LEU D CB  
12424 C CG  . LEU D 275 ? 0.5081 0.5592 0.4996 -0.0625 0.0170  -0.0039 576 LEU D CG  
12425 C CD1 . LEU D 275 ? 0.4922 0.5591 0.4859 -0.0746 0.0157  -0.0022 576 LEU D CD1 
12426 C CD2 . LEU D 275 ? 0.4811 0.5064 0.4587 -0.0628 0.0188  -0.0061 576 LEU D CD2 
12427 N N   . LEU D 276 ? 0.2326 0.2627 0.2245 -0.0369 0.0198  -0.0074 577 LEU D N   
12428 C CA  . LEU D 276 ? 0.3028 0.3154 0.2859 -0.0321 0.0212  -0.0103 577 LEU D CA  
12429 C C   . LEU D 276 ? 0.3135 0.3091 0.2811 -0.0391 0.0206  -0.0127 577 LEU D C   
12430 O O   . LEU D 276 ? 0.3441 0.3389 0.3053 -0.0457 0.0189  -0.0140 577 LEU D O   
12431 C CB  . LEU D 276 ? 0.2439 0.2584 0.2282 -0.0265 0.0216  -0.0118 577 LEU D CB  
12432 C CG  . LEU D 276 ? 0.3109 0.3110 0.2853 -0.0219 0.0231  -0.0156 577 LEU D CG  
12433 C CD1 . LEU D 276 ? 0.2344 0.2282 0.2095 -0.0146 0.0246  -0.0160 577 LEU D CD1 
12434 C CD2 . LEU D 276 ? 0.2974 0.3047 0.2744 -0.0186 0.0239  -0.0165 577 LEU D CD2 
12435 N N   . GLU D 277 ? 0.2988 0.2794 0.2585 -0.0380 0.0216  -0.0132 578 GLU D N   
12436 C CA  . GLU D 277 ? 0.3332 0.2925 0.2744 -0.0447 0.0211  -0.0153 578 GLU D CA  
12437 C C   . GLU D 277 ? 0.3903 0.3297 0.3197 -0.0353 0.0221  -0.0187 578 GLU D C   
12438 O O   . GLU D 277 ? 0.3399 0.2767 0.2722 -0.0260 0.0232  -0.0183 578 GLU D O   
12439 C CB  . GLU D 277 ? 0.4125 0.3670 0.3501 -0.0513 0.0214  -0.0130 578 GLU D CB  
12440 C CG  . GLU D 277 ? 0.5754 0.5053 0.4909 -0.0607 0.0207  -0.0146 578 GLU D CG  
12441 C CD  . GLU D 277 ? 0.7639 0.6670 0.6640 -0.0520 0.0215  -0.0165 578 GLU D CD  
12442 O OE1 . GLU D 277 ? 0.7996 0.7063 0.7078 -0.0421 0.0225  -0.0152 578 GLU D OE1 
12443 O OE2 . GLU D 277 ? 0.8177 0.6957 0.6967 -0.0547 0.0209  -0.0193 578 GLU D OE2 
12444 N N   . ILE D 278 ? 0.4065 0.3336 0.3227 -0.0371 0.0217  -0.0220 579 ILE D N   
12445 C CA  . ILE D 278 ? 0.4201 0.3275 0.3226 -0.0274 0.0231  -0.0258 579 ILE D CA  
12446 C C   . ILE D 278 ? 0.4604 0.3402 0.3380 -0.0350 0.0221  -0.0284 579 ILE D C   
12447 O O   . ILE D 278 ? 0.4575 0.3371 0.3290 -0.0448 0.0208  -0.0296 579 ILE D O   
12448 C CB  . ILE D 278 ? 0.5028 0.4210 0.4115 -0.0202 0.0245  -0.0281 579 ILE D CB  
12449 C CG1 . ILE D 278 ? 0.3789 0.3225 0.3097 -0.0149 0.0253  -0.0254 579 ILE D CG1 
12450 C CG2 . ILE D 278 ? 0.4779 0.3772 0.3719 -0.0093 0.0265  -0.0323 579 ILE D CG2 
12451 C CD1 . ILE D 278 ? 0.3662 0.3215 0.3023 -0.0110 0.0267  -0.0270 579 ILE D CD1 
12452 N N   . GLY D 279 ? 0.4434 0.2986 0.3049 -0.0306 0.0225  -0.0293 580 GLY D N   
12453 C CA  . GLY D 279 ? 0.4773 0.2993 0.3102 -0.0362 0.0218  -0.0321 580 GLY D CA  
12454 C C   . GLY D 279 ? 0.5187 0.3376 0.3434 -0.0558 0.0196  -0.0310 580 GLY D C   
12455 O O   . GLY D 279 ? 0.5462 0.3444 0.3498 -0.0632 0.0186  -0.0341 580 GLY D O   
12456 N N   . GLY D 280 ? 0.4629 0.3024 0.3032 -0.0646 0.0189  -0.0267 581 GLY D N   
12457 C CA  . GLY D 280 ? 0.5154 0.3605 0.3527 -0.0835 0.0169  -0.0253 581 GLY D CA  
12458 C C   . GLY D 280 ? 0.5677 0.4409 0.4210 -0.0888 0.0153  -0.0250 581 GLY D C   
12459 O O   . GLY D 280 ? 0.5855 0.4727 0.4423 -0.1036 0.0133  -0.0230 581 GLY D O   
12460 N N   . LEU D 281 ? 0.4895 0.3723 0.3522 -0.0773 0.0160  -0.0266 582 LEU D N   
12461 C CA  . LEU D 281 ? 0.4746 0.3837 0.3522 -0.0808 0.0143  -0.0257 582 LEU D CA  
12462 C C   . LEU D 281 ? 0.4438 0.3830 0.3475 -0.0761 0.0148  -0.0214 582 LEU D C   
12463 O O   . LEU D 281 ? 0.4600 0.4004 0.3721 -0.0651 0.0171  -0.0204 582 LEU D O   
12464 C CB  . LEU D 281 ? 0.4571 0.3621 0.3312 -0.0714 0.0152  -0.0292 582 LEU D CB  
12465 C CG  . LEU D 281 ? 0.4575 0.3297 0.3038 -0.0721 0.0156  -0.0343 582 LEU D CG  
12466 C CD1 . LEU D 281 ? 0.4944 0.3665 0.3395 -0.0614 0.0176  -0.0377 582 LEU D CD1 
12467 C CD2 . LEU D 281 ? 0.4761 0.3402 0.3071 -0.0906 0.0121  -0.0350 582 LEU D CD2 
12468 N N   . GLU D 282 ? 0.4194 0.3825 0.3350 -0.0841 0.0124  -0.0189 583 GLU D N   
12469 C CA  . GLU D 282 ? 0.3409 0.3316 0.2789 -0.0801 0.0127  -0.0148 583 GLU D CA  
12470 C C   . GLU D 282 ? 0.4313 0.4406 0.3809 -0.0751 0.0112  -0.0140 583 GLU D C   
12471 O O   . GLU D 282 ? 0.3875 0.4071 0.3362 -0.0830 0.0079  -0.0138 583 GLU D O   
12472 C CB  . GLU D 282 ? 0.4868 0.4920 0.4292 -0.0925 0.0114  -0.0120 583 GLU D CB  
12473 C CG  . GLU D 282 ? 0.5587 0.5444 0.4876 -0.0994 0.0130  -0.0123 583 GLU D CG  
12474 C CD  . GLU D 282 ? 0.7099 0.7152 0.6468 -0.1105 0.0129  -0.0090 583 GLU D CD  
12475 O OE1 . GLU D 282 ? 0.8336 0.8359 0.7718 -0.1090 0.0157  -0.0073 583 GLU D OE1 
12476 O OE2 . GLU D 282 ? 0.6835 0.7088 0.6255 -0.1203 0.0101  -0.0081 583 GLU D OE2 
12477 N N   . PHE D 283 ? 0.3725 0.3857 0.3316 -0.0627 0.0132  -0.0134 584 PHE D N   
12478 C CA  . PHE D 283 ? 0.3123 0.3406 0.2809 -0.0575 0.0122  -0.0121 584 PHE D CA  
12479 C C   . PHE D 283 ? 0.3719 0.4217 0.3570 -0.0546 0.0117  -0.0078 584 PHE D C   
12480 O O   . PHE D 283 ? 0.3537 0.4044 0.3463 -0.0466 0.0142  -0.0066 584 PHE D O   
12481 C CB  . PHE D 283 ? 0.3231 0.3420 0.2901 -0.0473 0.0149  -0.0141 584 PHE D CB  
12482 C CG  . PHE D 283 ? 0.3438 0.3430 0.2942 -0.0481 0.0158  -0.0186 584 PHE D CG  
12483 C CD1 . PHE D 283 ? 0.3960 0.3764 0.3370 -0.0446 0.0181  -0.0211 584 PHE D CD1 
12484 C CD2 . PHE D 283 ? 0.3461 0.3444 0.2885 -0.0518 0.0142  -0.0204 584 PHE D CD2 
12485 C CE1 . PHE D 283 ? 0.3639 0.3244 0.2876 -0.0435 0.0192  -0.0255 584 PHE D CE1 
12486 C CE2 . PHE D 283 ? 0.3827 0.3614 0.3080 -0.0517 0.0155  -0.0250 584 PHE D CE2 
12487 C CZ  . PHE D 283 ? 0.4217 0.3813 0.3376 -0.0471 0.0181  -0.0276 584 PHE D CZ  
12488 N N   . SER D 284 ? 0.2873 0.3547 0.2773 -0.0611 0.0085  -0.0057 585 SER D N   
12489 C CA  . SER D 284 ? 0.3490 0.4381 0.3537 -0.0581 0.0082  -0.0018 585 SER D CA  
12490 C C   . SER D 284 ? 0.2912 0.3888 0.3038 -0.0474 0.0078  0.0004  585 SER D C   
12491 O O   . SER D 284 ? 0.2934 0.4048 0.3165 -0.0416 0.0082  0.0034  585 SER D O   
12492 C CB  . SER D 284 ? 0.3714 0.4796 0.3791 -0.0683 0.0047  -0.0003 585 SER D CB  
12493 O OG  . SER D 284 ? 0.3969 0.5054 0.3975 -0.0737 0.0007  -0.0015 585 SER D OG  
12494 N N   . ALA D 285 ? 0.3642 0.4532 0.3707 -0.0447 0.0071  -0.0009 586 ALA D N   
12495 C CA  . ALA D 285 ? 0.3062 0.3983 0.3166 -0.0357 0.0071  0.0012  586 ALA D CA  
12496 C C   . ALA D 285 ? 0.2498 0.3248 0.2539 -0.0321 0.0104  -0.0014 586 ALA D C   
12497 O O   . ALA D 285 ? 0.2880 0.3543 0.2829 -0.0351 0.0103  -0.0041 586 ALA D O   
12498 C CB  . ALA D 285 ? 0.3495 0.4516 0.3581 -0.0369 0.0028  0.0029  586 ALA D CB  
12499 N N   . CYS D 286 ? 0.2482 0.3197 0.2569 -0.0258 0.0132  -0.0008 587 CYS D N   
12500 C CA  . CYS D 286 ? 0.2591 0.3186 0.2639 -0.0226 0.0163  -0.0031 587 CYS D CA  
12501 C C   . CYS D 286 ? 0.3075 0.3681 0.3174 -0.0162 0.0177  -0.0009 587 CYS D C   
12502 O O   . CYS D 286 ? 0.3026 0.3585 0.3148 -0.0136 0.0200  -0.0017 587 CYS D O   
12503 C CB  . CYS D 286 ? 0.2780 0.3275 0.2796 -0.0240 0.0182  -0.0059 587 CYS D CB  
12504 S SG  . CYS D 286 ? 0.3086 0.3620 0.3176 -0.0233 0.0189  -0.0038 587 CYS D SG  
12505 N N   . PRO D 287 ? 0.3039 0.3691 0.3140 -0.0138 0.0162  0.0019  588 PRO D N   
12506 C CA  . PRO D 287 ? 0.2653 0.3280 0.2772 -0.0085 0.0174  0.0040  588 PRO D CA  
12507 C C   . PRO D 287 ? 0.2813 0.3362 0.2911 -0.0086 0.0204  0.0019  588 PRO D C   
12508 O O   . PRO D 287 ? 0.3329 0.3857 0.3385 -0.0109 0.0214  -0.0002 588 PRO D O   
12509 C CB  . PRO D 287 ? 0.2845 0.3492 0.2923 -0.0066 0.0150  0.0071  588 PRO D CB  
12510 C CG  . PRO D 287 ? 0.3184 0.3854 0.3215 -0.0115 0.0132  0.0058  588 PRO D CG  
12511 C CD  . PRO D 287 ? 0.2848 0.3550 0.2909 -0.0158 0.0131  0.0032  588 PRO D CD  
12512 N N   . PHE D 288 ? 0.2806 0.3328 0.2935 -0.0060 0.0218  0.0022  589 PHE D N   
12513 C CA  . PHE D 288 ? 0.1812 0.2295 0.1936 -0.0062 0.0241  0.0005  589 PHE D CA  
12514 C C   . PHE D 288 ? 0.2419 0.2862 0.2531 -0.0045 0.0243  0.0027  589 PHE D C   
12515 O O   . PHE D 288 ? 0.2785 0.3215 0.2901 -0.0014 0.0234  0.0047  589 PHE D O   
12516 C CB  . PHE D 288 ? 0.2429 0.2901 0.2583 -0.0056 0.0252  -0.0022 589 PHE D CB  
12517 C CG  . PHE D 288 ? 0.2442 0.2906 0.2628 -0.0040 0.0248  -0.0012 589 PHE D CG  
12518 C CD1 . PHE D 288 ? 0.2859 0.3299 0.3059 -0.0018 0.0254  -0.0003 589 PHE D CD1 
12519 C CD2 . PHE D 288 ? 0.2085 0.2567 0.2278 -0.0056 0.0239  -0.0012 589 PHE D CD2 
12520 C CE1 . PHE D 288 ? 0.2766 0.3196 0.2983 -0.0003 0.0255  0.0004  589 PHE D CE1 
12521 C CE2 . PHE D 288 ? 0.2329 0.2817 0.2548 -0.0049 0.0242  -0.0002 589 PHE D CE2 
12522 C CZ  . PHE D 288 ? 0.1890 0.2349 0.2120 -0.0017 0.0252  0.0006  589 PHE D CZ  
12523 N N   . SER D 289 ? 0.2540 0.2963 0.2626 -0.0068 0.0257  0.0020  590 SER D N   
12524 C CA  . SER D 289 ? 0.2249 0.2606 0.2287 -0.0073 0.0257  0.0041  590 SER D CA  
12525 C C   . SER D 289 ? 0.2177 0.2556 0.2230 -0.0108 0.0273  0.0023  590 SER D C   
12526 O O   . SER D 289 ? 0.2339 0.2794 0.2425 -0.0122 0.0287  -0.0001 590 SER D O   
12527 C CB  . SER D 289 ? 0.2813 0.3117 0.2763 -0.0088 0.0250  0.0067  590 SER D CB  
12528 O OG  . SER D 289 ? 0.3139 0.3479 0.3069 -0.0136 0.0265  0.0055  590 SER D OG  
12529 N N   . GLY D 290 ? 0.2459 0.2779 0.2484 -0.0116 0.0270  0.0032  591 GLY D N   
12530 C CA  . GLY D 290 ? 0.2627 0.2982 0.2656 -0.0165 0.0279  0.0019  591 GLY D CA  
12531 C C   . GLY D 290 ? 0.3296 0.3536 0.3218 -0.0211 0.0275  0.0041  591 GLY D C   
12532 O O   . GLY D 290 ? 0.3210 0.3376 0.3044 -0.0233 0.0276  0.0062  591 GLY D O   
12533 N N   . TRP D 291 ? 0.3070 0.3269 0.2974 -0.0227 0.0267  0.0038  592 TRP D N   
12534 C CA  . TRP D 291 ? 0.3098 0.3140 0.2867 -0.0271 0.0261  0.0057  592 TRP D CA  
12535 C C   . TRP D 291 ? 0.2998 0.2956 0.2745 -0.0233 0.0250  0.0054  592 TRP D C   
12536 O O   . TRP D 291 ? 0.2732 0.2778 0.2575 -0.0197 0.0247  0.0037  592 TRP D O   
12537 C CB  . TRP D 291 ? 0.2439 0.2520 0.2170 -0.0381 0.0266  0.0053  592 TRP D CB  
12538 C CG  . TRP D 291 ? 0.2954 0.3209 0.2799 -0.0403 0.0265  0.0027  592 TRP D CG  
12539 C CD1 . TRP D 291 ? 0.3693 0.3941 0.3545 -0.0408 0.0247  0.0018  592 TRP D CD1 
12540 C CD2 . TRP D 291 ? 0.3215 0.3678 0.3176 -0.0412 0.0280  0.0008  592 TRP D CD2 
12541 N NE1 . TRP D 291 ? 0.2887 0.3337 0.2858 -0.0418 0.0244  -0.0004 592 TRP D NE1 
12542 C CE2 . TRP D 291 ? 0.3114 0.3700 0.3155 -0.0414 0.0267  -0.0011 592 TRP D CE2 
12543 C CE3 . TRP D 291 ? 0.3029 0.3586 0.3024 -0.0412 0.0303  0.0003  592 TRP D CE3 
12544 C CZ2 . TRP D 291 ? 0.3330 0.4134 0.3488 -0.0402 0.0276  -0.0034 592 TRP D CZ2 
12545 C CZ3 . TRP D 291 ? 0.3537 0.4301 0.3642 -0.0405 0.0319  -0.0023 592 TRP D CZ3 
12546 C CH2 . TRP D 291 ? 0.4259 0.5148 0.4447 -0.0394 0.0305  -0.0040 592 TRP D CH2 
12547 N N   . TYR D 292 ? 0.3148 0.2917 0.2750 -0.0237 0.0244  0.0070  593 TYR D N   
12548 C CA  . TYR D 292 ? 0.3408 0.3078 0.2969 -0.0183 0.0240  0.0067  593 TYR D CA  
12549 C C   . TYR D 292 ? 0.3661 0.3340 0.3214 -0.0244 0.0229  0.0048  593 TYR D C   
12550 O O   . TYR D 292 ? 0.3234 0.2925 0.2748 -0.0344 0.0222  0.0045  593 TYR D O   
12551 C CB  . TYR D 292 ? 0.3245 0.2684 0.2626 -0.0151 0.0239  0.0087  593 TYR D CB  
12552 C CG  . TYR D 292 ? 0.2677 0.2111 0.2076 -0.0037 0.0245  0.0103  593 TYR D CG  
12553 C CD1 . TYR D 292 ? 0.3427 0.2786 0.2746 -0.0012 0.0240  0.0128  593 TYR D CD1 
12554 C CD2 . TYR D 292 ? 0.2957 0.2474 0.2450 0.0041  0.0253  0.0094  593 TYR D CD2 
12555 C CE1 . TYR D 292 ? 0.2814 0.2199 0.2158 0.0096  0.0239  0.0144  593 TYR D CE1 
12556 C CE2 . TYR D 292 ? 0.3299 0.2853 0.2821 0.0138  0.0258  0.0109  593 TYR D CE2 
12557 C CZ  . TYR D 292 ? 0.2818 0.2314 0.2270 0.0169  0.0248  0.0134  593 TYR D CZ  
12558 O OH  . TYR D 292 ? 0.3355 0.2920 0.2847 0.0269  0.0247  0.0149  593 TYR D OH  
12559 N N   . MET D 293 ? 0.3710 0.3391 0.3297 -0.0188 0.0228  0.0038  594 MET D N   
12560 C CA  . MET D 293 ? 0.2691 0.2290 0.2200 -0.0226 0.0215  0.0026  594 MET D CA  
12561 C C   . MET D 293 ? 0.3028 0.2385 0.2357 -0.0190 0.0222  0.0036  594 MET D C   
12562 O O   . MET D 293 ? 0.3367 0.2687 0.2697 -0.0092 0.0239  0.0046  594 MET D O   
12563 C CB  . MET D 293 ? 0.2584 0.2289 0.2197 -0.0180 0.0211  0.0012  594 MET D CB  
12564 C CG  . MET D 293 ? 0.2645 0.2294 0.2187 -0.0227 0.0190  -0.0001 594 MET D CG  
12565 S SD  . MET D 293 ? 0.3276 0.3062 0.2938 -0.0178 0.0180  -0.0013 594 MET D SD  
12566 C CE  . MET D 293 ? 0.3138 0.2829 0.2774 -0.0075 0.0214  -0.0006 594 MET D CE  
12567 N N   . GLY D 294 ? 0.3585 0.2778 0.2751 -0.0270 0.0209  0.0033  595 GLY D N   
12568 C CA  . GLY D 294 ? 0.3282 0.2198 0.2233 -0.0238 0.0216  0.0041  595 GLY D CA  
12569 C C   . GLY D 294 ? 0.3861 0.2704 0.2785 -0.0114 0.0235  0.0036  595 GLY D C   
12570 O O   . GLY D 294 ? 0.4059 0.2747 0.2871 -0.0025 0.0250  0.0048  595 GLY D O   
12571 N N   . THR D 295 ? 0.3380 0.2336 0.2401 -0.0100 0.0234  0.0019  596 THR D N   
12572 C CA  . THR D 295 ? 0.3864 0.2764 0.2854 0.0006  0.0258  0.0013  596 THR D CA  
12573 C C   . THR D 295 ? 0.3416 0.2425 0.2515 0.0118  0.0284  0.0028  596 THR D C   
12574 O O   . THR D 295 ? 0.3418 0.2357 0.2458 0.0220  0.0310  0.0029  596 THR D O   
12575 C CB  . THR D 295 ? 0.3833 0.2845 0.2907 -0.0013 0.0252  -0.0005 596 THR D CB  
12576 O OG1 . THR D 295 ? 0.3089 0.2337 0.2362 -0.0036 0.0241  -0.0002 596 THR D OG1 
12577 C CG2 . THR D 295 ? 0.3897 0.2787 0.2835 -0.0113 0.0223  -0.0021 596 THR D CG2 
12578 N N   . GLU D 296 ? 0.3940 0.3132 0.3196 0.0102  0.0278  0.0039  597 GLU D N   
12579 C CA  . GLU D 296 ? 0.4342 0.3646 0.3694 0.0191  0.0294  0.0054  597 GLU D CA  
12580 C C   . GLU D 296 ? 0.4351 0.3496 0.3564 0.0272  0.0303  0.0071  597 GLU D C   
12581 O O   . GLU D 296 ? 0.4443 0.3633 0.3679 0.0381  0.0323  0.0078  597 GLU D O   
12582 C CB  . GLU D 296 ? 0.4757 0.4230 0.4249 0.0145  0.0281  0.0062  597 GLU D CB  
12583 C CG  . GLU D 296 ? 0.3836 0.3469 0.3466 0.0094  0.0274  0.0046  597 GLU D CG  
12584 C CD  . GLU D 296 ? 0.3018 0.2791 0.2759 0.0064  0.0266  0.0050  597 GLU D CD  
12585 O OE1 . GLU D 296 ? 0.2373 0.2242 0.2193 0.0110  0.0274  0.0058  597 GLU D OE1 
12586 O OE2 . GLU D 296 ? 0.2460 0.2252 0.2202 -0.0007 0.0253  0.0045  597 GLU D OE2 
12587 N N   . ILE D 297 ? 0.3866 0.2828 0.2926 0.0221  0.0286  0.0078  598 ILE D N   
12588 C CA  . ILE D 297 ? 0.3984 0.2735 0.2863 0.0300  0.0289  0.0096  598 ILE D CA  
12589 C C   . ILE D 297 ? 0.4440 0.2956 0.3124 0.0346  0.0304  0.0081  598 ILE D C   
12590 O O   . ILE D 297 ? 0.4154 0.2601 0.2770 0.0483  0.0325  0.0085  598 ILE D O   
12591 C CB  . ILE D 297 ? 0.3829 0.2451 0.2594 0.0212  0.0267  0.0112  598 ILE D CB  
12592 C CG1 . ILE D 297 ? 0.4008 0.2866 0.2960 0.0164  0.0257  0.0123  598 ILE D CG1 
12593 C CG2 . ILE D 297 ? 0.3728 0.2100 0.2279 0.0306  0.0266  0.0135  598 ILE D CG2 
12594 C CD1 . ILE D 297 ? 0.3751 0.2533 0.2619 0.0042  0.0241  0.0133  598 ILE D CD1 
12595 N N   . GLY D 298 ? 0.4078 0.2469 0.2660 0.0235  0.0292  0.0062  599 GLY D N   
12596 C CA  . GLY D 298 ? 0.4679 0.2788 0.3023 0.0257  0.0300  0.0046  599 GLY D CA  
12597 C C   . GLY D 298 ? 0.4365 0.2530 0.2748 0.0353  0.0331  0.0027  599 GLY D C   
12598 O O   . GLY D 298 ? 0.4984 0.2936 0.3180 0.0446  0.0353  0.0017  599 GLY D O   
12599 N N   . VAL D 299 ? 0.4444 0.2879 0.3051 0.0335  0.0336  0.0020  600 VAL D N   
12600 C CA  . VAL D 299 ? 0.4114 0.2611 0.2755 0.0412  0.0369  0.0005  600 VAL D CA  
12601 C C   . VAL D 299 ? 0.4548 0.3240 0.3334 0.0539  0.0400  0.0020  600 VAL D C   
12602 O O   . VAL D 299 ? 0.4973 0.3609 0.3681 0.0662  0.0436  0.0015  600 VAL D O   
12603 C CB  . VAL D 299 ? 0.4180 0.2826 0.2943 0.0318  0.0356  -0.0010 600 VAL D CB  
12604 C CG1 . VAL D 299 ? 0.4015 0.2688 0.2773 0.0390  0.0393  -0.0024 600 VAL D CG1 
12605 C CG2 . VAL D 299 ? 0.4829 0.3331 0.3469 0.0187  0.0318  -0.0024 600 VAL D CG2 
12606 N N   . ARG D 300 ? 0.4197 0.3131 0.3191 0.0509  0.0388  0.0035  601 ARG D N   
12607 C CA  . ARG D 300 ? 0.3593 0.2751 0.2741 0.0601  0.0415  0.0047  601 ARG D CA  
12608 C C   . ARG D 300 ? 0.4100 0.3236 0.3208 0.0708  0.0415  0.0069  601 ARG D C   
12609 O O   . ARG D 300 ? 0.4464 0.3626 0.3546 0.0838  0.0446  0.0071  601 ARG D O   
12610 C CB  . ARG D 300 ? 0.2734 0.2139 0.2096 0.0522  0.0401  0.0053  601 ARG D CB  
12611 C CG  . ARG D 300 ? 0.2912 0.2337 0.2309 0.0431  0.0394  0.0035  601 ARG D CG  
12612 C CD  . ARG D 300 ? 0.3286 0.2706 0.2646 0.0477  0.0432  0.0022  601 ARG D CD  
12613 N NE  . ARG D 300 ? 0.3416 0.3017 0.2878 0.0558  0.0468  0.0033  601 ARG D NE  
12614 C CZ  . ARG D 300 ? 0.2986 0.2798 0.2610 0.0522  0.0471  0.0042  601 ARG D CZ  
12615 N NH1 . ARG D 300 ? 0.2668 0.2514 0.2357 0.0425  0.0442  0.0039  601 ARG D NH1 
12616 N NH2 . ARG D 300 ? 0.3153 0.3143 0.2863 0.0583  0.0503  0.0052  601 ARG D NH2 
12617 N N   . ASP D 301 ? 0.4177 0.3276 0.3276 0.0661  0.0380  0.0086  602 ASP D N   
12618 C CA  . ASP D 301 ? 0.4663 0.3740 0.3718 0.0762  0.0372  0.0111  602 ASP D CA  
12619 C C   . ASP D 301 ? 0.4333 0.3144 0.3153 0.0880  0.0389  0.0110  602 ASP D C   
12620 O O   . ASP D 301 ? 0.4282 0.3146 0.3096 0.1032  0.0406  0.0121  602 ASP D O   
12621 C CB  . ASP D 301 ? 0.4196 0.3230 0.3239 0.0675  0.0334  0.0129  602 ASP D CB  
12622 C CG  . ASP D 301 ? 0.4576 0.3877 0.3843 0.0589  0.0321  0.0130  602 ASP D CG  
12623 O OD1 . ASP D 301 ? 0.4071 0.3601 0.3498 0.0630  0.0334  0.0132  602 ASP D OD1 
12624 O OD2 . ASP D 301 ? 0.4399 0.3677 0.3672 0.0476  0.0300  0.0129  602 ASP D OD2 
12625 N N   . TYR D 302 ? 0.3747 0.2272 0.2364 0.0815  0.0383  0.0094  603 TYR D N   
12626 C CA  . TYR D 302 ? 0.4101 0.2305 0.2443 0.0917  0.0395  0.0091  603 TYR D CA  
12627 C C   . TYR D 302 ? 0.5127 0.3315 0.3424 0.1018  0.0441  0.0065  603 TYR D C   
12628 O O   . TYR D 302 ? 0.5016 0.3074 0.3169 0.1179  0.0465  0.0066  603 TYR D O   
12629 C CB  . TYR D 302 ? 0.5119 0.3005 0.3235 0.0787  0.0368  0.0084  603 TYR D CB  
12630 C CG  . TYR D 302 ? 0.5967 0.3759 0.4015 0.0741  0.0333  0.0115  603 TYR D CG  
12631 C CD1 . TYR D 302 ? 0.5630 0.3199 0.3512 0.0588  0.0307  0.0115  603 TYR D CD1 
12632 C CD2 . TYR D 302 ? 0.5907 0.3844 0.4052 0.0844  0.0325  0.0145  603 TYR D CD2 
12633 C CE1 . TYR D 302 ? 0.5645 0.3121 0.3449 0.0539  0.0281  0.0145  603 TYR D CE1 
12634 C CE2 . TYR D 302 ? 0.5879 0.3717 0.3944 0.0804  0.0294  0.0175  603 TYR D CE2 
12635 C CZ  . TYR D 302 ? 0.6370 0.3972 0.4261 0.0650  0.0275  0.0175  603 TYR D CZ  
12636 O OH  . TYR D 302 ? 0.6053 0.3552 0.3850 0.0599  0.0248  0.0206  603 TYR D OH  
12637 N N   . CYS D 303 ? 0.4836 0.3149 0.3240 0.0936  0.0455  0.0042  604 CYS D N   
12638 C CA  . CYS D 303 ? 0.5065 0.3293 0.3365 0.1012  0.0499  0.0014  604 CYS D CA  
12639 C C   . CYS D 303 ? 0.5244 0.3792 0.3756 0.1077  0.0542  0.0011  604 CYS D C   
12640 O O   . CYS D 303 ? 0.5101 0.3597 0.3523 0.1164  0.0588  -0.0010 604 CYS D O   
12641 C CB  . CYS D 303 ? 0.5103 0.3140 0.3273 0.0874  0.0485  -0.0013 604 CYS D CB  
12642 S SG  . CYS D 303 ? 0.5680 0.3304 0.3544 0.0795  0.0444  -0.0012 604 CYS D SG  
12643 N N   . ASP D 304 ? 0.4009 0.2874 0.2778 0.1033  0.0532  0.0030  605 ASP D N   
12644 C CA  . ASP D 304 ? 0.4143 0.3305 0.3088 0.1099  0.0575  0.0031  605 ASP D CA  
12645 C C   . ASP D 304 ? 0.5224 0.4388 0.4096 0.1294  0.0613  0.0034  605 ASP D C   
12646 O O   . ASP D 304 ? 0.5040 0.4096 0.3825 0.1380  0.0591  0.0051  605 ASP D O   
12647 C CB  . ASP D 304 ? 0.3540 0.3016 0.2741 0.1033  0.0554  0.0053  605 ASP D CB  
12648 C CG  . ASP D 304 ? 0.4494 0.4051 0.3803 0.0875  0.0539  0.0045  605 ASP D CG  
12649 O OD1 . ASP D 304 ? 0.4354 0.3735 0.3554 0.0808  0.0534  0.0025  605 ASP D OD1 
12650 O OD2 . ASP D 304 ? 0.4521 0.4314 0.4017 0.0821  0.0528  0.0058  605 ASP D OD2 
12651 N N   . ASN D 305 ? 0.4815 0.4098 0.3710 0.1370  0.0672  0.0018  606 ASN D N   
12652 C CA  . ASN D 305 ? 0.5105 0.4435 0.3947 0.1573  0.0717  0.0019  606 ASN D CA  
12653 C C   . ASN D 305 ? 0.4280 0.3923 0.3319 0.1646  0.0703  0.0051  606 ASN D C   
12654 O O   . ASN D 305 ? 0.4798 0.4432 0.3770 0.1822  0.0712  0.0061  606 ASN D O   
12655 C CB  . ASN D 305 ? 0.4421 0.3872 0.3276 0.1624  0.0790  -0.0005 606 ASN D CB  
12656 C CG  . ASN D 305 ? 0.6106 0.5219 0.4719 0.1590  0.0806  -0.0039 606 ASN D CG  
12657 O OD1 . ASN D 305 ? 0.7100 0.6248 0.5750 0.1472  0.0817  -0.0053 606 ASN D OD1 
12658 N ND2 . ASN D 305 ? 0.7040 0.5809 0.5386 0.1693  0.0805  -0.0053 606 ASN D ND2 
12659 N N   . SER D 306 ? 0.5208 0.5126 0.4478 0.1519  0.0680  0.0067  607 SER D N   
12660 C CA  . SER D 306 ? 0.5253 0.5475 0.4708 0.1565  0.0659  0.0097  607 SER D CA  
12661 C C   . SER D 306 ? 0.4880 0.4992 0.4321 0.1505  0.0589  0.0119  607 SER D C   
12662 O O   . SER D 306 ? 0.4579 0.4939 0.4184 0.1491  0.0560  0.0143  607 SER D O   
12663 C CB  . SER D 306 ? 0.5106 0.5694 0.4804 0.1460  0.0678  0.0101  607 SER D CB  
12664 O OG  . SER D 306 ? 0.5538 0.6046 0.5268 0.1273  0.0648  0.0095  607 SER D OG  
12665 N N   . ARG D 307 ? 0.4234 0.3989 0.3479 0.1455  0.0563  0.0111  608 ARG D N   
12666 C CA  . ARG D 307 ? 0.4305 0.3931 0.3502 0.1407  0.0504  0.0133  608 ARG D CA  
12667 C C   . ARG D 307 ? 0.4489 0.3779 0.3418 0.1536  0.0496  0.0138  608 ARG D C   
12668 O O   . ARG D 307 ? 0.4131 0.3441 0.3002 0.1720  0.0523  0.0142  608 ARG D O   
12669 C CB  . ARG D 307 ? 0.3601 0.3131 0.2813 0.1209  0.0475  0.0123  608 ARG D CB  
12670 C CG  . ARG D 307 ? 0.3353 0.3176 0.2800 0.1091  0.0480  0.0119  608 ARG D CG  
12671 C CD  . ARG D 307 ? 0.4001 0.4097 0.3632 0.1079  0.0452  0.0143  608 ARG D CD  
12672 N NE  . ARG D 307 ? 0.3147 0.3118 0.2718 0.1042  0.0402  0.0161  608 ARG D NE  
12673 C CZ  . ARG D 307 ? 0.4001 0.3877 0.3566 0.0903  0.0377  0.0154  608 ARG D CZ  
12674 N NH1 . ARG D 307 ? 0.3370 0.3259 0.2988 0.0796  0.0389  0.0132  608 ARG D NH1 
12675 N NH2 . ARG D 307 ? 0.3493 0.3266 0.2996 0.0874  0.0339  0.0171  608 ARG D NH2 
12676 N N   . TYR D 308 ? 0.4331 0.3308 0.3084 0.1445  0.0461  0.0140  609 TYR D N   
12677 C CA  . TYR D 308 ? 0.4616 0.3238 0.3083 0.1558  0.0450  0.0149  609 TYR D CA  
12678 C C   . TYR D 308 ? 0.5180 0.3544 0.3428 0.1642  0.0494  0.0118  609 TYR D C   
12679 O O   . TYR D 308 ? 0.5541 0.3644 0.3553 0.1794  0.0499  0.0122  609 TYR D O   
12680 C CB  . TYR D 308 ? 0.4295 0.2657 0.2621 0.1419  0.0403  0.0161  609 TYR D CB  
12681 C CG  . TYR D 308 ? 0.5501 0.4005 0.3927 0.1419  0.0360  0.0199  609 TYR D CG  
12682 C CD1 . TYR D 308 ? 0.4683 0.3490 0.3364 0.1294  0.0342  0.0204  609 TYR D CD1 
12683 C CD2 . TYR D 308 ? 0.5737 0.4053 0.3980 0.1551  0.0335  0.0230  609 TYR D CD2 
12684 C CE1 . TYR D 308 ? 0.4790 0.3716 0.3546 0.1290  0.0303  0.0236  609 TYR D CE1 
12685 C CE2 . TYR D 308 ? 0.5098 0.3541 0.3420 0.1550  0.0292  0.0266  609 TYR D CE2 
12686 C CZ  . TYR D 308 ? 0.4499 0.3252 0.3080 0.1415  0.0277  0.0267  609 TYR D CZ  
12687 O OH  . TYR D 308 ? 0.5111 0.3977 0.3752 0.1411  0.0235  0.0300  609 TYR D OH  
12688 N N   . ASN D 309 ? 0.5422 0.3836 0.3725 0.1552  0.0525  0.0086  610 ASN D N   
12689 C CA  . ASN D 309 ? 0.5024 0.3279 0.3164 0.1647  0.0576  0.0054  610 ASN D CA  
12690 C C   . ASN D 309 ? 0.4994 0.2757 0.2761 0.1692  0.0567  0.0043  610 ASN D C   
12691 O O   . ASN D 309 ? 0.6067 0.3661 0.3646 0.1874  0.0602  0.0032  610 ASN D O   
12692 C CB  . ASN D 309 ? 0.6005 0.4532 0.4262 0.1846  0.0625  0.0057  610 ASN D CB  
12693 C CG  . ASN D 309 ? 0.6275 0.4699 0.4396 0.1941  0.0691  0.0019  610 ASN D CG  
12694 O OD1 . ASN D 309 ? 0.5610 0.3886 0.3649 0.1822  0.0701  -0.0009 610 ASN D OD1 
12695 N ND2 . ASN D 309 ? 0.5938 0.4445 0.4031 0.2162  0.0734  0.0019  610 ASN D ND2 
12696 N N   . ILE D 310 ? 0.5390 0.2914 0.3034 0.1521  0.0522  0.0046  611 ILE D N   
12697 C CA  . ILE D 310 ? 0.6228 0.3269 0.3500 0.1541  0.0506  0.0042  611 ILE D CA  
12698 C C   . ILE D 310 ? 0.6457 0.3191 0.3486 0.1487  0.0527  0.0000  611 ILE D C   
12699 O O   . ILE D 310 ? 0.7389 0.3685 0.4077 0.1478  0.0513  -0.0006 611 ILE D O   
12700 C CB  . ILE D 310 ? 0.6905 0.3811 0.4122 0.1378  0.0448  0.0069  611 ILE D CB  
12701 C CG1 . ILE D 310 ? 0.6325 0.3275 0.3621 0.1138  0.0428  0.0050  611 ILE D CG1 
12702 C CG2 . ILE D 310 ? 0.6842 0.4051 0.4296 0.1413  0.0424  0.0108  611 ILE D CG2 
12703 C CD1 . ILE D 310 ? 0.5791 0.2599 0.3007 0.0968  0.0380  0.0071  611 ILE D CD1 
12704 N N   . LEU D 311 ? 0.6251 0.3179 0.3420 0.1445  0.0559  -0.0028 612 LEU D N   
12705 C CA  . LEU D 311 ? 0.6201 0.2848 0.3145 0.1362  0.0569  -0.0067 612 LEU D CA  
12706 C C   . LEU D 311 ? 0.6341 0.2575 0.2914 0.1524  0.0600  -0.0089 612 LEU D C   
12707 O O   . LEU D 311 ? 0.7398 0.3214 0.3651 0.1439  0.0577  -0.0106 612 LEU D O   
12708 C CB  . LEU D 311 ? 0.5718 0.2646 0.2862 0.1324  0.0602  -0.0090 612 LEU D CB  
12709 C CG  . LEU D 311 ? 0.5617 0.2825 0.3028 0.1127  0.0566  -0.0080 612 LEU D CG  
12710 C CD1 . LEU D 311 ? 0.5401 0.2866 0.2984 0.1125  0.0604  -0.0098 612 LEU D CD1 
12711 C CD2 . LEU D 311 ? 0.5279 0.2242 0.2530 0.0932  0.0513  -0.0090 612 LEU D CD2 
12712 N N   . GLU D 312 ? 0.6583 0.2928 0.3184 0.1756  0.0652  -0.0090 613 GLU D N   
12713 C CA  . GLU D 312 ? 0.7524 0.3586 0.3829 0.1888  0.0669  -0.0097 613 GLU D CA  
12714 C C   . GLU D 312 ? 0.8755 0.4437 0.4768 0.1857  0.0617  -0.0073 613 GLU D C   
12715 O O   . GLU D 312 ? 0.8911 0.4221 0.4600 0.1804  0.0606  -0.0087 613 GLU D O   
12716 C CB  . GLU D 312 ? 0.9990 0.6365 0.6453 0.2109  0.0711  -0.0081 613 GLU D CB  
12717 C CG  . GLU D 312 ? 1.1254 0.7937 0.7911 0.2145  0.0773  -0.0106 613 GLU D CG  
12718 C CD  . GLU D 312 ? 1.2666 0.9728 0.9528 0.2337  0.0809  -0.0085 613 GLU D CD  
12719 O OE1 . GLU D 312 ? 1.2928 1.0047 0.9751 0.2431  0.0857  -0.0100 613 GLU D OE1 
12720 O OE2 . GLU D 312 ? 1.3007 1.0312 1.0065 0.2387  0.0787  -0.0052 613 GLU D OE2 
12721 N N   . GLU D 313 ? 0.8316 0.4085 0.4430 0.1884  0.0585  -0.0035 614 GLU D N   
12722 C CA  . GLU D 313 ? 0.8807 0.4231 0.4641 0.1861  0.0538  -0.0009 614 GLU D CA  
12723 C C   . GLU D 313 ? 0.9277 0.4363 0.4895 0.1617  0.0501  -0.0023 614 GLU D C   
12724 O O   . GLU D 313 ? 0.9455 0.4165 0.4732 0.1571  0.0480  -0.0023 614 GLU D O   
12725 C CB  . GLU D 313 ? 0.9986 0.5604 0.5995 0.1925  0.0510  0.0035  614 GLU D CB  
12726 C CG  . GLU D 313 ? 1.2204 0.7518 0.8006 0.1801  0.0454  0.0062  614 GLU D CG  
12727 C CD  . GLU D 313 ? 1.4065 0.9484 0.9922 0.1932  0.0428  0.0108  614 GLU D CD  
12728 O OE1 . GLU D 313 ? 1.4850 0.9960 1.0414 0.1957  0.0401  0.0124  614 GLU D OE1 
12729 O OE2 . GLU D 313 ? 1.4626 1.0435 1.0807 0.2008  0.0432  0.0127  614 GLU D OE2 
12730 N N   . VAL D 314 ? 0.9425 0.4647 0.5231 0.1453  0.0494  -0.0037 615 VAL D N   
12731 C CA  . VAL D 314 ? 0.8600 0.3560 0.4233 0.1204  0.0455  -0.0051 615 VAL D CA  
12732 C C   . VAL D 314 ? 0.8074 0.2806 0.3468 0.1149  0.0467  -0.0090 615 VAL D C   
12733 O O   . VAL D 314 ? 0.8144 0.2541 0.3236 0.1016  0.0435  -0.0092 615 VAL D O   
12734 C CB  . VAL D 314 ? 0.7968 0.3339 0.3969 0.1013  0.0430  -0.0042 615 VAL D CB  
12735 C CG1 . VAL D 314 ? 0.7120 0.2321 0.2991 0.0750  0.0391  -0.0059 615 VAL D CG1 
12736 C CG2 . VAL D 314 ? 0.7221 0.2827 0.3434 0.1020  0.0405  0.0004  615 VAL D CG2 
12737 N N   . ALA D 315 ? 0.7822 0.2739 0.3341 0.1243  0.0513  -0.0119 616 ALA D N   
12738 C CA  . ALA D 315 ? 0.8023 0.2735 0.3322 0.1191  0.0524  -0.0154 616 ALA D CA  
12739 C C   . ALA D 315 ? 0.8463 0.2835 0.3408 0.1284  0.0525  -0.0142 616 ALA D C   
12740 O O   . ALA D 315 ? 0.9231 0.3287 0.3882 0.1162  0.0505  -0.0157 616 ALA D O   
12741 C CB  . ALA D 315 ? 0.7560 0.2551 0.3059 0.1295  0.0580  -0.0182 616 ALA D CB  
12742 N N   . LYS D 316 ? 0.9637 0.4073 0.4598 0.1499  0.0546  -0.0116 617 LYS D N   
12743 C CA  . LYS D 316 ? 1.0284 0.4384 0.4894 0.1602  0.0544  -0.0104 617 LYS D CA  
12744 C C   . LYS D 316 ? 1.0648 0.4372 0.4955 0.1415  0.0489  -0.0093 617 LYS D C   
12745 O O   . LYS D 316 ? 1.1168 0.4542 0.5134 0.1344  0.0480  -0.0106 617 LYS D O   
12746 C CB  . LYS D 316 ? 1.0944 0.5207 0.5649 0.1841  0.0560  -0.0073 617 LYS D CB  
12747 C CG  . LYS D 316 ? 1.2101 0.6679 0.7006 0.2054  0.0618  -0.0080 617 LYS D CG  
12748 C CD  . LYS D 316 ? 1.3469 0.8183 0.8426 0.2275  0.0622  -0.0047 617 LYS D CD  
12749 C CE  . LYS D 316 ? 1.4454 0.9406 0.9511 0.2493  0.0679  -0.0054 617 LYS D CE  
12750 N NZ  . LYS D 316 ? 1.3981 0.9427 0.9456 0.2502  0.0715  -0.0062 617 LYS D NZ  
12751 N N   . LYS D 317 ? 1.0054 0.3854 0.4481 0.1326  0.0453  -0.0069 618 LYS D N   
12752 C CA  . LYS D 317 ? 1.0275 0.3758 0.4437 0.1134  0.0404  -0.0057 618 LYS D CA  
12753 C C   . LYS D 317 ? 1.0528 0.3863 0.4564 0.0885  0.0381  -0.0084 618 LYS D C   
12754 O O   . LYS D 317 ? 1.0634 0.3634 0.4342 0.0743  0.0351  -0.0083 618 LYS D O   
12755 C CB  . LYS D 317 ? 1.0082 0.3733 0.4448 0.1066  0.0374  -0.0026 618 LYS D CB  
12756 C CG  . LYS D 317 ? 1.1402 0.5097 0.5784 0.1274  0.0376  0.0009  618 LYS D CG  
12757 C CD  . LYS D 317 ? 1.3160 0.6472 0.7177 0.1214  0.0340  0.0028  618 LYS D CD  
12758 C CE  . LYS D 317 ? 1.3960 0.7199 0.7854 0.1468  0.0348  0.0049  618 LYS D CE  
12759 N NZ  . LYS D 317 ? 1.3467 0.7064 0.7692 0.1603  0.0347  0.0081  618 LYS D NZ  
12760 N N   . MET D 318 ? 0.9062 0.2648 0.3347 0.0824  0.0395  -0.0110 619 MET D N   
12761 C CA  . MET D 318 ? 0.9848 0.3337 0.4036 0.0600  0.0371  -0.0138 619 MET D CA  
12762 C C   . MET D 318 ? 0.9641 0.2900 0.3564 0.0658  0.0393  -0.0161 619 MET D C   
12763 O O   . MET D 318 ? 0.9730 0.2877 0.3530 0.0475  0.0369  -0.0181 619 MET D O   
12764 C CB  . MET D 318 ? 0.8695 0.2537 0.3240 0.0516  0.0372  -0.0159 619 MET D CB  
12765 C CG  . MET D 318 ? 0.8584 0.2614 0.3355 0.0392  0.0340  -0.0137 619 MET D CG  
12766 S SD  . MET D 318 ? 0.8476 0.2921 0.3653 0.0315  0.0344  -0.0163 619 MET D SD  
12767 C CE  . MET D 318 ? 0.8772 0.3072 0.3767 0.0101  0.0312  -0.0206 619 MET D CE  
12768 N N   . ASN D 319 ? 1.0347 0.3550 0.4186 0.0905  0.0437  -0.0156 620 ASN D N   
12769 C CA  . ASN D 319 ? 1.1643 0.4624 0.5224 0.0985  0.0465  -0.0174 620 ASN D CA  
12770 C C   . ASN D 319 ? 1.0476 0.3631 0.4211 0.0923  0.0483  -0.0208 620 ASN D C   
12771 O O   . ASN D 319 ? 1.0372 0.3307 0.3875 0.0826  0.0475  -0.0227 620 ASN D O   
12772 C CB  . ASN D 319 ? 1.3338 0.5859 0.6470 0.0858  0.0431  -0.0168 620 ASN D CB  
12773 C CG  . ASN D 319 ? 1.4817 0.7123 0.7738 0.0968  0.0424  -0.0138 620 ASN D CG  
12774 O OD1 . ASN D 319 ? 1.5626 0.7958 0.8546 0.1218  0.0461  -0.0129 620 ASN D OD1 
12775 N ND2 . ASN D 319 ? 1.5221 0.7331 0.7969 0.0782  0.0375  -0.0123 620 ASN D ND2 
12776 N N   . LEU D 320 ? 0.9884 0.3436 0.4003 0.0977  0.0506  -0.0216 621 LEU D N   
12777 C CA  . LEU D 320 ? 0.9939 0.3685 0.4220 0.0939  0.0527  -0.0250 621 LEU D CA  
12778 C C   . LEU D 320 ? 1.0648 0.4436 0.4906 0.1158  0.0592  -0.0261 621 LEU D C   
12779 O O   . LEU D 320 ? 1.1208 0.5041 0.5480 0.1369  0.0627  -0.0241 621 LEU D O   
12780 C CB  . LEU D 320 ? 0.8597 0.2741 0.3277 0.0904  0.0528  -0.0256 621 LEU D CB  
12781 C CG  . LEU D 320 ? 0.8909 0.3051 0.3645 0.0699  0.0467  -0.0243 621 LEU D CG  
12782 C CD1 . LEU D 320 ? 0.8224 0.2747 0.3346 0.0697  0.0473  -0.0247 621 LEU D CD1 
12783 C CD2 . LEU D 320 ? 0.8545 0.2492 0.3087 0.0447  0.0414  -0.0262 621 LEU D CD2 
12784 N N   . ASP D 321 ? 1.0630 0.4415 0.4854 0.1103  0.0607  -0.0292 622 ASP D N   
12785 C CA  . ASP D 321 ? 1.1201 0.5074 0.5440 0.1285  0.0673  -0.0306 622 ASP D CA  
12786 C C   . ASP D 321 ? 1.0237 0.4574 0.4880 0.1407  0.0719  -0.0307 622 ASP D C   
12787 O O   . ASP D 321 ? 1.0165 0.4737 0.5024 0.1310  0.0719  -0.0327 622 ASP D O   
12788 C CB  . ASP D 321 ? 1.1808 0.5550 0.5900 0.1163  0.0669  -0.0339 622 ASP D CB  
12789 C CG  . ASP D 321 ? 1.3568 0.7391 0.7662 0.1335  0.0740  -0.0355 622 ASP D CG  
12790 O OD1 . ASP D 321 ? 1.3072 0.7010 0.7235 0.1553  0.0790  -0.0340 622 ASP D OD1 
12791 O OD2 . ASP D 321 ? 1.3900 0.7682 0.7926 0.1250  0.0744  -0.0383 622 ASP D OD2 
12792 N N   . MET D 322 ? 0.9702 0.4181 0.4441 0.1618  0.0757  -0.0283 623 MET D N   
12793 C CA  . MET D 322 ? 0.9411 0.4348 0.4533 0.1729  0.0797  -0.0277 623 MET D CA  
12794 C C   . MET D 322 ? 1.0015 0.5161 0.5224 0.1893  0.0871  -0.0289 623 MET D C   
12795 O O   . MET D 322 ? 1.0750 0.6287 0.6257 0.2007  0.0910  -0.0278 623 MET D O   
12796 C CB  . MET D 322 ? 0.9017 0.4054 0.4243 0.1839  0.0783  -0.0239 623 MET D CB  
12797 C CG  . MET D 322 ? 0.9859 0.4790 0.5084 0.1674  0.0718  -0.0225 623 MET D CG  
12798 S SD  . MET D 322 ? 1.0349 0.5274 0.5579 0.1802  0.0694  -0.0178 623 MET D SD  
12799 C CE  . MET D 322 ? 0.8592 0.4093 0.4285 0.1953  0.0738  -0.0164 623 MET D CE  
12800 N N   . ARG D 323 ? 0.9092 0.3996 0.4047 0.1898  0.0890  -0.0311 624 ARG D N   
12801 C CA  . ARG D 323 ? 1.0194 0.5280 0.5212 0.2048  0.0964  -0.0325 624 ARG D CA  
12802 C C   . ARG D 323 ? 0.9432 0.4875 0.4736 0.1978  0.0997  -0.0345 624 ARG D C   
12803 O O   . ARG D 323 ? 0.9363 0.5154 0.4888 0.2102  0.1059  -0.0343 624 ARG D O   
12804 C CB  . ARG D 323 ? 1.1133 0.5834 0.5782 0.2056  0.0973  -0.0344 624 ARG D CB  
12805 C CG  . ARG D 323 ? 1.2161 0.7013 0.6840 0.2188  0.1051  -0.0365 624 ARG D CG  
12806 C CD  . ARG D 323 ? 1.2495 0.6924 0.6774 0.2216  0.1059  -0.0382 624 ARG D CD  
12807 N NE  . ARG D 323 ? 1.4294 0.8658 0.8499 0.2090  0.1070  -0.0416 624 ARG D NE  
12808 C CZ  . ARG D 323 ? 1.5926 1.0469 1.0200 0.2174  0.1140  -0.0438 624 ARG D CZ  
12809 N NH1 . ARG D 323 ? 1.6861 1.1678 1.1293 0.2380  0.1206  -0.0431 624 ARG D NH1 
12810 N NH2 . ARG D 323 ? 1.5960 1.0418 1.0144 0.2048  0.1143  -0.0468 624 ARG D NH2 
12811 N N   . LYS D 324 ? 0.8814 0.4184 0.4109 0.1774  0.0956  -0.0363 625 LYS D N   
12812 C CA  . LYS D 324 ? 0.9522 0.5149 0.5003 0.1692  0.0983  -0.0385 625 LYS D CA  
12813 C C   . LYS D 324 ? 0.8725 0.4494 0.4396 0.1538  0.0936  -0.0382 625 LYS D C   
12814 O O   . LYS D 324 ? 0.9288 0.4841 0.4851 0.1424  0.0869  -0.0377 625 LYS D O   
12815 C CB  . LYS D 324 ? 0.9796 0.5169 0.5027 0.1595  0.0979  -0.0416 625 LYS D CB  
12816 C CG  . LYS D 324 ? 1.1927 0.7547 0.7280 0.1620  0.1043  -0.0435 625 LYS D CG  
12817 C CD  . LYS D 324 ? 1.2519 0.7958 0.7644 0.1732  0.1092  -0.0450 625 LYS D CD  
12818 C CE  . LYS D 324 ? 1.3363 0.9122 0.8656 0.1811  0.1175  -0.0462 625 LYS D CE  
12819 N NZ  . LYS D 324 ? 1.4377 0.9996 0.9472 0.1955  0.1231  -0.0476 625 LYS D NZ  
12820 N N   . THR D 325 ? 0.7586 0.3721 0.3533 0.1528  0.0973  -0.0384 626 THR D N   
12821 C CA  . THR D 325 ? 0.8061 0.4330 0.4176 0.1386  0.0932  -0.0384 626 THR D CA  
12822 C C   . THR D 325 ? 0.7498 0.3511 0.3424 0.1183  0.0864  -0.0408 626 THR D C   
12823 O O   . THR D 325 ? 0.7404 0.3450 0.3433 0.1031  0.0784  -0.0384 626 THR D O   
12824 C CB  . THR D 325 ? 0.7859 0.4572 0.4295 0.1389  0.0976  -0.0368 626 THR D CB  
12825 O OG1 . THR D 325 ? 0.8257 0.4947 0.4587 0.1368  0.1019  -0.0396 626 THR D OG1 
12826 C CG2 . THR D 325 ? 0.8379 0.5371 0.5000 0.1579  0.1045  -0.0349 626 THR D CG2 
12827 N N   . SER D 326 ? 0.7779 0.3623 0.3503 0.1152  0.0873  -0.0432 627 SER D N   
12828 C CA  . SER D 326 ? 0.7137 0.2796 0.2703 0.0954  0.0807  -0.0455 627 SER D CA  
12829 C C   . SER D 326 ? 0.8163 0.3491 0.3513 0.0837  0.0728  -0.0454 627 SER D C   
12830 O O   . SER D 326 ? 0.8352 0.3579 0.3613 0.0649  0.0658  -0.0470 627 SER D O   
12831 C CB  . SER D 326 ? 0.8178 0.3744 0.3581 0.0955  0.0835  -0.0475 627 SER D CB  
12832 O OG  . SER D 326 ? 0.9069 0.4376 0.4243 0.1055  0.0857  -0.0475 627 SER D OG  
12833 N N   . SER D 327 ? 0.7969 0.3139 0.3228 0.0933  0.0733  -0.0434 628 SER D N   
12834 C CA  . SER D 327 ? 0.8400 0.3295 0.3482 0.0799  0.0658  -0.0425 628 SER D CA  
12835 C C   . SER D 327 ? 0.8141 0.3200 0.3424 0.0680  0.0609  -0.0420 628 SER D C   
12836 O O   . SER D 327 ? 0.8086 0.2965 0.3251 0.0520  0.0541  -0.0415 628 SER D O   
12837 C CB  . SER D 327 ? 0.8324 0.3004 0.3243 0.0931  0.0674  -0.0398 628 SER D CB  
12838 O OG  . SER D 327 ? 0.7996 0.2913 0.3149 0.1074  0.0706  -0.0375 628 SER D OG  
12839 N N   . LEU D 328 ? 0.7502 0.2987 0.3155 0.0732  0.0632  -0.0393 629 LEU D N   
12840 C CA  . LEU D 328 ? 0.7565 0.3358 0.3537 0.0624  0.0577  -0.0349 629 LEU D CA  
12841 C C   . LEU D 328 ? 0.7321 0.2963 0.3231 0.0636  0.0555  -0.0328 629 LEU D C   
12842 O O   . LEU D 328 ? 0.6625 0.2334 0.2632 0.0485  0.0491  -0.0305 629 LEU D O   
12843 C CB  . LEU D 328 ? 0.7258 0.3131 0.3286 0.0402  0.0499  -0.0348 629 LEU D CB  
12844 C CG  . LEU D 328 ? 0.6682 0.2692 0.2757 0.0383  0.0512  -0.0363 629 LEU D CG  
12845 C CD1 . LEU D 328 ? 0.6035 0.2245 0.2272 0.0194  0.0430  -0.0347 629 LEU D CD1 
12846 C CD2 . LEU D 328 ? 0.6092 0.2399 0.2402 0.0539  0.0587  -0.0348 629 LEU D CD2 
12847 N N   . TRP D 329 ? 0.6821 0.2263 0.2563 0.0826  0.0609  -0.0336 630 TRP D N   
12848 C CA  . TRP D 329 ? 0.6948 0.2228 0.2610 0.0862  0.0590  -0.0313 630 TRP D CA  
12849 C C   . TRP D 329 ? 0.6842 0.2527 0.2886 0.0863  0.0575  -0.0265 630 TRP D C   
12850 O O   . TRP D 329 ? 0.6987 0.2614 0.3032 0.0784  0.0529  -0.0239 630 TRP D O   
12851 C CB  . TRP D 329 ? 0.7264 0.2351 0.2731 0.1075  0.0640  -0.0307 630 TRP D CB  
12852 C CG  . TRP D 329 ? 0.7372 0.2781 0.3066 0.1286  0.0712  -0.0300 630 TRP D CG  
12853 C CD1 . TRP D 329 ? 0.8180 0.3705 0.3897 0.1375  0.0768  -0.0318 630 TRP D CD1 
12854 C CD2 . TRP D 329 ? 0.7778 0.3452 0.3710 0.1424  0.0732  -0.0270 630 TRP D CD2 
12855 N NE1 . TRP D 329 ? 0.8384 0.4249 0.4347 0.1550  0.0824  -0.0301 630 TRP D NE1 
12856 C CE2 . TRP D 329 ? 0.7866 0.3833 0.3967 0.1583  0.0801  -0.0270 630 TRP D CE2 
12857 C CE3 . TRP D 329 ? 0.7213 0.2915 0.3232 0.1420  0.0698  -0.0239 630 TRP D CE3 
12858 C CZ2 . TRP D 329 ? 0.7317 0.3622 0.3677 0.1730  0.0830  -0.0242 630 TRP D CZ2 
12859 C CZ3 . TRP D 329 ? 0.6828 0.2844 0.3092 0.1578  0.0726  -0.0211 630 TRP D CZ3 
12860 C CH2 . TRP D 329 ? 0.7376 0.3699 0.3813 0.1728  0.0790  -0.0212 630 TRP D CH2 
12861 N N   . LYS D 330 ? 0.6236 0.2321 0.2593 0.0938  0.0611  -0.0253 631 LYS D N   
12862 C CA  . LYS D 330 ? 0.5779 0.2237 0.2486 0.0917  0.0592  -0.0211 631 LYS D CA  
12863 C C   . LYS D 330 ? 0.6582 0.3147 0.3414 0.0694  0.0521  -0.0198 631 LYS D C   
12864 O O   . LYS D 330 ? 0.5970 0.2611 0.2910 0.0632  0.0484  -0.0169 631 LYS D O   
12865 C CB  . LYS D 330 ? 0.5842 0.2687 0.2830 0.1019  0.0644  -0.0203 631 LYS D CB  
12866 C CG  . LYS D 330 ? 0.6859 0.3717 0.3807 0.1250  0.0714  -0.0206 631 LYS D CG  
12867 C CD  . LYS D 330 ? 0.6293 0.3603 0.3574 0.1315  0.0755  -0.0187 631 LYS D CD  
12868 C CE  . LYS D 330 ? 0.6822 0.4206 0.4091 0.1546  0.0824  -0.0188 631 LYS D CE  
12869 N NZ  . LYS D 330 ? 0.7078 0.4924 0.4673 0.1584  0.0862  -0.0168 631 LYS D NZ  
12870 N N   . ASP D 331 ? 0.5867 0.2443 0.2680 0.0578  0.0502  -0.0219 632 ASP D N   
12871 C CA  . ASP D 331 ? 0.5774 0.2477 0.2708 0.0379  0.0434  -0.0209 632 ASP D CA  
12872 C C   . ASP D 331 ? 0.6074 0.2506 0.2801 0.0255  0.0384  -0.0208 632 ASP D C   
12873 O O   . ASP D 331 ? 0.6389 0.2973 0.3263 0.0130  0.0338  -0.0186 632 ASP D O   
12874 C CB  . ASP D 331 ? 0.5704 0.2432 0.2608 0.0295  0.0419  -0.0233 632 ASP D CB  
12875 C CG  . ASP D 331 ? 0.5822 0.2720 0.2833 0.0421  0.0481  -0.0238 632 ASP D CG  
12876 O OD1 . ASP D 331 ? 0.6727 0.3449 0.3558 0.0555  0.0540  -0.0260 632 ASP D OD1 
12877 O OD2 . ASP D 331 ? 0.5784 0.2988 0.3049 0.0387  0.0473  -0.0221 632 ASP D OD2 
12878 N N   . GLN D 332 ? 0.6332 0.2353 0.2700 0.0280  0.0394  -0.0233 633 GLN D N   
12879 C CA  . GLN D 332 ? 0.6757 0.2480 0.2885 0.0145  0.0348  -0.0232 633 GLN D CA  
12880 C C   . GLN D 332 ? 0.6856 0.2603 0.3054 0.0193  0.0348  -0.0196 633 GLN D C   
12881 O O   . GLN D 332 ? 0.6190 0.1977 0.2432 0.0040  0.0303  -0.0176 633 GLN D O   
12882 C CB  . GLN D 332 ? 0.7062 0.2292 0.2751 0.0175  0.0363  -0.0268 633 GLN D CB  
12883 C CG  . GLN D 332 ? 0.8843 0.3960 0.4377 0.0056  0.0340  -0.0306 633 GLN D CG  
12884 C CD  . GLN D 332 ? 0.9916 0.4498 0.4978 0.0003  0.0330  -0.0338 633 GLN D CD  
12885 O OE1 . GLN D 332 ? 1.1907 0.6335 0.6818 -0.0205 0.0270  -0.0340 633 GLN D OE1 
12886 N NE2 . GLN D 332 ? 0.9515 0.3901 0.4393 0.0187  0.0385  -0.0343 633 GLN D NE2 
12887 N N   . ALA D 333 ? 0.7050 0.2770 0.3246 0.0405  0.0400  -0.0187 634 ALA D N   
12888 C CA  . ALA D 333 ? 0.6972 0.2728 0.3237 0.0464  0.0396  -0.0150 634 ALA D CA  
12889 C C   . ALA D 333 ? 0.6389 0.2583 0.3039 0.0382  0.0372  -0.0120 634 ALA D C   
12890 O O   . ALA D 333 ? 0.6007 0.2215 0.2690 0.0297  0.0340  -0.0093 634 ALA D O   
12891 C CB  . ALA D 333 ? 0.7016 0.2744 0.3255 0.0722  0.0453  -0.0145 634 ALA D CB  
12892 N N   . LEU D 334 ? 0.6298 0.2831 0.3218 0.0399  0.0387  -0.0125 635 LEU D N   
12893 C CA  . LEU D 334 ? 0.6198 0.3125 0.3465 0.0338  0.0367  -0.0100 635 LEU D CA  
12894 C C   . LEU D 334 ? 0.6609 0.3551 0.3888 0.0130  0.0311  -0.0094 635 LEU D C   
12895 O O   . LEU D 334 ? 0.5313 0.2422 0.2751 0.0086  0.0293  -0.0068 635 LEU D O   
12896 C CB  . LEU D 334 ? 0.5631 0.2848 0.3120 0.0367  0.0388  -0.0110 635 LEU D CB  
12897 C CG  . LEU D 334 ? 0.5440 0.3038 0.3265 0.0314  0.0370  -0.0088 635 LEU D CG  
12898 C CD1 . LEU D 334 ? 0.5972 0.3718 0.3944 0.0418  0.0388  -0.0059 635 LEU D CD1 
12899 C CD2 . LEU D 334 ? 0.5125 0.2936 0.3105 0.0327  0.0387  -0.0098 635 LEU D CD2 
12900 N N   . VAL D 335 ? 0.6167 0.2947 0.3277 -0.0002 0.0282  -0.0119 636 VAL D N   
12901 C CA  . VAL D 335 ? 0.6428 0.3270 0.3566 -0.0205 0.0228  -0.0113 636 VAL D CA  
12902 C C   . VAL D 335 ? 0.6515 0.3139 0.3482 -0.0263 0.0216  -0.0093 636 VAL D C   
12903 O O   . VAL D 335 ? 0.6325 0.3128 0.3438 -0.0360 0.0194  -0.0071 636 VAL D O   
12904 C CB  . VAL D 335 ? 0.6431 0.3156 0.3413 -0.0339 0.0194  -0.0143 636 VAL D CB  
12905 C CG1 . VAL D 335 ? 0.6291 0.3086 0.3285 -0.0553 0.0139  -0.0136 636 VAL D CG1 
12906 C CG2 . VAL D 335 ? 0.5667 0.2642 0.2840 -0.0295 0.0199  -0.0156 636 VAL D CG2 
12907 N N   . GLU D 336 ? 0.5945 0.2169 0.2587 -0.0197 0.0233  -0.0101 637 GLU D N   
12908 C CA  . GLU D 336 ? 0.6608 0.2564 0.3035 -0.0253 0.0221  -0.0079 637 GLU D CA  
12909 C C   . GLU D 336 ? 0.6675 0.2833 0.3307 -0.0162 0.0233  -0.0042 637 GLU D C   
12910 O O   . GLU D 336 ? 0.6956 0.3118 0.3583 -0.0275 0.0211  -0.0017 637 GLU D O   
12911 C CB  . GLU D 336 ? 0.7424 0.2886 0.3445 -0.0164 0.0239  -0.0095 637 GLU D CB  
12912 C CG  . GLU D 336 ? 0.8087 0.3305 0.3860 -0.0271 0.0224  -0.0136 637 GLU D CG  
12913 C CD  . GLU D 336 ? 0.9322 0.4452 0.4966 -0.0547 0.0169  -0.0138 637 GLU D CD  
12914 O OE1 . GLU D 336 ? 0.8535 0.3749 0.4243 -0.0664 0.0147  -0.0108 637 GLU D OE1 
12915 O OE2 . GLU D 336 ? 1.0253 0.5234 0.5723 -0.0655 0.0147  -0.0171 637 GLU D OE2 
12916 N N   . ILE D 337 ? 0.6437 0.2785 0.3256 0.0031  0.0269  -0.0036 638 ILE D N   
12917 C CA  . ILE D 337 ? 0.6124 0.2695 0.3153 0.0111  0.0275  -0.0002 638 ILE D CA  
12918 C C   . ILE D 337 ? 0.6208 0.3124 0.3515 -0.0034 0.0250  0.0009  638 ILE D C   
12919 O O   . ILE D 337 ? 0.6130 0.3098 0.3481 -0.0083 0.0238  0.0036  638 ILE D O   
12920 C CB  . ILE D 337 ? 0.5796 0.2553 0.2991 0.0324  0.0315  -0.0001 638 ILE D CB  
12921 C CG1 . ILE D 337 ? 0.6294 0.2713 0.3205 0.0497  0.0343  -0.0006 638 ILE D CG1 
12922 C CG2 . ILE D 337 ? 0.5324 0.2393 0.2792 0.0375  0.0314  0.0031  638 ILE D CG2 
12923 C CD1 . ILE D 337 ? 0.6668 0.3228 0.3680 0.0678  0.0389  -0.0021 638 ILE D CD1 
12924 N N   . ASN D 338 ? 0.5685 0.2827 0.3164 -0.0102 0.0242  -0.0012 639 ASN D N   
12925 C CA  . ASN D 338 ? 0.5310 0.2789 0.3056 -0.0210 0.0221  -0.0004 639 ASN D CA  
12926 C C   . ASN D 338 ? 0.5861 0.3269 0.3503 -0.0410 0.0187  -0.0001 639 ASN D C   
12927 O O   . ASN D 338 ? 0.5598 0.3228 0.3408 -0.0484 0.0177  0.0014  639 ASN D O   
12928 C CB  . ASN D 338 ? 0.4397 0.2130 0.2348 -0.0202 0.0221  -0.0024 639 ASN D CB  
12929 C CG  . ASN D 338 ? 0.4646 0.2566 0.2785 -0.0040 0.0254  -0.0017 639 ASN D CG  
12930 O OD1 . ASN D 338 ? 0.4780 0.2964 0.3151 -0.0029 0.0255  -0.0003 639 ASN D OD1 
12931 N ND2 . ASN D 338 ? 0.4627 0.2400 0.2650 0.0086  0.0286  -0.0027 639 ASN D ND2 
12932 N N   . ILE D 339 ? 0.5360 0.2465 0.2719 -0.0503 0.0171  -0.0017 640 ILE D N   
12933 C CA  . ILE D 339 ? 0.5767 0.2760 0.2978 -0.0703 0.0142  -0.0010 640 ILE D CA  
12934 C C   . ILE D 339 ? 0.6652 0.3514 0.3772 -0.0688 0.0153  0.0023  640 ILE D C   
12935 O O   . ILE D 339 ? 0.5382 0.2384 0.2578 -0.0815 0.0142  0.0040  640 ILE D O   
12936 C CB  . ILE D 339 ? 0.5518 0.2152 0.2393 -0.0804 0.0123  -0.0034 640 ILE D CB  
12937 C CG1 . ILE D 339 ? 0.5563 0.2368 0.2536 -0.0866 0.0099  -0.0064 640 ILE D CG1 
12938 C CG2 . ILE D 339 ? 0.6085 0.2524 0.2739 -0.1008 0.0098  -0.0021 640 ILE D CG2 
12939 C CD1 . ILE D 339 ? 0.6238 0.2689 0.2871 -0.0969 0.0077  -0.0091 640 ILE D CD1 
12940 N N   . ALA D 340 ? 0.5926 0.2529 0.2882 -0.0523 0.0176  0.0034  641 ALA D N   
12941 C CA  . ALA D 340 ? 0.6018 0.2460 0.2852 -0.0490 0.0181  0.0069  641 ALA D CA  
12942 C C   . ALA D 340 ? 0.6320 0.3135 0.3470 -0.0462 0.0187  0.0092  641 ALA D C   
12943 O O   . ALA D 340 ? 0.5822 0.2644 0.2948 -0.0563 0.0179  0.0116  641 ALA D O   
12944 C CB  . ALA D 340 ? 0.5957 0.2092 0.2581 -0.0283 0.0202  0.0074  641 ALA D CB  
12945 N N   . VAL D 341 ? 0.5579 0.2697 0.3012 -0.0332 0.0202  0.0083  642 VAL D N   
12946 C CA  . VAL D 341 ? 0.5230 0.2678 0.2942 -0.0303 0.0207  0.0101  642 VAL D CA  
12947 C C   . VAL D 341 ? 0.5583 0.3237 0.3414 -0.0489 0.0192  0.0100  642 VAL D C   
12948 O O   . VAL D 341 ? 0.4901 0.2616 0.2759 -0.0540 0.0192  0.0123  642 VAL D O   
12949 C CB  . VAL D 341 ? 0.4935 0.2662 0.2910 -0.0166 0.0223  0.0088  642 VAL D CB  
12950 C CG1 . VAL D 341 ? 0.4422 0.2492 0.2679 -0.0176 0.0224  0.0098  642 VAL D CG1 
12951 C CG2 . VAL D 341 ? 0.4932 0.2518 0.2820 0.0027  0.0243  0.0096  642 VAL D CG2 
12952 N N   . LEU D 342 ? 0.5294 0.3062 0.3189 -0.0590 0.0179  0.0074  643 LEU D N   
12953 C CA  . LEU D 342 ? 0.5623 0.3631 0.3650 -0.0755 0.0165  0.0070  643 LEU D CA  
12954 C C   . LEU D 342 ? 0.6433 0.4244 0.4236 -0.0918 0.0157  0.0087  643 LEU D C   
12955 O O   . LEU D 342 ? 0.5571 0.3553 0.3466 -0.1004 0.0162  0.0102  643 LEU D O   
12956 C CB  . LEU D 342 ? 0.5274 0.3417 0.3378 -0.0823 0.0144  0.0040  643 LEU D CB  
12957 C CG  . LEU D 342 ? 0.4963 0.3359 0.3318 -0.0696 0.0150  0.0026  643 LEU D CG  
12958 C CD1 . LEU D 342 ? 0.4220 0.2648 0.2567 -0.0751 0.0125  -0.0001 643 LEU D CD1 
12959 C CD2 . LEU D 342 ? 0.3865 0.2607 0.2498 -0.0681 0.0158  0.0032  643 LEU D CD2 
12960 N N   . TYR D 343 ? 0.6006 0.3446 0.3496 -0.0970 0.0147  0.0085  644 TYR D N   
12961 C CA  . TYR D 343 ? 0.6152 0.3357 0.3386 -0.1141 0.0138  0.0103  644 TYR D CA  
12962 C C   . TYR D 343 ? 0.6118 0.3249 0.3305 -0.1093 0.0156  0.0140  644 TYR D C   
12963 O O   . TYR D 343 ? 0.6103 0.3265 0.3245 -0.1244 0.0157  0.0159  644 TYR D O   
12964 C CB  . TYR D 343 ? 0.5587 0.2340 0.2453 -0.1173 0.0126  0.0094  644 TYR D CB  
12965 C CG  . TYR D 343 ? 0.6072 0.2479 0.2602 -0.1326 0.0120  0.0118  644 TYR D CG  
12966 C CD1 . TYR D 343 ? 0.6731 0.3192 0.3198 -0.1582 0.0102  0.0115  644 TYR D CD1 
12967 C CD2 . TYR D 343 ? 0.6619 0.2644 0.2883 -0.1218 0.0129  0.0145  644 TYR D CD2 
12968 C CE1 . TYR D 343 ? 0.7039 0.3167 0.3176 -0.1743 0.0098  0.0138  644 TYR D CE1 
12969 C CE2 . TYR D 343 ? 0.7715 0.3378 0.3634 -0.1362 0.0122  0.0169  644 TYR D CE2 
12970 C CZ  . TYR D 343 ? 0.7774 0.3483 0.3626 -0.1633 0.0109  0.0166  644 TYR D CZ  
12971 O OH  . TYR D 343 ? 0.8124 0.3516 0.3644 -0.1774 0.0100  0.0185  644 TYR D OH  
12972 N N   . SER D 344 ? 0.6166 0.3221 0.3368 -0.0884 0.0168  0.0152  645 SER D N   
12973 C CA  . SER D 344 ? 0.6148 0.3097 0.3271 -0.0824 0.0176  0.0190  645 SER D CA  
12974 C C   . SER D 344 ? 0.6364 0.3698 0.3773 -0.0855 0.0187  0.0199  645 SER D C   
12975 O O   . SER D 344 ? 0.5830 0.3130 0.3160 -0.0949 0.0191  0.0225  645 SER D O   
12976 C CB  . SER D 344 ? 0.5917 0.2719 0.2992 -0.0585 0.0181  0.0199  645 SER D CB  
12977 O OG  . SER D 344 ? 0.6345 0.2727 0.3092 -0.0550 0.0176  0.0194  645 SER D OG  
12978 N N   . PHE D 345 ? 0.5212 0.2899 0.2939 -0.0776 0.0193  0.0176  646 PHE D N   
12979 C CA  . PHE D 345 ? 0.4528 0.2569 0.2516 -0.0798 0.0204  0.0178  646 PHE D CA  
12980 C C   . PHE D 345 ? 0.4918 0.3085 0.2912 -0.1007 0.0207  0.0174  646 PHE D C   
12981 O O   . PHE D 345 ? 0.4760 0.3020 0.2777 -0.1071 0.0221  0.0192  646 PHE D O   
12982 C CB  . PHE D 345 ? 0.4493 0.2842 0.2778 -0.0691 0.0208  0.0151  646 PHE D CB  
12983 C CG  . PHE D 345 ? 0.4596 0.2977 0.2969 -0.0508 0.0214  0.0161  646 PHE D CG  
12984 C CD1 . PHE D 345 ? 0.4704 0.2847 0.2929 -0.0380 0.0211  0.0170  646 PHE D CD1 
12985 C CD2 . PHE D 345 ? 0.3796 0.2454 0.2397 -0.0463 0.0223  0.0161  646 PHE D CD2 
12986 C CE1 . PHE D 345 ? 0.3982 0.2203 0.2308 -0.0215 0.0215  0.0180  646 PHE D CE1 
12987 C CE2 . PHE D 345 ? 0.4013 0.2723 0.2699 -0.0313 0.0224  0.0170  646 PHE D CE2 
12988 C CZ  . PHE D 345 ? 0.3638 0.2149 0.2197 -0.0192 0.0219  0.0181  646 PHE D CZ  
12989 N N   . GLN D 346 ? 0.5060 0.3237 0.3026 -0.1119 0.0194  0.0152  647 GLN D N   
12990 C CA  . GLN D 346 ? 0.5520 0.3869 0.3513 -0.1324 0.0195  0.0147  647 GLN D CA  
12991 C C   . GLN D 346 ? 0.5906 0.3986 0.3613 -0.1472 0.0200  0.0177  647 GLN D C   
12992 O O   . GLN D 346 ? 0.5809 0.4066 0.3563 -0.1609 0.0217  0.0186  647 GLN D O   
12993 C CB  . GLN D 346 ? 0.5384 0.3791 0.3389 -0.1412 0.0170  0.0118  647 GLN D CB  
12994 C CG  . GLN D 346 ? 0.5702 0.4417 0.3999 -0.1293 0.0164  0.0090  647 GLN D CG  
12995 C CD  . GLN D 346 ? 0.5919 0.4628 0.4182 -0.1358 0.0133  0.0065  647 GLN D CD  
12996 O OE1 . GLN D 346 ? 0.6604 0.5026 0.4606 -0.1462 0.0116  0.0066  647 GLN D OE1 
12997 N NE2 . GLN D 346 ? 0.6216 0.5223 0.4723 -0.1298 0.0122  0.0043  647 GLN D NE2 
12998 N N   . SER D 347 ? 0.5954 0.3597 0.3349 -0.1446 0.0189  0.0193  648 SER D N   
12999 C CA  . SER D 347 ? 0.6144 0.3471 0.3221 -0.1585 0.0191  0.0226  648 SER D CA  
13000 C C   . SER D 347 ? 0.6309 0.3689 0.3421 -0.1535 0.0212  0.0258  648 SER D C   
13001 O O   . SER D 347 ? 0.6527 0.3837 0.3492 -0.1695 0.0225  0.0283  648 SER D O   
13002 C CB  . SER D 347 ? 0.6537 0.3350 0.3252 -0.1531 0.0174  0.0235  648 SER D CB  
13003 O OG  . SER D 347 ? 0.6924 0.3652 0.3552 -0.1621 0.0154  0.0204  648 SER D OG  
13004 N N   . ASP D 348 ? 0.5955 0.3467 0.3256 -0.1328 0.0217  0.0258  649 ASP D N   
13005 C CA  . ASP D 348 ? 0.5524 0.3113 0.2878 -0.1268 0.0231  0.0286  649 ASP D CA  
13006 C C   . ASP D 348 ? 0.5763 0.3808 0.3435 -0.1309 0.0255  0.0268  649 ASP D C   
13007 O O   . ASP D 348 ? 0.5966 0.4116 0.3715 -0.1251 0.0268  0.0284  649 ASP D O   
13008 C CB  . ASP D 348 ? 0.6220 0.3713 0.3595 -0.1030 0.0219  0.0297  649 ASP D CB  
13009 C CG  . ASP D 348 ? 0.6814 0.3835 0.3831 -0.0972 0.0201  0.0327  649 ASP D CG  
13010 O OD1 . ASP D 348 ? 0.6954 0.3694 0.3693 -0.1128 0.0198  0.0337  649 ASP D OD1 
13011 O OD2 . ASP D 348 ? 0.7067 0.3997 0.4070 -0.0775 0.0190  0.0341  649 ASP D OD2 
13012 N N   . LYS D 349 ? 0.4991 0.3304 0.2838 -0.1402 0.0259  0.0235  650 LYS D N   
13013 C CA  . LYS D 349 ? 0.5265 0.4010 0.3405 -0.1426 0.0283  0.0215  650 LYS D CA  
13014 C C   . LYS D 349 ? 0.4511 0.3416 0.2865 -0.1227 0.0286  0.0206  650 LYS D C   
13015 O O   . LYS D 349 ? 0.4528 0.3619 0.2997 -0.1211 0.0309  0.0209  650 LYS D O   
13016 C CB  . LYS D 349 ? 0.5832 0.4639 0.3898 -0.1585 0.0313  0.0235  650 LYS D CB  
13017 C CG  . LYS D 349 ? 0.7672 0.6366 0.5537 -0.1817 0.0313  0.0243  650 LYS D CG  
13018 C CD  . LYS D 349 ? 0.9090 0.7894 0.6906 -0.1976 0.0352  0.0263  650 LYS D CD  
13019 C CE  . LYS D 349 ? 1.0451 0.9272 0.8142 -0.2233 0.0357  0.0264  650 LYS D CE  
13020 N NZ  . LYS D 349 ? 1.0822 0.9394 0.8358 -0.2270 0.0315  0.0255  650 LYS D NZ  
13021 N N   . VAL D 350 ? 0.4203 0.3025 0.2593 -0.1082 0.0265  0.0196  651 VAL D N   
13022 C CA  . VAL D 350 ? 0.3968 0.2955 0.2565 -0.0911 0.0266  0.0186  651 VAL D CA  
13023 C C   . VAL D 350 ? 0.4938 0.4156 0.3749 -0.0877 0.0261  0.0149  651 VAL D C   
13024 O O   . VAL D 350 ? 0.4351 0.3465 0.3102 -0.0890 0.0244  0.0138  651 VAL D O   
13025 C CB  . VAL D 350 ? 0.3933 0.2671 0.2409 -0.0762 0.0249  0.0207  651 VAL D CB  
13026 C CG1 . VAL D 350 ? 0.3549 0.2489 0.2247 -0.0610 0.0248  0.0195  651 VAL D CG1 
13027 C CG2 . VAL D 350 ? 0.4406 0.2911 0.2655 -0.0787 0.0248  0.0248  651 VAL D CG2 
13028 N N   . THR D 351 ? 0.3900 0.3411 0.2940 -0.0835 0.0275  0.0130  652 THR D N   
13029 C CA  . THR D 351 ? 0.3620 0.3346 0.2850 -0.0801 0.0268  0.0098  652 THR D CA  
13030 C C   . THR D 351 ? 0.4044 0.3640 0.3263 -0.0691 0.0248  0.0094  652 THR D C   
13031 O O   . THR D 351 ? 0.3672 0.3168 0.2872 -0.0579 0.0248  0.0106  652 THR D O   
13032 C CB  . THR D 351 ? 0.3560 0.3553 0.2998 -0.0738 0.0286  0.0080  652 THR D CB  
13033 O OG1 . THR D 351 ? 0.3757 0.3863 0.3190 -0.0833 0.0312  0.0085  652 THR D OG1 
13034 C CG2 . THR D 351 ? 0.2912 0.3116 0.2525 -0.0707 0.0277  0.0050  652 THR D CG2 
13035 N N   . ILE D 352 ? 0.3911 0.3518 0.3133 -0.0730 0.0232  0.0077  653 ILE D N   
13036 C CA  . ILE D 352 ? 0.3581 0.3103 0.2807 -0.0633 0.0218  0.0067  653 ILE D CA  
13037 C C   . ILE D 352 ? 0.3285 0.2957 0.2596 -0.0687 0.0201  0.0044  653 ILE D C   
13038 O O   . ILE D 352 ? 0.3466 0.3239 0.2774 -0.0812 0.0195  0.0039  653 ILE D O   
13039 C CB  . ILE D 352 ? 0.3109 0.2297 0.2096 -0.0621 0.0212  0.0083  653 ILE D CB  
13040 C CG1 . ILE D 352 ? 0.3607 0.2724 0.2609 -0.0488 0.0210  0.0075  653 ILE D CG1 
13041 C CG2 . ILE D 352 ? 0.3479 0.2534 0.2297 -0.0768 0.0197  0.0080  653 ILE D CG2 
13042 C CD1 . ILE D 352 ? 0.3999 0.2811 0.2785 -0.0423 0.0212  0.0093  653 ILE D CD1 
13043 N N   . VAL D 353 ? 0.3259 0.2961 0.2647 -0.0597 0.0192  0.0030  654 VAL D N   
13044 C CA  . VAL D 353 ? 0.3733 0.3565 0.3189 -0.0634 0.0168  0.0011  654 VAL D CA  
13045 C C   . VAL D 353 ? 0.3877 0.3518 0.3224 -0.0590 0.0156  0.0006  654 VAL D C   
13046 O O   . VAL D 353 ? 0.4541 0.4071 0.3868 -0.0481 0.0171  0.0011  654 VAL D O   
13047 C CB  . VAL D 353 ? 0.3294 0.3396 0.2968 -0.0566 0.0170  -0.0003 654 VAL D CB  
13048 C CG1 . VAL D 353 ? 0.2673 0.2736 0.2404 -0.0432 0.0182  -0.0002 654 VAL D CG1 
13049 C CG2 . VAL D 353 ? 0.4260 0.4518 0.4000 -0.0606 0.0139  -0.0020 654 VAL D CG2 
13050 N N   . ASP D 354 ? 0.3778 0.3378 0.3039 -0.0681 0.0129  -0.0005 655 ASP D N   
13051 C CA  . ASP D 354 ? 0.3908 0.3333 0.3059 -0.0640 0.0118  -0.0013 655 ASP D CA  
13052 C C   . ASP D 354 ? 0.4270 0.3866 0.3579 -0.0557 0.0108  -0.0025 655 ASP D C   
13053 O O   . ASP D 354 ? 0.3479 0.3319 0.2959 -0.0552 0.0100  -0.0029 655 ASP D O   
13054 C CB  . ASP D 354 ? 0.4185 0.3471 0.3155 -0.0774 0.0088  -0.0022 655 ASP D CB  
13055 C CG  . ASP D 354 ? 0.5167 0.4712 0.4250 -0.0878 0.0052  -0.0034 655 ASP D CG  
13056 O OD1 . ASP D 354 ? 0.6859 0.6471 0.5914 -0.1014 0.0044  -0.0030 655 ASP D OD1 
13057 O OD2 . ASP D 354 ? 0.5390 0.5080 0.4586 -0.0825 0.0032  -0.0045 655 ASP D OD2 
13058 N N   . HIS D 355 ? 0.3970 0.3421 0.3204 -0.0485 0.0113  -0.0030 656 HIS D N   
13059 C CA  . HIS D 355 ? 0.3846 0.3417 0.3197 -0.0405 0.0108  -0.0036 656 HIS D CA  
13060 C C   . HIS D 355 ? 0.4059 0.3776 0.3458 -0.0468 0.0064  -0.0048 656 HIS D C   
13061 O O   . HIS D 355 ? 0.3852 0.3723 0.3379 -0.0408 0.0054  -0.0049 656 HIS D O   
13062 C CB  . HIS D 355 ? 0.4019 0.3402 0.3262 -0.0325 0.0129  -0.0039 656 HIS D CB  
13063 C CG  . HIS D 355 ? 0.3987 0.3136 0.3009 -0.0381 0.0119  -0.0048 656 HIS D CG  
13064 N ND1 . HIS D 355 ? 0.4147 0.3094 0.3007 -0.0418 0.0130  -0.0044 656 HIS D ND1 
13065 C CD2 . HIS D 355 ? 0.3783 0.2841 0.2696 -0.0407 0.0098  -0.0063 656 HIS D CD2 
13066 C CE1 . HIS D 355 ? 0.4794 0.3524 0.3447 -0.0465 0.0117  -0.0058 656 HIS D CE1 
13067 N NE2 . HIS D 355 ? 0.4497 0.3298 0.3182 -0.0463 0.0098  -0.0071 656 HIS D NE2 
13068 N N   . HIS D 356 ? 0.3019 0.2692 0.2309 -0.0589 0.0034  -0.0055 657 HIS D N   
13069 C CA  . HIS D 356 ? 0.3022 0.2885 0.2376 -0.0654 -0.0015 -0.0064 657 HIS D CA  
13070 C C   . HIS D 356 ? 0.3455 0.3618 0.3011 -0.0654 -0.0019 -0.0061 657 HIS D C   
13071 O O   . HIS D 356 ? 0.3664 0.4017 0.3351 -0.0595 -0.0042 -0.0064 657 HIS D O   
13072 C CB  . HIS D 356 ? 0.3381 0.3136 0.2565 -0.0803 -0.0047 -0.0072 657 HIS D CB  
13073 C CG  . HIS D 356 ? 0.4578 0.4017 0.3539 -0.0795 -0.0041 -0.0080 657 HIS D CG  
13074 N ND1 . HIS D 356 ? 0.4146 0.3537 0.3072 -0.0737 -0.0056 -0.0089 657 HIS D ND1 
13075 C CD2 . HIS D 356 ? 0.4647 0.3790 0.3396 -0.0824 -0.0017 -0.0080 657 HIS D CD2 
13076 C CE1 . HIS D 356 ? 0.4917 0.4009 0.3624 -0.0733 -0.0038 -0.0097 657 HIS D CE1 
13077 N NE2 . HIS D 356 ? 0.4579 0.3512 0.3174 -0.0780 -0.0016 -0.0093 657 HIS D NE2 
13078 N N   . SER D 357 ? 0.3348 0.3545 0.2917 -0.0712 0.0003  -0.0055 658 SER D N   
13079 C CA  . SER D 357 ? 0.3346 0.3826 0.3094 -0.0708 0.0008  -0.0055 658 SER D CA  
13080 C C   . SER D 357 ? 0.2744 0.3287 0.2623 -0.0561 0.0034  -0.0053 658 SER D C   
13081 O O   . SER D 357 ? 0.2842 0.3606 0.2865 -0.0508 0.0023  -0.0060 658 SER D O   
13082 C CB  . SER D 357 ? 0.3640 0.4108 0.3343 -0.0811 0.0034  -0.0047 658 SER D CB  
13083 O OG  . SER D 357 ? 0.5365 0.6095 0.5234 -0.0793 0.0050  -0.0049 658 SER D OG  
13084 N N   . ALA D 358 ? 0.2552 0.2901 0.2374 -0.0492 0.0066  -0.0046 659 ALA D N   
13085 C CA  . ALA D 358 ? 0.2543 0.2936 0.2468 -0.0374 0.0090  -0.0044 659 ALA D CA  
13086 C C   . ALA D 358 ? 0.3422 0.3872 0.3399 -0.0300 0.0066  -0.0050 659 ALA D C   
13087 O O   . ALA D 358 ? 0.2626 0.3213 0.2713 -0.0233 0.0065  -0.0054 659 ALA D O   
13088 C CB  . ALA D 358 ? 0.2599 0.2791 0.2447 -0.0326 0.0123  -0.0033 659 ALA D CB  
13089 N N   . THR D 359 ? 0.2974 0.3299 0.2853 -0.0308 0.0046  -0.0050 660 THR D N   
13090 C CA  . THR D 359 ? 0.2592 0.2945 0.2495 -0.0241 0.0023  -0.0051 660 THR D CA  
13091 C C   . THR D 359 ? 0.2638 0.3210 0.2628 -0.0252 -0.0022 -0.0057 660 THR D C   
13092 O O   . THR D 359 ? 0.2788 0.3445 0.2848 -0.0167 -0.0035 -0.0057 660 THR D O   
13093 C CB  . THR D 359 ? 0.2402 0.2567 0.2165 -0.0250 0.0016  -0.0050 660 THR D CB  
13094 O OG1 . THR D 359 ? 0.3143 0.3255 0.2803 -0.0355 -0.0007 -0.0057 660 THR D OG1 
13095 C CG2 . THR D 359 ? 0.2577 0.2572 0.2283 -0.0201 0.0065  -0.0044 660 THR D CG2 
13096 N N   . GLU D 360 ? 0.2191 0.2861 0.2172 -0.0356 -0.0047 -0.0062 661 GLU D N   
13097 C CA  . GLU D 360 ? 0.2627 0.3564 0.2717 -0.0363 -0.0089 -0.0068 661 GLU D CA  
13098 C C   . GLU D 360 ? 0.3503 0.4616 0.3737 -0.0281 -0.0065 -0.0072 661 GLU D C   
13099 O O   . GLU D 360 ? 0.3228 0.4477 0.3541 -0.0189 -0.0089 -0.0074 661 GLU D O   
13100 C CB  . GLU D 360 ? 0.3500 0.4540 0.3563 -0.0511 -0.0114 -0.0073 661 GLU D CB  
13101 C CG  . GLU D 360 ? 0.4087 0.5461 0.4286 -0.0521 -0.0155 -0.0078 661 GLU D CG  
13102 C CD  . GLU D 360 ? 0.6981 0.8493 0.7162 -0.0690 -0.0177 -0.0082 661 GLU D CD  
13103 O OE1 . GLU D 360 ? 0.7595 0.8936 0.7663 -0.0798 -0.0148 -0.0080 661 GLU D OE1 
13104 O OE2 . GLU D 360 ? 0.8442 1.0236 0.8716 -0.0718 -0.0224 -0.0086 661 GLU D OE2 
13105 N N   . SER D 361 ? 0.2904 0.3997 0.3155 -0.0307 -0.0019 -0.0072 662 SER D N   
13106 C CA  A SER D 361 ? 0.3240 0.4473 0.3604 -0.0232 0.0009  -0.0079 662 SER D CA  
13107 C CA  B SER D 361 ? 0.3265 0.4499 0.3630 -0.0232 0.0009  -0.0079 662 SER D CA  
13108 C C   . SER D 361 ? 0.2908 0.4049 0.3279 -0.0099 0.0014  -0.0078 662 SER D C   
13109 O O   . SER D 361 ? 0.2810 0.4081 0.3259 -0.0011 0.0012  -0.0087 662 SER D O   
13110 C CB  A SER D 361 ? 0.3296 0.4474 0.3645 -0.0284 0.0057  -0.0077 662 SER D CB  
13111 C CB  B SER D 361 ? 0.3298 0.4480 0.3649 -0.0285 0.0057  -0.0077 662 SER D CB  
13112 O OG  A SER D 361 ? 0.3329 0.4589 0.3657 -0.0416 0.0054  -0.0075 662 SER D OG  
13113 O OG  B SER D 361 ? 0.2878 0.3828 0.3156 -0.0247 0.0085  -0.0068 662 SER D OG  
13114 N N   . PHE D 362 ? 0.3234 0.4148 0.3512 -0.0084 0.0022  -0.0069 663 PHE D N   
13115 C CA  . PHE D 362 ? 0.3309 0.4126 0.3577 0.0019  0.0030  -0.0066 663 PHE D CA  
13116 C C   . PHE D 362 ? 0.3674 0.4547 0.3945 0.0088  -0.0014 -0.0065 663 PHE D C   
13117 O O   . PHE D 362 ? 0.3203 0.4071 0.3487 0.0184  -0.0014 -0.0068 663 PHE D O   
13118 C CB  . PHE D 362 ? 0.2212 0.2808 0.2388 0.0012  0.0055  -0.0055 663 PHE D CB  
13119 C CG  . PHE D 362 ? 0.2840 0.3341 0.2997 0.0092  0.0066  -0.0051 663 PHE D CG  
13120 C CD1 . PHE D 362 ? 0.2884 0.3388 0.3078 0.0127  0.0095  -0.0056 663 PHE D CD1 
13121 C CD2 . PHE D 362 ? 0.2993 0.3398 0.3080 0.0123  0.0046  -0.0042 663 PHE D CD2 
13122 C CE1 . PHE D 362 ? 0.3462 0.3863 0.3617 0.0183  0.0103  -0.0053 663 PHE D CE1 
13123 C CE2 . PHE D 362 ? 0.3666 0.3969 0.3715 0.0181  0.0057  -0.0036 663 PHE D CE2 
13124 C CZ  . PHE D 362 ? 0.3793 0.4089 0.3873 0.0206  0.0085  -0.0042 663 PHE D CZ  
13125 N N   . ILE D 363 ? 0.2878 0.3784 0.3115 0.0042  -0.0057 -0.0062 664 ILE D N   
13126 C CA  . ILE D 363 ? 0.2890 0.3877 0.3132 0.0109  -0.0109 -0.0058 664 ILE D CA  
13127 C C   . ILE D 363 ? 0.2965 0.4194 0.3326 0.0177  -0.0121 -0.0069 664 ILE D C   
13128 O O   . ILE D 363 ? 0.2663 0.3906 0.3027 0.0294  -0.0141 -0.0068 664 ILE D O   
13129 C CB  . ILE D 363 ? 0.3021 0.4036 0.3211 0.0029  -0.0157 -0.0055 664 ILE D CB  
13130 C CG1 . ILE D 363 ? 0.2752 0.3510 0.2803 -0.0010 -0.0142 -0.0047 664 ILE D CG1 
13131 C CG2 . ILE D 363 ? 0.2404 0.3547 0.2612 0.0101  -0.0220 -0.0050 664 ILE D CG2 
13132 C CD1 . ILE D 363 ? 0.3425 0.4021 0.3411 0.0082  -0.0134 -0.0035 664 ILE D CD1 
13133 N N   . LYS D 364 ? 0.2781 0.4199 0.3229 0.0107  -0.0108 -0.0080 665 LYS D N   
13134 C CA  . LYS D 364 ? 0.3337 0.5012 0.3907 0.0173  -0.0107 -0.0093 665 LYS D CA  
13135 C C   . LYS D 364 ? 0.2943 0.4520 0.3511 0.0282  -0.0065 -0.0101 665 LYS D C   
13136 O O   . LYS D 364 ? 0.2157 0.3824 0.2759 0.0407  -0.0076 -0.0109 665 LYS D O   
13137 C CB  . LYS D 364 ? 0.2890 0.4763 0.3536 0.0053  -0.0088 -0.0101 665 LYS D CB  
13138 C CG  . LYS D 364 ? 0.5198 0.7388 0.5982 0.0109  -0.0081 -0.0117 665 LYS D CG  
13139 C CD  . LYS D 364 ? 0.7111 0.9491 0.7949 0.0211  -0.0141 -0.0116 665 LYS D CD  
13140 C CE  . LYS D 364 ? 0.7932 1.0627 0.8906 0.0312  -0.0129 -0.0134 665 LYS D CE  
13141 N NZ  . LYS D 364 ? 0.9078 1.1945 1.0094 0.0441  -0.0192 -0.0130 665 LYS D NZ  
13142 N N   . HIS D 365 ? 0.2345 0.3726 0.2858 0.0241  -0.0019 -0.0099 666 HIS D N   
13143 C CA  . HIS D 365 ? 0.2381 0.3647 0.2871 0.0324  0.0017  -0.0107 666 HIS D CA  
13144 C C   . HIS D 365 ? 0.3367 0.4483 0.3776 0.0432  -0.0008 -0.0101 666 HIS D C   
13145 O O   . HIS D 365 ? 0.2781 0.3895 0.3182 0.0541  -0.0003 -0.0112 666 HIS D O   
13146 C CB  . HIS D 365 ? 0.2387 0.3478 0.2828 0.0253  0.0060  -0.0102 666 HIS D CB  
13147 C CG  . HIS D 365 ? 0.2471 0.3436 0.2875 0.0318  0.0091  -0.0110 666 HIS D CG  
13148 N ND1 . HIS D 365 ? 0.2177 0.3243 0.2624 0.0377  0.0113  -0.0131 666 HIS D ND1 
13149 C CD2 . HIS D 365 ? 0.2346 0.3098 0.2665 0.0328  0.0104  -0.0102 666 HIS D CD2 
13150 C CE1 . HIS D 365 ? 0.2998 0.3893 0.3374 0.0417  0.0135  -0.0136 666 HIS D CE1 
13151 N NE2 . HIS D 365 ? 0.2704 0.3418 0.3008 0.0381  0.0129  -0.0118 666 HIS D NE2 
13152 N N   . MET D 366 ? 0.3170 0.4145 0.3499 0.0403  -0.0034 -0.0082 667 MET D N   
13153 C CA  . MET D 366 ? 0.2774 0.3592 0.3004 0.0493  -0.0060 -0.0071 667 MET D CA  
13154 C C   . MET D 366 ? 0.2233 0.3202 0.2496 0.0610  -0.0103 -0.0076 667 MET D C   
13155 O O   . MET D 366 ? 0.2708 0.3576 0.2907 0.0723  -0.0105 -0.0079 667 MET D O   
13156 C CB  . MET D 366 ? 0.3307 0.3991 0.3450 0.0437  -0.0082 -0.0051 667 MET D CB  
13157 C CG  . MET D 366 ? 0.3497 0.3965 0.3562 0.0384  -0.0039 -0.0042 667 MET D CG  
13158 S SD  . MET D 366 ? 0.4683 0.4992 0.4628 0.0345  -0.0060 -0.0021 667 MET D SD  
13159 C CE  . MET D 366 ? 0.4521 0.4703 0.4355 0.0453  -0.0094 -0.0007 667 MET D CE  
13160 N N   . GLU D 367 ? 0.2305 0.3515 0.2657 0.0587  -0.0142 -0.0077 668 GLU D N   
13161 C CA  A GLU D 367 ? 0.3155 0.4564 0.3559 0.0707  -0.0187 -0.0081 668 GLU D CA  
13162 C CA  B GLU D 367 ? 0.3160 0.4560 0.3559 0.0710  -0.0187 -0.0080 668 GLU D CA  
13163 C C   . GLU D 367 ? 0.2953 0.4438 0.3405 0.0813  -0.0151 -0.0103 668 GLU D C   
13164 O O   . GLU D 367 ? 0.3388 0.4834 0.3788 0.0964  -0.0170 -0.0105 668 GLU D O   
13165 C CB  A GLU D 367 ? 0.3415 0.5126 0.3934 0.0633  -0.0226 -0.0082 668 GLU D CB  
13166 C CB  B GLU D 367 ? 0.3435 0.5141 0.3947 0.0650  -0.0232 -0.0080 668 GLU D CB  
13167 C CG  A GLU D 367 ? 0.3704 0.5715 0.4319 0.0750  -0.0272 -0.0087 668 GLU D CG  
13168 C CG  B GLU D 367 ? 0.4079 0.5757 0.4575 0.0483  -0.0237 -0.0073 668 GLU D CG  
13169 C CD  A GLU D 367 ? 0.4509 0.6875 0.5267 0.0644  -0.0294 -0.0093 668 GLU D CD  
13170 C CD  B GLU D 367 ? 0.4094 0.5685 0.4497 0.0469  -0.0297 -0.0054 668 GLU D CD  
13171 O OE1 A GLU D 367 ? 0.4539 0.6868 0.5282 0.0478  -0.0290 -0.0089 668 GLU D OE1 
13172 O OE1 B GLU D 367 ? 0.4291 0.5607 0.4564 0.0499  -0.0293 -0.0040 668 GLU D OE1 
13173 O OE2 A GLU D 367 ? 0.4759 0.7443 0.5636 0.0727  -0.0315 -0.0103 668 GLU D OE2 
13174 O OE2 B GLU D 367 ? 0.3904 0.5708 0.4359 0.0417  -0.0349 -0.0052 668 GLU D OE2 
13175 N N   . ASN D 368 ? 0.2847 0.4428 0.3380 0.0738  -0.0099 -0.0120 669 ASN D N   
13176 C CA  . ASN D 368 ? 0.2675 0.4334 0.3247 0.0829  -0.0058 -0.0145 669 ASN D CA  
13177 C C   . ASN D 368 ? 0.2908 0.4260 0.3334 0.0922  -0.0040 -0.0148 669 ASN D C   
13178 O O   . ASN D 368 ? 0.3079 0.4427 0.3469 0.1069  -0.0039 -0.0163 669 ASN D O   
13179 C CB  . ASN D 368 ? 0.3020 0.4771 0.3667 0.0714  -0.0002 -0.0158 669 ASN D CB  
13180 C CG  . ASN D 368 ? 0.3464 0.5519 0.4240 0.0612  -0.0013 -0.0158 669 ASN D CG  
13181 O OD1 . ASN D 368 ? 0.3372 0.5665 0.4222 0.0654  -0.0056 -0.0157 669 ASN D OD1 
13182 N ND2 . ASN D 368 ? 0.3416 0.5464 0.4208 0.0471  0.0024  -0.0157 669 ASN D ND2 
13183 N N   . GLU D 369 ? 0.2391 0.3481 0.2720 0.0836  -0.0024 -0.0134 670 GLU D N   
13184 C CA  . GLU D 369 ? 0.2387 0.3185 0.2570 0.0889  -0.0003 -0.0137 670 GLU D CA  
13185 C C   . GLU D 369 ? 0.2866 0.3516 0.2923 0.1012  -0.0048 -0.0124 670 GLU D C   
13186 O O   . GLU D 369 ? 0.3994 0.4492 0.3943 0.1123  -0.0040 -0.0137 670 GLU D O   
13187 C CB  . GLU D 369 ? 0.2283 0.2887 0.2411 0.0759  0.0022  -0.0123 670 GLU D CB  
13188 C CG  . GLU D 369 ? 0.3099 0.3798 0.3314 0.0661  0.0067  -0.0135 670 GLU D CG  
13189 C CD  . GLU D 369 ? 0.3573 0.4220 0.3757 0.0708  0.0107  -0.0160 670 GLU D CD  
13190 O OE1 . GLU D 369 ? 0.2971 0.3434 0.3078 0.0658  0.0131  -0.0159 670 GLU D OE1 
13191 O OE2 . GLU D 369 ? 0.3038 0.3839 0.3271 0.0793  0.0113  -0.0182 670 GLU D OE2 
13192 N N   . TYR D 370 ? 0.3174 0.3848 0.3225 0.0999  -0.0098 -0.0100 671 TYR D N   
13193 C CA  . TYR D 370 ? 0.2734 0.3262 0.2651 0.1123  -0.0146 -0.0084 671 TYR D CA  
13194 C C   . TYR D 370 ? 0.3362 0.4069 0.3322 0.1294  -0.0169 -0.0101 671 TYR D C   
13195 O O   . TYR D 370 ? 0.3829 0.4350 0.3644 0.1435  -0.0184 -0.0101 671 TYR D O   
13196 C CB  . TYR D 370 ? 0.2733 0.3264 0.2629 0.1072  -0.0197 -0.0055 671 TYR D CB  
13197 C CG  . TYR D 370 ? 0.3666 0.3914 0.3433 0.0970  -0.0176 -0.0035 671 TYR D CG  
13198 C CD1 . TYR D 370 ? 0.2769 0.3032 0.2599 0.0823  -0.0136 -0.0036 671 TYR D CD1 
13199 C CD2 . TYR D 370 ? 0.4146 0.4110 0.3718 0.1024  -0.0195 -0.0014 671 TYR D CD2 
13200 C CE1 . TYR D 370 ? 0.3035 0.3075 0.2759 0.0738  -0.0113 -0.0019 671 TYR D CE1 
13201 C CE2 . TYR D 370 ? 0.4080 0.3815 0.3540 0.0921  -0.0170 0.0004  671 TYR D CE2 
13202 C CZ  . TYR D 370 ? 0.4119 0.3911 0.3666 0.0783  -0.0127 0.0000  671 TYR D CZ  
13203 O OH  . TYR D 370 ? 0.4978 0.4578 0.4425 0.0692  -0.0099 0.0017  671 TYR D OH  
13204 N N   . ARG D 371 ? 0.3368 0.4434 0.3518 0.1285  -0.0169 -0.0116 672 ARG D N   
13205 C CA  . ARG D 371 ? 0.4038 0.5332 0.4252 0.1454  -0.0187 -0.0133 672 ARG D CA  
13206 C C   . ARG D 371 ? 0.4218 0.5389 0.4363 0.1554  -0.0133 -0.0164 672 ARG D C   
13207 O O   . ARG D 371 ? 0.3804 0.4893 0.3848 0.1738  -0.0149 -0.0171 672 ARG D O   
13208 C CB  . ARG D 371 ? 0.3958 0.5692 0.4397 0.1396  -0.0192 -0.0143 672 ARG D CB  
13209 C CG  . ARG D 371 ? 0.6077 0.8116 0.6609 0.1573  -0.0213 -0.0159 672 ARG D CG  
13210 C CD  . ARG D 371 ? 0.8168 1.0660 0.8927 0.1489  -0.0200 -0.0173 672 ARG D CD  
13211 N NE  . ARG D 371 ? 0.9643 1.2207 1.0461 0.1288  -0.0225 -0.0153 672 ARG D NE  
13212 C CZ  . ARG D 371 ? 0.9669 1.2284 1.0554 0.1107  -0.0180 -0.0159 672 ARG D CZ  
13213 N NH1 . ARG D 371 ? 0.8561 1.1189 0.9478 0.1094  -0.0109 -0.0182 672 ARG D NH1 
13214 N NH2 . ARG D 371 ? 0.9394 1.2033 1.0298 0.0941  -0.0208 -0.0141 672 ARG D NH2 
13215 N N   . CYS D 372 ? 0.3419 0.4560 0.3598 0.1443  -0.0070 -0.0182 673 CYS D N   
13216 C CA  . CYS D 372 ? 0.3847 0.4892 0.3958 0.1538  -0.0020 -0.0215 673 CYS D CA  
13217 C C   . CYS D 372 ? 0.4238 0.4846 0.4125 0.1527  -0.0003 -0.0213 673 CYS D C   
13218 O O   . CYS D 372 ? 0.5501 0.5939 0.5252 0.1654  0.0014  -0.0236 673 CYS D O   
13219 C CB  . CYS D 372 ? 0.4096 0.5364 0.4353 0.1442  0.0039  -0.0240 673 CYS D CB  
13220 S SG  . CYS D 372 ? 0.6279 0.7380 0.6527 0.1216  0.0073  -0.0227 673 CYS D SG  
13221 N N   . ARG D 373 ? 0.3390 0.3811 0.3224 0.1380  -0.0008 -0.0188 674 ARG D N   
13222 C CA  . ARG D 373 ? 0.4046 0.4097 0.3688 0.1333  0.0014  -0.0186 674 ARG D CA  
13223 C C   . ARG D 373 ? 0.4685 0.4458 0.4151 0.1346  -0.0027 -0.0154 674 ARG D C   
13224 O O   . ARG D 373 ? 0.4533 0.3983 0.3809 0.1320  -0.0013 -0.0151 674 ARG D O   
13225 C CB  . ARG D 373 ? 0.4520 0.4580 0.4233 0.1147  0.0053  -0.0183 674 ARG D CB  
13226 C CG  . ARG D 373 ? 0.4224 0.4030 0.3802 0.1096  0.0092  -0.0198 674 ARG D CG  
13227 C CD  . ARG D 373 ? 0.3667 0.3513 0.3329 0.0921  0.0117  -0.0187 674 ARG D CD  
13228 N NE  . ARG D 373 ? 0.4098 0.3726 0.3636 0.0863  0.0147  -0.0199 674 ARG D NE  
13229 C CZ  . ARG D 373 ? 0.4640 0.4238 0.4199 0.0724  0.0164  -0.0187 674 ARG D CZ  
13230 N NH1 . ARG D 373 ? 0.3576 0.3322 0.3263 0.0640  0.0159  -0.0164 674 ARG D NH1 
13231 N NH2 . ARG D 373 ? 0.5116 0.4535 0.4560 0.0671  0.0184  -0.0199 674 ARG D NH2 
13232 N N   . GLY D 374 ? 0.4589 0.4475 0.4101 0.1372  -0.0077 -0.0128 675 GLY D N   
13233 C CA  . GLY D 374 ? 0.4064 0.3688 0.3401 0.1375  -0.0115 -0.0095 675 GLY D CA  
13234 C C   . GLY D 374 ? 0.3955 0.3473 0.3279 0.1196  -0.0100 -0.0071 675 GLY D C   
13235 O O   . GLY D 374 ? 0.4283 0.3544 0.3434 0.1176  -0.0116 -0.0045 675 GLY D O   
13236 N N   . GLY D 375 ? 0.3297 0.2998 0.2784 0.1069  -0.0066 -0.0079 676 GLY D N   
13237 C CA  . GLY D 375 ? 0.3031 0.2660 0.2514 0.0920  -0.0051 -0.0058 676 GLY D CA  
13238 C C   . GLY D 375 ? 0.4261 0.4055 0.3898 0.0807  -0.0008 -0.0072 676 GLY D C   
13239 O O   . GLY D 375 ? 0.4104 0.4028 0.3828 0.0828  0.0015  -0.0098 676 GLY D O   
13240 N N   . CYS D 376 ? 0.4045 0.3822 0.3701 0.0693  0.0002  -0.0054 677 CYS D N   
13241 C CA  . CYS D 376 ? 0.3871 0.3764 0.3644 0.0587  0.0040  -0.0062 677 CYS D CA  
13242 C C   . CYS D 376 ? 0.4283 0.4044 0.3994 0.0491  0.0058  -0.0040 677 CYS D C   
13243 O O   . CYS D 376 ? 0.3629 0.3398 0.3332 0.0465  0.0041  -0.0023 677 CYS D O   
13244 C CB  . CYS D 376 ? 0.3289 0.3434 0.3211 0.0568  0.0027  -0.0067 677 CYS D CB  
13245 S SG  . CYS D 376 ? 0.3337 0.3576 0.3362 0.0447  0.0069  -0.0071 677 CYS D SG  
13246 N N   . PRO D 377 ? 0.3221 0.2861 0.2878 0.0438  0.0092  -0.0041 678 PRO D N   
13247 C CA  . PRO D 377 ? 0.3100 0.2664 0.2720 0.0345  0.0116  -0.0022 678 PRO D CA  
13248 C C   . PRO D 377 ? 0.3497 0.3221 0.3240 0.0291  0.0129  -0.0020 678 PRO D C   
13249 O O   . PRO D 377 ? 0.2606 0.2459 0.2452 0.0280  0.0140  -0.0034 678 PRO D O   
13250 C CB  . PRO D 377 ? 0.3847 0.3318 0.3418 0.0296  0.0146  -0.0029 678 PRO D CB  
13251 C CG  . PRO D 377 ? 0.3920 0.3490 0.3566 0.0342  0.0148  -0.0056 678 PRO D CG  
13252 C CD  . PRO D 377 ? 0.3829 0.3440 0.3476 0.0450  0.0113  -0.0063 678 PRO D CD  
13253 N N   . ALA D 378 ? 0.3377 0.3073 0.3089 0.0261  0.0128  -0.0002 679 ALA D N   
13254 C CA  . ALA D 378 ? 0.3053 0.2860 0.2846 0.0220  0.0138  -0.0002 679 ALA D CA  
13255 C C   . ALA D 378 ? 0.3146 0.2881 0.2879 0.0173  0.0164  0.0015  679 ALA D C   
13256 O O   . ALA D 378 ? 0.3308 0.2934 0.2938 0.0179  0.0155  0.0029  679 ALA D O   
13257 C CB  . ALA D 378 ? 0.2647 0.2551 0.2480 0.0250  0.0100  -0.0008 679 ALA D CB  
13258 N N   . ASP D 379 ? 0.2727 0.2523 0.2518 0.0133  0.0196  0.0014  680 ASP D N   
13259 C CA  . ASP D 379 ? 0.2928 0.2694 0.2681 0.0098  0.0232  0.0027  680 ASP D CA  
13260 C C   . ASP D 379 ? 0.2851 0.2635 0.2599 0.0103  0.0228  0.0025  680 ASP D C   
13261 O O   . ASP D 379 ? 0.2649 0.2495 0.2452 0.0098  0.0239  0.0018  680 ASP D O   
13262 C CB  . ASP D 379 ? 0.3327 0.3160 0.3141 0.0066  0.0267  0.0028  680 ASP D CB  
13263 C CG  . ASP D 379 ? 0.3664 0.3510 0.3458 0.0039  0.0309  0.0040  680 ASP D CG  
13264 O OD1 . ASP D 379 ? 0.3289 0.3195 0.3118 0.0006  0.0335  0.0046  680 ASP D OD1 
13265 O OD2 . ASP D 379 ? 0.3635 0.3446 0.3378 0.0051  0.0316  0.0044  680 ASP D OD2 
13266 N N   . TRP D 380 ? 0.2979 0.2688 0.2639 0.0110  0.0211  0.0031  681 TRP D N   
13267 C CA  . TRP D 380 ? 0.2858 0.2559 0.2483 0.0108  0.0201  0.0025  681 TRP D CA  
13268 C C   . TRP D 380 ? 0.2449 0.2162 0.2082 0.0097  0.0246  0.0022  681 TRP D C   
13269 O O   . TRP D 380 ? 0.2540 0.2259 0.2175 0.0094  0.0239  0.0012  681 TRP D O   
13270 C CB  . TRP D 380 ? 0.2831 0.2434 0.2338 0.0112  0.0184  0.0035  681 TRP D CB  
13271 C CG  . TRP D 380 ? 0.2910 0.2491 0.2359 0.0106  0.0155  0.0028  681 TRP D CG  
13272 C CD1 . TRP D 380 ? 0.3818 0.3424 0.3256 0.0115  0.0095  0.0024  681 TRP D CD1 
13273 C CD2 . TRP D 380 ? 0.2902 0.2429 0.2282 0.0090  0.0184  0.0021  681 TRP D CD2 
13274 N NE1 . TRP D 380 ? 0.3173 0.2740 0.2535 0.0089  0.0080  0.0016  681 TRP D NE1 
13275 C CE2 . TRP D 380 ? 0.3526 0.3025 0.2841 0.0076  0.0136  0.0012  681 TRP D CE2 
13276 C CE3 . TRP D 380 ? 0.3257 0.2762 0.2618 0.0090  0.0245  0.0020  681 TRP D CE3 
13277 C CZ2 . TRP D 380 ? 0.3786 0.3201 0.2996 0.0056  0.0149  0.0001  681 TRP D CZ2 
13278 C CZ3 . TRP D 380 ? 0.3605 0.3033 0.2869 0.0090  0.0261  0.0008  681 TRP D CZ3 
13279 C CH2 . TRP D 380 ? 0.3172 0.2539 0.2352 0.0069  0.0213  -0.0002 681 TRP D CH2 
13280 N N   . VAL D 381 ? 0.2481 0.2197 0.2109 0.0090  0.0292  0.0032  682 VAL D N   
13281 C CA  . VAL D 381 ? 0.2919 0.2666 0.2556 0.0101  0.0338  0.0030  682 VAL D CA  
13282 C C   . VAL D 381 ? 0.3516 0.3324 0.3232 0.0114  0.0333  0.0023  682 VAL D C   
13283 O O   . VAL D 381 ? 0.2941 0.2729 0.2629 0.0137  0.0352  0.0017  682 VAL D O   
13284 C CB  . VAL D 381 ? 0.2306 0.2103 0.1956 0.0085  0.0385  0.0044  682 VAL D CB  
13285 C CG1 . VAL D 381 ? 0.2621 0.2496 0.2304 0.0113  0.0432  0.0043  682 VAL D CG1 
13286 C CG2 . VAL D 381 ? 0.2374 0.2084 0.1912 0.0065  0.0395  0.0053  682 VAL D CG2 
13287 N N   . TRP D 382 ? 0.2374 0.2241 0.2169 0.0102  0.0311  0.0022  683 TRP D N   
13288 C CA  . TRP D 382 ? 0.2710 0.2630 0.2568 0.0108  0.0307  0.0017  683 TRP D CA  
13289 C C   . TRP D 382 ? 0.2417 0.2319 0.2269 0.0095  0.0269  0.0007  683 TRP D C   
13290 O O   . TRP D 382 ? 0.2694 0.2592 0.2545 0.0092  0.0269  0.0004  683 TRP D O   
13291 C CB  . TRP D 382 ? 0.2911 0.2911 0.2850 0.0096  0.0309  0.0021  683 TRP D CB  
13292 C CG  . TRP D 382 ? 0.2868 0.2934 0.2837 0.0099  0.0345  0.0032  683 TRP D CG  
13293 C CD1 . TRP D 382 ? 0.3006 0.3086 0.2951 0.0091  0.0376  0.0041  683 TRP D CD1 
13294 C CD2 . TRP D 382 ? 0.2925 0.3074 0.2956 0.0112  0.0353  0.0036  683 TRP D CD2 
13295 N NE1 . TRP D 382 ? 0.2387 0.2580 0.2390 0.0097  0.0404  0.0049  683 TRP D NE1 
13296 C CE2 . TRP D 382 ? 0.3231 0.3465 0.3286 0.0115  0.0387  0.0047  683 TRP D CE2 
13297 C CE3 . TRP D 382 ? 0.2903 0.3070 0.2966 0.0119  0.0335  0.0033  683 TRP D CE3 
13298 C CZ2 . TRP D 382 ? 0.3095 0.3443 0.3213 0.0135  0.0396  0.0056  683 TRP D CZ2 
13299 C CZ3 . TRP D 382 ? 0.3370 0.3618 0.3477 0.0137  0.0345  0.0043  683 TRP D CZ3 
13300 C CH2 . TRP D 382 ? 0.3010 0.3354 0.3149 0.0149  0.0372  0.0054  683 TRP D CH2 
13301 N N   . ILE D 383 ? 0.2434 0.2329 0.2274 0.0086  0.0236  0.0002  684 ILE D N   
13302 C CA  . ILE D 383 ? 0.2773 0.2702 0.2627 0.0067  0.0198  -0.0007 684 ILE D CA  
13303 C C   . ILE D 383 ? 0.3236 0.3092 0.3003 0.0042  0.0189  -0.0013 684 ILE D C   
13304 O O   . ILE D 383 ? 0.3016 0.2883 0.2780 0.0007  0.0175  -0.0019 684 ILE D O   
13305 C CB  . ILE D 383 ? 0.2907 0.2874 0.2778 0.0082  0.0163  -0.0009 684 ILE D CB  
13306 C CG1 . ILE D 383 ? 0.3284 0.3290 0.3213 0.0106  0.0172  -0.0009 684 ILE D CG1 
13307 C CG2 . ILE D 383 ? 0.2558 0.2601 0.2451 0.0062  0.0122  -0.0019 684 ILE D CG2 
13308 C CD1 . ILE D 383 ? 0.2626 0.2721 0.2634 0.0096  0.0176  -0.0018 684 ILE D CD1 
13309 N N   . VAL D 384 ? 0.2414 0.2182 0.2093 0.0052  0.0197  -0.0011 685 VAL D N   
13310 C CA  . VAL D 384 ? 0.2477 0.2146 0.2043 0.0026  0.0187  -0.0020 685 VAL D CA  
13311 C C   . VAL D 384 ? 0.2708 0.2309 0.2234 0.0033  0.0220  -0.0022 685 VAL D C   
13312 O O   . VAL D 384 ? 0.3191 0.2794 0.2736 0.0079  0.0262  -0.0015 685 VAL D O   
13313 C CB  . VAL D 384 ? 0.2729 0.2308 0.2193 0.0041  0.0196  -0.0019 685 VAL D CB  
13314 C CG1 . VAL D 384 ? 0.2643 0.2096 0.1967 0.0014  0.0187  -0.0033 685 VAL D CG1 
13315 C CG2 . VAL D 384 ? 0.2733 0.2357 0.2213 0.0041  0.0156  -0.0013 685 VAL D CG2 
13316 N N   . PRO D 385 ? 0.3064 0.2605 0.2527 -0.0012 0.0201  -0.0030 686 PRO D N   
13317 C CA  . PRO D 385 ? 0.3318 0.2767 0.2722 0.0003  0.0227  -0.0029 686 PRO D CA  
13318 C C   . PRO D 385 ? 0.3765 0.3077 0.3048 0.0059  0.0265  -0.0033 686 PRO D C   
13319 O O   . PRO D 385 ? 0.3846 0.3098 0.3052 0.0058  0.0263  -0.0041 686 PRO D O   
13320 C CB  . PRO D 385 ? 0.3890 0.3278 0.3217 -0.0080 0.0192  -0.0037 686 PRO D CB  
13321 C CG  . PRO D 385 ? 0.4023 0.3578 0.3461 -0.0127 0.0152  -0.0038 686 PRO D CG  
13322 C CD  . PRO D 385 ? 0.3882 0.3466 0.3341 -0.0083 0.0150  -0.0038 686 PRO D CD  
13323 N N   . PRO D 386 ? 0.3845 0.3108 0.3103 0.0117  0.0299  -0.0027 687 PRO D N   
13324 C CA  . PRO D 386 ? 0.3238 0.2396 0.2390 0.0193  0.0342  -0.0032 687 PRO D CA  
13325 C C   . PRO D 386 ? 0.3901 0.2826 0.2838 0.0181  0.0338  -0.0050 687 PRO D C   
13326 O O   . PRO D 386 ? 0.4308 0.3124 0.3135 0.0260  0.0379  -0.0057 687 PRO D O   
13327 C CB  . PRO D 386 ? 0.3401 0.2612 0.2610 0.0266  0.0371  -0.0018 687 PRO D CB  
13328 C CG  . PRO D 386 ? 0.3152 0.2350 0.2377 0.0208  0.0335  -0.0011 687 PRO D CG  
13329 C CD  . PRO D 386 ? 0.3259 0.2567 0.2578 0.0122  0.0298  -0.0015 687 PRO D CD  
13330 N N   . MET D 387 ? 0.3540 0.2388 0.2408 0.0086  0.0292  -0.0058 688 MET D N   
13331 C CA  . MET D 387 ? 0.4181 0.2800 0.2827 0.0048  0.0280  -0.0078 688 MET D CA  
13332 C C   . MET D 387 ? 0.4879 0.3552 0.3535 -0.0067 0.0224  -0.0085 688 MET D C   
13333 O O   . MET D 387 ? 0.4152 0.3014 0.2969 -0.0114 0.0194  -0.0075 688 MET D O   
13334 C CB  . MET D 387 ? 0.3967 0.2375 0.2448 0.0038  0.0280  -0.0079 688 MET D CB  
13335 C CG  . MET D 387 ? 0.4916 0.3366 0.3432 -0.0078 0.0236  -0.0071 688 MET D CG  
13336 S SD  . MET D 387 ? 0.5711 0.3882 0.4004 -0.0108 0.0235  -0.0067 688 MET D SD  
13337 C CE  . MET D 387 ? 0.5887 0.3769 0.3889 -0.0198 0.0211  -0.0096 688 MET D CE  
13338 N N   . SER D 388 ? 0.4764 0.3276 0.3242 -0.0102 0.0210  -0.0105 689 SER D N   
13339 C CA  . SER D 388 ? 0.4510 0.3060 0.2965 -0.0217 0.0149  -0.0113 689 SER D CA  
13340 C C   . SER D 388 ? 0.4069 0.2875 0.2729 -0.0215 0.0123  -0.0100 689 SER D C   
13341 O O   . SER D 388 ? 0.4479 0.3422 0.3216 -0.0293 0.0071  -0.0098 689 SER D O   
13342 C CB  . SER D 388 ? 0.5617 0.4135 0.4029 -0.0329 0.0112  -0.0113 689 SER D CB  
13343 O OG  . SER D 388 ? 0.6303 0.4537 0.4486 -0.0330 0.0133  -0.0124 689 SER D OG  
13344 N N   . GLY D 389 ? 0.3828 0.2697 0.2567 -0.0123 0.0162  -0.0091 690 GLY D N   
13345 C CA  . GLY D 389 ? 0.3585 0.2654 0.2494 -0.0107 0.0145  -0.0076 690 GLY D CA  
13346 C C   . GLY D 389 ? 0.3971 0.3116 0.2882 -0.0172 0.0078  -0.0078 690 GLY D C   
13347 O O   . GLY D 389 ? 0.3360 0.2677 0.2408 -0.0198 0.0042  -0.0070 690 GLY D O   
13348 N N   . SER D 390 ? 0.3200 0.2223 0.1955 -0.0196 0.0060  -0.0090 691 SER D N   
13349 C CA  . SER D 390 ? 0.3303 0.2420 0.2067 -0.0241 -0.0007 -0.0088 691 SER D CA  
13350 C C   . SER D 390 ? 0.3474 0.2652 0.2227 -0.0349 -0.0069 -0.0097 691 SER D C   
13351 O O   . SER D 390 ? 0.4089 0.3393 0.2874 -0.0385 -0.0133 -0.0094 691 SER D O   
13352 C CB  . SER D 390 ? 0.3698 0.2674 0.2294 -0.0232 -0.0009 -0.0095 691 SER D CB  
13353 O OG  . SER D 390 ? 0.4288 0.3065 0.2689 -0.0282 -0.0003 -0.0118 691 SER D OG  
13354 N N   . ILE D 391 ? 0.3821 0.2919 0.2523 -0.0405 -0.0056 -0.0107 692 ILE D N   
13355 C CA  . ILE D 391 ? 0.4475 0.3680 0.3195 -0.0523 -0.0114 -0.0112 692 ILE D CA  
13356 C C   . ILE D 391 ? 0.4216 0.3656 0.3153 -0.0514 -0.0113 -0.0097 692 ILE D C   
13357 O O   . ILE D 391 ? 0.5045 0.4623 0.4029 -0.0609 -0.0152 -0.0099 692 ILE D O   
13358 C CB  . ILE D 391 ? 0.4862 0.3838 0.3370 -0.0622 -0.0112 -0.0130 692 ILE D CB  
13359 C CG1 . ILE D 391 ? 0.5302 0.4118 0.3767 -0.0565 -0.0045 -0.0127 692 ILE D CG1 
13360 C CG2 . ILE D 391 ? 0.5504 0.4264 0.3780 -0.0646 -0.0128 -0.0149 692 ILE D CG2 
13361 C CD1 . ILE D 391 ? 0.6642 0.5262 0.4924 -0.0670 -0.0050 -0.0138 692 ILE D CD1 
13362 N N   . THR D 392 ? 0.4647 0.4146 0.3716 -0.0405 -0.0067 -0.0084 693 THR D N   
13363 C CA  . THR D 392 ? 0.4035 0.3761 0.3303 -0.0383 -0.0071 -0.0073 693 THR D CA  
13364 C C   . THR D 392 ? 0.4159 0.4042 0.3530 -0.0320 -0.0104 -0.0065 693 THR D C   
13365 O O   . THR D 392 ? 0.3583 0.3373 0.2885 -0.0270 -0.0104 -0.0061 693 THR D O   
13366 C CB  . THR D 392 ? 0.3622 0.3317 0.2958 -0.0313 -0.0010 -0.0065 693 THR D CB  
13367 O OG1 . THR D 392 ? 0.3907 0.3553 0.3254 -0.0218 0.0021  -0.0057 693 THR D OG1 
13368 C CG2 . THR D 392 ? 0.3360 0.2867 0.2571 -0.0347 0.0024  -0.0069 693 THR D CG2 
13369 N N   . PRO D 393 ? 0.3479 0.3593 0.3000 -0.0319 -0.0134 -0.0061 694 PRO D N   
13370 C CA  . PRO D 393 ? 0.3235 0.3481 0.2827 -0.0247 -0.0174 -0.0053 694 PRO D CA  
13371 C C   . PRO D 393 ? 0.3404 0.3574 0.3020 -0.0138 -0.0135 -0.0041 694 PRO D C   
13372 O O   . PRO D 393 ? 0.4047 0.4217 0.3644 -0.0079 -0.0163 -0.0031 694 PRO D O   
13373 C CB  . PRO D 393 ? 0.3537 0.4055 0.3285 -0.0260 -0.0202 -0.0055 694 PRO D CB  
13374 C CG  . PRO D 393 ? 0.2994 0.3504 0.2775 -0.0316 -0.0155 -0.0060 694 PRO D CG  
13375 C CD  . PRO D 393 ? 0.3171 0.3438 0.2780 -0.0388 -0.0137 -0.0065 694 PRO D CD  
13376 N N   . VAL D 394 ? 0.3351 0.3448 0.2993 -0.0116 -0.0075 -0.0040 695 VAL D N   
13377 C CA  . VAL D 394 ? 0.3229 0.3278 0.2898 -0.0032 -0.0042 -0.0029 695 VAL D CA  
13378 C C   . VAL D 394 ? 0.2809 0.2689 0.2353 -0.0013 -0.0026 -0.0022 695 VAL D C   
13379 O O   . VAL D 394 ? 0.2645 0.2487 0.2182 0.0042  -0.0016 -0.0010 695 VAL D O   
13380 C CB  . VAL D 394 ? 0.2868 0.2912 0.2605 -0.0020 0.0012  -0.0029 695 VAL D CB  
13381 C CG1 . VAL D 394 ? 0.2158 0.2378 0.2019 -0.0025 0.0000  -0.0035 695 VAL D CG1 
13382 C CG2 . VAL D 394 ? 0.2658 0.2577 0.2317 -0.0064 0.0048  -0.0033 695 VAL D CG2 
13383 N N   . PHE D 395 ? 0.3043 0.2808 0.2470 -0.0062 -0.0021 -0.0030 696 PHE D N   
13384 C CA  . PHE D 395 ? 0.3646 0.3258 0.2943 -0.0043 -0.0001 -0.0026 696 PHE D CA  
13385 C C   . PHE D 395 ? 0.3698 0.3324 0.2957 -0.0016 -0.0048 -0.0014 696 PHE D C   
13386 O O   . PHE D 395 ? 0.2995 0.2530 0.2190 0.0021  -0.0024 -0.0002 696 PHE D O   
13387 C CB  . PHE D 395 ? 0.4415 0.3896 0.3573 -0.0097 0.0005  -0.0042 696 PHE D CB  
13388 C CG  . PHE D 395 ? 0.3975 0.3299 0.2984 -0.0076 0.0032  -0.0043 696 PHE D CG  
13389 C CD1 . PHE D 395 ? 0.4310 0.3536 0.3277 -0.0040 0.0104  -0.0045 696 PHE D CD1 
13390 C CD2 . PHE D 395 ? 0.3244 0.2531 0.2153 -0.0091 -0.0014 -0.0041 696 PHE D CD2 
13391 C CE1 . PHE D 395 ? 0.3630 0.2731 0.2461 -0.0018 0.0138  -0.0048 696 PHE D CE1 
13392 C CE2 . PHE D 395 ? 0.4255 0.3394 0.3014 -0.0075 0.0016  -0.0042 696 PHE D CE2 
13393 C CZ  . PHE D 395 ? 0.4619 0.3667 0.3339 -0.0040 0.0096  -0.0047 696 PHE D CZ  
13394 N N   . HIS D 396 ? 0.2966 0.2716 0.2262 -0.0034 -0.0116 -0.0016 697 HIS D N   
13395 C CA  . HIS D 396 ? 0.3269 0.3040 0.2518 -0.0002 -0.0174 -0.0004 697 HIS D CA  
13396 C C   . HIS D 396 ? 0.3830 0.3699 0.3176 0.0080  -0.0191 0.0011  697 HIS D C   
13397 O O   . HIS D 396 ? 0.3978 0.3876 0.3290 0.0125  -0.0248 0.0024  697 HIS D O   
13398 C CB  . HIS D 396 ? 0.3448 0.3322 0.2679 -0.0066 -0.0246 -0.0014 697 HIS D CB  
13399 C CG  . HIS D 396 ? 0.3977 0.3724 0.3084 -0.0155 -0.0232 -0.0032 697 HIS D CG  
13400 N ND1 . HIS D 396 ? 0.4101 0.3679 0.3030 -0.0172 -0.0237 -0.0034 697 HIS D ND1 
13401 C CD2 . HIS D 396 ? 0.4127 0.3861 0.3236 -0.0227 -0.0211 -0.0049 697 HIS D CD2 
13402 C CE1 . HIS D 396 ? 0.4381 0.3845 0.3206 -0.0247 -0.0219 -0.0055 697 HIS D CE1 
13403 N NE2 . HIS D 396 ? 0.4761 0.4307 0.3687 -0.0282 -0.0205 -0.0063 697 HIS D NE2 
13404 N N   . GLN D 397 ? 0.3115 0.3021 0.2565 0.0104  -0.0147 0.0009  698 GLN D N   
13405 C CA  . GLN D 397 ? 0.2992 0.2969 0.2520 0.0181  -0.0156 0.0017  698 GLN D CA  
13406 C C   . GLN D 397 ? 0.2928 0.2739 0.2385 0.0218  -0.0112 0.0032  698 GLN D C   
13407 O O   . GLN D 397 ? 0.3554 0.3306 0.3023 0.0189  -0.0051 0.0028  698 GLN D O   
13408 C CB  . GLN D 397 ? 0.3165 0.3285 0.2837 0.0173  -0.0134 0.0002  698 GLN D CB  
13409 C CG  . GLN D 397 ? 0.2770 0.2941 0.2506 0.0257  -0.0135 0.0005  698 GLN D CG  
13410 C CD  . GLN D 397 ? 0.3130 0.3423 0.2882 0.0325  -0.0203 0.0009  698 GLN D CD  
13411 O OE1 . GLN D 397 ? 0.2578 0.3061 0.2406 0.0297  -0.0241 0.0000  698 GLN D OE1 
13412 N NE2 . GLN D 397 ? 0.2849 0.3034 0.2521 0.0412  -0.0220 0.0025  698 GLN D NE2 
13413 N N   . GLU D 398 ? 0.2899 0.2636 0.2274 0.0278  -0.0143 0.0050  699 GLU D N   
13414 C CA  . GLU D 398 ? 0.2766 0.2345 0.2067 0.0300  -0.0102 0.0065  699 GLU D CA  
13415 C C   . GLU D 398 ? 0.3389 0.3019 0.2789 0.0328  -0.0077 0.0055  699 GLU D C   
13416 O O   . GLU D 398 ? 0.2752 0.2518 0.2245 0.0374  -0.0107 0.0044  699 GLU D O   
13417 C CB  . GLU D 398 ? 0.3161 0.2615 0.2321 0.0358  -0.0145 0.0089  699 GLU D CB  
13418 C CG  . GLU D 398 ? 0.3057 0.2428 0.2089 0.0323  -0.0163 0.0100  699 GLU D CG  
13419 C CD  . GLU D 398 ? 0.4125 0.3369 0.3005 0.0383  -0.0213 0.0128  699 GLU D CD  
13420 O OE1 . GLU D 398 ? 0.4159 0.3288 0.2898 0.0352  -0.0217 0.0141  699 GLU D OE1 
13421 O OE2 . GLU D 398 ? 0.4082 0.3326 0.2967 0.0466  -0.0247 0.0135  699 GLU D OE2 
13422 N N   . MET D 399 ? 0.2930 0.2464 0.2308 0.0298  -0.0020 0.0059  700 MET D N   
13423 C CA  . MET D 399 ? 0.3333 0.2893 0.2782 0.0314  0.0005  0.0049  700 MET D CA  
13424 C C   . MET D 399 ? 0.3939 0.3318 0.3269 0.0311  0.0030  0.0065  700 MET D C   
13425 O O   . MET D 399 ? 0.4674 0.3939 0.3900 0.0268  0.0052  0.0082  700 MET D O   
13426 C CB  . MET D 399 ? 0.3074 0.2733 0.2637 0.0257  0.0049  0.0034  700 MET D CB  
13427 C CG  . MET D 399 ? 0.2585 0.2395 0.2241 0.0243  0.0027  0.0019  700 MET D CG  
13428 S SD  . MET D 399 ? 0.3418 0.3274 0.3144 0.0176  0.0078  0.0009  700 MET D SD  
13429 C CE  . MET D 399 ? 0.3084 0.3058 0.2853 0.0147  0.0039  -0.0004 700 MET D CE  
13430 N N   . LEU D 400 ? 0.3754 0.3101 0.3085 0.0353  0.0027  0.0058  701 LEU D N   
13431 C CA  . LEU D 400 ? 0.3372 0.2540 0.2586 0.0329  0.0054  0.0068  701 LEU D CA  
13432 C C   . LEU D 400 ? 0.3842 0.3081 0.3152 0.0274  0.0099  0.0053  701 LEU D C   
13433 O O   . LEU D 400 ? 0.3949 0.3311 0.3371 0.0305  0.0093  0.0032  701 LEU D O   
13434 C CB  . LEU D 400 ? 0.3379 0.2410 0.2481 0.0419  0.0017  0.0070  701 LEU D CB  
13435 C CG  . LEU D 400 ? 0.4659 0.3583 0.3631 0.0485  -0.0034 0.0092  701 LEU D CG  
13436 C CD1 . LEU D 400 ? 0.5061 0.3864 0.3934 0.0598  -0.0069 0.0090  701 LEU D CD1 
13437 C CD2 . LEU D 400 ? 0.4213 0.2953 0.3025 0.0408  -0.0010 0.0120  701 LEU D CD2 
13438 N N   . ASN D 401 ? 0.3922 0.3100 0.3189 0.0191  0.0142  0.0063  702 ASN D N   
13439 C CA  . ASN D 401 ? 0.3419 0.2670 0.2768 0.0135  0.0179  0.0052  702 ASN D CA  
13440 C C   . ASN D 401 ? 0.4061 0.3143 0.3283 0.0103  0.0186  0.0055  702 ASN D C   
13441 O O   . ASN D 401 ? 0.3995 0.2920 0.3070 0.0061  0.0194  0.0075  702 ASN D O   
13442 C CB  . ASN D 401 ? 0.3913 0.3265 0.3327 0.0064  0.0222  0.0059  702 ASN D CB  
13443 C CG  . ASN D 401 ? 0.3845 0.3326 0.3378 0.0031  0.0246  0.0046  702 ASN D CG  
13444 O OD1 . ASN D 401 ? 0.3843 0.3345 0.3417 0.0060  0.0230  0.0029  702 ASN D OD1 
13445 N ND2 . ASN D 401 ? 0.3376 0.2946 0.2958 -0.0022 0.0284  0.0053  702 ASN D ND2 
13446 N N   . TYR D 402 ? 0.4026 0.3125 0.3285 0.0117  0.0185  0.0034  703 TYR D N   
13447 C CA  . TYR D 402 ? 0.2996 0.1922 0.2120 0.0074  0.0193  0.0032  703 TYR D CA  
13448 C C   . TYR D 402 ? 0.3824 0.2856 0.3048 0.0057  0.0205  0.0007  703 TYR D C   
13449 O O   . TYR D 402 ? 0.3302 0.2513 0.2678 0.0100  0.0202  -0.0007 703 TYR D O   
13450 C CB  . TYR D 402 ? 0.3230 0.1926 0.2175 0.0156  0.0158  0.0032  703 TYR D CB  
13451 C CG  . TYR D 402 ? 0.4116 0.2895 0.3133 0.0291  0.0123  0.0015  703 TYR D CG  
13452 C CD1 . TYR D 402 ? 0.4205 0.3004 0.3248 0.0355  0.0118  -0.0014 703 TYR D CD1 
13453 C CD2 . TYR D 402 ? 0.3968 0.2821 0.3023 0.0352  0.0094  0.0028  703 TYR D CD2 
13454 C CE1 . TYR D 402 ? 0.3129 0.2044 0.2249 0.0479  0.0090  -0.0029 703 TYR D CE1 
13455 C CE2 . TYR D 402 ? 0.3449 0.2417 0.2580 0.0465  0.0059  0.0014  703 TYR D CE2 
13456 C CZ  . TYR D 402 ? 0.4212 0.3224 0.3383 0.0529  0.0059  -0.0014 703 TYR D CZ  
13457 O OH  . TYR D 402 ? 0.4474 0.3638 0.3732 0.0640  0.0029  -0.0028 703 TYR D OH  
13458 N N   . ARG D 403 ? 0.3933 0.2845 0.3055 -0.0015 0.0217  0.0003  704 ARG D N   
13459 C CA  . ARG D 403 ? 0.4351 0.3363 0.3552 -0.0061 0.0230  -0.0016 704 ARG D CA  
13460 C C   . ARG D 403 ? 0.5280 0.4135 0.4369 -0.0007 0.0214  -0.0043 704 ARG D C   
13461 O O   . ARG D 403 ? 0.5217 0.3829 0.4107 -0.0037 0.0210  -0.0043 704 ARG D O   
13462 C CB  . ARG D 403 ? 0.3923 0.2956 0.3103 -0.0200 0.0256  -0.0002 704 ARG D CB  
13463 C CG  . ARG D 403 ? 0.4000 0.3201 0.3287 -0.0238 0.0279  0.0023  704 ARG D CG  
13464 C CD  . ARG D 403 ? 0.5459 0.4730 0.4744 -0.0371 0.0307  0.0036  704 ARG D CD  
13465 N NE  . ARG D 403 ? 0.6503 0.5949 0.5912 -0.0399 0.0308  0.0023  704 ARG D NE  
13466 C CZ  . ARG D 403 ? 0.7357 0.6897 0.6779 -0.0511 0.0322  0.0030  704 ARG D CZ  
13467 N NH1 . ARG D 403 ? 0.7284 0.6766 0.6605 -0.0619 0.0341  0.0048  704 ARG D NH1 
13468 N NH2 . ARG D 403 ? 0.7431 0.7133 0.6963 -0.0523 0.0315  0.0020  704 ARG D NH2 
13469 N N   . LEU D 404 ? 0.4636 0.3618 0.3837 0.0072  0.0209  -0.0066 705 LEU D N   
13470 C CA  . LEU D 404 ? 0.4041 0.2915 0.3157 0.0136  0.0202  -0.0097 705 LEU D CA  
13471 C C   . LEU D 404 ? 0.3423 0.2380 0.2591 0.0065  0.0217  -0.0115 705 LEU D C   
13472 O O   . LEU D 404 ? 0.3661 0.2816 0.2978 0.0005  0.0228  -0.0104 705 LEU D O   
13473 C CB  . LEU D 404 ? 0.3875 0.2857 0.3077 0.0274  0.0188  -0.0112 705 LEU D CB  
13474 C CG  . LEU D 404 ? 0.3834 0.2764 0.2995 0.0359  0.0162  -0.0094 705 LEU D CG  
13475 C CD1 . LEU D 404 ? 0.3702 0.2791 0.2968 0.0486  0.0147  -0.0111 705 LEU D CD1 
13476 C CD2 . LEU D 404 ? 0.3374 0.1990 0.2289 0.0380  0.0149  -0.0089 705 LEU D CD2 
13477 N N   . THR D 405 ? 0.4023 0.2811 0.3048 0.0076  0.0217  -0.0142 706 THR D N   
13478 C CA  . THR D 405 ? 0.4096 0.2944 0.3146 0.0016  0.0227  -0.0163 706 THR D CA  
13479 C C   . THR D 405 ? 0.4656 0.3522 0.3712 0.0131  0.0231  -0.0198 706 THR D C   
13480 O O   . THR D 405 ? 0.4169 0.2913 0.3135 0.0246  0.0225  -0.0211 706 THR D O   
13481 C CB  . THR D 405 ? 0.5343 0.3965 0.4191 -0.0096 0.0225  -0.0169 706 THR D CB  
13482 O OG1 . THR D 405 ? 0.5513 0.4229 0.4401 -0.0173 0.0229  -0.0185 706 THR D OG1 
13483 C CG2 . THR D 405 ? 0.5205 0.3513 0.3811 -0.0019 0.0217  -0.0194 706 THR D CG2 
13484 N N   . PRO D 406 ? 0.4523 0.3555 0.3688 0.0111  0.0243  -0.0212 707 PRO D N   
13485 C CA  . PRO D 406 ? 0.4003 0.3207 0.3288 0.0004  0.0245  -0.0197 707 PRO D CA  
13486 C C   . PRO D 406 ? 0.3776 0.3173 0.3232 -0.0011 0.0244  -0.0162 707 PRO D C   
13487 O O   . PRO D 406 ? 0.3765 0.3205 0.3277 0.0064  0.0242  -0.0153 707 PRO D O   
13488 C CB  . PRO D 406 ? 0.3866 0.3182 0.3210 0.0040  0.0257  -0.0222 707 PRO D CB  
13489 C CG  . PRO D 406 ? 0.3755 0.2906 0.2959 0.0139  0.0265  -0.0259 707 PRO D CG  
13490 C CD  . PRO D 406 ? 0.4136 0.3197 0.3302 0.0216  0.0255  -0.0247 707 PRO D CD  
13491 N N   . SER D 407 ? 0.2690 0.2207 0.2222 -0.0103 0.0245  -0.0142 708 SER D N   
13492 C CA  . SER D 407 ? 0.2899 0.2571 0.2567 -0.0106 0.0247  -0.0112 708 SER D CA  
13493 C C   . SER D 407 ? 0.2492 0.2337 0.2264 -0.0164 0.0248  -0.0098 708 SER D C   
13494 O O   . SER D 407 ? 0.2678 0.2521 0.2410 -0.0225 0.0241  -0.0106 708 SER D O   
13495 C CB  . SER D 407 ? 0.4327 0.3913 0.3935 -0.0146 0.0248  -0.0090 708 SER D CB  
13496 O OG  . SER D 407 ? 0.4707 0.4231 0.4229 -0.0254 0.0248  -0.0087 708 SER D OG  
13497 N N   . PHE D 408 ? 0.3066 0.3048 0.2956 -0.0141 0.0253  -0.0076 709 PHE D N   
13498 C CA  . PHE D 408 ? 0.2943 0.3079 0.2922 -0.0180 0.0253  -0.0054 709 PHE D CA  
13499 C C   . PHE D 408 ? 0.3409 0.3570 0.3390 -0.0230 0.0261  -0.0033 709 PHE D C   
13500 O O   . PHE D 408 ? 0.3455 0.3556 0.3415 -0.0208 0.0271  -0.0026 709 PHE D O   
13501 C CB  . PHE D 408 ? 0.2516 0.2755 0.2592 -0.0121 0.0256  -0.0044 709 PHE D CB  
13502 C CG  . PHE D 408 ? 0.3032 0.3278 0.3112 -0.0090 0.0252  -0.0060 709 PHE D CG  
13503 C CD1 . PHE D 408 ? 0.2984 0.3203 0.3067 -0.0036 0.0257  -0.0073 709 PHE D CD1 
13504 C CD2 . PHE D 408 ? 0.2913 0.3208 0.2990 -0.0121 0.0244  -0.0063 709 PHE D CD2 
13505 C CE1 . PHE D 408 ? 0.2389 0.2640 0.2479 -0.0015 0.0261  -0.0089 709 PHE D CE1 
13506 C CE2 . PHE D 408 ? 0.2336 0.2638 0.2407 -0.0098 0.0247  -0.0078 709 PHE D CE2 
13507 C CZ  . PHE D 408 ? 0.2253 0.2537 0.2332 -0.0046 0.0259  -0.0091 709 PHE D CZ  
13508 N N   . GLU D 409 ? 0.3166 0.3430 0.3170 -0.0300 0.0257  -0.0022 710 GLU D N   
13509 C CA  . GLU D 409 ? 0.3013 0.3341 0.3025 -0.0363 0.0270  -0.0003 710 GLU D CA  
13510 C C   . GLU D 409 ? 0.3401 0.3955 0.3538 -0.0353 0.0272  0.0019  710 GLU D C   
13511 O O   . GLU D 409 ? 0.3028 0.3661 0.3213 -0.0325 0.0255  0.0019  710 GLU D O   
13512 C CB  . GLU D 409 ? 0.3097 0.3349 0.3002 -0.0477 0.0263  -0.0010 710 GLU D CB  
13513 C CG  . GLU D 409 ? 0.4380 0.4373 0.4126 -0.0478 0.0259  -0.0032 710 GLU D CG  
13514 C CD  . GLU D 409 ? 0.5369 0.5254 0.5070 -0.0441 0.0275  -0.0021 710 GLU D CD  
13515 O OE1 . GLU D 409 ? 0.5678 0.5674 0.5443 -0.0456 0.0294  0.0002  710 GLU D OE1 
13516 O OE2 . GLU D 409 ? 0.5595 0.5284 0.5189 -0.0392 0.0269  -0.0037 710 GLU D OE2 
13517 N N   . TYR D 410 ? 0.2487 0.3142 0.2665 -0.0370 0.0294  0.0038  711 TYR D N   
13518 C CA  . TYR D 410 ? 0.2287 0.3175 0.2575 -0.0359 0.0297  0.0059  711 TYR D CA  
13519 C C   . TYR D 410 ? 0.2287 0.3300 0.2581 -0.0467 0.0279  0.0062  711 TYR D C   
13520 O O   . TYR D 410 ? 0.3186 0.4095 0.3384 -0.0569 0.0276  0.0051  711 TYR D O   
13521 C CB  . TYR D 410 ? 0.3147 0.4121 0.3476 -0.0335 0.0333  0.0076  711 TYR D CB  
13522 C CG  . TYR D 410 ? 0.4063 0.4938 0.4386 -0.0233 0.0348  0.0074  711 TYR D CG  
13523 C CD1 . TYR D 410 ? 0.7056 0.7785 0.7305 -0.0237 0.0366  0.0070  711 TYR D CD1 
13524 C CD2 . TYR D 410 ? 0.5733 0.6651 0.6107 -0.0140 0.0341  0.0078  711 TYR D CD2 
13525 C CE1 . TYR D 410 ? 0.7850 0.8498 0.8087 -0.0155 0.0374  0.0067  711 TYR D CE1 
13526 C CE2 . TYR D 410 ? 0.7401 0.8219 0.7751 -0.0064 0.0353  0.0076  711 TYR D CE2 
13527 C CZ  . TYR D 410 ? 0.6723 0.7416 0.7010 -0.0075 0.0368  0.0069  711 TYR D CZ  
13528 O OH  . TYR D 410 ? 0.5491 0.6091 0.5748 -0.0009 0.0374  0.0066  711 TYR D OH  
13529 N N   . GLN D 411 ? 0.1861 0.3094 0.2257 -0.0444 0.0265  0.0077  712 GLN D N   
13530 C CA  . GLN D 411 ? 0.2777 0.4186 0.3200 -0.0545 0.0242  0.0083  712 GLN D CA  
13531 C C   . GLN D 411 ? 0.2682 0.4387 0.3245 -0.0491 0.0248  0.0110  712 GLN D C   
13532 O O   . GLN D 411 ? 0.2911 0.4636 0.3525 -0.0361 0.0262  0.0120  712 GLN D O   
13533 C CB  . GLN D 411 ? 0.3279 0.4632 0.3656 -0.0570 0.0198  0.0069  712 GLN D CB  
13534 C CG  . GLN D 411 ? 0.2504 0.3893 0.2935 -0.0451 0.0179  0.0076  712 GLN D CG  
13535 C CD  . GLN D 411 ? 0.2340 0.3636 0.2699 -0.0480 0.0144  0.0059  712 GLN D CD  
13536 O OE1 . GLN D 411 ? 0.3332 0.4634 0.3635 -0.0590 0.0121  0.0047  712 GLN D OE1 
13537 N NE2 . GLN D 411 ? 0.2665 0.3866 0.3012 -0.0390 0.0141  0.0056  712 GLN D NE2 
13538 N N   . PRO D 412 ? 0.2944 0.4884 0.3563 -0.0585 0.0239  0.0122  713 PRO D N   
13539 C CA  . PRO D 412 ? 0.3923 0.6181 0.4685 -0.0516 0.0247  0.0147  713 PRO D CA  
13540 C C   . PRO D 412 ? 0.3926 0.6260 0.4741 -0.0401 0.0207  0.0158  713 PRO D C   
13541 O O   . PRO D 412 ? 0.3439 0.5662 0.4195 -0.0426 0.0166  0.0148  713 PRO D O   
13542 C CB  . PRO D 412 ? 0.3983 0.6485 0.4786 -0.0671 0.0239  0.0156  713 PRO D CB  
13543 C CG  . PRO D 412 ? 0.3799 0.6083 0.4461 -0.0819 0.0212  0.0134  713 PRO D CG  
13544 C CD  . PRO D 412 ? 0.3585 0.5507 0.4127 -0.0763 0.0227  0.0113  713 PRO D CD  
13545 N N   . ASP D 413 ? 0.4239 0.6738 0.5145 -0.0266 0.0222  0.0178  714 ASP D N   
13546 C CA  . ASP D 413 ? 0.4285 0.6870 0.5229 -0.0147 0.0183  0.0195  714 ASP D CA  
13547 C C   . ASP D 413 ? 0.3985 0.6808 0.4984 -0.0230 0.0128  0.0205  714 ASP D C   
13548 O O   . ASP D 413 ? 0.4085 0.7175 0.5166 -0.0316 0.0133  0.0213  714 ASP D O   
13549 C CB  . ASP D 413 ? 0.5239 0.7978 0.6260 0.0013  0.0212  0.0215  714 ASP D CB  
13550 C CG  . ASP D 413 ? 0.5743 0.8220 0.6686 0.0107  0.0254  0.0204  714 ASP D CG  
13551 O OD1 . ASP D 413 ? 0.5981 0.8184 0.6827 0.0108  0.0241  0.0191  714 ASP D OD1 
13552 O OD2 . ASP D 413 ? 0.5794 0.8354 0.6772 0.0177  0.0301  0.0208  714 ASP D OD2 
13553 N N   . PRO D 414 ? 0.3758 0.6506 0.4709 -0.0215 0.0076  0.0207  715 PRO D N   
13554 C CA  . PRO D 414 ? 0.2700 0.5645 0.3677 -0.0319 0.0019  0.0212  715 PRO D CA  
13555 C C   . PRO D 414 ? 0.3470 0.6818 0.4593 -0.0266 -0.0004 0.0244  715 PRO D C   
13556 O O   . PRO D 414 ? 0.3999 0.7585 0.5172 -0.0390 -0.0040 0.0248  715 PRO D O   
13557 C CB  . PRO D 414 ? 0.3068 0.5816 0.3947 -0.0285 -0.0025 0.0208  715 PRO D CB  
13558 C CG  . PRO D 414 ? 0.2459 0.5022 0.3305 -0.0127 0.0002  0.0215  715 PRO D CG  
13559 C CD  . PRO D 414 ? 0.3403 0.5898 0.4268 -0.0109 0.0067  0.0205  715 PRO D CD  
13560 N N   . TRP D 415 ? 0.3454 0.6897 0.4643 -0.0087 0.0017  0.0265  716 TRP D N   
13561 C CA  . TRP D 415 ? 0.3881 0.7737 0.5216 -0.0018 -0.0003 0.0294  716 TRP D CA  
13562 C C   . TRP D 415 ? 0.4150 0.8290 0.5596 -0.0122 0.0038  0.0292  716 TRP D C   
13563 O O   . TRP D 415 ? 0.4019 0.8565 0.5601 -0.0118 0.0016  0.0314  716 TRP D O   
13564 C CB  . TRP D 415 ? 0.3122 0.6979 0.4472 0.0220  0.0009  0.0316  716 TRP D CB  
13565 C CG  . TRP D 415 ? 0.3553 0.7187 0.4853 0.0297  0.0082  0.0302  716 TRP D CG  
13566 C CD1 . TRP D 415 ? 0.4154 0.7940 0.5529 0.0328  0.0145  0.0300  716 TRP D CD1 
13567 C CD2 . TRP D 415 ? 0.3704 0.6929 0.4861 0.0348  0.0100  0.0288  716 TRP D CD2 
13568 N NE1 . TRP D 415 ? 0.3929 0.7411 0.5207 0.0397  0.0197  0.0284  716 TRP D NE1 
13569 C CE2 . TRP D 415 ? 0.4106 0.7248 0.5254 0.0408  0.0168  0.0277  716 TRP D CE2 
13570 C CE3 . TRP D 415 ? 0.3930 0.6866 0.4964 0.0343  0.0066  0.0282  716 TRP D CE3 
13571 C CZ2 . TRP D 415 ? 0.4510 0.7296 0.5534 0.0455  0.0196  0.0262  716 TRP D CZ2 
13572 C CZ3 . TRP D 415 ? 0.3831 0.6431 0.4752 0.0390  0.0099  0.0268  716 TRP D CZ3 
13573 C CH2 . TRP D 415 ? 0.4634 0.7163 0.5551 0.0442  0.0160  0.0258  716 TRP D CH2 
13574 N N   . ASN D 416 ? 0.5057 0.9006 0.6445 -0.0217 0.0097  0.0269  717 ASN D N   
13575 C CA  . ASN D 416 ? 0.5363 0.9549 0.6826 -0.0347 0.0138  0.0268  717 ASN D CA  
13576 C C   . ASN D 416 ? 0.5461 0.9733 0.6902 -0.0581 0.0098  0.0261  717 ASN D C   
13577 O O   . ASN D 416 ? 0.5274 0.9847 0.6799 -0.0704 0.0115  0.0268  717 ASN D O   
13578 C CB  . ASN D 416 ? 0.4737 0.8664 0.6121 -0.0365 0.0212  0.0250  717 ASN D CB  
13579 C CG  . ASN D 416 ? 0.5251 0.9102 0.6645 -0.0155 0.0257  0.0254  717 ASN D CG  
13580 O OD1 . ASN D 416 ? 0.5976 1.0075 0.7470 -0.0004 0.0256  0.0274  717 ASN D OD1 
13581 N ND2 . ASN D 416 ? 0.4405 0.7908 0.5684 -0.0141 0.0295  0.0236  717 ASN D ND2 
13582 N N   . THR D 417 ? 0.4869 0.8880 0.6185 -0.0651 0.0049  0.0245  718 THR D N   
13583 C CA  . THR D 417 ? 0.5000 0.8996 0.6241 -0.0877 0.0014  0.0230  718 THR D CA  
13584 C C   . THR D 417 ? 0.5117 0.9238 0.6361 -0.0908 -0.0071 0.0236  718 THR D C   
13585 O O   . THR D 417 ? 0.4613 0.8804 0.5810 -0.1105 -0.0108 0.0227  718 THR D O   
13586 C CB  . THR D 417 ? 0.5336 0.8866 0.6383 -0.0960 0.0036  0.0197  718 THR D CB  
13587 O OG1 . THR D 417 ? 0.5990 0.9240 0.6973 -0.0809 0.0029  0.0188  718 THR D OG1 
13588 C CG2 . THR D 417 ? 0.5395 0.8824 0.6417 -0.0992 0.0110  0.0192  718 THR D CG2 
13589 N N   . HIS D 418 ? 0.4683 0.8822 0.5962 -0.0730 -0.0105 0.0252  719 HIS D N   
13590 C CA  . HIS D 418 ? 0.5384 0.9579 0.6631 -0.0754 -0.0187 0.0258  719 HIS D CA  
13591 C C   . HIS D 418 ? 0.5518 1.0214 0.6922 -0.0786 -0.0239 0.0287  719 HIS D C   
13592 O O   . HIS D 418 ? 0.5392 1.0389 0.6950 -0.0643 -0.0224 0.0315  719 HIS D O   
13593 C CB  . HIS D 418 ? 0.4746 0.8747 0.5946 -0.0557 -0.0205 0.0268  719 HIS D CB  
13594 C CG  . HIS D 418 ? 0.4758 0.8793 0.5907 -0.0572 -0.0287 0.0276  719 HIS D CG  
13595 N ND1 . HIS D 418 ? 0.4603 0.8388 0.5597 -0.0709 -0.0315 0.0247  719 HIS D ND1 
13596 C CD2 . HIS D 418 ? 0.4344 0.8625 0.5564 -0.0461 -0.0350 0.0311  719 HIS D CD2 
13597 C CE1 . HIS D 418 ? 0.4894 0.8772 0.5866 -0.0692 -0.0389 0.0262  719 HIS D CE1 
13598 N NE2 . HIS D 418 ? 0.5068 0.9247 0.6175 -0.0543 -0.0414 0.0303  719 HIS D NE2 
13599 N N   . VAL D 419 ? 0.6185 1.0973 0.7544 -0.0970 -0.0301 0.0279  720 VAL D N   
13600 C CA  . VAL D 419 ? 0.6770 1.1931 0.8215 -0.0989 -0.0358 0.0303  720 VAL D CA  
13601 C C   . VAL D 419 ? 0.6366 1.1556 0.7797 -0.0883 -0.0441 0.0321  720 VAL D C   
13602 O O   . VAL D 419 ? 0.5963 1.0880 0.7251 -0.0951 -0.0476 0.0300  720 VAL D O   
13603 C CB  . VAL D 419 ? 0.6980 1.2151 0.8328 -0.1246 -0.0372 0.0284  720 VAL D CB  
13604 C CG1 . VAL D 419 ? 0.6779 1.2046 0.8167 -0.1313 -0.0300 0.0282  720 VAL D CG1 
13605 C CG2 . VAL D 419 ? 0.7162 1.1967 0.8324 -0.1416 -0.0387 0.0246  720 VAL D CG2 
13606 N N   . TRP D 420 ? 0.6701 1.2147 0.8238 -0.0703 -0.0464 0.0356  721 TRP D N   
13607 C CA  . TRP D 420 ? 0.6445 1.1905 0.7962 -0.0564 -0.0539 0.0381  721 TRP D CA  
13608 C C   . TRP D 420 ? 0.7138 1.2744 0.8609 -0.0689 -0.0619 0.0385  721 TRP D C   
13609 O O   . TRP D 420 ? 0.7434 1.3197 0.8917 -0.0851 -0.0615 0.0376  721 TRP D O   
13610 C CB  . TRP D 420 ? 0.5770 1.1388 0.7390 -0.0296 -0.0525 0.0417  721 TRP D CB  
13611 C CG  . TRP D 420 ? 0.6282 1.1706 0.7912 -0.0151 -0.0458 0.0415  721 TRP D CG  
13612 C CD1 . TRP D 420 ? 0.6426 1.1821 0.8105 -0.0167 -0.0369 0.0398  721 TRP D CD1 
13613 C CD2 . TRP D 420 ? 0.5692 1.0796 0.7212 0.0026  -0.0458 0.0425  721 TRP D CD2 
13614 N NE1 . TRP D 420 ? 0.5722 1.0817 0.7340 -0.0009 -0.0318 0.0396  721 TRP D NE1 
13615 C CE2 . TRP D 420 ? 0.5449 1.0334 0.6956 0.0107  -0.0368 0.0411  721 TRP D CE2 
13616 C CE3 . TRP D 420 ? 0.4886 0.9828 0.6290 0.0115  -0.0522 0.0444  721 TRP D CE3 
13617 C CZ2 . TRP D 420 ? 0.4546 0.9063 0.5929 0.0264  -0.0341 0.0413  721 TRP D CZ2 
13618 C CZ3 . TRP D 420 ? 0.4535 0.9107 0.5813 0.0271  -0.0492 0.0449  721 TRP D CZ3 
13619 C CH2 . TRP D 420 ? 0.4793 0.9160 0.6063 0.0339  -0.0403 0.0432  721 TRP D CH2 
13620 N N   . LYS D 421 ? 0.7688 1.3230 0.9091 -0.0612 -0.0694 0.0401  722 LYS D N   
13621 C CA  . LYS D 421 ? 0.8223 1.3859 0.9558 -0.0723 -0.0776 0.0404  722 LYS D CA  
13622 C C   . LYS D 421 ? 0.8203 1.4047 0.9593 -0.0525 -0.0835 0.0450  722 LYS D C   
13623 O O   . LYS D 421 ? 0.8098 1.4138 0.9612 -0.0350 -0.0806 0.0475  722 LYS D O   
13624 C CB  . LYS D 421 ? 0.8593 1.3915 0.9744 -0.0848 -0.0818 0.0376  722 LYS D CB  
13625 C CG  . LYS D 421 ? 0.8785 1.3781 0.9850 -0.0955 -0.0752 0.0333  722 LYS D CG  
13626 C CD  . LYS D 421 ? 0.8959 1.3972 1.0004 -0.1188 -0.0717 0.0300  722 LYS D CD  
13627 C CE  . LYS D 421 ? 0.8581 1.3191 0.9501 -0.1270 -0.0644 0.0257  722 LYS D CE  
13628 N NZ  . LYS D 421 ? 0.7803 1.1986 0.8493 -0.1312 -0.0656 0.0222  722 LYS D NZ  
# 
