data_9CW3
# 
_entry.id   9CW3 
# 
_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   9CW3         pdb_00009cw3 10.2210/pdb9cw3/pdb 
WWPDB D_1000286254 ?            ?                   
# 
_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                        9CW3 
_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-{5-[(4,4-difluoropiperidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' 353.357   4   ? ? ? 
? 
5 non-polymer syn GLYCEROL                                                                                     92.094    6   ? ? ? 
? 
6 non-polymer syn 'ZINC ION'                                                                                   65.409    2   ? ? ? 
? 
7 water       nat water                                                                                        18.015    670 ? ? ? 
? 
# 
_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-{5-[(4,4-difluoropiperidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' A1A0A 
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 
A1A0A non-polymer         . '(6M)-6-{5-[(4,4-difluoropiperidin-1-yl)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' ? 
'C18 H19 F4 N3'    353.357 
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   304 304 ARG ARG 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 ?   ?   ?   A . n 
A 1 44  GLN 44  345 ?   ?   ?   A . n 
A 1 45  HIS 45  346 ?   ?   ?   A . n 
A 1 46  ALA 46  347 ?   ?   ?   A . n 
A 1 47  ARG 47  348 ?   ?   ?   A . n 
A 1 48  ARG 48  349 ?   ?   ?   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 ?   ?   ?   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  345 345 GLN GLN B . n 
B 1 45  HIS 45  346 346 HIS HIS B . n 
B 1 46  ALA 46  347 347 ALA ALA B . n 
B 1 47  ARG 47  348 348 ARG ARG B . n 
B 1 48  ARG 48  349 349 ARG ARG B . n 
B 1 49  PRO 49  350 350 PRO PRO B . n 
B 1 50  GLU 50  351 351 GLU GLU 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 ?   ?   ?   B . n 
B 1 423 VAL 423 724 ?   ?   ?   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  344 344 SER SER C . n 
C 1 44  GLN 44  345 345 GLN GLN C . n 
C 1 45  HIS 45  346 346 HIS HIS C . n 
C 1 46  ALA 46  347 347 ALA ALA C . n 
C 1 47  ARG 47  348 348 ARG ARG C . n 
C 1 48  ARG 48  349 349 ARG ARG C . n 
C 1 49  PRO 49  350 350 PRO PRO C . n 
C 1 50  GLU 50  351 351 GLU GLU 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 ?   ?   ?   C . n 
C 1 423 VAL 423 724 ?   ?   ?   C . n 
D 1 1   CYS 1   302 ?   ?   ?   D . n 
D 1 2   PRO 2   303 ?   ?   ?   D . n 
D 1 3   ARG 3   304 304 ARG ARG 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 ?   ?   ?   D . n 
D 1 45  HIS 45  346 ?   ?   ?   D . n 
D 1 46  ALA 46  347 ?   ?   ?   D . n 
D 1 47  ARG 47  348 ?   ?   ?   D . n 
D 1 48  ARG 48  349 ?   ?   ?   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        A1A0A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0A 
_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 A1A0A 1   803  800 A1A0A 2V5 A . 
H  5 GOL   1   804  881 GOL   GOL A . 
I  5 GOL   1   805  882 GOL   GOL A . 
J  6 ZN    1   801  900 ZN    ZN  B . 
K  2 HEM   1   802  750 HEM   HEM B . 
L  3 H4B   1   803  760 H4B   BH4 B . 
M  4 A1A0A 1   804  800 A1A0A 2V5 B . 
N  5 GOL   1   805  881 GOL   GOL B . 
O  2 HEM   1   801  750 HEM   HEM C . 
P  3 H4B   1   802  760 H4B   BH4 C . 
Q  4 A1A0A 1   803  800 A1A0A 2V5 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 A1A0A 1   803  800 A1A0A 2V5 D . 
X  5 GOL   1   804  881 GOL   GOL D . 
Y  7 HOH   1   901  492 HOH   HOH A . 
Y  7 HOH   2   902  520 HOH   HOH A . 
Y  7 HOH   3   903  194 HOH   HOH A . 
Y  7 HOH   4   904  327 HOH   HOH A . 
Y  7 HOH   5   905  524 HOH   HOH A . 
Y  7 HOH   6   906  501 HOH   HOH A . 
Y  7 HOH   7   907  473 HOH   HOH A . 
Y  7 HOH   8   908  483 HOH   HOH A . 
Y  7 HOH   9   909  339 HOH   HOH A . 
Y  7 HOH   10  910  154 HOH   HOH A . 
Y  7 HOH   11  911  170 HOH   HOH A . 
Y  7 HOH   12  912  340 HOH   HOH A . 
Y  7 HOH   13  913  155 HOH   HOH A . 
Y  7 HOH   14  914  522 HOH   HOH A . 
Y  7 HOH   15  915  184 HOH   HOH A . 
Y  7 HOH   16  916  490 HOH   HOH A . 
Y  7 HOH   17  917  489 HOH   HOH A . 
Y  7 HOH   18  918  516 HOH   HOH A . 
Y  7 HOH   19  919  151 HOH   HOH A . 
Y  7 HOH   20  920  202 HOH   HOH A . 
Y  7 HOH   21  921  519 HOH   HOH A . 
Y  7 HOH   22  922  527 HOH   HOH A . 
Y  7 HOH   23  923  277 HOH   HOH A . 
Y  7 HOH   24  924  116 HOH   HOH A . 
Y  7 HOH   25  925  280 HOH   HOH A . 
Y  7 HOH   26  926  289 HOH   HOH A . 
Y  7 HOH   27  927  81  HOH   HOH A . 
Y  7 HOH   28  928  32  HOH   HOH A . 
Y  7 HOH   29  929  449 HOH   HOH A . 
Y  7 HOH   30  930  538 HOH   HOH A . 
Y  7 HOH   31  931  258 HOH   HOH A . 
Y  7 HOH   32  932  39  HOH   HOH A . 
Y  7 HOH   33  933  28  HOH   HOH A . 
Y  7 HOH   34  934  329 HOH   HOH A . 
Y  7 HOH   35  935  368 HOH   HOH A . 
Y  7 HOH   36  936  7   HOH   HOH A . 
Y  7 HOH   37  937  29  HOH   HOH A . 
Y  7 HOH   38  938  530 HOH   HOH A . 
Y  7 HOH   39  939  4   HOH   HOH A . 
Y  7 HOH   40  940  104 HOH   HOH A . 
Y  7 HOH   41  941  179 HOH   HOH A . 
Y  7 HOH   42  942  187 HOH   HOH A . 
Y  7 HOH   43  943  361 HOH   HOH A . 
Y  7 HOH   44  944  494 HOH   HOH A . 
Y  7 HOH   45  945  173 HOH   HOH A . 
Y  7 HOH   46  946  321 HOH   HOH A . 
Y  7 HOH   47  947  369 HOH   HOH A . 
Y  7 HOH   48  948  88  HOH   HOH A . 
Y  7 HOH   49  949  266 HOH   HOH A . 
Y  7 HOH   50  950  142 HOH   HOH A . 
Y  7 HOH   51  951  51  HOH   HOH A . 
Y  7 HOH   52  952  414 HOH   HOH A . 
Y  7 HOH   53  953  94  HOH   HOH A . 
Y  7 HOH   54  954  57  HOH   HOH A . 
Y  7 HOH   55  955  53  HOH   HOH A . 
Y  7 HOH   56  956  350 HOH   HOH A . 
Y  7 HOH   57  957  503 HOH   HOH A . 
Y  7 HOH   58  958  33  HOH   HOH A . 
Y  7 HOH   59  959  271 HOH   HOH A . 
Y  7 HOH   60  960  58  HOH   HOH A . 
Y  7 HOH   61  961  267 HOH   HOH A . 
Y  7 HOH   62  962  234 HOH   HOH A . 
Y  7 HOH   63  963  159 HOH   HOH A . 
Y  7 HOH   64  964  147 HOH   HOH A . 
Y  7 HOH   65  965  130 HOH   HOH A . 
Y  7 HOH   66  966  283 HOH   HOH A . 
Y  7 HOH   67  967  344 HOH   HOH A . 
Y  7 HOH   68  968  343 HOH   HOH A . 
Y  7 HOH   69  969  97  HOH   HOH A . 
Y  7 HOH   70  970  26  HOH   HOH A . 
Y  7 HOH   71  971  148 HOH   HOH A . 
Y  7 HOH   72  972  386 HOH   HOH A . 
Y  7 HOH   73  973  211 HOH   HOH A . 
Y  7 HOH   74  974  286 HOH   HOH A . 
Y  7 HOH   75  975  216 HOH   HOH A . 
Y  7 HOH   76  976  509 HOH   HOH A . 
Y  7 HOH   77  977  163 HOH   HOH A . 
Y  7 HOH   78  978  152 HOH   HOH A . 
Y  7 HOH   79  979  114 HOH   HOH A . 
Y  7 HOH   80  980  84  HOH   HOH A . 
Y  7 HOH   81  981  178 HOH   HOH A . 
Y  7 HOH   82  982  109 HOH   HOH A . 
Y  7 HOH   83  983  415 HOH   HOH A . 
Y  7 HOH   84  984  99  HOH   HOH A . 
Y  7 HOH   85  985  508 HOH   HOH A . 
Y  7 HOH   86  986  507 HOH   HOH A . 
Y  7 HOH   87  987  222 HOH   HOH A . 
Y  7 HOH   88  988  511 HOH   HOH A . 
Y  7 HOH   89  989  358 HOH   HOH A . 
Y  7 HOH   90  990  384 HOH   HOH A . 
Y  7 HOH   91  991  291 HOH   HOH A . 
Y  7 HOH   92  992  443 HOH   HOH A . 
Y  7 HOH   93  993  103 HOH   HOH A . 
Y  7 HOH   94  994  515 HOH   HOH A . 
Y  7 HOH   95  995  139 HOH   HOH A . 
Y  7 HOH   96  996  236 HOH   HOH A . 
Y  7 HOH   97  997  60  HOH   HOH A . 
Y  7 HOH   98  998  478 HOH   HOH A . 
Y  7 HOH   99  999  412 HOH   HOH A . 
Y  7 HOH   100 1000 484 HOH   HOH A . 
Y  7 HOH   101 1001 416 HOH   HOH A . 
Y  7 HOH   102 1002 537 HOH   HOH A . 
Y  7 HOH   103 1003 268 HOH   HOH A . 
Y  7 HOH   104 1004 295 HOH   HOH A . 
Y  7 HOH   105 1005 502 HOH   HOH A . 
Y  7 HOH   106 1006 513 HOH   HOH A . 
Y  7 HOH   107 1007 171 HOH   HOH A . 
Y  7 HOH   108 1008 75  HOH   HOH A . 
Y  7 HOH   109 1009 186 HOH   HOH A . 
Y  7 HOH   110 1010 337 HOH   HOH A . 
Y  7 HOH   111 1011 145 HOH   HOH A . 
Y  7 HOH   112 1012 193 HOH   HOH A . 
Y  7 HOH   113 1013 536 HOH   HOH A . 
Y  7 HOH   114 1014 439 HOH   HOH A . 
Y  7 HOH   115 1015 125 HOH   HOH A . 
Y  7 HOH   116 1016 48  HOH   HOH A . 
Y  7 HOH   117 1017 532 HOH   HOH A . 
Y  7 HOH   118 1018 433 HOH   HOH A . 
Y  7 HOH   119 1019 52  HOH   HOH A . 
Y  7 HOH   120 1020 475 HOH   HOH A . 
Y  7 HOH   121 1021 534 HOH   HOH A . 
Y  7 HOH   122 1022 360 HOH   HOH A . 
Y  7 HOH   123 1023 265 HOH   HOH A . 
Y  7 HOH   124 1024 180 HOH   HOH A . 
Y  7 HOH   125 1025 385 HOH   HOH A . 
Y  7 HOH   126 1026 401 HOH   HOH A . 
Y  7 HOH   127 1027 175 HOH   HOH A . 
Y  7 HOH   128 1028 531 HOH   HOH A . 
Y  7 HOH   129 1029 398 HOH   HOH A . 
Y  7 HOH   130 1030 495 HOH   HOH A . 
Y  7 HOH   131 1031 447 HOH   HOH A . 
Y  7 HOH   132 1032 446 HOH   HOH A . 
Y  7 HOH   133 1033 244 HOH   HOH A . 
Y  7 HOH   134 1034 196 HOH   HOH A . 
Y  7 HOH   135 1035 477 HOH   HOH A . 
Y  7 HOH   136 1036 497 HOH   HOH A . 
Y  7 HOH   137 1037 444 HOH   HOH A . 
Y  7 HOH   138 1038 233 HOH   HOH A . 
Y  7 HOH   139 1039 264 HOH   HOH A . 
Y  7 HOH   140 1040 207 HOH   HOH A . 
Y  7 HOH   141 1041 517 HOH   HOH A . 
Y  7 HOH   142 1042 397 HOH   HOH A . 
Y  7 HOH   143 1043 134 HOH   HOH A . 
Y  7 HOH   144 1044 422 HOH   HOH A . 
Y  7 HOH   145 1045 445 HOH   HOH A . 
Y  7 HOH   146 1046 474 HOH   HOH A . 
Y  7 HOH   147 1047 428 HOH   HOH A . 
Y  7 HOH   148 1048 526 HOH   HOH A . 
Y  7 HOH   149 1049 491 HOH   HOH A . 
Y  7 HOH   150 1050 220 HOH   HOH A . 
Y  7 HOH   151 1051 512 HOH   HOH A . 
Y  7 HOH   152 1052 42  HOH   HOH A . 
Y  7 HOH   153 1053 237 HOH   HOH A . 
Y  7 HOH   154 1054 514 HOH   HOH A . 
Y  7 HOH   155 1055 221 HOH   HOH A . 
Y  7 HOH   156 1056 498 HOH   HOH A . 
Y  7 HOH   157 1057 411 HOH   HOH A . 
Y  7 HOH   158 1058 521 HOH   HOH A . 
Y  7 HOH   159 1059 506 HOH   HOH A . 
Y  7 HOH   160 1060 442 HOH   HOH A . 
Y  7 HOH   161 1061 256 HOH   HOH A . 
Y  7 HOH   162 1062 493 HOH   HOH A . 
Y  7 HOH   163 1063 299 HOH   HOH A . 
Y  7 HOH   164 1064 575 HOH   HOH A . 
Y  7 HOH   165 1065 448 HOH   HOH A . 
Y  7 HOH   166 1066 413 HOH   HOH A . 
Y  7 HOH   167 1067 602 HOH   HOH A . 
Y  7 HOH   168 1068 427 HOH   HOH A . 
Y  7 HOH   169 1069 496 HOH   HOH A . 
Y  7 HOH   170 1070 518 HOH   HOH A . 
Y  7 HOH   171 1071 533 HOH   HOH A . 
Y  7 HOH   172 1072 525 HOH   HOH A . 
Y  7 HOH   173 1073 394 HOH   HOH A . 
Y  7 HOH   174 1074 479 HOH   HOH A . 
Y  7 HOH   175 1075 604 HOH   HOH A . 
Y  7 HOH   176 1076 302 HOH   HOH A . 
Y  7 HOH   177 1077 399 HOH   HOH A . 
Y  7 HOH   178 1078 432 HOH   HOH A . 
Y  7 HOH   179 1079 424 HOH   HOH A . 
Y  7 HOH   180 1080 504 HOH   HOH A . 
Y  7 HOH   181 1081 500 HOH   HOH A . 
Y  7 HOH   182 1082 259 HOH   HOH A . 
Y  7 HOH   183 1083 505 HOH   HOH A . 
Y  7 HOH   184 1084 331 HOH   HOH A . 
Y  7 HOH   185 1085 523 HOH   HOH A . 
Y  7 HOH   186 1086 326 HOH   HOH A . 
Y  7 HOH   187 1087 488 HOH   HOH A . 
Y  7 HOH   188 1088 510 HOH   HOH A . 
Y  7 HOH   189 1089 499 HOH   HOH A . 
Y  7 HOH   190 1090 431 HOH   HOH A . 
Y  7 HOH   191 1091 419 HOH   HOH A . 
Z  7 HOH   1   901  34  HOH   HOH B . 
Z  7 HOH   2   902  485 HOH   HOH B . 
Z  7 HOH   3   903  3   HOH   HOH B . 
Z  7 HOH   4   904  5   HOH   HOH B . 
Z  7 HOH   5   905  555 HOH   HOH B . 
Z  7 HOH   6   906  560 HOH   HOH B . 
Z  7 HOH   7   907  481 HOH   HOH B . 
Z  7 HOH   8   908  260 HOH   HOH B . 
Z  7 HOH   9   909  352 HOH   HOH B . 
Z  7 HOH   10  910  8   HOH   HOH B . 
Z  7 HOH   11  911  637 HOH   HOH B . 
Z  7 HOH   12  912  365 HOH   HOH B . 
Z  7 HOH   13  913  396 HOH   HOH B . 
Z  7 HOH   14  914  351 HOH   HOH B . 
Z  7 HOH   15  915  172 HOH   HOH B . 
Z  7 HOH   16  916  93  HOH   HOH B . 
Z  7 HOH   17  917  567 HOH   HOH B . 
Z  7 HOH   18  918  86  HOH   HOH B . 
Z  7 HOH   19  919  209 HOH   HOH B . 
Z  7 HOH   20  920  123 HOH   HOH B . 
Z  7 HOH   21  921  454 HOH   HOH B . 
Z  7 HOH   22  922  336 HOH   HOH B . 
Z  7 HOH   23  923  64  HOH   HOH B . 
Z  7 HOH   24  924  165 HOH   HOH B . 
Z  7 HOH   25  925  35  HOH   HOH B . 
Z  7 HOH   26  926  55  HOH   HOH B . 
Z  7 HOH   27  927  482 HOH   HOH B . 
Z  7 HOH   28  928  76  HOH   HOH B . 
Z  7 HOH   29  929  188 HOH   HOH B . 
Z  7 HOH   30  930  12  HOH   HOH B . 
Z  7 HOH   31  931  204 HOH   HOH B . 
Z  7 HOH   32  932  110 HOH   HOH B . 
Z  7 HOH   33  933  15  HOH   HOH B . 
Z  7 HOH   34  934  374 HOH   HOH B . 
Z  7 HOH   35  935  166 HOH   HOH B . 
Z  7 HOH   36  936  543 HOH   HOH B . 
Z  7 HOH   37  937  231 HOH   HOH B . 
Z  7 HOH   38  938  191 HOH   HOH B . 
Z  7 HOH   39  939  198 HOH   HOH B . 
Z  7 HOH   40  940  61  HOH   HOH B . 
Z  7 HOH   41  941  129 HOH   HOH B . 
Z  7 HOH   42  942  353 HOH   HOH B . 
Z  7 HOH   43  943  50  HOH   HOH B . 
Z  7 HOH   44  944  140 HOH   HOH B . 
Z  7 HOH   45  945  257 HOH   HOH B . 
Z  7 HOH   46  946  476 HOH   HOH B . 
Z  7 HOH   47  947  320 HOH   HOH B . 
Z  7 HOH   48  948  117 HOH   HOH B . 
Z  7 HOH   49  949  111 HOH   HOH B . 
Z  7 HOH   50  950  164 HOH   HOH B . 
Z  7 HOH   51  951  285 HOH   HOH B . 
Z  7 HOH   52  952  389 HOH   HOH B . 
Z  7 HOH   53  953  373 HOH   HOH B . 
Z  7 HOH   54  954  246 HOH   HOH B . 
Z  7 HOH   55  955  355 HOH   HOH B . 
Z  7 HOH   56  956  294 HOH   HOH B . 
Z  7 HOH   57  957  118 HOH   HOH B . 
Z  7 HOH   58  958  455 HOH   HOH B . 
Z  7 HOH   59  959  262 HOH   HOH B . 
Z  7 HOH   60  960  108 HOH   HOH B . 
Z  7 HOH   61  961  317 HOH   HOH B . 
Z  7 HOH   62  962  215 HOH   HOH B . 
Z  7 HOH   63  963  59  HOH   HOH B . 
Z  7 HOH   64  964  571 HOH   HOH B . 
Z  7 HOH   65  965  92  HOH   HOH B . 
Z  7 HOH   66  966  354 HOH   HOH B . 
Z  7 HOH   67  967  78  HOH   HOH B . 
Z  7 HOH   68  968  564 HOH   HOH B . 
Z  7 HOH   69  969  380 HOH   HOH B . 
Z  7 HOH   70  970  345 HOH   HOH B . 
Z  7 HOH   71  971  558 HOH   HOH B . 
Z  7 HOH   72  972  44  HOH   HOH B . 
Z  7 HOH   73  973  541 HOH   HOH B . 
Z  7 HOH   74  974  450 HOH   HOH B . 
Z  7 HOH   75  975  46  HOH   HOH B . 
Z  7 HOH   76  976  200 HOH   HOH B . 
Z  7 HOH   77  977  310 HOH   HOH B . 
Z  7 HOH   78  978  36  HOH   HOH B . 
Z  7 HOH   79  979  335 HOH   HOH B . 
Z  7 HOH   80  980  559 HOH   HOH B . 
Z  7 HOH   81  981  141 HOH   HOH B . 
Z  7 HOH   82  982  561 HOH   HOH B . 
Z  7 HOH   83  983  218 HOH   HOH B . 
Z  7 HOH   84  984  529 HOH   HOH B . 
Z  7 HOH   85  985  305 HOH   HOH B . 
Z  7 HOH   86  986  174 HOH   HOH B . 
Z  7 HOH   87  987  214 HOH   HOH B . 
Z  7 HOH   88  988  243 HOH   HOH B . 
Z  7 HOH   89  989  282 HOH   HOH B . 
Z  7 HOH   90  990  313 HOH   HOH B . 
Z  7 HOH   91  991  550 HOH   HOH B . 
Z  7 HOH   92  992  85  HOH   HOH B . 
Z  7 HOH   93  993  556 HOH   HOH B . 
Z  7 HOH   94  994  199 HOH   HOH B . 
Z  7 HOH   95  995  566 HOH   HOH B . 
Z  7 HOH   96  996  290 HOH   HOH B . 
Z  7 HOH   97  997  330 HOH   HOH B . 
Z  7 HOH   98  998  552 HOH   HOH B . 
Z  7 HOH   99  999  227 HOH   HOH B . 
Z  7 HOH   100 1000 119 HOH   HOH B . 
Z  7 HOH   101 1001 263 HOH   HOH B . 
Z  7 HOH   102 1002 570 HOH   HOH B . 
Z  7 HOH   103 1003 568 HOH   HOH B . 
Z  7 HOH   104 1004 456 HOH   HOH B . 
Z  7 HOH   105 1005 325 HOH   HOH B . 
Z  7 HOH   106 1006 301 HOH   HOH B . 
Z  7 HOH   107 1007 332 HOH   HOH B . 
Z  7 HOH   108 1008 366 HOH   HOH B . 
Z  7 HOH   109 1009 551 HOH   HOH B . 
Z  7 HOH   110 1010 535 HOH   HOH B . 
Z  7 HOH   111 1011 113 HOH   HOH B . 
Z  7 HOH   112 1012 381 HOH   HOH B . 
Z  7 HOH   113 1013 458 HOH   HOH B . 
Z  7 HOH   114 1014 549 HOH   HOH B . 
Z  7 HOH   115 1015 457 HOH   HOH B . 
Z  7 HOH   116 1016 324 HOH   HOH B . 
Z  7 HOH   117 1017 539 HOH   HOH B . 
Z  7 HOH   118 1018 296 HOH   HOH B . 
Z  7 HOH   119 1019 563 HOH   HOH B . 
Z  7 HOH   120 1020 390 HOH   HOH B . 
Z  7 HOH   121 1021 451 HOH   HOH B . 
Z  7 HOH   122 1022 293 HOH   HOH B . 
Z  7 HOH   123 1023 565 HOH   HOH B . 
Z  7 HOH   124 1024 569 HOH   HOH B . 
Z  7 HOH   125 1025 270 HOH   HOH B . 
Z  7 HOH   126 1026 160 HOH   HOH B . 
Z  7 HOH   127 1027 540 HOH   HOH B . 
Z  7 HOH   128 1028 542 HOH   HOH B . 
Z  7 HOH   129 1029 573 HOH   HOH B . 
Z  7 HOH   130 1030 553 HOH   HOH B . 
Z  7 HOH   131 1031 245 HOH   HOH B . 
Z  7 HOH   132 1032 528 HOH   HOH B . 
Z  7 HOH   133 1033 453 HOH   HOH B . 
Z  7 HOH   134 1034 452 HOH   HOH B . 
Z  7 HOH   135 1035 547 HOH   HOH B . 
Z  7 HOH   136 1036 319 HOH   HOH B . 
Z  7 HOH   137 1037 546 HOH   HOH B . 
Z  7 HOH   138 1038 487 HOH   HOH B . 
Z  7 HOH   139 1039 557 HOH   HOH B . 
Z  7 HOH   140 1040 544 HOH   HOH B . 
Z  7 HOH   141 1041 545 HOH   HOH B . 
Z  7 HOH   142 1042 554 HOH   HOH B . 
Z  7 HOH   143 1043 480 HOH   HOH B . 
Z  7 HOH   144 1044 304 HOH   HOH B . 
Z  7 HOH   145 1045 562 HOH   HOH B . 
Z  7 HOH   146 1046 574 HOH   HOH B . 
Z  7 HOH   147 1047 418 HOH   HOH B . 
Z  7 HOH   148 1048 548 HOH   HOH B . 
Z  7 HOH   149 1049 572 HOH   HOH B . 
Z  7 HOH   150 1050 338 HOH   HOH B . 
Z  7 HOH   151 1051 486 HOH   HOH B . 
Z  7 HOH   152 1052 440 HOH   HOH B . 
AA 7 HOH   1   901  592 HOH   HOH C . 
AA 7 HOH   2   902  630 HOH   HOH C . 
AA 7 HOH   3   903  625 HOH   HOH C . 
AA 7 HOH   4   904  612 HOH   HOH C . 
AA 7 HOH   5   905  38  HOH   HOH C . 
AA 7 HOH   6   906  1   HOH   HOH C . 
AA 7 HOH   7   907  9   HOH   HOH C . 
AA 7 HOH   8   908  10  HOH   HOH C . 
AA 7 HOH   9   909  584 HOH   HOH C . 
AA 7 HOH   10  910  621 HOH   HOH C . 
AA 7 HOH   11  911  144 HOH   HOH C . 
AA 7 HOH   12  912  600 HOH   HOH C . 
AA 7 HOH   13  913  599 HOH   HOH C . 
AA 7 HOH   14  914  348 HOH   HOH C . 
AA 7 HOH   15  915  16  HOH   HOH C . 
AA 7 HOH   16  916  98  HOH   HOH C . 
AA 7 HOH   17  917  287 HOH   HOH C . 
AA 7 HOH   18  918  467 HOH   HOH C . 
AA 7 HOH   19  919  223 HOH   HOH C . 
AA 7 HOH   20  920  27  HOH   HOH C . 
AA 7 HOH   21  921  18  HOH   HOH C . 
AA 7 HOH   22  922  127 HOH   HOH C . 
AA 7 HOH   23  923  347 HOH   HOH C . 
AA 7 HOH   24  924  149 HOH   HOH C . 
AA 7 HOH   25  925  157 HOH   HOH C . 
AA 7 HOH   26  926  405 HOH   HOH C . 
AA 7 HOH   27  927  87  HOH   HOH C . 
AA 7 HOH   28  928  615 HOH   HOH C . 
AA 7 HOH   29  929  577 HOH   HOH C . 
AA 7 HOH   30  930  334 HOH   HOH C . 
AA 7 HOH   31  931  176 HOH   HOH C . 
AA 7 HOH   32  932  251 HOH   HOH C . 
AA 7 HOH   33  933  471 HOH   HOH C . 
AA 7 HOH   34  934  66  HOH   HOH C . 
AA 7 HOH   35  935  70  HOH   HOH C . 
AA 7 HOH   36  936  25  HOH   HOH C . 
AA 7 HOH   37  937  624 HOH   HOH C . 
AA 7 HOH   38  938  30  HOH   HOH C . 
AA 7 HOH   39  939  403 HOH   HOH C . 
AA 7 HOH   40  940  156 HOH   HOH C . 
AA 7 HOH   41  941  21  HOH   HOH C . 
AA 7 HOH   42  942  101 HOH   HOH C . 
AA 7 HOH   43  943  169 HOH   HOH C . 
AA 7 HOH   44  944  212 HOH   HOH C . 
AA 7 HOH   45  945  23  HOH   HOH C . 
AA 7 HOH   46  946  314 HOH   HOH C . 
AA 7 HOH   47  947  208 HOH   HOH C . 
AA 7 HOH   48  948  586 HOH   HOH C . 
AA 7 HOH   49  949  82  HOH   HOH C . 
AA 7 HOH   50  950  31  HOH   HOH C . 
AA 7 HOH   51  951  362 HOH   HOH C . 
AA 7 HOH   52  952  37  HOH   HOH C . 
AA 7 HOH   53  953  628 HOH   HOH C . 
AA 7 HOH   54  954  158 HOH   HOH C . 
AA 7 HOH   55  955  619 HOH   HOH C . 
AA 7 HOH   56  956  177 HOH   HOH C . 
AA 7 HOH   57  957  379 HOH   HOH C . 
AA 7 HOH   58  958  213 HOH   HOH C . 
AA 7 HOH   59  959  400 HOH   HOH C . 
AA 7 HOH   60  960  40  HOH   HOH C . 
AA 7 HOH   61  961  115 HOH   HOH C . 
AA 7 HOH   62  962  124 HOH   HOH C . 
AA 7 HOH   63  963  601 HOH   HOH C . 
AA 7 HOH   64  964  623 HOH   HOH C . 
AA 7 HOH   65  965  138 HOH   HOH C . 
AA 7 HOH   66  966  226 HOH   HOH C . 
AA 7 HOH   67  967  62  HOH   HOH C . 
AA 7 HOH   68  968  420 HOH   HOH C . 
AA 7 HOH   69  969  131 HOH   HOH C . 
AA 7 HOH   70  970  610 HOH   HOH C . 
AA 7 HOH   71  971  247 HOH   HOH C . 
AA 7 HOH   72  972  183 HOH   HOH C . 
AA 7 HOH   73  973  328 HOH   HOH C . 
AA 7 HOH   74  974  614 HOH   HOH C . 
AA 7 HOH   75  975  607 HOH   HOH C . 
AA 7 HOH   76  976  273 HOH   HOH C . 
AA 7 HOH   77  977  620 HOH   HOH C . 
AA 7 HOH   78  978  315 HOH   HOH C . 
AA 7 HOH   79  979  41  HOH   HOH C . 
AA 7 HOH   80  980  80  HOH   HOH C . 
AA 7 HOH   81  981  580 HOH   HOH C . 
AA 7 HOH   82  982  14  HOH   HOH C . 
AA 7 HOH   83  983  393 HOH   HOH C . 
AA 7 HOH   84  984  248 HOH   HOH C . 
AA 7 HOH   85  985  278 HOH   HOH C . 
AA 7 HOH   86  986  254 HOH   HOH C . 
AA 7 HOH   87  987  240 HOH   HOH C . 
AA 7 HOH   88  988  595 HOH   HOH C . 
AA 7 HOH   89  989  622 HOH   HOH C . 
AA 7 HOH   90  990  133 HOH   HOH C . 
AA 7 HOH   91  991  609 HOH   HOH C . 
AA 7 HOH   92  992  56  HOH   HOH C . 
AA 7 HOH   93  993  95  HOH   HOH C . 
AA 7 HOH   94  994  255 HOH   HOH C . 
AA 7 HOH   95  995  426 HOH   HOH C . 
AA 7 HOH   96  996  392 HOH   HOH C . 
AA 7 HOH   97  997  579 HOH   HOH C . 
AA 7 HOH   98  998  284 HOH   HOH C . 
AA 7 HOH   99  999  429 HOH   HOH C . 
AA 7 HOH   100 1000 593 HOH   HOH C . 
AA 7 HOH   101 1001 269 HOH   HOH C . 
AA 7 HOH   102 1002 591 HOH   HOH C . 
AA 7 HOH   103 1003 311 HOH   HOH C . 
AA 7 HOH   104 1004 192 HOH   HOH C . 
AA 7 HOH   105 1005 356 HOH   HOH C . 
AA 7 HOH   106 1006 182 HOH   HOH C . 
AA 7 HOH   107 1007 197 HOH   HOH C . 
AA 7 HOH   108 1008 407 HOH   HOH C . 
AA 7 HOH   109 1009 617 HOH   HOH C . 
AA 7 HOH   110 1010 303 HOH   HOH C . 
AA 7 HOH   111 1011 406 HOH   HOH C . 
AA 7 HOH   112 1012 239 HOH   HOH C . 
AA 7 HOH   113 1013 594 HOH   HOH C . 
AA 7 HOH   114 1014 377 HOH   HOH C . 
AA 7 HOH   115 1015 126 HOH   HOH C . 
AA 7 HOH   116 1016 312 HOH   HOH C . 
AA 7 HOH   117 1017 230 HOH   HOH C . 
AA 7 HOH   118 1018 382 HOH   HOH C . 
AA 7 HOH   119 1019 596 HOH   HOH C . 
AA 7 HOH   120 1020 359 HOH   HOH C . 
AA 7 HOH   121 1021 388 HOH   HOH C . 
AA 7 HOH   122 1022 668 HOH   HOH C . 
AA 7 HOH   123 1023 626 HOH   HOH C . 
AA 7 HOH   124 1024 603 HOH   HOH C . 
AA 7 HOH   125 1025 128 HOH   HOH C . 
AA 7 HOH   126 1026 190 HOH   HOH C . 
AA 7 HOH   127 1027 597 HOH   HOH C . 
AA 7 HOH   128 1028 421 HOH   HOH C . 
AA 7 HOH   129 1029 576 HOH   HOH C . 
AA 7 HOH   130 1030 589 HOH   HOH C . 
AA 7 HOH   131 1031 618 HOH   HOH C . 
AA 7 HOH   132 1032 608 HOH   HOH C . 
AA 7 HOH   133 1033 468 HOH   HOH C . 
AA 7 HOH   134 1034 181 HOH   HOH C . 
AA 7 HOH   135 1035 578 HOH   HOH C . 
AA 7 HOH   136 1036 470 HOH   HOH C . 
AA 7 HOH   137 1037 631 HOH   HOH C . 
AA 7 HOH   138 1038 469 HOH   HOH C . 
AA 7 HOH   139 1039 441 HOH   HOH C . 
AA 7 HOH   140 1040 670 HOH   HOH C . 
AA 7 HOH   141 1041 581 HOH   HOH C . 
AA 7 HOH   142 1042 100 HOH   HOH C . 
AA 7 HOH   143 1043 611 HOH   HOH C . 
AA 7 HOH   144 1044 590 HOH   HOH C . 
AA 7 HOH   145 1045 472 HOH   HOH C . 
AA 7 HOH   146 1046 391 HOH   HOH C . 
AA 7 HOH   147 1047 232 HOH   HOH C . 
AA 7 HOH   148 1048 587 HOH   HOH C . 
AA 7 HOH   149 1049 292 HOH   HOH C . 
AA 7 HOH   150 1050 588 HOH   HOH C . 
AA 7 HOH   151 1051 274 HOH   HOH C . 
AA 7 HOH   152 1052 598 HOH   HOH C . 
AA 7 HOH   153 1053 308 HOH   HOH C . 
AA 7 HOH   154 1054 606 HOH   HOH C . 
AA 7 HOH   155 1055 627 HOH   HOH C . 
AA 7 HOH   156 1056 582 HOH   HOH C . 
AA 7 HOH   157 1057 616 HOH   HOH C . 
AA 7 HOH   158 1058 370 HOH   HOH C . 
AA 7 HOH   159 1059 613 HOH   HOH C . 
AA 7 HOH   160 1060 376 HOH   HOH C . 
AA 7 HOH   161 1061 210 HOH   HOH C . 
AA 7 HOH   162 1062 605 HOH   HOH C . 
BA 7 HOH   1   901  466 HOH   HOH D . 
BA 7 HOH   2   902  664 HOH   HOH D . 
BA 7 HOH   3   903  349 HOH   HOH D . 
BA 7 HOH   4   904  660 HOH   HOH D . 
BA 7 HOH   5   905  640 HOH   HOH D . 
BA 7 HOH   6   906  662 HOH   HOH D . 
BA 7 HOH   7   907  461 HOH   HOH D . 
BA 7 HOH   8   908  195 HOH   HOH D . 
BA 7 HOH   9   909  121 HOH   HOH D . 
BA 7 HOH   10  910  49  HOH   HOH D . 
BA 7 HOH   11  911  459 HOH   HOH D . 
BA 7 HOH   12  912  665 HOH   HOH D . 
BA 7 HOH   13  913  24  HOH   HOH D . 
BA 7 HOH   14  914  235 HOH   HOH D . 
BA 7 HOH   15  915  647 HOH   HOH D . 
BA 7 HOH   16  916  6   HOH   HOH D . 
BA 7 HOH   17  917  463 HOH   HOH D . 
BA 7 HOH   18  918  272 HOH   HOH D . 
BA 7 HOH   19  919  105 HOH   HOH D . 
BA 7 HOH   20  920  363 HOH   HOH D . 
BA 7 HOH   21  921  367 HOH   HOH D . 
BA 7 HOH   22  922  656 HOH   HOH D . 
BA 7 HOH   23  923  464 HOH   HOH D . 
BA 7 HOH   24  924  583 HOH   HOH D . 
BA 7 HOH   25  925  54  HOH   HOH D . 
BA 7 HOH   26  926  65  HOH   HOH D . 
BA 7 HOH   27  927  63  HOH   HOH D . 
BA 7 HOH   28  928  378 HOH   HOH D . 
BA 7 HOH   29  929  167 HOH   HOH D . 
BA 7 HOH   30  930  161 HOH   HOH D . 
BA 7 HOH   31  931  652 HOH   HOH D . 
BA 7 HOH   32  932  107 HOH   HOH D . 
BA 7 HOH   33  933  346 HOH   HOH D . 
BA 7 HOH   34  934  648 HOH   HOH D . 
BA 7 HOH   35  935  2   HOH   HOH D . 
BA 7 HOH   36  936  341 HOH   HOH D . 
BA 7 HOH   37  937  13  HOH   HOH D . 
BA 7 HOH   38  938  106 HOH   HOH D . 
BA 7 HOH   39  939  11  HOH   HOH D . 
BA 7 HOH   40  940  19  HOH   HOH D . 
BA 7 HOH   41  941  96  HOH   HOH D . 
BA 7 HOH   42  942  77  HOH   HOH D . 
BA 7 HOH   43  943  22  HOH   HOH D . 
BA 7 HOH   44  944  659 HOH   HOH D . 
BA 7 HOH   45  945  47  HOH   HOH D . 
BA 7 HOH   46  946  71  HOH   HOH D . 
BA 7 HOH   47  947  69  HOH   HOH D . 
BA 7 HOH   48  948  661 HOH   HOH D . 
BA 7 HOH   49  949  17  HOH   HOH D . 
BA 7 HOH   50  950  146 HOH   HOH D . 
BA 7 HOH   51  951  437 HOH   HOH D . 
BA 7 HOH   52  952  68  HOH   HOH D . 
BA 7 HOH   53  953  298 HOH   HOH D . 
BA 7 HOH   54  954  203 HOH   HOH D . 
BA 7 HOH   55  955  649 HOH   HOH D . 
BA 7 HOH   56  956  387 HOH   HOH D . 
BA 7 HOH   57  957  189 HOH   HOH D . 
BA 7 HOH   58  958  309 HOH   HOH D . 
BA 7 HOH   59  959  185 HOH   HOH D . 
BA 7 HOH   60  960  67  HOH   HOH D . 
BA 7 HOH   61  961  168 HOH   HOH D . 
BA 7 HOH   62  962  288 HOH   HOH D . 
BA 7 HOH   63  963  132 HOH   HOH D . 
BA 7 HOH   64  964  136 HOH   HOH D . 
BA 7 HOH   65  965  238 HOH   HOH D . 
BA 7 HOH   66  966  634 HOH   HOH D . 
BA 7 HOH   67  967  242 HOH   HOH D . 
BA 7 HOH   68  968  275 HOH   HOH D . 
BA 7 HOH   69  969  89  HOH   HOH D . 
BA 7 HOH   70  970  20  HOH   HOH D . 
BA 7 HOH   71  971  79  HOH   HOH D . 
BA 7 HOH   72  972  641 HOH   HOH D . 
BA 7 HOH   73  973  102 HOH   HOH D . 
BA 7 HOH   74  974  229 HOH   HOH D . 
BA 7 HOH   75  975  261 HOH   HOH D . 
BA 7 HOH   76  976  73  HOH   HOH D . 
BA 7 HOH   77  977  90  HOH   HOH D . 
BA 7 HOH   78  978  137 HOH   HOH D . 
BA 7 HOH   79  979  430 HOH   HOH D . 
BA 7 HOH   80  980  252 HOH   HOH D . 
BA 7 HOH   81  981  650 HOH   HOH D . 
BA 7 HOH   82  982  250 HOH   HOH D . 
BA 7 HOH   83  983  122 HOH   HOH D . 
BA 7 HOH   84  984  281 HOH   HOH D . 
BA 7 HOH   85  985  404 HOH   HOH D . 
BA 7 HOH   86  986  143 HOH   HOH D . 
BA 7 HOH   87  987  669 HOH   HOH D . 
BA 7 HOH   88  988  316 HOH   HOH D . 
BA 7 HOH   89  989  43  HOH   HOH D . 
BA 7 HOH   90  990  74  HOH   HOH D . 
BA 7 HOH   91  991  423 HOH   HOH D . 
BA 7 HOH   92  992  217 HOH   HOH D . 
BA 7 HOH   93  993  409 HOH   HOH D . 
BA 7 HOH   94  994  318 HOH   HOH D . 
BA 7 HOH   95  995  206 HOH   HOH D . 
BA 7 HOH   96  996  45  HOH   HOH D . 
BA 7 HOH   97  997  436 HOH   HOH D . 
BA 7 HOH   98  998  323 HOH   HOH D . 
BA 7 HOH   99  999  201 HOH   HOH D . 
BA 7 HOH   100 1000 241 HOH   HOH D . 
BA 7 HOH   101 1001 395 HOH   HOH D . 
BA 7 HOH   102 1002 306 HOH   HOH D . 
BA 7 HOH   103 1003 91  HOH   HOH D . 
BA 7 HOH   104 1004 639 HOH   HOH D . 
BA 7 HOH   105 1005 205 HOH   HOH D . 
BA 7 HOH   106 1006 629 HOH   HOH D . 
BA 7 HOH   107 1007 383 HOH   HOH D . 
BA 7 HOH   108 1008 357 HOH   HOH D . 
BA 7 HOH   109 1009 83  HOH   HOH D . 
BA 7 HOH   110 1010 322 HOH   HOH D . 
BA 7 HOH   111 1011 658 HOH   HOH D . 
BA 7 HOH   112 1012 465 HOH   HOH D . 
BA 7 HOH   113 1013 371 HOH   HOH D . 
BA 7 HOH   114 1014 112 HOH   HOH D . 
BA 7 HOH   115 1015 228 HOH   HOH D . 
BA 7 HOH   116 1016 435 HOH   HOH D . 
BA 7 HOH   117 1017 438 HOH   HOH D . 
BA 7 HOH   118 1018 654 HOH   HOH D . 
BA 7 HOH   119 1019 297 HOH   HOH D . 
BA 7 HOH   120 1020 425 HOH   HOH D . 
BA 7 HOH   121 1021 72  HOH   HOH D . 
BA 7 HOH   122 1022 249 HOH   HOH D . 
BA 7 HOH   123 1023 307 HOH   HOH D . 
BA 7 HOH   124 1024 645 HOH   HOH D . 
BA 7 HOH   125 1025 153 HOH   HOH D . 
BA 7 HOH   126 1026 342 HOH   HOH D . 
BA 7 HOH   127 1027 253 HOH   HOH D . 
BA 7 HOH   128 1028 642 HOH   HOH D . 
BA 7 HOH   129 1029 224 HOH   HOH D . 
BA 7 HOH   130 1030 635 HOH   HOH D . 
BA 7 HOH   131 1031 120 HOH   HOH D . 
BA 7 HOH   132 1032 276 HOH   HOH D . 
BA 7 HOH   133 1033 585 HOH   HOH D . 
BA 7 HOH   134 1034 644 HOH   HOH D . 
BA 7 HOH   135 1035 667 HOH   HOH D . 
BA 7 HOH   136 1036 150 HOH   HOH D . 
BA 7 HOH   137 1037 653 HOH   HOH D . 
BA 7 HOH   138 1038 663 HOH   HOH D . 
BA 7 HOH   139 1039 162 HOH   HOH D . 
BA 7 HOH   140 1040 657 HOH   HOH D . 
BA 7 HOH   141 1041 219 HOH   HOH D . 
BA 7 HOH   142 1042 333 HOH   HOH D . 
BA 7 HOH   143 1043 372 HOH   HOH D . 
BA 7 HOH   144 1044 364 HOH   HOH D . 
BA 7 HOH   145 1045 638 HOH   HOH D . 
BA 7 HOH   146 1046 462 HOH   HOH D . 
BA 7 HOH   147 1047 636 HOH   HOH D . 
BA 7 HOH   148 1048 417 HOH   HOH D . 
BA 7 HOH   149 1049 375 HOH   HOH D . 
BA 7 HOH   150 1050 643 HOH   HOH D . 
BA 7 HOH   151 1051 135 HOH   HOH D . 
BA 7 HOH   152 1052 632 HOH   HOH D . 
BA 7 HOH   153 1053 225 HOH   HOH D . 
BA 7 HOH   154 1054 655 HOH   HOH D . 
BA 7 HOH   155 1055 410 HOH   HOH D . 
BA 7 HOH   156 1056 666 HOH   HOH D . 
BA 7 HOH   157 1057 646 HOH   HOH D . 
BA 7 HOH   158 1058 300 HOH   HOH D . 
BA 7 HOH   159 1059 434 HOH   HOH D . 
BA 7 HOH   160 1060 460 HOH   HOH D . 
BA 7 HOH   161 1061 651 HOH   HOH D . 
BA 7 HOH   162 1062 279 HOH   HOH D . 
BA 7 HOH   163 1063 402 HOH   HOH D . 
BA 7 HOH   164 1064 408 HOH   HOH D . 
BA 7 HOH   165 1065 633 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 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CW3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.462 
_cell.length_a_esd                 ? 
_cell.length_b                     52.052 
_cell.length_b_esd                 ? 
_cell.length_c                     164.763 
_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                         9CW3 
_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                   9CW3 
_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             2.74 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CW3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.19 
_reflns.d_resolution_low                               49.63 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     104426 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.585 
_reflns.pdbx_Rpim_I_all                                0.181 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1069191 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.985 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.556 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.19 
_reflns_shell.d_res_low                                     2.23 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           38235 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5066 
_reflns_shell.percent_possible_obs                          98.8 
_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                               7.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.5 
_reflns_shell.pdbx_Rrim_I_all                               9.814 
_reflns_shell.pdbx_Rpim_I_all                               3.292 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.205 
_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                                  9.221 
_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                                 9CW3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.190 
_refine.ls_d_res_low                             49.63 
_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                     104300 
_refine.ls_number_reflns_R_free                  10122 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1961 
_refine.ls_R_factor_R_free                       0.2510 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1932 
_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                          0.01 
_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                 31.12 
_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                            0.34 
_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        13571 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         378 
_refine_hist.number_atoms_solvent             670 
_refine_hist.number_atoms_total               14619 
_refine_hist.d_res_high                       2.190 
_refine_hist.d_res_low                        49.63 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 14420 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.952  ? 19635 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.300 ? 8421  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 2025  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 2477  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.1901 2.2149 . . 353 6237 98.00  . . . . 0.3175 . . . . . . . . . . . 0.3683 
'X-RAY DIFFRACTION' 2.2149 2.2410 . . 329 6430 100.00 . . . . 0.3266 . . . . . . . . . . . 0.3974 
'X-RAY DIFFRACTION' 2.2410 2.2683 . . 342 6443 100.00 . . . . 0.3659 . . . . . . . . . . . 0.4415 
'X-RAY DIFFRACTION' 2.2683 2.2970 . . 312 6277 100.00 . . . . 0.3162 . . . . . . . . . . . 0.3684 
'X-RAY DIFFRACTION' 2.2970 2.3273 . . 329 6568 100.00 . . . . 0.3095 . . . . . . . . . . . 0.3541 
'X-RAY DIFFRACTION' 2.3273 2.3592 . . 366 6344 100.00 . . . . 0.3044 . . . . . . . . . . . 0.3658 
'X-RAY DIFFRACTION' 2.3592 2.3929 . . 315 6391 100.00 . . . . 0.2933 . . . . . . . . . . . 0.3736 
'X-RAY DIFFRACTION' 2.3929 2.4286 . . 362 6308 100.00 . . . . 0.2868 . . . . . . . . . . . 0.3300 
'X-RAY DIFFRACTION' 2.4286 2.4665 . . 332 6550 100.00 . . . . 0.3036 . . . . . . . . . . . 0.3943 
'X-RAY DIFFRACTION' 2.4665 2.5070 . . 357 6302 100.00 . . . . 0.2801 . . . . . . . . . . . 0.3248 
'X-RAY DIFFRACTION' 2.5070 2.5502 . . 348 6373 100.00 . . . . 0.2674 . . . . . . . . . . . 0.2970 
'X-RAY DIFFRACTION' 2.5502 2.5966 . . 346 6452 100.00 . . . . 0.2550 . . . . . . . . . . . 0.3028 
'X-RAY DIFFRACTION' 2.5966 2.6465 . . 365 6298 100.00 . . . . 0.2520 . . . . . . . . . . . 0.3047 
'X-RAY DIFFRACTION' 2.6465 2.7005 . . 348 6413 100.00 . . . . 0.2594 . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 2.7005 2.7592 . . 338 6499 100.00 . . . . 0.2638 . . . . . . . . . . . 0.3322 
'X-RAY DIFFRACTION' 2.7592 2.8234 . . 281 6404 100.00 . . . . 0.2406 . . . . . . . . . . . 0.3208 
'X-RAY DIFFRACTION' 2.8234 2.8940 . . 291 6502 100.00 . . . . 0.2314 . . . . . . . . . . . 0.2968 
'X-RAY DIFFRACTION' 2.8940 2.9722 . . 372 6265 100.00 . . . . 0.2276 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 2.9722 3.0597 . . 318 6507 100.00 . . . . 0.2241 . . . . . . . . . . . 0.3108 
'X-RAY DIFFRACTION' 3.0597 3.1584 . . 326 6381 100.00 . . . . 0.2164 . . . . . . . . . . . 0.2974 
'X-RAY DIFFRACTION' 3.1584 3.2713 . . 340 6435 100.00 . . . . 0.2076 . . . . . . . . . . . 0.2687 
'X-RAY DIFFRACTION' 3.2713 3.4022 . . 335 6349 100.00 . . . . 0.1805 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 3.4022 3.5570 . . 341 6424 100.00 . . . . 0.1711 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 3.5570 3.7445 . . 343 6472 100.00 . . . . 0.1600 . . . . . . . . . . . 0.2274 
'X-RAY DIFFRACTION' 3.7445 3.9790 . . 364 6354 100.00 . . . . 0.1496 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 3.9790 4.2861 . . 305 6430 100.00 . . . . 0.1313 . . . . . . . . . . . 0.1662 
'X-RAY DIFFRACTION' 4.2861 4.7171 . . 299 6461 100.00 . . . . 0.1255 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 4.7171 5.3990 . . 403 6343 100.00 . . . . 0.1307 . . . . . . . . . . . 0.1755 
'X-RAY DIFFRACTION' 5.3990 6.7994 . . 326 6419 100.00 . . . . 0.1534 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 6.7994 49.63  . . 336 6403 100.00 . . . . 0.1483 . . . . . . . . . . . 0.2068 
# 
_struct.entry_id                     9CW3 
_struct.title                        
;Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain bound with 6-(5-((4,4-difluoropiperidin-1-yl)methyl)-2,3-difluorophenyl)-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        9CW3 
_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 5 ? 
J  N N 6 ? 
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 9CW3 A 1 ? 421 ? P29475 302 ? 722 ? 302 722 
2 1 9CW3 B 1 ? 421 ? P29475 302 ? 722 ? 302 722 
3 1 9CW3 C 1 ? 421 ? P29475 302 ? 722 ? 302 722 
4 1 9CW3 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 9CW3 ALA A 53  ? UNP P29475 ARG 354 'engineered mutation' 354 1  
1 9CW3 ASP A 56  ? UNP P29475 GLY 357 'engineered mutation' 357 2  
1 9CW3 LEU A 422 ? UNP P29475 ?   ?   'expression tag'      723 3  
1 9CW3 VAL A 423 ? UNP P29475 ?   ?   'expression tag'      724 4  
2 9CW3 ALA B 53  ? UNP P29475 ARG 354 'engineered mutation' 354 5  
2 9CW3 ASP B 56  ? UNP P29475 GLY 357 'engineered mutation' 357 6  
2 9CW3 LEU B 422 ? UNP P29475 ?   ?   'expression tag'      723 7  
2 9CW3 VAL B 423 ? UNP P29475 ?   ?   'expression tag'      724 8  
3 9CW3 ALA C 53  ? UNP P29475 ARG 354 'engineered mutation' 354 9  
3 9CW3 ASP C 56  ? UNP P29475 GLY 357 'engineered mutation' 357 10 
3 9CW3 LEU C 422 ? UNP P29475 ?   ?   'expression tag'      723 11 
3 9CW3 VAL C 423 ? UNP P29475 ?   ?   'expression tag'      724 12 
4 9CW3 ALA D 53  ? UNP P29475 ARG 354 'engineered mutation' 354 13 
4 9CW3 ASP D 56  ? UNP P29475 GLY 357 'engineered mutation' 357 14 
4 9CW3 LEU D 422 ? UNP P29475 ?   ?   'expression tag'      723 15 
4 9CW3 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)' 9970  ? 
1 MORE         -84   ? 
1 'SSA (A^2)'  33970 ? 
2 'ABSA (A^2)' 9960  ? 
2 MORE         -82   ? 
2 'SSA (A^2)'  34220 ? 
# 
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 ? ASN A 319 ? ILE A 611 ASN A 620 1 ? 10 
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 ? THR A 417 ? ASP A 714 THR A 718 5 ? 5  
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 211 ? ASN B 503 GLN B 512 1 ? 10 
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 258 ? GLY B 262 ? PHE B 559 GLY B 563 5 ? 5  
HELX_P HELX_P30 AD3 MET B 293 ? VAL B 299 ? MET B 594 VAL B 600 1 ? 7  
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 ? ASN B 319 ? ILE B 611 ASN B 620 1 ? 10 
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 ? THR B 392 ? SER B 689 THR B 693 5 ? 5  
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 ? ASN C 319 ? ILE C 611 ASN C 620 1 ? 10 
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 ? THR C 417 ? ASP C 714 THR C 718 5 ? 5  
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 J ZN  .  ZN ? ? A CYS 331 B ZN  801 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc2  metalc ? ? A CYS 35  SG ? ? ? 1_555 J ZN  .  ZN ? ? A CYS 336 B ZN  801 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc3  metalc ? ? A CYS 119 SG ? ? ? 1_555 E HEM .  FE ? ? A CYS 420 A HEM 801 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc4  metalc ? ? B CYS 30  SG ? ? ? 1_555 J ZN  .  ZN ? ? B CYS 331 B ZN  801 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc5  metalc ? ? B CYS 35  SG ? ? ? 1_555 J ZN  .  ZN ? ? B CYS 336 B ZN  801 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc6  metalc ? ? B CYS 119 SG ? ? ? 1_555 K HEM .  FE ? ? B CYS 420 B HEM 802 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
metalc7  metalc ? ? C CYS 30  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 331 C ZN  806 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc8  metalc ? ? C CYS 35  SG ? ? ? 1_555 T ZN  .  ZN ? ? C CYS 336 C ZN  806 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc9  metalc ? ? C CYS 119 SG ? ? ? 1_555 O HEM .  FE ? ? C CYS 420 C HEM 801 1_555 ? ? ? ? ? ? ? 2.446 ? ? 
metalc10 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 30 SG ? ? C ZN  806 D CYS 331 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc11 metalc ? ? T ZN  .   ZN ? ? ? 1_555 D CYS 35 SG ? ? C ZN  806 D CYS 336 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc12 metalc ? ? D CYS 119 SG ? ? ? 1_555 U HEM .  FE ? ? D CYS 420 D HEM 801 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
# 
_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 ? J ZN  . ? B ZN  801 ? 1_555 SG ? A CYS 35 ? A CYS 336 ? 1_555 117.3 ? 
2  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? J ZN  . ? B ZN  801 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 115.0 ? 
3  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? J ZN  . ? B ZN  801 ? 1_555 SG ? B CYS 30 ? B CYS 331 ? 1_555 103.6 ? 
4  SG ? A CYS 30  ? A CYS 331 ? 1_555 ZN ? J ZN  . ? B ZN  801 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 106.0 ? 
5  SG ? A CYS 35  ? A CYS 336 ? 1_555 ZN ? J ZN  . ? B ZN  801 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 101.7 ? 
6  SG ? B CYS 30  ? B CYS 331 ? 1_555 ZN ? J ZN  . ? B ZN  801 ? 1_555 SG ? B CYS 35 ? B CYS 336 ? 1_555 112.8 ? 
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 94.5  ? 
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 94.7  ? 
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 83.3  ? 
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 96.6  ? 
11 NA ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 NC ? E HEM .  ? A HEM 801 ? 1_555 168.4 ? 
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 92.5  ? 
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_555 102.9 ? 
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 93.4  ? 
15 NB ? E HEM .   ? A HEM 801 ? 1_555 FE ? E HEM . ? A HEM 801 ? 1_555 ND ? E HEM .  ? A HEM 801 ? 1_555 162.3 ? 
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 87.3  ? 
17 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NA ? K HEM .  ? B HEM 802 ? 1_555 98.7  ? 
18 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NB ? K HEM .  ? B HEM 802 ? 1_555 97.3  ? 
19 NA ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NB ? K HEM .  ? B HEM 802 ? 1_555 87.4  ? 
20 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NC ? K HEM .  ? B HEM 802 ? 1_555 96.1  ? 
21 NA ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NC ? K HEM .  ? B HEM 802 ? 1_555 165.1 ? 
22 NB ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 NC ? K HEM .  ? B HEM 802 ? 1_555 89.8  ? 
23 SG ? B CYS 119 ? B CYS 420 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 ND ? K HEM .  ? B HEM 802 ? 1_555 102.5 ? 
24 NA ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 ND ? K HEM .  ? B HEM 802 ? 1_555 90.5  ? 
25 NB ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 ND ? K HEM .  ? B HEM 802 ? 1_555 160.1 ? 
26 NC ? K HEM .   ? B HEM 802 ? 1_555 FE ? K HEM . ? B HEM 802 ? 1_555 ND ? K HEM .  ? B HEM 802 ? 1_555 87.2  ? 
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_555 113.8 ? 
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_555 119.4 ? 
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_555 106.6 ? 
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_555 105.2 ? 
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 99.3  ? 
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_555 110.8 ? 
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 96.8  ? 
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 97.6  ? 
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 88.8  ? 
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 97.4  ? 
37 NA ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 NC ? O HEM .  ? C HEM 801 ? 1_555 165.8 ? 
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 88.7  ? 
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_555 100.8 ? 
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 90.5  ? 
41 NB ? O HEM .   ? C HEM 801 ? 1_555 FE ? O HEM . ? C HEM 801 ? 1_555 ND ? O HEM .  ? C HEM 801 ? 1_555 161.6 ? 
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 87.5  ? 
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 94.6  ? 
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 98.7  ? 
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 83.1  ? 
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 99.1  ? 
47 NA ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 NC ? U HEM .  ? D HEM 801 ? 1_555 166.1 ? 
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 92.4  ? 
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_555 100.4 ? 
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 92.5  ? 
51 NB ? U HEM .   ? D HEM 801 ? 1_555 FE ? U HEM . ? D HEM 801 ? 1_555 ND ? U HEM .  ? D HEM 801 ? 1_555 160.7 ? 
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 87.5  ? 
# 
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 -2.88 
2 THR 405 B . ? THR 706 B PRO 406 B ? PRO 707 B 1 0.82  
3 THR 405 C . ? THR 706 C PRO 406 C ? PRO 707 C 1 -3.31 
4 THR 405 D . ? THR 706 D PRO 406 D ? PRO 707 D 1 -2.12 
# 
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 ? 4 ? 
AB7 ? 3 ? 
AB8 ? 2 ? 
AB9 ? 2 ? 
AC1 ? 3 ? 
AC2 ? 2 ? 
AC3 ? 2 ? 
AC4 ? 4 ? 
AC5 ? 3 ? 
AC6 ? 2 ? 
AC7 ? 2 ? 
AC8 ? 3 ? 
AC9 ? 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 ? anti-parallel 
AB6 1 2 ? parallel      
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC2 1 2 ? parallel      
AC3 1 2 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC8 2 3 ? anti-parallel 
AC9 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 LEU C 5   ? LYS C 8   ? LEU C 306 LYS C 309 
AB5 2 VAL C 15  ? ASP C 18  ? VAL C 316 ASP C 319 
AB6 1 GLN C 129 ? ASP C 132 ? GLN C 430 ASP C 433 
AB6 2 ALA C 162 ? ILE C 165 ? ALA C 463 ILE C 466 
AB6 3 PHE C 288 ? SER C 289 ? PHE C 589 SER C 590 
AB6 4 ALA C 270 ? VAL C 271 ? ALA C 571 VAL C 572 
AB7 1 ARG C 177 ? VAL C 178 ? ARG C 478 VAL C 479 
AB7 2 LEU C 226 ? GLN C 229 ? LEU C 527 GLN C 530 
AB7 3 GLU C 236 ? PHE C 238 ? GLU C 537 PHE C 539 
AB8 1 GLY C 188 ? LYS C 190 ? GLY C 489 LYS C 491 
AB8 2 THR C 196 ? GLY C 198 ? THR C 497 GLY C 499 
AB9 1 GLU C 247 ? PRO C 249 ? GLU C 548 PRO C 550 
AB9 2 LYS C 264 ? TYR C 266 ? LYS C 565 TYR C 567 
AC1 1 LEU C 281 ? PHE C 283 ? LEU C 582 PHE C 584 
AC1 2 LEU C 275 ? ILE C 278 ? LEU C 576 ILE C 579 
AC1 3 SER C 407 ? GLU C 409 ? SER C 708 GLU C 710 
AC2 1 TYR C 292 ? MET C 293 ? TYR C 593 MET C 594 
AC2 2 ILE C 352 ? VAL C 353 ? ILE C 653 VAL C 654 
AC3 1 LEU D 5   ? LYS D 8   ? LEU D 306 LYS D 309 
AC3 2 VAL D 15  ? ASP D 18  ? VAL D 316 ASP D 319 
AC4 1 GLN D 129 ? ASP D 132 ? GLN D 430 ASP D 433 
AC4 2 ALA D 162 ? ILE D 165 ? ALA D 463 ILE D 466 
AC4 3 PHE D 288 ? SER D 289 ? PHE D 589 SER D 590 
AC4 4 ALA D 270 ? VAL D 271 ? ALA D 571 VAL D 572 
AC5 1 ARG D 177 ? VAL D 178 ? ARG D 478 VAL D 479 
AC5 2 LEU D 226 ? GLN D 229 ? LEU D 527 GLN D 530 
AC5 3 GLU D 236 ? PHE D 238 ? GLU D 537 PHE D 539 
AC6 1 GLY D 188 ? LYS D 190 ? GLY D 489 LYS D 491 
AC6 2 THR D 196 ? GLY D 198 ? THR D 497 GLY D 499 
AC7 1 GLU D 247 ? PRO D 249 ? GLU D 548 PRO D 550 
AC7 2 LYS D 264 ? TYR D 266 ? LYS D 565 TYR D 567 
AC8 1 LEU D 281 ? PHE D 283 ? LEU D 582 PHE D 584 
AC8 2 LEU D 275 ? ILE D 278 ? LEU D 576 ILE D 579 
AC8 3 SER D 407 ? GLU D 409 ? SER D 708 GLU D 710 
AC9 1 TYR D 292 ? MET D 293 ? TYR D 593 MET D 594 
AC9 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 228 ? N LEU A 529 O GLU A 236 ? O GLU A 537 
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 LEU C 5   ? N LEU C 306 O ASP C 18  ? O ASP C 319 
AB6 1 2 N PHE C 131 ? N PHE C 432 O ILE C 163 ? O ILE C 464 
AB6 2 3 N ALA C 162 ? N ALA C 463 O SER C 289 ? O SER C 590 
AB6 3 4 O PHE C 288 ? O PHE C 589 N VAL C 271 ? N VAL C 572 
AB7 1 2 N ARG C 177 ? N ARG C 478 O GLN C 229 ? O GLN C 530 
AB7 2 3 N LEU C 226 ? N LEU C 527 O PHE C 238 ? O PHE C 539 
AB8 1 2 N TYR C 189 ? N TYR C 490 O LEU C 197 ? O LEU C 498 
AB9 1 2 N VAL C 248 ? N VAL C 549 O TRP C 265 ? O TRP C 566 
AC1 1 2 O LEU C 281 ? O LEU C 582 N ILE C 278 ? N ILE C 579 
AC1 2 3 N GLU C 277 ? N GLU C 578 O SER C 407 ? O SER C 708 
AC2 1 2 N TYR C 292 ? N TYR C 593 O VAL C 353 ? O VAL C 654 
AC3 1 2 N LEU D 5   ? N LEU D 306 O ASP D 18  ? O ASP D 319 
AC4 1 2 N PHE D 131 ? N PHE D 432 O ILE D 163 ? O ILE D 464 
AC4 2 3 N ALA D 162 ? N ALA D 463 O SER D 289 ? O SER D 590 
AC4 3 4 O PHE D 288 ? O PHE D 589 N VAL D 271 ? N VAL D 572 
AC5 1 2 N ARG D 177 ? N ARG D 478 O GLN D 229 ? O GLN D 530 
AC5 2 3 N LEU D 226 ? N LEU D 527 O PHE D 238 ? O PHE D 539 
AC6 1 2 N TYR D 189 ? N TYR D 490 O LEU D 197 ? O LEU D 498 
AC7 1 2 N VAL D 248 ? N VAL D 549 O TRP D 265 ? O TRP D 566 
AC8 1 2 O PHE D 283 ? O PHE D 584 N LEU D 276 ? N LEU D 577 
AC8 2 3 N LEU D 275 ? N LEU D 576 O GLU D 409 ? O GLU D 710 
AC9 1 2 N TYR D 292 ? N TYR D 593 O VAL D 353 ? O VAL D 654 
# 
_pdbx_entry_details.entry_id                   9CW3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A ILE 509 ? ? O A HOH 901 ? ? 1.97 
2 1 O C ARG 376 ? ? O C HOH 901 ? ? 2.10 
# 
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 GLU A 314 ? ? 76.71   -1.56   
2  1 THR A 326 ? ? -149.28 22.11   
3  1 ASP A 352 ? ? -76.02  30.61   
4  1 THR A 471 ? ? -118.83 -83.77  
5  1 CYS A 587 ? ? -151.26 51.38   
6  1 ARG A 608 ? ? -111.23 -131.82 
7  1 ASN A 620 ? ? 70.36   35.52   
8  1 CYS A 677 ? ? -169.62 100.70  
9  1 PRO B 350 ? ? -61.55  -170.56 
10 1 GLU B 351 ? ? -58.28  -77.06  
11 1 ASP B 352 ? ? -96.31  -145.99 
12 1 ARG B 376 ? ? -105.55 -109.88 
13 1 PHE B 377 ? ? 69.69   113.02  
14 1 LYS B 428 ? ? -107.08 58.34   
15 1 THR B 471 ? ? -108.67 -72.40  
16 1 CYS B 587 ? ? -152.07 58.79   
17 1 ARG B 608 ? ? -119.62 -129.12 
18 1 ASN B 620 ? ? 61.49   65.01   
19 1 ASP B 622 ? ? -65.09  92.30   
20 1 HIS C 346 ? ? -59.55  106.39  
21 1 PRO C 350 ? ? -60.11  -169.78 
22 1 ASP C 352 ? ? -109.76 -151.32 
23 1 ARG C 376 ? ? -102.30 -111.95 
24 1 PHE C 377 ? ? 68.93   118.47  
25 1 ARG C 423 ? ? -65.64  0.87    
26 1 LYS C 428 ? ? -109.66 68.09   
27 1 THR C 471 ? ? -118.22 -73.39  
28 1 SER C 496 ? ? -75.43  -167.68 
29 1 CYS C 587 ? ? -151.46 57.23   
30 1 ARG C 608 ? ? -114.95 -133.60 
31 1 ASN C 620 ? ? 63.06   61.00   
32 1 CYS C 677 ? ? -160.76 111.08  
33 1 LYS D 428 ? ? -104.52 79.85   
34 1 THR D 471 ? ? -119.82 -83.36  
35 1 CYS D 587 ? ? -147.72 54.48   
36 1 ARG D 608 ? ? -113.42 -130.54 
37 1 CYS D 677 ? ? -165.14 103.89  
# 
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 -34.4037 7.7554  -38.5475 0.3015 ? -0.0053 ? 0.0520  ? 0.2580 ? 0.0585 ? 0.3031 ? 0.8519 ? -0.2205 
? 0.1020  ? 0.5282 ? 0.2541 ? 1.9386 ? -0.0308 ? -0.0439 ? -0.0456 ? -0.0029 ? 0.0128 ? 0.0478  ? 0.1432  ? -0.0009 ? 0.0171 ? 
2 'X-RAY DIFFRACTION' ? refined -34.6000 9.7614  -0.9578  0.3519 ? -0.0106 ? -0.0033 ? 0.2639 ? 0.0326 ? 0.2970 ? 0.9633 ? -0.1642 
? -0.0580 ? 0.5301 ? 0.0781 ? 2.7890 ? -0.0746 ? 0.0350  ? 0.0575  ? 0.0713  ? 0.0324 ? -0.0115 ? -0.1114 ? 0.0922  ? 0.0441 ? 
3 'X-RAY DIFFRACTION' ? refined 24.5776  31.4957 -81.3961 0.3034 ? 0.0045  ? 0.0089  ? 0.2250 ? 0.0308 ? 0.2733 ? 0.9609 ? 0.1376  
? 0.0355  ? 0.6304 ? 0.0420 ? 2.9050 ? -0.0738 ? -0.0265 ? -0.0707 ? -0.0695 ? 0.0212 ? -0.0064 ? 0.1252  ? 0.0746  ? 0.0456 ? 
4 'X-RAY DIFFRACTION' ? refined 24.7934  33.5236 -43.8498 0.2608 ? 0.0020  ? -0.0384 ? 0.2226 ? 0.0507 ? 0.2812 ? 0.7346 ? 0.1477  
? -0.0064 ? 0.4887 ? 0.2324 ? 1.9635 ? -0.0335 ? 0.0400  ? 0.0281  ? 0.0194  ? 0.0069 ? 0.0485  ? -0.1003 ? -0.0117 ? 0.0245 ? 
# 
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 304:722)' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '(chain B and resid 305:722)' 
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? '(chain C and resid 304:722)' 
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? '(chain D and resid 304:722)' 
# 
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 SER 344 ? A SER 43  
4  1 Y 1 A GLN 345 ? A GLN 44  
5  1 Y 1 A HIS 346 ? A HIS 45  
6  1 Y 1 A ALA 347 ? A ALA 46  
7  1 Y 1 A ARG 348 ? A ARG 47  
8  1 Y 1 A ARG 349 ? A ARG 48  
9  1 Y 1 A LEU 723 ? A LEU 422 
10 1 Y 1 A VAL 724 ? A VAL 423 
11 1 Y 1 B CYS 302 ? B CYS 1   
12 1 Y 1 B PRO 303 ? B PRO 2   
13 1 Y 1 B ARG 304 ? B ARG 3   
14 1 Y 1 B LEU 723 ? B LEU 422 
15 1 Y 1 B VAL 724 ? B VAL 423 
16 1 Y 1 C CYS 302 ? C CYS 1   
17 1 Y 1 C PRO 303 ? C PRO 2   
18 1 Y 1 C LEU 723 ? C LEU 422 
19 1 Y 1 C VAL 724 ? C VAL 423 
20 1 Y 1 D CYS 302 ? D CYS 1   
21 1 Y 1 D PRO 303 ? D PRO 2   
22 1 Y 1 D GLN 345 ? D GLN 44  
23 1 Y 1 D HIS 346 ? D HIS 45  
24 1 Y 1 D ALA 347 ? D ALA 46  
25 1 Y 1 D ARG 348 ? D ARG 47  
26 1 Y 1 D ARG 349 ? D ARG 48  
27 1 Y 1 D LEU 723 ? D LEU 422 
28 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 
A1A0A C11  C  Y N 1   
A1A0A C12  C  Y N 2   
A1A0A C15  C  Y N 3   
A1A0A N02  N  N N 4   
A1A0A C03  C  Y N 5   
A1A0A C04  C  Y N 6   
A1A0A C06  C  Y N 7   
A1A0A C22  C  N N 8   
A1A0A C23  C  N N 9   
A1A0A C02  C  Y N 10  
A1A0A C05  C  Y N 11  
A1A0A C07  C  N N 12  
A1A0A C13  C  Y N 13  
A1A0A C14  C  Y N 14  
A1A0A C16  C  Y N 15  
A1A0A C17  C  N N 16  
A1A0A C24  C  N N 17  
A1A0A C25  C  N N 18  
A1A0A C26  C  N N 19  
A1A0A F12  F  N N 20  
A1A0A F13  F  N N 21  
A1A0A F27  F  N N 22  
A1A0A F28  F  N N 23  
A1A0A N01  N  Y N 24  
A1A0A N21  N  N N 25  
A1A0A H1   H  N N 26  
A1A0A H2   H  N N 27  
A1A0A H3   H  N N 28  
A1A0A H4   H  N N 29  
A1A0A H5   H  N N 30  
A1A0A H6   H  N N 31  
A1A0A H7   H  N N 32  
A1A0A H8   H  N N 33  
A1A0A H9   H  N N 34  
A1A0A H10  H  N N 35  
A1A0A H11  H  N N 36  
A1A0A H12  H  N N 37  
A1A0A H13  H  N N 38  
A1A0A H14  H  N N 39  
A1A0A H15  H  N N 40  
A1A0A H16  H  N N 41  
A1A0A H17  H  N N 42  
A1A0A H18  H  N N 43  
A1A0A H19  H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
GOL   C1   C  N N 181 
GOL   O1   O  N N 182 
GOL   C2   C  N N 183 
GOL   O2   O  N N 184 
GOL   C3   C  N N 185 
GOL   O3   O  N N 186 
GOL   H11  H  N N 187 
GOL   H12  H  N N 188 
GOL   HO1  H  N N 189 
GOL   H2   H  N N 190 
GOL   HO2  H  N N 191 
GOL   H31  H  N N 192 
GOL   H32  H  N N 193 
GOL   HO3  H  N N 194 
H4B   N1   N  Y N 195 
H4B   C2   C  Y N 196 
H4B   N2   N  N N 197 
H4B   N3   N  Y N 198 
H4B   C4   C  Y N 199 
H4B   O4   O  N N 200 
H4B   C4A  C  Y N 201 
H4B   C8A  C  Y N 202 
H4B   N5   N  N N 203 
H4B   N8   N  N N 204 
H4B   C6   C  N R 205 
H4B   C7   C  N N 206 
H4B   C9   C  N R 207 
H4B   O9   O  N N 208 
H4B   C10  C  N S 209 
H4B   C11  C  N N 210 
H4B   O10  O  N N 211 
H4B   HN21 H  N N 212 
H4B   HN22 H  N N 213 
H4B   HN3  H  N N 214 
H4B   HN5  H  N N 215 
H4B   HN8  H  N N 216 
H4B   H6   H  N N 217 
H4B   H71  H  N N 218 
H4B   H72  H  N N 219 
H4B   H9   H  N N 220 
H4B   HO9  H  N N 221 
H4B   H10  H  N N 222 
H4B   H111 H  N N 223 
H4B   H112 H  N N 224 
H4B   H113 H  N N 225 
H4B   HO0  H  N N 226 
HEM   CHA  C  N N 227 
HEM   CHB  C  N N 228 
HEM   CHC  C  N N 229 
HEM   CHD  C  N N 230 
HEM   C1A  C  Y N 231 
HEM   C2A  C  Y N 232 
HEM   C3A  C  Y N 233 
HEM   C4A  C  Y N 234 
HEM   CMA  C  N N 235 
HEM   CAA  C  N N 236 
HEM   CBA  C  N N 237 
HEM   CGA  C  N N 238 
HEM   O1A  O  N N 239 
HEM   O2A  O  N N 240 
HEM   C1B  C  N N 241 
HEM   C2B  C  N N 242 
HEM   C3B  C  N N 243 
HEM   C4B  C  N N 244 
HEM   CMB  C  N N 245 
HEM   CAB  C  N N 246 
HEM   CBB  C  N N 247 
HEM   C1C  C  Y N 248 
HEM   C2C  C  Y N 249 
HEM   C3C  C  Y N 250 
HEM   C4C  C  Y N 251 
HEM   CMC  C  N N 252 
HEM   CAC  C  N N 253 
HEM   CBC  C  N N 254 
HEM   C1D  C  N N 255 
HEM   C2D  C  N N 256 
HEM   C3D  C  N N 257 
HEM   C4D  C  N N 258 
HEM   CMD  C  N N 259 
HEM   CAD  C  N N 260 
HEM   CBD  C  N N 261 
HEM   CGD  C  N N 262 
HEM   O1D  O  N N 263 
HEM   O2D  O  N N 264 
HEM   NA   N  Y N 265 
HEM   NB   N  N N 266 
HEM   NC   N  Y N 267 
HEM   ND   N  N N 268 
HEM   FE   FE N N 269 
HEM   HHB  H  N N 270 
HEM   HHC  H  N N 271 
HEM   HHD  H  N N 272 
HEM   HMA  H  N N 273 
HEM   HMAA H  N N 274 
HEM   HMAB H  N N 275 
HEM   HAA  H  N N 276 
HEM   HAAA H  N N 277 
HEM   HBA  H  N N 278 
HEM   HBAA H  N N 279 
HEM   HMB  H  N N 280 
HEM   HMBA H  N N 281 
HEM   HMBB H  N N 282 
HEM   HAB  H  N N 283 
HEM   HBB  H  N N 284 
HEM   HBBA H  N N 285 
HEM   HMC  H  N N 286 
HEM   HMCA H  N N 287 
HEM   HMCB H  N N 288 
HEM   HAC  H  N N 289 
HEM   HBC  H  N N 290 
HEM   HBCA H  N N 291 
HEM   HMD  H  N N 292 
HEM   HMDA H  N N 293 
HEM   HMDB H  N N 294 
HEM   HAD  H  N N 295 
HEM   HADA H  N N 296 
HEM   HBD  H  N N 297 
HEM   HBDA H  N N 298 
HEM   H2A  H  N N 299 
HEM   H2D  H  N N 300 
HEM   HHA  H  N N 301 
HIS   N    N  N N 302 
HIS   CA   C  N S 303 
HIS   C    C  N N 304 
HIS   O    O  N N 305 
HIS   CB   C  N N 306 
HIS   CG   C  Y N 307 
HIS   ND1  N  Y N 308 
HIS   CD2  C  Y N 309 
HIS   CE1  C  Y N 310 
HIS   NE2  N  Y N 311 
HIS   OXT  O  N N 312 
HIS   H    H  N N 313 
HIS   H2   H  N N 314 
HIS   HA   H  N N 315 
HIS   HB2  H  N N 316 
HIS   HB3  H  N N 317 
HIS   HD1  H  N N 318 
HIS   HD2  H  N N 319 
HIS   HE1  H  N N 320 
HIS   HE2  H  N N 321 
HIS   HXT  H  N N 322 
HOH   O    O  N N 323 
HOH   H1   H  N N 324 
HOH   H2   H  N N 325 
ILE   N    N  N N 326 
ILE   CA   C  N S 327 
ILE   C    C  N N 328 
ILE   O    O  N N 329 
ILE   CB   C  N S 330 
ILE   CG1  C  N N 331 
ILE   CG2  C  N N 332 
ILE   CD1  C  N N 333 
ILE   OXT  O  N N 334 
ILE   H    H  N N 335 
ILE   H2   H  N N 336 
ILE   HA   H  N N 337 
ILE   HB   H  N N 338 
ILE   HG12 H  N N 339 
ILE   HG13 H  N N 340 
ILE   HG21 H  N N 341 
ILE   HG22 H  N N 342 
ILE   HG23 H  N N 343 
ILE   HD11 H  N N 344 
ILE   HD12 H  N N 345 
ILE   HD13 H  N N 346 
ILE   HXT  H  N N 347 
LEU   N    N  N N 348 
LEU   CA   C  N S 349 
LEU   C    C  N N 350 
LEU   O    O  N N 351 
LEU   CB   C  N N 352 
LEU   CG   C  N N 353 
LEU   CD1  C  N N 354 
LEU   CD2  C  N N 355 
LEU   OXT  O  N N 356 
LEU   H    H  N N 357 
LEU   H2   H  N N 358 
LEU   HA   H  N N 359 
LEU   HB2  H  N N 360 
LEU   HB3  H  N N 361 
LEU   HG   H  N N 362 
LEU   HD11 H  N N 363 
LEU   HD12 H  N N 364 
LEU   HD13 H  N N 365 
LEU   HD21 H  N N 366 
LEU   HD22 H  N N 367 
LEU   HD23 H  N N 368 
LEU   HXT  H  N N 369 
LYS   N    N  N N 370 
LYS   CA   C  N S 371 
LYS   C    C  N N 372 
LYS   O    O  N N 373 
LYS   CB   C  N N 374 
LYS   CG   C  N N 375 
LYS   CD   C  N N 376 
LYS   CE   C  N N 377 
LYS   NZ   N  N N 378 
LYS   OXT  O  N N 379 
LYS   H    H  N N 380 
LYS   H2   H  N N 381 
LYS   HA   H  N N 382 
LYS   HB2  H  N N 383 
LYS   HB3  H  N N 384 
LYS   HG2  H  N N 385 
LYS   HG3  H  N N 386 
LYS   HD2  H  N N 387 
LYS   HD3  H  N N 388 
LYS   HE2  H  N N 389 
LYS   HE3  H  N N 390 
LYS   HZ1  H  N N 391 
LYS   HZ2  H  N N 392 
LYS   HZ3  H  N N 393 
LYS   HXT  H  N N 394 
MET   N    N  N N 395 
MET   CA   C  N S 396 
MET   C    C  N N 397 
MET   O    O  N N 398 
MET   CB   C  N N 399 
MET   CG   C  N N 400 
MET   SD   S  N N 401 
MET   CE   C  N N 402 
MET   OXT  O  N N 403 
MET   H    H  N N 404 
MET   H2   H  N N 405 
MET   HA   H  N N 406 
MET   HB2  H  N N 407 
MET   HB3  H  N N 408 
MET   HG2  H  N N 409 
MET   HG3  H  N N 410 
MET   HE1  H  N N 411 
MET   HE2  H  N N 412 
MET   HE3  H  N N 413 
MET   HXT  H  N N 414 
PHE   N    N  N N 415 
PHE   CA   C  N S 416 
PHE   C    C  N N 417 
PHE   O    O  N N 418 
PHE   CB   C  N N 419 
PHE   CG   C  Y N 420 
PHE   CD1  C  Y N 421 
PHE   CD2  C  Y N 422 
PHE   CE1  C  Y N 423 
PHE   CE2  C  Y N 424 
PHE   CZ   C  Y N 425 
PHE   OXT  O  N N 426 
PHE   H    H  N N 427 
PHE   H2   H  N N 428 
PHE   HA   H  N N 429 
PHE   HB2  H  N N 430 
PHE   HB3  H  N N 431 
PHE   HD1  H  N N 432 
PHE   HD2  H  N N 433 
PHE   HE1  H  N N 434 
PHE   HE2  H  N N 435 
PHE   HZ   H  N N 436 
PHE   HXT  H  N N 437 
PRO   N    N  N N 438 
PRO   CA   C  N S 439 
PRO   C    C  N N 440 
PRO   O    O  N N 441 
PRO   CB   C  N N 442 
PRO   CG   C  N N 443 
PRO   CD   C  N N 444 
PRO   OXT  O  N N 445 
PRO   H    H  N N 446 
PRO   HA   H  N N 447 
PRO   HB2  H  N N 448 
PRO   HB3  H  N N 449 
PRO   HG2  H  N N 450 
PRO   HG3  H  N N 451 
PRO   HD2  H  N N 452 
PRO   HD3  H  N N 453 
PRO   HXT  H  N N 454 
SER   N    N  N N 455 
SER   CA   C  N S 456 
SER   C    C  N N 457 
SER   O    O  N N 458 
SER   CB   C  N N 459 
SER   OG   O  N N 460 
SER   OXT  O  N N 461 
SER   H    H  N N 462 
SER   H2   H  N N 463 
SER   HA   H  N N 464 
SER   HB2  H  N N 465 
SER   HB3  H  N N 466 
SER   HG   H  N N 467 
SER   HXT  H  N N 468 
THR   N    N  N N 469 
THR   CA   C  N S 470 
THR   C    C  N N 471 
THR   O    O  N N 472 
THR   CB   C  N R 473 
THR   OG1  O  N N 474 
THR   CG2  C  N N 475 
THR   OXT  O  N N 476 
THR   H    H  N N 477 
THR   H2   H  N N 478 
THR   HA   H  N N 479 
THR   HB   H  N N 480 
THR   HG1  H  N N 481 
THR   HG21 H  N N 482 
THR   HG22 H  N N 483 
THR   HG23 H  N N 484 
THR   HXT  H  N N 485 
TRP   N    N  N N 486 
TRP   CA   C  N S 487 
TRP   C    C  N N 488 
TRP   O    O  N N 489 
TRP   CB   C  N N 490 
TRP   CG   C  Y N 491 
TRP   CD1  C  Y N 492 
TRP   CD2  C  Y N 493 
TRP   NE1  N  Y N 494 
TRP   CE2  C  Y N 495 
TRP   CE3  C  Y N 496 
TRP   CZ2  C  Y N 497 
TRP   CZ3  C  Y N 498 
TRP   CH2  C  Y N 499 
TRP   OXT  O  N N 500 
TRP   H    H  N N 501 
TRP   H2   H  N N 502 
TRP   HA   H  N N 503 
TRP   HB2  H  N N 504 
TRP   HB3  H  N N 505 
TRP   HD1  H  N N 506 
TRP   HE1  H  N N 507 
TRP   HE3  H  N N 508 
TRP   HZ2  H  N N 509 
TRP   HZ3  H  N N 510 
TRP   HH2  H  N N 511 
TRP   HXT  H  N N 512 
TYR   N    N  N N 513 
TYR   CA   C  N S 514 
TYR   C    C  N N 515 
TYR   O    O  N N 516 
TYR   CB   C  N N 517 
TYR   CG   C  Y N 518 
TYR   CD1  C  Y N 519 
TYR   CD2  C  Y N 520 
TYR   CE1  C  Y N 521 
TYR   CE2  C  Y N 522 
TYR   CZ   C  Y N 523 
TYR   OH   O  N N 524 
TYR   OXT  O  N N 525 
TYR   H    H  N N 526 
TYR   H2   H  N N 527 
TYR   HA   H  N N 528 
TYR   HB2  H  N N 529 
TYR   HB3  H  N N 530 
TYR   HD1  H  N N 531 
TYR   HD2  H  N N 532 
TYR   HE1  H  N N 533 
TYR   HE2  H  N N 534 
TYR   HH   H  N N 535 
TYR   HXT  H  N N 536 
VAL   N    N  N N 537 
VAL   CA   C  N S 538 
VAL   C    C  N N 539 
VAL   O    O  N N 540 
VAL   CB   C  N N 541 
VAL   CG1  C  N N 542 
VAL   CG2  C  N N 543 
VAL   OXT  O  N N 544 
VAL   H    H  N N 545 
VAL   H2   H  N N 546 
VAL   HA   H  N N 547 
VAL   HB   H  N N 548 
VAL   HG11 H  N N 549 
VAL   HG12 H  N N 550 
VAL   HG13 H  N N 551 
VAL   HG21 H  N N 552 
VAL   HG22 H  N N 553 
VAL   HG23 H  N N 554 
VAL   HXT  H  N N 555 
ZN    ZN   ZN N N 556 
# 
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 
A1A0A C07 C04  sing N N 1   
A1A0A C04 C03  doub Y N 2   
A1A0A C04 C05  sing Y N 3   
A1A0A C03 C02  sing Y N 4   
A1A0A C05 C06  doub Y N 5   
A1A0A C02 N01  doub Y N 6   
A1A0A C02 N02  sing N N 7   
A1A0A C06 N01  sing Y N 8   
A1A0A C06 C11  sing N N 9   
A1A0A F12 C12  sing N N 10  
A1A0A C23 C22  sing N N 11  
A1A0A C23 C24  sing N N 12  
A1A0A F27 C24  sing N N 13  
A1A0A C11 C12  doub Y N 14  
A1A0A C11 C16  sing Y N 15  
A1A0A C12 C13  sing Y N 16  
A1A0A C22 N21  sing N N 17  
A1A0A C24 F28  sing N N 18  
A1A0A C24 C25  sing N N 19  
A1A0A C16 C15  doub Y N 20  
A1A0A C13 F13  sing N N 21  
A1A0A C13 C14  doub Y N 22  
A1A0A C15 C14  sing Y N 23  
A1A0A C15 C17  sing N N 24  
A1A0A N21 C17  sing N N 25  
A1A0A N21 C26  sing N N 26  
A1A0A C25 C26  sing N N 27  
A1A0A N02 H1   sing N N 28  
A1A0A N02 H2   sing N N 29  
A1A0A C03 H3   sing N N 30  
A1A0A C22 H4   sing N N 31  
A1A0A C22 H5   sing N N 32  
A1A0A C23 H6   sing N N 33  
A1A0A C23 H7   sing N N 34  
A1A0A C05 H8   sing N N 35  
A1A0A C07 H9   sing N N 36  
A1A0A C07 H10  sing N N 37  
A1A0A C07 H11  sing N N 38  
A1A0A C14 H12  sing N N 39  
A1A0A C16 H13  sing N N 40  
A1A0A C17 H14  sing N N 41  
A1A0A C17 H15  sing N N 42  
A1A0A C25 H16  sing N N 43  
A1A0A C25 H17  sing N N 44  
A1A0A C26 H18  sing N N 45  
A1A0A C26 H19  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
GOL   C1  O1   sing N N 175 
GOL   C1  C2   sing N N 176 
GOL   C1  H11  sing N N 177 
GOL   C1  H12  sing N N 178 
GOL   O1  HO1  sing N N 179 
GOL   C2  O2   sing N N 180 
GOL   C2  C3   sing N N 181 
GOL   C2  H2   sing N N 182 
GOL   O2  HO2  sing N N 183 
GOL   C3  O3   sing N N 184 
GOL   C3  H31  sing N N 185 
GOL   C3  H32  sing N N 186 
GOL   O3  HO3  sing N N 187 
H4B   N1  C2   doub Y N 188 
H4B   N1  C8A  sing Y N 189 
H4B   C2  N2   sing N N 190 
H4B   C2  N3   sing Y N 191 
H4B   N2  HN21 sing N N 192 
H4B   N2  HN22 sing N N 193 
H4B   N3  C4   sing Y N 194 
H4B   N3  HN3  sing N N 195 
H4B   C4  O4   doub N N 196 
H4B   C4  C4A  sing Y N 197 
H4B   C4A C8A  doub Y N 198 
H4B   C4A N5   sing N N 199 
H4B   C8A N8   sing N N 200 
H4B   N5  C6   sing N N 201 
H4B   N5  HN5  sing N N 202 
H4B   N8  C7   sing N N 203 
H4B   N8  HN8  sing N N 204 
H4B   C6  C7   sing N N 205 
H4B   C6  C9   sing N N 206 
H4B   C6  H6   sing N N 207 
H4B   C7  H71  sing N N 208 
H4B   C7  H72  sing N N 209 
H4B   C9  O9   sing N N 210 
H4B   C9  C10  sing N N 211 
H4B   C9  H9   sing N N 212 
H4B   O9  HO9  sing N N 213 
H4B   C10 C11  sing N N 214 
H4B   C10 O10  sing N N 215 
H4B   C10 H10  sing N N 216 
H4B   C11 H111 sing N N 217 
H4B   C11 H112 sing N N 218 
H4B   C11 H113 sing N N 219 
H4B   O10 HO0  sing N N 220 
HEM   CHA C1A  sing N N 221 
HEM   CHA C4D  doub N N 222 
HEM   CHA HHA  sing N N 223 
HEM   CHB C4A  sing N N 224 
HEM   CHB C1B  doub N N 225 
HEM   CHB HHB  sing N N 226 
HEM   CHC C4B  sing N N 227 
HEM   CHC C1C  doub N N 228 
HEM   CHC HHC  sing N N 229 
HEM   CHD C4C  doub N N 230 
HEM   CHD C1D  sing N N 231 
HEM   CHD HHD  sing N N 232 
HEM   C1A C2A  doub Y N 233 
HEM   C1A NA   sing Y N 234 
HEM   C2A C3A  sing Y N 235 
HEM   C2A CAA  sing N N 236 
HEM   C3A C4A  doub Y N 237 
HEM   C3A CMA  sing N N 238 
HEM   C4A NA   sing Y N 239 
HEM   CMA HMA  sing N N 240 
HEM   CMA HMAA sing N N 241 
HEM   CMA HMAB sing N N 242 
HEM   CAA CBA  sing N N 243 
HEM   CAA HAA  sing N N 244 
HEM   CAA HAAA sing N N 245 
HEM   CBA CGA  sing N N 246 
HEM   CBA HBA  sing N N 247 
HEM   CBA HBAA sing N N 248 
HEM   CGA O1A  doub N N 249 
HEM   CGA O2A  sing N N 250 
HEM   C1B C2B  sing N N 251 
HEM   C1B NB   sing N N 252 
HEM   C2B C3B  doub N N 253 
HEM   C2B CMB  sing N N 254 
HEM   C3B C4B  sing N N 255 
HEM   C3B CAB  sing N N 256 
HEM   C4B NB   doub N N 257 
HEM   CMB HMB  sing N N 258 
HEM   CMB HMBA sing N N 259 
HEM   CMB HMBB sing N N 260 
HEM   CAB CBB  doub N N 261 
HEM   CAB HAB  sing N N 262 
HEM   CBB HBB  sing N N 263 
HEM   CBB HBBA sing N N 264 
HEM   C1C C2C  sing Y N 265 
HEM   C1C NC   sing Y N 266 
HEM   C2C C3C  doub Y N 267 
HEM   C2C CMC  sing N N 268 
HEM   C3C C4C  sing Y N 269 
HEM   C3C CAC  sing N N 270 
HEM   C4C NC   sing Y N 271 
HEM   CMC HMC  sing N N 272 
HEM   CMC HMCA sing N N 273 
HEM   CMC HMCB sing N N 274 
HEM   CAC CBC  doub N N 275 
HEM   CAC HAC  sing N N 276 
HEM   CBC HBC  sing N N 277 
HEM   CBC HBCA sing N N 278 
HEM   C1D C2D  sing N N 279 
HEM   C1D ND   doub N N 280 
HEM   C2D C3D  doub N N 281 
HEM   C2D CMD  sing N N 282 
HEM   C3D C4D  sing N N 283 
HEM   C3D CAD  sing N N 284 
HEM   C4D ND   sing N N 285 
HEM   CMD HMD  sing N N 286 
HEM   CMD HMDA sing N N 287 
HEM   CMD HMDB sing N N 288 
HEM   CAD CBD  sing N N 289 
HEM   CAD HAD  sing N N 290 
HEM   CAD HADA sing N N 291 
HEM   CBD CGD  sing N N 292 
HEM   CBD HBD  sing N N 293 
HEM   CBD HBDA sing N N 294 
HEM   CGD O1D  doub N N 295 
HEM   CGD O2D  sing N N 296 
HEM   O2A H2A  sing N N 297 
HEM   O2D H2D  sing N N 298 
HEM   FE  NA   sing N N 299 
HEM   FE  NB   sing N N 300 
HEM   FE  NC   sing N N 301 
HEM   FE  ND   sing N N 302 
HIS   N   CA   sing N N 303 
HIS   N   H    sing N N 304 
HIS   N   H2   sing N N 305 
HIS   CA  C    sing N N 306 
HIS   CA  CB   sing N N 307 
HIS   CA  HA   sing N N 308 
HIS   C   O    doub N N 309 
HIS   C   OXT  sing N N 310 
HIS   CB  CG   sing N N 311 
HIS   CB  HB2  sing N N 312 
HIS   CB  HB3  sing N N 313 
HIS   CG  ND1  sing Y N 314 
HIS   CG  CD2  doub Y N 315 
HIS   ND1 CE1  doub Y N 316 
HIS   ND1 HD1  sing N N 317 
HIS   CD2 NE2  sing Y N 318 
HIS   CD2 HD2  sing N N 319 
HIS   CE1 NE2  sing Y N 320 
HIS   CE1 HE1  sing N N 321 
HIS   NE2 HE2  sing N N 322 
HIS   OXT HXT  sing N N 323 
HOH   O   H1   sing N N 324 
HOH   O   H2   sing N N 325 
ILE   N   CA   sing N N 326 
ILE   N   H    sing N N 327 
ILE   N   H2   sing N N 328 
ILE   CA  C    sing N N 329 
ILE   CA  CB   sing N N 330 
ILE   CA  HA   sing N N 331 
ILE   C   O    doub N N 332 
ILE   C   OXT  sing N N 333 
ILE   CB  CG1  sing N N 334 
ILE   CB  CG2  sing N N 335 
ILE   CB  HB   sing N N 336 
ILE   CG1 CD1  sing N N 337 
ILE   CG1 HG12 sing N N 338 
ILE   CG1 HG13 sing N N 339 
ILE   CG2 HG21 sing N N 340 
ILE   CG2 HG22 sing N N 341 
ILE   CG2 HG23 sing N N 342 
ILE   CD1 HD11 sing N N 343 
ILE   CD1 HD12 sing N N 344 
ILE   CD1 HD13 sing N N 345 
ILE   OXT HXT  sing N N 346 
LEU   N   CA   sing N N 347 
LEU   N   H    sing N N 348 
LEU   N   H2   sing N N 349 
LEU   CA  C    sing N N 350 
LEU   CA  CB   sing N N 351 
LEU   CA  HA   sing N N 352 
LEU   C   O    doub N N 353 
LEU   C   OXT  sing N N 354 
LEU   CB  CG   sing N N 355 
LEU   CB  HB2  sing N N 356 
LEU   CB  HB3  sing N N 357 
LEU   CG  CD1  sing N N 358 
LEU   CG  CD2  sing N N 359 
LEU   CG  HG   sing N N 360 
LEU   CD1 HD11 sing N N 361 
LEU   CD1 HD12 sing N N 362 
LEU   CD1 HD13 sing N N 363 
LEU   CD2 HD21 sing N N 364 
LEU   CD2 HD22 sing N N 365 
LEU   CD2 HD23 sing N N 366 
LEU   OXT HXT  sing N N 367 
LYS   N   CA   sing N N 368 
LYS   N   H    sing N N 369 
LYS   N   H2   sing N N 370 
LYS   CA  C    sing N N 371 
LYS   CA  CB   sing N N 372 
LYS   CA  HA   sing N N 373 
LYS   C   O    doub N N 374 
LYS   C   OXT  sing N N 375 
LYS   CB  CG   sing N N 376 
LYS   CB  HB2  sing N N 377 
LYS   CB  HB3  sing N N 378 
LYS   CG  CD   sing N N 379 
LYS   CG  HG2  sing N N 380 
LYS   CG  HG3  sing N N 381 
LYS   CD  CE   sing N N 382 
LYS   CD  HD2  sing N N 383 
LYS   CD  HD3  sing N N 384 
LYS   CE  NZ   sing N N 385 
LYS   CE  HE2  sing N N 386 
LYS   CE  HE3  sing N N 387 
LYS   NZ  HZ1  sing N N 388 
LYS   NZ  HZ2  sing N N 389 
LYS   NZ  HZ3  sing N N 390 
LYS   OXT HXT  sing N N 391 
MET   N   CA   sing N N 392 
MET   N   H    sing N N 393 
MET   N   H2   sing N N 394 
MET   CA  C    sing N N 395 
MET   CA  CB   sing N N 396 
MET   CA  HA   sing N N 397 
MET   C   O    doub N N 398 
MET   C   OXT  sing N N 399 
MET   CB  CG   sing N N 400 
MET   CB  HB2  sing N N 401 
MET   CB  HB3  sing N N 402 
MET   CG  SD   sing N N 403 
MET   CG  HG2  sing N N 404 
MET   CG  HG3  sing N N 405 
MET   SD  CE   sing N N 406 
MET   CE  HE1  sing N N 407 
MET   CE  HE2  sing N N 408 
MET   CE  HE3  sing N N 409 
MET   OXT HXT  sing N N 410 
PHE   N   CA   sing N N 411 
PHE   N   H    sing N N 412 
PHE   N   H2   sing N N 413 
PHE   CA  C    sing N N 414 
PHE   CA  CB   sing N N 415 
PHE   CA  HA   sing N N 416 
PHE   C   O    doub N N 417 
PHE   C   OXT  sing N N 418 
PHE   CB  CG   sing N N 419 
PHE   CB  HB2  sing N N 420 
PHE   CB  HB3  sing N N 421 
PHE   CG  CD1  doub Y N 422 
PHE   CG  CD2  sing Y N 423 
PHE   CD1 CE1  sing Y N 424 
PHE   CD1 HD1  sing N N 425 
PHE   CD2 CE2  doub Y N 426 
PHE   CD2 HD2  sing N N 427 
PHE   CE1 CZ   doub Y N 428 
PHE   CE1 HE1  sing N N 429 
PHE   CE2 CZ   sing Y N 430 
PHE   CE2 HE2  sing N N 431 
PHE   CZ  HZ   sing N N 432 
PHE   OXT HXT  sing N N 433 
PRO   N   CA   sing N N 434 
PRO   N   CD   sing N N 435 
PRO   N   H    sing N N 436 
PRO   CA  C    sing N N 437 
PRO   CA  CB   sing N N 438 
PRO   CA  HA   sing N N 439 
PRO   C   O    doub N N 440 
PRO   C   OXT  sing N N 441 
PRO   CB  CG   sing N N 442 
PRO   CB  HB2  sing N N 443 
PRO   CB  HB3  sing N N 444 
PRO   CG  CD   sing N N 445 
PRO   CG  HG2  sing N N 446 
PRO   CG  HG3  sing N N 447 
PRO   CD  HD2  sing N N 448 
PRO   CD  HD3  sing N N 449 
PRO   OXT HXT  sing N N 450 
SER   N   CA   sing N N 451 
SER   N   H    sing N N 452 
SER   N   H2   sing N N 453 
SER   CA  C    sing N N 454 
SER   CA  CB   sing N N 455 
SER   CA  HA   sing N N 456 
SER   C   O    doub N N 457 
SER   C   OXT  sing N N 458 
SER   CB  OG   sing N N 459 
SER   CB  HB2  sing N N 460 
SER   CB  HB3  sing N N 461 
SER   OG  HG   sing N N 462 
SER   OXT HXT  sing N N 463 
THR   N   CA   sing N N 464 
THR   N   H    sing N N 465 
THR   N   H2   sing N N 466 
THR   CA  C    sing N N 467 
THR   CA  CB   sing N N 468 
THR   CA  HA   sing N N 469 
THR   C   O    doub N N 470 
THR   C   OXT  sing N N 471 
THR   CB  OG1  sing N N 472 
THR   CB  CG2  sing N N 473 
THR   CB  HB   sing N N 474 
THR   OG1 HG1  sing N N 475 
THR   CG2 HG21 sing N N 476 
THR   CG2 HG22 sing N N 477 
THR   CG2 HG23 sing N N 478 
THR   OXT HXT  sing N N 479 
TRP   N   CA   sing N N 480 
TRP   N   H    sing N N 481 
TRP   N   H2   sing N N 482 
TRP   CA  C    sing N N 483 
TRP   CA  CB   sing N N 484 
TRP   CA  HA   sing N N 485 
TRP   C   O    doub N N 486 
TRP   C   OXT  sing N N 487 
TRP   CB  CG   sing N N 488 
TRP   CB  HB2  sing N N 489 
TRP   CB  HB3  sing N N 490 
TRP   CG  CD1  doub Y N 491 
TRP   CG  CD2  sing Y N 492 
TRP   CD1 NE1  sing Y N 493 
TRP   CD1 HD1  sing N N 494 
TRP   CD2 CE2  doub Y N 495 
TRP   CD2 CE3  sing Y N 496 
TRP   NE1 CE2  sing Y N 497 
TRP   NE1 HE1  sing N N 498 
TRP   CE2 CZ2  sing Y N 499 
TRP   CE3 CZ3  doub Y N 500 
TRP   CE3 HE3  sing N N 501 
TRP   CZ2 CH2  doub Y N 502 
TRP   CZ2 HZ2  sing N N 503 
TRP   CZ3 CH2  sing Y N 504 
TRP   CZ3 HZ3  sing N N 505 
TRP   CH2 HH2  sing N N 506 
TRP   OXT HXT  sing N N 507 
TYR   N   CA   sing N N 508 
TYR   N   H    sing N N 509 
TYR   N   H2   sing N N 510 
TYR   CA  C    sing N N 511 
TYR   CA  CB   sing N N 512 
TYR   CA  HA   sing N N 513 
TYR   C   O    doub N N 514 
TYR   C   OXT  sing N N 515 
TYR   CB  CG   sing N N 516 
TYR   CB  HB2  sing N N 517 
TYR   CB  HB3  sing N N 518 
TYR   CG  CD1  doub Y N 519 
TYR   CG  CD2  sing Y N 520 
TYR   CD1 CE1  sing Y N 521 
TYR   CD1 HD1  sing N N 522 
TYR   CD2 CE2  doub Y N 523 
TYR   CD2 HD2  sing N N 524 
TYR   CE1 CZ   doub Y N 525 
TYR   CE1 HE1  sing N N 526 
TYR   CE2 CZ   sing Y N 527 
TYR   CE2 HE2  sing N N 528 
TYR   CZ  OH   sing N N 529 
TYR   OH  HH   sing N N 530 
TYR   OXT HXT  sing N N 531 
VAL   N   CA   sing N N 532 
VAL   N   H    sing N N 533 
VAL   N   H2   sing N N 534 
VAL   CA  C    sing N N 535 
VAL   CA  CB   sing N N 536 
VAL   CA  HA   sing N N 537 
VAL   C   O    doub N N 538 
VAL   C   OXT  sing N N 539 
VAL   CB  CG1  sing N N 540 
VAL   CB  CG2  sing N N 541 
VAL   CB  HB   sing N N 542 
VAL   CG1 HG11 sing N N 543 
VAL   CG1 HG12 sing N N 544 
VAL   CG1 HG13 sing N N 545 
VAL   CG2 HG21 sing N N 546 
VAL   CG2 HG22 sing N N 547 
VAL   CG2 HG23 sing N N 548 
VAL   OXT HXT  sing N N 549 
# 
_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                    9CW3 
_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]   0.008442 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019211 
_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]   0.006069 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ARG   A  1 3   ? -51.133 28.125  -20.945  1.00 97.53  ? 304  ARG   A N   1 
ATOM   2     C  CA  . ARG   A  1 3   ? -50.758 29.206  -21.851  1.00 101.06 ? 304  ARG   A CA  1 
ATOM   3     C  C   . ARG   A  1 3   ? -49.231 29.333  -21.960  1.00 100.60 ? 304  ARG   A C   1 
ATOM   4     O  O   . ARG   A  1 3   ? -48.709 29.854  -22.949  1.00 106.07 ? 304  ARG   A O   1 
ATOM   5     C  CB  . ARG   A  1 3   ? -51.381 30.524  -21.392  1.00 105.85 ? 304  ARG   A CB  1 
ATOM   6     C  CG  . ARG   A  1 3   ? -51.127 31.711  -22.308  1.00 113.92 ? 304  ARG   A CG  1 
ATOM   7     C  CD  . ARG   A  1 3   ? -52.040 32.875  -21.947  1.00 126.36 ? 304  ARG   A CD  1 
ATOM   8     N  NE  . ARG   A  1 3   ? -51.417 34.175  -22.189  1.00 136.18 ? 304  ARG   A NE  1 
ATOM   9     C  CZ  . ARG   A  1 3   ? -50.993 34.994  -21.229  1.00 141.31 ? 304  ARG   A CZ  1 
ATOM   10    N  NH1 . ARG   A  1 3   ? -51.126 34.653  -19.953  1.00 138.81 ? 304  ARG   A NH1 1 
ATOM   11    N  NH2 . ARG   A  1 3   ? -50.437 36.158  -21.543  1.00 144.43 ? 304  ARG   A NH2 1 
ATOM   12    N  N   . PHE   A  1 4   ? -48.520 28.845  -20.945  1.00 90.31  ? 305  PHE   A N   1 
ATOM   13    C  CA  . PHE   A  1 4   ? -47.064 28.833  -20.941  1.00 80.38  ? 305  PHE   A CA  1 
ATOM   14    C  C   . PHE   A  1 4   ? -46.593 27.628  -20.140  1.00 67.76  ? 305  PHE   A C   1 
ATOM   15    O  O   . PHE   A  1 4   ? -47.254 27.204  -19.190  1.00 63.97  ? 305  PHE   A O   1 
ATOM   16    C  CB  . PHE   A  1 4   ? -46.469 30.118  -20.340  1.00 90.40  ? 305  PHE   A CB  1 
ATOM   17    C  CG  . PHE   A  1 4   ? -46.740 31.369  -21.149  1.00 103.77 ? 305  PHE   A CG  1 
ATOM   18    C  CD1 . PHE   A  1 4   ? -45.905 31.735  -22.200  1.00 103.27 ? 305  PHE   A CD1 1 
ATOM   19    C  CD2 . PHE   A  1 4   ? -47.817 32.196  -20.844  1.00 111.20 ? 305  PHE   A CD2 1 
ATOM   20    C  CE1 . PHE   A  1 4   ? -46.145 32.896  -22.943  1.00 101.19 ? 305  PHE   A CE1 1 
ATOM   21    C  CE2 . PHE   A  1 4   ? -48.064 33.357  -21.585  1.00 109.53 ? 305  PHE   A CE2 1 
ATOM   22    C  CZ  . PHE   A  1 4   ? -47.224 33.703  -22.635  1.00 103.53 ? 305  PHE   A CZ  1 
ATOM   23    N  N   . LEU   A  1 5   ? -45.451 27.069  -20.539  1.00 58.58  ? 306  LEU   A N   1 
ATOM   24    C  CA  . LEU   A  1 5   ? -44.801 25.995  -19.800  1.00 49.88  ? 306  LEU   A CA  1 
ATOM   25    C  C   . LEU   A  1 5   ? -43.313 26.281  -19.738  1.00 52.29  ? 306  LEU   A C   1 
ATOM   26    O  O   . LEU   A  1 5   ? -42.729 26.748  -20.717  1.00 59.23  ? 306  LEU   A O   1 
ATOM   27    C  CB  . LEU   A  1 5   ? -45.041 24.632  -20.446  1.00 45.19  ? 306  LEU   A CB  1 
ATOM   28    C  CG  . LEU   A  1 5   ? -46.420 24.028  -20.192  1.00 48.16  ? 306  LEU   A CG  1 
ATOM   29    C  CD1 . LEU   A  1 5   ? -46.620 22.711  -20.940  1.00 44.42  ? 306  LEU   A CD1 1 
ATOM   30    C  CD2 . LEU   A  1 5   ? -46.606 23.837  -18.689  1.00 49.24  ? 306  LEU   A CD2 1 
ATOM   31    N  N   . LYS   A  1 6   ? -42.700 26.019  -18.591  1.00 55.91  ? 307  LYS   A N   1 
ATOM   32    C  CA  . LYS   A  1 6   ? -41.280 26.284  -18.410  1.00 50.32  ? 307  LYS   A CA  1 
ATOM   33    C  C   . LYS   A  1 6   ? -40.506 24.982  -18.280  1.00 42.81  ? 307  LYS   A C   1 
ATOM   34    O  O   . LYS   A  1 6   ? -40.995 24.007  -17.695  1.00 45.28  ? 307  LYS   A O   1 
ATOM   35    C  CB  . LYS   A  1 6   ? -41.024 27.170  -17.188  1.00 52.86  ? 307  LYS   A CB  1 
ATOM   36    C  CG  . LYS   A  1 6   ? -41.287 28.647  -17.430  1.00 59.62  ? 307  LYS   A CG  1 
ATOM   37    C  CD  . LYS   A  1 6   ? -40.845 29.471  -16.236  1.00 71.94  ? 307  LYS   A CD  1 
ATOM   38    C  CE  . LYS   A  1 6   ? -41.564 30.805  -16.186  1.00 79.64  ? 307  LYS   A CE  1 
ATOM   39    N  NZ  . LYS   A  1 6   ? -41.453 31.520  -17.486  1.00 82.17  ? 307  LYS   A NZ  1 
ATOM   40    N  N   . VAL   A  1 7   ? -39.312 24.969  -18.865  1.00 41.03  ? 308  VAL   A N   1 
ATOM   41    C  CA  . VAL   A  1 7   ? -38.347 23.892  -18.705  1.00 41.76  ? 308  VAL   A CA  1 
ATOM   42    C  C   . VAL   A  1 7   ? -37.062 24.522  -18.198  1.00 44.09  ? 308  VAL   A C   1 
ATOM   43    O  O   . VAL   A  1 7   ? -36.742 25.672  -18.514  1.00 50.08  ? 308  VAL   A O   1 
ATOM   44    C  CB  . VAL   A  1 7   ? -38.074 23.087  -20.005  1.00 36.92  ? 308  VAL   A CB  1 
ATOM   45    C  CG1 . VAL   A  1 7   ? -39.310 22.336  -20.441  1.00 37.35  ? 308  VAL   A CG1 1 
ATOM   46    C  CG2 . VAL   A  1 7   ? -37.536 23.994  -21.134  1.00 39.19  ? 308  VAL   A CG2 1 
ATOM   47    N  N   . LYS   A  1 8   ? -36.316 23.752  -17.423  1.00 44.78  ? 309  LYS   A N   1 
ATOM   48    C  CA  . LYS   A  1 8   ? -35.135 24.243  -16.737  1.00 45.45  ? 309  LYS   A CA  1 
ATOM   49    C  C   . LYS   A  1 8   ? -33.973 23.287  -16.969  1.00 46.73  ? 309  LYS   A C   1 
ATOM   50    O  O   . LYS   A  1 8   ? -34.147 22.064  -16.946  1.00 44.64  ? 309  LYS   A O   1 
ATOM   51    C  CB  . LYS   A  1 8   ? -35.425 24.402  -15.235  1.00 39.35  ? 309  LYS   A CB  1 
ATOM   52    C  CG  . LYS   A  1 8   ? -34.215 24.704  -14.372  1.00 49.87  ? 309  LYS   A CG  1 
ATOM   53    C  CD  . LYS   A  1 8   ? -34.615 24.980  -12.917  1.00 47.99  ? 309  LYS   A CD  1 
ATOM   54    C  CE  . LYS   A  1 8   ? -33.415 25.426  -12.089  1.00 54.68  ? 309  LYS   A CE  1 
ATOM   55    N  NZ  . LYS   A  1 8   ? -33.644 25.315  -10.611  1.00 55.26  ? 309  LYS   A NZ  1 
ATOM   56    N  N   . ASN   A  1 9   ? -32.793 23.851  -17.212  1.00 49.27  ? 310  ASN   A N   1 
ATOM   57    C  CA  . ASN   A  1 9   ? -31.556 23.083  -17.213  1.00 47.12  ? 310  ASN   A CA  1 
ATOM   58    C  C   . ASN   A  1 9   ? -30.980 23.146  -15.808  1.00 46.92  ? 310  ASN   A C   1 
ATOM   59    O  O   . ASN   A  1 9   ? -30.681 24.233  -15.305  1.00 47.68  ? 310  ASN   A O   1 
ATOM   60    C  CB  . ASN   A  1 9   ? -30.553 23.619  -18.239  1.00 45.16  ? 310  ASN   A CB  1 
ATOM   61    C  CG  . ASN   A  1 9   ? -29.358 22.685  -18.436  1.00 47.53  ? 310  ASN   A CG  1 
ATOM   62    O  OD1 . ASN   A  1 9   ? -28.556 22.476  -17.518  1.00 44.38  ? 310  ASN   A OD1 1 
ATOM   63    N  ND2 . ASN   A  1 9   ? -29.233 22.127  -19.639  1.00 51.60  ? 310  ASN   A ND2 1 
ATOM   64    N  N   . TRP   A  1 10  ? -30.849 21.984  -15.170  1.00 49.48  ? 311  TRP   A N   1 
ATOM   65    C  CA  . TRP   A  1 10  ? -30.473 21.924  -13.762  1.00 44.53  ? 311  TRP   A CA  1 
ATOM   66    C  C   . TRP   A  1 10  ? -28.975 22.051  -13.532  1.00 44.85  ? 311  TRP   A C   1 
ATOM   67    O  O   . TRP   A  1 10  ? -28.556 22.220  -12.384  1.00 44.48  ? 311  TRP   A O   1 
ATOM   68    C  CB  . TRP   A  1 10  ? -31.010 20.632  -13.149  1.00 40.97  ? 311  TRP   A CB  1 
ATOM   69    C  CG  . TRP   A  1 10  ? -32.484 20.737  -12.914  1.00 43.60  ? 311  TRP   A CG  1 
ATOM   70    C  CD1 . TRP   A  1 10  ? -33.479 20.374  -13.769  1.00 41.42  ? 311  TRP   A CD1 1 
ATOM   71    C  CD2 . TRP   A  1 10  ? -33.129 21.290  -11.760  1.00 42.58  ? 311  TRP   A CD2 1 
ATOM   72    N  NE1 . TRP   A  1 10  ? -34.712 20.648  -13.213  1.00 39.78  ? 311  TRP   A NE1 1 
ATOM   73    C  CE2 . TRP   A  1 10  ? -34.522 21.208  -11.977  1.00 38.79  ? 311  TRP   A CE2 1 
ATOM   74    C  CE3 . TRP   A  1 10  ? -32.667 21.831  -10.560  1.00 54.81  ? 311  TRP   A CE3 1 
ATOM   75    C  CZ2 . TRP   A  1 10  ? -35.453 21.656  -11.044  1.00 44.07  ? 311  TRP   A CZ2 1 
ATOM   76    C  CZ3 . TRP   A  1 10  ? -33.601 22.269  -9.622   1.00 53.72  ? 311  TRP   A CZ3 1 
ATOM   77    C  CH2 . TRP   A  1 10  ? -34.974 22.178  -9.872   1.00 47.85  ? 311  TRP   A CH2 1 
ATOM   78    N  N   . GLU   A  1 11  ? -28.170 21.972  -14.590  1.00 41.40  ? 312  GLU   A N   1 
ATOM   79    C  CA  . GLU   A  1 11  ? -26.736 22.227  -14.567  1.00 49.66  ? 312  GLU   A CA  1 
ATOM   80    C  C   . GLU   A  1 11  ? -26.409 23.716  -14.733  1.00 54.59  ? 312  GLU   A C   1 
ATOM   81    O  O   . GLU   A  1 11  ? -25.520 24.230  -14.043  1.00 56.61  ? 312  GLU   A O   1 
ATOM   82    C  CB  . GLU   A  1 11  ? -26.057 21.402  -15.673  1.00 53.03  ? 312  GLU   A CB  1 
ATOM   83    C  CG  . GLU   A  1 11  ? -24.547 21.454  -15.674  1.00 55.68  ? 312  GLU   A CG  1 
ATOM   84    C  CD  . GLU   A  1 11  ? -23.924 20.848  -16.921  1.00 58.14  ? 312  GLU   A CD  1 
ATOM   85    O  OE1 . GLU   A  1 11  ? -24.662 20.425  -17.842  1.00 56.41  ? 312  GLU   A OE1 1 
ATOM   86    O  OE2 . GLU   A  1 11  ? -22.679 20.809  -16.979  1.00 63.22  ? 312  GLU   A OE2 1 
ATOM   87    N  N   . THR   A  1 12  ? -27.130 24.423  -15.616  1.00 47.62  ? 313  THR   A N   1 
ATOM   88    C  CA  . THR   A  1 12  ? -26.846 25.814  -15.963  1.00 43.20  ? 313  THR   A CA  1 
ATOM   89    C  C   . THR   A  1 12  ? -27.787 26.830  -15.331  1.00 52.89  ? 313  THR   A C   1 
ATOM   90    O  O   . THR   A  1 12  ? -27.463 28.020  -15.340  1.00 61.72  ? 313  THR   A O   1 
ATOM   91    C  CB  . THR   A  1 12  ? -26.946 26.036  -17.475  1.00 46.09  ? 313  THR   A CB  1 
ATOM   92    O  OG1 . THR   A  1 12  ? -28.324 25.977  -17.854  1.00 50.96  ? 313  THR   A OG1 1 
ATOM   93    C  CG2 . THR   A  1 12  ? -26.166 24.989  -18.241  1.00 46.88  ? 313  THR   A CG2 1 
ATOM   94    N  N   . GLU   A  1 13  ? -28.958 26.411  -14.853  1.00 53.54  ? 314  GLU   A N   1 
ATOM   95    C  CA  . GLU   A  1 13  ? -30.052 27.241  -14.319  1.00 51.84  ? 314  GLU   A CA  1 
ATOM   96    C  C   . GLU   A  1 13  ? -30.865 27.934  -15.418  1.00 54.68  ? 314  GLU   A C   1 
ATOM   97    O  O   . GLU   A  1 13  ? -31.843 28.626  -15.078  1.00 52.78  ? 314  GLU   A O   1 
ATOM   98    C  CB  . GLU   A  1 13  ? -29.575 28.314  -13.324  1.00 63.97  ? 314  GLU   A CB  1 
ATOM   99    C  CG  . GLU   A  1 13  ? -28.704 27.810  -12.178  1.00 66.61  ? 314  GLU   A CG  1 
ATOM   100   C  CD  . GLU   A  1 13  ? -29.502 27.480  -10.938  1.00 78.97  ? 314  GLU   A CD  1 
ATOM   101   O  OE1 . GLU   A  1 13  ? -30.516 26.756  -11.048  1.00 84.87  ? 314  GLU   A OE1 1 
ATOM   102   O  OE2 . GLU   A  1 13  ? -29.121 27.953  -9.849   1.00 84.08  ? 314  GLU   A OE2 1 
ATOM   103   N  N   . VAL   A  1 14  ? -30.518 27.768  -16.705  1.00 48.80  ? 315  VAL   A N   1 
ATOM   104   C  CA  . VAL   A  1 14  ? -31.276 28.387  -17.790  1.00 52.63  ? 315  VAL   A CA  1 
ATOM   105   C  C   . VAL   A  1 14  ? -32.710 27.872  -17.791  1.00 56.00  ? 315  VAL   A C   1 
ATOM   106   O  O   . VAL   A  1 14  ? -32.959 26.669  -17.633  1.00 56.66  ? 315  VAL   A O   1 
ATOM   107   C  CB  . VAL   A  1 14  ? -30.599 28.107  -19.146  1.00 55.76  ? 315  VAL   A CB  1 
ATOM   108   C  CG1 . VAL   A  1 14  ? -31.464 28.599  -20.312  1.00 49.03  ? 315  VAL   A CG1 1 
ATOM   109   C  CG2 . VAL   A  1 14  ? -29.222 28.744  -19.209  1.00 57.09  ? 315  VAL   A CG2 1 
ATOM   110   N  N   . VAL   A  1 15  ? -33.665 28.781  -17.994  1.00 57.56  ? 316  VAL   A N   1 
ATOM   111   C  CA  . VAL   A  1 15  ? -35.081 28.432  -18.054  1.00 55.66  ? 316  VAL   A CA  1 
ATOM   112   C  C   . VAL   A  1 15  ? -35.687 28.954  -19.353  1.00 51.61  ? 316  VAL   A C   1 
ATOM   113   O  O   . VAL   A  1 15  ? -35.577 30.145  -19.663  1.00 53.11  ? 316  VAL   A O   1 
ATOM   114   C  CB  . VAL   A  1 15  ? -35.859 28.983  -16.845  1.00 49.90  ? 316  VAL   A CB  1 
ATOM   115   C  CG1 . VAL   A  1 15  ? -37.308 28.506  -16.904  1.00 45.92  ? 316  VAL   A CG1 1 
ATOM   116   C  CG2 . VAL   A  1 15  ? -35.190 28.561  -15.542  1.00 47.79  ? 316  VAL   A CG2 1 
ATOM   117   N  N   . LEU   A  1 16  ? -36.356 28.068  -20.089  1.00 56.03  ? 317  LEU   A N   1 
ATOM   118   C  CA  . LEU   A  1 16  ? -36.997 28.379  -21.360  1.00 48.76  ? 317  LEU   A CA  1 
ATOM   119   C  C   . LEU   A  1 16  ? -38.508 28.240  -21.236  1.00 47.19  ? 317  LEU   A C   1 
ATOM   120   O  O   . LEU   A  1 16  ? -39.014 27.508  -20.379  1.00 48.07  ? 317  LEU   A O   1 
ATOM   121   C  CB  . LEU   A  1 16  ? -36.493 27.455  -22.464  1.00 40.14  ? 317  LEU   A CB  1 
ATOM   122   C  CG  . LEU   A  1 16  ? -34.986 27.248  -22.424  1.00 42.63  ? 317  LEU   A CG  1 
ATOM   123   C  CD1 . LEU   A  1 16  ? -34.554 26.102  -23.374  1.00 33.43  ? 317  LEU   A CD1 1 
ATOM   124   C  CD2 . LEU   A  1 16  ? -34.277 28.559  -22.739  1.00 46.81  ? 317  LEU   A CD2 1 
ATOM   125   N  N   . THR   A  1 17  ? -39.228 28.949  -22.099  1.00 38.96  ? 318  THR   A N   1 
ATOM   126   C  CA  . THR   A  1 17  ? -40.680 29.021  -22.029  1.00 43.95  ? 318  THR   A CA  1 
ATOM   127   C  C   . THR   A  1 17  ? -41.276 28.449  -23.306  1.00 50.41  ? 318  THR   A C   1 
ATOM   128   O  O   . THR   A  1 17  ? -41.117 29.028  -24.385  1.00 53.71  ? 318  THR   A O   1 
ATOM   129   C  CB  . THR   A  1 17  ? -41.151 30.459  -21.829  1.00 46.49  ? 318  THR   A CB  1 
ATOM   130   O  OG1 . THR   A  1 17  ? -40.550 30.998  -20.651  1.00 50.41  ? 318  THR   A OG1 1 
ATOM   131   C  CG2 . THR   A  1 17  ? -42.662 30.508  -21.706  1.00 40.83  ? 318  THR   A CG2 1 
ATOM   132   N  N   . ASP   A  1 18  ? -41.992 27.338  -23.175  1.00 48.75  ? 319  ASP   A N   1 
ATOM   133   C  CA  . ASP   A  1 18  ? -42.562 26.646  -24.319  1.00 47.47  ? 319  ASP   A CA  1 
ATOM   134   C  C   . ASP   A  1 18  ? -43.986 27.138  -24.547  1.00 49.65  ? 319  ASP   A C   1 
ATOM   135   O  O   . ASP   A  1 18  ? -44.888 26.856  -23.747  1.00 46.34  ? 319  ASP   A O   1 
ATOM   136   C  CB  . ASP   A  1 18  ? -42.526 25.140  -24.094  1.00 45.43  ? 319  ASP   A CB  1 
ATOM   137   C  CG  . ASP   A  1 18  ? -42.891 24.364  -25.333  1.00 45.06  ? 319  ASP   A CG  1 
ATOM   138   O  OD1 . ASP   A  1 18  ? -44.055 24.480  -25.779  1.00 49.85  ? 319  ASP   A OD1 1 
ATOM   139   O  OD2 . ASP   A  1 18  ? -42.010 23.657  -25.873  1.00 46.06  ? 319  ASP   A OD2 1 
ATOM   140   N  N   . THR   A  1 19  ? -44.185 27.883  -25.637  1.00 46.43  ? 320  THR   A N   1 
ATOM   141   C  CA  . THR   A  1 19  ? -45.523 28.203  -26.116  1.00 48.20  ? 320  THR   A CA  1 
ATOM   142   C  C   . THR   A  1 19  ? -45.942 27.347  -27.303  1.00 50.86  ? 320  THR   A C   1 
ATOM   143   O  O   . THR   A  1 19  ? -47.145 27.217  -27.556  1.00 56.47  ? 320  THR   A O   1 
ATOM   144   C  CB  . THR   A  1 19  ? -45.608 29.674  -26.525  1.00 50.74  ? 320  THR   A CB  1 
ATOM   145   O  OG1 . THR   A  1 19  ? -44.777 29.879  -27.670  1.00 53.65  ? 320  THR   A OG1 1 
ATOM   146   C  CG2 . THR   A  1 19  ? -45.130 30.578  -25.396  1.00 51.69  ? 320  THR   A CG2 1 
ATOM   147   N  N   . LEU   A  1 20  ? -44.977 26.748  -28.012  1.00 40.32  ? 321  LEU   A N   1 
ATOM   148   C  CA  . LEU   A  1 20  ? -45.260 26.015  -29.245  1.00 44.76  ? 321  LEU   A CA  1 
ATOM   149   C  C   . LEU   A  1 20  ? -46.131 24.786  -29.005  1.00 46.21  ? 321  LEU   A C   1 
ATOM   150   O  O   . LEU   A  1 20  ? -46.868 24.372  -29.907  1.00 40.97  ? 321  LEU   A O   1 
ATOM   151   C  CB  . LEU   A  1 20  ? -43.940 25.613  -29.917  1.00 39.67  ? 321  LEU   A CB  1 
ATOM   152   C  CG  . LEU   A  1 20  ? -43.940 24.641  -31.104  1.00 43.90  ? 321  LEU   A CG  1 
ATOM   153   C  CD1 . LEU   A  1 20  ? -44.709 25.225  -32.284  1.00 41.01  ? 321  LEU   A CD1 1 
ATOM   154   C  CD2 . LEU   A  1 20  ? -42.508 24.263  -31.520  1.00 41.70  ? 321  LEU   A CD2 1 
ATOM   155   N  N   . HIS   A  1 21  ? -46.081 24.206  -27.798  1.00 44.67  ? 322  HIS   A N   1 
ATOM   156   C  CA  . HIS   A  1 21  ? -46.866 23.013  -27.502  1.00 37.22  ? 322  HIS   A CA  1 
ATOM   157   C  C   . HIS   A  1 21  ? -48.357 23.234  -27.680  1.00 42.32  ? 322  HIS   A C   1 
ATOM   158   O  O   . HIS   A  1 21  ? -49.109 22.260  -27.764  1.00 47.34  ? 322  HIS   A O   1 
ATOM   159   C  CB  . HIS   A  1 21  ? -46.607 22.540  -26.068  1.00 41.33  ? 322  HIS   A CB  1 
ATOM   160   C  CG  . HIS   A  1 21  ? -47.181 23.444  -25.018  1.00 42.41  ? 322  HIS   A CG  1 
ATOM   161   N  ND1 . HIS   A  1 21  ? -46.503 24.539  -24.524  1.00 46.49  ? 322  HIS   A ND1 1 
ATOM   162   C  CD2 . HIS   A  1 21  ? -48.367 23.415  -24.371  1.00 45.22  ? 322  HIS   A CD2 1 
ATOM   163   C  CE1 . HIS   A  1 21  ? -47.253 25.153  -23.626  1.00 47.72  ? 322  HIS   A CE1 1 
ATOM   164   N  NE2 . HIS   A  1 21  ? -48.387 24.487  -23.510  1.00 48.59  ? 322  HIS   A NE2 1 
ATOM   165   N  N   . LEU   A  1 22  ? -48.809 24.488  -27.714  1.00 47.63  ? 323  LEU   A N   1 
ATOM   166   C  CA  . LEU   A  1 22  ? -50.223 24.755  -27.948  1.00 52.52  ? 323  LEU   A CA  1 
ATOM   167   C  C   . LEU   A  1 22  ? -50.643 24.385  -29.364  1.00 56.65  ? 323  LEU   A C   1 
ATOM   168   O  O   . LEU   A  1 22  ? -51.833 24.152  -29.607  1.00 56.85  ? 323  LEU   A O   1 
ATOM   169   C  CB  . LEU   A  1 22  ? -50.527 26.228  -27.660  1.00 52.41  ? 323  LEU   A CB  1 
ATOM   170   C  CG  . LEU   A  1 22  ? -50.110 26.690  -26.257  1.00 57.99  ? 323  LEU   A CG  1 
ATOM   171   C  CD1 . LEU   A  1 22  ? -50.256 28.196  -26.079  1.00 53.15  ? 323  LEU   A CD1 1 
ATOM   172   C  CD2 . LEU   A  1 22  ? -50.875 25.933  -25.163  1.00 59.15  ? 323  LEU   A CD2 1 
ATOM   173   N  N   . LYS   A  1 23  ? -49.689 24.297  -30.290  1.00 53.99  ? 324  LYS   A N   1 
ATOM   174   C  CA  . LYS   A  1 23  ? -49.969 23.943  -31.671  1.00 55.32  ? 324  LYS   A CA  1 
ATOM   175   C  C   . LYS   A  1 23  ? -50.061 22.445  -31.897  1.00 59.26  ? 324  LYS   A C   1 
ATOM   176   O  O   . LYS   A  1 23  ? -50.547 22.036  -32.952  1.00 62.85  ? 324  LYS   A O   1 
ATOM   177   C  CB  . LYS   A  1 23  ? -48.896 24.533  -32.596  1.00 51.77  ? 324  LYS   A CB  1 
ATOM   178   C  CG  . LYS   A  1 23  ? -48.971 26.056  -32.765  1.00 60.03  ? 324  LYS   A CG  1 
ATOM   179   C  CD  . LYS   A  1 23  ? -50.153 26.464  -33.636  1.00 69.57  ? 324  LYS   A CD  1 
ATOM   180   C  CE  . LYS   A  1 23  ? -51.018 27.517  -32.958  1.00 79.48  ? 324  LYS   A CE  1 
ATOM   181   N  NZ  . LYS   A  1 23  ? -50.222 28.702  -32.535  1.00 84.11  ? 324  LYS   A NZ  1 
ATOM   182   N  N   . SER   A  1 24  ? -49.613 21.619  -30.956  1.00 62.71  ? 325  SER   A N   1 
ATOM   183   C  CA  . SER   A  1 24  ? -49.700 20.179  -31.157  1.00 60.86  ? 325  SER   A CA  1 
ATOM   184   C  C   . SER   A  1 24  ? -51.160 19.748  -31.185  1.00 65.60  ? 325  SER   A C   1 
ATOM   185   O  O   . SER   A  1 24  ? -52.037 20.425  -30.646  1.00 60.93  ? 325  SER   A O   1 
ATOM   186   C  CB  . SER   A  1 24  ? -48.939 19.425  -30.064  1.00 54.82  ? 325  SER   A CB  1 
ATOM   187   O  OG  . SER   A  1 24  ? -49.682 19.358  -28.864  1.00 58.89  ? 325  SER   A OG  1 
ATOM   188   N  N   . THR   A  1 25  ? -51.427 18.618  -31.856  1.00 74.23  ? 326  THR   A N   1 
ATOM   189   C  CA  . THR   A  1 25  ? -52.817 18.193  -31.985  1.00 87.79  ? 326  THR   A CA  1 
ATOM   190   C  C   . THR   A  1 25  ? -52.985 16.680  -32.060  1.00 91.01  ? 326  THR   A C   1 
ATOM   191   O  O   . THR   A  1 25  ? -54.011 16.216  -32.570  1.00 98.84  ? 326  THR   A O   1 
ATOM   192   C  CB  . THR   A  1 25  ? -53.481 18.820  -33.232  1.00 93.12  ? 326  THR   A CB  1 
ATOM   193   O  OG1 . THR   A  1 25  ? -52.496 19.049  -34.255  1.00 94.42  ? 326  THR   A OG1 1 
ATOM   194   C  CG2 . THR   A  1 25  ? -54.208 20.126  -32.870  1.00 91.72  ? 326  THR   A CG2 1 
ATOM   195   N  N   . LEU   A  1 26  ? -52.028 15.896  -31.577  1.00 85.05  ? 327  LEU   A N   1 
ATOM   196   C  CA  . LEU   A  1 26  ? -52.147 14.452  -31.676  1.00 82.52  ? 327  LEU   A CA  1 
ATOM   197   C  C   . LEU   A  1 26  ? -51.499 13.813  -30.452  1.00 78.97  ? 327  LEU   A C   1 
ATOM   198   O  O   . LEU   A  1 26  ? -50.637 14.412  -29.803  1.00 86.07  ? 327  LEU   A O   1 
ATOM   199   C  CB  . LEU   A  1 26  ? -51.558 13.920  -33.002  1.00 82.38  ? 327  LEU   A CB  1 
ATOM   200   C  CG  . LEU   A  1 26  ? -50.460 14.542  -33.895  1.00 78.77  ? 327  LEU   A CG  1 
ATOM   201   C  CD1 . LEU   A  1 26  ? -50.344 13.750  -35.210  1.00 71.70  ? 327  LEU   A CD1 1 
ATOM   202   C  CD2 . LEU   A  1 26  ? -50.609 16.030  -34.215  1.00 78.40  ? 327  LEU   A CD2 1 
ATOM   203   N  N   . GLU   A  1 27  ? -51.939 12.593  -30.142  1.00 67.52  ? 328  GLU   A N   1 
ATOM   204   C  CA  . GLU   A  1 27  ? -51.676 11.981  -28.843  1.00 65.85  ? 328  GLU   A CA  1 
ATOM   205   C  C   . GLU   A  1 27  ? -50.189 11.753  -28.602  1.00 61.07  ? 328  GLU   A C   1 
ATOM   206   O  O   . GLU   A  1 27  ? -49.431 11.435  -29.518  1.00 66.54  ? 328  GLU   A O   1 
ATOM   207   C  CB  . GLU   A  1 27  ? -52.403 10.640  -28.729  1.00 72.10  ? 328  GLU   A CB  1 
ATOM   208   C  CG  . GLU   A  1 27  ? -53.796 10.684  -28.127  1.00 80.63  ? 328  GLU   A CG  1 
ATOM   209   C  CD  . GLU   A  1 27  ? -54.429 9.302   -28.067  1.00 92.58  ? 328  GLU   A CD  1 
ATOM   210   O  OE1 . GLU   A  1 27  ? -54.268 8.527   -29.038  1.00 96.92  ? 328  GLU   A OE1 1 
ATOM   211   O  OE2 . GLU   A  1 27  ? -55.077 8.980   -27.050  1.00 96.21  ? 328  GLU   A OE2 1 
ATOM   212   N  N   . THR   A  1 28  ? -49.780 11.903  -27.340  1.00 51.97  ? 329  THR   A N   1 
ATOM   213   C  CA  . THR   A  1 28  ? -48.485 11.408  -26.895  1.00 47.20  ? 329  THR   A CA  1 
ATOM   214   C  C   . THR   A  1 28  ? -48.555 9.987   -26.367  1.00 42.47  ? 329  THR   A C   1 
ATOM   215   O  O   . THR   A  1 28  ? -47.516 9.336   -26.252  1.00 54.43  ? 329  THR   A O   1 
ATOM   216   C  CB  . THR   A  1 28  ? -47.904 12.288  -25.775  1.00 60.03  ? 329  THR   A CB  1 
ATOM   217   O  OG1 . THR   A  1 28  ? -48.711 12.175  -24.576  1.00 56.07  ? 329  THR   A OG1 1 
ATOM   218   C  CG2 . THR   A  1 28  ? -47.803 13.742  -26.219  1.00 57.47  ? 329  THR   A CG2 1 
ATOM   219   N  N   . GLY   A  1 29  ? -49.744 9.506   -26.019  1.00 43.77  ? 330  GLY   A N   1 
ATOM   220   C  CA  . GLY   A  1 29  ? -49.908 8.243   -25.352  1.00 39.91  ? 330  GLY   A CA  1 
ATOM   221   C  C   . GLY   A  1 29  ? -50.122 8.356   -23.852  1.00 49.22  ? 330  GLY   A C   1 
ATOM   222   O  O   . GLY   A  1 29  ? -50.695 7.440   -23.247  1.00 50.90  ? 330  GLY   A O   1 
ATOM   223   N  N   . CYS   A  1 30  ? -49.705 9.459   -23.243  1.00 40.61  ? 331  CYS   A N   1 
ATOM   224   C  CA  . CYS   A  1 30  ? -49.919 9.644   -21.816  1.00 35.16  ? 331  CYS   A CA  1 
ATOM   225   C  C   . CYS   A  1 30  ? -51.356 10.070  -21.536  1.00 40.07  ? 331  CYS   A C   1 
ATOM   226   O  O   . CYS   A  1 30  ? -52.077 10.532  -22.424  1.00 42.61  ? 331  CYS   A O   1 
ATOM   227   C  CB  . CYS   A  1 30  ? -48.964 10.701  -21.262  1.00 31.62  ? 331  CYS   A CB  1 
ATOM   228   S  SG  . CYS   A  1 30  ? -47.205 10.369  -21.476  1.00 39.29  ? 331  CYS   A SG  1 
ATOM   229   N  N   . THR   A  1 31  ? -51.767 9.917   -20.277  1.00 40.78  ? 332  THR   A N   1 
ATOM   230   C  CA  . THR   A  1 31  ? -53.019 10.467  -19.775  1.00 45.76  ? 332  THR   A CA  1 
ATOM   231   C  C   . THR   A  1 31  ? -52.697 11.418  -18.627  1.00 43.40  ? 332  THR   A C   1 
ATOM   232   O  O   . THR   A  1 31  ? -51.542 11.570  -18.228  1.00 47.85  ? 332  THR   A O   1 
ATOM   233   C  CB  . THR   A  1 31  ? -53.996 9.364   -19.317  1.00 58.14  ? 332  THR   A CB  1 
ATOM   234   O  OG1 . THR   A  1 31  ? -53.685 8.949   -17.978  1.00 60.51  ? 332  THR   A OG1 1 
ATOM   235   C  CG2 . THR   A  1 31  ? -53.944 8.151   -20.244  1.00 54.30  ? 332  THR   A CG2 1 
ATOM   236   N  N   . GLU   A  1 32  ? -53.734 12.065  -18.088  1.00 37.81  ? 333  GLU   A N   1 
ATOM   237   C  CA  . GLU   A  1 32  ? -53.505 12.968  -16.964  1.00 51.44  ? 333  GLU   A CA  1 
ATOM   238   C  C   . GLU   A  1 32  ? -53.014 12.231  -15.730  1.00 53.95  ? 333  GLU   A C   1 
ATOM   239   O  O   . GLU   A  1 32  ? -52.372 12.850  -14.876  1.00 59.52  ? 333  GLU   A O   1 
ATOM   240   C  CB  . GLU   A  1 32  ? -54.774 13.761  -16.641  1.00 56.54  ? 333  GLU   A CB  1 
ATOM   241   C  CG  . GLU   A  1 32  ? -55.319 14.488  -17.863  1.00 68.49  ? 333  GLU   A CG  1 
ATOM   242   C  CD  . GLU   A  1 32  ? -56.276 15.604  -17.524  1.00 76.45  ? 333  GLU   A CD  1 
ATOM   243   O  OE1 . GLU   A  1 32  ? -55.873 16.788  -17.631  1.00 75.63  ? 333  GLU   A OE1 1 
ATOM   244   O  OE2 . GLU   A  1 32  ? -57.432 15.292  -17.163  1.00 81.64  ? 333  GLU   A OE2 1 
ATOM   245   N  N   . TYR   A  1 33  ? -53.261 10.919  -15.631  1.00 52.99  ? 334  TYR   A N   1 
ATOM   246   C  CA  . TYR   A  1 33  ? -52.884 10.168  -14.443  1.00 48.67  ? 334  TYR   A CA  1 
ATOM   247   C  C   . TYR   A  1 33  ? -51.848 9.081   -14.683  1.00 47.54  ? 334  TYR   A C   1 
ATOM   248   O  O   . TYR   A  1 33  ? -51.471 8.402   -13.728  1.00 50.10  ? 334  TYR   A O   1 
ATOM   249   C  CB  . TYR   A  1 33  ? -54.126 9.551   -13.782  1.00 45.83  ? 334  TYR   A CB  1 
ATOM   250   C  CG  . TYR   A  1 33  ? -55.018 10.599  -13.148  1.00 61.15  ? 334  TYR   A CG  1 
ATOM   251   C  CD1 . TYR   A  1 33  ? -54.808 11.022  -11.843  1.00 56.79  ? 334  TYR   A CD1 1 
ATOM   252   C  CD2 . TYR   A  1 33  ? -56.055 11.181  -13.866  1.00 62.73  ? 334  TYR   A CD2 1 
ATOM   253   C  CE1 . TYR   A  1 33  ? -55.610 11.987  -11.276  1.00 68.71  ? 334  TYR   A CE1 1 
ATOM   254   C  CE2 . TYR   A  1 33  ? -56.858 12.143  -13.308  1.00 61.18  ? 334  TYR   A CE2 1 
ATOM   255   C  CZ  . TYR   A  1 33  ? -56.636 12.541  -12.013  1.00 72.28  ? 334  TYR   A CZ  1 
ATOM   256   O  OH  . TYR   A  1 33  ? -57.437 13.505  -11.449  1.00 81.85  ? 334  TYR   A OH  1 
ATOM   257   N  N   . ILE   A  1 34  ? -51.360 8.888   -15.907  1.00 55.64  ? 335  ILE   A N   1 
ATOM   258   C  CA  . ILE   A  1 34  ? -50.262 7.945   -16.098  1.00 51.80  ? 335  ILE   A CA  1 
ATOM   259   C  C   . ILE   A  1 34  ? -49.367 8.430   -17.224  1.00 52.98  ? 335  ILE   A C   1 
ATOM   260   O  O   . ILE   A  1 34  ? -49.843 8.878   -18.270  1.00 64.61  ? 335  ILE   A O   1 
ATOM   261   C  CB  . ILE   A  1 34  ? -50.775 6.499   -16.312  1.00 58.52  ? 335  ILE   A CB  1 
ATOM   262   C  CG1 . ILE   A  1 34  ? -49.884 5.735   -17.277  1.00 66.71  ? 335  ILE   A CG1 1 
ATOM   263   C  CG2 . ILE   A  1 34  ? -52.255 6.445   -16.703  1.00 59.64  ? 335  ILE   A CG2 1 
ATOM   264   C  CD1 . ILE   A  1 34  ? -49.906 4.277   -16.995  1.00 73.39  ? 335  ILE   A CD1 1 
ATOM   265   N  N   . CYS   A  1 35  ? -48.059 8.373   -16.987  1.00 44.98  ? 336  CYS   A N   1 
ATOM   266   C  CA  . CYS   A  1 35  ? -47.062 8.749   -17.982  1.00 42.51  ? 336  CYS   A CA  1 
ATOM   267   C  C   . CYS   A  1 35  ? -46.579 7.499   -18.699  1.00 42.61  ? 336  CYS   A C   1 
ATOM   268   O  O   . CYS   A  1 35  ? -46.260 6.492   -18.052  1.00 39.38  ? 336  CYS   A O   1 
ATOM   269   C  CB  . CYS   A  1 35  ? -45.879 9.472   -17.335  1.00 38.59  ? 336  CYS   A CB  1 
ATOM   270   S  SG  . CYS   A  1 35  ? -44.574 9.986   -18.475  1.00 40.32  ? 336  CYS   A SG  1 
ATOM   271   N  N   . MET   A  1 36  ? -46.553 7.560   -20.034  1.00 38.89  ? 337  MET   A N   1 
ATOM   272   C  CA  . MET   A  1 36  ? -46.043 6.483   -20.878  1.00 41.28  ? 337  MET   A CA  1 
ATOM   273   C  C   . MET   A  1 36  ? -44.801 6.928   -21.638  1.00 43.35  ? 337  MET   A C   1 
ATOM   274   O  O   . MET   A  1 36  ? -44.528 6.441   -22.739  1.00 42.63  ? 337  MET   A O   1 
ATOM   275   C  CB  . MET   A  1 36  ? -47.128 5.982   -21.831  1.00 42.33  ? 337  MET   A CB  1 
ATOM   276   C  CG  . MET   A  1 36  ? -48.399 5.629   -21.086  1.00 56.65  ? 337  MET   A CG  1 
ATOM   277   S  SD  . MET   A  1 36  ? -49.457 4.422   -21.881  1.00 65.52  ? 337  MET   A SD  1 
ATOM   278   C  CE  . MET   A  1 36  ? -51.058 4.941   -21.257  1.00 69.85  ? 337  MET   A CE  1 
ATOM   279   N  N   . GLY   A  1 37  ? -44.039 7.844   -21.028  1.00 35.61  ? 338  GLY   A N   1 
ATOM   280   C  CA  . GLY   A  1 37  ? -42.835 8.379   -21.638  1.00 37.19  ? 338  GLY   A CA  1 
ATOM   281   C  C   . GLY   A  1 37  ? -41.797 7.368   -22.092  1.00 36.23  ? 338  GLY   A C   1 
ATOM   282   O  O   . GLY   A  1 37  ? -40.974 7.685   -22.952  1.00 46.89  ? 338  GLY   A O   1 
ATOM   283   N  N   . SER   A  1 38  ? -41.795 6.156   -21.531  1.00 31.58  ? 339  SER   A N   1 
ATOM   284   C  CA  . SER   A  1 38  ? -40.813 5.149   -21.944  1.00 35.89  ? 339  SER   A CA  1 
ATOM   285   C  C   . SER   A  1 38  ? -41.405 4.018   -22.793  1.00 37.00  ? 339  SER   A C   1 
ATOM   286   O  O   . SER   A  1 38  ? -40.699 3.051   -23.096  1.00 43.78  ? 339  SER   A O   1 
ATOM   287   C  CB  . SER   A  1 38  ? -40.084 4.556   -20.724  1.00 38.44  ? 339  SER   A CB  1 
ATOM   288   O  OG  . SER   A  1 38  ? -40.939 3.808   -19.860  1.00 33.63  ? 339  SER   A OG  1 
ATOM   289   N  N   . ILE   A  1 39  ? -42.678 4.105   -23.172  1.00 34.18  ? 340  ILE   A N   1 
ATOM   290   C  CA  . ILE   A  1 39  ? -43.270 3.136   -24.089  1.00 39.52  ? 340  ILE   A CA  1 
ATOM   291   C  C   . ILE   A  1 39  ? -42.747 3.411   -25.500  1.00 40.20  ? 340  ILE   A C   1 
ATOM   292   O  O   . ILE   A  1 39  ? -42.748 4.564   -25.969  1.00 38.57  ? 340  ILE   A O   1 
ATOM   293   C  CB  . ILE   A  1 39  ? -44.805 3.223   -24.032  1.00 45.56  ? 340  ILE   A CB  1 
ATOM   294   C  CG1 . ILE   A  1 39  ? -45.316 3.010   -22.596  1.00 44.33  ? 340  ILE   A CG1 1 
ATOM   295   C  CG2 . ILE   A  1 39  ? -45.464 2.302   -25.090  1.00 38.79  ? 340  ILE   A CG2 1 
ATOM   296   C  CD1 . ILE   A  1 39  ? -44.793 1.777   -21.914  1.00 44.86  ? 340  ILE   A CD1 1 
ATOM   297   N  N   . MET   A  1 40  ? -42.271 2.363   -26.179  1.00 38.30  ? 341  MET   A N   1 
ATOM   298   C  CA  . MET   A  1 40  ? -41.645 2.597   -27.484  1.00 47.35  ? 341  MET   A CA  1 
ATOM   299   C  C   . MET   A  1 40  ? -42.666 2.991   -28.548  1.00 49.63  ? 341  MET   A C   1 
ATOM   300   O  O   . MET   A  1 40  ? -42.448 3.956   -29.290  1.00 59.75  ? 341  MET   A O   1 
ATOM   301   C  CB  . MET   A  1 40  ? -40.845 1.393   -27.947  1.00 54.05  ? 341  MET   A CB  1 
ATOM   302   C  CG  . MET   A  1 40  ? -39.904 1.825   -29.067  1.00 66.78  ? 341  MET   A CG  1 
ATOM   303   S  SD  . MET   A  1 40  ? -38.621 0.641   -29.433  1.00 81.15  ? 341  MET   A SD  1 
ATOM   304   C  CE  . MET   A  1 40  ? -37.882 0.396   -27.826  1.00 73.12  ? 341  MET   A CE  1 
ATOM   305   N  N   . HIS   A  1 41  ? -43.779 2.260   -28.650  1.00 53.08  ? 342  HIS   A N   1 
ATOM   306   C  CA  . HIS   A  1 41  ? -44.870 2.606   -29.569  1.00 59.55  ? 342  HIS   A CA  1 
ATOM   307   C  C   . HIS   A  1 41  ? -46.187 2.625   -28.802  1.00 59.43  ? 342  HIS   A C   1 
ATOM   308   O  O   . HIS   A  1 41  ? -46.844 1.585   -28.669  1.00 59.71  ? 342  HIS   A O   1 
ATOM   309   C  CB  . HIS   A  1 41  ? -44.978 1.618   -30.735  1.00 65.94  ? 342  HIS   A CB  1 
ATOM   310   C  CG  . HIS   A  1 41  ? -43.667 1.181   -31.325  1.00 76.70  ? 342  HIS   A CG  1 
ATOM   311   N  ND1 . HIS   A  1 41  ? -42.829 2.034   -32.012  1.00 77.16  ? 342  HIS   A ND1 1 
ATOM   312   C  CD2 . HIS   A  1 41  ? -43.080 -0.040  -31.376  1.00 78.94  ? 342  HIS   A CD2 1 
ATOM   313   C  CE1 . HIS   A  1 41  ? -41.767 1.366   -32.428  1.00 75.87  ? 342  HIS   A CE1 1 
ATOM   314   N  NE2 . HIS   A  1 41  ? -41.896 0.104   -32.058  1.00 76.96  ? 342  HIS   A NE2 1 
ATOM   315   N  N   . PRO   A  1 42  ? -46.622 3.794   -28.291  1.00 66.37  ? 343  PRO   A N   1 
ATOM   316   C  CA  . PRO   A  1 42  ? -47.869 3.856   -27.504  1.00 66.37  ? 343  PRO   A CA  1 
ATOM   317   C  C   . PRO   A  1 42  ? -49.150 3.716   -28.332  1.00 70.29  ? 343  PRO   A C   1 
ATOM   318   O  O   . PRO   A  1 42  ? -49.306 4.389   -29.354  1.00 77.31  ? 343  PRO   A O   1 
ATOM   319   C  CB  . PRO   A  1 42  ? -47.813 5.247   -26.849  1.00 69.36  ? 343  PRO   A CB  1 
ATOM   320   C  CG  . PRO   A  1 42  ? -46.388 5.695   -26.983  1.00 69.39  ? 343  PRO   A CG  1 
ATOM   321   C  CD  . PRO   A  1 42  ? -45.898 5.073   -28.262  1.00 68.65  ? 343  PRO   A CD  1 
ATOM   322   N  N   . PRO   A  1 49  ? -54.614 -1.101  -43.175  1.00 131.59 ? 350  PRO   A N   1 
ATOM   323   C  CA  . PRO   A  1 49  ? -54.312 -0.364  -44.410  1.00 134.60 ? 350  PRO   A CA  1 
ATOM   324   C  C   . PRO   A  1 49  ? -55.484 0.485   -44.908  1.00 139.52 ? 350  PRO   A C   1 
ATOM   325   O  O   . PRO   A  1 49  ? -55.271 1.503   -45.567  1.00 136.97 ? 350  PRO   A O   1 
ATOM   326   C  CB  . PRO   A  1 49  ? -53.977 -1.477  -45.415  1.00 132.10 ? 350  PRO   A CB  1 
ATOM   327   C  CG  . PRO   A  1 49  ? -54.508 -2.744  -44.805  1.00 129.92 ? 350  PRO   A CG  1 
ATOM   328   C  CD  . PRO   A  1 49  ? -54.388 -2.547  -43.329  1.00 129.61 ? 350  PRO   A CD  1 
ATOM   329   N  N   . GLU   A  1 50  ? -56.709 0.061   -44.590  1.00 148.50 ? 351  GLU   A N   1 
ATOM   330   C  CA  . GLU   A  1 50  ? -57.913 0.789   -44.977  1.00 152.27 ? 351  GLU   A CA  1 
ATOM   331   C  C   . GLU   A  1 50  ? -58.105 2.079   -44.185  1.00 148.22 ? 351  GLU   A C   1 
ATOM   332   O  O   . GLU   A  1 50  ? -59.075 2.803   -44.440  1.00 148.49 ? 351  GLU   A O   1 
ATOM   333   C  CB  . GLU   A  1 50  ? -59.141 -0.114  -44.809  1.00 155.92 ? 351  GLU   A CB  1 
ATOM   334   C  CG  . GLU   A  1 50  ? -60.287 0.158   -45.784  1.00 155.18 ? 351  GLU   A CG  1 
ATOM   335   C  CD  . GLU   A  1 50  ? -59.967 -0.272  -47.206  1.00 151.71 ? 351  GLU   A CD  1 
ATOM   336   O  OE1 . GLU   A  1 50  ? -59.429 0.552   -47.978  1.00 148.93 ? 351  GLU   A OE1 1 
ATOM   337   O  OE2 . GLU   A  1 50  ? -60.246 -1.441  -47.548  1.00 150.63 ? 351  GLU   A OE2 1 
ATOM   338   N  N   . ASP   A  1 51  ? -57.207 2.388   -43.245  1.00 140.06 ? 352  ASP   A N   1 
ATOM   339   C  CA  . ASP   A  1 51  ? -57.293 3.611   -42.452  1.00 130.41 ? 352  ASP   A CA  1 
ATOM   340   C  C   . ASP   A  1 51  ? -56.855 4.836   -43.255  1.00 115.57 ? 352  ASP   A C   1 
ATOM   341   O  O   . ASP   A  1 51  ? -56.323 5.793   -42.680  1.00 115.29 ? 352  ASP   A O   1 
ATOM   342   C  CB  . ASP   A  1 51  ? -56.443 3.488   -41.174  1.00 129.56 ? 352  ASP   A CB  1 
ATOM   343   C  CG  . ASP   A  1 51  ? -57.192 2.824   -40.011  1.00 128.32 ? 352  ASP   A CG  1 
ATOM   344   O  OD1 . ASP   A  1 51  ? -57.347 1.584   -40.019  1.00 128.10 ? 352  ASP   A OD1 1 
ATOM   345   O  OD2 . ASP   A  1 51  ? -57.608 3.544   -39.075  1.00 126.35 ? 352  ASP   A OD2 1 
ATOM   346   N  N   . VAL   A  1 52  ? -57.065 4.819   -44.577  1.00 97.51  ? 353  VAL   A N   1 
ATOM   347   C  CA  . VAL   A  1 52  ? -56.791 5.999   -45.390  1.00 82.00  ? 353  VAL   A CA  1 
ATOM   348   C  C   . VAL   A  1 52  ? -57.882 7.031   -45.146  1.00 69.22  ? 353  VAL   A C   1 
ATOM   349   O  O   . VAL   A  1 52  ? -59.071 6.696   -45.029  1.00 67.60  ? 353  VAL   A O   1 
ATOM   350   C  CB  . VAL   A  1 52  ? -56.677 5.648   -46.889  1.00 79.66  ? 353  VAL   A CB  1 
ATOM   351   C  CG1 . VAL   A  1 52  ? -55.593 4.605   -47.114  1.00 75.90  ? 353  VAL   A CG1 1 
ATOM   352   C  CG2 . VAL   A  1 52  ? -58.017 5.175   -47.468  1.00 77.25  ? 353  VAL   A CG2 1 
ATOM   353   N  N   . ALA   A  1 53  ? -57.476 8.296   -45.062  1.00 62.69  ? 354  ALA   A N   1 
ATOM   354   C  CA  . ALA   A  1 53  ? -58.369 9.347   -44.596  1.00 61.52  ? 354  ALA   A CA  1 
ATOM   355   C  C   . ALA   A  1 53  ? -59.517 9.561   -45.571  1.00 65.30  ? 354  ALA   A C   1 
ATOM   356   O  O   . ALA   A  1 53  ? -59.341 9.476   -46.788  1.00 68.06  ? 354  ALA   A O   1 
ATOM   357   C  CB  . ALA   A  1 53  ? -57.595 10.650  -44.402  1.00 57.03  ? 354  ALA   A CB  1 
ATOM   358   N  N   . THR   A  1 54  ? -60.701 9.830   -45.031  1.00 71.67  ? 355  THR   A N   1 
ATOM   359   C  CA  . THR   A  1 54  ? -61.833 10.173  -45.876  1.00 76.39  ? 355  THR   A CA  1 
ATOM   360   C  C   . THR   A  1 54  ? -61.712 11.615  -46.358  1.00 79.00  ? 355  THR   A C   1 
ATOM   361   O  O   . THR   A  1 54  ? -60.833 12.373  -45.932  1.00 76.33  ? 355  THR   A O   1 
ATOM   362   C  CB  . THR   A  1 54  ? -63.149 10.005  -45.123  1.00 76.72  ? 355  THR   A CB  1 
ATOM   363   O  OG1 . THR   A  1 54  ? -63.277 11.066  -44.170  1.00 79.66  ? 355  THR   A OG1 1 
ATOM   364   C  CG2 . THR   A  1 54  ? -63.175 8.676   -44.400  1.00 76.69  ? 355  THR   A CG2 1 
ATOM   365   N  N   . LYS   A  1 55  ? -62.621 11.994  -47.258  1.00 82.11  ? 356  LYS   A N   1 
ATOM   366   C  CA  . LYS   A  1 55  ? -62.657 13.370  -47.737  1.00 77.35  ? 356  LYS   A CA  1 
ATOM   367   C  C   . LYS   A  1 55  ? -62.753 14.346  -46.570  1.00 70.41  ? 356  LYS   A C   1 
ATOM   368   O  O   . LYS   A  1 55  ? -61.878 15.197  -46.379  1.00 65.59  ? 356  LYS   A O   1 
ATOM   369   C  CB  . LYS   A  1 55  ? -63.829 13.563  -48.703  1.00 79.09  ? 356  LYS   A CB  1 
ATOM   370   C  CG  . LYS   A  1 55  ? -63.476 13.396  -50.167  1.00 73.82  ? 356  LYS   A CG  1 
ATOM   371   C  CD  . LYS   A  1 55  ? -64.705 13.599  -51.030  1.00 74.59  ? 356  LYS   A CD  1 
ATOM   372   C  CE  . LYS   A  1 55  ? -64.466 13.080  -52.442  1.00 82.14  ? 356  LYS   A CE  1 
ATOM   373   N  NZ  . LYS   A  1 55  ? -65.691 13.154  -53.302  1.00 86.57  ? 356  LYS   A NZ  1 
ATOM   374   N  N   . ASP   A  1 56  ? -63.809 14.220  -45.762  1.00 75.69  ? 357  ASP   A N   1 
ATOM   375   C  CA  . ASP   A  1 56  ? -64.027 15.172  -44.676  1.00 76.69  ? 357  ASP   A CA  1 
ATOM   376   C  C   . ASP   A  1 56  ? -62.892 15.140  -43.657  1.00 67.74  ? 357  ASP   A C   1 
ATOM   377   O  O   . ASP   A  1 56  ? -62.570 16.173  -43.062  1.00 71.11  ? 357  ASP   A O   1 
ATOM   378   C  CB  . ASP   A  1 56  ? -65.373 14.895  -44.000  1.00 86.59  ? 357  ASP   A CB  1 
ATOM   379   C  CG  . ASP   A  1 56  ? -66.529 14.906  -44.983  1.00 89.65  ? 357  ASP   A CG  1 
ATOM   380   O  OD1 . ASP   A  1 56  ? -66.428 15.596  -46.024  1.00 81.03  ? 357  ASP   A OD1 1 
ATOM   381   O  OD2 . ASP   A  1 56  ? -67.536 14.220  -44.711  1.00 96.90  ? 357  ASP   A OD2 1 
ATOM   382   N  N   . GLN   A  1 57  ? -62.265 13.977  -43.455  1.00 57.16  ? 358  GLN   A N   1 
ATOM   383   C  CA  . GLN   A  1 57  ? -61.075 13.916  -42.612  1.00 49.32  ? 358  GLN   A CA  1 
ATOM   384   C  C   . GLN   A  1 57  ? -59.935 14.750  -43.185  1.00 53.90  ? 358  GLN   A C   1 
ATOM   385   O  O   . GLN   A  1 57  ? -59.235 15.446  -42.441  1.00 50.58  ? 358  GLN   A O   1 
ATOM   386   C  CB  . GLN   A  1 57  ? -60.632 12.468  -42.437  1.00 58.81  ? 358  GLN   A CB  1 
ATOM   387   C  CG  . GLN   A  1 57  ? -61.512 11.664  -41.491  1.00 73.06  ? 358  GLN   A CG  1 
ATOM   388   C  CD  . GLN   A  1 57  ? -60.969 10.272  -41.230  1.00 78.16  ? 358  GLN   A CD  1 
ATOM   389   O  OE1 . GLN   A  1 57  ? -60.627 9.535   -42.159  1.00 78.12  ? 358  GLN   A OE1 1 
ATOM   390   N  NE2 . GLN   A  1 57  ? -60.877 9.908   -39.957  1.00 79.24  ? 358  GLN   A NE2 1 
ATOM   391   N  N   . LEU   A  1 58  ? -59.738 14.698  -44.513  1.00 52.59  ? 359  LEU   A N   1 
ATOM   392   C  CA  . LEU   A  1 58  ? -58.546 15.283  -45.128  1.00 54.20  ? 359  LEU   A CA  1 
ATOM   393   C  C   . LEU   A  1 58  ? -58.608 16.808  -45.213  1.00 49.70  ? 359  LEU   A C   1 
ATOM   394   O  O   . LEU   A  1 58  ? -57.563 17.465  -45.131  1.00 44.96  ? 359  LEU   A O   1 
ATOM   395   C  CB  . LEU   A  1 58  ? -58.325 14.687  -46.530  1.00 46.74  ? 359  LEU   A CB  1 
ATOM   396   C  CG  . LEU   A  1 58  ? -56.953 14.899  -47.170  1.00 47.76  ? 359  LEU   A CG  1 
ATOM   397   C  CD1 . LEU   A  1 58  ? -55.812 14.500  -46.234  1.00 46.07  ? 359  LEU   A CD1 1 
ATOM   398   C  CD2 . LEU   A  1 58  ? -56.840 14.131  -48.481  1.00 50.55  ? 359  LEU   A CD2 1 
ATOM   399   N  N   . PHE   A  1 59  ? -59.803 17.385  -45.372  1.00 51.87  ? 360  PHE   A N   1 
ATOM   400   C  CA  . PHE   A  1 59  ? -59.942 18.824  -45.557  1.00 58.09  ? 360  PHE   A CA  1 
ATOM   401   C  C   . PHE   A  1 59  ? -59.211 19.616  -44.473  1.00 60.66  ? 360  PHE   A C   1 
ATOM   402   O  O   . PHE   A  1 59  ? -58.326 20.416  -44.805  1.00 66.25  ? 360  PHE   A O   1 
ATOM   403   C  CB  . PHE   A  1 59  ? -61.419 19.224  -45.609  1.00 72.34  ? 360  PHE   A CB  1 
ATOM   404   C  CG  . PHE   A  1 59  ? -62.081 18.981  -46.946  1.00 81.10  ? 360  PHE   A CG  1 
ATOM   405   C  CD1 . PHE   A  1 59  ? -61.657 19.652  -48.082  1.00 78.45  ? 360  PHE   A CD1 1 
ATOM   406   C  CD2 . PHE   A  1 59  ? -63.159 18.108  -47.058  1.00 83.62  ? 360  PHE   A CD2 1 
ATOM   407   C  CE1 . PHE   A  1 59  ? -62.286 19.440  -49.305  1.00 75.68  ? 360  PHE   A CE1 1 
ATOM   408   C  CE2 . PHE   A  1 59  ? -63.786 17.895  -48.284  1.00 77.86  ? 360  PHE   A CE2 1 
ATOM   409   C  CZ  . PHE   A  1 59  ? -63.349 18.559  -49.399  1.00 72.87  ? 360  PHE   A CZ  1 
ATOM   410   N  N   . PRO   A  1 60  ? -59.505 19.424  -43.180  1.00 61.82  ? 361  PRO   A N   1 
ATOM   411   C  CA  . PRO   A  1 60  ? -58.854 20.284  -42.181  1.00 55.44  ? 361  PRO   A CA  1 
ATOM   412   C  C   . PRO   A  1 60  ? -57.374 20.003  -42.029  1.00 47.01  ? 361  PRO   A C   1 
ATOM   413   O  O   . PRO   A  1 60  ? -56.609 20.925  -41.724  1.00 54.56  ? 361  PRO   A O   1 
ATOM   414   C  CB  . PRO   A  1 60  ? -59.629 19.983  -40.896  1.00 57.63  ? 361  PRO   A CB  1 
ATOM   415   C  CG  . PRO   A  1 60  ? -60.111 18.608  -41.070  1.00 59.64  ? 361  PRO   A CG  1 
ATOM   416   C  CD  . PRO   A  1 60  ? -60.334 18.387  -42.537  1.00 60.23  ? 361  PRO   A CD  1 
ATOM   417   N  N   . LEU   A  1 61  ? -56.934 18.765  -42.251  1.00 42.78  ? 362  LEU   A N   1 
ATOM   418   C  CA  . LEU   A  1 61  ? -55.506 18.488  -42.168  1.00 44.45  ? 362  LEU   A CA  1 
ATOM   419   C  C   . LEU   A  1 61  ? -54.748 19.240  -43.244  1.00 48.37  ? 362  LEU   A C   1 
ATOM   420   O  O   . LEU   A  1 61  ? -53.652 19.756  -42.997  1.00 48.62  ? 362  LEU   A O   1 
ATOM   421   C  CB  . LEU   A  1 61  ? -55.236 16.992  -42.295  1.00 40.35  ? 362  LEU   A CB  1 
ATOM   422   C  CG  . LEU   A  1 61  ? -55.847 16.090  -41.243  1.00 45.57  ? 362  LEU   A CG  1 
ATOM   423   C  CD1 . LEU   A  1 61  ? -55.386 14.654  -41.476  1.00 44.34  ? 362  LEU   A CD1 1 
ATOM   424   C  CD2 . LEU   A  1 61  ? -55.466 16.595  -39.859  1.00 50.10  ? 362  LEU   A CD2 1 
ATOM   425   N  N   . ALA   A  1 62  ? -55.309 19.297  -44.458  1.00 47.38  ? 363  ALA   A N   1 
ATOM   426   C  CA  . ALA   A  1 62  ? -54.643 20.034  -45.521  1.00 48.71  ? 363  ALA   A CA  1 
ATOM   427   C  C   . ALA   A  1 62  ? -54.721 21.533  -45.268  1.00 51.07  ? 363  ALA   A C   1 
ATOM   428   O  O   . ALA   A  1 62  ? -53.729 22.247  -45.455  1.00 54.76  ? 363  ALA   A O   1 
ATOM   429   C  CB  . ALA   A  1 62  ? -55.235 19.666  -46.882  1.00 52.39  ? 363  ALA   A CB  1 
ATOM   430   N  N   . LYS   A  1 63  ? -55.878 22.029  -44.815  1.00 53.06  ? 364  LYS   A N   1 
ATOM   431   C  CA  . LYS   A  1 63  ? -55.960 23.442  -44.464  1.00 52.72  ? 364  LYS   A CA  1 
ATOM   432   C  C   . LYS   A  1 63  ? -54.879 23.809  -43.455  1.00 52.46  ? 364  LYS   A C   1 
ATOM   433   O  O   . LYS   A  1 63  ? -54.145 24.787  -43.646  1.00 51.35  ? 364  LYS   A O   1 
ATOM   434   C  CB  . LYS   A  1 63  ? -57.338 23.791  -43.909  1.00 54.30  ? 364  LYS   A CB  1 
ATOM   435   C  CG  . LYS   A  1 63  ? -57.510 25.297  -43.701  1.00 56.33  ? 364  LYS   A CG  1 
ATOM   436   C  CD  . LYS   A  1 63  ? -58.469 25.632  -42.572  1.00 65.91  ? 364  LYS   A CD  1 
ATOM   437   C  CE  . LYS   A  1 63  ? -59.088 27.024  -42.745  1.00 71.70  ? 364  LYS   A CE  1 
ATOM   438   N  NZ  . LYS   A  1 63  ? -58.164 28.150  -42.412  1.00 72.09  ? 364  LYS   A NZ  1 
ATOM   439   N  N   . GLU   A  1 64  ? -54.754 23.016  -42.384  1.00 50.93  ? 365  GLU   A N   1 
ATOM   440   C  CA  . GLU   A  1 64  ? -53.748 23.279  -41.354  1.00 49.53  ? 365  GLU   A CA  1 
ATOM   441   C  C   . GLU   A  1 64  ? -52.353 23.377  -41.960  1.00 47.59  ? 365  GLU   A C   1 
ATOM   442   O  O   . GLU   A  1 64  ? -51.621 24.343  -41.715  1.00 38.64  ? 365  GLU   A O   1 
ATOM   443   C  CB  . GLU   A  1 64  ? -53.797 22.183  -40.279  1.00 55.59  ? 365  GLU   A CB  1 
ATOM   444   C  CG  . GLU   A  1 64  ? -53.010 22.479  -38.992  1.00 66.60  ? 365  GLU   A CG  1 
ATOM   445   C  CD  . GLU   A  1 64  ? -52.832 21.238  -38.090  1.00 80.26  ? 365  GLU   A CD  1 
ATOM   446   O  OE1 . GLU   A  1 64  ? -52.071 21.318  -37.089  1.00 81.89  ? 365  GLU   A OE1 1 
ATOM   447   O  OE2 . GLU   A  1 64  ? -53.444 20.180  -38.382  1.00 78.26  ? 365  GLU   A OE2 1 
ATOM   448   N  N   . PHE   A  1 65  ? -51.975 22.394  -42.779  1.00 50.19  ? 366  PHE   A N   1 
ATOM   449   C  CA  . PHE   A  1 65  ? -50.630 22.406  -43.335  1.00 49.28  ? 366  PHE   A CA  1 
ATOM   450   C  C   . PHE   A  1 65  ? -50.430 23.577  -44.297  1.00 41.27  ? 366  PHE   A C   1 
ATOM   451   O  O   . PHE   A  1 65  ? -49.403 24.262  -44.238  1.00 46.28  ? 366  PHE   A O   1 
ATOM   452   C  CB  . PHE   A  1 65  ? -50.319 21.081  -44.027  1.00 52.53  ? 366  PHE   A CB  1 
ATOM   453   C  CG  . PHE   A  1 65  ? -49.064 21.128  -44.829  1.00 48.81  ? 366  PHE   A CG  1 
ATOM   454   C  CD1 . PHE   A  1 65  ? -47.830 21.092  -44.205  1.00 49.61  ? 366  PHE   A CD1 1 
ATOM   455   C  CD2 . PHE   A  1 65  ? -49.116 21.256  -46.199  1.00 43.23  ? 366  PHE   A CD2 1 
ATOM   456   C  CE1 . PHE   A  1 65  ? -46.673 21.162  -44.930  1.00 49.44  ? 366  PHE   A CE1 1 
ATOM   457   C  CE2 . PHE   A  1 65  ? -47.961 21.326  -46.932  1.00 50.84  ? 366  PHE   A CE2 1 
ATOM   458   C  CZ  . PHE   A  1 65  ? -46.735 21.277  -46.297  1.00 52.72  ? 366  PHE   A CZ  1 
ATOM   459   N  N   . ILE   A  1 66  ? -51.396 23.833  -45.180  1.00 44.83  ? 367  ILE   A N   1 
ATOM   460   C  CA  . ILE   A  1 66  ? -51.238 24.935  -46.129  1.00 45.27  ? 367  ILE   A CA  1 
ATOM   461   C  C   . ILE   A  1 66  ? -51.141 26.269  -45.389  1.00 47.08  ? 367  ILE   A C   1 
ATOM   462   O  O   . ILE   A  1 66  ? -50.330 27.139  -45.748  1.00 42.97  ? 367  ILE   A O   1 
ATOM   463   C  CB  . ILE   A  1 66  ? -52.386 24.930  -47.155  1.00 45.88  ? 367  ILE   A CB  1 
ATOM   464   C  CG1 . ILE   A  1 66  ? -52.327 23.666  -48.019  1.00 45.43  ? 367  ILE   A CG1 1 
ATOM   465   C  CG2 . ILE   A  1 66  ? -52.325 26.183  -48.038  1.00 44.59  ? 367  ILE   A CG2 1 
ATOM   466   C  CD1 . ILE   A  1 66  ? -51.037 23.522  -48.826  1.00 41.04  ? 367  ILE   A CD1 1 
ATOM   467   N  N   . ASP   A  1 67  ? -51.956 26.442  -44.336  1.00 41.52  ? 368  ASP   A N   1 
ATOM   468   C  CA  . ASP   A  1 67  ? -51.875 27.646  -43.508  1.00 42.23  ? 368  ASP   A CA  1 
ATOM   469   C  C   . ASP   A  1 67  ? -50.507 27.768  -42.864  1.00 44.02  ? 368  ASP   A C   1 
ATOM   470   O  O   . ASP   A  1 67  ? -49.927 28.859  -42.810  1.00 51.76  ? 368  ASP   A O   1 
ATOM   471   C  CB  . ASP   A  1 67  ? -52.952 27.624  -42.421  1.00 41.92  ? 368  ASP   A CB  1 
ATOM   472   C  CG  . ASP   A  1 67  ? -54.351 27.825  -42.966  1.00 48.61  ? 368  ASP   A CG  1 
ATOM   473   O  OD1 . ASP   A  1 67  ? -54.518 28.177  -44.166  1.00 44.56  ? 368  ASP   A OD1 1 
ATOM   474   O  OD2 . ASP   A  1 67  ? -55.293 27.626  -42.175  1.00 50.83  ? 368  ASP   A OD2 1 
ATOM   475   N  N   . GLN   A  1 68  ? -49.991 26.651  -42.354  1.00 39.46  ? 369  GLN   A N   1 
ATOM   476   C  CA  . GLN   A  1 68  ? -48.680 26.637  -41.724  1.00 43.86  ? 369  GLN   A CA  1 
ATOM   477   C  C   . GLN   A  1 68  ? -47.597 27.012  -42.730  1.00 49.85  ? 369  GLN   A C   1 
ATOM   478   O  O   . GLN   A  1 68  ? -46.712 27.827  -42.440  1.00 52.06  ? 369  GLN   A O   1 
ATOM   479   C  CB  . GLN   A  1 68  ? -48.440 25.248  -41.120  1.00 44.37  ? 369  GLN   A CB  1 
ATOM   480   C  CG  . GLN   A  1 68  ? -47.156 25.059  -40.342  1.00 55.92  ? 369  GLN   A CG  1 
ATOM   481   C  CD  . GLN   A  1 68  ? -46.795 23.577  -40.142  1.00 62.99  ? 369  GLN   A CD  1 
ATOM   482   O  OE1 . GLN   A  1 68  ? -45.614 23.216  -40.059  1.00 63.66  ? 369  GLN   A OE1 1 
ATOM   483   N  NE2 . GLN   A  1 68  ? -47.816 22.717  -40.071  1.00 52.87  ? 369  GLN   A NE2 1 
ATOM   484   N  N   . TYR   A  1 69  ? -47.676 26.454  -43.934  1.00 48.20  ? 370  TYR   A N   1 
ATOM   485   C  CA  . TYR   A  1 69  ? -46.676 26.761  -44.943  1.00 49.43  ? 370  TYR   A CA  1 
ATOM   486   C  C   . TYR   A  1 69  ? -46.738 28.227  -45.356  1.00 44.69  ? 370  TYR   A C   1 
ATOM   487   O  O   . TYR   A  1 69  ? -45.699 28.874  -45.524  1.00 43.86  ? 370  TYR   A O   1 
ATOM   488   C  CB  . TYR   A  1 69  ? -46.841 25.839  -46.156  1.00 43.59  ? 370  TYR   A CB  1 
ATOM   489   C  CG  . TYR   A  1 69  ? -45.999 26.290  -47.313  1.00 53.10  ? 370  TYR   A CG  1 
ATOM   490   C  CD1 . TYR   A  1 69  ? -44.649 25.991  -47.367  1.00 58.40  ? 370  TYR   A CD1 1 
ATOM   491   C  CD2 . TYR   A  1 69  ? -46.544 27.045  -48.340  1.00 52.75  ? 370  TYR   A CD2 1 
ATOM   492   C  CE1 . TYR   A  1 69  ? -43.870 26.412  -48.411  1.00 53.58  ? 370  TYR   A CE1 1 
ATOM   493   C  CE2 . TYR   A  1 69  ? -45.768 27.470  -49.395  1.00 55.63  ? 370  TYR   A CE2 1 
ATOM   494   C  CZ  . TYR   A  1 69  ? -44.429 27.152  -49.423  1.00 57.89  ? 370  TYR   A CZ  1 
ATOM   495   O  OH  . TYR   A  1 69  ? -43.630 27.558  -50.466  1.00 60.35  ? 370  TYR   A OH  1 
ATOM   496   N  N   . TYR   A  1 70  ? -47.933 28.783  -45.518  1.00 44.99  ? 371  TYR   A N   1 
ATOM   497   C  CA  . TYR   A  1 70  ? -47.956 30.191  -45.892  1.00 49.53  ? 371  TYR   A CA  1 
ATOM   498   C  C   . TYR   A  1 70  ? -47.597 31.100  -44.725  1.00 54.98  ? 371  TYR   A C   1 
ATOM   499   O  O   . TYR   A  1 70  ? -47.093 32.206  -44.946  1.00 56.46  ? 371  TYR   A O   1 
ATOM   500   C  CB  . TYR   A  1 70  ? -49.304 30.570  -46.505  1.00 49.30  ? 371  TYR   A CB  1 
ATOM   501   C  CG  . TYR   A  1 70  ? -49.304 30.203  -47.960  1.00 52.61  ? 371  TYR   A CG  1 
ATOM   502   C  CD1 . TYR   A  1 70  ? -48.758 31.051  -48.909  1.00 52.70  ? 371  TYR   A CD1 1 
ATOM   503   C  CD2 . TYR   A  1 70  ? -49.769 28.972  -48.372  1.00 50.27  ? 371  TYR   A CD2 1 
ATOM   504   C  CE1 . TYR   A  1 70  ? -48.718 30.690  -50.234  1.00 57.93  ? 371  TYR   A CE1 1 
ATOM   505   C  CE2 . TYR   A  1 70  ? -49.730 28.607  -49.677  1.00 53.15  ? 371  TYR   A CE2 1 
ATOM   506   C  CZ  . TYR   A  1 70  ? -49.210 29.466  -50.613  1.00 55.98  ? 371  TYR   A CZ  1 
ATOM   507   O  OH  . TYR   A  1 70  ? -49.191 29.078  -51.931  1.00 55.08  ? 371  TYR   A OH  1 
ATOM   508   N  N   . SER   A  1 71  ? -47.811 30.659  -43.487  1.00 52.81  ? 372  SER   A N   1 
ATOM   509   C  CA  . SER   A  1 71  ? -47.289 31.424  -42.363  1.00 58.86  ? 372  SER   A CA  1 
ATOM   510   C  C   . SER   A  1 71  ? -45.765 31.438  -42.388  1.00 57.61  ? 372  SER   A C   1 
ATOM   511   O  O   . SER   A  1 71  ? -45.140 32.497  -42.265  1.00 59.22  ? 372  SER   A O   1 
ATOM   512   C  CB  . SER   A  1 71  ? -47.818 30.858  -41.049  1.00 66.56  ? 372  SER   A CB  1 
ATOM   513   O  OG  . SER   A  1 71  ? -47.043 31.306  -39.954  1.00 76.59  ? 372  SER   A OG  1 
ATOM   514   N  N   . SER   A  1 72  ? -45.153 30.271  -42.609  1.00 53.43  ? 373  SER   A N   1 
ATOM   515   C  CA  . SER   A  1 72  ? -43.695 30.163  -42.586  1.00 52.67  ? 373  SER   A CA  1 
ATOM   516   C  C   . SER   A  1 72  ? -43.015 31.118  -43.562  1.00 63.68  ? 373  SER   A C   1 
ATOM   517   O  O   . SER   A  1 72  ? -41.887 31.557  -43.311  1.00 68.91  ? 373  SER   A O   1 
ATOM   518   C  CB  . SER   A  1 72  ? -43.279 28.742  -42.922  1.00 48.71  ? 373  SER   A CB  1 
ATOM   519   O  OG  . SER   A  1 72  ? -43.310 28.572  -44.333  1.00 53.59  ? 373  SER   A OG  1 
ATOM   520   N  N   . ILE   A  1 73  ? -43.657 31.433  -44.683  1.00 60.78  ? 374  ILE   A N   1 
ATOM   521   C  CA  . ILE   A  1 73  ? -43.040 32.253  -45.716  1.00 62.65  ? 374  ILE   A CA  1 
ATOM   522   C  C   . ILE   A  1 73  ? -43.633 33.660  -45.742  1.00 66.73  ? 374  ILE   A C   1 
ATOM   523   O  O   . ILE   A  1 73  ? -43.521 34.359  -46.751  1.00 66.37  ? 374  ILE   A O   1 
ATOM   524   C  CB  . ILE   A  1 73  ? -43.139 31.589  -47.098  1.00 59.16  ? 374  ILE   A CB  1 
ATOM   525   C  CG1 . ILE   A  1 73  ? -44.607 31.452  -47.522  1.00 54.60  ? 374  ILE   A CG1 1 
ATOM   526   C  CG2 . ILE   A  1 73  ? -42.413 30.251  -47.086  1.00 56.16  ? 374  ILE   A CG2 1 
ATOM   527   C  CD1 . ILE   A  1 73  ? -44.811 31.054  -48.975  1.00 49.97  ? 374  ILE   A CD1 1 
ATOM   528   N  N   . LYS   A  1 74  ? -44.270 34.077  -44.646  1.00 71.47  ? 375  LYS   A N   1 
ATOM   529   C  CA  . LYS   A  1 74  ? -44.792 35.437  -44.506  1.00 77.16  ? 375  LYS   A CA  1 
ATOM   530   C  C   . LYS   A  1 74  ? -45.715 35.800  -45.669  1.00 73.95  ? 375  LYS   A C   1 
ATOM   531   O  O   . LYS   A  1 74  ? -45.637 36.888  -46.236  1.00 85.82  ? 375  LYS   A O   1 
ATOM   532   C  CB  . LYS   A  1 74  ? -43.649 36.450  -44.376  1.00 80.03  ? 375  LYS   A CB  1 
ATOM   533   C  CG  . LYS   A  1 74  ? -42.770 36.268  -43.148  1.00 81.38  ? 375  LYS   A CG  1 
ATOM   534   C  CD  . LYS   A  1 74  ? -43.033 37.361  -42.114  1.00 91.91  ? 375  LYS   A CD  1 
ATOM   535   C  CE  . LYS   A  1 74  ? -42.260 37.102  -40.826  1.00 93.12  ? 375  LYS   A CE  1 
ATOM   536   N  NZ  . LYS   A  1 74  ? -42.477 35.720  -40.294  1.00 91.16  ? 375  LYS   A NZ  1 
ATOM   537   N  N   . ARG   A  1 75  ? -46.590 34.861  -46.044  1.00 64.99  ? 376  ARG   A N   1 
ATOM   538   C  CA  . ARG   A  1 75  ? -47.606 35.102  -47.065  1.00 61.14  ? 376  ARG   A CA  1 
ATOM   539   C  C   . ARG   A  1 75  ? -48.993 34.667  -46.594  1.00 57.72  ? 376  ARG   A C   1 
ATOM   540   O  O   . ARG   A  1 75  ? -49.864 34.381  -47.426  1.00 56.17  ? 376  ARG   A O   1 
ATOM   541   C  CB  . ARG   A  1 75  ? -47.259 34.396  -48.381  1.00 62.35  ? 376  ARG   A CB  1 
ATOM   542   C  CG  . ARG   A  1 75  ? -45.971 34.871  -49.061  1.00 62.68  ? 376  ARG   A CG  1 
ATOM   543   C  CD  . ARG   A  1 75  ? -46.078 36.322  -49.498  1.00 65.76  ? 376  ARG   A CD  1 
ATOM   544   N  NE  . ARG   A  1 75  ? -45.106 36.664  -50.533  1.00 70.70  ? 376  ARG   A NE  1 
ATOM   545   C  CZ  . ARG   A  1 75  ? -43.884 37.133  -50.293  1.00 72.95  ? 376  ARG   A CZ  1 
ATOM   546   N  NH1 . ARG   A  1 75  ? -43.077 37.414  -51.309  1.00 71.41  ? 376  ARG   A NH1 1 
ATOM   547   N  NH2 . ARG   A  1 75  ? -43.470 37.323  -49.043  1.00 74.03  ? 376  ARG   A NH2 1 
ATOM   548   N  N   . PHE   A  1 76  ? -49.222 34.619  -45.282  1.00 56.15  ? 377  PHE   A N   1 
ATOM   549   C  CA  . PHE   A  1 76  ? -50.512 34.179  -44.760  1.00 49.50  ? 377  PHE   A CA  1 
ATOM   550   C  C   . PHE   A  1 76  ? -51.602 35.199  -45.093  1.00 59.19  ? 377  PHE   A C   1 
ATOM   551   O  O   . PHE   A  1 76  ? -51.425 36.405  -44.892  1.00 61.88  ? 377  PHE   A O   1 
ATOM   552   C  CB  . PHE   A  1 76  ? -50.426 33.960  -43.249  1.00 56.07  ? 377  PHE   A CB  1 
ATOM   553   C  CG  . PHE   A  1 76  ? -51.668 33.361  -42.656  1.00 55.62  ? 377  PHE   A CG  1 
ATOM   554   C  CD1 . PHE   A  1 76  ? -52.756 34.160  -42.331  1.00 56.54  ? 377  PHE   A CD1 1 
ATOM   555   C  CD2 . PHE   A  1 76  ? -51.757 31.997  -42.447  1.00 51.25  ? 377  PHE   A CD2 1 
ATOM   556   C  CE1 . PHE   A  1 76  ? -53.907 33.605  -41.802  1.00 58.61  ? 377  PHE   A CE1 1 
ATOM   557   C  CE2 . PHE   A  1 76  ? -52.901 31.437  -41.920  1.00 53.79  ? 377  PHE   A CE2 1 
ATOM   558   C  CZ  . PHE   A  1 76  ? -53.978 32.242  -41.594  1.00 58.88  ? 377  PHE   A CZ  1 
ATOM   559   N  N   . GLY   A  1 77  ? -52.741 34.712  -45.594  1.00 57.83  ? 378  GLY   A N   1 
ATOM   560   C  CA  . GLY   A  1 77  ? -53.806 35.574  -46.064  1.00 57.29  ? 378  GLY   A CA  1 
ATOM   561   C  C   . GLY   A  1 77  ? -53.637 36.095  -47.479  1.00 63.20  ? 378  GLY   A C   1 
ATOM   562   O  O   . GLY   A  1 77  ? -54.557 36.742  -47.997  1.00 65.91  ? 378  GLY   A O   1 
ATOM   563   N  N   . SER   A  1 78  ? -52.506 35.824  -48.125  1.00 60.20  ? 379  SER   A N   1 
ATOM   564   C  CA  . SER   A  1 78  ? -52.221 36.389  -49.434  1.00 60.73  ? 379  SER   A CA  1 
ATOM   565   C  C   . SER   A  1 78  ? -53.105 35.767  -50.509  1.00 62.38  ? 379  SER   A C   1 
ATOM   566   O  O   . SER   A  1 78  ? -53.710 34.705  -50.323  1.00 57.17  ? 379  SER   A O   1 
ATOM   567   C  CB  . SER   A  1 78  ? -50.757 36.176  -49.801  1.00 64.84  ? 379  SER   A CB  1 
ATOM   568   O  OG  . SER   A  1 78  ? -50.493 34.798  -49.999  1.00 60.24  ? 379  SER   A OG  1 
ATOM   569   N  N   . LYS   A  1 79  ? -53.169 36.454  -51.654  1.00 57.58  ? 380  LYS   A N   1 
ATOM   570   C  CA  . LYS   A  1 79  ? -53.909 35.924  -52.793  1.00 62.19  ? 380  LYS   A CA  1 
ATOM   571   C  C   . LYS   A  1 79  ? -53.434 34.513  -53.135  1.00 56.62  ? 380  LYS   A C   1 
ATOM   572   O  O   . LYS   A  1 79  ? -54.245 33.597  -53.304  1.00 62.12  ? 380  LYS   A O   1 
ATOM   573   C  CB  . LYS   A  1 79  ? -53.768 36.866  -53.998  1.00 71.60  ? 380  LYS   A CB  1 
ATOM   574   C  CG  . LYS   A  1 79  ? -54.829 36.681  -55.102  1.00 77.85  ? 380  LYS   A CG  1 
ATOM   575   C  CD  . LYS   A  1 79  ? -54.513 37.528  -56.346  1.00 89.83  ? 380  LYS   A CD  1 
ATOM   576   C  CE  . LYS   A  1 79  ? -55.696 38.399  -56.789  1.00 97.38  ? 380  LYS   A CE  1 
ATOM   577   N  NZ  . LYS   A  1 79  ? -56.785 37.630  -57.458  1.00 98.98  ? 380  LYS   A NZ  1 
ATOM   578   N  N   . ALA   A  1 80  ? -52.114 34.311  -53.201  1.00 48.28  ? 381  ALA   A N   1 
ATOM   579   C  CA  . ALA   A  1 80  ? -51.582 32.981  -53.489  1.00 50.73  ? 381  ALA   A CA  1 
ATOM   580   C  C   . ALA   A  1 80  ? -51.983 31.969  -52.420  1.00 55.96  ? 381  ALA   A C   1 
ATOM   581   O  O   . ALA   A  1 80  ? -52.255 30.803  -52.732  1.00 56.72  ? 381  ALA   A O   1 
ATOM   582   C  CB  . ALA   A  1 80  ? -50.062 33.041  -53.614  1.00 47.43  ? 381  ALA   A CB  1 
ATOM   583   N  N   . HIS   A  1 81  ? -52.006 32.394  -51.154  1.00 53.13  ? 382  HIS   A N   1 
ATOM   584   C  CA  . HIS   A  1 81  ? -52.454 31.517  -50.074  1.00 54.84  ? 382  HIS   A CA  1 
ATOM   585   C  C   . HIS   A  1 81  ? -53.894 31.069  -50.297  1.00 51.17  ? 382  HIS   A C   1 
ATOM   586   O  O   . HIS   A  1 81  ? -54.197 29.871  -50.257  1.00 50.92  ? 382  HIS   A O   1 
ATOM   587   C  CB  . HIS   A  1 81  ? -52.308 32.239  -48.728  1.00 52.39  ? 382  HIS   A CB  1 
ATOM   588   C  CG  . HIS   A  1 81  ? -52.735 31.430  -47.541  1.00 55.52  ? 382  HIS   A CG  1 
ATOM   589   N  ND1 . HIS   A  1 81  ? -52.905 31.989  -46.288  1.00 55.36  ? 382  HIS   A ND1 1 
ATOM   590   C  CD2 . HIS   A  1 81  ? -53.005 30.109  -47.402  1.00 52.80  ? 382  HIS   A CD2 1 
ATOM   591   C  CE1 . HIS   A  1 81  ? -53.266 31.050  -45.433  1.00 50.96  ? 382  HIS   A CE1 1 
ATOM   592   N  NE2 . HIS   A  1 81  ? -53.327 29.897  -46.081  1.00 56.02  ? 382  HIS   A NE2 1 
ATOM   593   N  N   . MET   A  1 82  ? -54.793 32.022  -50.555  1.00 48.50  ? 383  MET   A N   1 
ATOM   594   C  CA  . MET   A  1 82  ? -56.211 31.690  -50.661  1.00 55.03  ? 383  MET   A CA  1 
ATOM   595   C  C   . MET   A  1 82  ? -56.503 30.844  -51.895  1.00 58.36  ? 383  MET   A C   1 
ATOM   596   O  O   . MET   A  1 82  ? -57.320 29.916  -51.837  1.00 59.01  ? 383  MET   A O   1 
ATOM   597   C  CB  . MET   A  1 82  ? -57.043 32.967  -50.673  1.00 57.22  ? 383  MET   A CB  1 
ATOM   598   C  CG  . MET   A  1 82  ? -57.029 33.697  -49.350  1.00 73.23  ? 383  MET   A CG  1 
ATOM   599   S  SD  . MET   A  1 82  ? -57.927 32.786  -48.078  1.00 80.76  ? 383  MET   A SD  1 
ATOM   600   C  CE  . MET   A  1 82  ? -56.986 33.213  -46.617  1.00 77.41  ? 383  MET   A CE  1 
ATOM   601   N  N   . GLU   A  1 83  ? -55.851 31.145  -53.021  1.00 58.49  ? 384  GLU   A N   1 
ATOM   602   C  CA  . GLU   A  1 83  ? -56.090 30.355  -54.224  1.00 58.56  ? 384  GLU   A CA  1 
ATOM   603   C  C   . GLU   A  1 83  ? -55.570 28.935  -54.049  1.00 59.56  ? 384  GLU   A C   1 
ATOM   604   O  O   . GLU   A  1 83  ? -56.237 27.972  -54.445  1.00 60.69  ? 384  GLU   A O   1 
ATOM   605   C  CB  . GLU   A  1 83  ? -55.453 31.035  -55.434  1.00 61.03  ? 384  GLU   A CB  1 
ATOM   606   C  CG  . GLU   A  1 83  ? -56.140 32.344  -55.815  1.00 71.10  ? 384  GLU   A CG  1 
ATOM   607   C  CD  . GLU   A  1 83  ? -55.493 33.040  -56.998  1.00 82.17  ? 384  GLU   A CD  1 
ATOM   608   O  OE1 . GLU   A  1 83  ? -54.412 32.587  -57.440  1.00 82.11  ? 384  GLU   A OE1 1 
ATOM   609   O  OE2 . GLU   A  1 83  ? -56.071 34.042  -57.482  1.00 88.18  ? 384  GLU   A OE2 1 
ATOM   610   N  N   . ARG   A  1 84  ? -54.394 28.787  -53.433  1.00 56.29  ? 385  ARG   A N   1 
ATOM   611   C  CA  . ARG   A  1 84  ? -53.880 27.457  -53.131  1.00 55.89  ? 385  ARG   A CA  1 
ATOM   612   C  C   . ARG   A  1 84  ? -54.877 26.661  -52.302  1.00 54.47  ? 385  ARG   A C   1 
ATOM   613   O  O   . ARG   A  1 84  ? -55.144 25.491  -52.602  1.00 51.94  ? 385  ARG   A O   1 
ATOM   614   C  CB  . ARG   A  1 84  ? -52.543 27.565  -52.406  1.00 55.18  ? 385  ARG   A CB  1 
ATOM   615   C  CG  . ARG   A  1 84  ? -51.924 26.233  -52.031  1.00 54.86  ? 385  ARG   A CG  1 
ATOM   616   C  CD  . ARG   A  1 84  ? -51.834 25.322  -53.231  1.00 51.76  ? 385  ARG   A CD  1 
ATOM   617   N  NE  . ARG   A  1 84  ? -51.089 24.097  -52.941  1.00 54.65  ? 385  ARG   A NE  1 
ATOM   618   C  CZ  . ARG   A  1 84  ? -51.234 22.968  -53.628  1.00 49.09  ? 385  ARG   A CZ  1 
ATOM   619   N  NH1 . ARG   A  1 84  ? -52.103 22.917  -54.627  1.00 53.60  ? 385  ARG   A NH1 1 
ATOM   620   N  NH2 . ARG   A  1 84  ? -50.525 21.891  -53.318  1.00 40.92  ? 385  ARG   A NH2 1 
ATOM   621   N  N   . LEU   A  1 85  ? -55.469 27.298  -51.286  1.00 57.98  ? 386  LEU   A N   1 
ATOM   622   C  CA  . LEU   A  1 85  ? -56.417 26.621  -50.401  1.00 58.80  ? 386  LEU   A CA  1 
ATOM   623   C  C   . LEU   A  1 85  ? -57.591 26.040  -51.173  1.00 64.49  ? 386  LEU   A C   1 
ATOM   624   O  O   . LEU   A  1 85  ? -57.950 24.872  -50.989  1.00 65.36  ? 386  LEU   A O   1 
ATOM   625   C  CB  . LEU   A  1 85  ? -56.928 27.588  -49.335  1.00 59.18  ? 386  LEU   A CB  1 
ATOM   626   C  CG  . LEU   A  1 85  ? -56.765 27.178  -47.874  1.00 60.77  ? 386  LEU   A CG  1 
ATOM   627   C  CD1 . LEU   A  1 85  ? -56.940 25.675  -47.702  1.00 65.92  ? 386  LEU   A CD1 1 
ATOM   628   C  CD2 . LEU   A  1 85  ? -55.422 27.623  -47.364  1.00 60.00  ? 386  LEU   A CD2 1 
ATOM   629   N  N   . GLU   A  1 86  ? -58.226 26.844  -52.028  1.00 71.23  ? 387  GLU   A N   1 
ATOM   630   C  CA  . GLU   A  1 86  ? -59.377 26.321  -52.755  1.00 73.08  ? 387  GLU   A CA  1 
ATOM   631   C  C   . GLU   A  1 86  ? -58.946 25.339  -53.835  1.00 62.46  ? 387  GLU   A C   1 
ATOM   632   O  O   . GLU   A  1 86  ? -59.693 24.409  -54.153  1.00 63.94  ? 387  GLU   A O   1 
ATOM   633   C  CB  . GLU   A  1 86  ? -60.214 27.461  -53.338  1.00 84.13  ? 387  GLU   A CB  1 
ATOM   634   C  CG  . GLU   A  1 86  ? -59.712 28.048  -54.638  1.00 91.83  ? 387  GLU   A CG  1 
ATOM   635   C  CD  . GLU   A  1 86  ? -60.821 28.752  -55.400  1.00 96.35  ? 387  GLU   A CD  1 
ATOM   636   O  OE1 . GLU   A  1 86  ? -61.879 28.122  -55.614  1.00 99.05  ? 387  GLU   A OE1 1 
ATOM   637   O  OE2 . GLU   A  1 86  ? -60.641 29.931  -55.771  1.00 95.28  ? 387  GLU   A OE2 1 
ATOM   638   N  N   . GLU   A  1 87  ? -57.739 25.505  -54.377  1.00 53.99  ? 388  GLU   A N   1 
ATOM   639   C  CA  . GLU   A  1 87  ? -57.192 24.497  -55.279  1.00 53.36  ? 388  GLU   A CA  1 
ATOM   640   C  C   . GLU   A  1 87  ? -57.053 23.145  -54.585  1.00 61.07  ? 388  GLU   A C   1 
ATOM   641   O  O   . GLU   A  1 87  ? -57.372 22.105  -55.176  1.00 64.56  ? 388  GLU   A O   1 
ATOM   642   C  CB  . GLU   A  1 87  ? -55.843 24.952  -55.825  1.00 52.31  ? 388  GLU   A CB  1 
ATOM   643   C  CG  . GLU   A  1 87  ? -55.291 24.015  -56.881  1.00 59.34  ? 388  GLU   A CG  1 
ATOM   644   C  CD  . GLU   A  1 87  ? -53.874 24.347  -57.296  1.00 58.71  ? 388  GLU   A CD  1 
ATOM   645   O  OE1 . GLU   A  1 87  ? -53.069 24.751  -56.435  1.00 58.40  ? 388  GLU   A OE1 1 
ATOM   646   O  OE2 . GLU   A  1 87  ? -53.562 24.195  -58.491  1.00 59.48  ? 388  GLU   A OE2 1 
ATOM   647   N  N   . VAL   A  1 88  ? -56.562 23.134  -53.339  1.00 51.50  ? 389  VAL   A N   1 
ATOM   648   C  CA  . VAL   A  1 88  ? -56.472 21.882  -52.585  1.00 47.02  ? 389  VAL   A CA  1 
ATOM   649   C  C   . VAL   A  1 88  ? -57.857 21.293  -52.389  1.00 51.87  ? 389  VAL   A C   1 
ATOM   650   O  O   . VAL   A  1 88  ? -58.074 20.092  -52.581  1.00 49.27  ? 389  VAL   A O   1 
ATOM   651   C  CB  . VAL   A  1 88  ? -55.776 22.101  -51.227  1.00 46.72  ? 389  VAL   A CB  1 
ATOM   652   C  CG1 . VAL   A  1 88  ? -55.989 20.886  -50.332  1.00 47.19  ? 389  VAL   A CG1 1 
ATOM   653   C  CG2 . VAL   A  1 88  ? -54.294 22.353  -51.406  1.00 46.14  ? 389  VAL   A CG2 1 
ATOM   654   N  N   . ASN   A  1 89  ? -58.811 22.136  -51.989  1.00 62.00  ? 390  ASN   A N   1 
ATOM   655   C  CA  . ASN   A  1 89  ? -60.166 21.672  -51.719  1.00 68.25  ? 390  ASN   A CA  1 
ATOM   656   C  C   . ASN   A  1 89  ? -60.798 21.054  -52.957  1.00 67.07  ? 390  ASN   A C   1 
ATOM   657   O  O   . ASN   A  1 89  ? -61.470 20.020  -52.868  1.00 70.92  ? 390  ASN   A O   1 
ATOM   658   C  CB  . ASN   A  1 89  ? -61.011 22.833  -51.203  1.00 78.61  ? 390  ASN   A CB  1 
ATOM   659   C  CG  . ASN   A  1 89  ? -61.037 22.910  -49.689  1.00 88.47  ? 390  ASN   A CG  1 
ATOM   660   O  OD1 . ASN   A  1 89  ? -62.104 22.819  -49.083  1.00 97.93  ? 390  ASN   A OD1 1 
ATOM   661   N  ND2 . ASN   A  1 89  ? -59.864 23.063  -49.068  1.00 81.84  ? 390  ASN   A ND2 1 
ATOM   662   N  N   . LYS   A  1 90  ? -60.599 21.679  -54.118  1.00 62.99  ? 391  LYS   A N   1 
ATOM   663   C  CA  . LYS   A  1 90  ? -61.129 21.129  -55.360  1.00 64.56  ? 391  LYS   A CA  1 
ATOM   664   C  C   . LYS   A  1 90  ? -60.593 19.728  -55.609  1.00 59.95  ? 391  LYS   A C   1 
ATOM   665   O  O   . LYS   A  1 90  ? -61.357 18.817  -55.949  1.00 65.70  ? 391  LYS   A O   1 
ATOM   666   C  CB  . LYS   A  1 90  ? -60.789 22.049  -56.537  1.00 73.21  ? 391  LYS   A CB  1 
ATOM   667   C  CG  . LYS   A  1 90  ? -61.603 23.337  -56.592  1.00 81.08  ? 391  LYS   A CG  1 
ATOM   668   C  CD  . LYS   A  1 90  ? -61.167 24.215  -57.758  1.00 86.32  ? 391  LYS   A CD  1 
ATOM   669   C  CE  . LYS   A  1 90  ? -61.998 25.490  -57.849  1.00 88.47  ? 391  LYS   A CE  1 
ATOM   670   N  NZ  . LYS   A  1 90  ? -61.545 26.363  -58.978  1.00 88.49  ? 391  LYS   A NZ  1 
ATOM   671   N  N   . GLU   A  1 91  ? -59.276 19.537  -55.456  1.00 49.14  ? 392  GLU   A N   1 
ATOM   672   C  CA  . GLU   A  1 91  ? -58.695 18.210  -55.648  1.00 49.49  ? 392  GLU   A CA  1 
ATOM   673   C  C   . GLU   A  1 91  ? -59.321 17.191  -54.700  1.00 56.65  ? 392  GLU   A C   1 
ATOM   674   O  O   . GLU   A  1 91  ? -59.679 16.082  -55.108  1.00 60.26  ? 392  GLU   A O   1 
ATOM   675   C  CB  . GLU   A  1 91  ? -57.179 18.258  -55.453  1.00 50.44  ? 392  GLU   A CB  1 
ATOM   676   C  CG  . GLU   A  1 91  ? -56.397 18.870  -56.603  1.00 50.54  ? 392  GLU   A CG  1 
ATOM   677   C  CD  . GLU   A  1 91  ? -54.904 18.595  -56.511  1.00 56.20  ? 392  GLU   A CD  1 
ATOM   678   O  OE1 . GLU   A  1 91  ? -54.471 17.478  -56.866  1.00 60.45  ? 392  GLU   A OE1 1 
ATOM   679   O  OE2 . GLU   A  1 91  ? -54.157 19.499  -56.084  1.00 63.12  ? 392  GLU   A OE2 1 
ATOM   680   N  N   . ILE   A  1 92  ? -59.466 17.552  -53.426  1.00 57.66  ? 393  ILE   A N   1 
ATOM   681   C  CA  . ILE   A  1 92  ? -60.039 16.621  -52.458  1.00 59.75  ? 393  ILE   A CA  1 
ATOM   682   C  C   . ILE   A  1 92  ? -61.475 16.276  -52.836  1.00 72.89  ? 393  ILE   A C   1 
ATOM   683   O  O   . ILE   A  1 92  ? -61.907 15.126  -52.698  1.00 80.46  ? 393  ILE   A O   1 
ATOM   684   C  CB  . ILE   A  1 92  ? -59.942 17.212  -51.042  1.00 51.44  ? 393  ILE   A CB  1 
ATOM   685   C  CG1 . ILE   A  1 92  ? -58.485 17.561  -50.725  1.00 50.90  ? 393  ILE   A CG1 1 
ATOM   686   C  CG2 . ILE   A  1 92  ? -60.509 16.247  -50.009  1.00 56.49  ? 393  ILE   A CG2 1 
ATOM   687   C  CD1 . ILE   A  1 92  ? -58.264 18.114  -49.349  1.00 36.06  ? 393  ILE   A CD1 1 
ATOM   688   N  N   . ASP   A  1 93  ? -62.237 17.260  -53.321  1.00 76.31  ? 394  ASP   A N   1 
ATOM   689   C  CA  . ASP   A  1 93  ? -63.599 16.991  -53.778  1.00 73.92  ? 394  ASP   A CA  1 
ATOM   690   C  C   . ASP   A  1 93  ? -63.606 16.057  -54.981  1.00 69.41  ? 394  ASP   A C   1 
ATOM   691   O  O   . ASP   A  1 93  ? -64.339 15.061  -55.002  1.00 70.61  ? 394  ASP   A O   1 
ATOM   692   C  CB  . ASP   A  1 93  ? -64.309 18.293  -54.130  1.00 80.93  ? 394  ASP   A CB  1 
ATOM   693   C  CG  . ASP   A  1 93  ? -65.293 18.717  -53.080  1.00 91.41  ? 394  ASP   A CG  1 
ATOM   694   O  OD1 . ASP   A  1 93  ? -65.106 18.338  -51.905  1.00 96.55  ? 394  ASP   A OD1 1 
ATOM   695   O  OD2 . ASP   A  1 93  ? -66.260 19.423  -53.433  1.00 93.71  ? 394  ASP   A OD2 1 
ATOM   696   N  N   . THR   A  1 94  ? -62.815 16.377  -56.009  1.00 61.78  ? 395  THR   A N   1 
ATOM   697   C  CA  . THR   A  1 94  ? -62.779 15.534  -57.199  1.00 69.25  ? 395  THR   A CA  1 
ATOM   698   C  C   . THR   A  1 94  ? -62.171 14.173  -56.889  1.00 76.71  ? 395  THR   A C   1 
ATOM   699   O  O   . THR   A  1 94  ? -62.822 13.133  -57.048  1.00 84.24  ? 395  THR   A O   1 
ATOM   700   C  CB  . THR   A  1 94  ? -61.990 16.217  -58.321  1.00 67.54  ? 395  THR   A CB  1 
ATOM   701   O  OG1 . THR   A  1 94  ? -61.246 17.314  -57.786  1.00 74.64  ? 395  THR   A OG1 1 
ATOM   702   C  CG2 . THR   A  1 94  ? -62.918 16.714  -59.409  1.00 60.65  ? 395  THR   A CG2 1 
ATOM   703   N  N   . THR   A  1 95  ? -60.921 14.164  -56.432  1.00 72.85  ? 396  THR   A N   1 
ATOM   704   C  CA  . THR   A  1 95  ? -60.088 12.973  -56.444  1.00 62.38  ? 396  THR   A CA  1 
ATOM   705   C  C   . THR   A  1 95  ? -59.965 12.301  -55.087  1.00 69.15  ? 396  THR   A C   1 
ATOM   706   O  O   . THR   A  1 95  ? -59.327 11.245  -54.999  1.00 73.69  ? 396  THR   A O   1 
ATOM   707   C  CB  . THR   A  1 95  ? -58.686 13.327  -56.952  1.00 55.94  ? 396  THR   A CB  1 
ATOM   708   O  OG1 . THR   A  1 95  ? -57.970 14.014  -55.919  1.00 60.12  ? 396  THR   A OG1 1 
ATOM   709   C  CG2 . THR   A  1 95  ? -58.760 14.215  -58.203  1.00 49.39  ? 396  THR   A CG2 1 
ATOM   710   N  N   . SER   A  1 96  ? -60.532 12.889  -54.034  1.00 62.76  ? 397  SER   A N   1 
ATOM   711   C  CA  . SER   A  1 96  ? -60.458 12.399  -52.663  1.00 65.97  ? 397  SER   A CA  1 
ATOM   712   C  C   . SER   A  1 96  ? -59.063 12.522  -52.064  1.00 57.78  ? 397  SER   A C   1 
ATOM   713   O  O   . SER   A  1 96  ? -58.803 11.938  -51.014  1.00 53.19  ? 397  SER   A O   1 
ATOM   714   C  CB  . SER   A  1 96  ? -60.944 10.949  -52.557  1.00 72.20  ? 397  SER   A CB  1 
ATOM   715   O  OG  . SER   A  1 96  ? -62.234 10.820  -53.131  1.00 76.34  ? 397  SER   A OG  1 
ATOM   716   N  N   . THR   A  1 97  ? -58.168 13.268  -52.702  1.00 57.53  ? 398  THR   A N   1 
ATOM   717   C  CA  . THR   A  1 97  ? -56.794 13.477  -52.253  1.00 51.27  ? 398  THR   A CA  1 
ATOM   718   C  C   . THR   A  1 97  ? -56.252 14.662  -53.042  1.00 53.90  ? 398  THR   A C   1 
ATOM   719   O  O   . THR   A  1 97  ? -56.943 15.215  -53.903  1.00 56.35  ? 398  THR   A O   1 
ATOM   720   C  CB  . THR   A  1 97  ? -55.928 12.233  -52.454  1.00 48.58  ? 398  THR   A CB  1 
ATOM   721   O  OG1 . THR   A  1 97  ? -54.599 12.496  -51.990  1.00 50.53  ? 398  THR   A OG1 1 
ATOM   722   C  CG2 . THR   A  1 97  ? -55.886 11.830  -53.938  1.00 44.13  ? 398  THR   A CG2 1 
ATOM   723   N  N   . TYR   A  1 98  ? -55.009 15.050  -52.751  1.00 47.71  ? 399  TYR   A N   1 
ATOM   724   C  CA  . TYR   A  1 98  ? -54.402 16.171  -53.460  1.00 49.09  ? 399  TYR   A CA  1 
ATOM   725   C  C   . TYR   A  1 98  ? -52.905 15.941  -53.610  1.00 47.50  ? 399  TYR   A C   1 
ATOM   726   O  O   . TYR   A  1 98  ? -52.336 14.989  -53.065  1.00 48.96  ? 399  TYR   A O   1 
ATOM   727   C  CB  . TYR   A  1 98  ? -54.697 17.505  -52.756  1.00 47.98  ? 399  TYR   A CB  1 
ATOM   728   C  CG  . TYR   A  1 98  ? -54.017 17.716  -51.422  1.00 48.79  ? 399  TYR   A CG  1 
ATOM   729   C  CD1 . TYR   A  1 98  ? -54.440 17.034  -50.281  1.00 50.19  ? 399  TYR   A CD1 1 
ATOM   730   C  CD2 . TYR   A  1 98  ? -52.969 18.622  -51.291  1.00 47.37  ? 399  TYR   A CD2 1 
ATOM   731   C  CE1 . TYR   A  1 98  ? -53.823 17.230  -49.058  1.00 45.02  ? 399  TYR   A CE1 1 
ATOM   732   C  CE2 . TYR   A  1 98  ? -52.348 18.830  -50.063  1.00 51.03  ? 399  TYR   A CE2 1 
ATOM   733   C  CZ  . TYR   A  1 98  ? -52.778 18.128  -48.954  1.00 47.60  ? 399  TYR   A CZ  1 
ATOM   734   O  OH  . TYR   A  1 98  ? -52.176 18.328  -47.737  1.00 50.95  ? 399  TYR   A OH  1 
ATOM   735   N  N   . GLN   A  1 99  ? -52.268 16.828  -54.371  1.00 38.48  ? 400  GLN   A N   1 
ATOM   736   C  CA  . GLN   A  1 99  ? -50.841 16.747  -54.654  1.00 41.31  ? 400  GLN   A CA  1 
ATOM   737   C  C   . GLN   A  1 99  ? -50.127 17.958  -54.071  1.00 46.50  ? 400  GLN   A C   1 
ATOM   738   O  O   . GLN   A  1 99  ? -50.526 19.097  -54.341  1.00 50.99  ? 400  GLN   A O   1 
ATOM   739   C  CB  . GLN   A  1 99  ? -50.577 16.688  -56.167  1.00 48.33  ? 400  GLN   A CB  1 
ATOM   740   C  CG  . GLN   A  1 99  ? -51.097 15.452  -56.840  1.00 48.22  ? 400  GLN   A CG  1 
ATOM   741   C  CD  . GLN   A  1 99  ? -50.512 14.204  -56.220  1.00 51.16  ? 400  GLN   A CD  1 
ATOM   742   O  OE1 . GLN   A  1 99  ? -49.291 14.039  -56.154  1.00 59.15  ? 400  GLN   A OE1 1 
ATOM   743   N  NE2 . GLN   A  1 99  ? -51.379 13.322  -55.747  1.00 44.32  ? 400  GLN   A NE2 1 
ATOM   744   N  N   . LEU   A  1 100 ? -49.058 17.719  -53.306  1.00 40.80  ? 401  LEU   A N   1 
ATOM   745   C  CA  . LEU   A  1 100 ? -48.214 18.827  -52.858  1.00 41.25  ? 401  LEU   A CA  1 
ATOM   746   C  C   . LEU   A  1 100 ? -47.452 19.427  -54.035  1.00 45.93  ? 401  LEU   A C   1 
ATOM   747   O  O   . LEU   A  1 100 ? -47.032 18.709  -54.944  1.00 51.94  ? 401  LEU   A O   1 
ATOM   748   C  CB  . LEU   A  1 100 ? -47.220 18.359  -51.788  1.00 29.83  ? 401  LEU   A CB  1 
ATOM   749   C  CG  . LEU   A  1 100 ? -47.858 17.795  -50.508  1.00 29.79  ? 401  LEU   A CG  1 
ATOM   750   C  CD1 . LEU   A  1 100 ? -46.805 17.169  -49.563  1.00 28.84  ? 401  LEU   A CD1 1 
ATOM   751   C  CD2 . LEU   A  1 100 ? -48.657 18.875  -49.786  1.00 32.28  ? 401  LEU   A CD2 1 
ATOM   752   N  N   . LYS   A  1 101 ? -47.285 20.754  -54.016  1.00 45.24  ? 402  LYS   A N   1 
ATOM   753   C  CA  . LYS   A  1 101 ? -46.272 21.416  -54.834  1.00 35.90  ? 402  LYS   A CA  1 
ATOM   754   C  C   . LYS   A  1 101 ? -44.876 21.022  -54.356  1.00 42.19  ? 402  LYS   A C   1 
ATOM   755   O  O   . LYS   A  1 101 ? -44.696 20.519  -53.245  1.00 49.14  ? 402  LYS   A O   1 
ATOM   756   C  CB  . LYS   A  1 101 ? -46.422 22.936  -54.766  1.00 37.69  ? 402  LYS   A CB  1 
ATOM   757   C  CG  . LYS   A  1 101 ? -47.766 23.445  -55.262  1.00 56.05  ? 402  LYS   A CG  1 
ATOM   758   C  CD  . LYS   A  1 101 ? -47.634 24.172  -56.596  1.00 66.66  ? 402  LYS   A CD  1 
ATOM   759   C  CE  . LYS   A  1 101 ? -48.786 23.855  -57.538  1.00 73.42  ? 402  LYS   A CE  1 
ATOM   760   N  NZ  . LYS   A  1 101 ? -50.097 23.960  -56.857  1.00 78.28  ? 402  LYS   A NZ  1 
ATOM   761   N  N   . ASP   A  1 102 ? -43.875 21.287  -55.198  1.00 47.35  ? 403  ASP   A N   1 
ATOM   762   C  CA  . ASP   A  1 102 ? -42.504 20.941  -54.835  1.00 45.12  ? 403  ASP   A CA  1 
ATOM   763   C  C   . ASP   A  1 102 ? -42.065 21.698  -53.591  1.00 40.57  ? 403  ASP   A C   1 
ATOM   764   O  O   . ASP   A  1 102 ? -41.465 21.119  -52.679  1.00 44.84  ? 403  ASP   A O   1 
ATOM   765   C  CB  . ASP   A  1 102 ? -41.554 21.231  -55.997  1.00 53.19  ? 403  ASP   A CB  1 
ATOM   766   C  CG  . ASP   A  1 102 ? -41.853 20.382  -57.232  1.00 64.21  ? 403  ASP   A CG  1 
ATOM   767   O  OD1 . ASP   A  1 102 ? -42.762 19.523  -57.173  1.00 58.83  ? 403  ASP   A OD1 1 
ATOM   768   O  OD2 . ASP   A  1 102 ? -41.177 20.587  -58.266  1.00 71.95  ? 403  ASP   A OD2 1 
ATOM   769   N  N   . THR   A  1 103 ? -42.351 23.003  -53.543  1.00 41.92  ? 404  THR   A N   1 
ATOM   770   C  CA  . THR   A  1 103 ? -41.995 23.816  -52.382  1.00 44.45  ? 404  THR   A CA  1 
ATOM   771   C  C   . THR   A  1 103 ? -42.590 23.257  -51.089  1.00 41.61  ? 404  THR   A C   1 
ATOM   772   O  O   . THR   A  1 103 ? -41.914 23.189  -50.065  1.00 41.27  ? 404  THR   A O   1 
ATOM   773   C  CB  . THR   A  1 103 ? -42.480 25.245  -52.586  1.00 45.13  ? 404  THR   A CB  1 
ATOM   774   O  OG1 . THR   A  1 103 ? -43.828 25.201  -53.060  1.00 45.01  ? 404  THR   A OG1 1 
ATOM   775   C  CG2 . THR   A  1 103 ? -41.607 25.967  -53.588  1.00 53.58  ? 404  THR   A CG2 1 
ATOM   776   N  N   . GLU   A  1 104 ? -43.873 22.891  -51.120  1.00 43.45  ? 405  GLU   A N   1 
ATOM   777   C  CA  . GLU   A  1 104 ? -44.540 22.374  -49.934  1.00 37.24  ? 405  GLU   A CA  1 
ATOM   778   C  C   . GLU   A  1 104 ? -43.948 21.036  -49.523  1.00 42.64  ? 405  GLU   A C   1 
ATOM   779   O  O   . GLU   A  1 104 ? -43.844 20.735  -48.326  1.00 43.20  ? 405  GLU   A O   1 
ATOM   780   C  CB  . GLU   A  1 104 ? -46.047 22.230  -50.192  1.00 32.40  ? 405  GLU   A CB  1 
ATOM   781   C  CG  . GLU   A  1 104 ? -46.730 23.466  -50.744  1.00 32.73  ? 405  GLU   A CG  1 
ATOM   782   C  CD  . GLU   A  1 104 ? -48.099 23.171  -51.332  1.00 40.35  ? 405  GLU   A CD  1 
ATOM   783   O  OE1 . GLU   A  1 104 ? -48.913 24.111  -51.468  1.00 47.32  ? 405  GLU   A OE1 1 
ATOM   784   O  OE2 . GLU   A  1 104 ? -48.357 21.998  -51.666  1.00 47.73  ? 405  GLU   A OE2 1 
ATOM   785   N  N   . LEU   A  1 105 ? -43.564 20.216  -50.504  1.00 40.11  ? 406  LEU   A N   1 
ATOM   786   C  CA  . LEU   A  1 105 ? -42.969 18.922  -50.199  1.00 43.28  ? 406  LEU   A CA  1 
ATOM   787   C  C   . LEU   A  1 105 ? -41.647 19.097  -49.461  1.00 45.95  ? 406  LEU   A C   1 
ATOM   788   O  O   . LEU   A  1 105 ? -41.401 18.444  -48.444  1.00 39.98  ? 406  LEU   A O   1 
ATOM   789   C  CB  . LEU   A  1 105 ? -42.768 18.115  -51.484  1.00 39.67  ? 406  LEU   A CB  1 
ATOM   790   C  CG  . LEU   A  1 105 ? -42.208 16.705  -51.292  1.00 37.09  ? 406  LEU   A CG  1 
ATOM   791   C  CD1 . LEU   A  1 105 ? -43.283 15.715  -50.860  1.00 38.29  ? 406  LEU   A CD1 1 
ATOM   792   C  CD2 . LEU   A  1 105 ? -41.536 16.241  -52.560  1.00 39.41  ? 406  LEU   A CD2 1 
ATOM   793   N  N   . ILE   A  1 106 ? -40.782 19.978  -49.970  1.00 42.59  ? 407  ILE   A N   1 
ATOM   794   C  CA  . ILE   A  1 106 ? -39.507 20.250  -49.312  1.00 36.57  ? 407  ILE   A CA  1 
ATOM   795   C  C   . ILE   A  1 106 ? -39.731 20.804  -47.907  1.00 35.78  ? 407  ILE   A C   1 
ATOM   796   O  O   . ILE   A  1 106 ? -39.028 20.433  -46.963  1.00 33.01  ? 407  ILE   A O   1 
ATOM   797   C  CB  . ILE   A  1 106 ? -38.670 21.218  -50.167  1.00 37.11  ? 407  ILE   A CB  1 
ATOM   798   C  CG1 . ILE   A  1 106 ? -38.127 20.509  -51.408  1.00 35.23  ? 407  ILE   A CG1 1 
ATOM   799   C  CG2 . ILE   A  1 106 ? -37.556 21.847  -49.347  1.00 36.64  ? 407  ILE   A CG2 1 
ATOM   800   C  CD1 . ILE   A  1 106 ? -37.691 21.472  -52.495  1.00 35.26  ? 407  ILE   A CD1 1 
ATOM   801   N  N   . TYR   A  1 107 ? -40.692 21.721  -47.761  1.00 36.46  ? 408  TYR   A N   1 
ATOM   802   C  CA  . TYR   A  1 107 ? -40.980 22.330  -46.470  1.00 40.89  ? 408  TYR   A CA  1 
ATOM   803   C  C   . TYR   A  1 107 ? -41.477 21.288  -45.480  1.00 44.13  ? 408  TYR   A C   1 
ATOM   804   O  O   . TYR   A  1 107 ? -41.033 21.249  -44.326  1.00 33.91  ? 408  TYR   A O   1 
ATOM   805   C  CB  . TYR   A  1 107 ? -42.017 23.441  -46.640  1.00 37.97  ? 408  TYR   A CB  1 
ATOM   806   C  CG  . TYR   A  1 107 ? -42.627 23.894  -45.325  1.00 38.35  ? 408  TYR   A CG  1 
ATOM   807   C  CD1 . TYR   A  1 107 ? -43.748 23.258  -44.799  1.00 39.34  ? 408  TYR   A CD1 1 
ATOM   808   C  CD2 . TYR   A  1 107 ? -42.077 24.949  -44.615  1.00 32.46  ? 408  TYR   A CD2 1 
ATOM   809   C  CE1 . TYR   A  1 107 ? -44.297 23.653  -43.584  1.00 40.74  ? 408  TYR   A CE1 1 
ATOM   810   C  CE2 . TYR   A  1 107 ? -42.622 25.359  -43.400  1.00 38.88  ? 408  TYR   A CE2 1 
ATOM   811   C  CZ  . TYR   A  1 107 ? -43.729 24.707  -42.887  1.00 42.84  ? 408  TYR   A CZ  1 
ATOM   812   O  OH  . TYR   A  1 107 ? -44.278 25.121  -41.690  1.00 48.09  ? 408  TYR   A OH  1 
ATOM   813   N  N   . GLY   A  1 108 ? -42.415 20.443  -45.927  1.00 40.95  ? 409  GLY   A N   1 
ATOM   814   C  CA  . GLY   A  1 108 ? -42.938 19.377  -45.089  1.00 29.73  ? 409  GLY   A CA  1 
ATOM   815   C  C   . GLY   A  1 108 ? -41.878 18.388  -44.648  1.00 33.91  ? 409  GLY   A C   1 
ATOM   816   O  O   . GLY   A  1 108 ? -41.824 18.016  -43.479  1.00 37.78  ? 409  GLY   A O   1 
ATOM   817   N  N   . ALA   A  1 109 ? -41.010 17.955  -45.571  1.00 29.84  ? 410  ALA   A N   1 
ATOM   818   C  CA  . ALA   A  1 109 ? -39.989 16.975  -45.207  1.00 36.59  ? 410  ALA   A CA  1 
ATOM   819   C  C   . ALA   A  1 109 ? -38.993 17.549  -44.211  1.00 38.29  ? 410  ALA   A C   1 
ATOM   820   O  O   . ALA   A  1 109 ? -38.563 16.852  -43.282  1.00 34.34  ? 410  ALA   A O   1 
ATOM   821   C  CB  . ALA   A  1 109 ? -39.250 16.470  -46.440  1.00 36.22  ? 410  ALA   A CB  1 
ATOM   822   N  N   . LYS   A  1 110 ? -38.603 18.806  -44.395  1.00 24.65  ? 411  LYS   A N   1 
ATOM   823   C  CA  . LYS   A  1 110 ? -37.691 19.433  -43.449  1.00 38.36  ? 411  LYS   A CA  1 
ATOM   824   C  C   . LYS   A  1 110 ? -38.344 19.602  -42.083  1.00 44.23  ? 411  LYS   A C   1 
ATOM   825   O  O   . LYS   A  1 110 ? -37.694 19.415  -41.055  1.00 42.14  ? 411  LYS   A O   1 
ATOM   826   C  CB  . LYS   A  1 110 ? -37.216 20.785  -43.978  1.00 36.05  ? 411  LYS   A CB  1 
ATOM   827   C  CG  . LYS   A  1 110 ? -36.314 20.692  -45.208  1.00 36.91  ? 411  LYS   A CG  1 
ATOM   828   C  CD  . LYS   A  1 110 ? -35.924 22.068  -45.727  1.00 36.41  ? 411  LYS   A CD  1 
ATOM   829   C  CE  . LYS   A  1 110 ? -34.875 21.932  -46.809  1.00 39.89  ? 411  LYS   A CE  1 
ATOM   830   N  NZ  . LYS   A  1 110 ? -34.212 23.209  -47.122  1.00 49.65  ? 411  LYS   A NZ  1 
ATOM   831   N  N   . HIS   A  1 111 ? -39.627 19.939  -42.049  1.00 43.14  ? 412  HIS   A N   1 
ATOM   832   C  CA  . HIS   A  1 111 ? -40.258 20.172  -40.758  1.00 44.10  ? 412  HIS   A CA  1 
ATOM   833   C  C   . HIS   A  1 111 ? -40.576 18.869  -40.033  1.00 45.37  ? 412  HIS   A C   1 
ATOM   834   O  O   . HIS   A  1 111 ? -40.438 18.797  -38.809  1.00 38.56  ? 412  HIS   A O   1 
ATOM   835   C  CB  . HIS   A  1 111 ? -41.492 21.044  -40.943  1.00 30.92  ? 412  HIS   A CB  1 
ATOM   836   C  CG  . HIS   A  1 111 ? -41.160 22.501  -40.961  1.00 39.87  ? 412  HIS   A CG  1 
ATOM   837   N  ND1 . HIS   A  1 111 ? -40.411 23.080  -41.965  1.00 38.65  ? 412  HIS   A ND1 1 
ATOM   838   C  CD2 . HIS   A  1 111 ? -41.413 23.484  -40.064  1.00 38.08  ? 412  HIS   A CD2 1 
ATOM   839   C  CE1 . HIS   A  1 111 ? -40.236 24.362  -41.692  1.00 45.56  ? 412  HIS   A CE1 1 
ATOM   840   N  NE2 . HIS   A  1 111 ? -40.838 24.634  -40.547  1.00 38.11  ? 412  HIS   A NE2 1 
ATOM   841   N  N   . ALA   A  1 112 ? -40.949 17.820  -40.769  1.00 45.08  ? 413  ALA   A N   1 
ATOM   842   C  CA  . ALA   A  1 112 ? -41.069 16.500  -40.166  1.00 43.76  ? 413  ALA   A CA  1 
ATOM   843   C  C   . ALA   A  1 112 ? -39.789 16.084  -39.454  1.00 40.64  ? 413  ALA   A C   1 
ATOM   844   O  O   . ALA   A  1 112 ? -39.836 15.398  -38.432  1.00 34.01  ? 413  ALA   A O   1 
ATOM   845   C  CB  . ALA   A  1 112 ? -41.422 15.474  -41.229  1.00 36.89  ? 413  ALA   A CB  1 
ATOM   846   N  N   . TRP   A  1 113 ? -38.632 16.455  -39.998  1.00 37.91  ? 414  TRP   A N   1 
ATOM   847   C  CA  . TRP   A  1 113 ? -37.388 16.197  -39.285  1.00 35.64  ? 414  TRP   A CA  1 
ATOM   848   C  C   . TRP   A  1 113 ? -37.248 17.140  -38.103  1.00 37.87  ? 414  TRP   A C   1 
ATOM   849   O  O   . TRP   A  1 113 ? -36.869 16.718  -37.008  1.00 39.03  ? 414  TRP   A O   1 
ATOM   850   C  CB  . TRP   A  1 113 ? -36.194 16.329  -40.227  1.00 36.41  ? 414  TRP   A CB  1 
ATOM   851   C  CG  . TRP   A  1 113 ? -34.855 16.051  -39.607  1.00 37.58  ? 414  TRP   A CG  1 
ATOM   852   C  CD1 . TRP   A  1 113 ? -34.596 15.413  -38.402  1.00 33.42  ? 414  TRP   A CD1 1 
ATOM   853   C  CD2 . TRP   A  1 113 ? -33.576 16.392  -40.159  1.00 40.25  ? 414  TRP   A CD2 1 
ATOM   854   N  NE1 . TRP   A  1 113 ? -33.235 15.339  -38.194  1.00 23.07  ? 414  TRP   A NE1 1 
ATOM   855   C  CE2 . TRP   A  1 113 ? -32.589 15.959  -39.238  1.00 44.69  ? 414  TRP   A CE2 1 
ATOM   856   C  CE3 . TRP   A  1 113 ? -33.167 17.015  -41.346  1.00 33.44  ? 414  TRP   A CE3 1 
ATOM   857   C  CZ2 . TRP   A  1 113 ? -31.219 16.138  -39.474  1.00 39.76  ? 414  TRP   A CZ2 1 
ATOM   858   C  CZ3 . TRP   A  1 113 ? -31.807 17.205  -41.567  1.00 28.63  ? 414  TRP   A CZ3 1 
ATOM   859   C  CH2 . TRP   A  1 113 ? -30.851 16.750  -40.645  1.00 37.02  ? 414  TRP   A CH2 1 
ATOM   860   N  N   . ARG   A  1 114 ? -37.567 18.418  -38.313  1.00 33.58  ? 415  ARG   A N   1 
ATOM   861   C  CA  . ARG   A  1 114 ? -37.526 19.412  -37.253  1.00 29.93  ? 415  ARG   A CA  1 
ATOM   862   C  C   . ARG   A  1 114 ? -38.400 19.011  -36.070  1.00 41.25  ? 415  ARG   A C   1 
ATOM   863   O  O   . ARG   A  1 114 ? -38.077 19.334  -34.925  1.00 28.95  ? 415  ARG   A O   1 
ATOM   864   C  CB  . ARG   A  1 114 ? -37.997 20.746  -37.810  1.00 28.22  ? 415  ARG   A CB  1 
ATOM   865   C  CG  . ARG   A  1 114 ? -37.674 21.960  -36.984  1.00 34.14  ? 415  ARG   A CG  1 
ATOM   866   C  CD  . ARG   A  1 114 ? -38.334 23.198  -37.567  1.00 32.96  ? 415  ARG   A CD  1 
ATOM   867   N  NE  . ARG   A  1 114 ? -37.975 24.402  -36.825  1.00 35.58  ? 415  ARG   A NE  1 
ATOM   868   C  CZ  . ARG   A  1 114 ? -38.329 25.636  -37.167  1.00 39.12  ? 415  ARG   A CZ  1 
ATOM   869   N  NH1 . ARG   A  1 114 ? -37.954 26.672  -36.413  1.00 34.62  ? 415  ARG   A NH1 1 
ATOM   870   N  NH2 . ARG   A  1 114 ? -39.043 25.839  -38.269  1.00 36.73  ? 415  ARG   A NH2 1 
ATOM   871   N  N   . ASN   A  1 115 ? -39.510 18.330  -36.340  1.00 38.81  ? 416  ASN   A N   1 
ATOM   872   C  CA  . ASN   A  1 115 ? -40.501 17.954  -35.350  1.00 38.92  ? 416  ASN   A CA  1 
ATOM   873   C  C   . ASN   A  1 115 ? -40.226 16.596  -34.721  1.00 39.50  ? 416  ASN   A C   1 
ATOM   874   O  O   . ASN   A  1 115 ? -41.019 16.153  -33.886  1.00 46.76  ? 416  ASN   A O   1 
ATOM   875   C  CB  . ASN   A  1 115 ? -41.894 17.930  -35.991  1.00 34.41  ? 416  ASN   A CB  1 
ATOM   876   C  CG  . ASN   A  1 115 ? -42.400 19.313  -36.385  1.00 35.00  ? 416  ASN   A CG  1 
ATOM   877   O  OD1 . ASN   A  1 115 ? -41.884 20.339  -35.939  1.00 34.71  ? 416  ASN   A OD1 1 
ATOM   878   N  ND2 . ASN   A  1 115 ? -43.442 19.337  -37.223  1.00 35.49  ? 416  ASN   A ND2 1 
ATOM   879   N  N   . ALA   A  1 116 ? -39.147 15.914  -35.118  1.00 36.62  ? 417  ALA   A N   1 
ATOM   880   C  CA  . ALA   A  1 116 ? -38.855 14.573  -34.626  1.00 36.52  ? 417  ALA   A CA  1 
ATOM   881   C  C   . ALA   A  1 116 ? -38.325 14.622  -33.187  1.00 37.15  ? 417  ALA   A C   1 
ATOM   882   O  O   . ALA   A  1 116 ? -37.125 14.778  -32.970  1.00 31.74  ? 417  ALA   A O   1 
ATOM   883   C  CB  . ALA   A  1 116 ? -37.860 13.873  -35.560  1.00 33.74  ? 417  ALA   A CB  1 
ATOM   884   N  N   . SER   A  1 117 ? -39.221 14.476  -32.203  1.00 39.42  ? 418  SER   A N   1 
ATOM   885   C  CA  A SER   A  1 117 ? -38.815 14.691  -30.818  0.74 36.11  ? 418  SER   A CA  1 
ATOM   886   C  CA  B SER   A  1 117 ? -38.865 14.631  -30.793  0.26 35.95  ? 418  SER   A CA  1 
ATOM   887   C  C   . SER   A  1 117 ? -37.684 13.761  -30.379  1.00 40.65  ? 418  SER   A C   1 
ATOM   888   O  O   . SER   A  1 117 ? -36.942 14.118  -29.463  1.00 44.11  ? 418  SER   A O   1 
ATOM   889   C  CB  A SER   A  1 117 ? -40.021 14.544  -29.889  0.74 31.98  ? 418  SER   A CB  1 
ATOM   890   C  CB  B SER   A  1 117 ? -40.070 14.289  -29.917  0.26 32.85  ? 418  SER   A CB  1 
ATOM   891   O  OG  A SER   A  1 117 ? -40.491 13.211  -29.820  0.74 32.88  ? 418  SER   A OG  1 
ATOM   892   O  OG  B SER   A  1 117 ? -41.083 15.277  -29.982  0.26 30.94  ? 418  SER   A OG  1 
ATOM   893   N  N   . ARG   A  1 118 ? -37.505 12.606  -31.027  1.00 37.73  ? 419  ARG   A N   1 
ATOM   894   C  CA  . ARG   A  1 118 ? -36.482 11.652  -30.625  1.00 30.86  ? 419  ARG   A CA  1 
ATOM   895   C  C   . ARG   A  1 118 ? -35.134 11.829  -31.315  1.00 36.85  ? 419  ARG   A C   1 
ATOM   896   O  O   . ARG   A  1 118 ? -34.216 11.065  -31.010  1.00 40.28  ? 419  ARG   A O   1 
ATOM   897   C  CB  . ARG   A  1 118 ? -36.972 10.219  -30.863  1.00 31.83  ? 419  ARG   A CB  1 
ATOM   898   C  CG  . ARG   A  1 118 ? -38.157 9.818   -30.000  1.00 29.11  ? 419  ARG   A CG  1 
ATOM   899   C  CD  . ARG   A  1 118 ? -38.562 8.388   -30.209  1.00 27.43  ? 419  ARG   A CD  1 
ATOM   900   N  NE  . ARG   A  1 118 ? -39.541 8.012   -29.187  1.00 41.17  ? 419  ARG   A NE  1 
ATOM   901   C  CZ  . ARG   A  1 118 ? -40.254 6.888   -29.187  1.00 45.87  ? 419  ARG   A CZ  1 
ATOM   902   N  NH1 . ARG   A  1 118 ? -40.112 5.999   -30.161  1.00 44.16  ? 419  ARG   A NH1 1 
ATOM   903   N  NH2 . ARG   A  1 118 ? -41.124 6.664   -28.212  1.00 45.61  ? 419  ARG   A NH2 1 
ATOM   904   N  N   . CYS   A  1 119 ? -34.971 12.787  -32.230  1.00 36.78  ? 420  CYS   A N   1 
ATOM   905   C  CA  . CYS   A  1 119 ? -33.719 12.924  -32.980  1.00 32.58  ? 420  CYS   A CA  1 
ATOM   906   C  C   . CYS   A  1 119 ? -32.849 14.019  -32.365  1.00 29.46  ? 420  CYS   A C   1 
ATOM   907   O  O   . CYS   A  1 119 ? -33.281 15.170  -32.231  1.00 29.94  ? 420  CYS   A O   1 
ATOM   908   C  CB  . CYS   A  1 119 ? -33.985 13.215  -34.459  1.00 35.50  ? 420  CYS   A CB  1 
ATOM   909   S  SG  . CYS   A  1 119 ? -32.490 13.624  -35.445  1.00 36.07  ? 420  CYS   A SG  1 
ATOM   910   N  N   . VAL   A  1 120 ? -31.624 13.650  -31.985  1.00 35.19  ? 421  VAL   A N   1 
ATOM   911   C  CA  . VAL   A  1 120 ? -30.687 14.598  -31.394  1.00 29.54  ? 421  VAL   A CA  1 
ATOM   912   C  C   . VAL   A  1 120 ? -29.939 15.400  -32.444  1.00 38.78  ? 421  VAL   A C   1 
ATOM   913   O  O   . VAL   A  1 120 ? -29.288 16.396  -32.100  1.00 32.18  ? 421  VAL   A O   1 
ATOM   914   C  CB  . VAL   A  1 120 ? -29.731 13.824  -30.463  1.00 43.40  ? 421  VAL   A CB  1 
ATOM   915   C  CG1 . VAL   A  1 120 ? -28.744 12.958  -31.240  1.00 23.92  ? 421  VAL   A CG1 1 
ATOM   916   C  CG2 . VAL   A  1 120 ? -29.027 14.746  -29.441  1.00 39.79  ? 421  VAL   A CG2 1 
ATOM   917   N  N   . GLY   A  1 121 ? -30.043 15.020  -33.726  1.00 39.95  ? 422  GLY   A N   1 
ATOM   918   C  CA  . GLY   A  1 121 ? -29.281 15.681  -34.761  1.00 25.45  ? 422  GLY   A CA  1 
ATOM   919   C  C   . GLY   A  1 121 ? -29.962 16.847  -35.451  1.00 37.03  ? 422  GLY   A C   1 
ATOM   920   O  O   . GLY   A  1 121 ? -29.503 17.280  -36.513  1.00 43.69  ? 422  GLY   A O   1 
ATOM   921   N  N   . ARG   A  1 122 ? -31.025 17.391  -34.857  1.00 35.23  ? 423  ARG   A N   1 
ATOM   922   C  CA  . ARG   A  1 122 ? -31.884 18.348  -35.545  1.00 34.72  ? 423  ARG   A CA  1 
ATOM   923   C  C   . ARG   A  1 122 ? -31.308 19.751  -35.700  1.00 36.46  ? 423  ARG   A C   1 
ATOM   924   O  O   . ARG   A  1 122 ? -31.966 20.588  -36.332  1.00 35.07  ? 423  ARG   A O   1 
ATOM   925   C  CB  . ARG   A  1 122 ? -33.220 18.438  -34.836  1.00 30.03  ? 423  ARG   A CB  1 
ATOM   926   C  CG  . ARG   A  1 122 ? -34.108 17.243  -35.053  1.00 34.42  ? 423  ARG   A CG  1 
ATOM   927   C  CD  . ARG   A  1 122 ? -35.374 17.462  -34.273  1.00 35.76  ? 423  ARG   A CD  1 
ATOM   928   N  NE  . ARG   A  1 122 ? -35.230 17.065  -32.876  1.00 37.13  ? 423  ARG   A NE  1 
ATOM   929   C  CZ  . ARG   A  1 122 ? -36.104 17.393  -31.930  1.00 42.67  ? 423  ARG   A CZ  1 
ATOM   930   N  NH1 . ARG   A  1 122 ? -37.165 18.147  -32.240  1.00 24.31  ? 423  ARG   A NH1 1 
ATOM   931   N  NH2 . ARG   A  1 122 ? -35.921 16.963  -30.680  1.00 37.97  ? 423  ARG   A NH2 1 
ATOM   932   N  N   . ILE   A  1 123 ? -30.127 20.052  -35.149  1.00 33.04  ? 424  ILE   A N   1 
ATOM   933   C  CA  . ILE   A  1 123 ? -29.523 21.348  -35.445  1.00 33.98  ? 424  ILE   A CA  1 
ATOM   934   C  C   . ILE   A  1 123 ? -29.268 21.503  -36.942  1.00 39.00  ? 424  ILE   A C   1 
ATOM   935   O  O   . ILE   A  1 123 ? -29.130 22.624  -37.432  1.00 42.19  ? 424  ILE   A O   1 
ATOM   936   C  CB  . ILE   A  1 123 ? -28.212 21.572  -34.650  1.00 36.15  ? 424  ILE   A CB  1 
ATOM   937   C  CG1 . ILE   A  1 123 ? -27.788 23.042  -34.736  1.00 38.08  ? 424  ILE   A CG1 1 
ATOM   938   C  CG2 . ILE   A  1 123 ? -27.086 20.719  -35.198  1.00 38.52  ? 424  ILE   A CG2 1 
ATOM   939   C  CD1 . ILE   A  1 123 ? -26.656 23.432  -33.833  1.00 37.19  ? 424  ILE   A CD1 1 
ATOM   940   N  N   . GLN   A  1 124 ? -29.245 20.403  -37.683  1.00 44.58  ? 425  GLN   A N   1 
ATOM   941   C  CA  . GLN   A  1 124 ? -28.997 20.397  -39.120  1.00 49.51  ? 425  GLN   A CA  1 
ATOM   942   C  C   . GLN   A  1 124 ? -30.272 20.398  -39.962  1.00 51.50  ? 425  GLN   A C   1 
ATOM   943   O  O   . GLN   A  1 124 ? -30.169 20.358  -41.193  1.00 47.07  ? 425  GLN   A O   1 
ATOM   944   C  CB  . GLN   A  1 124 ? -28.159 19.164  -39.491  1.00 53.08  ? 425  GLN   A CB  1 
ATOM   945   C  CG  . GLN   A  1 124 ? -26.769 19.103  -38.869  1.00 51.93  ? 425  GLN   A CG  1 
ATOM   946   C  CD  . GLN   A  1 124 ? -25.748 19.836  -39.711  1.00 53.93  ? 425  GLN   A CD  1 
ATOM   947   O  OE1 . GLN   A  1 124 ? -26.065 20.301  -40.796  1.00 55.13  ? 425  GLN   A OE1 1 
ATOM   948   N  NE2 . GLN   A  1 124 ? -24.520 19.941  -39.218  1.00 57.08  ? 425  GLN   A NE2 1 
ATOM   949   N  N   . TRP   A  1 125 ? -31.460 20.470  -39.333  1.00 44.35  ? 426  TRP   A N   1 
ATOM   950   C  CA  . TRP   A  1 125 ? -32.712 20.160  -40.026  1.00 35.67  ? 426  TRP   A CA  1 
ATOM   951   C  C   . TRP   A  1 125 ? -32.930 20.991  -41.289  1.00 46.84  ? 426  TRP   A C   1 
ATOM   952   O  O   . TRP   A  1 125 ? -33.577 20.526  -42.232  1.00 51.55  ? 426  TRP   A O   1 
ATOM   953   C  CB  . TRP   A  1 125 ? -33.915 20.357  -39.099  1.00 34.31  ? 426  TRP   A CB  1 
ATOM   954   C  CG  . TRP   A  1 125 ? -34.270 21.806  -38.852  1.00 40.45  ? 426  TRP   A CG  1 
ATOM   955   C  CD1 . TRP   A  1 125 ? -33.760 22.624  -37.874  1.00 46.27  ? 426  TRP   A CD1 1 
ATOM   956   C  CD2 . TRP   A  1 125 ? -35.211 22.603  -39.588  1.00 39.76  ? 426  TRP   A CD2 1 
ATOM   957   N  NE1 . TRP   A  1 125 ? -34.321 23.881  -37.966  1.00 40.79  ? 426  TRP   A NE1 1 
ATOM   958   C  CE2 . TRP   A  1 125 ? -35.209 23.895  -39.011  1.00 38.83  ? 426  TRP   A CE2 1 
ATOM   959   C  CE3 . TRP   A  1 125 ? -36.054 22.351  -40.676  1.00 38.12  ? 426  TRP   A CE3 1 
ATOM   960   C  CZ2 . TRP   A  1 125 ? -36.022 24.929  -39.486  1.00 37.33  ? 426  TRP   A CZ2 1 
ATOM   961   C  CZ3 . TRP   A  1 125 ? -36.852 23.378  -41.148  1.00 37.34  ? 426  TRP   A CZ3 1 
ATOM   962   C  CH2 . TRP   A  1 125 ? -36.832 24.652  -40.553  1.00 41.39  ? 426  TRP   A CH2 1 
ATOM   963   N  N   . SER   A  1 126 ? -32.438 22.225  -41.329  1.00 41.53  ? 427  SER   A N   1 
ATOM   964   C  CA  . SER   A  1 126 ? -32.763 23.041  -42.485  1.00 39.61  ? 427  SER   A CA  1 
ATOM   965   C  C   . SER   A  1 126 ? -31.856 22.750  -43.676  1.00 39.89  ? 427  SER   A C   1 
ATOM   966   O  O   . SER   A  1 126 ? -32.191 23.153  -44.787  1.00 41.09  ? 427  SER   A O   1 
ATOM   967   C  CB  . SER   A  1 126 ? -32.702 24.525  -42.136  1.00 34.27  ? 427  SER   A CB  1 
ATOM   968   O  OG  . SER   A  1 126 ? -31.355 24.946  -41.993  1.00 42.36  ? 427  SER   A OG  1 
ATOM   969   N  N   . LYS   A  1 127 ? -30.734 22.056  -43.475  1.00 44.07  ? 428  LYS   A N   1 
ATOM   970   C  CA  . LYS   A  1 127 ? -29.835 21.673  -44.564  1.00 46.05  ? 428  LYS   A CA  1 
ATOM   971   C  C   . LYS   A  1 127 ? -30.120 20.218  -44.922  1.00 57.81  ? 428  LYS   A C   1 
ATOM   972   O  O   . LYS   A  1 127 ? -29.426 19.296  -44.493  1.00 76.13  ? 428  LYS   A O   1 
ATOM   973   C  CB  . LYS   A  1 127 ? -28.374 21.876  -44.162  1.00 46.32  ? 428  LYS   A CB  1 
ATOM   974   C  CG  . LYS   A  1 127 ? -27.967 23.325  -43.944  1.00 60.44  ? 428  LYS   A CG  1 
ATOM   975   C  CD  . LYS   A  1 127 ? -26.654 23.649  -44.662  1.00 75.42  ? 428  LYS   A CD  1 
ATOM   976   C  CE  . LYS   A  1 127 ? -26.894 24.331  -46.022  1.00 80.28  ? 428  LYS   A CE  1 
ATOM   977   N  NZ  . LYS   A  1 127 ? -26.235 23.636  -47.175  1.00 76.90  ? 428  LYS   A NZ  1 
ATOM   978   N  N   . LEU   A  1 128 ? -31.176 20.009  -45.702  1.00 44.96  ? 429  LEU   A N   1 
ATOM   979   C  CA  . LEU   A  1 128 ? -31.642 18.670  -46.038  1.00 43.46  ? 429  LEU   A CA  1 
ATOM   980   C  C   . LEU   A  1 128 ? -31.942 18.632  -47.525  1.00 38.76  ? 429  LEU   A C   1 
ATOM   981   O  O   . LEU   A  1 128 ? -32.705 19.461  -48.024  1.00 45.58  ? 429  LEU   A O   1 
ATOM   982   C  CB  . LEU   A  1 128 ? -32.894 18.278  -45.232  1.00 28.12  ? 429  LEU   A CB  1 
ATOM   983   C  CG  . LEU   A  1 128 ? -33.554 16.940  -45.621  1.00 30.45  ? 429  LEU   A CG  1 
ATOM   984   C  CD1 . LEU   A  1 128 ? -32.702 15.729  -45.245  1.00 32.45  ? 429  LEU   A CD1 1 
ATOM   985   C  CD2 . LEU   A  1 128 ? -34.984 16.794  -45.097  1.00 23.82  ? 429  LEU   A CD2 1 
ATOM   986   N  N   . GLN   A  1 129 ? -31.349 17.684  -48.228  1.00 36.98  ? 430  GLN   A N   1 
ATOM   987   C  CA  . GLN   A  1 129 ? -31.548 17.562  -49.667  1.00 35.78  ? 430  GLN   A CA  1 
ATOM   988   C  C   . GLN   A  1 129 ? -32.756 16.658  -49.901  1.00 36.90  ? 430  GLN   A C   1 
ATOM   989   O  O   . GLN   A  1 129 ? -32.742 15.489  -49.510  1.00 39.31  ? 430  GLN   A O   1 
ATOM   990   C  CB  . GLN   A  1 129 ? -30.287 17.011  -50.327  1.00 46.73  ? 430  GLN   A CB  1 
ATOM   991   C  CG  . GLN   A  1 129 ? -30.253 17.146  -51.846  1.00 50.49  ? 430  GLN   A CG  1 
ATOM   992   C  CD  . GLN   A  1 129 ? -30.519 18.567  -52.306  1.00 50.78  ? 430  GLN   A CD  1 
ATOM   993   O  OE1 . GLN   A  1 129 ? -31.532 18.836  -52.944  1.00 62.27  ? 430  GLN   A OE1 1 
ATOM   994   N  NE2 . GLN   A  1 129 ? -29.620 19.485  -51.969  1.00 34.64  ? 430  GLN   A NE2 1 
ATOM   995   N  N   . VAL   A  1 130 ? -33.818 17.204  -50.500  1.00 36.79  ? 431  VAL   A N   1 
ATOM   996   C  CA  . VAL   A  1 130 ? -35.052 16.458  -50.748  1.00 36.20  ? 431  VAL   A CA  1 
ATOM   997   C  C   . VAL   A  1 130 ? -35.056 15.962  -52.190  1.00 40.76  ? 431  VAL   A C   1 
ATOM   998   O  O   . VAL   A  1 130 ? -34.887 16.747  -53.124  1.00 39.39  ? 431  VAL   A O   1 
ATOM   999   C  CB  . VAL   A  1 130 ? -36.299 17.311  -50.461  1.00 33.21  ? 431  VAL   A CB  1 
ATOM   1000  C  CG1 . VAL   A  1 130 ? -37.549 16.511  -50.767  1.00 37.38  ? 431  VAL   A CG1 1 
ATOM   1001  C  CG2 . VAL   A  1 130 ? -36.323 17.781  -48.990  1.00 34.40  ? 431  VAL   A CG2 1 
ATOM   1002  N  N   . PHE   A  1 131 ? -35.264 14.663  -52.374  1.00 46.51  ? 432  PHE   A N   1 
ATOM   1003  C  CA  . PHE   A  1 131 ? -35.317 14.045  -53.696  1.00 37.36  ? 432  PHE   A CA  1 
ATOM   1004  C  C   . PHE   A  1 131 ? -36.759 13.630  -53.960  1.00 39.91  ? 432  PHE   A C   1 
ATOM   1005  O  O   . PHE   A  1 131 ? -37.256 12.674  -53.355  1.00 43.44  ? 432  PHE   A O   1 
ATOM   1006  C  CB  . PHE   A  1 131 ? -34.354 12.858  -53.778  1.00 29.38  ? 432  PHE   A CB  1 
ATOM   1007  C  CG  . PHE   A  1 131 ? -32.907 13.271  -53.839  1.00 30.86  ? 432  PHE   A CG  1 
ATOM   1008  C  CD1 . PHE   A  1 131 ? -32.447 14.057  -54.906  1.00 39.88  ? 432  PHE   A CD1 1 
ATOM   1009  C  CD2 . PHE   A  1 131 ? -32.004 12.899  -52.848  1.00 38.41  ? 432  PHE   A CD2 1 
ATOM   1010  C  CE1 . PHE   A  1 131 ? -31.127 14.464  -54.982  1.00 25.98  ? 432  PHE   A CE1 1 
ATOM   1011  C  CE2 . PHE   A  1 131 ? -30.668 13.308  -52.906  1.00 25.15  ? 432  PHE   A CE2 1 
ATOM   1012  C  CZ  . PHE   A  1 131 ? -30.230 14.089  -53.985  1.00 36.41  ? 432  PHE   A CZ  1 
ATOM   1013  N  N   . ASP   A  1 132 ? -37.433 14.362  -54.851  1.00 35.75  ? 433  ASP   A N   1 
ATOM   1014  C  CA  . ASP   A  1 132 ? -38.841 14.121  -55.172  1.00 33.28  ? 433  ASP   A CA  1 
ATOM   1015  C  C   . ASP   A  1 132 ? -38.925 12.945  -56.139  1.00 40.38  ? 433  ASP   A C   1 
ATOM   1016  O  O   . ASP   A  1 132 ? -38.622 13.082  -57.324  1.00 46.37  ? 433  ASP   A O   1 
ATOM   1017  C  CB  . ASP   A  1 132 ? -39.458 15.384  -55.763  1.00 37.20  ? 433  ASP   A CB  1 
ATOM   1018  C  CG  . ASP   A  1 132 ? -40.920 15.216  -56.158  1.00 40.37  ? 433  ASP   A CG  1 
ATOM   1019  O  OD1 . ASP   A  1 132 ? -41.504 14.128  -55.972  1.00 38.48  ? 433  ASP   A OD1 1 
ATOM   1020  O  OD2 . ASP   A  1 132 ? -41.494 16.206  -56.658  1.00 42.50  ? 433  ASP   A OD2 1 
ATOM   1021  N  N   . ALA   A  1 133 ? -39.348 11.781  -55.640  1.00 36.55  ? 434  ALA   A N   1 
ATOM   1022  C  CA  . ALA   A  1 133 ? -39.522 10.589  -56.461  1.00 36.40  ? 434  ALA   A CA  1 
ATOM   1023  C  C   . ALA   A  1 133 ? -40.996 10.239  -56.644  1.00 29.14  ? 434  ALA   A C   1 
ATOM   1024  O  O   . ALA   A  1 133 ? -41.355 9.071   -56.808  1.00 33.07  ? 434  ALA   A O   1 
ATOM   1025  C  CB  . ALA   A  1 133 ? -38.765 9.401   -55.864  1.00 33.96  ? 434  ALA   A CB  1 
ATOM   1026  N  N   . ARG   A  1 134 ? -41.864 11.243  -56.635  1.00 27.07  ? 435  ARG   A N   1 
ATOM   1027  C  CA  . ARG   A  1 134 ? -43.288 10.966  -56.738  1.00 28.37  ? 435  ARG   A CA  1 
ATOM   1028  C  C   . ARG   A  1 134 ? -43.712 10.502  -58.129  1.00 39.32  ? 435  ARG   A C   1 
ATOM   1029  O  O   . ARG   A  1 134 ? -44.856 10.069  -58.288  1.00 42.37  ? 435  ARG   A O   1 
ATOM   1030  C  CB  . ARG   A  1 134 ? -44.074 12.203  -56.303  1.00 33.53  ? 435  ARG   A CB  1 
ATOM   1031  C  CG  . ARG   A  1 134 ? -44.235 12.305  -54.754  1.00 34.93  ? 435  ARG   A CG  1 
ATOM   1032  C  CD  . ARG   A  1 134 ? -44.896 13.609  -54.367  1.00 32.03  ? 435  ARG   A CD  1 
ATOM   1033  N  NE  . ARG   A  1 134 ? -44.169 14.729  -54.957  1.00 35.61  ? 435  ARG   A NE  1 
ATOM   1034  C  CZ  . ARG   A  1 134 ? -44.630 15.971  -55.014  1.00 39.59  ? 435  ARG   A CZ  1 
ATOM   1035  N  NH1 . ARG   A  1 134 ? -45.825 16.246  -54.500  1.00 39.15  ? 435  ARG   A NH1 1 
ATOM   1036  N  NH2 . ARG   A  1 134 ? -43.908 16.926  -55.601  1.00 38.79  ? 435  ARG   A NH2 1 
ATOM   1037  N  N   . ASP   A  1 135 ? -42.825 10.543  -59.126  1.00 39.65  ? 436  ASP   A N   1 
ATOM   1038  C  CA  . ASP   A  1 135 ? -43.157 10.053  -60.460  1.00 42.48  ? 436  ASP   A CA  1 
ATOM   1039  C  C   . ASP   A  1 135 ? -42.806 8.586   -60.652  1.00 47.46  ? 436  ASP   A C   1 
ATOM   1040  O  O   . ASP   A  1 135 ? -43.036 8.046   -61.742  1.00 46.55  ? 436  ASP   A O   1 
ATOM   1041  C  CB  . ASP   A  1 135 ? -42.453 10.893  -61.537  1.00 41.99  ? 436  ASP   A CB  1 
ATOM   1042  C  CG  . ASP   A  1 135 ? -40.940 10.758  -61.504  1.00 44.28  ? 436  ASP   A CG  1 
ATOM   1043  O  OD1 . ASP   A  1 135 ? -40.389 10.180  -60.536  1.00 45.07  ? 436  ASP   A OD1 1 
ATOM   1044  O  OD2 . ASP   A  1 135 ? -40.297 11.251  -62.453  1.00 45.72  ? 436  ASP   A OD2 1 
ATOM   1045  N  N   . CYS   A  1 136 ? -42.270 7.939   -59.616  1.00 46.24  ? 437  CYS   A N   1 
ATOM   1046  C  CA  . CYS   A  1 136 ? -41.825 6.553   -59.708  1.00 42.64  ? 437  CYS   A CA  1 
ATOM   1047  C  C   . CYS   A  1 136 ? -43.015 5.606   -59.812  1.00 46.03  ? 437  CYS   A C   1 
ATOM   1048  O  O   . CYS   A  1 136 ? -44.062 5.832   -59.193  1.00 36.75  ? 437  CYS   A O   1 
ATOM   1049  C  CB  . CYS   A  1 136 ? -40.988 6.212   -58.477  1.00 32.13  ? 437  CYS   A CB  1 
ATOM   1050  S  SG  . CYS   A  1 136 ? -40.083 4.681   -58.536  1.00 37.94  ? 437  CYS   A SG  1 
ATOM   1051  N  N   . THR   A  1 137 ? -42.872 4.540   -60.617  1.00 31.97  ? 438  THR   A N   1 
ATOM   1052  C  CA  . THR   A  1 137 ? -43.959 3.573   -60.734  1.00 35.89  ? 438  THR   A CA  1 
ATOM   1053  C  C   . THR   A  1 137 ? -43.562 2.110   -60.561  1.00 35.61  ? 438  THR   A C   1 
ATOM   1054  O  O   . THR   A  1 137 ? -44.456 1.267   -60.434  1.00 38.27  ? 438  THR   A O   1 
ATOM   1055  C  CB  . THR   A  1 137 ? -44.682 3.719   -62.089  1.00 42.02  ? 438  THR   A CB  1 
ATOM   1056  O  OG1 . THR   A  1 137 ? -43.851 3.227   -63.144  1.00 33.21  ? 438  THR   A OG1 1 
ATOM   1057  C  CG2 . THR   A  1 137 ? -45.051 5.182   -62.369  1.00 41.90  ? 438  THR   A CG2 1 
ATOM   1058  N  N   . THR   A  1 138 ? -42.281 1.766   -60.567  1.00 34.15  ? 439  THR   A N   1 
ATOM   1059  C  CA  . THR   A  1 138 ? -41.890 0.363   -60.483  1.00 37.86  ? 439  THR   A CA  1 
ATOM   1060  C  C   . THR   A  1 138 ? -40.789 0.175   -59.439  1.00 32.63  ? 439  THR   A C   1 
ATOM   1061  O  O   . THR   A  1 138 ? -40.137 1.131   -58.997  1.00 37.91  ? 439  THR   A O   1 
ATOM   1062  C  CB  . THR   A  1 138 ? -41.402 -0.172  -61.841  1.00 42.96  ? 439  THR   A CB  1 
ATOM   1063  O  OG1 . THR   A  1 138 ? -40.205 0.519   -62.221  1.00 44.56  ? 439  THR   A OG1 1 
ATOM   1064  C  CG2 . THR   A  1 138 ? -42.467 -0.008  -62.923  1.00 38.07  ? 439  THR   A CG2 1 
ATOM   1065  N  N   . ALA   A  1 139 ? -40.570 -1.088  -59.062  1.00 33.44  ? 440  ALA   A N   1 
ATOM   1066  C  CA  . ALA   A  1 139 ? -39.488 -1.395  -58.127  1.00 37.07  ? 440  ALA   A CA  1 
ATOM   1067  C  C   . ALA   A  1 139 ? -38.129 -1.053  -58.722  1.00 41.07  ? 440  ALA   A C   1 
ATOM   1068  O  O   . ALA   A  1 139 ? -37.244 -0.552  -58.013  1.00 35.98  ? 440  ALA   A O   1 
ATOM   1069  C  CB  . ALA   A  1 139 ? -39.543 -2.862  -57.713  1.00 39.20  ? 440  ALA   A CB  1 
ATOM   1070  N  N   . HIS   A  1 140 ? -37.951 -1.309  -60.032  1.00 43.86  ? 441  HIS   A N   1 
ATOM   1071  C  CA  . HIS   A  1 140 ? -36.736 -0.880  -60.725  1.00 38.94  ? 441  HIS   A CA  1 
ATOM   1072  C  C   . HIS   A  1 140 ? -36.525 0.621   -60.600  1.00 42.11  ? 441  HIS   A C   1 
ATOM   1073  O  O   . HIS   A  1 140 ? -35.401 1.077   -60.357  1.00 40.69  ? 441  HIS   A O   1 
ATOM   1074  C  CB  . HIS   A  1 140 ? -36.791 -1.281  -62.204  1.00 35.80  ? 441  HIS   A CB  1 
ATOM   1075  C  CG  . HIS   A  1 140 ? -36.345 -2.682  -62.455  1.00 39.78  ? 441  HIS   A CG  1 
ATOM   1076  N  ND1 . HIS   A  1 140 ? -37.219 -3.748  -62.486  1.00 44.18  ? 441  HIS   A ND1 1 
ATOM   1077  C  CD2 . HIS   A  1 140 ? -35.111 -3.200  -62.638  1.00 32.15  ? 441  HIS   A CD2 1 
ATOM   1078  C  CE1 . HIS   A  1 140 ? -36.542 -4.860  -62.697  1.00 33.33  ? 441  HIS   A CE1 1 
ATOM   1079  N  NE2 . HIS   A  1 140 ? -35.260 -4.557  -62.787  1.00 43.06  ? 441  HIS   A NE2 1 
ATOM   1080  N  N   . GLY   A  1 141 ? -37.589 1.404   -60.792  1.00 45.39  ? 442  GLY   A N   1 
ATOM   1081  C  CA  . GLY   A  1 141 ? -37.476 2.838   -60.610  1.00 44.17  ? 442  GLY   A CA  1 
ATOM   1082  C  C   . GLY   A  1 141 ? -37.026 3.216   -59.212  1.00 38.89  ? 442  GLY   A C   1 
ATOM   1083  O  O   . GLY   A  1 141 ? -36.171 4.093   -59.043  1.00 34.95  ? 442  GLY   A O   1 
ATOM   1084  N  N   . MET   A  1 142 ? -37.590 2.555   -58.191  1.00 43.37  ? 443  MET   A N   1 
ATOM   1085  C  CA  . MET   A  1 142 ? -37.220 2.847   -56.804  1.00 35.98  ? 443  MET   A CA  1 
ATOM   1086  C  C   . MET   A  1 142 ? -35.741 2.560   -56.554  1.00 39.10  ? 443  MET   A C   1 
ATOM   1087  O  O   . MET   A  1 142 ? -35.043 3.354   -55.902  1.00 32.55  ? 443  MET   A O   1 
ATOM   1088  C  CB  . MET   A  1 142 ? -38.082 2.021   -55.842  1.00 34.99  ? 443  MET   A CB  1 
ATOM   1089  C  CG  . MET   A  1 142 ? -39.579 2.247   -55.931  1.00 32.88  ? 443  MET   A CG  1 
ATOM   1090  S  SD  . MET   A  1 142 ? -40.534 1.177   -54.804  1.00 40.28  ? 443  MET   A SD  1 
ATOM   1091  C  CE  . MET   A  1 142 ? -40.196 1.940   -53.211  1.00 34.90  ? 443  MET   A CE  1 
ATOM   1092  N  N   . PHE   A  1 143 ? -35.251 1.422   -57.062  1.00 33.02  ? 444  PHE   A N   1 
ATOM   1093  C  CA  . PHE   A  1 143 ? -33.833 1.093   -56.946  1.00 36.19  ? 444  PHE   A CA  1 
ATOM   1094  C  C   . PHE   A  1 143 ? -32.950 2.192   -57.547  1.00 42.50  ? 444  PHE   A C   1 
ATOM   1095  O  O   . PHE   A  1 143 ? -31.982 2.636   -56.917  1.00 47.46  ? 444  PHE   A O   1 
ATOM   1096  C  CB  . PHE   A  1 143 ? -33.584 -0.261  -57.610  1.00 42.41  ? 444  PHE   A CB  1 
ATOM   1097  C  CG  . PHE   A  1 143 ? -32.141 -0.621  -57.746  1.00 42.06  ? 444  PHE   A CG  1 
ATOM   1098  C  CD1 . PHE   A  1 143 ? -31.416 -1.055  -56.656  1.00 33.61  ? 444  PHE   A CD1 1 
ATOM   1099  C  CD2 . PHE   A  1 143 ? -31.507 -0.540  -58.977  1.00 40.54  ? 444  PHE   A CD2 1 
ATOM   1100  C  CE1 . PHE   A  1 143 ? -30.083 -1.402  -56.782  1.00 30.79  ? 444  PHE   A CE1 1 
ATOM   1101  C  CE2 . PHE   A  1 143 ? -30.165 -0.874  -59.120  1.00 34.83  ? 444  PHE   A CE2 1 
ATOM   1102  C  CZ  . PHE   A  1 143 ? -29.452 -1.306  -58.027  1.00 40.93  ? 444  PHE   A CZ  1 
ATOM   1103  N  N   . ASN   A  1 144 ? -33.267 2.644   -58.767  1.00 40.49  ? 445  ASN   A N   1 
ATOM   1104  C  CA  . ASN   A  1 144 ? -32.518 3.751   -59.374  1.00 37.11  ? 445  ASN   A CA  1 
ATOM   1105  C  C   . ASN   A  1 144 ? -32.515 4.981   -58.460  1.00 37.57  ? 445  ASN   A C   1 
ATOM   1106  O  O   . ASN   A  1 144 ? -31.460 5.541   -58.154  1.00 38.48  ? 445  ASN   A O   1 
ATOM   1107  C  CB  . ASN   A  1 144 ? -33.118 4.090   -60.743  1.00 37.33  ? 445  ASN   A CB  1 
ATOM   1108  C  CG  . ASN   A  1 144 ? -32.297 5.121   -61.520  1.00 40.04  ? 445  ASN   A CG  1 
ATOM   1109  O  OD1 . ASN   A  1 144 ? -32.781 6.187   -61.880  1.00 44.34  ? 445  ASN   A OD1 1 
ATOM   1110  N  ND2 . ASN   A  1 144 ? -31.056 4.802   -61.765  1.00 35.31  ? 445  ASN   A ND2 1 
ATOM   1111  N  N   . TYR   A  1 145 ? -33.695 5.395   -57.999  1.00 35.98  ? 446  TYR   A N   1 
ATOM   1112  C  CA  . TYR   A  1 145 ? -33.799 6.519   -57.070  1.00 42.87  ? 446  TYR   A CA  1 
ATOM   1113  C  C   . TYR   A  1 145 ? -32.972 6.303   -55.800  1.00 35.24  ? 446  TYR   A C   1 
ATOM   1114  O  O   . TYR   A  1 145 ? -32.356 7.240   -55.281  1.00 34.31  ? 446  TYR   A O   1 
ATOM   1115  C  CB  . TYR   A  1 145 ? -35.268 6.751   -56.713  1.00 38.04  ? 446  TYR   A CB  1 
ATOM   1116  C  CG  . TYR   A  1 145 ? -35.961 7.773   -57.585  1.00 47.45  ? 446  TYR   A CG  1 
ATOM   1117  C  CD1 . TYR   A  1 145 ? -35.516 9.088   -57.602  1.00 42.95  ? 446  TYR   A CD1 1 
ATOM   1118  C  CD2 . TYR   A  1 145 ? -37.062 7.430   -58.393  1.00 26.90  ? 446  TYR   A CD2 1 
ATOM   1119  C  CE1 . TYR   A  1 145 ? -36.125 10.035  -58.374  1.00 32.98  ? 446  TYR   A CE1 1 
ATOM   1120  C  CE2 . TYR   A  1 145 ? -37.698 8.394   -59.152  1.00 27.20  ? 446  TYR   A CE2 1 
ATOM   1121  C  CZ  . TYR   A  1 145 ? -37.213 9.694   -59.137  1.00 30.28  ? 446  TYR   A CZ  1 
ATOM   1122  O  OH  . TYR   A  1 145 ? -37.793 10.688  -59.880  1.00 35.75  ? 446  TYR   A OH  1 
ATOM   1123  N  N   . ILE   A  1 146 ? -32.937 5.078   -55.289  1.00 32.44  ? 447  ILE   A N   1 
ATOM   1124  C  CA  . ILE   A  1 146 ? -32.217 4.845   -54.037  1.00 33.69  ? 447  ILE   A CA  1 
ATOM   1125  C  C   . ILE   A  1 146 ? -30.713 4.786   -54.260  1.00 35.15  ? 447  ILE   A C   1 
ATOM   1126  O  O   . ILE   A  1 146 ? -29.938 5.244   -53.409  1.00 32.10  ? 447  ILE   A O   1 
ATOM   1127  C  CB  . ILE   A  1 146 ? -32.766 3.572   -53.360  1.00 33.70  ? 447  ILE   A CB  1 
ATOM   1128  C  CG1 . ILE   A  1 146 ? -34.144 3.867   -52.772  1.00 31.58  ? 447  ILE   A CG1 1 
ATOM   1129  C  CG2 . ILE   A  1 146 ? -31.819 3.047   -52.291  1.00 31.50  ? 447  ILE   A CG2 1 
ATOM   1130  C  CD1 . ILE   A  1 146 ? -34.963 2.641   -52.407  1.00 32.11  ? 447  ILE   A CD1 1 
ATOM   1131  N  N   . CYS   A  1 147 ? -30.264 4.253   -55.407  1.00 38.59  ? 448  CYS   A N   1 
ATOM   1132  C  CA  . CYS   A  1 147 ? -28.838 4.285   -55.711  1.00 31.14  ? 448  CYS   A CA  1 
ATOM   1133  C  C   . CYS   A  1 147 ? -28.331 5.712   -55.812  1.00 31.45  ? 448  CYS   A C   1 
ATOM   1134  O  O   . CYS   A  1 147 ? -27.226 6.025   -55.347  1.00 36.13  ? 448  CYS   A O   1 
ATOM   1135  C  CB  . CYS   A  1 147 ? -28.548 3.540   -57.010  1.00 37.24  ? 448  CYS   A CB  1 
ATOM   1136  S  SG  . CYS   A  1 147 ? -28.590 1.787   -56.857  1.00 40.05  ? 448  CYS   A SG  1 
ATOM   1137  N  N   . ASN   A  1 148 ? -29.117 6.592   -56.433  1.00 39.10  ? 449  ASN   A N   1 
ATOM   1138  C  CA  . ASN   A  1 148 ? -28.704 7.983   -56.538  1.00 26.53  ? 449  ASN   A CA  1 
ATOM   1139  C  C   . ASN   A  1 148 ? -28.708 8.652   -55.157  1.00 30.36  ? 449  ASN   A C   1 
ATOM   1140  O  O   . ASN   A  1 148 ? -27.806 9.435   -54.837  1.00 35.62  ? 449  ASN   A O   1 
ATOM   1141  C  CB  . ASN   A  1 148 ? -29.607 8.724   -57.532  1.00 29.44  ? 449  ASN   A CB  1 
ATOM   1142  C  CG  . ASN   A  1 148 ? -29.465 8.206   -58.993  1.00 39.21  ? 449  ASN   A CG  1 
ATOM   1143  O  OD1 . ASN   A  1 148 ? -28.489 7.534   -59.360  1.00 37.68  ? 449  ASN   A OD1 1 
ATOM   1144  N  ND2 . ASN   A  1 148 ? -30.460 8.528   -59.817  1.00 30.48  ? 449  ASN   A ND2 1 
ATOM   1145  N  N   . HIS   A  1 149 ? -29.695 8.328   -54.312  1.00 35.30  ? 450  HIS   A N   1 
ATOM   1146  C  CA  . HIS   A  1 149 ? -29.685 8.808   -52.926  1.00 31.41  ? 450  HIS   A CA  1 
ATOM   1147  C  C   . HIS   A  1 149 ? -28.379 8.414   -52.244  1.00 25.71  ? 450  HIS   A C   1 
ATOM   1148  O  O   . HIS   A  1 149 ? -27.630 9.268   -51.760  1.00 30.69  ? 450  HIS   A O   1 
ATOM   1149  C  CB  . HIS   A  1 149 ? -30.894 8.246   -52.162  1.00 36.88  ? 450  HIS   A CB  1 
ATOM   1150  C  CG  . HIS   A  1 149 ? -31.049 8.766   -50.751  1.00 41.49  ? 450  HIS   A CG  1 
ATOM   1151  N  ND1 . HIS   A  1 149 ? -32.237 9.287   -50.282  1.00 35.19  ? 450  HIS   A ND1 1 
ATOM   1152  C  CD2 . HIS   A  1 149 ? -30.186 8.807   -49.706  1.00 37.23  ? 450  HIS   A CD2 1 
ATOM   1153  C  CE1 . HIS   A  1 149 ? -32.095 9.648   -49.019  1.00 38.71  ? 450  HIS   A CE1 1 
ATOM   1154  N  NE2 . HIS   A  1 149 ? -30.861 9.366   -48.643  1.00 38.32  ? 450  HIS   A NE2 1 
ATOM   1155  N  N   . VAL   A  1 150 ? -28.055 7.118   -52.276  1.00 29.84  ? 451  VAL   A N   1 
ATOM   1156  C  CA  . VAL   A  1 150 ? -26.901 6.619   -51.536  1.00 32.56  ? 451  VAL   A CA  1 
ATOM   1157  C  C   . VAL   A  1 150 ? -25.623 7.295   -52.001  1.00 38.05  ? 451  VAL   A C   1 
ATOM   1158  O  O   . VAL   A  1 150 ? -24.774 7.680   -51.188  1.00 39.89  ? 451  VAL   A O   1 
ATOM   1159  C  CB  . VAL   A  1 150 ? -26.820 5.094   -51.681  1.00 32.66  ? 451  VAL   A CB  1 
ATOM   1160  C  CG1 . VAL   A  1 150 ? -25.474 4.602   -51.249  1.00 26.26  ? 451  VAL   A CG1 1 
ATOM   1161  C  CG2 . VAL   A  1 150 ? -27.956 4.426   -50.897  1.00 27.75  ? 451  VAL   A CG2 1 
ATOM   1162  N  N   . LYS   A  1 151 ? -25.461 7.442   -53.317  1.00 43.27  ? 452  LYS   A N   1 
ATOM   1163  C  CA  . LYS   A  1 151 ? -24.231 8.008   -53.847  1.00 40.62  ? 452  LYS   A CA  1 
ATOM   1164  C  C   . LYS   A  1 151 ? -24.119 9.477   -53.477  1.00 33.95  ? 452  LYS   A C   1 
ATOM   1165  O  O   . LYS   A  1 151 ? -23.035 9.958   -53.136  1.00 40.38  ? 452  LYS   A O   1 
ATOM   1166  C  CB  . LYS   A  1 151 ? -24.182 7.818   -55.369  1.00 34.49  ? 452  LYS   A CB  1 
ATOM   1167  C  CG  . LYS   A  1 151 ? -22.962 8.411   -56.055  1.00 34.96  ? 452  LYS   A CG  1 
ATOM   1168  C  CD  . LYS   A  1 151 ? -22.818 7.757   -57.424  1.00 39.21  ? 452  LYS   A CD  1 
ATOM   1169  C  CE  . LYS   A  1 151 ? -21.575 8.175   -58.204  1.00 44.54  ? 452  LYS   A CE  1 
ATOM   1170  N  NZ  . LYS   A  1 151 ? -21.549 7.472   -59.521  1.00 43.39  ? 452  LYS   A NZ  1 
ATOM   1171  N  N   . TYR   A  1 152 ? -25.234 10.203  -53.555  1.00 34.20  ? 453  TYR   A N   1 
ATOM   1172  C  CA  . TYR   A  1 152 ? -25.233 11.607  -53.173  1.00 37.70  ? 453  TYR   A CA  1 
ATOM   1173  C  C   . TYR   A  1 152 ? -24.915 11.760  -51.691  1.00 34.12  ? 453  TYR   A C   1 
ATOM   1174  O  O   . TYR   A  1 152 ? -24.007 12.508  -51.308  1.00 31.51  ? 453  TYR   A O   1 
ATOM   1175  C  CB  . TYR   A  1 152 ? -26.591 12.244  -53.486  1.00 39.15  ? 453  TYR   A CB  1 
ATOM   1176  C  CG  . TYR   A  1 152 ? -26.680 13.643  -52.920  1.00 41.17  ? 453  TYR   A CG  1 
ATOM   1177  C  CD1 . TYR   A  1 152 ? -26.155 14.713  -53.623  1.00 45.92  ? 453  TYR   A CD1 1 
ATOM   1178  C  CD2 . TYR   A  1 152 ? -27.255 13.891  -51.669  1.00 40.81  ? 453  TYR   A CD2 1 
ATOM   1179  C  CE1 . TYR   A  1 152 ? -26.205 15.981  -53.128  1.00 44.69  ? 453  TYR   A CE1 1 
ATOM   1180  C  CE2 . TYR   A  1 152 ? -27.299 15.167  -51.158  1.00 40.35  ? 453  TYR   A CE2 1 
ATOM   1181  C  CZ  . TYR   A  1 152 ? -26.770 16.210  -51.897  1.00 40.97  ? 453  TYR   A CZ  1 
ATOM   1182  O  OH  . TYR   A  1 152 ? -26.794 17.505  -51.430  1.00 47.07  ? 453  TYR   A OH  1 
ATOM   1183  N  N   . ALA   A  1 153 ? -25.687 11.066  -50.849  1.00 35.85  ? 454  ALA   A N   1 
ATOM   1184  C  CA  . ALA   A  1 153 ? -25.524 11.140  -49.398  1.00 38.93  ? 454  ALA   A CA  1 
ATOM   1185  C  C   . ALA   A  1 153 ? -24.107 10.779  -48.969  1.00 38.42  ? 454  ALA   A C   1 
ATOM   1186  O  O   . ALA   A  1 153 ? -23.509 11.483  -48.153  1.00 36.62  ? 454  ALA   A O   1 
ATOM   1187  C  CB  . ALA   A  1 153 ? -26.545 10.225  -48.725  1.00 24.73  ? 454  ALA   A CB  1 
ATOM   1188  N  N   . THR   A  1 154 ? -23.545 9.701   -49.533  1.00 42.30  ? 455  THR   A N   1 
ATOM   1189  C  CA  . THR   A  1 154 ? -22.235 9.220   -49.103  1.00 35.31  ? 455  THR   A CA  1 
ATOM   1190  C  C   . THR   A  1 154 ? -21.128 10.214  -49.449  1.00 43.41  ? 455  THR   A C   1 
ATOM   1191  O  O   . THR   A  1 154 ? -20.283 10.523  -48.600  1.00 47.10  ? 455  THR   A O   1 
ATOM   1192  C  CB  . THR   A  1 154 ? -21.956 7.848   -49.718  1.00 34.97  ? 455  THR   A CB  1 
ATOM   1193  O  OG1 . THR   A  1 154 ? -22.928 6.918   -49.243  1.00 39.45  ? 455  THR   A OG1 1 
ATOM   1194  C  CG2 . THR   A  1 154 ? -20.570 7.350   -49.344  1.00 27.41  ? 455  THR   A CG2 1 
ATOM   1195  N  N   . ASN   A  1 155 ? -21.101 10.713  -50.699  1.00 43.69  ? 456  ASN   A N   1 
ATOM   1196  C  CA  . ASN   A  1 155 ? -20.210 11.816  -51.094  1.00 34.31  ? 456  ASN   A CA  1 
ATOM   1197  C  C   . ASN   A  1 155 ? -18.753 11.541  -50.691  1.00 41.44  ? 456  ASN   A C   1 
ATOM   1198  O  O   . ASN   A  1 155 ? -18.025 12.428  -50.235  1.00 33.26  ? 456  ASN   A O   1 
ATOM   1199  C  CB  . ASN   A  1 155 ? -20.716 13.147  -50.518  1.00 29.27  ? 456  ASN   A CB  1 
ATOM   1200  C  CG  . ASN   A  1 155 ? -19.955 14.343  -51.026  1.00 38.08  ? 456  ASN   A CG  1 
ATOM   1201  O  OD1 . ASN   A  1 155 ? -19.615 14.436  -52.198  1.00 46.29  ? 456  ASN   A OD1 1 
ATOM   1202  N  ND2 . ASN   A  1 155 ? -19.678 15.268  -50.144  1.00 36.88  ? 456  ASN   A ND2 1 
ATOM   1203  N  N   . LYS   A  1 156 ? -18.328 10.285  -50.862  1.00 46.73  ? 457  LYS   A N   1 
ATOM   1204  C  CA  . LYS   A  1 156 ? -16.942 9.847   -50.634  1.00 44.58  ? 457  LYS   A CA  1 
ATOM   1205  C  C   . LYS   A  1 156 ? -16.491 10.017  -49.185  1.00 39.48  ? 457  LYS   A C   1 
ATOM   1206  O  O   . LYS   A  1 156 ? -15.299 10.191  -48.914  1.00 32.02  ? 457  LYS   A O   1 
ATOM   1207  C  CB  . LYS   A  1 156 ? -15.976 10.561  -51.586  1.00 45.39  ? 457  LYS   A CB  1 
ATOM   1208  C  CG  . LYS   A  1 156 ? -16.230 10.188  -53.031  1.00 48.57  ? 457  LYS   A CG  1 
ATOM   1209  C  CD  . LYS   A  1 156 ? -15.058 10.491  -53.940  1.00 61.12  ? 457  LYS   A CD  1 
ATOM   1210  C  CE  . LYS   A  1 156 ? -15.437 11.524  -54.993  1.00 72.56  ? 457  LYS   A CE  1 
ATOM   1211  N  NZ  . LYS   A  1 156 ? -14.635 11.379  -56.255  1.00 79.37  ? 457  LYS   A NZ  1 
ATOM   1212  N  N   . GLY   A  1 157 ? -17.440 9.930   -48.245  1.00 41.45  ? 458  GLY   A N   1 
ATOM   1213  C  CA  . GLY   A  1 157 ? -17.179 10.048  -46.834  1.00 39.17  ? 458  GLY   A CA  1 
ATOM   1214  C  C   . GLY   A  1 157 ? -17.602 11.369  -46.237  1.00 45.27  ? 458  GLY   A C   1 
ATOM   1215  O  O   . GLY   A  1 157 ? -17.717 11.481  -45.004  1.00 45.51  ? 458  GLY   A O   1 
ATOM   1216  N  N   . ASN   A  1 158 ? -17.835 12.375  -47.076  1.00 38.98  ? 459  ASN   A N   1 
ATOM   1217  C  CA  . ASN   A  1 158 ? -18.218 13.688  -46.573  1.00 42.99  ? 459  ASN   A CA  1 
ATOM   1218  C  C   . ASN   A  1 158 ? -19.741 13.768  -46.602  1.00 42.68  ? 459  ASN   A C   1 
ATOM   1219  O  O   . ASN   A  1 158 ? -20.345 14.368  -47.488  1.00 45.06  ? 459  ASN   A O   1 
ATOM   1220  C  CB  . ASN   A  1 158 ? -17.557 14.778  -47.393  1.00 42.03  ? 459  ASN   A CB  1 
ATOM   1221  C  CG  . ASN   A  1 158 ? -17.968 16.143  -46.958  1.00 44.15  ? 459  ASN   A CG  1 
ATOM   1222  O  OD1 . ASN   A  1 158 ? -18.462 16.341  -45.846  1.00 43.95  ? 459  ASN   A OD1 1 
ATOM   1223  N  ND2 . ASN   A  1 158 ? -17.771 17.108  -47.829  1.00 39.79  ? 459  ASN   A ND2 1 
ATOM   1224  N  N   . LEU   A  1 159 ? -20.362 13.161  -45.590  1.00 37.24  ? 460  LEU   A N   1 
ATOM   1225  C  CA  . LEU   A  1 159 ? -21.777 12.813  -45.662  1.00 40.63  ? 460  LEU   A CA  1 
ATOM   1226  C  C   . LEU   A  1 159 ? -22.683 14.040  -45.697  1.00 35.84  ? 460  LEU   A C   1 
ATOM   1227  O  O   . LEU   A  1 159 ? -22.399 15.088  -45.115  1.00 36.23  ? 460  LEU   A O   1 
ATOM   1228  C  CB  . LEU   A  1 159 ? -22.178 11.926  -44.480  1.00 36.96  ? 460  LEU   A CB  1 
ATOM   1229  C  CG  . LEU   A  1 159 ? -21.331 10.657  -44.412  1.00 47.10  ? 460  LEU   A CG  1 
ATOM   1230  C  CD1 . LEU   A  1 159 ? -21.801 9.715   -43.313  1.00 53.51  ? 460  LEU   A CD1 1 
ATOM   1231  C  CD2 . LEU   A  1 159 ? -21.350 9.965   -45.753  1.00 42.17  ? 460  LEU   A CD2 1 
ATOM   1232  N  N   . ARG   A  1 160 ? -23.796 13.874  -46.389  1.00 33.75  ? 461  ARG   A N   1 
ATOM   1233  C  CA  . ARG   A  1 160 ? -24.778 14.912  -46.630  1.00 35.00  ? 461  ARG   A CA  1 
ATOM   1234  C  C   . ARG   A  1 160 ? -26.136 14.298  -46.367  1.00 33.83  ? 461  ARG   A C   1 
ATOM   1235  O  O   . ARG   A  1 160 ? -26.408 13.182  -46.817  1.00 37.81  ? 461  ARG   A O   1 
ATOM   1236  C  CB  . ARG   A  1 160 ? -24.727 15.438  -48.074  1.00 33.87  ? 461  ARG   A CB  1 
ATOM   1237  C  CG  . ARG   A  1 160 ? -23.448 16.130  -48.453  1.00 34.87  ? 461  ARG   A CG  1 
ATOM   1238  C  CD  . ARG   A  1 160 ? -23.569 16.693  -49.844  1.00 40.67  ? 461  ARG   A CD  1 
ATOM   1239  N  NE  . ARG   A  1 160 ? -23.482 15.637  -50.833  1.00 36.20  ? 461  ARG   A NE  1 
ATOM   1240  C  CZ  . ARG   A  1 160 ? -23.119 15.861  -52.088  1.00 38.22  ? 461  ARG   A CZ  1 
ATOM   1241  N  NH1 . ARG   A  1 160 ? -22.847 17.092  -52.473  1.00 34.35  ? 461  ARG   A NH1 1 
ATOM   1242  N  NH2 . ARG   A  1 160 ? -23.035 14.866  -52.947  1.00 29.47  ? 461  ARG   A NH2 1 
ATOM   1243  N  N   . SER   A  1 161 ? -26.983 15.012  -45.647  1.00 32.89  ? 462  SER   A N   1 
ATOM   1244  C  CA  . SER   A  1 161 ? -28.244 14.412  -45.264  1.00 38.28  ? 462  SER   A CA  1 
ATOM   1245  C  C   . SER   A  1 161 ? -29.254 14.584  -46.401  1.00 33.86  ? 462  SER   A C   1 
ATOM   1246  O  O   . SER   A  1 161 ? -29.199 15.544  -47.170  1.00 40.49  ? 462  SER   A O   1 
ATOM   1247  C  CB  . SER   A  1 161 ? -28.723 15.012  -43.936  1.00 34.44  ? 462  SER   A CB  1 
ATOM   1248  O  OG  . SER   A  1 161 ? -29.274 16.298  -44.101  1.00 43.91  ? 462  SER   A OG  1 
ATOM   1249  N  N   . ALA   A  1 162 ? -30.157 13.616  -46.530  1.00 35.07  ? 463  ALA   A N   1 
ATOM   1250  C  CA  . ALA   A  1 162 ? -31.010 13.582  -47.708  1.00 38.00  ? 463  ALA   A CA  1 
ATOM   1251  C  C   . ALA   A  1 162 ? -32.194 12.667  -47.453  1.00 37.36  ? 463  ALA   A C   1 
ATOM   1252  O  O   . ALA   A  1 162 ? -32.152 11.779  -46.595  1.00 28.03  ? 463  ALA   A O   1 
ATOM   1253  C  CB  . ALA   A  1 162 ? -30.234 13.112  -48.956  1.00 29.87  ? 463  ALA   A CB  1 
ATOM   1254  N  N   . ILE   A  1 163 ? -33.254 12.897  -48.229  1.00 39.81  ? 464  ILE   A N   1 
ATOM   1255  C  CA  . ILE   A  1 163 ? -34.453 12.074  -48.193  1.00 36.41  ? 464  ILE   A CA  1 
ATOM   1256  C  C   . ILE   A  1 163 ? -34.970 11.913  -49.622  1.00 38.22  ? 464  ILE   A C   1 
ATOM   1257  O  O   . ILE   A  1 163 ? -34.880 12.831  -50.444  1.00 41.78  ? 464  ILE   A O   1 
ATOM   1258  C  CB  . ILE   A  1 163 ? -35.532 12.677  -47.259  1.00 25.37  ? 464  ILE   A CB  1 
ATOM   1259  C  CG1 . ILE   A  1 163 ? -36.717 11.719  -47.082  1.00 30.15  ? 464  ILE   A CG1 1 
ATOM   1260  C  CG2 . ILE   A  1 163 ? -36.000 14.025  -47.748  1.00 30.54  ? 464  ILE   A CG2 1 
ATOM   1261  C  CD1 . ILE   A  1 163 ? -37.796 12.246  -46.118  1.00 32.01  ? 464  ILE   A CD1 1 
ATOM   1262  N  N   . THR   A  1 164 ? -35.503 10.728  -49.916  1.00 38.02  ? 465  THR   A N   1 
ATOM   1263  C  CA  . THR   A  1 164 ? -36.140 10.443  -51.195  1.00 38.00  ? 465  THR   A CA  1 
ATOM   1264  C  C   . THR   A  1 164 ? -37.585 10.042  -50.957  1.00 30.66  ? 465  THR   A C   1 
ATOM   1265  O  O   . THR   A  1 164 ? -37.853 9.045   -50.282  1.00 28.13  ? 465  THR   A O   1 
ATOM   1266  C  CB  . THR   A  1 164 ? -35.417 9.328   -51.946  1.00 37.30  ? 465  THR   A CB  1 
ATOM   1267  O  OG1 . THR   A  1 164 ? -34.104 9.778   -52.295  1.00 29.76  ? 465  THR   A OG1 1 
ATOM   1268  C  CG2 . THR   A  1 164 ? -36.201 8.982   -53.199  1.00 33.28  ? 465  THR   A CG2 1 
ATOM   1269  N  N   . ILE   A  1 165 ? -38.511 10.792  -51.538  1.00 29.00  ? 466  ILE   A N   1 
ATOM   1270  C  CA  . ILE   A  1 165 ? -39.929 10.656  -51.241  1.00 37.08  ? 466  ILE   A CA  1 
ATOM   1271  C  C   . ILE   A  1 165 ? -40.633 9.983   -52.417  1.00 42.06  ? 466  ILE   A C   1 
ATOM   1272  O  O   . ILE   A  1 165 ? -40.689 10.533  -53.526  1.00 38.18  ? 466  ILE   A O   1 
ATOM   1273  C  CB  . ILE   A  1 165 ? -40.550 12.019  -50.911  1.00 36.54  ? 466  ILE   A CB  1 
ATOM   1274  C  CG1 . ILE   A  1 165 ? -39.877 12.604  -49.663  1.00 35.51  ? 466  ILE   A CG1 1 
ATOM   1275  C  CG2 . ILE   A  1 165 ? -42.040 11.888  -50.725  1.00 35.51  ? 466  ILE   A CG2 1 
ATOM   1276  C  CD1 . ILE   A  1 165 ? -40.318 14.017  -49.357  1.00 37.90  ? 466  ILE   A CD1 1 
ATOM   1277  N  N   . PHE   A  1 166 ? -41.205 8.820   -52.158  1.00 41.56  ? 467  PHE   A N   1 
ATOM   1278  C  CA  . PHE   A  1 166 ? -41.904 8.027   -53.158  1.00 33.49  ? 467  PHE   A CA  1 
ATOM   1279  C  C   . PHE   A  1 166 ? -43.388 8.364   -53.160  1.00 33.02  ? 467  PHE   A C   1 
ATOM   1280  O  O   . PHE   A  1 166 ? -43.847 9.170   -52.357  1.00 39.39  ? 467  PHE   A O   1 
ATOM   1281  C  CB  . PHE   A  1 166 ? -41.628 6.556   -52.892  1.00 33.98  ? 467  PHE   A CB  1 
ATOM   1282  C  CG  . PHE   A  1 166 ? -40.253 6.142   -53.310  1.00 35.00  ? 467  PHE   A CG  1 
ATOM   1283  C  CD1 . PHE   A  1 166 ? -39.908 6.107   -54.675  1.00 27.42  ? 467  PHE   A CD1 1 
ATOM   1284  C  CD2 . PHE   A  1 166 ? -39.296 5.801   -52.361  1.00 32.32  ? 467  PHE   A CD2 1 
ATOM   1285  C  CE1 . PHE   A  1 166 ? -38.638 5.731   -55.076  1.00 27.88  ? 467  PHE   A CE1 1 
ATOM   1286  C  CE2 . PHE   A  1 166 ? -38.015 5.420   -52.750  1.00 37.65  ? 467  PHE   A CE2 1 
ATOM   1287  C  CZ  . PHE   A  1 166 ? -37.680 5.381   -54.116  1.00 34.91  ? 467  PHE   A CZ  1 
ATOM   1288  N  N   . PRO   A  1 167 ? -44.172 7.825   -54.105  1.00 34.51  ? 468  PRO   A N   1 
ATOM   1289  C  CA  . PRO   A  1 167 ? -45.572 8.271   -54.215  1.00 37.53  ? 468  PRO   A CA  1 
ATOM   1290  C  C   . PRO   A  1 167 ? -46.373 8.000   -52.944  1.00 34.43  ? 468  PRO   A C   1 
ATOM   1291  O  O   . PRO   A  1 167 ? -46.231 6.956   -52.302  1.00 40.00  ? 468  PRO   A O   1 
ATOM   1292  C  CB  . PRO   A  1 167 ? -46.114 7.469   -55.410  1.00 36.68  ? 468  PRO   A CB  1 
ATOM   1293  C  CG  . PRO   A  1 167 ? -44.909 7.196   -56.245  1.00 34.72  ? 468  PRO   A CG  1 
ATOM   1294  C  CD  . PRO   A  1 167 ? -43.780 6.991   -55.265  1.00 36.22  ? 468  PRO   A CD  1 
ATOM   1295  N  N   . GLN   A  1 168 ? -47.229 8.961   -52.595  1.00 34.87  ? 469  GLN   A N   1 
ATOM   1296  C  CA  . GLN   A  1 168 ? -48.018 8.888   -51.372  1.00 35.69  ? 469  GLN   A CA  1 
ATOM   1297  C  C   . GLN   A  1 168 ? -49.041 7.761   -51.453  1.00 44.69  ? 469  GLN   A C   1 
ATOM   1298  O  O   . GLN   A  1 168 ? -49.406 7.282   -52.532  1.00 49.92  ? 469  GLN   A O   1 
ATOM   1299  C  CB  . GLN   A  1 168 ? -48.755 10.199  -51.134  1.00 38.95  ? 469  GLN   A CB  1 
ATOM   1300  C  CG  . GLN   A  1 168 ? -49.857 10.415  -52.171  1.00 44.98  ? 469  GLN   A CG  1 
ATOM   1301  C  CD  . GLN   A  1 168 ? -50.146 11.866  -52.428  1.00 43.62  ? 469  GLN   A CD  1 
ATOM   1302  O  OE1 . GLN   A  1 168 ? -49.236 12.669  -52.586  1.00 47.05  ? 469  GLN   A OE1 1 
ATOM   1303  N  NE2 . GLN   A  1 168 ? -51.427 12.220  -52.455  1.00 44.76  ? 469  GLN   A NE2 1 
ATOM   1304  N  N   . ARG   A  1 169 ? -49.526 7.360   -50.286  1.00 45.41  ? 470  ARG   A N   1 
ATOM   1305  C  CA  . ARG   A  1 169 ? -50.571 6.351   -50.193  1.00 39.30  ? 470  ARG   A CA  1 
ATOM   1306  C  C   . ARG   A  1 169 ? -51.835 6.843   -50.895  1.00 37.44  ? 470  ARG   A C   1 
ATOM   1307  O  O   . ARG   A  1 169 ? -52.086 8.050   -50.986  1.00 44.54  ? 470  ARG   A O   1 
ATOM   1308  C  CB  . ARG   A  1 169 ? -50.822 6.040   -48.707  1.00 44.86  ? 470  ARG   A CB  1 
ATOM   1309  C  CG  . ARG   A  1 169 ? -51.961 5.098   -48.406  1.00 48.75  ? 470  ARG   A CG  1 
ATOM   1310  C  CD  . ARG   A  1 169 ? -51.947 4.691   -46.936  1.00 51.07  ? 470  ARG   A CD  1 
ATOM   1311  N  NE  . ARG   A  1 169 ? -51.009 3.605   -46.689  1.00 50.73  ? 470  ARG   A NE  1 
ATOM   1312  C  CZ  . ARG   A  1 169 ? -50.308 3.468   -45.570  1.00 61.60  ? 470  ARG   A CZ  1 
ATOM   1313  N  NH1 . ARG   A  1 169 ? -50.442 4.367   -44.605  1.00 68.36  ? 470  ARG   A NH1 1 
ATOM   1314  N  NH2 . ARG   A  1 169 ? -49.463 2.448   -45.419  1.00 57.95  ? 470  ARG   A NH2 1 
ATOM   1315  N  N   . THR   A  1 170 ? -52.613 5.902   -51.443  1.00 36.29  ? 471  THR   A N   1 
ATOM   1316  C  CA  . THR   A  1 170 ? -53.895 6.243   -52.060  1.00 33.29  ? 471  THR   A CA  1 
ATOM   1317  C  C   . THR   A  1 170 ? -55.027 5.531   -51.329  1.00 36.13  ? 471  THR   A C   1 
ATOM   1318  O  O   . THR   A  1 170 ? -55.663 6.115   -50.448  1.00 47.20  ? 471  THR   A O   1 
ATOM   1319  C  CB  . THR   A  1 170 ? -53.931 5.900   -53.576  1.00 45.23  ? 471  THR   A CB  1 
ATOM   1320  O  OG1 . THR   A  1 170 ? -53.856 4.484   -53.792  1.00 50.93  ? 471  THR   A OG1 1 
ATOM   1321  C  CG2 . THR   A  1 170 ? -52.788 6.555   -54.328  1.00 43.01  ? 471  THR   A CG2 1 
ATOM   1322  N  N   . ASP   A  1 171 ? -55.299 4.275   -51.675  1.00 45.13  ? 472  ASP   A N   1 
ATOM   1323  C  CA  . ASP   A  1 171 ? -56.343 3.506   -51.011  1.00 50.27  ? 472  ASP   A CA  1 
ATOM   1324  C  C   . ASP   A  1 171 ? -55.787 2.509   -50.003  1.00 64.14  ? 472  ASP   A C   1 
ATOM   1325  O  O   . ASP   A  1 171 ? -56.552 1.717   -49.445  1.00 74.64  ? 472  ASP   A O   1 
ATOM   1326  C  CB  . ASP   A  1 171 ? -57.219 2.782   -52.038  1.00 59.38  ? 472  ASP   A CB  1 
ATOM   1327  C  CG  . ASP   A  1 171 ? -56.417 1.958   -53.036  1.00 65.62  ? 472  ASP   A CG  1 
ATOM   1328  O  OD1 . ASP   A  1 171 ? -55.205 1.769   -52.827  1.00 69.02  ? 472  ASP   A OD1 1 
ATOM   1329  O  OD2 . ASP   A  1 171 ? -57.008 1.497   -54.038  1.00 67.02  ? 472  ASP   A OD2 1 
ATOM   1330  N  N   . GLY   A  1 172 ? -54.479 2.550   -49.737  1.00 61.35  ? 473  GLY   A N   1 
ATOM   1331  C  CA  . GLY   A  1 172 ? -53.832 1.555   -48.912  1.00 53.67  ? 473  GLY   A CA  1 
ATOM   1332  C  C   . GLY   A  1 172 ? -53.543 0.248   -49.613  1.00 57.21  ? 473  GLY   A C   1 
ATOM   1333  O  O   . GLY   A  1 172 ? -52.809 -0.582  -49.063  1.00 54.08  ? 473  GLY   A O   1 
ATOM   1334  N  N   . LYS   A  1 173 ? -54.082 0.042   -50.816  1.00 59.83  ? 474  LYS   A N   1 
ATOM   1335  C  CA  . LYS   A  1 173 ? -53.857 -1.166  -51.597  1.00 60.71  ? 474  LYS   A CA  1 
ATOM   1336  C  C   . LYS   A  1 173 ? -52.781 -0.999  -52.661  1.00 57.12  ? 474  LYS   A C   1 
ATOM   1337  O  O   . LYS   A  1 173 ? -52.539 -1.934  -53.430  1.00 59.67  ? 474  LYS   A O   1 
ATOM   1338  C  CB  . LYS   A  1 173 ? -55.171 -1.614  -52.243  1.00 67.41  ? 474  LYS   A CB  1 
ATOM   1339  C  CG  . LYS   A  1 173 ? -56.114 -2.249  -51.247  1.00 76.85  ? 474  LYS   A CG  1 
ATOM   1340  C  CD  . LYS   A  1 173 ? -57.569 -2.038  -51.608  1.00 84.97  ? 474  LYS   A CD  1 
ATOM   1341  C  CE  . LYS   A  1 173 ? -58.467 -2.543  -50.484  1.00 88.85  ? 474  LYS   A CE  1 
ATOM   1342  N  NZ  . LYS   A  1 173 ? -59.912 -2.330  -50.777  1.00 89.56  ? 474  LYS   A NZ  1 
ATOM   1343  N  N   . HIS   A  1 174 ? -52.113 0.153   -52.709  1.00 52.50  ? 475  HIS   A N   1 
ATOM   1344  C  CA  . HIS   A  1 174 ? -51.098 0.426   -53.722  1.00 49.68  ? 475  HIS   A CA  1 
ATOM   1345  C  C   . HIS   A  1 174 ? -49.904 1.134   -53.113  1.00 48.21  ? 475  HIS   A C   1 
ATOM   1346  O  O   . HIS   A  1 174 ? -49.319 2.033   -53.727  1.00 42.73  ? 475  HIS   A O   1 
ATOM   1347  C  CB  . HIS   A  1 174 ? -51.677 1.256   -54.864  1.00 48.20  ? 475  HIS   A CB  1 
ATOM   1348  C  CG  . HIS   A  1 174 ? -52.833 0.597   -55.539  1.00 56.75  ? 475  HIS   A CG  1 
ATOM   1349  N  ND1 . HIS   A  1 174 ? -54.117 0.667   -55.045  1.00 59.42  ? 475  HIS   A ND1 1 
ATOM   1350  C  CD2 . HIS   A  1 174 ? -52.892 -0.179  -56.645  1.00 59.49  ? 475  HIS   A CD2 1 
ATOM   1351  C  CE1 . HIS   A  1 174 ? -54.923 -0.021  -55.833  1.00 61.94  ? 475  HIS   A CE1 1 
ATOM   1352  N  NE2 . HIS   A  1 174 ? -54.205 -0.543  -56.812  1.00 64.17  ? 475  HIS   A NE2 1 
ATOM   1353  N  N   . ASP   A  1 175 ? -49.530 0.748   -51.892  1.00 49.18  ? 476  ASP   A N   1 
ATOM   1354  C  CA  . ASP   A  1 175 ? -48.448 1.427   -51.195  1.00 43.02  ? 476  ASP   A CA  1 
ATOM   1355  C  C   . ASP   A  1 175 ? -47.114 1.177   -51.884  1.00 41.96  ? 476  ASP   A C   1 
ATOM   1356  O  O   . ASP   A  1 175 ? -46.873 0.116   -52.468  1.00 41.70  ? 476  ASP   A O   1 
ATOM   1357  C  CB  . ASP   A  1 175 ? -48.330 0.956   -49.744  1.00 56.93  ? 476  ASP   A CB  1 
ATOM   1358  C  CG  . ASP   A  1 175 ? -49.510 1.367   -48.872  1.00 53.34  ? 476  ASP   A CG  1 
ATOM   1359  O  OD1 . ASP   A  1 175 ? -50.264 2.309   -49.223  1.00 47.65  ? 476  ASP   A OD1 1 
ATOM   1360  O  OD2 . ASP   A  1 175 ? -49.668 0.720   -47.824  1.00 49.07  ? 476  ASP   A OD2 1 
ATOM   1361  N  N   . PHE   A  1 176 ? -46.248 2.177   -51.816  1.00 40.25  ? 477  PHE   A N   1 
ATOM   1362  C  CA  . PHE   A  1 176 ? -44.828 1.982   -52.041  1.00 41.51  ? 477  PHE   A CA  1 
ATOM   1363  C  C   . PHE   A  1 176 ? -44.184 1.742   -50.677  1.00 45.75  ? 477  PHE   A C   1 
ATOM   1364  O  O   . PHE   A  1 176 ? -44.468 2.467   -49.710  1.00 48.74  ? 477  PHE   A O   1 
ATOM   1365  C  CB  . PHE   A  1 176 ? -44.206 3.199   -52.729  1.00 37.45  ? 477  PHE   A CB  1 
ATOM   1366  C  CG  . PHE   A  1 176 ? -44.619 3.375   -54.175  1.00 47.22  ? 477  PHE   A CG  1 
ATOM   1367  C  CD1 . PHE   A  1 176 ? -45.934 3.652   -54.519  1.00 43.32  ? 477  PHE   A CD1 1 
ATOM   1368  C  CD2 . PHE   A  1 176 ? -43.683 3.297   -55.184  1.00 39.64  ? 477  PHE   A CD2 1 
ATOM   1369  C  CE1 . PHE   A  1 176 ? -46.296 3.828   -55.818  1.00 49.06  ? 477  PHE   A CE1 1 
ATOM   1370  C  CE2 . PHE   A  1 176 ? -44.047 3.476   -56.492  1.00 44.24  ? 477  PHE   A CE2 1 
ATOM   1371  C  CZ  . PHE   A  1 176 ? -45.354 3.740   -56.816  1.00 42.76  ? 477  PHE   A CZ  1 
ATOM   1372  N  N   . ARG   A  1 177 ? -43.345 0.713   -50.588  1.00 34.44  ? 478  ARG   A N   1 
ATOM   1373  C  CA  . ARG   A  1 177 ? -42.655 0.403   -49.343  1.00 38.94  ? 478  ARG   A CA  1 
ATOM   1374  C  C   . ARG   A  1 177 ? -41.221 0.018   -49.643  1.00 35.44  ? 478  ARG   A C   1 
ATOM   1375  O  O   . ARG   A  1 177 ? -40.974 -0.779  -50.553  1.00 36.09  ? 478  ARG   A O   1 
ATOM   1376  C  CB  . ARG   A  1 177 ? -43.340 -0.749  -48.585  1.00 35.88  ? 478  ARG   A CB  1 
ATOM   1377  C  CG  . ARG   A  1 177 ? -44.685 -0.383  -48.008  1.00 43.27  ? 478  ARG   A CG  1 
ATOM   1378  C  CD  . ARG   A  1 177 ? -44.553 0.749   -46.984  1.00 49.40  ? 478  ARG   A CD  1 
ATOM   1379  N  NE  . ARG   A  1 177 ? -43.826 0.338   -45.784  1.00 50.82  ? 478  ARG   A NE  1 
ATOM   1380  C  CZ  . ARG   A  1 177 ? -44.378 -0.276  -44.735  1.00 47.38  ? 478  ARG   A CZ  1 
ATOM   1381  N  NH1 . ARG   A  1 177 ? -45.672 -0.575  -44.731  1.00 45.50  ? 478  ARG   A NH1 1 
ATOM   1382  N  NH2 . ARG   A  1 177 ? -43.632 -0.593  -43.688  1.00 38.61  ? 478  ARG   A NH2 1 
ATOM   1383  N  N   . VAL   A  1 178 ? -40.282 0.557   -48.874  1.00 31.96  ? 479  VAL   A N   1 
ATOM   1384  C  CA  . VAL   A  1 178 ? -38.978 -0.077  -48.744  1.00 40.72  ? 479  VAL   A CA  1 
ATOM   1385  C  C   . VAL   A  1 178 ? -39.110 -1.106  -47.636  1.00 45.33  ? 479  VAL   A C   1 
ATOM   1386  O  O   . VAL   A  1 178 ? -39.423 -0.759  -46.493  1.00 44.86  ? 479  VAL   A O   1 
ATOM   1387  C  CB  . VAL   A  1 178 ? -37.866 0.935   -48.434  1.00 45.59  ? 479  VAL   A CB  1 
ATOM   1388  C  CG1 . VAL   A  1 178 ? -36.543 0.203   -48.321  1.00 42.67  ? 479  VAL   A CG1 1 
ATOM   1389  C  CG2 . VAL   A  1 178 ? -37.768 2.011   -49.527  1.00 47.54  ? 479  VAL   A CG2 1 
ATOM   1390  N  N   . TRP   A  1 179 ? -38.914 -2.378  -47.974  1.00 46.97  ? 480  TRP   A N   1 
ATOM   1391  C  CA  . TRP   A  1 179 ? -39.086 -3.407  -46.953  1.00 38.09  ? 480  TRP   A CA  1 
ATOM   1392  C  C   . TRP   A  1 179 ? -37.909 -3.450  -45.983  1.00 35.75  ? 480  TRP   A C   1 
ATOM   1393  O  O   . TRP   A  1 179 ? -38.078 -3.872  -44.837  1.00 44.48  ? 480  TRP   A O   1 
ATOM   1394  C  CB  . TRP   A  1 179 ? -39.299 -4.776  -47.604  1.00 31.41  ? 480  TRP   A CB  1 
ATOM   1395  C  CG  . TRP   A  1 179 ? -40.703 -4.969  -48.087  1.00 35.97  ? 480  TRP   A CG  1 
ATOM   1396  C  CD1 . TRP   A  1 179 ? -41.539 -4.007  -48.599  1.00 37.32  ? 480  TRP   A CD1 1 
ATOM   1397  C  CD2 . TRP   A  1 179 ? -41.453 -6.192  -48.084  1.00 33.68  ? 480  TRP   A CD2 1 
ATOM   1398  N  NE1 . TRP   A  1 179 ? -42.750 -4.573  -48.941  1.00 35.24  ? 480  TRP   A NE1 1 
ATOM   1399  C  CE2 . TRP   A  1 179 ? -42.726 -5.906  -48.622  1.00 35.86  ? 480  TRP   A CE2 1 
ATOM   1400  C  CE3 . TRP   A  1 179 ? -41.170 -7.504  -47.688  1.00 33.78  ? 480  TRP   A CE3 1 
ATOM   1401  C  CZ2 . TRP   A  1 179 ? -43.717 -6.877  -48.749  1.00 38.55  ? 480  TRP   A CZ2 1 
ATOM   1402  C  CZ3 . TRP   A  1 179 ? -42.151 -8.462  -47.817  1.00 38.25  ? 480  TRP   A CZ3 1 
ATOM   1403  C  CH2 . TRP   A  1 179 ? -43.407 -8.148  -48.355  1.00 39.94  ? 480  TRP   A CH2 1 
ATOM   1404  N  N   . ASN   A  1 180 ? -36.721 -3.045  -46.423  1.00 36.66  ? 481  ASN   A N   1 
ATOM   1405  C  CA  . ASN   A  1 180 ? -35.588 -2.886  -45.525  1.00 37.12  ? 481  ASN   A CA  1 
ATOM   1406  C  C   . ASN   A  1 180 ? -35.906 -1.863  -44.442  1.00 37.95  ? 481  ASN   A C   1 
ATOM   1407  O  O   . ASN   A  1 180 ? -36.632 -0.895  -44.676  1.00 37.93  ? 481  ASN   A O   1 
ATOM   1408  C  CB  . ASN   A  1 180 ? -34.370 -2.406  -46.298  1.00 31.87  ? 481  ASN   A CB  1 
ATOM   1409  C  CG  . ASN   A  1 180 ? -34.074 -3.252  -47.510  1.00 36.47  ? 481  ASN   A CG  1 
ATOM   1410  O  OD1 . ASN   A  1 180 ? -34.841 -3.285  -48.479  1.00 38.10  ? 481  ASN   A OD1 1 
ATOM   1411  N  ND2 . ASN   A  1 180 ? -32.941 -3.932  -47.472  1.00 37.21  ? 481  ASN   A ND2 1 
ATOM   1412  N  N   . SER   A  1 181 ? -35.319 -2.055  -43.257  1.00 30.57  ? 482  SER   A N   1 
ATOM   1413  C  CA  . SER   A  1 181 ? -35.513 -1.050  -42.221  1.00 35.20  ? 482  SER   A CA  1 
ATOM   1414  C  C   . SER   A  1 181 ? -34.477 0.054   -42.357  1.00 38.02  ? 482  SER   A C   1 
ATOM   1415  O  O   . SER   A  1 181 ? -34.799 1.231   -42.152  1.00 38.30  ? 482  SER   A O   1 
ATOM   1416  C  CB  . SER   A  1 181 ? -35.521 -1.685  -40.812  1.00 34.00  ? 482  SER   A CB  1 
ATOM   1417  O  OG  . SER   A  1 181 ? -34.350 -2.422  -40.483  1.00 34.00  ? 482  SER   A OG  1 
ATOM   1418  N  N   . GLN   A  1 182 ? -33.257 -0.285  -42.762  1.00 36.57  ? 483  GLN   A N   1 
ATOM   1419  C  CA  . GLN   A  1 182 ? -32.330 0.719   -43.269  1.00 39.68  ? 483  GLN   A CA  1 
ATOM   1420  C  C   . GLN   A  1 182 ? -31.878 0.334   -44.674  1.00 36.23  ? 483  GLN   A C   1 
ATOM   1421  O  O   . GLN   A  1 182 ? -32.015 -0.819  -45.088  1.00 32.87  ? 483  GLN   A O   1 
ATOM   1422  C  CB  . GLN   A  1 182 ? -31.113 0.904   -42.354  1.00 42.90  ? 483  GLN   A CB  1 
ATOM   1423  C  CG  . GLN   A  1 182 ? -31.439 1.450   -40.959  1.00 51.53  ? 483  GLN   A CG  1 
ATOM   1424  C  CD  . GLN   A  1 182 ? -30.245 1.368   -40.016  1.00 51.03  ? 483  GLN   A CD  1 
ATOM   1425  O  OE1 . GLN   A  1 182 ? -29.137 1.804   -40.339  1.00 50.00  ? 483  GLN   A OE1 1 
ATOM   1426  N  NE2 . GLN   A  1 182 ? -30.461 0.775   -38.864  1.00 55.04  ? 483  GLN   A NE2 1 
ATOM   1427  N  N   . LEU   A  1 183 ? -31.340 1.314   -45.416  1.00 34.49  ? 484  LEU   A N   1 
ATOM   1428  C  CA  . LEU   A  1 183 ? -30.912 1.028   -46.795  1.00 39.41  ? 484  LEU   A CA  1 
ATOM   1429  C  C   . LEU   A  1 183 ? -29.677 0.139   -46.805  1.00 40.28  ? 484  LEU   A C   1 
ATOM   1430  O  O   . LEU   A  1 183 ? -29.548 -0.743  -47.658  1.00 37.53  ? 484  LEU   A O   1 
ATOM   1431  C  CB  . LEU   A  1 183 ? -30.636 2.323   -47.566  1.00 30.36  ? 484  LEU   A CB  1 
ATOM   1432  C  CG  . LEU   A  1 183 ? -31.783 3.313   -47.756  1.00 30.50  ? 484  LEU   A CG  1 
ATOM   1433  C  CD1 . LEU   A  1 183 ? -31.289 4.568   -48.474  1.00 26.18  ? 484  LEU   A CD1 1 
ATOM   1434  C  CD2 . LEU   A  1 183 ? -32.935 2.688   -48.497  1.00 25.03  ? 484  LEU   A CD2 1 
ATOM   1435  N  N   . ILE   A  1 184 ? -28.786 0.326   -45.837  1.00 32.78  ? 485  ILE   A N   1 
ATOM   1436  C  CA  . ILE   A  1 184 ? -27.637 -0.548  -45.636  1.00 38.02  ? 485  ILE   A CA  1 
ATOM   1437  C  C   . ILE   A  1 184 ? -27.721 -1.134  -44.225  1.00 40.16  ? 485  ILE   A C   1 
ATOM   1438  O  O   . ILE   A  1 184 ? -27.649 -0.390  -43.242  1.00 34.41  ? 485  ILE   A O   1 
ATOM   1439  C  CB  . ILE   A  1 184 ? -26.320 0.205   -45.830  1.00 38.10  ? 485  ILE   A CB  1 
ATOM   1440  C  CG1 . ILE   A  1 184 ? -26.290 0.880   -47.201  1.00 44.23  ? 485  ILE   A CG1 1 
ATOM   1441  C  CG2 . ILE   A  1 184 ? -25.158 -0.736  -45.683  1.00 36.97  ? 485  ILE   A CG2 1 
ATOM   1442  C  CD1 . ILE   A  1 184 ? -25.055 1.678   -47.411  1.00 50.44  ? 485  ILE   A CD1 1 
ATOM   1443  N  N   . ARG   A  1 185 ? -27.923 -2.451  -44.132  1.00 42.17  ? 486  ARG   A N   1 
ATOM   1444  C  CA  . ARG   A  1 185 ? -27.732 -3.234  -42.908  1.00 44.00  ? 486  ARG   A CA  1 
ATOM   1445  C  C   . ARG   A  1 185 ? -27.044 -4.538  -43.285  1.00 47.45  ? 486  ARG   A C   1 
ATOM   1446  O  O   . ARG   A  1 185 ? -27.045 -4.951  -44.450  1.00 42.15  ? 486  ARG   A O   1 
ATOM   1447  C  CB  . ARG   A  1 185 ? -29.031 -3.620  -42.164  1.00 41.32  ? 486  ARG   A CB  1 
ATOM   1448  C  CG  . ARG   A  1 185 ? -30.143 -2.608  -42.063  1.00 52.86  ? 486  ARG   A CG  1 
ATOM   1449  C  CD  . ARG   A  1 185 ? -30.259 -2.006  -40.659  1.00 56.95  ? 486  ARG   A CD  1 
ATOM   1450  N  NE  . ARG   A  1 185 ? -29.926 -2.903  -39.555  1.00 63.25  ? 486  ARG   A NE  1 
ATOM   1451  C  CZ  . ARG   A  1 185 ? -30.683 -3.080  -38.468  1.00 63.83  ? 486  ARG   A CZ  1 
ATOM   1452  N  NH1 . ARG   A  1 185 ? -31.838 -2.442  -38.332  1.00 58.93  ? 486  ARG   A NH1 1 
ATOM   1453  N  NH2 . ARG   A  1 185 ? -30.286 -3.902  -37.508  1.00 60.21  ? 486  ARG   A NH2 1 
ATOM   1454  N  N   . TYR   A  1 186 ? -26.482 -5.204  -42.284  1.00 36.31  ? 487  TYR   A N   1 
ATOM   1455  C  CA  . TYR   A  1 186 ? -25.882 -6.508  -42.506  1.00 40.16  ? 487  TYR   A CA  1 
ATOM   1456  C  C   . TYR   A  1 186 ? -26.871 -7.643  -42.230  1.00 45.05  ? 487  TYR   A C   1 
ATOM   1457  O  O   . TYR   A  1 186 ? -27.786 -7.524  -41.412  1.00 51.25  ? 487  TYR   A O   1 
ATOM   1458  C  CB  . TYR   A  1 186 ? -24.634 -6.663  -41.642  1.00 31.05  ? 487  TYR   A CB  1 
ATOM   1459  C  CG  . TYR   A  1 186 ? -23.550 -5.669  -41.943  1.00 41.94  ? 487  TYR   A CG  1 
ATOM   1460  C  CD1 . TYR   A  1 186 ? -22.920 -5.668  -43.180  1.00 46.58  ? 487  TYR   A CD1 1 
ATOM   1461  C  CD2 . TYR   A  1 186 ? -23.133 -4.748  -40.992  1.00 42.32  ? 487  TYR   A CD2 1 
ATOM   1462  C  CE1 . TYR   A  1 186 ? -21.911 -4.775  -43.468  1.00 48.25  ? 487  TYR   A CE1 1 
ATOM   1463  C  CE2 . TYR   A  1 186 ? -22.121 -3.832  -41.278  1.00 46.06  ? 487  TYR   A CE2 1 
ATOM   1464  C  CZ  . TYR   A  1 186 ? -21.509 -3.857  -42.521  1.00 40.77  ? 487  TYR   A CZ  1 
ATOM   1465  O  OH  . TYR   A  1 186 ? -20.488 -2.972  -42.831  1.00 34.90  ? 487  TYR   A OH  1 
ATOM   1466  N  N   . ALA   A  1 187 ? -26.661 -8.760  -42.918  1.00 37.64  ? 488  ALA   A N   1 
ATOM   1467  C  CA  . ALA   A  1 187 ? -27.534 -9.912  -42.778  1.00 42.72  ? 488  ALA   A CA  1 
ATOM   1468  C  C   . ALA   A  1 187 ? -27.306 -10.620 -41.448  1.00 49.02  ? 488  ALA   A C   1 
ATOM   1469  O  O   . ALA   A  1 187 ? -26.255 -10.493 -40.810  1.00 39.16  ? 488  ALA   A O   1 
ATOM   1470  C  CB  . ALA   A  1 187 ? -27.302 -10.901 -43.916  1.00 39.60  ? 488  ALA   A CB  1 
ATOM   1471  N  N   . GLY   A  1 188 ? -28.318 -11.372 -41.046  1.00 54.79  ? 489  GLY   A N   1 
ATOM   1472  C  CA  . GLY   A  1 188 ? -28.221 -12.230 -39.876  1.00 48.28  ? 489  GLY   A CA  1 
ATOM   1473  C  C   . GLY   A  1 188 ? -28.691 -13.627 -40.206  1.00 57.46  ? 489  GLY   A C   1 
ATOM   1474  O  O   . GLY   A  1 188 ? -29.698 -13.809 -40.883  1.00 60.60  ? 489  GLY   A O   1 
ATOM   1475  N  N   . TYR   A  1 189 ? -27.926 -14.615 -39.751  1.00 64.21  ? 490  TYR   A N   1 
ATOM   1476  C  CA  . TYR   A  1 189 ? -28.231 -16.018 -39.999  1.00 50.68  ? 490  TYR   A CA  1 
ATOM   1477  C  C   . TYR   A  1 189 ? -28.204 -16.745 -38.671  1.00 55.30  ? 490  TYR   A C   1 
ATOM   1478  O  O   . TYR   A  1 189 ? -27.172 -16.745 -37.994  1.00 53.42  ? 490  TYR   A O   1 
ATOM   1479  C  CB  . TYR   A  1 189 ? -27.223 -16.656 -40.948  1.00 41.44  ? 490  TYR   A CB  1 
ATOM   1480  C  CG  . TYR   A  1 189 ? -26.857 -15.840 -42.160  1.00 51.93  ? 490  TYR   A CG  1 
ATOM   1481  C  CD1 . TYR   A  1 189 ? -27.610 -15.918 -43.327  1.00 53.81  ? 490  TYR   A CD1 1 
ATOM   1482  C  CD2 . TYR   A  1 189 ? -25.731 -15.022 -42.159  1.00 55.44  ? 490  TYR   A CD2 1 
ATOM   1483  C  CE1 . TYR   A  1 189 ? -27.269 -15.179 -44.461  1.00 50.05  ? 490  TYR   A CE1 1 
ATOM   1484  C  CE2 . TYR   A  1 189 ? -25.375 -14.282 -43.295  1.00 55.12  ? 490  TYR   A CE2 1 
ATOM   1485  C  CZ  . TYR   A  1 189 ? -26.149 -14.367 -44.436  1.00 52.50  ? 490  TYR   A CZ  1 
ATOM   1486  O  OH  . TYR   A  1 189 ? -25.804 -13.637 -45.549  1.00 55.61  ? 490  TYR   A OH  1 
ATOM   1487  N  N   . LYS   A  1 190 ? -29.321 -17.375 -38.315  1.00 51.10  ? 491  LYS   A N   1 
ATOM   1488  C  CA  . LYS   A  1 190 ? -29.348 -18.285 -37.180  1.00 58.32  ? 491  LYS   A CA  1 
ATOM   1489  C  C   . LYS   A  1 190 ? -28.766 -19.630 -37.603  1.00 54.97  ? 491  LYS   A C   1 
ATOM   1490  O  O   . LYS   A  1 190 ? -29.175 -20.197 -38.621  1.00 63.67  ? 491  LYS   A O   1 
ATOM   1491  C  CB  . LYS   A  1 190 ? -30.777 -18.452 -36.657  1.00 71.32  ? 491  LYS   A CB  1 
ATOM   1492  C  CG  . LYS   A  1 190 ? -30.878 -18.799 -35.164  1.00 85.18  ? 491  LYS   A CG  1 
ATOM   1493  C  CD  . LYS   A  1 190 ? -30.861 -17.546 -34.293  1.00 87.91  ? 491  LYS   A CD  1 
ATOM   1494  C  CE  . LYS   A  1 190 ? -31.077 -17.884 -32.822  1.00 92.11  ? 491  LYS   A CE  1 
ATOM   1495  N  NZ  . LYS   A  1 190 ? -32.393 -18.544 -32.560  1.00 94.81  ? 491  LYS   A NZ  1 
ATOM   1496  N  N   . GLN   A  1 191 ? -27.789 -20.125 -36.835  1.00 45.92  ? 492  GLN   A N   1 
ATOM   1497  C  CA  . GLN   A  1 191 ? -27.162 -21.416 -37.067  1.00 56.57  ? 492  GLN   A CA  1 
ATOM   1498  C  C   . GLN   A  1 191 ? -27.994 -22.538 -36.450  1.00 59.50  ? 492  GLN   A C   1 
ATOM   1499  O  O   . GLN   A  1 191 ? -28.827 -22.298 -35.573  1.00 67.08  ? 492  GLN   A O   1 
ATOM   1500  C  CB  . GLN   A  1 191 ? -25.752 -21.423 -36.479  1.00 62.33  ? 492  GLN   A CB  1 
ATOM   1501  C  CG  . GLN   A  1 191 ? -24.865 -20.290 -36.975  1.00 57.83  ? 492  GLN   A CG  1 
ATOM   1502  C  CD  . GLN   A  1 191 ? -24.615 -20.367 -38.468  1.00 59.87  ? 492  GLN   A CD  1 
ATOM   1503  O  OE1 . GLN   A  1 191 ? -25.193 -19.610 -39.247  1.00 61.56  ? 492  GLN   A OE1 1 
ATOM   1504  N  NE2 . GLN   A  1 191 ? -23.756 -21.292 -38.875  1.00 62.54  ? 492  GLN   A NE2 1 
ATOM   1505  N  N   . PRO   A  1 192 ? -27.795 -23.779 -36.895  1.00 53.43  ? 493  PRO   A N   1 
ATOM   1506  C  CA  . PRO   A  1 192 ? -28.509 -24.898 -36.253  1.00 58.85  ? 493  PRO   A CA  1 
ATOM   1507  C  C   . PRO   A  1 192 ? -28.113 -25.110 -34.801  1.00 64.23  ? 493  PRO   A C   1 
ATOM   1508  O  O   . PRO   A  1 192 ? -28.894 -25.706 -34.042  1.00 67.17  ? 493  PRO   A O   1 
ATOM   1509  C  CB  . PRO   A  1 192 ? -28.136 -26.113 -37.120  1.00 61.88  ? 493  PRO   A CB  1 
ATOM   1510  C  CG  . PRO   A  1 192 ? -26.915 -25.691 -37.902  1.00 57.54  ? 493  PRO   A CG  1 
ATOM   1511  C  CD  . PRO   A  1 192 ? -27.013 -24.206 -38.069  1.00 54.43  ? 493  PRO   A CD  1 
ATOM   1512  N  N   . ASP   A  1 193 ? -26.932 -24.652 -34.389  1.00 57.76  ? 494  ASP   A N   1 
ATOM   1513  C  CA  . ASP   A  1 193 ? -26.487 -24.855 -33.015  1.00 60.11  ? 494  ASP   A CA  1 
ATOM   1514  C  C   . ASP   A  1 193 ? -27.036 -23.800 -32.060  1.00 60.05  ? 494  ASP   A C   1 
ATOM   1515  O  O   . ASP   A  1 193 ? -26.643 -23.769 -30.887  1.00 67.89  ? 494  ASP   A O   1 
ATOM   1516  C  CB  . ASP   A  1 193 ? -24.951 -24.904 -32.951  1.00 54.08  ? 494  ASP   A CB  1 
ATOM   1517  C  CG  . ASP   A  1 193 ? -24.292 -23.538 -33.127  1.00 57.57  ? 494  ASP   A CG  1 
ATOM   1518  O  OD1 . ASP   A  1 193 ? -24.958 -22.559 -33.523  1.00 59.61  ? 494  ASP   A OD1 1 
ATOM   1519  O  OD2 . ASP   A  1 193 ? -23.077 -23.444 -32.853  1.00 61.95  ? 494  ASP   A OD2 1 
ATOM   1520  N  N   . GLY   A  1 194 ? -27.943 -22.952 -32.533  1.00 53.52  ? 495  GLY   A N   1 
ATOM   1521  C  CA  . GLY   A  1 194 ? -28.476 -21.875 -31.749  1.00 54.94  ? 495  GLY   A CA  1 
ATOM   1522  C  C   . GLY   A  1 194 ? -27.738 -20.561 -31.883  1.00 52.04  ? 495  GLY   A C   1 
ATOM   1523  O  O   . GLY   A  1 194 ? -28.339 -19.509 -31.656  1.00 55.71  ? 495  GLY   A O   1 
ATOM   1524  N  N   . SER   A  1 195 ? -26.462 -20.582 -32.258  1.00 54.05  ? 496  SER   A N   1 
ATOM   1525  C  CA  . SER   A  1 195 ? -25.714 -19.342 -32.413  1.00 61.69  ? 496  SER   A CA  1 
ATOM   1526  C  C   . SER   A  1 195 ? -26.242 -18.527 -33.602  1.00 59.29  ? 496  SER   A C   1 
ATOM   1527  O  O   . SER   A  1 195 ? -27.104 -18.968 -34.364  1.00 61.03  ? 496  SER   A O   1 
ATOM   1528  C  CB  . SER   A  1 195 ? -24.228 -19.634 -32.599  1.00 62.75  ? 496  SER   A CB  1 
ATOM   1529  O  OG  . SER   A  1 195 ? -24.008 -20.273 -33.834  1.00 64.47  ? 496  SER   A OG  1 
ATOM   1530  N  N   . THR   A  1 196 ? -25.715 -17.313 -33.752  1.00 56.65  ? 497  THR   A N   1 
ATOM   1531  C  CA  . THR   A  1 196 ? -26.142 -16.408 -34.812  1.00 56.83  ? 497  THR   A CA  1 
ATOM   1532  C  C   . THR   A  1 196 ? -24.930 -15.788 -35.496  1.00 59.49  ? 497  THR   A C   1 
ATOM   1533  O  O   . THR   A  1 196 ? -24.068 -15.210 -34.832  1.00 64.50  ? 497  THR   A O   1 
ATOM   1534  C  CB  . THR   A  1 196 ? -27.042 -15.288 -34.273  1.00 58.92  ? 497  THR   A CB  1 
ATOM   1535  O  OG1 . THR   A  1 196 ? -28.100 -15.844 -33.477  1.00 62.51  ? 497  THR   A OG1 1 
ATOM   1536  C  CG2 . THR   A  1 196 ? -27.635 -14.484 -35.441  1.00 58.18  ? 497  THR   A CG2 1 
ATOM   1537  N  N   . LEU   A  1 197 ? -24.876 -15.889 -36.821  1.00 61.30  ? 498  LEU   A N   1 
ATOM   1538  C  CA  . LEU   A  1 197 ? -23.830 -15.259 -37.616  1.00 55.60  ? 498  LEU   A CA  1 
ATOM   1539  C  C   . LEU   A  1 197 ? -24.349 -13.943 -38.171  1.00 52.25  ? 498  LEU   A C   1 
ATOM   1540  O  O   . LEU   A  1 197 ? -25.493 -13.863 -38.626  1.00 54.89  ? 498  LEU   A O   1 
ATOM   1541  C  CB  . LEU   A  1 197 ? -23.383 -16.171 -38.756  1.00 55.19  ? 498  LEU   A CB  1 
ATOM   1542  C  CG  . LEU   A  1 197 ? -22.379 -15.537 -39.716  1.00 60.54  ? 498  LEU   A CG  1 
ATOM   1543  C  CD1 . LEU   A  1 197 ? -21.131 -15.091 -38.963  1.00 56.08  ? 498  LEU   A CD1 1 
ATOM   1544  C  CD2 . LEU   A  1 197 ? -22.028 -16.486 -40.873  1.00 63.58  ? 498  LEU   A CD2 1 
ATOM   1545  N  N   . GLY   A  1 198 ? -23.511 -12.904 -38.111  1.00 52.38  ? 499  GLY   A N   1 
ATOM   1546  C  CA  . GLY   A  1 198 ? -23.910 -11.567 -38.521  1.00 53.86  ? 499  GLY   A CA  1 
ATOM   1547  C  C   . GLY   A  1 198 ? -24.708 -10.773 -37.497  1.00 58.67  ? 499  GLY   A C   1 
ATOM   1548  O  O   . GLY   A  1 198 ? -24.452 -10.841 -36.292  1.00 65.02  ? 499  GLY   A O   1 
ATOM   1549  N  N   . ASP   A  1 199 ? -25.704 -10.032 -37.972  1.00 53.50  ? 500  ASP   A N   1 
ATOM   1550  C  CA  . ASP   A  1 199 ? -26.472 -9.123  -37.137  1.00 51.12  ? 500  ASP   A CA  1 
ATOM   1551  C  C   . ASP   A  1 199 ? -27.774 -9.788  -36.710  1.00 54.22  ? 500  ASP   A C   1 
ATOM   1552  O  O   . ASP   A  1 199 ? -28.706 -9.887  -37.525  1.00 56.95  ? 500  ASP   A O   1 
ATOM   1553  C  CB  . ASP   A  1 199 ? -26.755 -7.829  -37.898  1.00 48.89  ? 500  ASP   A CB  1 
ATOM   1554  C  CG  . ASP   A  1 199 ? -27.336 -6.733  -37.019  1.00 48.88  ? 500  ASP   A CG  1 
ATOM   1555  O  OD1 . ASP   A  1 199 ? -28.164 -7.049  -36.127  1.00 47.83  ? 500  ASP   A OD1 1 
ATOM   1556  O  OD2 . ASP   A  1 199 ? -26.963 -5.551  -37.233  1.00 39.54  ? 500  ASP   A OD2 1 
ATOM   1557  N  N   . PRO   A  1 200 ? -27.898 -10.214 -35.451  1.00 48.73  ? 501  PRO   A N   1 
ATOM   1558  C  CA  . PRO   A  1 200 ? -29.113 -10.926 -35.011  1.00 49.11  ? 501  PRO   A CA  1 
ATOM   1559  C  C   . PRO   A  1 200 ? -30.399 -10.145 -35.199  1.00 51.77  ? 501  PRO   A C   1 
ATOM   1560  O  O   . PRO   A  1 200 ? -31.464 -10.764 -35.318  1.00 51.21  ? 501  PRO   A O   1 
ATOM   1561  C  CB  . PRO   A  1 200 ? -28.841 -11.190 -33.522  1.00 42.45  ? 501  PRO   A CB  1 
ATOM   1562  C  CG  . PRO   A  1 200 ? -27.345 -11.174 -33.417  1.00 41.38  ? 501  PRO   A CG  1 
ATOM   1563  C  CD  . PRO   A  1 200 ? -26.874 -10.145 -34.400  1.00 41.11  ? 501  PRO   A CD  1 
ATOM   1564  N  N   . ALA   A  1 201 ? -30.332 -8.811  -35.242  1.00 58.81  ? 502  ALA   A N   1 
ATOM   1565  C  CA  . ALA   A  1 201 ? -31.509 -7.974  -35.470  1.00 48.87  ? 502  ALA   A CA  1 
ATOM   1566  C  C   . ALA   A  1 201 ? -32.154 -8.189  -36.834  1.00 52.66  ? 502  ALA   A C   1 
ATOM   1567  O  O   . ALA   A  1 201 ? -33.326 -7.844  -37.017  1.00 48.55  ? 502  ALA   A O   1 
ATOM   1568  C  CB  . ALA   A  1 201 ? -31.137 -6.501  -35.351  1.00 36.68  ? 502  ALA   A CB  1 
ATOM   1569  N  N   . ASN   A  1 202 ? -31.422 -8.727  -37.804  1.00 49.71  ? 503  ASN   A N   1 
ATOM   1570  C  CA  . ASN   A  1 202 ? -31.928 -8.777  -39.167  1.00 49.78  ? 503  ASN   A CA  1 
ATOM   1571  C  C   . ASN   A  1 202 ? -32.212 -10.201 -39.620  1.00 49.22  ? 503  ASN   A C   1 
ATOM   1572  O  O   . ASN   A  1 202 ? -32.346 -10.446 -40.823  1.00 51.42  ? 503  ASN   A O   1 
ATOM   1573  C  CB  . ASN   A  1 202 ? -30.941 -8.080  -40.105  1.00 38.61  ? 503  ASN   A CB  1 
ATOM   1574  C  CG  . ASN   A  1 202 ? -30.767 -6.606  -39.773  1.00 41.17  ? 503  ASN   A CG  1 
ATOM   1575  O  OD1 . ASN   A  1 202 ? -31.743 -5.914  -39.484  1.00 47.16  ? 503  ASN   A OD1 1 
ATOM   1576  N  ND2 . ASN   A  1 202 ? -29.524 -6.115  -39.827  1.00 40.29  ? 503  ASN   A ND2 1 
ATOM   1577  N  N   . VAL   A  1 203 ? -32.333 -11.140 -38.674  1.00 44.27  ? 504  VAL   A N   1 
ATOM   1578  C  CA  . VAL   A  1 203 ? -32.493 -12.547 -39.033  1.00 40.83  ? 504  VAL   A CA  1 
ATOM   1579  C  C   . VAL   A  1 203 ? -33.785 -12.771 -39.812  1.00 51.24  ? 504  VAL   A C   1 
ATOM   1580  O  O   . VAL   A  1 203 ? -33.801 -13.491 -40.822  1.00 49.10  ? 504  VAL   A O   1 
ATOM   1581  C  CB  . VAL   A  1 203 ? -32.423 -13.438 -37.781  1.00 45.19  ? 504  VAL   A CB  1 
ATOM   1582  C  CG1 . VAL   A  1 203 ? -33.189 -14.732 -38.014  1.00 41.13  ? 504  VAL   A CG1 1 
ATOM   1583  C  CG2 . VAL   A  1 203 ? -30.979 -13.749 -37.459  1.00 49.78  ? 504  VAL   A CG2 1 
ATOM   1584  N  N   . GLN   A  1 204 ? -34.886 -12.164 -39.368  1.00 52.37  ? 505  GLN   A N   1 
ATOM   1585  C  CA  . GLN   A  1 204 ? -36.151 -12.416 -40.048  1.00 56.81  ? 505  GLN   A CA  1 
ATOM   1586  C  C   . GLN   A  1 204 ? -36.158 -11.783 -41.433  1.00 59.16  ? 505  GLN   A C   1 
ATOM   1587  O  O   . GLN   A  1 204 ? -36.634 -12.394 -42.401  1.00 59.35  ? 505  GLN   A O   1 
ATOM   1588  C  CB  . GLN   A  1 204 ? -37.324 -11.898 -39.225  1.00 64.42  ? 505  GLN   A CB  1 
ATOM   1589  C  CG  . GLN   A  1 204 ? -38.604 -12.666 -39.507  1.00 76.43  ? 505  GLN   A CG  1 
ATOM   1590  C  CD  . GLN   A  1 204 ? -39.830 -11.774 -39.568  1.00 79.98  ? 505  GLN   A CD  1 
ATOM   1591  O  OE1 . GLN   A  1 204 ? -39.955 -10.805 -38.807  1.00 68.77  ? 505  GLN   A OE1 1 
ATOM   1592  N  NE2 . GLN   A  1 204 ? -40.744 -12.094 -40.487  1.00 85.42  ? 505  GLN   A NE2 1 
ATOM   1593  N  N   . PHE   A  1 205 ? -35.627 -10.564 -41.550  1.00 51.05  ? 506  PHE   A N   1 
ATOM   1594  C  CA  . PHE   A  1 205 ? -35.543 -9.942  -42.861  1.00 44.61  ? 506  PHE   A CA  1 
ATOM   1595  C  C   . PHE   A  1 205 ? -34.601 -10.715 -43.780  1.00 46.21  ? 506  PHE   A C   1 
ATOM   1596  O  O   . PHE   A  1 205 ? -34.885 -10.876 -44.971  1.00 50.86  ? 506  PHE   A O   1 
ATOM   1597  C  CB  . PHE   A  1 205 ? -35.096 -8.492  -42.741  1.00 42.53  ? 506  PHE   A CB  1 
ATOM   1598  C  CG  . PHE   A  1 205 ? -35.040 -7.801  -44.059  1.00 45.21  ? 506  PHE   A CG  1 
ATOM   1599  C  CD1 . PHE   A  1 205 ? -36.198 -7.297  -44.627  1.00 49.72  ? 506  PHE   A CD1 1 
ATOM   1600  C  CD2 . PHE   A  1 205 ? -33.850 -7.720  -44.775  1.00 46.43  ? 506  PHE   A CD2 1 
ATOM   1601  C  CE1 . PHE   A  1 205 ? -36.170 -6.674  -45.875  1.00 46.86  ? 506  PHE   A CE1 1 
ATOM   1602  C  CE2 . PHE   A  1 205 ? -33.812 -7.095  -46.016  1.00 42.65  ? 506  PHE   A CE2 1 
ATOM   1603  C  CZ  . PHE   A  1 205 ? -34.975 -6.569  -46.566  1.00 40.75  ? 506  PHE   A CZ  1 
ATOM   1604  N  N   . THR   A  1 206 ? -33.476 -11.198 -43.244  1.00 48.73  ? 507  THR   A N   1 
ATOM   1605  C  CA  . THR   A  1 206 ? -32.589 -12.057 -44.025  1.00 44.95  ? 507  THR   A CA  1 
ATOM   1606  C  C   . THR   A  1 206 ? -33.328 -13.294 -44.531  1.00 50.98  ? 507  THR   A C   1 
ATOM   1607  O  O   . THR   A  1 206 ? -33.130 -13.718 -45.677  1.00 52.47  ? 507  THR   A O   1 
ATOM   1608  C  CB  . THR   A  1 206 ? -31.359 -12.452 -43.195  1.00 36.61  ? 507  THR   A CB  1 
ATOM   1609  O  OG1 . THR   A  1 206 ? -30.624 -11.282 -42.819  1.00 35.90  ? 507  THR   A OG1 1 
ATOM   1610  C  CG2 . THR   A  1 206 ? -30.444 -13.360 -43.978  1.00 39.44  ? 507  THR   A CG2 1 
ATOM   1611  N  N   . GLU   A  1 207 ? -34.201 -13.873 -43.704  1.00 52.20  ? 508  GLU   A N   1 
ATOM   1612  C  CA  . GLU   A  1 207 ? -34.969 -15.033 -44.145  1.00 55.72  ? 508  GLU   A CA  1 
ATOM   1613  C  C   . GLU   A  1 207 ? -35.957 -14.653 -45.244  1.00 55.86  ? 508  GLU   A C   1 
ATOM   1614  O  O   . GLU   A  1 207 ? -36.168 -15.426 -46.186  1.00 59.87  ? 508  GLU   A O   1 
ATOM   1615  C  CB  . GLU   A  1 207 ? -35.694 -15.671 -42.954  1.00 58.29  ? 508  GLU   A CB  1 
ATOM   1616  C  CG  . GLU   A  1 207 ? -34.800 -16.457 -41.998  1.00 60.67  ? 508  GLU   A CG  1 
ATOM   1617  C  CD  . GLU   A  1 207 ? -35.504 -16.805 -40.682  1.00 78.00  ? 508  GLU   A CD  1 
ATOM   1618  O  OE1 . GLU   A  1 207 ? -36.618 -16.282 -40.438  1.00 81.02  ? 508  GLU   A OE1 1 
ATOM   1619  O  OE2 . GLU   A  1 207 ? -34.942 -17.595 -39.888  1.00 79.82  ? 508  GLU   A OE2 1 
ATOM   1620  N  N   . ILE   A  1 208 ? -36.580 -13.475 -45.138  1.00 50.80  ? 509  ILE   A N   1 
ATOM   1621  C  CA  . ILE   A  1 208 ? -37.489 -13.026 -46.189  1.00 50.43  ? 509  ILE   A CA  1 
ATOM   1622  C  C   . ILE   A  1 208 ? -36.728 -12.822 -47.490  1.00 55.90  ? 509  ILE   A C   1 
ATOM   1623  O  O   . ILE   A  1 208 ? -37.243 -13.103 -48.573  1.00 73.77  ? 509  ILE   A O   1 
ATOM   1624  C  CB  . ILE   A  1 208 ? -38.221 -11.738 -45.771  1.00 50.12  ? 509  ILE   A CB  1 
ATOM   1625  C  CG1 . ILE   A  1 208 ? -39.029 -11.953 -44.498  1.00 52.49  ? 509  ILE   A CG1 1 
ATOM   1626  C  CG2 . ILE   A  1 208 ? -39.145 -11.258 -46.883  1.00 41.93  ? 509  ILE   A CG2 1 
ATOM   1627  C  CD1 . ILE   A  1 208 ? -39.603 -10.667 -43.939  1.00 52.12  ? 509  ILE   A CD1 1 
ATOM   1628  N  N   . CYS   A  1 209 ? -35.495 -12.316 -47.410  1.00 46.24  ? 510  CYS   A N   1 
ATOM   1629  C  CA  . CYS   A  1 209 ? -34.713 -12.115 -48.630  1.00 46.39  ? 510  CYS   A CA  1 
ATOM   1630  C  C   . CYS   A  1 209 ? -34.388 -13.442 -49.288  1.00 53.90  ? 510  CYS   A C   1 
ATOM   1631  O  O   . CYS   A  1 209 ? -34.557 -13.608 -50.503  1.00 55.33  ? 510  CYS   A O   1 
ATOM   1632  C  CB  . CYS   A  1 209 ? -33.418 -11.366 -48.328  1.00 47.57  ? 510  CYS   A CB  1 
ATOM   1633  S  SG  . CYS   A  1 209 ? -33.653 -9.650  -47.975  1.00 46.67  ? 510  CYS   A SG  1 
ATOM   1634  N  N   . ILE   A  1 210 ? -33.899 -14.392 -48.497  1.00 55.63  ? 511  ILE   A N   1 
ATOM   1635  C  CA  . ILE   A  1 210 ? -33.465 -15.666 -49.046  1.00 56.26  ? 511  ILE   A CA  1 
ATOM   1636  C  C   . ILE   A  1 210 ? -34.618 -16.362 -49.747  1.00 55.47  ? 511  ILE   A C   1 
ATOM   1637  O  O   . ILE   A  1 210 ? -34.469 -16.876 -50.863  1.00 60.07  ? 511  ILE   A O   1 
ATOM   1638  C  CB  . ILE   A  1 210 ? -32.862 -16.526 -47.925  1.00 52.74  ? 511  ILE   A CB  1 
ATOM   1639  C  CG1 . ILE   A  1 210 ? -31.545 -15.896 -47.470  1.00 44.00  ? 511  ILE   A CG1 1 
ATOM   1640  C  CG2 . ILE   A  1 210 ? -32.690 -17.948 -48.396  1.00 41.85  ? 511  ILE   A CG2 1 
ATOM   1641  C  CD1 . ILE   A  1 210 ? -31.055 -16.430 -46.133  1.00 47.54  ? 511  ILE   A CD1 1 
ATOM   1642  N  N   . GLN   A  1 211 ? -35.795 -16.356 -49.126  1.00 55.83  ? 512  GLN   A N   1 
ATOM   1643  C  CA  . GLN   A  1 211 ? -36.923 -17.068 -49.711  1.00 67.30  ? 512  GLN   A CA  1 
ATOM   1644  C  C   . GLN   A  1 211 ? -37.378 -16.409 -51.010  1.00 71.47  ? 512  GLN   A C   1 
ATOM   1645  O  O   . GLN   A  1 211 ? -37.869 -17.094 -51.915  1.00 73.32  ? 512  GLN   A O   1 
ATOM   1646  C  CB  . GLN   A  1 211 ? -38.050 -17.166 -48.681  1.00 72.49  ? 512  GLN   A CB  1 
ATOM   1647  C  CG  . GLN   A  1 211 ? -39.399 -17.579 -49.209  1.00 82.74  ? 512  GLN   A CG  1 
ATOM   1648  C  CD  . GLN   A  1 211 ? -40.486 -17.266 -48.210  1.00 93.25  ? 512  GLN   A CD  1 
ATOM   1649  O  OE1 . GLN   A  1 211 ? -40.308 -16.416 -47.338  1.00 93.40  ? 512  GLN   A OE1 1 
ATOM   1650  N  NE2 . GLN   A  1 211 ? -41.616 -17.953 -48.322  1.00 99.39  ? 512  GLN   A NE2 1 
ATOM   1651  N  N   . GLN   A  1 212 ? -37.171 -15.099 -51.143  1.00 69.33  ? 513  GLN   A N   1 
ATOM   1652  C  CA  . GLN   A  1 212 ? -37.404 -14.389 -52.394  1.00 67.89  ? 513  GLN   A CA  1 
ATOM   1653  C  C   . GLN   A  1 212 ? -36.322 -14.638 -53.439  1.00 62.24  ? 513  GLN   A C   1 
ATOM   1654  O  O   . GLN   A  1 212 ? -36.398 -14.057 -54.527  1.00 58.44  ? 513  GLN   A O   1 
ATOM   1655  C  CB  . GLN   A  1 212 ? -37.498 -12.877 -52.156  1.00 69.02  ? 513  GLN   A CB  1 
ATOM   1656  C  CG  . GLN   A  1 212 ? -38.690 -12.386 -51.359  1.00 63.81  ? 513  GLN   A CG  1 
ATOM   1657  C  CD  . GLN   A  1 212 ? -40.010 -12.946 -51.839  1.00 69.43  ? 513  GLN   A CD  1 
ATOM   1658  O  OE1 . GLN   A  1 212 ? -40.827 -13.396 -51.032  1.00 72.79  ? 513  GLN   A OE1 1 
ATOM   1659  N  NE2 . GLN   A  1 212 ? -40.237 -12.914 -53.155  1.00 66.99  ? 513  GLN   A NE2 1 
ATOM   1660  N  N   . GLY   A  1 213 ? -35.302 -15.438 -53.130  1.00 57.84  ? 514  GLY   A N   1 
ATOM   1661  C  CA  . GLY   A  1 213 ? -34.313 -15.836 -54.112  1.00 56.88  ? 514  GLY   A CA  1 
ATOM   1662  C  C   . GLY   A  1 213 ? -32.928 -15.262 -53.918  1.00 61.10  ? 514  GLY   A C   1 
ATOM   1663  O  O   . GLY   A  1 213 ? -32.049 -15.526 -54.745  1.00 63.34  ? 514  GLY   A O   1 
ATOM   1664  N  N   . TRP   A  1 214 ? -32.699 -14.486 -52.868  1.00 57.10  ? 515  TRP   A N   1 
ATOM   1665  C  CA  . TRP   A  1 214 ? -31.360 -13.993 -52.585  1.00 51.37  ? 515  TRP   A CA  1 
ATOM   1666  C  C   . TRP   A  1 214 ? -30.419 -15.144 -52.264  1.00 53.98  ? 515  TRP   A C   1 
ATOM   1667  O  O   . TRP   A  1 214 ? -30.758 -16.045 -51.494  1.00 58.07  ? 515  TRP   A O   1 
ATOM   1668  C  CB  . TRP   A  1 214 ? -31.409 -13.019 -51.415  1.00 53.63  ? 515  TRP   A CB  1 
ATOM   1669  C  CG  . TRP   A  1 214 ? -30.122 -12.333 -51.160  1.00 53.98  ? 515  TRP   A CG  1 
ATOM   1670  C  CD1 . TRP   A  1 214 ? -29.388 -11.629 -52.057  1.00 53.98  ? 515  TRP   A CD1 1 
ATOM   1671  C  CD2 . TRP   A  1 214 ? -29.417 -12.261 -49.916  1.00 52.44  ? 515  TRP   A CD2 1 
ATOM   1672  N  NE1 . TRP   A  1 214 ? -28.262 -11.126 -51.458  1.00 52.96  ? 515  TRP   A NE1 1 
ATOM   1673  C  CE2 . TRP   A  1 214 ? -28.255 -11.498 -50.142  1.00 51.92  ? 515  TRP   A CE2 1 
ATOM   1674  C  CE3 . TRP   A  1 214 ? -29.655 -12.761 -48.638  1.00 48.40  ? 515  TRP   A CE3 1 
ATOM   1675  C  CZ2 . TRP   A  1 214 ? -27.331 -11.229 -49.141  1.00 44.08  ? 515  TRP   A CZ2 1 
ATOM   1676  C  CZ3 . TRP   A  1 214 ? -28.746 -12.483 -47.649  1.00 52.95  ? 515  TRP   A CZ3 1 
ATOM   1677  C  CH2 . TRP   A  1 214 ? -27.596 -11.723 -47.904  1.00 48.93  ? 515  TRP   A CH2 1 
ATOM   1678  N  N   . LYS   A  1 215 ? -29.230 -15.109 -52.851  1.00 53.46  ? 516  LYS   A N   1 
ATOM   1679  C  CA  . LYS   A  1 215 ? -28.208 -16.107 -52.573  1.00 48.24  ? 516  LYS   A CA  1 
ATOM   1680  C  C   . LYS   A  1 215 ? -27.232 -15.518 -51.580  1.00 49.99  ? 516  LYS   A C   1 
ATOM   1681  O  O   . LYS   A  1 215 ? -26.396 -14.688 -51.962  1.00 53.00  ? 516  LYS   A O   1 
ATOM   1682  C  CB  . LYS   A  1 215 ? -27.491 -16.513 -53.859  1.00 60.75  ? 516  LYS   A CB  1 
ATOM   1683  C  CG  . LYS   A  1 215 ? -28.431 -17.072 -54.916  1.00 68.46  ? 516  LYS   A CG  1 
ATOM   1684  C  CD  . LYS   A  1 215 ? -28.928 -18.453 -54.520  1.00 71.89  ? 516  LYS   A CD  1 
ATOM   1685  C  CE  . LYS   A  1 215 ? -30.354 -18.698 -54.986  1.00 76.26  ? 516  LYS   A CE  1 
ATOM   1686  N  NZ  . LYS   A  1 215 ? -31.342 -18.090 -54.039  1.00 79.19  ? 516  LYS   A NZ  1 
ATOM   1687  N  N   . PRO   A  1 216 ? -27.283 -15.904 -50.309  1.00 60.74  ? 517  PRO   A N   1 
ATOM   1688  C  CA  . PRO   A  1 216 ? -26.528 -15.186 -49.277  1.00 50.20  ? 517  PRO   A CA  1 
ATOM   1689  C  C   . PRO   A  1 216 ? -25.103 -15.696 -49.191  1.00 52.41  ? 517  PRO   A C   1 
ATOM   1690  O  O   . PRO   A  1 216 ? -24.861 -16.905 -49.310  1.00 52.98  ? 517  PRO   A O   1 
ATOM   1691  C  CB  . PRO   A  1 216 ? -27.310 -15.513 -47.999  1.00 49.83  ? 517  PRO   A CB  1 
ATOM   1692  C  CG  . PRO   A  1 216 ? -27.782 -16.913 -48.238  1.00 55.70  ? 517  PRO   A CG  1 
ATOM   1693  C  CD  . PRO   A  1 216 ? -28.038 -17.037 -49.743  1.00 58.86  ? 517  PRO   A CD  1 
ATOM   1694  N  N   . PRO   A  1 217 ? -24.121 -14.810 -48.999  1.00 52.90  ? 518  PRO   A N   1 
ATOM   1695  C  CA  . PRO   A  1 217 ? -22.745 -15.288 -48.789  1.00 52.29  ? 518  PRO   A CA  1 
ATOM   1696  C  C   . PRO   A  1 217 ? -22.519 -15.944 -47.438  1.00 55.79  ? 518  PRO   A C   1 
ATOM   1697  O  O   . PRO   A  1 217 ? -21.452 -16.536 -47.240  1.00 57.64  ? 518  PRO   A O   1 
ATOM   1698  C  CB  . PRO   A  1 217 ? -21.891 -14.022 -48.946  1.00 47.24  ? 518  PRO   A CB  1 
ATOM   1699  C  CG  . PRO   A  1 217 ? -22.825 -12.892 -48.901  1.00 45.40  ? 518  PRO   A CG  1 
ATOM   1700  C  CD  . PRO   A  1 217 ? -24.166 -13.381 -49.339  1.00 42.48  ? 518  PRO   A CD  1 
ATOM   1701  N  N   . ARG   A  1 218 ? -23.484 -15.890 -46.522  1.00 64.65  ? 519  ARG   A N   1 
ATOM   1702  C  CA  . ARG   A  1 218 ? -23.359 -16.482 -45.187  1.00 62.48  ? 519  ARG   A CA  1 
ATOM   1703  C  C   . ARG   A  1 218 ? -22.037 -16.085 -44.524  1.00 64.41  ? 519  ARG   A C   1 
ATOM   1704  O  O   . ARG   A  1 218 ? -21.207 -16.923 -44.165  1.00 69.85  ? 519  ARG   A O   1 
ATOM   1705  C  CB  . ARG   A  1 218 ? -23.519 -18.005 -45.246  1.00 65.93  ? 519  ARG   A CB  1 
ATOM   1706  C  CG  . ARG   A  1 218 ? -24.850 -18.435 -45.834  1.00 65.72  ? 519  ARG   A CG  1 
ATOM   1707  C  CD  . ARG   A  1 218 ? -25.367 -19.755 -45.282  1.00 67.19  ? 519  ARG   A CD  1 
ATOM   1708  N  NE  . ARG   A  1 218 ? -26.812 -19.667 -45.076  1.00 75.89  ? 519  ARG   A NE  1 
ATOM   1709  C  CZ  . ARG   A  1 218 ? -27.403 -19.644 -43.883  1.00 80.01  ? 519  ARG   A CZ  1 
ATOM   1710  N  NH1 . ARG   A  1 218 ? -28.727 -19.538 -43.798  1.00 79.45  ? 519  ARG   A NH1 1 
ATOM   1711  N  NH2 . ARG   A  1 218 ? -26.672 -19.744 -42.776  1.00 79.86  ? 519  ARG   A NH2 1 
ATOM   1712  N  N   . GLY   A  1 219 ? -21.851 -14.772 -44.388  1.00 65.00  ? 520  GLY   A N   1 
ATOM   1713  C  CA  . GLY   A  1 219 ? -20.713 -14.208 -43.688  1.00 64.39  ? 520  GLY   A CA  1 
ATOM   1714  C  C   . GLY   A  1 219 ? -21.165 -13.327 -42.545  1.00 62.17  ? 520  GLY   A C   1 
ATOM   1715  O  O   . GLY   A  1 219 ? -22.358 -13.272 -42.241  1.00 62.57  ? 520  GLY   A O   1 
ATOM   1716  N  N   . ARG   A  1 220 ? -20.234 -12.617 -41.910  1.00 60.76  ? 521  ARG   A N   1 
ATOM   1717  C  CA  . ARG   A  1 220 ? -20.594 -11.797 -40.769  1.00 50.39  ? 521  ARG   A CA  1 
ATOM   1718  C  C   . ARG   A  1 220 ? -21.070 -10.404 -41.155  1.00 50.78  ? 521  ARG   A C   1 
ATOM   1719  O  O   . ARG   A  1 220 ? -21.782 -9.775  -40.366  1.00 57.76  ? 521  ARG   A O   1 
ATOM   1720  C  CB  . ARG   A  1 220 ? -19.409 -11.673 -39.810  1.00 56.07  ? 521  ARG   A CB  1 
ATOM   1721  C  CG  . ARG   A  1 220 ? -19.821 -11.314 -38.374  1.00 60.91  ? 521  ARG   A CG  1 
ATOM   1722  C  CD  . ARG   A  1 220 ? -18.603 -11.118 -37.504  1.00 64.99  ? 521  ARG   A CD  1 
ATOM   1723  N  NE  . ARG   A  1 220 ? -18.932 -10.845 -36.110  1.00 65.39  ? 521  ARG   A NE  1 
ATOM   1724  C  CZ  . ARG   A  1 220 ? -18.042 -10.491 -35.181  1.00 67.06  ? 521  ARG   A CZ  1 
ATOM   1725  N  NH1 . ARG   A  1 220 ? -16.757 -10.361 -35.500  1.00 63.09  ? 521  ARG   A NH1 1 
ATOM   1726  N  NH2 . ARG   A  1 220 ? -18.441 -10.259 -33.929  1.00 63.05  ? 521  ARG   A NH2 1 
ATOM   1727  N  N   . PHE   A  1 221 ? -20.689 -9.900  -42.324  1.00 48.62  ? 522  PHE   A N   1 
ATOM   1728  C  CA  . PHE   A  1 221 ? -20.993 -8.525  -42.712  1.00 49.92  ? 522  PHE   A CA  1 
ATOM   1729  C  C   . PHE   A  1 221 ? -21.458 -8.478  -44.168  1.00 46.82  ? 522  PHE   A C   1 
ATOM   1730  O  O   . PHE   A  1 221 ? -20.967 -7.699  -44.981  1.00 43.90  ? 522  PHE   A O   1 
ATOM   1731  C  CB  . PHE   A  1 221 ? -19.788 -7.611  -42.476  1.00 51.63  ? 522  PHE   A CB  1 
ATOM   1732  C  CG  . PHE   A  1 221 ? -19.390 -7.499  -41.025  1.00 55.31  ? 522  PHE   A CG  1 
ATOM   1733  C  CD1 . PHE   A  1 221 ? -20.218 -6.865  -40.114  1.00 50.94  ? 522  PHE   A CD1 1 
ATOM   1734  C  CD2 . PHE   A  1 221 ? -18.191 -8.039  -40.568  1.00 57.74  ? 522  PHE   A CD2 1 
ATOM   1735  C  CE1 . PHE   A  1 221 ? -19.862 -6.765  -38.769  1.00 54.33  ? 522  PHE   A CE1 1 
ATOM   1736  C  CE2 . PHE   A  1 221 ? -17.826 -7.941  -39.218  1.00 58.14  ? 522  PHE   A CE2 1 
ATOM   1737  C  CZ  . PHE   A  1 221 ? -18.667 -7.304  -38.322  1.00 55.94  ? 522  PHE   A CZ  1 
ATOM   1738  N  N   . ASP   A  1 222 ? -22.435 -9.315  -44.500  1.00 44.81  ? 523  ASP   A N   1 
ATOM   1739  C  CA  . ASP   A  1 222 ? -23.047 -9.320  -45.820  1.00 42.89  ? 523  ASP   A CA  1 
ATOM   1740  C  C   . ASP   A  1 222 ? -24.024 -8.154  -45.919  1.00 48.16  ? 523  ASP   A C   1 
ATOM   1741  O  O   . ASP   A  1 222 ? -25.039 -8.129  -45.215  1.00 49.31  ? 523  ASP   A O   1 
ATOM   1742  C  CB  . ASP   A  1 222 ? -23.756 -10.649 -46.067  1.00 41.90  ? 523  ASP   A CB  1 
ATOM   1743  C  CG  . ASP   A  1 222 ? -22.858 -11.841 -45.818  1.00 46.78  ? 523  ASP   A CG  1 
ATOM   1744  O  OD1 . ASP   A  1 222 ? -21.623 -11.666 -45.743  1.00 54.84  ? 523  ASP   A OD1 1 
ATOM   1745  O  OD2 . ASP   A  1 222 ? -23.389 -12.959 -45.706  1.00 49.09  ? 523  ASP   A OD2 1 
ATOM   1746  N  N   . VAL   A  1 223 ? -23.725 -7.178  -46.784  1.00 43.24  ? 524  VAL   A N   1 
ATOM   1747  C  CA  . VAL   A  1 223 ? -24.681 -6.101  -47.027  1.00 40.24  ? 524  VAL   A CA  1 
ATOM   1748  C  C   . VAL   A  1 223 ? -25.959 -6.712  -47.581  1.00 40.59  ? 524  VAL   A C   1 
ATOM   1749  O  O   . VAL   A  1 223 ? -25.917 -7.563  -48.474  1.00 36.02  ? 524  VAL   A O   1 
ATOM   1750  C  CB  . VAL   A  1 223 ? -24.085 -5.063  -47.987  1.00 39.17  ? 524  VAL   A CB  1 
ATOM   1751  C  CG1 . VAL   A  1 223 ? -25.111 -3.996  -48.317  1.00 37.79  ? 524  VAL   A CG1 1 
ATOM   1752  C  CG2 . VAL   A  1 223 ? -22.815 -4.463  -47.393  1.00 32.80  ? 524  VAL   A CG2 1 
ATOM   1753  N  N   . LEU   A  1 224 ? -27.095 -6.330  -47.031  1.00 40.82  ? 525  LEU   A N   1 
ATOM   1754  C  CA  . LEU   A  1 224 ? -28.303 -7.007  -47.466  1.00 43.75  ? 525  LEU   A CA  1 
ATOM   1755  C  C   . LEU   A  1 224 ? -28.762 -6.458  -48.819  1.00 44.14  ? 525  LEU   A C   1 
ATOM   1756  O  O   . LEU   A  1 224 ? -28.337 -5.381  -49.237  1.00 37.86  ? 525  LEU   A O   1 
ATOM   1757  C  CB  . LEU   A  1 224 ? -29.394 -6.856  -46.415  1.00 45.40  ? 525  LEU   A CB  1 
ATOM   1758  C  CG  . LEU   A  1 224 ? -29.359 -7.827  -45.220  1.00 42.31  ? 525  LEU   A CG  1 
ATOM   1759  C  CD1 . LEU   A  1 224 ? -30.017 -7.189  -44.040  1.00 42.65  ? 525  LEU   A CD1 1 
ATOM   1760  C  CD2 . LEU   A  1 224 ? -30.039 -9.165  -45.543  1.00 42.65  ? 525  LEU   A CD2 1 
ATOM   1761  N  N   . PRO   A  1 225 ? -29.605 -7.192  -49.541  1.00 43.28  ? 526  PRO   A N   1 
ATOM   1762  C  CA  . PRO   A  1 225 ? -30.177 -6.636  -50.770  1.00 41.78  ? 526  PRO   A CA  1 
ATOM   1763  C  C   . PRO   A  1 225 ? -31.361 -5.749  -50.453  1.00 37.15  ? 526  PRO   A C   1 
ATOM   1764  O  O   . PRO   A  1 225 ? -32.058 -5.932  -49.453  1.00 44.14  ? 526  PRO   A O   1 
ATOM   1765  C  CB  . PRO   A  1 225 ? -30.619 -7.880  -51.550  1.00 37.10  ? 526  PRO   A CB  1 
ATOM   1766  C  CG  . PRO   A  1 225 ? -30.957 -8.866  -50.469  1.00 38.44  ? 526  PRO   A CG  1 
ATOM   1767  C  CD  . PRO   A  1 225 ? -29.926 -8.625  -49.393  1.00 39.68  ? 526  PRO   A CD  1 
ATOM   1768  N  N   . LEU   A  1 226 ? -31.582 -4.765  -51.313  1.00 31.06  ? 527  LEU   A N   1 
ATOM   1769  C  CA  . LEU   A  1 226 ? -32.814 -3.999  -51.224  1.00 35.59  ? 527  LEU   A CA  1 
ATOM   1770  C  C   . LEU   A  1 226 ? -33.997 -4.875  -51.618  1.00 44.96  ? 527  LEU   A C   1 
ATOM   1771  O  O   . LEU   A  1 226 ? -33.884 -5.755  -52.478  1.00 47.37  ? 527  LEU   A O   1 
ATOM   1772  C  CB  . LEU   A  1 226 ? -32.737 -2.765  -52.114  1.00 37.82  ? 527  LEU   A CB  1 
ATOM   1773  C  CG  . LEU   A  1 226 ? -31.765 -1.700  -51.602  1.00 45.53  ? 527  LEU   A CG  1 
ATOM   1774  C  CD1 . LEU   A  1 226 ? -31.616 -0.538  -52.574  1.00 46.05  ? 527  LEU   A CD1 1 
ATOM   1775  C  CD2 . LEU   A  1 226 ? -32.238 -1.192  -50.260  1.00 39.52  ? 527  LEU   A CD2 1 
ATOM   1776  N  N   . LEU   A  1 227 ? -35.123 -4.654  -50.945  1.00 47.42  ? 528  LEU   A N   1 
ATOM   1777  C  CA  . LEU   A  1 227 ? -36.385 -5.343  -51.190  1.00 43.95  ? 528  LEU   A CA  1 
ATOM   1778  C  C   . LEU   A  1 227 ? -37.417 -4.247  -51.379  1.00 45.68  ? 528  LEU   A C   1 
ATOM   1779  O  O   . LEU   A  1 227 ? -37.817 -3.593  -50.407  1.00 44.31  ? 528  LEU   A O   1 
ATOM   1780  C  CB  . LEU   A  1 227 ? -36.777 -6.249  -50.020  1.00 45.30  ? 528  LEU   A CB  1 
ATOM   1781  C  CG  . LEU   A  1 227 ? -37.213 -7.682  -50.313  1.00 43.90  ? 528  LEU   A CG  1 
ATOM   1782  C  CD1 . LEU   A  1 227 ? -38.162 -8.171  -49.243  1.00 36.56  ? 528  LEU   A CD1 1 
ATOM   1783  C  CD2 . LEU   A  1 227 ? -37.806 -7.825  -51.732  1.00 47.38  ? 528  LEU   A CD2 1 
ATOM   1784  N  N   . LEU   A  1 228 ? -37.849 -4.044  -52.612  1.00 36.82  ? 529  LEU   A N   1 
ATOM   1785  C  CA  . LEU   A  1 228 ? -38.543 -2.818  -52.971  1.00 40.20  ? 529  LEU   A CA  1 
ATOM   1786  C  C   . LEU   A  1 228 ? -39.929 -3.133  -53.512  1.00 42.26  ? 529  LEU   A C   1 
ATOM   1787  O  O   . LEU   A  1 228 ? -40.092 -4.014  -54.372  1.00 32.92  ? 529  LEU   A O   1 
ATOM   1788  C  CB  . LEU   A  1 228 ? -37.736 -2.017  -53.990  1.00 35.81  ? 529  LEU   A CB  1 
ATOM   1789  C  CG  . LEU   A  1 228 ? -36.355 -1.644  -53.462  1.00 31.76  ? 529  LEU   A CG  1 
ATOM   1790  C  CD1 . LEU   A  1 228 ? -35.568 -0.881  -54.527  1.00 34.42  ? 529  LEU   A CD1 1 
ATOM   1791  C  CD2 . LEU   A  1 228 ? -36.501 -0.796  -52.206  1.00 32.34  ? 529  LEU   A CD2 1 
ATOM   1792  N  N   . GLN   A  1 229 ? -40.918 -2.397  -53.011  1.00 36.67  ? 530  GLN   A N   1 
ATOM   1793  C  CA  . GLN   A  1 229 ? -42.314 -2.596  -53.369  1.00 44.31  ? 530  GLN   A CA  1 
ATOM   1794  C  C   . GLN   A  1 229 ? -42.869 -1.297  -53.926  1.00 41.45  ? 530  GLN   A C   1 
ATOM   1795  O  O   . GLN   A  1 229 ? -42.837 -0.262  -53.251  1.00 34.14  ? 530  GLN   A O   1 
ATOM   1796  C  CB  . GLN   A  1 229 ? -43.126 -3.047  -52.153  1.00 40.80  ? 530  GLN   A CB  1 
ATOM   1797  C  CG  . GLN   A  1 229 ? -44.612 -2.802  -52.290  1.00 39.33  ? 530  GLN   A CG  1 
ATOM   1798  C  CD  . GLN   A  1 229 ? -45.388 -3.375  -51.128  1.00 49.85  ? 530  GLN   A CD  1 
ATOM   1799  O  OE1 . GLN   A  1 229 ? -44.955 -3.295  -49.977  1.00 51.39  ? 530  GLN   A OE1 1 
ATOM   1800  N  NE2 . GLN   A  1 229 ? -46.534 -3.974  -51.423  1.00 51.70  ? 530  GLN   A NE2 1 
ATOM   1801  N  N   . ALA   A  1 230 ? -43.395 -1.358  -55.144  1.00 39.18  ? 531  ALA   A N   1 
ATOM   1802  C  CA  . ALA   A  1 230 ? -43.990 -0.205  -55.804  1.00 43.87  ? 531  ALA   A CA  1 
ATOM   1803  C  C   . ALA   A  1 230 ? -45.444 -0.507  -56.125  1.00 46.01  ? 531  ALA   A C   1 
ATOM   1804  O  O   . ALA   A  1 230 ? -45.747 -1.558  -56.703  1.00 43.09  ? 531  ALA   A O   1 
ATOM   1805  C  CB  . ALA   A  1 230 ? -43.230 0.154   -57.086  1.00 49.28  ? 531  ALA   A CB  1 
ATOM   1806  N  N   . ASN   A  1 231 ? -46.337 0.407   -55.729  1.00 47.90  ? 532  ASN   A N   1 
ATOM   1807  C  CA  . ASN   A  1 231 ? -47.745 0.385   -56.142  1.00 50.95  ? 532  ASN   A CA  1 
ATOM   1808  C  C   . ASN   A  1 231 ? -48.491 -0.844  -55.621  1.00 49.53  ? 532  ASN   A C   1 
ATOM   1809  O  O   . ASN   A  1 231 ? -49.455 -1.303  -56.234  1.00 52.14  ? 532  ASN   A O   1 
ATOM   1810  C  CB  . ASN   A  1 231 ? -47.867 0.475   -57.666  1.00 54.88  ? 532  ASN   A CB  1 
ATOM   1811  C  CG  . ASN   A  1 231 ? -48.996 1.376   -58.111  1.00 63.16  ? 532  ASN   A CG  1 
ATOM   1812  O  OD1 . ASN   A  1 231 ? -48.881 2.603   -58.072  1.00 66.89  ? 532  ASN   A OD1 1 
ATOM   1813  N  ND2 . ASN   A  1 231 ? -50.089 0.774   -58.562  1.00 69.63  ? 532  ASN   A ND2 1 
ATOM   1814  N  N   . GLY   A  1 232 ? -48.079 -1.374  -54.473  1.00 51.14  ? 533  GLY   A N   1 
ATOM   1815  C  CA  . GLY   A  1 232 ? -48.758 -2.513  -53.891  1.00 44.44  ? 533  GLY   A CA  1 
ATOM   1816  C  C   . GLY   A  1 232 ? -48.412 -3.846  -54.510  1.00 45.82  ? 533  GLY   A C   1 
ATOM   1817  O  O   . GLY   A  1 232 ? -48.982 -4.866  -54.103  1.00 48.34  ? 533  GLY   A O   1 
ATOM   1818  N  N   . ASN   A  1 233 ? -47.514 -3.877  -55.492  1.00 45.69  ? 534  ASN   A N   1 
ATOM   1819  C  CA  . ASN   A  1 233 ? -47.103 -5.147  -56.058  1.00 43.26  ? 534  ASN   A CA  1 
ATOM   1820  C  C   . ASN   A  1 233 ? -46.169 -5.880  -55.099  1.00 47.71  ? 534  ASN   A C   1 
ATOM   1821  O  O   . ASN   A  1 233 ? -45.753 -5.354  -54.058  1.00 39.09  ? 534  ASN   A O   1 
ATOM   1822  C  CB  . ASN   A  1 233 ? -46.453 -4.927  -57.414  1.00 46.79  ? 534  ASN   A CB  1 
ATOM   1823  C  CG  . ASN   A  1 233 ? -47.450 -4.405  -58.435  1.00 47.75  ? 534  ASN   A CG  1 
ATOM   1824  O  OD1 . ASN   A  1 233 ? -48.579 -4.884  -58.505  1.00 48.54  ? 534  ASN   A OD1 1 
ATOM   1825  N  ND2 . ASN   A  1 233 ? -47.061 -3.387  -59.181  1.00 45.58  ? 534  ASN   A ND2 1 
ATOM   1826  N  N   . ASP   A  1 234 ? -45.873 -7.133  -55.441  1.00 48.82  ? 535  ASP   A N   1 
ATOM   1827  C  CA  . ASP   A  1 234 ? -44.939 -7.900  -54.641  1.00 52.39  ? 535  ASP   A CA  1 
ATOM   1828  C  C   . ASP   A  1 234 ? -43.589 -7.192  -54.663  1.00 48.37  ? 535  ASP   A C   1 
ATOM   1829  O  O   . ASP   A  1 234 ? -43.248 -6.536  -55.643  1.00 54.86  ? 535  ASP   A O   1 
ATOM   1830  C  CB  . ASP   A  1 234 ? -44.808 -9.328  -55.176  1.00 56.87  ? 535  ASP   A CB  1 
ATOM   1831  C  CG  . ASP   A  1 234 ? -46.087 -10.146 -55.010  1.00 50.30  ? 535  ASP   A CG  1 
ATOM   1832  O  OD1 . ASP   A  1 234 ? -46.930 -9.784  -54.166  1.00 49.49  ? 535  ASP   A OD1 1 
ATOM   1833  O  OD2 . ASP   A  1 234 ? -46.246 -11.158 -55.721  1.00 55.44  ? 535  ASP   A OD2 1 
ATOM   1834  N  N   . PRO   A  1 235 ? -42.832 -7.243  -53.581  1.00 51.38  ? 536  PRO   A N   1 
ATOM   1835  C  CA  . PRO   A  1 235 ? -41.530 -6.576  -53.576  1.00 45.11  ? 536  PRO   A CA  1 
ATOM   1836  C  C   . PRO   A  1 235 ? -40.516 -7.363  -54.393  1.00 40.33  ? 536  PRO   A C   1 
ATOM   1837  O  O   . PRO   A  1 235 ? -40.668 -8.560  -54.631  1.00 38.60  ? 536  PRO   A O   1 
ATOM   1838  C  CB  . PRO   A  1 235 ? -41.152 -6.549  -52.091  1.00 46.78  ? 536  PRO   A CB  1 
ATOM   1839  C  CG  . PRO   A  1 235 ? -41.844 -7.740  -51.529  1.00 45.11  ? 536  PRO   A CG  1 
ATOM   1840  C  CD  . PRO   A  1 235 ? -43.159 -7.829  -52.270  1.00 48.69  ? 536  PRO   A CD  1 
ATOM   1841  N  N   . GLU   A  1 236 ? -39.460 -6.666  -54.823  1.00 41.44  ? 537  GLU   A N   1 
ATOM   1842  C  CA  . GLU   A  1 236 ? -38.454 -7.257  -55.695  1.00 33.96  ? 537  GLU   A CA  1 
ATOM   1843  C  C   . GLU   A  1 236 ? -37.050 -7.025  -55.141  1.00 32.72  ? 537  GLU   A C   1 
ATOM   1844  O  O   . GLU   A  1 236 ? -36.780 -6.005  -54.501  1.00 38.46  ? 537  GLU   A O   1 
ATOM   1845  C  CB  . GLU   A  1 236 ? -38.584 -6.671  -57.131  1.00 37.70  ? 537  GLU   A CB  1 
ATOM   1846  C  CG  . GLU   A  1 236 ? -39.961 -6.896  -57.773  1.00 40.38  ? 537  GLU   A CG  1 
ATOM   1847  C  CD  . GLU   A  1 236 ? -40.217 -5.981  -58.976  1.00 49.23  ? 537  GLU   A CD  1 
ATOM   1848  O  OE1 . GLU   A  1 236 ? -39.261 -5.641  -59.704  1.00 53.71  ? 537  GLU   A OE1 1 
ATOM   1849  O  OE2 . GLU   A  1 236 ? -41.378 -5.573  -59.179  1.00 52.21  ? 537  GLU   A OE2 1 
ATOM   1850  N  N   . LEU   A  1 237 ? -36.148 -7.974  -55.408  1.00 36.48  ? 538  LEU   A N   1 
ATOM   1851  C  CA  . LEU   A  1 237 ? -34.774 -7.900  -54.924  1.00 37.29  ? 538  LEU   A CA  1 
ATOM   1852  C  C   . LEU   A  1 237 ? -33.890 -7.111  -55.888  1.00 46.15  ? 538  LEU   A C   1 
ATOM   1853  O  O   . LEU   A  1 237 ? -34.112 -7.111  -57.102  1.00 52.60  ? 538  LEU   A O   1 
ATOM   1854  C  CB  . LEU   A  1 237 ? -34.200 -9.305  -54.714  1.00 36.94  ? 538  LEU   A CB  1 
ATOM   1855  C  CG  . LEU   A  1 237 ? -34.874 -10.156 -53.637  1.00 44.38  ? 538  LEU   A CG  1 
ATOM   1856  C  CD1 . LEU   A  1 237 ? -34.365 -11.573 -53.696  1.00 49.48  ? 538  LEU   A CD1 1 
ATOM   1857  C  CD2 . LEU   A  1 237 ? -34.665 -9.560  -52.236  1.00 38.14  ? 538  LEU   A CD2 1 
ATOM   1858  N  N   . PHE   A  1 238 ? -32.904 -6.407  -55.321  1.00 42.16  ? 539  PHE   A N   1 
ATOM   1859  C  CA  . PHE   A  1 238 ? -31.872 -5.657  -56.041  1.00 39.69  ? 539  PHE   A CA  1 
ATOM   1860  C  C   . PHE   A  1 238 ? -30.628 -5.581  -55.163  1.00 46.91  ? 539  PHE   A C   1 
ATOM   1861  O  O   . PHE   A  1 238 ? -30.732 -5.277  -53.969  1.00 38.78  ? 539  PHE   A O   1 
ATOM   1862  C  CB  . PHE   A  1 238 ? -32.280 -4.216  -56.361  1.00 32.33  ? 539  PHE   A CB  1 
ATOM   1863  C  CG  . PHE   A  1 238 ? -33.569 -4.086  -57.074  1.00 37.47  ? 539  PHE   A CG  1 
ATOM   1864  C  CD1 . PHE   A  1 238 ? -33.612 -4.136  -58.454  1.00 41.00  ? 539  PHE   A CD1 1 
ATOM   1865  C  CD2 . PHE   A  1 238 ? -34.737 -3.891  -56.369  1.00 49.11  ? 539  PHE   A CD2 1 
ATOM   1866  C  CE1 . PHE   A  1 238 ? -34.805 -4.005  -59.105  1.00 51.47  ? 539  PHE   A CE1 1 
ATOM   1867  C  CE2 . PHE   A  1 238 ? -35.934 -3.766  -57.015  1.00 52.18  ? 539  PHE   A CE2 1 
ATOM   1868  C  CZ  . PHE   A  1 238 ? -35.971 -3.817  -58.378  1.00 55.85  ? 539  PHE   A CZ  1 
ATOM   1869  N  N   . GLN   A  1 239 ? -29.457 -5.814  -55.758  1.00 43.28  ? 540  GLN   A N   1 
ATOM   1870  C  CA  . GLN   A  1 239 ? -28.190 -5.723  -55.037  1.00 47.83  ? 540  GLN   A CA  1 
ATOM   1871  C  C   . GLN   A  1 239 ? -27.617 -4.325  -55.227  1.00 47.75  ? 540  GLN   A C   1 
ATOM   1872  O  O   . GLN   A  1 239 ? -27.337 -3.925  -56.361  1.00 43.48  ? 540  GLN   A O   1 
ATOM   1873  C  CB  . GLN   A  1 239 ? -27.196 -6.775  -55.530  1.00 49.14  ? 540  GLN   A CB  1 
ATOM   1874  C  CG  . GLN   A  1 239 ? -25.769 -6.610  -54.989  1.00 59.92  ? 540  GLN   A CG  1 
ATOM   1875  C  CD  . GLN   A  1 239 ? -24.695 -6.649  -56.084  1.00 75.20  ? 540  GLN   A CD  1 
ATOM   1876  O  OE1 . GLN   A  1 239 ? -24.679 -5.812  -56.997  1.00 84.40  ? 540  GLN   A OE1 1 
ATOM   1877  N  NE2 . GLN   A  1 239 ? -23.794 -7.618  -55.991  1.00 73.11  ? 540  GLN   A NE2 1 
ATOM   1878  N  N   . ILE   A  1 240 ? -27.478 -3.576  -54.133  1.00 42.99  ? 541  ILE   A N   1 
ATOM   1879  C  CA  . ILE   A  1 240 ? -26.825 -2.262  -54.227  1.00 44.67  ? 541  ILE   A CA  1 
ATOM   1880  C  C   . ILE   A  1 240 ? -25.417 -2.455  -54.771  1.00 44.75  ? 541  ILE   A C   1 
ATOM   1881  O  O   . ILE   A  1 240 ? -24.710 -3.390  -54.342  1.00 44.28  ? 541  ILE   A O   1 
ATOM   1882  C  CB  . ILE   A  1 240 ? -26.782 -1.552  -52.861  1.00 39.78  ? 541  ILE   A CB  1 
ATOM   1883  C  CG1 . ILE   A  1 240 ? -28.176 -1.405  -52.255  1.00 40.39  ? 541  ILE   A CG1 1 
ATOM   1884  C  CG2 . ILE   A  1 240 ? -26.149 -0.194  -53.006  1.00 34.30  ? 541  ILE   A CG2 1 
ATOM   1885  C  CD1 . ILE   A  1 240 ? -28.177 -0.926  -50.798  1.00 36.85  ? 541  ILE   A CD1 1 
ATOM   1886  N  N   . PRO   A  1 241 ? -24.960 -1.637  -55.714  1.00 44.09  ? 542  PRO   A N   1 
ATOM   1887  C  CA  . PRO   A  1 241 ? -23.600 -1.792  -56.243  1.00 44.32  ? 542  PRO   A CA  1 
ATOM   1888  C  C   . PRO   A  1 241 ? -22.568 -1.578  -55.149  1.00 38.79  ? 542  PRO   A C   1 
ATOM   1889  O  O   . PRO   A  1 241 ? -22.596 -0.553  -54.446  1.00 33.92  ? 542  PRO   A O   1 
ATOM   1890  C  CB  . PRO   A  1 241 ? -23.516 -0.700  -57.322  1.00 37.50  ? 542  PRO   A CB  1 
ATOM   1891  C  CG  . PRO   A  1 241 ? -24.941 -0.499  -57.745  1.00 38.41  ? 542  PRO   A CG  1 
ATOM   1892  C  CD  . PRO   A  1 241 ? -25.721 -0.622  -56.453  1.00 39.67  ? 542  PRO   A CD  1 
ATOM   1893  N  N   . PRO   A  1 242 ? -21.645 -2.531  -54.983  1.00 34.69  ? 543  PRO   A N   1 
ATOM   1894  C  CA  . PRO   A  1 242 ? -20.748 -2.507  -53.818  1.00 43.13  ? 543  PRO   A CA  1 
ATOM   1895  C  C   . PRO   A  1 242 ? -19.925 -1.246  -53.711  1.00 48.98  ? 543  PRO   A C   1 
ATOM   1896  O  O   . PRO   A  1 242 ? -19.617 -0.800  -52.592  1.00 47.60  ? 543  PRO   A O   1 
ATOM   1897  C  CB  . PRO   A  1 242 ? -19.863 -3.740  -54.045  1.00 39.63  ? 543  PRO   A CB  1 
ATOM   1898  C  CG  . PRO   A  1 242 ? -20.721 -4.661  -54.811  1.00 41.84  ? 543  PRO   A CG  1 
ATOM   1899  C  CD  . PRO   A  1 242 ? -21.520 -3.785  -55.744  1.00 41.64  ? 543  PRO   A CD  1 
ATOM   1900  N  N   . GLU   A  1 243 ? -19.561 -0.657  -54.849  1.00 34.22  ? 544  GLU   A N   1 
ATOM   1901  C  CA  . GLU   A  1 243 ? -18.814 0.592   -54.853  1.00 35.18  ? 544  GLU   A CA  1 
ATOM   1902  C  C   . GLU   A  1 243 ? -19.620 1.756   -54.294  1.00 36.46  ? 544  GLU   A C   1 
ATOM   1903  O  O   . GLU   A  1 243 ? -19.045 2.823   -54.063  1.00 41.20  ? 544  GLU   A O   1 
ATOM   1904  C  CB  . GLU   A  1 243 ? -18.345 0.926   -56.283  1.00 41.04  ? 544  GLU   A CB  1 
ATOM   1905  C  CG  . GLU   A  1 243 ? -19.470 1.228   -57.250  1.00 33.12  ? 544  GLU   A CG  1 
ATOM   1906  C  CD  . GLU   A  1 243 ? -19.991 -0.009  -57.976  1.00 41.92  ? 544  GLU   A CD  1 
ATOM   1907  O  OE1 . GLU   A  1 243 ? -19.669 -1.136  -57.555  1.00 43.63  ? 544  GLU   A OE1 1 
ATOM   1908  O  OE2 . GLU   A  1 243 ? -20.706 0.146   -58.995  1.00 54.30  ? 544  GLU   A OE2 1 
ATOM   1909  N  N   . LEU   A  1 244 ? -20.926 1.597   -54.095  1.00 34.92  ? 545  LEU   A N   1 
ATOM   1910  C  CA  . LEU   A  1 244 ? -21.736 2.645   -53.481  1.00 32.30  ? 545  LEU   A CA  1 
ATOM   1911  C  C   . LEU   A  1 244 ? -21.883 2.492   -51.956  1.00 31.17  ? 545  LEU   A C   1 
ATOM   1912  O  O   . LEU   A  1 244 ? -22.424 3.402   -51.317  1.00 34.67  ? 545  LEU   A O   1 
ATOM   1913  C  CB  . LEU   A  1 244 ? -23.142 2.688   -54.121  1.00 28.40  ? 545  LEU   A CB  1 
ATOM   1914  C  CG  . LEU   A  1 244 ? -23.408 3.122   -55.576  1.00 38.58  ? 545  LEU   A CG  1 
ATOM   1915  C  CD1 . LEU   A  1 244 ? -24.906 3.220   -55.794  1.00 28.13  ? 545  LEU   A CD1 1 
ATOM   1916  C  CD2 . LEU   A  1 244 ? -22.743 4.433   -55.945  1.00 31.77  ? 545  LEU   A CD2 1 
ATOM   1917  N  N   . VAL   A  1 245 ? -21.422 1.388   -51.361  1.00 28.83  ? 546  VAL   A N   1 
ATOM   1918  C  CA  . VAL   A  1 245 ? -21.569 1.133   -49.926  1.00 40.76  ? 546  VAL   A CA  1 
ATOM   1919  C  C   . VAL   A  1 245 ? -20.227 1.427   -49.263  1.00 45.14  ? 546  VAL   A C   1 
ATOM   1920  O  O   . VAL   A  1 245 ? -19.282 0.639   -49.359  1.00 42.56  ? 546  VAL   A O   1 
ATOM   1921  C  CB  . VAL   A  1 245 ? -22.019 -0.302  -49.644  1.00 42.04  ? 546  VAL   A CB  1 
ATOM   1922  C  CG1 . VAL   A  1 245 ? -22.182 -0.526  -48.122  1.00 41.52  ? 546  VAL   A CG1 1 
ATOM   1923  C  CG2 . VAL   A  1 245 ? -23.314 -0.620  -50.387  1.00 38.27  ? 546  VAL   A CG2 1 
ATOM   1924  N  N   . LEU   A  1 246 ? -20.126 2.557   -48.579  1.00 28.48  ? 547  LEU   A N   1 
ATOM   1925  C  CA  . LEU   A  1 246 ? -18.863 2.902   -47.952  1.00 34.56  ? 547  LEU   A CA  1 
ATOM   1926  C  C   . LEU   A  1 246 ? -18.799 2.251   -46.574  1.00 37.50  ? 547  LEU   A C   1 
ATOM   1927  O  O   . LEU   A  1 246 ? -19.781 2.276   -45.823  1.00 43.18  ? 547  LEU   A O   1 
ATOM   1928  C  CB  . LEU   A  1 246 ? -18.712 4.421   -47.860  1.00 33.52  ? 547  LEU   A CB  1 
ATOM   1929  C  CG  . LEU   A  1 246 ? -17.529 4.990   -47.082  1.00 34.95  ? 547  LEU   A CG  1 
ATOM   1930  C  CD1 . LEU   A  1 246 ? -16.233 4.416   -47.578  1.00 38.48  ? 547  LEU   A CD1 1 
ATOM   1931  C  CD2 . LEU   A  1 246 ? -17.512 6.494   -47.225  1.00 41.94  ? 547  LEU   A CD2 1 
ATOM   1932  N  N   . GLU   A  1 247 ? -17.660 1.635   -46.257  1.00 35.49  ? 548  GLU   A N   1 
ATOM   1933  C  CA  . GLU   A  1 247 ? -17.501 0.897   -45.009  1.00 40.35  ? 548  GLU   A CA  1 
ATOM   1934  C  C   . GLU   A  1 247 ? -16.185 1.258   -44.329  1.00 44.52  ? 548  GLU   A C   1 
ATOM   1935  O  O   . GLU   A  1 247 ? -15.183 1.570   -44.984  1.00 40.76  ? 548  GLU   A O   1 
ATOM   1936  C  CB  . GLU   A  1 247 ? -17.557 -0.625  -45.228  1.00 42.74  ? 548  GLU   A CB  1 
ATOM   1937  C  CG  . GLU   A  1 247 ? -18.871 -1.158  -45.746  1.00 41.48  ? 548  GLU   A CG  1 
ATOM   1938  C  CD  . GLU   A  1 247 ? -18.855 -2.651  -45.934  1.00 44.04  ? 548  GLU   A CD  1 
ATOM   1939  O  OE1 . GLU   A  1 247 ? -17.863 -3.175  -46.472  1.00 47.73  ? 548  GLU   A OE1 1 
ATOM   1940  O  OE2 . GLU   A  1 247 ? -19.821 -3.316  -45.510  1.00 52.44  ? 548  GLU   A OE2 1 
ATOM   1941  N  N   . VAL   A  1 248 ? -16.196 1.178   -43.000  1.00 37.50  ? 549  VAL   A N   1 
ATOM   1942  C  CA  . VAL   A  1 248 ? -15.071 1.579   -42.167  1.00 37.01  ? 549  VAL   A CA  1 
ATOM   1943  C  C   . VAL   A  1 248 ? -14.589 0.373   -41.372  1.00 44.51  ? 549  VAL   A C   1 
ATOM   1944  O  O   . VAL   A  1 248 ? -15.306 -0.111  -40.483  1.00 40.64  ? 549  VAL   A O   1 
ATOM   1945  C  CB  . VAL   A  1 248 ? -15.456 2.713   -41.197  1.00 37.41  ? 549  VAL   A CB  1 
ATOM   1946  C  CG1 . VAL   A  1 248 ? -14.262 3.098   -40.325  1.00 38.38  ? 549  VAL   A CG1 1 
ATOM   1947  C  CG2 . VAL   A  1 248 ? -16.016 3.915   -41.928  1.00 36.40  ? 549  VAL   A CG2 1 
ATOM   1948  N  N   . PRO   A  1 249 ? -13.391 -0.130  -41.634  1.00 41.50  ? 550  PRO   A N   1 
ATOM   1949  C  CA  . PRO   A  1 249 ? -12.842 -1.181  -40.767  1.00 43.78  ? 550  PRO   A CA  1 
ATOM   1950  C  C   . PRO   A  1 249 ? -12.478 -0.590  -39.409  1.00 46.39  ? 550  PRO   A C   1 
ATOM   1951  O  O   . PRO   A  1 249 ? -11.825 0.450   -39.337  1.00 39.78  ? 550  PRO   A O   1 
ATOM   1952  C  CB  . PRO   A  1 249 ? -11.611 -1.676  -41.532  1.00 35.19  ? 550  PRO   A CB  1 
ATOM   1953  C  CG  . PRO   A  1 249 ? -11.233 -0.510  -42.446  1.00 35.53  ? 550  PRO   A CG  1 
ATOM   1954  C  CD  . PRO   A  1 249 ? -12.472 0.298   -42.705  1.00 34.22  ? 550  PRO   A CD  1 
ATOM   1955  N  N   . ILE   A  1 250 ? -12.917 -1.249  -38.330  1.00 47.05  ? 551  ILE   A N   1 
ATOM   1956  C  CA  . ILE   A  1 250 ? -12.769 -0.701  -36.973  1.00 43.10  ? 551  ILE   A CA  1 
ATOM   1957  C  C   . ILE   A  1 250 ? -11.434 -1.151  -36.388  1.00 46.22  ? 551  ILE   A C   1 
ATOM   1958  O  O   . ILE   A  1 250 ? -11.197 -2.349  -36.189  1.00 45.98  ? 551  ILE   A O   1 
ATOM   1959  C  CB  . ILE   A  1 250 ? -13.934 -1.113  -36.050  1.00 42.51  ? 551  ILE   A CB  1 
ATOM   1960  C  CG1 . ILE   A  1 250 ? -15.283 -0.747  -36.661  1.00 43.54  ? 551  ILE   A CG1 1 
ATOM   1961  C  CG2 . ILE   A  1 250 ? -13.806 -0.424  -34.690  1.00 43.48  ? 551  ILE   A CG2 1 
ATOM   1962  C  CD1 . ILE   A  1 250 ? -15.339 0.641   -37.254  1.00 44.17  ? 551  ILE   A CD1 1 
ATOM   1963  N  N   . ARG   A  1 251 ? -10.562 -0.191  -36.106  1.00 44.12  ? 552  ARG   A N   1 
ATOM   1964  C  CA  . ARG   A  1 251 ? -9.328  -0.450  -35.381  1.00 48.68  ? 552  ARG   A CA  1 
ATOM   1965  C  C   . ARG   A  1 251 ? -9.255  0.497   -34.179  1.00 43.61  ? 552  ARG   A C   1 
ATOM   1966  O  O   . ARG   A  1 251 ? -10.070 1.411   -34.031  1.00 44.56  ? 552  ARG   A O   1 
ATOM   1967  C  CB  . ARG   A  1 251 ? -8.102  -0.298  -36.294  1.00 41.75  ? 552  ARG   A CB  1 
ATOM   1968  C  CG  . ARG   A  1 251 ? -7.979  1.064   -36.971  1.00 51.33  ? 552  ARG   A CG  1 
ATOM   1969  C  CD  . ARG   A  1 251 ? -8.830  1.216   -38.259  1.00 48.32  ? 552  ARG   A CD  1 
ATOM   1970  N  NE  . ARG   A  1 251 ? -8.408  2.406   -38.985  1.00 50.95  ? 552  ARG   A NE  1 
ATOM   1971  C  CZ  . ARG   A  1 251 ? -9.008  2.911   -40.060  1.00 56.52  ? 552  ARG   A CZ  1 
ATOM   1972  N  NH1 . ARG   A  1 251 ? -8.509  3.998   -40.629  1.00 60.56  ? 552  ARG   A NH1 1 
ATOM   1973  N  NH2 . ARG   A  1 251 ? -10.094 2.345   -40.570  1.00 49.87  ? 552  ARG   A NH2 1 
ATOM   1974  N  N   . HIS   A  1 252 ? -8.270  0.271   -33.308  1.00 45.40  ? 553  HIS   A N   1 
ATOM   1975  C  CA  . HIS   A  1 252 ? -8.135  1.050   -32.079  1.00 48.48  ? 553  HIS   A CA  1 
ATOM   1976  C  C   . HIS   A  1 252 ? -6.785  1.761   -32.059  1.00 50.22  ? 553  HIS   A C   1 
ATOM   1977  O  O   . HIS   A  1 252 ? -5.766  1.163   -32.423  1.00 53.29  ? 553  HIS   A O   1 
ATOM   1978  C  CB  . HIS   A  1 252 ? -8.280  0.143   -30.832  1.00 45.33  ? 553  HIS   A CB  1 
ATOM   1979  C  CG  . HIS   A  1 252 ? -8.388  0.883   -29.533  1.00 49.49  ? 553  HIS   A CG  1 
ATOM   1980  N  ND1 . HIS   A  1 252 ? -7.296  1.429   -28.894  1.00 53.16  ? 553  HIS   A ND1 1 
ATOM   1981  C  CD2 . HIS   A  1 252 ? -9.454  1.138   -28.737  1.00 50.56  ? 553  HIS   A CD2 1 
ATOM   1982  C  CE1 . HIS   A  1 252 ? -7.687  2.001   -27.769  1.00 53.30  ? 553  HIS   A CE1 1 
ATOM   1983  N  NE2 . HIS   A  1 252 ? -8.993  1.842   -27.652  1.00 49.94  ? 553  HIS   A NE2 1 
ATOM   1984  N  N   . PRO   A  1 253 ? -6.744  3.033   -31.652  1.00 52.55  ? 554  PRO   A N   1 
ATOM   1985  C  CA  . PRO   A  1 253 ? -5.489  3.799   -31.760  1.00 50.74  ? 554  PRO   A CA  1 
ATOM   1986  C  C   . PRO   A  1 253 ? -4.380  3.301   -30.856  1.00 55.17  ? 554  PRO   A C   1 
ATOM   1987  O  O   . PRO   A  1 253 ? -3.207  3.576   -31.141  1.00 61.40  ? 554  PRO   A O   1 
ATOM   1988  C  CB  . PRO   A  1 253 ? -5.919  5.215   -31.364  1.00 52.60  ? 554  PRO   A CB  1 
ATOM   1989  C  CG  . PRO   A  1 253 ? -7.033  4.969   -30.370  1.00 57.01  ? 554  PRO   A CG  1 
ATOM   1990  C  CD  . PRO   A  1 253 ? -7.803  3.814   -30.986  1.00 60.06  ? 554  PRO   A CD  1 
ATOM   1991  N  N   . LYS   A  1 254 ? -4.706  2.587   -29.777  1.00 50.62  ? 555  LYS   A N   1 
ATOM   1992  C  CA  . LYS   A  1 254 ? -3.710  2.099   -28.838  1.00 48.89  ? 555  LYS   A CA  1 
ATOM   1993  C  C   . LYS   A  1 254 ? -3.650  0.580   -28.741  1.00 56.25  ? 555  LYS   A C   1 
ATOM   1994  O  O   . LYS   A  1 254 ? -2.587  0.042   -28.429  1.00 62.78  ? 555  LYS   A O   1 
ATOM   1995  C  CB  . LYS   A  1 254 ? -3.971  2.689   -27.436  1.00 67.71  ? 555  LYS   A CB  1 
ATOM   1996  C  CG  . LYS   A  1 254 ? -4.159  4.221   -27.406  1.00 74.47  ? 555  LYS   A CG  1 
ATOM   1997  C  CD  . LYS   A  1 254 ? -3.082  4.943   -26.586  1.00 82.47  ? 555  LYS   A CD  1 
ATOM   1998  C  CE  . LYS   A  1 254 ? -1.696  4.893   -27.247  1.00 88.23  ? 555  LYS   A CE  1 
ATOM   1999  N  NZ  . LYS   A  1 254 ? -1.448  5.994   -28.230  1.00 86.23  ? 555  LYS   A NZ  1 
ATOM   2000  N  N   . PHE   A  1 255 ? -4.743  -0.126  -29.015  1.00 56.92  ? 556  PHE   A N   1 
ATOM   2001  C  CA  . PHE   A  1 255 ? -4.777  -1.584  -28.911  1.00 58.53  ? 556  PHE   A CA  1 
ATOM   2002  C  C   . PHE   A  1 255 ? -4.508  -2.178  -30.289  1.00 59.91  ? 556  PHE   A C   1 
ATOM   2003  O  O   . PHE   A  1 255 ? -5.386  -2.183  -31.158  1.00 59.34  ? 556  PHE   A O   1 
ATOM   2004  C  CB  . PHE   A  1 255 ? -6.116  -2.063  -28.361  1.00 60.31  ? 556  PHE   A CB  1 
ATOM   2005  C  CG  . PHE   A  1 255 ? -6.327  -1.760  -26.908  1.00 55.01  ? 556  PHE   A CG  1 
ATOM   2006  C  CD1 . PHE   A  1 255 ? -5.261  -1.702  -26.038  1.00 58.68  ? 556  PHE   A CD1 1 
ATOM   2007  C  CD2 . PHE   A  1 255 ? -7.602  -1.544  -26.411  1.00 54.30  ? 556  PHE   A CD2 1 
ATOM   2008  C  CE1 . PHE   A  1 255 ? -5.462  -1.429  -24.697  1.00 55.77  ? 556  PHE   A CE1 1 
ATOM   2009  C  CE2 . PHE   A  1 255 ? -7.813  -1.268  -25.070  1.00 51.99  ? 556  PHE   A CE2 1 
ATOM   2010  C  CZ  . PHE   A  1 255 ? -6.740  -1.213  -24.216  1.00 50.88  ? 556  PHE   A CZ  1 
ATOM   2011  N  N   . GLU   A  1 256 ? -3.290  -2.693  -30.479  1.00 64.24  ? 557  GLU   A N   1 
ATOM   2012  C  CA  . GLU   A  1 256 ? -2.916  -3.279  -31.765  1.00 64.68  ? 557  GLU   A CA  1 
ATOM   2013  C  C   . GLU   A  1 256 ? -3.865  -4.400  -32.164  1.00 58.32  ? 557  GLU   A C   1 
ATOM   2014  O  O   . GLU   A  1 256 ? -4.197  -4.556  -33.343  1.00 57.09  ? 557  GLU   A O   1 
ATOM   2015  C  CB  . GLU   A  1 256 ? -1.484  -3.810  -31.696  1.00 74.36  ? 557  GLU   A CB  1 
ATOM   2016  C  CG  . GLU   A  1 256 ? -0.430  -2.868  -32.229  1.00 88.32  ? 557  GLU   A CG  1 
ATOM   2017  C  CD  . GLU   A  1 256 ? -0.145  -3.093  -33.707  1.00 106.37 ? 557  GLU   A CD  1 
ATOM   2018  O  OE1 . GLU   A  1 256 ? -1.100  -3.074  -34.519  1.00 109.93 ? 557  GLU   A OE1 1 
ATOM   2019  O  OE2 . GLU   A  1 256 ? 1.038   -3.303  -34.054  1.00 111.98 ? 557  GLU   A OE2 1 
ATOM   2020  N  N   . TRP   A  1 257 ? -4.312  -5.187  -31.191  1.00 57.05  ? 558  TRP   A N   1 
ATOM   2021  C  CA  . TRP   A  1 257 ? -5.084  -6.390  -31.458  1.00 58.23  ? 558  TRP   A CA  1 
ATOM   2022  C  C   . TRP   A  1 257 ? -6.495  -6.105  -31.942  1.00 56.70  ? 558  TRP   A C   1 
ATOM   2023  O  O   . TRP   A  1 257 ? -7.175  -7.037  -32.379  1.00 62.40  ? 558  TRP   A O   1 
ATOM   2024  C  CB  . TRP   A  1 257 ? -5.156  -7.243  -30.188  1.00 67.36  ? 558  TRP   A CB  1 
ATOM   2025  C  CG  . TRP   A  1 257 ? -5.483  -6.445  -28.951  1.00 67.21  ? 558  TRP   A CG  1 
ATOM   2026  C  CD1 . TRP   A  1 257 ? -4.590  -5.857  -28.097  1.00 69.53  ? 558  TRP   A CD1 1 
ATOM   2027  C  CD2 . TRP   A  1 257 ? -6.790  -6.142  -28.433  1.00 70.89  ? 558  TRP   A CD2 1 
ATOM   2028  N  NE1 . TRP   A  1 257 ? -5.259  -5.206  -27.081  1.00 71.10  ? 558  TRP   A NE1 1 
ATOM   2029  C  CE2 . TRP   A  1 257 ? -6.608  -5.364  -27.263  1.00 67.31  ? 558  TRP   A CE2 1 
ATOM   2030  C  CE3 . TRP   A  1 257 ? -8.095  -6.449  -28.843  1.00 69.30  ? 558  TRP   A CE3 1 
ATOM   2031  C  CZ2 . TRP   A  1 257 ? -7.684  -4.892  -26.495  1.00 62.33  ? 558  TRP   A CZ2 1 
ATOM   2032  C  CZ3 . TRP   A  1 257 ? -9.166  -5.969  -28.081  1.00 65.79  ? 558  TRP   A CZ3 1 
ATOM   2033  C  CH2 . TRP   A  1 257 ? -8.948  -5.208  -26.915  1.00 59.73  ? 558  TRP   A CH2 1 
ATOM   2034  N  N   . PHE   A  1 258 ? -6.961  -4.862  -31.860  1.00 54.04  ? 559  PHE   A N   1 
ATOM   2035  C  CA  . PHE   A  1 258 ? -8.384  -4.614  -32.057  1.00 51.18  ? 559  PHE   A CA  1 
ATOM   2036  C  C   . PHE   A  1 258 ? -8.801  -4.877  -33.502  1.00 57.09  ? 559  PHE   A C   1 
ATOM   2037  O  O   . PHE   A  1 258 ? -9.887  -5.417  -33.752  1.00 54.82  ? 559  PHE   A O   1 
ATOM   2038  C  CB  . PHE   A  1 258 ? -8.720  -3.190  -31.634  1.00 44.95  ? 559  PHE   A CB  1 
ATOM   2039  C  CG  . PHE   A  1 258 ? -10.167 -2.975  -31.354  1.00 49.67  ? 559  PHE   A CG  1 
ATOM   2040  C  CD1 . PHE   A  1 258 ? -11.061 -2.766  -32.393  1.00 40.06  ? 559  PHE   A CD1 1 
ATOM   2041  C  CD2 . PHE   A  1 258 ? -10.645 -2.977  -30.043  1.00 48.79  ? 559  PHE   A CD2 1 
ATOM   2042  C  CE1 . PHE   A  1 258 ? -12.398 -2.580  -32.136  1.00 41.85  ? 559  PHE   A CE1 1 
ATOM   2043  C  CE2 . PHE   A  1 258 ? -11.980 -2.786  -29.788  1.00 46.08  ? 559  PHE   A CE2 1 
ATOM   2044  C  CZ  . PHE   A  1 258 ? -12.859 -2.594  -30.834  1.00 39.98  ? 559  PHE   A CZ  1 
ATOM   2045  N  N   . LYS   A  1 259 ? -7.945  -4.518  -34.465  1.00 51.61  ? 560  LYS   A N   1 
ATOM   2046  C  CA  . LYS   A  1 259 ? -8.231  -4.814  -35.866  1.00 54.81  ? 560  LYS   A CA  1 
ATOM   2047  C  C   . LYS   A  1 259 ? -8.488  -6.303  -36.094  1.00 56.67  ? 560  LYS   A C   1 
ATOM   2048  O  O   . LYS   A  1 259 ? -9.282  -6.670  -36.970  1.00 51.97  ? 560  LYS   A O   1 
ATOM   2049  C  CB  . LYS   A  1 259 ? -7.081  -4.322  -36.750  1.00 49.23  ? 560  LYS   A CB  1 
ATOM   2050  C  CG  . LYS   A  1 259 ? -5.711  -4.852  -36.361  1.00 50.60  ? 560  LYS   A CG  1 
ATOM   2051  C  CD  . LYS   A  1 259 ? -4.688  -4.655  -37.498  1.00 64.59  ? 560  LYS   A CD  1 
ATOM   2052  C  CE  . LYS   A  1 259 ? -3.288  -5.101  -37.070  1.00 68.06  ? 560  LYS   A CE  1 
ATOM   2053  N  NZ  . LYS   A  1 259 ? -2.814  -4.345  -35.873  1.00 71.93  ? 560  LYS   A NZ  1 
ATOM   2054  N  N   . ASP   A  1 260 ? -7.853  -7.167  -35.299  1.00 58.24  ? 561  ASP   A N   1 
ATOM   2055  C  CA  . ASP   A  1 260 ? -8.033  -8.614  -35.386  1.00 61.97  ? 561  ASP   A CA  1 
ATOM   2056  C  C   . ASP   A  1 260 ? -9.423  -9.078  -34.962  1.00 61.74  ? 561  ASP   A C   1 
ATOM   2057  O  O   . ASP   A  1 260 ? -9.763  -10.246 -35.178  1.00 61.78  ? 561  ASP   A O   1 
ATOM   2058  C  CB  . ASP   A  1 260 ? -6.976  -9.322  -34.531  1.00 69.07  ? 561  ASP   A CB  1 
ATOM   2059  C  CG  . ASP   A  1 260 ? -5.565  -8.906  -34.892  1.00 81.77  ? 561  ASP   A CG  1 
ATOM   2060  O  OD1 . ASP   A  1 260 ? -5.350  -8.483  -36.050  1.00 87.02  ? 561  ASP   A OD1 1 
ATOM   2061  O  OD2 . ASP   A  1 260 ? -4.673  -8.996  -34.022  1.00 86.58  ? 561  ASP   A OD2 1 
ATOM   2062  N  N   . LEU   A  1 261 ? -10.229 -8.216  -34.345  1.00 54.63  ? 562  LEU   A N   1 
ATOM   2063  C  CA  . LEU   A  1 261 ? -11.611 -8.595  -34.109  1.00 51.17  ? 562  LEU   A CA  1 
ATOM   2064  C  C   . LEU   A  1 261 ? -12.380 -8.745  -35.418  1.00 58.23  ? 562  LEU   A C   1 
ATOM   2065  O  O   . LEU   A  1 261 ? -13.417 -9.420  -35.441  1.00 61.16  ? 562  LEU   A O   1 
ATOM   2066  C  CB  . LEU   A  1 261 ? -12.267 -7.572  -33.183  1.00 46.53  ? 562  LEU   A CB  1 
ATOM   2067  C  CG  . LEU   A  1 261 ? -11.578 -7.544  -31.808  1.00 44.11  ? 562  LEU   A CG  1 
ATOM   2068  C  CD1 . LEU   A  1 261 ? -12.167 -6.509  -30.872  1.00 42.18  ? 562  LEU   A CD1 1 
ATOM   2069  C  CD2 . LEU   A  1 261 ? -11.658 -8.916  -31.179  1.00 42.55  ? 562  LEU   A CD2 1 
ATOM   2070  N  N   . GLY   A  1 262 ? -11.876 -8.156  -36.502  1.00 52.63  ? 563  GLY   A N   1 
ATOM   2071  C  CA  . GLY   A  1 262 ? -12.489 -8.273  -37.812  1.00 59.93  ? 563  GLY   A CA  1 
ATOM   2072  C  C   . GLY   A  1 262 ? -13.716 -7.414  -38.028  1.00 63.04  ? 563  GLY   A C   1 
ATOM   2073  O  O   . GLY   A  1 262 ? -14.563 -7.751  -38.865  1.00 60.71  ? 563  GLY   A O   1 
ATOM   2074  N  N   . LEU   A  1 263 ? -13.838 -6.310  -37.303  1.00 58.71  ? 564  LEU   A N   1 
ATOM   2075  C  CA  . LEU   A  1 263 ? -15.064 -5.533  -37.292  1.00 49.26  ? 564  LEU   A CA  1 
ATOM   2076  C  C   . LEU   A  1 263 ? -14.987 -4.378  -38.284  1.00 44.31  ? 564  LEU   A C   1 
ATOM   2077  O  O   . LEU   A  1 263 ? -13.947 -3.724  -38.427  1.00 42.64  ? 564  LEU   A O   1 
ATOM   2078  C  CB  . LEU   A  1 263 ? -15.356 -4.985  -35.892  1.00 50.62  ? 564  LEU   A CB  1 
ATOM   2079  C  CG  . LEU   A  1 263 ? -15.511 -5.928  -34.689  1.00 55.97  ? 564  LEU   A CG  1 
ATOM   2080  C  CD1 . LEU   A  1 263 ? -15.481 -5.108  -33.421  1.00 45.12  ? 564  LEU   A CD1 1 
ATOM   2081  C  CD2 . LEU   A  1 263 ? -16.791 -6.750  -34.740  1.00 54.09  ? 564  LEU   A CD2 1 
ATOM   2082  N  N   . LYS   A  1 264 ? -16.108 -4.140  -38.960  1.00 46.72  ? 565  LYS   A N   1 
ATOM   2083  C  CA  . LYS   A  1 264 ? -16.330 -2.964  -39.785  1.00 48.86  ? 565  LYS   A CA  1 
ATOM   2084  C  C   . LYS   A  1 264 ? -17.766 -2.514  -39.573  1.00 41.56  ? 565  LYS   A C   1 
ATOM   2085  O  O   . LYS   A  1 264 ? -18.585 -3.247  -39.012  1.00 51.95  ? 565  LYS   A O   1 
ATOM   2086  C  CB  . LYS   A  1 264 ? -16.075 -3.247  -41.273  1.00 42.97  ? 565  LYS   A CB  1 
ATOM   2087  C  CG  . LYS   A  1 264 ? -16.996 -4.304  -41.887  1.00 46.24  ? 565  LYS   A CG  1 
ATOM   2088  C  CD  . LYS   A  1 264 ? -16.613 -4.597  -43.359  1.00 52.59  ? 565  LYS   A CD  1 
ATOM   2089  C  CE  . LYS   A  1 264 ? -16.756 -6.076  -43.736  1.00 57.88  ? 565  LYS   A CE  1 
ATOM   2090  N  NZ  . LYS   A  1 264 ? -17.582 -6.286  -44.971  1.00 60.22  ? 565  LYS   A NZ  1 
ATOM   2091  N  N   . TRP   A  1 265 ? -18.079 -1.299  -40.015  1.00 33.06  ? 566  TRP   A N   1 
ATOM   2092  C  CA  . TRP   A  1 265 ? -19.470 -0.864  -40.078  1.00 38.25  ? 566  TRP   A CA  1 
ATOM   2093  C  C   . TRP   A  1 265 ? -19.675 -0.037  -41.342  1.00 46.17  ? 566  TRP   A C   1 
ATOM   2094  O  O   . TRP   A  1 265 ? -18.715 0.421   -41.971  1.00 52.87  ? 566  TRP   A O   1 
ATOM   2095  C  CB  . TRP   A  1 265 ? -19.892 -0.062  -38.828  1.00 35.41  ? 566  TRP   A CB  1 
ATOM   2096  C  CG  . TRP   A  1 265 ? -21.373 -0.097  -38.588  1.00 34.87  ? 566  TRP   A CG  1 
ATOM   2097  C  CD1 . TRP   A  1 265 ? -22.266 0.930   -38.759  1.00 39.88  ? 566  TRP   A CD1 1 
ATOM   2098  C  CD2 . TRP   A  1 265 ? -22.141 -1.223  -38.152  1.00 33.76  ? 566  TRP   A CD2 1 
ATOM   2099  N  NE1 . TRP   A  1 265 ? -23.542 0.511   -38.443  1.00 34.92  ? 566  TRP   A NE1 1 
ATOM   2100  C  CE2 . TRP   A  1 265 ? -23.491 -0.805  -38.068  1.00 33.36  ? 566  TRP   A CE2 1 
ATOM   2101  C  CE3 . TRP   A  1 265 ? -21.815 -2.536  -37.795  1.00 36.09  ? 566  TRP   A CE3 1 
ATOM   2102  C  CZ2 . TRP   A  1 265 ? -24.509 -1.657  -37.659  1.00 30.93  ? 566  TRP   A CZ2 1 
ATOM   2103  C  CZ3 . TRP   A  1 265 ? -22.828 -3.382  -37.390  1.00 39.03  ? 566  TRP   A CZ3 1 
ATOM   2104  C  CH2 . TRP   A  1 265 ? -24.160 -2.941  -37.324  1.00 37.25  ? 566  TRP   A CH2 1 
ATOM   2105  N  N   . TYR   A  1 266 ? -20.939 0.142   -41.719  1.00 36.30  ? 567  TYR   A N   1 
ATOM   2106  C  CA  . TYR   A  1 266 ? -21.216 0.990   -42.865  1.00 33.58  ? 567  TYR   A CA  1 
ATOM   2107  C  C   . TYR   A  1 266 ? -21.258 2.458   -42.454  1.00 37.37  ? 567  TYR   A C   1 
ATOM   2108  O  O   . TYR   A  1 266 ? -21.499 2.805   -41.296  1.00 42.71  ? 567  TYR   A O   1 
ATOM   2109  C  CB  . TYR   A  1 266 ? -22.530 0.597   -43.531  1.00 39.06  ? 567  TYR   A CB  1 
ATOM   2110  C  CG  . TYR   A  1 266 ? -23.676 0.353   -42.574  1.00 41.99  ? 567  TYR   A CG  1 
ATOM   2111  C  CD1 . TYR   A  1 266 ? -23.907 -0.909  -42.037  1.00 41.20  ? 567  TYR   A CD1 1 
ATOM   2112  C  CD2 . TYR   A  1 266 ? -24.547 1.377   -42.237  1.00 37.46  ? 567  TYR   A CD2 1 
ATOM   2113  C  CE1 . TYR   A  1 266 ? -24.971 -1.138  -41.183  1.00 40.11  ? 567  TYR   A CE1 1 
ATOM   2114  C  CE2 . TYR   A  1 266 ? -25.598 1.165   -41.395  1.00 32.70  ? 567  TYR   A CE2 1 
ATOM   2115  C  CZ  . TYR   A  1 266 ? -25.812 -0.090  -40.857  1.00 40.20  ? 567  TYR   A CZ  1 
ATOM   2116  O  OH  . TYR   A  1 266 ? -26.881 -0.283  -40.006  1.00 44.86  ? 567  TYR   A OH  1 
ATOM   2117  N  N   . GLY   A  1 267 ? -21.012 3.330   -43.426  1.00 37.76  ? 568  GLY   A N   1 
ATOM   2118  C  CA  . GLY   A  1 267 ? -20.866 4.731   -43.118  1.00 31.94  ? 568  GLY   A CA  1 
ATOM   2119  C  C   . GLY   A  1 267 ? -22.165 5.504   -43.074  1.00 32.90  ? 568  GLY   A C   1 
ATOM   2120  O  O   . GLY   A  1 267 ? -22.223 6.591   -42.492  1.00 35.04  ? 568  GLY   A O   1 
ATOM   2121  N  N   . LEU   A  1 268 ? -23.218 4.970   -43.676  1.00 30.31  ? 569  LEU   A N   1 
ATOM   2122  C  CA  . LEU   A  1 268 ? -24.386 5.784   -44.012  1.00 38.04  ? 569  LEU   A CA  1 
ATOM   2123  C  C   . LEU   A  1 268 ? -25.618 5.279   -43.287  1.00 38.04  ? 569  LEU   A C   1 
ATOM   2124  O  O   . LEU   A  1 268 ? -26.187 4.243   -43.679  1.00 38.42  ? 569  LEU   A O   1 
ATOM   2125  C  CB  . LEU   A  1 268 ? -24.626 5.780   -45.529  1.00 32.73  ? 569  LEU   A CB  1 
ATOM   2126  C  CG  . LEU   A  1 268 ? -25.749 6.709   -45.972  1.00 34.72  ? 569  LEU   A CG  1 
ATOM   2127  C  CD1 . LEU   A  1 268 ? -25.284 8.153   -45.967  1.00 36.50  ? 569  LEU   A CD1 1 
ATOM   2128  C  CD2 . LEU   A  1 268 ? -26.317 6.317   -47.323  1.00 34.60  ? 569  LEU   A CD2 1 
ATOM   2129  N  N   . PRO   A  1 269 ? -26.081 5.962   -42.237  1.00 36.32  ? 570  PRO   A N   1 
ATOM   2130  C  CA  . PRO   A  1 269 ? -27.325 5.522   -41.589  1.00 32.24  ? 570  PRO   A CA  1 
ATOM   2131  C  C   . PRO   A  1 269 ? -28.512 6.063   -42.372  1.00 27.11  ? 570  PRO   A C   1 
ATOM   2132  O  O   . PRO   A  1 269 ? -28.673 7.275   -42.522  1.00 34.71  ? 570  PRO   A O   1 
ATOM   2133  C  CB  . PRO   A  1 269 ? -27.233 6.137   -40.177  1.00 25.09  ? 570  PRO   A CB  1 
ATOM   2134  C  CG  . PRO   A  1 269 ? -26.437 7.399   -40.379  1.00 29.60  ? 570  PRO   A CG  1 
ATOM   2135  C  CD  . PRO   A  1 269 ? -25.486 7.139   -41.567  1.00 30.40  ? 570  PRO   A CD  1 
ATOM   2136  N  N   . ALA   A  1 270 ? -29.362 5.161   -42.840  1.00 32.30  ? 571  ALA   A N   1 
ATOM   2137  C  CA  . ALA   A  1 270 ? -30.417 5.501   -43.793  1.00 33.54  ? 571  ALA   A CA  1 
ATOM   2138  C  C   . ALA   A  1 270 ? -31.692 4.731   -43.437  1.00 38.96  ? 571  ALA   A C   1 
ATOM   2139  O  O   . ALA   A  1 270 ? -31.865 3.589   -43.861  1.00 41.30  ? 571  ALA   A O   1 
ATOM   2140  C  CB  . ALA   A  1 270 ? -29.931 5.194   -45.211  1.00 32.30  ? 571  ALA   A CB  1 
ATOM   2141  N  N   . VAL   A  1 271 ? -32.578 5.367   -42.668  1.00 36.98  ? 572  VAL   A N   1 
ATOM   2142  C  CA  . VAL   A  1 271 ? -33.785 4.721   -42.158  1.00 31.43  ? 572  VAL   A CA  1 
ATOM   2143  C  C   . VAL   A  1 271 ? -34.844 4.700   -43.243  1.00 29.60  ? 572  VAL   A C   1 
ATOM   2144  O  O   . VAL   A  1 271 ? -35.199 5.746   -43.794  1.00 34.76  ? 572  VAL   A O   1 
ATOM   2145  C  CB  . VAL   A  1 271 ? -34.320 5.460   -40.915  1.00 37.10  ? 572  VAL   A CB  1 
ATOM   2146  C  CG1 . VAL   A  1 271 ? -35.752 5.037   -40.663  1.00 27.20  ? 572  VAL   A CG1 1 
ATOM   2147  C  CG2 . VAL   A  1 271 ? -33.450 5.193   -39.690  1.00 24.57  ? 572  VAL   A CG2 1 
ATOM   2148  N  N   . SER   A  1 272 ? -35.415 3.524   -43.498  1.00 38.80  ? 573  SER   A N   1 
ATOM   2149  C  CA  . SER   A  1 272 ? -36.288 3.368   -44.651  1.00 39.85  ? 573  SER   A CA  1 
ATOM   2150  C  C   . SER   A  1 272 ? -37.668 2.787   -44.340  1.00 40.41  ? 573  SER   A C   1 
ATOM   2151  O  O   . SER   A  1 272 ? -38.478 2.643   -45.264  1.00 43.06  ? 573  SER   A O   1 
ATOM   2152  C  CB  . SER   A  1 272 ? -35.589 2.507   -45.721  1.00 34.33  ? 573  SER   A CB  1 
ATOM   2153  O  OG  . SER   A  1 272 ? -35.016 1.319   -45.182  1.00 25.23  ? 573  SER   A OG  1 
ATOM   2154  N  N   . ASN   A  1 273 ? -37.985 2.495   -43.077  1.00 32.37  ? 574  ASN   A N   1 
ATOM   2155  C  CA  . ASN   A  1 273 ? -39.246 1.840   -42.730  1.00 34.94  ? 574  ASN   A CA  1 
ATOM   2156  C  C   . ASN   A  1 273 ? -40.264 2.767   -42.075  1.00 35.74  ? 574  ASN   A C   1 
ATOM   2157  O  O   . ASN   A  1 273 ? -41.323 2.295   -41.647  1.00 32.92  ? 574  ASN   A O   1 
ATOM   2158  C  CB  . ASN   A  1 273 ? -38.986 0.645   -41.814  1.00 32.63  ? 574  ASN   A CB  1 
ATOM   2159  C  CG  . ASN   A  1 273 ? -38.328 1.049   -40.515  1.00 41.70  ? 574  ASN   A CG  1 
ATOM   2160  O  OD1 . ASN   A  1 273 ? -37.916 2.199   -40.345  1.00 40.02  ? 574  ASN   A OD1 1 
ATOM   2161  N  ND2 . ASN   A  1 273 ? -38.204 0.104   -39.597  1.00 45.11  ? 574  ASN   A ND2 1 
ATOM   2162  N  N   . MET   A  1 274 ? -39.988 4.064   -42.001  1.00 30.87  ? 575  MET   A N   1 
ATOM   2163  C  CA  . MET   A  1 274 ? -40.910 4.996   -41.375  1.00 37.98  ? 575  MET   A CA  1 
ATOM   2164  C  C   . MET   A  1 274 ? -41.831 5.617   -42.414  1.00 45.88  ? 575  MET   A C   1 
ATOM   2165  O  O   . MET   A  1 274 ? -41.665 5.438   -43.621  1.00 53.73  ? 575  MET   A O   1 
ATOM   2166  C  CB  . MET   A  1 274 ? -40.148 6.083   -40.611  1.00 24.32  ? 575  MET   A CB  1 
ATOM   2167  C  CG  . MET   A  1 274 ? -39.513 5.508   -39.303  1.00 45.86  ? 575  MET   A CG  1 
ATOM   2168  S  SD  . MET   A  1 274 ? -38.824 6.766   -38.237  1.00 43.73  ? 575  MET   A SD  1 
ATOM   2169  C  CE  . MET   A  1 274 ? -40.284 7.287   -37.360  1.00 38.82  ? 575  MET   A CE  1 
ATOM   2170  N  N   . LEU   A  1 275 ? -42.811 6.367   -41.928  1.00 34.92  ? 576  LEU   A N   1 
ATOM   2171  C  CA  . LEU   A  1 275 ? -43.833 6.959   -42.775  1.00 28.76  ? 576  LEU   A CA  1 
ATOM   2172  C  C   . LEU   A  1 275 ? -43.837 8.459   -42.559  1.00 39.50  ? 576  LEU   A C   1 
ATOM   2173  O  O   . LEU   A  1 275 ? -43.894 8.925   -41.418  1.00 39.27  ? 576  LEU   A O   1 
ATOM   2174  C  CB  . LEU   A  1 275 ? -45.209 6.352   -42.481  1.00 32.93  ? 576  LEU   A CB  1 
ATOM   2175  C  CG  . LEU   A  1 275 ? -46.436 6.809   -43.268  1.00 39.91  ? 576  LEU   A CG  1 
ATOM   2176  C  CD1 . LEU   A  1 275 ? -47.405 5.634   -43.406  1.00 36.92  ? 576  LEU   A CD1 1 
ATOM   2177  C  CD2 . LEU   A  1 275 ? -47.119 8.004   -42.593  1.00 33.23  ? 576  LEU   A CD2 1 
ATOM   2178  N  N   . LEU   A  1 276 ? -43.779 9.203   -43.658  1.00 41.77  ? 577  LEU   A N   1 
ATOM   2179  C  CA  . LEU   A  1 276 ? -43.770 10.658  -43.634  1.00 42.43  ? 577  LEU   A CA  1 
ATOM   2180  C  C   . LEU   A  1 276 ? -45.185 11.178  -43.862  1.00 46.00  ? 577  LEU   A C   1 
ATOM   2181  O  O   . LEU   A  1 276 ? -45.830 10.816  -44.852  1.00 43.22  ? 577  LEU   A O   1 
ATOM   2182  C  CB  . LEU   A  1 276 ? -42.809 11.200  -44.695  1.00 30.32  ? 577  LEU   A CB  1 
ATOM   2183  C  CG  . LEU   A  1 276 ? -42.950 12.679  -45.035  1.00 37.81  ? 577  LEU   A CG  1 
ATOM   2184  C  CD1 . LEU   A  1 276 ? -42.662 13.549  -43.826  1.00 24.54  ? 577  LEU   A CD1 1 
ATOM   2185  C  CD2 . LEU   A  1 276 ? -42.028 13.056  -46.214  1.00 35.57  ? 577  LEU   A CD2 1 
ATOM   2186  N  N   . GLU   A  1 277 ? -45.664 12.020  -42.945  1.00 45.46  ? 578  GLU   A N   1 
ATOM   2187  C  CA  . GLU   A  1 277 ? -47.039 12.505  -42.956  1.00 41.67  ? 578  GLU   A CA  1 
ATOM   2188  C  C   . GLU   A  1 277 ? -47.033 14.020  -43.110  1.00 43.82  ? 578  GLU   A C   1 
ATOM   2189  O  O   . GLU   A  1 277 ? -46.588 14.737  -42.212  1.00 39.53  ? 578  GLU   A O   1 
ATOM   2190  C  CB  . GLU   A  1 277 ? -47.768 12.074  -41.687  1.00 44.97  ? 578  GLU   A CB  1 
ATOM   2191  C  CG  . GLU   A  1 277 ? -49.231 12.429  -41.658  1.00 53.11  ? 578  GLU   A CG  1 
ATOM   2192  C  CD  . GLU   A  1 277 ? -49.482 13.703  -40.901  1.00 63.84  ? 578  GLU   A CD  1 
ATOM   2193  O  OE1 . GLU   A  1 277 ? -50.172 14.609  -41.432  1.00 65.16  ? 578  GLU   A OE1 1 
ATOM   2194  O  OE2 . GLU   A  1 277 ? -48.966 13.798  -39.768  1.00 70.14  ? 578  GLU   A OE2 1 
ATOM   2195  N  N   . ILE   A  1 278 ? -47.533 14.505  -44.245  1.00 43.96  ? 579  ILE   A N   1 
ATOM   2196  C  CA  . ILE   A  1 278 ? -47.587 15.929  -44.560  1.00 40.46  ? 579  ILE   A CA  1 
ATOM   2197  C  C   . ILE   A  1 278 ? -49.009 16.271  -44.975  1.00 43.83  ? 579  ILE   A C   1 
ATOM   2198  O  O   . ILE   A  1 278 ? -49.507 15.737  -45.978  1.00 48.37  ? 579  ILE   A O   1 
ATOM   2199  C  CB  . ILE   A  1 278 ? -46.610 16.312  -45.684  1.00 43.70  ? 579  ILE   A CB  1 
ATOM   2200  C  CG1 . ILE   A  1 278 ? -45.182 15.901  -45.332  1.00 45.39  ? 579  ILE   A CG1 1 
ATOM   2201  C  CG2 . ILE   A  1 278 ? -46.680 17.795  -45.938  1.00 43.61  ? 579  ILE   A CG2 1 
ATOM   2202  C  CD1 . ILE   A  1 278 ? -44.224 16.031  -46.474  1.00 47.79  ? 579  ILE   A CD1 1 
ATOM   2203  N  N   . GLY   A  1 279 ? -49.650 17.166  -44.220  1.00 38.02  ? 580  GLY   A N   1 
ATOM   2204  C  CA  . GLY   A  1 279 ? -50.973 17.664  -44.568  1.00 37.01  ? 580  GLY   A CA  1 
ATOM   2205  C  C   . GLY   A  1 279 ? -52.044 16.601  -44.659  1.00 46.05  ? 580  GLY   A C   1 
ATOM   2206  O  O   . GLY   A  1 279 ? -53.005 16.755  -45.428  1.00 41.82  ? 580  GLY   A O   1 
ATOM   2207  N  N   . GLY   A  1 280 ? -51.922 15.531  -43.869  1.00 47.46  ? 581  GLY   A N   1 
ATOM   2208  C  CA  . GLY   A  1 280 ? -52.799 14.393  -43.984  1.00 45.30  ? 581  GLY   A CA  1 
ATOM   2209  C  C   . GLY   A  1 280 ? -52.410 13.403  -45.058  1.00 43.27  ? 581  GLY   A C   1 
ATOM   2210  O  O   . GLY   A  1 280 ? -53.005 12.322  -45.124  1.00 46.79  ? 581  GLY   A O   1 
ATOM   2211  N  N   . LEU   A  1 281 ? -51.440 13.731  -45.908  1.00 35.98  ? 582  LEU   A N   1 
ATOM   2212  C  CA  . LEU   A  1 281 ? -50.969 12.788  -46.909  1.00 46.92  ? 582  LEU   A CA  1 
ATOM   2213  C  C   . LEU   A  1 281 ? -49.924 11.868  -46.291  1.00 46.18  ? 582  LEU   A C   1 
ATOM   2214  O  O   . LEU   A  1 281 ? -49.093 12.298  -45.486  1.00 43.19  ? 582  LEU   A O   1 
ATOM   2215  C  CB  . LEU   A  1 281 ? -50.382 13.529  -48.114  1.00 44.77  ? 582  LEU   A CB  1 
ATOM   2216  C  CG  . LEU   A  1 281 ? -51.338 14.430  -48.893  1.00 44.93  ? 582  LEU   A CG  1 
ATOM   2217  C  CD1 . LEU   A  1 281 ? -50.579 15.248  -49.918  1.00 51.97  ? 582  LEU   A CD1 1 
ATOM   2218  C  CD2 . LEU   A  1 281 ? -52.390 13.590  -49.565  1.00 43.64  ? 582  LEU   A CD2 1 
ATOM   2219  N  N   . GLU   A  1 282 ? -49.959 10.596  -46.672  1.00 43.77  ? 583  GLU   A N   1 
ATOM   2220  C  CA  . GLU   A  1 282 ? -49.110 9.580   -46.062  1.00 44.12  ? 583  GLU   A CA  1 
ATOM   2221  C  C   . GLU   A  1 282 ? -48.111 9.054   -47.093  1.00 46.89  ? 583  GLU   A C   1 
ATOM   2222  O  O   . GLU   A  1 282 ? -48.506 8.426   -48.082  1.00 43.62  ? 583  GLU   A O   1 
ATOM   2223  C  CB  . GLU   A  1 282 ? -49.966 8.447   -45.489  1.00 46.19  ? 583  GLU   A CB  1 
ATOM   2224  C  CG  . GLU   A  1 282 ? -50.872 8.855   -44.313  1.00 46.15  ? 583  GLU   A CG  1 
ATOM   2225  C  CD  . GLU   A  1 282 ? -51.700 7.689   -43.790  1.00 57.16  ? 583  GLU   A CD  1 
ATOM   2226  O  OE1 . GLU   A  1 282 ? -52.168 6.871   -44.613  1.00 57.81  ? 583  GLU   A OE1 1 
ATOM   2227  O  OE2 . GLU   A  1 282 ? -51.871 7.574   -42.554  1.00 61.53  ? 583  GLU   A OE2 1 
ATOM   2228  N  N   . PHE   A  1 283 ? -46.824 9.295   -46.847  1.00 42.97  ? 584  PHE   A N   1 
ATOM   2229  C  CA  . PHE   A  1 283 ? -45.745 8.852   -47.730  1.00 34.49  ? 584  PHE   A CA  1 
ATOM   2230  C  C   . PHE   A  1 283 ? -45.112 7.606   -47.125  1.00 38.04  ? 584  PHE   A C   1 
ATOM   2231  O  O   . PHE   A  1 283 ? -44.177 7.686   -46.331  1.00 34.59  ? 584  PHE   A O   1 
ATOM   2232  C  CB  . PHE   A  1 283 ? -44.728 9.971   -47.924  1.00 30.55  ? 584  PHE   A CB  1 
ATOM   2233  C  CG  . PHE   A  1 283 ? -45.272 11.127  -48.722  1.00 42.71  ? 584  PHE   A CG  1 
ATOM   2234  C  CD1 . PHE   A  1 283 ? -45.347 11.051  -50.113  1.00 37.57  ? 584  PHE   A CD1 1 
ATOM   2235  C  CD2 . PHE   A  1 283 ? -45.745 12.270  -48.087  1.00 31.90  ? 584  PHE   A CD2 1 
ATOM   2236  C  CE1 . PHE   A  1 283 ? -45.861 12.094  -50.842  1.00 31.68  ? 584  PHE   A CE1 1 
ATOM   2237  C  CE2 . PHE   A  1 283 ? -46.269 13.320  -48.817  1.00 31.49  ? 584  PHE   A CE2 1 
ATOM   2238  C  CZ  . PHE   A  1 283 ? -46.322 13.232  -50.205  1.00 36.36  ? 584  PHE   A CZ  1 
ATOM   2239  N  N   . SER   A  1 284 ? -45.629 6.436   -47.515  1.00 35.93  ? 585  SER   A N   1 
ATOM   2240  C  CA  . SER   A  1 284 ? -45.233 5.192   -46.865  1.00 38.52  ? 585  SER   A CA  1 
ATOM   2241  C  C   . SER   A  1 284 ? -43.804 4.760   -47.179  1.00 37.80  ? 585  SER   A C   1 
ATOM   2242  O  O   . SER   A  1 284 ? -43.311 3.821   -46.538  1.00 30.61  ? 585  SER   A O   1 
ATOM   2243  C  CB  . SER   A  1 284 ? -46.204 4.074   -47.245  1.00 39.69  ? 585  SER   A CB  1 
ATOM   2244  O  OG  . SER   A  1 284 ? -46.516 4.136   -48.621  1.00 48.14  ? 585  SER   A OG  1 
ATOM   2245  N  N   . ALA   A  1 285 ? -43.137 5.384   -48.152  1.00 37.56  ? 586  ALA   A N   1 
ATOM   2246  C  CA  . ALA   A  1 285 ? -41.763 5.033   -48.504  1.00 36.96  ? 586  ALA   A CA  1 
ATOM   2247  C  C   . ALA   A  1 285 ? -40.984 6.324   -48.727  1.00 41.83  ? 586  ALA   A C   1 
ATOM   2248  O  O   . ALA   A  1 285 ? -41.176 7.007   -49.746  1.00 37.38  ? 586  ALA   A O   1 
ATOM   2249  C  CB  . ALA   A  1 285 ? -41.714 4.132   -49.734  1.00 37.22  ? 586  ALA   A CB  1 
ATOM   2250  N  N   . CYS   A  1 286 ? -40.091 6.648   -47.773  1.00 27.43  ? 587  CYS   A N   1 
ATOM   2251  C  CA  . CYS   A  1 286 ? -39.473 7.961   -47.675  1.00 25.49  ? 587  CYS   A CA  1 
ATOM   2252  C  C   . CYS   A  1 286 ? -38.088 7.887   -47.045  1.00 35.43  ? 587  CYS   A C   1 
ATOM   2253  O  O   . CYS   A  1 286 ? -37.805 8.654   -46.114  1.00 41.69  ? 587  CYS   A O   1 
ATOM   2254  C  CB  . CYS   A  1 286 ? -40.364 8.890   -46.845  1.00 31.29  ? 587  CYS   A CB  1 
ATOM   2255  S  SG  . CYS   A  1 286 ? -40.587 8.327   -45.065  1.00 37.76  ? 587  CYS   A SG  1 
ATOM   2256  N  N   . PRO   A  1 287 ? -37.191 7.023   -47.530  1.00 36.51  ? 588  PRO   A N   1 
ATOM   2257  C  CA  . PRO   A  1 287 ? -35.965 6.743   -46.773  1.00 30.79  ? 588  PRO   A CA  1 
ATOM   2258  C  C   . PRO   A  1 287 ? -35.098 7.981   -46.624  1.00 35.99  ? 588  PRO   A C   1 
ATOM   2259  O  O   . PRO   A  1 287 ? -34.936 8.767   -47.563  1.00 35.29  ? 588  PRO   A O   1 
ATOM   2260  C  CB  . PRO   A  1 287 ? -35.271 5.671   -47.617  1.00 32.64  ? 588  PRO   A CB  1 
ATOM   2261  C  CG  . PRO   A  1 287 ? -35.726 5.949   -48.981  1.00 35.77  ? 588  PRO   A CG  1 
ATOM   2262  C  CD  . PRO   A  1 287 ? -37.154 6.381   -48.856  1.00 38.06  ? 588  PRO   A CD  1 
ATOM   2263  N  N   . PHE   A  1 288 ? -34.514 8.146   -45.436  1.00 28.72  ? 589  PHE   A N   1 
ATOM   2264  C  CA  . PHE   A  1 288 ? -33.722 9.335   -45.159  1.00 29.58  ? 589  PHE   A CA  1 
ATOM   2265  C  C   . PHE   A  1 288 ? -32.417 8.938   -44.497  1.00 30.46  ? 589  PHE   A C   1 
ATOM   2266  O  O   . PHE   A  1 288 ? -32.287 7.863   -43.915  1.00 29.67  ? 589  PHE   A O   1 
ATOM   2267  C  CB  . PHE   A  1 288 ? -34.486 10.357  -44.295  1.00 33.84  ? 589  PHE   A CB  1 
ATOM   2268  C  CG  . PHE   A  1 288 ? -35.055 9.777   -43.010  1.00 43.17  ? 589  PHE   A CG  1 
ATOM   2269  C  CD1 . PHE   A  1 288 ? -34.267 9.662   -41.872  1.00 41.65  ? 589  PHE   A CD1 1 
ATOM   2270  C  CD2 . PHE   A  1 288 ? -36.378 9.346   -42.951  1.00 39.86  ? 589  PHE   A CD2 1 
ATOM   2271  C  CE1 . PHE   A  1 288 ? -34.786 9.126   -40.700  1.00 36.90  ? 589  PHE   A CE1 1 
ATOM   2272  C  CE2 . PHE   A  1 288 ? -36.900 8.814   -41.783  1.00 38.28  ? 589  PHE   A CE2 1 
ATOM   2273  C  CZ  . PHE   A  1 288 ? -36.098 8.702   -40.655  1.00 31.57  ? 589  PHE   A CZ  1 
ATOM   2274  N  N   . SER   A  1 289 ? -31.435 9.816   -44.612  1.00 32.29  ? 590  SER   A N   1 
ATOM   2275  C  CA  . SER   A  1 289 ? -30.110 9.466   -44.149  1.00 31.20  ? 590  SER   A CA  1 
ATOM   2276  C  C   . SER   A  1 289 ? -29.434 10.714  -43.606  1.00 30.75  ? 590  SER   A C   1 
ATOM   2277  O  O   . SER   A  1 289 ? -29.757 11.840  -43.990  1.00 28.91  ? 590  SER   A O   1 
ATOM   2278  C  CB  . SER   A  1 289 ? -29.285 8.846   -45.285  1.00 31.02  ? 590  SER   A CB  1 
ATOM   2279  O  OG  . SER   A  1 289 ? -29.180 9.781   -46.347  1.00 38.49  ? 590  SER   A OG  1 
ATOM   2280  N  N   . GLY   A  1 290 ? -28.479 10.498  -42.707  1.00 30.48  ? 591  GLY   A N   1 
ATOM   2281  C  CA  . GLY   A  1 290 ? -27.661 11.581  -42.206  1.00 29.25  ? 591  GLY   A CA  1 
ATOM   2282  C  C   . GLY   A  1 290 ? -26.245 11.085  -42.027  1.00 38.69  ? 591  GLY   A C   1 
ATOM   2283  O  O   . GLY   A  1 290 ? -25.605 10.672  -42.996  1.00 45.85  ? 591  GLY   A O   1 
ATOM   2284  N  N   . TRP   A  1 291 ? -25.747 11.122  -40.794  1.00 39.34  ? 592  TRP   A N   1 
ATOM   2285  C  CA  . TRP   A  1 291 ? -24.484 10.494  -40.438  1.00 30.02  ? 592  TRP   A CA  1 
ATOM   2286  C  C   . TRP   A  1 291 ? -24.597 10.034  -38.995  1.00 38.08  ? 592  TRP   A C   1 
ATOM   2287  O  O   . TRP   A  1 291 ? -25.454 10.503  -38.240  1.00 38.12  ? 592  TRP   A O   1 
ATOM   2288  C  CB  . TRP   A  1 291 ? -23.285 11.441  -40.626  1.00 30.44  ? 592  TRP   A CB  1 
ATOM   2289  C  CG  . TRP   A  1 291 ? -23.417 12.741  -39.888  1.00 37.38  ? 592  TRP   A CG  1 
ATOM   2290  C  CD1 . TRP   A  1 291 ? -23.162 12.967  -38.557  1.00 39.87  ? 592  TRP   A CD1 1 
ATOM   2291  C  CD2 . TRP   A  1 291 ? -23.841 13.990  -40.429  1.00 40.84  ? 592  TRP   A CD2 1 
ATOM   2292  N  NE1 . TRP   A  1 291 ? -23.412 14.278  -38.245  1.00 40.59  ? 592  TRP   A NE1 1 
ATOM   2293  C  CE2 . TRP   A  1 291 ? -23.827 14.930  -39.376  1.00 45.30  ? 592  TRP   A CE2 1 
ATOM   2294  C  CE3 . TRP   A  1 291 ? -24.234 14.411  -41.703  1.00 47.65  ? 592  TRP   A CE3 1 
ATOM   2295  C  CZ2 . TRP   A  1 291 ? -24.189 16.265  -39.562  1.00 55.15  ? 592  TRP   A CZ2 1 
ATOM   2296  C  CZ3 . TRP   A  1 291 ? -24.596 15.739  -41.886  1.00 51.41  ? 592  TRP   A CZ3 1 
ATOM   2297  C  CH2 . TRP   A  1 291 ? -24.565 16.649  -40.827  1.00 54.75  ? 592  TRP   A CH2 1 
ATOM   2298  N  N   . TYR   A  1 292 ? -23.713 9.116   -38.620  1.00 42.82  ? 593  TYR   A N   1 
ATOM   2299  C  CA  . TYR   A  1 292 ? -23.787 8.457   -37.325  1.00 39.04  ? 593  TYR   A CA  1 
ATOM   2300  C  C   . TYR   A  1 292 ? -23.273 9.316   -36.186  1.00 36.17  ? 593  TYR   A C   1 
ATOM   2301  O  O   . TYR   A  1 292 ? -22.306 10.076  -36.327  1.00 37.35  ? 593  TYR   A O   1 
ATOM   2302  C  CB  . TYR   A  1 292 ? -22.971 7.178   -37.322  1.00 34.67  ? 593  TYR   A CB  1 
ATOM   2303  C  CG  . TYR   A  1 292 ? -23.742 5.973   -37.725  1.00 42.49  ? 593  TYR   A CG  1 
ATOM   2304  C  CD1 . TYR   A  1 292 ? -24.793 5.510   -36.940  1.00 39.02  ? 593  TYR   A CD1 1 
ATOM   2305  C  CD2 . TYR   A  1 292 ? -23.404 5.266   -38.879  1.00 32.72  ? 593  TYR   A CD2 1 
ATOM   2306  C  CE1 . TYR   A  1 292 ? -25.493 4.384   -37.303  1.00 39.08  ? 593  TYR   A CE1 1 
ATOM   2307  C  CE2 . TYR   A  1 292 ? -24.094 4.146   -39.245  1.00 34.71  ? 593  TYR   A CE2 1 
ATOM   2308  C  CZ  . TYR   A  1 292 ? -25.135 3.704   -38.459  1.00 38.81  ? 593  TYR   A CZ  1 
ATOM   2309  O  OH  . TYR   A  1 292 ? -25.825 2.575   -38.825  1.00 40.60  ? 593  TYR   A OH  1 
ATOM   2310  N  N   . MET   A  1 293 ? -23.928 9.159   -35.046  1.00 31.80  ? 594  MET   A N   1 
ATOM   2311  C  CA  . MET   A  1 293 ? -23.301 9.385   -33.763  1.00 28.45  ? 594  MET   A CA  1 
ATOM   2312  C  C   . MET   A  1 293 ? -22.618 8.086   -33.374  1.00 31.41  ? 594  MET   A C   1 
ATOM   2313  O  O   . MET   A  1 293 ? -23.150 7.000   -33.623  1.00 32.61  ? 594  MET   A O   1 
ATOM   2314  C  CB  . MET   A  1 293 ? -24.342 9.809   -32.731  1.00 31.89  ? 594  MET   A CB  1 
ATOM   2315  C  CG  . MET   A  1 293 ? -23.805 10.044  -31.331  1.00 32.93  ? 594  MET   A CG  1 
ATOM   2316  S  SD  . MET   A  1 293 ? -25.002 11.021  -30.404  1.00 34.00  ? 594  MET   A SD  1 
ATOM   2317  C  CE  . MET   A  1 293 ? -26.200 9.777   -29.944  1.00 27.27  ? 594  MET   A CE  1 
ATOM   2318  N  N   . GLY   A  1 294 ? -21.419 8.197   -32.794  1.00 28.91  ? 595  GLY   A N   1 
ATOM   2319  C  CA  . GLY   A  1 294 ? -20.602 7.014   -32.550  1.00 31.20  ? 595  GLY   A CA  1 
ATOM   2320  C  C   . GLY   A  1 294 ? -21.268 5.949   -31.693  1.00 39.97  ? 595  GLY   A C   1 
ATOM   2321  O  O   . GLY   A  1 294 ? -21.032 4.749   -31.890  1.00 40.06  ? 595  GLY   A O   1 
ATOM   2322  N  N   . THR   A  1 295 ? -22.112 6.358   -30.739  1.00 38.18  ? 596  THR   A N   1 
ATOM   2323  C  CA  . THR   A  1 295 ? -22.670 5.383   -29.806  1.00 38.66  ? 596  THR   A CA  1 
ATOM   2324  C  C   . THR   A  1 295 ? -23.737 4.522   -30.448  1.00 39.46  ? 596  THR   A C   1 
ATOM   2325  O  O   . THR   A  1 295 ? -24.016 3.439   -29.931  1.00 30.75  ? 596  THR   A O   1 
ATOM   2326  C  CB  . THR   A  1 295 ? -23.300 6.050   -28.586  1.00 36.73  ? 596  THR   A CB  1 
ATOM   2327  O  OG1 . THR   A  1 295 ? -24.317 6.971   -29.026  1.00 33.15  ? 596  THR   A OG1 1 
ATOM   2328  C  CG2 . THR   A  1 295 ? -22.248 6.737   -27.714  1.00 29.67  ? 596  THR   A CG2 1 
ATOM   2329  N  N   . GLU   A  1 296 ? -24.381 4.997   -31.523  1.00 30.24  ? 597  GLU   A N   1 
ATOM   2330  C  CA  . GLU   A  1 296 ? -25.312 4.133   -32.233  1.00 35.36  ? 597  GLU   A CA  1 
ATOM   2331  C  C   . GLU   A  1 296 ? -24.614 2.840   -32.628  1.00 37.72  ? 597  GLU   A C   1 
ATOM   2332  O  O   . GLU   A  1 296 ? -25.179 1.748   -32.501  1.00 42.08  ? 597  GLU   A O   1 
ATOM   2333  C  CB  . GLU   A  1 296 ? -25.868 4.845   -33.474  1.00 43.46  ? 597  GLU   A CB  1 
ATOM   2334  C  CG  . GLU   A  1 296 ? -26.652 6.119   -33.201  1.00 43.68  ? 597  GLU   A CG  1 
ATOM   2335  C  CD  . GLU   A  1 296 ? -27.253 6.711   -34.472  1.00 43.98  ? 597  GLU   A CD  1 
ATOM   2336  O  OE1 . GLU   A  1 296 ? -28.239 6.135   -34.977  1.00 43.62  ? 597  GLU   A OE1 1 
ATOM   2337  O  OE2 . GLU   A  1 296 ? -26.736 7.743   -34.957  1.00 42.14  ? 597  GLU   A OE2 1 
ATOM   2338  N  N   . ILE   A  1 297 ? -23.361 2.952   -33.074  1.00 29.66  ? 598  ILE   A N   1 
ATOM   2339  C  CA  . ILE   A  1 297 ? -22.584 1.782   -33.464  1.00 42.57  ? 598  ILE   A CA  1 
ATOM   2340  C  C   . ILE   A  1 297 ? -21.915 1.168   -32.250  1.00 40.11  ? 598  ILE   A C   1 
ATOM   2341  O  O   . ILE   A  1 297 ? -22.043 -0.034  -32.002  1.00 39.24  ? 598  ILE   A O   1 
ATOM   2342  C  CB  . ILE   A  1 297 ? -21.521 2.147   -34.525  1.00 32.97  ? 598  ILE   A CB  1 
ATOM   2343  C  CG1 . ILE   A  1 297 ? -22.105 2.986   -35.654  1.00 30.37  ? 598  ILE   A CG1 1 
ATOM   2344  C  CG2 . ILE   A  1 297 ? -20.837 0.886   -35.043  1.00 33.37  ? 598  ILE   A CG2 1 
ATOM   2345  C  CD1 . ILE   A  1 297 ? -21.059 3.478   -36.641  1.00 36.62  ? 598  ILE   A CD1 1 
ATOM   2346  N  N   . GLY   A  1 298 ? -21.179 1.998   -31.496  1.00 40.74  ? 599  GLY   A N   1 
ATOM   2347  C  CA  . GLY   A  1 298 ? -20.304 1.485   -30.449  1.00 49.13  ? 599  GLY   A CA  1 
ATOM   2348  C  C   . GLY   A  1 298 ? -21.043 0.887   -29.261  1.00 47.65  ? 599  GLY   A C   1 
ATOM   2349  O  O   . GLY   A  1 298 ? -20.611 -0.123  -28.705  1.00 51.31  ? 599  GLY   A O   1 
ATOM   2350  N  N   . VAL   A  1 299 ? -22.167 1.481   -28.871  1.00 43.66  ? 600  VAL   A N   1 
ATOM   2351  C  CA  . VAL   A  1 299 ? -22.921 0.999   -27.713  1.00 45.18  ? 600  VAL   A CA  1 
ATOM   2352  C  C   . VAL   A  1 299 ? -24.034 0.043   -28.118  1.00 47.42  ? 600  VAL   A C   1 
ATOM   2353  O  O   . VAL   A  1 299 ? -24.134 -1.073  -27.593  1.00 35.27  ? 600  VAL   A O   1 
ATOM   2354  C  CB  . VAL   A  1 299 ? -23.482 2.189   -26.916  1.00 42.10  ? 600  VAL   A CB  1 
ATOM   2355  C  CG1 . VAL   A  1 299 ? -24.210 1.681   -25.671  1.00 36.76  ? 600  VAL   A CG1 1 
ATOM   2356  C  CG2 . VAL   A  1 299 ? -22.363 3.135   -26.535  1.00 48.59  ? 600  VAL   A CG2 1 
ATOM   2357  N  N   . ARG   A  1 300 ? -24.896 0.461   -29.051  1.00 48.58  ? 601  ARG   A N   1 
ATOM   2358  C  CA  . ARG   A  1 300 ? -26.090 -0.325  -29.357  1.00 55.36  ? 601  ARG   A CA  1 
ATOM   2359  C  C   . ARG   A  1 300 ? -25.789 -1.447  -30.362  1.00 50.46  ? 601  ARG   A C   1 
ATOM   2360  O  O   . ARG   A  1 300 ? -25.958 -2.629  -30.038  1.00 47.44  ? 601  ARG   A O   1 
ATOM   2361  C  CB  . ARG   A  1 300 ? -27.228 0.597   -29.839  1.00 44.79  ? 601  ARG   A CB  1 
ATOM   2362  C  CG  . ARG   A  1 300 ? -27.607 1.775   -28.880  1.00 39.01  ? 601  ARG   A CG  1 
ATOM   2363  C  CD  . ARG   A  1 300 ? -28.081 1.334   -27.435  1.00 37.15  ? 601  ARG   A CD  1 
ATOM   2364  N  NE  . ARG   A  1 300 ? -29.058 0.243   -27.494  1.00 36.19  ? 601  ARG   A NE  1 
ATOM   2365  C  CZ  . ARG   A  1 300 ? -30.342 0.409   -27.789  1.00 27.54  ? 601  ARG   A CZ  1 
ATOM   2366  N  NH1 . ARG   A  1 300 ? -30.831 1.624   -28.025  1.00 38.75  ? 601  ARG   A NH1 1 
ATOM   2367  N  NH2 . ARG   A  1 300 ? -31.128 -0.641  -27.886  1.00 37.94  ? 601  ARG   A NH2 1 
ATOM   2368  N  N   . ASP   A  1 301 ? -25.316 -1.101  -31.575  1.00 44.85  ? 602  ASP   A N   1 
ATOM   2369  C  CA  . ASP   A  1 301 ? -25.064 -2.114  -32.612  1.00 45.61  ? 602  ASP   A CA  1 
ATOM   2370  C  C   . ASP   A  1 301 ? -24.116 -3.202  -32.129  1.00 47.44  ? 602  ASP   A C   1 
ATOM   2371  O  O   . ASP   A  1 301 ? -24.387 -4.396  -32.311  1.00 42.92  ? 602  ASP   A O   1 
ATOM   2372  C  CB  . ASP   A  1 301 ? -24.493 -1.474  -33.884  1.00 40.01  ? 602  ASP   A CB  1 
ATOM   2373  C  CG  . ASP   A  1 301 ? -25.463 -0.536  -34.542  1.00 36.88  ? 602  ASP   A CG  1 
ATOM   2374  O  OD1 . ASP   A  1 301 ? -26.686 -0.761  -34.424  1.00 45.35  ? 602  ASP   A OD1 1 
ATOM   2375  O  OD2 . ASP   A  1 301 ? -25.001 0.443   -35.158  1.00 42.80  ? 602  ASP   A OD2 1 
ATOM   2376  N  N   . TYR   A  1 302 ? -23.000 -2.807  -31.504  1.00 50.53  ? 603  TYR   A N   1 
ATOM   2377  C  CA  . TYR   A  1 302 ? -21.941 -3.737  -31.119  1.00 49.02  ? 603  TYR   A CA  1 
ATOM   2378  C  C   . TYR   A  1 302 ? -22.149 -4.408  -29.768  1.00 49.66  ? 603  TYR   A C   1 
ATOM   2379  O  O   . TYR   A  1 302 ? -21.657 -5.527  -29.571  1.00 53.50  ? 603  TYR   A O   1 
ATOM   2380  C  CB  . TYR   A  1 302 ? -20.597 -3.013  -31.092  1.00 49.02  ? 603  TYR   A CB  1 
ATOM   2381  C  CG  . TYR   A  1 302 ? -19.954 -2.886  -32.448  1.00 42.89  ? 603  TYR   A CG  1 
ATOM   2382  C  CD1 . TYR   A  1 302 ? -20.513 -3.504  -33.562  1.00 40.47  ? 603  TYR   A CD1 1 
ATOM   2383  C  CD2 . TYR   A  1 302 ? -18.787 -2.157  -32.614  1.00 36.35  ? 603  TYR   A CD2 1 
ATOM   2384  C  CE1 . TYR   A  1 302 ? -19.915 -3.398  -34.803  1.00 44.17  ? 603  TYR   A CE1 1 
ATOM   2385  C  CE2 . TYR   A  1 302 ? -18.179 -2.043  -33.865  1.00 41.84  ? 603  TYR   A CE2 1 
ATOM   2386  C  CZ  . TYR   A  1 302 ? -18.755 -2.662  -34.955  1.00 42.72  ? 603  TYR   A CZ  1 
ATOM   2387  O  OH  . TYR   A  1 302 ? -18.166 -2.556  -36.203  1.00 45.92  ? 603  TYR   A OH  1 
ATOM   2388  N  N   . CYS   A  1 303 ? -22.854 -3.762  -28.825  1.00 48.17  ? 604  CYS   A N   1 
ATOM   2389  C  CA  . CYS   A  1 303 ? -22.829 -4.204  -27.433  1.00 58.32  ? 604  CYS   A CA  1 
ATOM   2390  C  C   . CYS   A  1 303 ? -24.174 -4.576  -26.823  1.00 55.32  ? 604  CYS   A C   1 
ATOM   2391  O  O   . CYS   A  1 303 ? -24.181 -5.142  -25.723  1.00 53.17  ? 604  CYS   A O   1 
ATOM   2392  C  CB  . CYS   A  1 303 ? -22.172 -3.138  -26.543  1.00 55.76  ? 604  CYS   A CB  1 
ATOM   2393  S  SG  . CYS   A  1 303 ? -20.393 -3.037  -26.763  1.00 48.53  ? 604  CYS   A SG  1 
ATOM   2394  N  N   . ASP   A  1 304 ? -25.301 -4.272  -27.469  1.00 50.32  ? 605  ASP   A N   1 
ATOM   2395  C  CA  . ASP   A  1 304 ? -26.569 -4.842  -27.027  1.00 47.19  ? 605  ASP   A CA  1 
ATOM   2396  C  C   . ASP   A  1 304 ? -26.451 -6.358  -26.981  1.00 46.74  ? 605  ASP   A C   1 
ATOM   2397  O  O   . ASP   A  1 304 ? -25.852 -6.973  -27.870  1.00 54.00  ? 605  ASP   A O   1 
ATOM   2398  C  CB  . ASP   A  1 304 ? -27.709 -4.466  -27.975  1.00 46.50  ? 605  ASP   A CB  1 
ATOM   2399  C  CG  . ASP   A  1 304 ? -28.331 -3.107  -27.683  1.00 47.31  ? 605  ASP   A CG  1 
ATOM   2400  O  OD1 . ASP   A  1 304 ? -27.747 -2.281  -26.937  1.00 44.24  ? 605  ASP   A OD1 1 
ATOM   2401  O  OD2 . ASP   A  1 304 ? -29.434 -2.877  -28.230  1.00 46.63  ? 605  ASP   A OD2 1 
ATOM   2402  N  N   . ASN   A  1 305 ? -27.036 -6.972  -25.948  1.00 42.10  ? 606  ASN   A N   1 
ATOM   2403  C  CA  . ASN   A  1 305 ? -26.967 -8.427  -25.855  1.00 46.83  ? 606  ASN   A CA  1 
ATOM   2404  C  C   . ASN   A  1 305 ? -27.660 -9.096  -27.039  1.00 44.69  ? 606  ASN   A C   1 
ATOM   2405  O  O   . ASN   A  1 305 ? -27.203 -10.145 -27.508  1.00 48.94  ? 606  ASN   A O   1 
ATOM   2406  C  CB  . ASN   A  1 305 ? -27.564 -8.912  -24.532  1.00 61.42  ? 606  ASN   A CB  1 
ATOM   2407  C  CG  . ASN   A  1 305 ? -26.629 -8.679  -23.340  1.00 68.28  ? 606  ASN   A CG  1 
ATOM   2408  O  OD1 . ASN   A  1 305 ? -25.487 -9.163  -23.312  1.00 66.06  ? 606  ASN   A OD1 1 
ATOM   2409  N  ND2 . ASN   A  1 305 ? -27.119 -7.944  -22.347  1.00 75.56  ? 606  ASN   A ND2 1 
ATOM   2410  N  N   . SER   A  1 306 ? -28.739 -8.492  -27.545  1.00 40.86  ? 607  SER   A N   1 
ATOM   2411  C  CA  . SER   A  1 306 ? -29.470 -8.970  -28.714  1.00 52.60  ? 607  SER   A CA  1 
ATOM   2412  C  C   . SER   A  1 306 ? -28.819 -8.591  -30.043  1.00 56.73  ? 607  SER   A C   1 
ATOM   2413  O  O   . SER   A  1 306 ? -29.352 -8.982  -31.082  1.00 51.81  ? 607  SER   A O   1 
ATOM   2414  C  CB  . SER   A  1 306 ? -30.908 -8.432  -28.710  1.00 58.39  ? 607  SER   A CB  1 
ATOM   2415  O  OG  . SER   A  1 306 ? -31.623 -8.816  -27.545  1.00 72.11  ? 607  SER   A OG  1 
ATOM   2416  N  N   . ARG   A  1 307 ? -27.714 -7.857  -30.050  1.00 56.23  ? 608  ARG   A N   1 
ATOM   2417  C  CA  . ARG   A  1 307 ? -27.079 -7.382  -31.282  1.00 57.30  ? 608  ARG   A CA  1 
ATOM   2418  C  C   . ARG   A  1 307 ? -25.751 -8.103  -31.468  1.00 53.93  ? 608  ARG   A C   1 
ATOM   2419  O  O   . ARG   A  1 307 ? -25.731 -9.337  -31.367  1.00 61.70  ? 608  ARG   A O   1 
ATOM   2420  C  CB  . ARG   A  1 307 ? -27.011 -5.858  -31.247  1.00 56.91  ? 608  ARG   A CB  1 
ATOM   2421  C  CG  . ARG   A  1 307 ? -28.383 -5.178  -31.231  1.00 51.08  ? 608  ARG   A CG  1 
ATOM   2422  C  CD  . ARG   A  1 307 ? -29.203 -5.452  -32.507  1.00 50.49  ? 608  ARG   A CD  1 
ATOM   2423  N  NE  . ARG   A  1 307 ? -28.495 -5.080  -33.732  1.00 51.41  ? 608  ARG   A NE  1 
ATOM   2424  C  CZ  . ARG   A  1 307 ? -28.203 -3.831  -34.088  1.00 49.46  ? 608  ARG   A CZ  1 
ATOM   2425  N  NH1 . ARG   A  1 307 ? -28.529 -2.800  -33.309  1.00 39.26  ? 608  ARG   A NH1 1 
ATOM   2426  N  NH2 . ARG   A  1 307 ? -27.553 -3.610  -35.221  1.00 45.03  ? 608  ARG   A NH2 1 
ATOM   2427  N  N   . TYR   A  1 308 ? -24.633 -7.417  -31.760  1.00 42.81  ? 609  TYR   A N   1 
ATOM   2428  C  CA  . TYR   A  1 308 ? -23.397 -8.145  -32.046  1.00 43.66  ? 609  TYR   A CA  1 
ATOM   2429  C  C   . TYR   A  1 308 ? -22.688 -8.635  -30.793  1.00 54.72  ? 609  TYR   A C   1 
ATOM   2430  O  O   . TYR   A  1 308 ? -21.818 -9.505  -30.905  1.00 63.53  ? 609  TYR   A O   1 
ATOM   2431  C  CB  . TYR   A  1 308 ? -22.426 -7.297  -32.870  1.00 46.21  ? 609  TYR   A CB  1 
ATOM   2432  C  CG  . TYR   A  1 308 ? -22.613 -7.461  -34.366  1.00 52.82  ? 609  TYR   A CG  1 
ATOM   2433  C  CD1 . TYR   A  1 308 ? -23.573 -6.716  -35.055  1.00 52.53  ? 609  TYR   A CD1 1 
ATOM   2434  C  CD2 . TYR   A  1 308 ? -21.825 -8.359  -35.092  1.00 48.12  ? 609  TYR   A CD2 1 
ATOM   2435  C  CE1 . TYR   A  1 308 ? -23.746 -6.863  -36.438  1.00 50.50  ? 609  TYR   A CE1 1 
ATOM   2436  C  CE2 . TYR   A  1 308 ? -21.991 -8.511  -36.465  1.00 42.53  ? 609  TYR   A CE2 1 
ATOM   2437  C  CZ  . TYR   A  1 308 ? -22.958 -7.766  -37.124  1.00 49.32  ? 609  TYR   A CZ  1 
ATOM   2438  O  OH  . TYR   A  1 308 ? -23.125 -7.914  -38.477  1.00 56.07  ? 609  TYR   A OH  1 
ATOM   2439  N  N   . ASN   A  1 309 ? -23.009 -8.069  -29.624  1.00 44.65  ? 610  ASN   A N   1 
ATOM   2440  C  CA  . ASN   A  1 309 ? -22.650 -8.639  -28.317  1.00 53.25  ? 610  ASN   A CA  1 
ATOM   2441  C  C   . ASN   A  1 309 ? -21.144 -8.931  -28.176  1.00 54.00  ? 610  ASN   A C   1 
ATOM   2442  O  O   . ASN   A  1 309 ? -20.727 -10.034 -27.804  1.00 44.02  ? 610  ASN   A O   1 
ATOM   2443  C  CB  . ASN   A  1 309 ? -23.484 -9.895  -28.048  1.00 46.72  ? 610  ASN   A CB  1 
ATOM   2444  C  CG  . ASN   A  1 309 ? -23.468 -10.296 -26.604  1.00 48.08  ? 610  ASN   A CG  1 
ATOM   2445  O  OD1 . ASN   A  1 309 ? -23.449 -9.450  -25.713  1.00 57.39  ? 610  ASN   A OD1 1 
ATOM   2446  N  ND2 . ASN   A  1 309 ? -23.455 -11.592 -26.358  1.00 43.95  ? 610  ASN   A ND2 1 
ATOM   2447  N  N   . ILE   A  1 310 ? -20.314 -7.913  -28.432  1.00 53.77  ? 611  ILE   A N   1 
ATOM   2448  C  CA  . ILE   A  1 310 ? -18.866 -8.106  -28.441  1.00 52.27  ? 611  ILE   A CA  1 
ATOM   2449  C  C   . ILE   A  1 310 ? -18.195 -7.681  -27.140  1.00 54.46  ? 611  ILE   A C   1 
ATOM   2450  O  O   . ILE   A  1 310 ? -16.957 -7.713  -27.063  1.00 55.59  ? 611  ILE   A O   1 
ATOM   2451  C  CB  . ILE   A  1 310 ? -18.209 -7.377  -29.629  1.00 60.16  ? 611  ILE   A CB  1 
ATOM   2452  C  CG1 . ILE   A  1 310 ? -18.152 -5.867  -29.384  1.00 62.31  ? 611  ILE   A CG1 1 
ATOM   2453  C  CG2 . ILE   A  1 310 ? -18.963 -7.653  -30.927  1.00 58.29  ? 611  ILE   A CG2 1 
ATOM   2454  C  CD1 . ILE   A  1 310 ? -17.105 -5.168  -30.231  1.00 58.29  ? 611  ILE   A CD1 1 
ATOM   2455  N  N   . LEU   A  1 311 ? -18.965 -7.272  -26.118  1.00 39.31  ? 612  LEU   A N   1 
ATOM   2456  C  CA  . LEU   A  1 311 ? -18.358 -6.891  -24.844  1.00 42.80  ? 612  LEU   A CA  1 
ATOM   2457  C  C   . LEU   A  1 311 ? -17.446 -7.997  -24.320  1.00 50.31  ? 612  LEU   A C   1 
ATOM   2458  O  O   . LEU   A  1 311 ? -16.265 -7.763  -24.037  1.00 53.54  ? 612  LEU   A O   1 
ATOM   2459  C  CB  . LEU   A  1 311 ? -19.439 -6.560  -23.808  1.00 40.32  ? 612  LEU   A CB  1 
ATOM   2460  C  CG  . LEU   A  1 311 ? -20.079 -5.190  -23.983  1.00 37.81  ? 612  LEU   A CG  1 
ATOM   2461  C  CD1 . LEU   A  1 311 ? -21.304 -4.987  -23.087  1.00 37.93  ? 612  LEU   A CD1 1 
ATOM   2462  C  CD2 . LEU   A  1 311 ? -19.034 -4.115  -23.763  1.00 35.60  ? 612  LEU   A CD2 1 
ATOM   2463  N  N   . GLU   A  1 312 ? -17.981 -9.216  -24.206  1.00 53.05  ? 613  GLU   A N   1 
ATOM   2464  C  CA  . GLU   A  1 312 ? -17.214 -10.325 -23.643  1.00 59.61  ? 613  GLU   A CA  1 
ATOM   2465  C  C   . GLU   A  1 312 ? -15.923 -10.554 -24.421  1.00 64.67  ? 613  GLU   A C   1 
ATOM   2466  O  O   . GLU   A  1 312 ? -14.858 -10.772 -23.829  1.00 64.34  ? 613  GLU   A O   1 
ATOM   2467  C  CB  . GLU   A  1 312 ? -18.085 -11.581 -23.637  1.00 67.99  ? 613  GLU   A CB  1 
ATOM   2468  C  CG  . GLU   A  1 312 ? -17.491 -12.762 -22.918  1.00 81.37  ? 613  GLU   A CG  1 
ATOM   2469  C  CD  . GLU   A  1 312 ? -18.518 -13.842 -22.651  1.00 86.88  ? 613  GLU   A CD  1 
ATOM   2470  O  OE1 . GLU   A  1 312 ? -19.723 -13.575 -22.868  1.00 90.16  ? 613  GLU   A OE1 1 
ATOM   2471  O  OE2 . GLU   A  1 312 ? -18.118 -14.948 -22.225  1.00 79.96  ? 613  GLU   A OE2 1 
ATOM   2472  N  N   . GLU   A  1 313 ? -16.001 -10.469 -25.753  1.00 61.72  ? 614  GLU   A N   1 
ATOM   2473  C  CA  . GLU   A  1 313 ? -14.830 -10.662 -26.598  1.00 64.02  ? 614  GLU   A CA  1 
ATOM   2474  C  C   . GLU   A  1 313 ? -13.755 -9.619  -26.315  1.00 56.46  ? 614  GLU   A C   1 
ATOM   2475  O  O   . GLU   A  1 313 ? -12.565 -9.946  -26.227  1.00 61.16  ? 614  GLU   A O   1 
ATOM   2476  C  CB  . GLU   A  1 313 ? -15.257 -10.602 -28.064  1.00 69.00  ? 614  GLU   A CB  1 
ATOM   2477  C  CG  . GLU   A  1 313 ? -15.019 -11.864 -28.843  1.00 71.87  ? 614  GLU   A CG  1 
ATOM   2478  C  CD  . GLU   A  1 313 ? -13.754 -11.785 -29.653  1.00 83.23  ? 614  GLU   A CD  1 
ATOM   2479  O  OE1 . GLU   A  1 313 ? -12.748 -11.282 -29.108  1.00 90.95  ? 614  GLU   A OE1 1 
ATOM   2480  O  OE2 . GLU   A  1 313 ? -13.768 -12.204 -30.835  1.00 83.88  ? 614  GLU   A OE2 1 
ATOM   2481  N  N   . VAL   A  1 314 ? -14.157 -8.358  -26.179  1.00 50.65  ? 615  VAL   A N   1 
ATOM   2482  C  CA  . VAL   A  1 314 ? -13.204 -7.265  -26.035  1.00 46.44  ? 615  VAL   A CA  1 
ATOM   2483  C  C   . VAL   A  1 314 ? -12.618 -7.246  -24.635  1.00 54.22  ? 615  VAL   A C   1 
ATOM   2484  O  O   . VAL   A  1 314 ? -11.421 -6.998  -24.452  1.00 54.64  ? 615  VAL   A O   1 
ATOM   2485  C  CB  . VAL   A  1 314 ? -13.898 -5.939  -26.398  1.00 50.68  ? 615  VAL   A CB  1 
ATOM   2486  C  CG1 . VAL   A  1 314 ? -13.053 -4.744  -25.984  1.00 50.50  ? 615  VAL   A CG1 1 
ATOM   2487  C  CG2 . VAL   A  1 314 ? -14.201 -5.891  -27.920  1.00 55.06  ? 615  VAL   A CG2 1 
ATOM   2488  N  N   . ALA   A  1 315 ? -13.451 -7.516  -23.629  1.00 53.10  ? 616  ALA   A N   1 
ATOM   2489  C  CA  . ALA   A  1 315 ? -12.958 -7.591  -22.262  1.00 46.83  ? 616  ALA   A CA  1 
ATOM   2490  C  C   . ALA   A  1 315 ? -11.920 -8.695  -22.126  1.00 56.98  ? 616  ALA   A C   1 
ATOM   2491  O  O   . ALA   A  1 315 ? -10.885 -8.503  -21.478  1.00 53.36  ? 616  ALA   A O   1 
ATOM   2492  C  CB  . ALA   A  1 315 ? -14.128 -7.802  -21.303  1.00 43.69  ? 616  ALA   A CB  1 
ATOM   2493  N  N   . LYS   A  1 316 ? -12.157 -9.846  -22.766  1.00 63.31  ? 617  LYS   A N   1 
ATOM   2494  C  CA  . LYS   A  1 316 ? -11.180 -10.931 -22.735  1.00 69.82  ? 617  LYS   A CA  1 
ATOM   2495  C  C   . LYS   A  1 316 ? -9.822  -10.455 -23.237  1.00 68.23  ? 617  LYS   A C   1 
ATOM   2496  O  O   . LYS   A  1 316 ? -8.803  -10.601 -22.554  1.00 60.93  ? 617  LYS   A O   1 
ATOM   2497  C  CB  . LYS   A  1 316 ? -11.665 -12.112 -23.577  1.00 71.84  ? 617  LYS   A CB  1 
ATOM   2498  C  CG  . LYS   A  1 316 ? -12.568 -13.098 -22.872  1.00 77.56  ? 617  LYS   A CG  1 
ATOM   2499  C  CD  . LYS   A  1 316 ? -13.200 -14.035 -23.897  1.00 80.92  ? 617  LYS   A CD  1 
ATOM   2500  C  CE  . LYS   A  1 316 ? -13.769 -15.290 -23.255  1.00 80.37  ? 617  LYS   A CE  1 
ATOM   2501  N  NZ  . LYS   A  1 316 ? -14.894 -14.984 -22.335  1.00 76.64  ? 617  LYS   A NZ  1 
ATOM   2502  N  N   . LYS   A  1 317 ? -9.794  -9.882  -24.444  1.00 63.63  ? 618  LYS   A N   1 
ATOM   2503  C  CA  . LYS   A  1 317 ? -8.539  -9.362  -24.971  1.00 61.83  ? 618  LYS   A CA  1 
ATOM   2504  C  C   . LYS   A  1 317 ? -7.982  -8.254  -24.087  1.00 65.62  ? 618  LYS   A C   1 
ATOM   2505  O  O   . LYS   A  1 317 ? -6.768  -8.027  -24.072  1.00 71.42  ? 618  LYS   A O   1 
ATOM   2506  C  CB  . LYS   A  1 317 ? -8.731  -8.839  -26.395  1.00 55.23  ? 618  LYS   A CB  1 
ATOM   2507  C  CG  . LYS   A  1 317 ? -9.433  -9.797  -27.343  1.00 60.90  ? 618  LYS   A CG  1 
ATOM   2508  C  CD  . LYS   A  1 317 ? -8.536  -10.194 -28.495  1.00 52.52  ? 618  LYS   A CD  1 
ATOM   2509  C  CE  . LYS   A  1 317 ? -8.438  -11.705 -28.580  1.00 64.46  ? 618  LYS   A CE  1 
ATOM   2510  N  NZ  . LYS   A  1 317 ? -7.490  -12.191 -29.634  1.00 68.33  ? 618  LYS   A NZ  1 
ATOM   2511  N  N   . MET   A  1 318 ? -8.846  -7.540  -23.361  1.00 58.84  ? 619  MET   A N   1 
ATOM   2512  C  CA  . MET   A  1 318 ? -8.356  -6.485  -22.483  1.00 59.55  ? 619  MET   A CA  1 
ATOM   2513  C  C   . MET   A  1 318 ? -7.771  -7.036  -21.196  1.00 62.19  ? 619  MET   A C   1 
ATOM   2514  O  O   . MET   A  1 318 ? -7.106  -6.287  -20.476  1.00 65.63  ? 619  MET   A O   1 
ATOM   2515  C  CB  . MET   A  1 318 ? -9.468  -5.480  -22.154  1.00 53.90  ? 619  MET   A CB  1 
ATOM   2516  C  CG  . MET   A  1 318 ? -9.753  -4.496  -23.287  1.00 50.01  ? 619  MET   A CG  1 
ATOM   2517  S  SD  . MET   A  1 318 ? -10.993 -3.234  -22.927  1.00 54.66  ? 619  MET   A SD  1 
ATOM   2518  C  CE  . MET   A  1 318 ? -10.171 -2.364  -21.588  1.00 45.17  ? 619  MET   A CE  1 
ATOM   2519  N  N   . ASN   A  1 319 ? -8.000  -8.319  -20.908  1.00 64.08  ? 620  ASN   A N   1 
ATOM   2520  C  CA  . ASN   A  1 319 ? -7.547  -8.981  -19.685  1.00 73.82  ? 620  ASN   A CA  1 
ATOM   2521  C  C   . ASN   A  1 319 ? -8.300  -8.506  -18.440  1.00 70.49  ? 620  ASN   A C   1 
ATOM   2522  O  O   . ASN   A  1 319 ? -7.716  -8.422  -17.361  1.00 66.77  ? 620  ASN   A O   1 
ATOM   2523  C  CB  . ASN   A  1 319 ? -6.041  -8.802  -19.475  1.00 76.47  ? 620  ASN   A CB  1 
ATOM   2524  C  CG  . ASN   A  1 319 ? -5.264  -9.957  -19.972  1.00 80.59  ? 620  ASN   A CG  1 
ATOM   2525  O  OD1 . ASN   A  1 319 ? -5.233  -11.008 -19.334  1.00 91.48  ? 620  ASN   A OD1 1 
ATOM   2526  N  ND2 . ASN   A  1 319 ? -4.609  -9.783  -21.117  1.00 80.50  ? 620  ASN   A ND2 1 
ATOM   2527  N  N   . LEU   A  1 320 ? -9.592  -8.207  -18.558  1.00 64.65  ? 621  LEU   A N   1 
ATOM   2528  C  CA  . LEU   A  1 320 ? -10.354 -7.697  -17.427  1.00 63.85  ? 621  LEU   A CA  1 
ATOM   2529  C  C   . LEU   A  1 320 ? -10.867 -8.845  -16.569  1.00 68.29  ? 621  LEU   A C   1 
ATOM   2530  O  O   . LEU   A  1 320 ? -11.090 -9.960  -17.056  1.00 68.61  ? 621  LEU   A O   1 
ATOM   2531  C  CB  . LEU   A  1 320 ? -11.524 -6.848  -17.919  1.00 64.76  ? 621  LEU   A CB  1 
ATOM   2532  C  CG  . LEU   A  1 320 ? -11.137 -5.638  -18.768  1.00 59.00  ? 621  LEU   A CG  1 
ATOM   2533  C  CD1 . LEU   A  1 320 ? -12.380 -4.897  -19.218  1.00 47.02  ? 621  LEU   A CD1 1 
ATOM   2534  C  CD2 . LEU   A  1 320 ? -10.217 -4.724  -17.974  1.00 61.30  ? 621  LEU   A CD2 1 
ATOM   2535  N  N   . ASP   A  1 321 ? -11.024 -8.571  -15.271  1.00 68.00  ? 622  ASP   A N   1 
ATOM   2536  C  CA  . ASP   A  1 321 ? -11.667 -9.521  -14.370  1.00 60.51  ? 622  ASP   A CA  1 
ATOM   2537  C  C   . ASP   A  1 321 ? -13.153 -9.546  -14.673  1.00 56.98  ? 622  ASP   A C   1 
ATOM   2538  O  O   . ASP   A  1 321 ? -13.863 -8.563  -14.437  1.00 63.78  ? 622  ASP   A O   1 
ATOM   2539  C  CB  . ASP   A  1 321 ? -11.438 -9.150  -12.910  1.00 72.28  ? 622  ASP   A CB  1 
ATOM   2540  C  CG  . ASP   A  1 321 ? -12.297 -9.980  -11.967  1.00 82.64  ? 622  ASP   A CG  1 
ATOM   2541  O  OD1 . ASP   A  1 321 ? -12.539 -11.171 -12.277  1.00 84.98  ? 622  ASP   A OD1 1 
ATOM   2542  O  OD2 . ASP   A  1 321 ? -12.756 -9.440  -10.937  1.00 89.74  ? 622  ASP   A OD2 1 
ATOM   2543  N  N   . MET   A  1 322 ? -13.632 -10.664 -15.202  1.00 60.44  ? 623  MET   A N   1 
ATOM   2544  C  CA  . MET   A  1 322 ? -15.025 -10.772 -15.599  1.00 63.69  ? 623  MET   A CA  1 
ATOM   2545  C  C   . MET   A  1 322 ? -15.816 -11.669 -14.658  1.00 68.67  ? 623  MET   A C   1 
ATOM   2546  O  O   . MET   A  1 322 ? -16.941 -12.063 -14.979  1.00 70.92  ? 623  MET   A O   1 
ATOM   2547  C  CB  . MET   A  1 322 ? -15.111 -11.265 -17.037  1.00 58.47  ? 623  MET   A CB  1 
ATOM   2548  C  CG  . MET   A  1 322 ? -14.400 -10.339 -18.016  1.00 64.73  ? 623  MET   A CG  1 
ATOM   2549  S  SD  . MET   A  1 322 ? -14.253 -10.997 -19.694  1.00 65.95  ? 623  MET   A SD  1 
ATOM   2550  C  CE  . MET   A  1 322 ? -15.916 -11.584 -19.954  1.00 64.43  ? 623  MET   A CE  1 
ATOM   2551  N  N   . ARG   A  1 323 ? -15.247 -11.987 -13.493  1.00 69.41  ? 624  ARG   A N   1 
ATOM   2552  C  CA  . ARG   A  1 323 ? -15.934 -12.834 -12.527  1.00 78.57  ? 624  ARG   A CA  1 
ATOM   2553  C  C   . ARG   A  1 323 ? -17.006 -12.083 -11.747  1.00 81.45  ? 624  ARG   A C   1 
ATOM   2554  O  O   . ARG   A  1 323 ? -17.971 -12.704 -11.290  1.00 89.79  ? 624  ARG   A O   1 
ATOM   2555  C  CB  . ARG   A  1 323 ? -14.927 -13.450 -11.558  1.00 85.41  ? 624  ARG   A CB  1 
ATOM   2556  C  CG  . ARG   A  1 323 ? -14.111 -14.594 -12.143  1.00 87.97  ? 624  ARG   A CG  1 
ATOM   2557  C  CD  . ARG   A  1 323 ? -12.924 -14.897 -11.256  1.00 95.10  ? 624  ARG   A CD  1 
ATOM   2558  N  NE  . ARG   A  1 323 ? -12.156 -13.682 -10.997  1.00 99.62  ? 624  ARG   A NE  1 
ATOM   2559  C  CZ  . ARG   A  1 323 ? -11.128 -13.602 -10.159  1.00 101.65 ? 624  ARG   A CZ  1 
ATOM   2560  N  NH1 . ARG   A  1 323 ? -10.730 -14.676 -9.486   1.00 99.55  ? 624  ARG   A NH1 1 
ATOM   2561  N  NH2 . ARG   A  1 323 ? -10.497 -12.444 -9.996   1.00 102.91 ? 624  ARG   A NH2 1 
ATOM   2562  N  N   . LYS   A  1 324 ? -16.868 -10.769 -11.573  1.00 76.20  ? 625  LYS   A N   1 
ATOM   2563  C  CA  . LYS   A  1 324 ? -17.854 -9.996  -10.830  1.00 79.07  ? 625  LYS   A CA  1 
ATOM   2564  C  C   . LYS   A  1 324 ? -18.156 -8.696  -11.558  1.00 74.87  ? 625  LYS   A C   1 
ATOM   2565  O  O   . LYS   A  1 324 ? -17.246 -8.021  -12.050  1.00 74.29  ? 625  LYS   A O   1 
ATOM   2566  C  CB  . LYS   A  1 324 ? -17.381 -9.701  -9.392   1.00 84.92  ? 625  LYS   A CB  1 
ATOM   2567  C  CG  . LYS   A  1 324 ? -15.950 -9.194  -9.285   1.00 87.92  ? 625  LYS   A CG  1 
ATOM   2568  C  CD  . LYS   A  1 324 ? -15.578 -8.888  -7.841   1.00 89.61  ? 625  LYS   A CD  1 
ATOM   2569  C  CE  . LYS   A  1 324 ? -14.067 -8.787  -7.667   1.00 87.91  ? 625  LYS   A CE  1 
ATOM   2570  N  NZ  . LYS   A  1 324 ? -13.448 -7.856  -8.653   1.00 82.47  ? 625  LYS   A NZ  1 
ATOM   2571  N  N   . THR   A  1 325 ? -19.450 -8.355  -11.612  1.00 70.31  ? 626  THR   A N   1 
ATOM   2572  C  CA  . THR   A  1 325 ? -19.895 -7.145  -12.301  1.00 62.29  ? 626  THR   A CA  1 
ATOM   2573  C  C   . THR   A  1 325 ? -19.236 -5.898  -11.739  1.00 58.53  ? 626  THR   A C   1 
ATOM   2574  O  O   . THR   A  1 325 ? -18.962 -4.950  -12.484  1.00 56.17  ? 626  THR   A O   1 
ATOM   2575  C  CB  . THR   A  1 325 ? -21.415 -7.000  -12.189  1.00 58.08  ? 626  THR   A CB  1 
ATOM   2576  O  OG1 . THR   A  1 325 ? -21.797 -7.136  -10.811  1.00 60.85  ? 626  THR   A OG1 1 
ATOM   2577  C  CG2 . THR   A  1 325 ? -22.145 -8.046  -13.024  1.00 44.29  ? 626  THR   A CG2 1 
ATOM   2578  N  N   . SER   A  1 326 ? -18.992 -5.874  -10.431  1.00 60.82  ? 627  SER   A N   1 
ATOM   2579  C  CA  . SER   A  1 326 ? -18.483 -4.680  -9.773   1.00 60.45  ? 627  SER   A CA  1 
ATOM   2580  C  C   . SER   A  1 326 ? -17.079 -4.304  -10.222  1.00 53.10  ? 627  SER   A C   1 
ATOM   2581  O  O   . SER   A  1 326 ? -16.617 -3.214  -9.876   1.00 54.09  ? 627  SER   A O   1 
ATOM   2582  C  CB  . SER   A  1 326 ? -18.525 -4.854  -8.248   1.00 55.56  ? 627  SER   A CB  1 
ATOM   2583  O  OG  . SER   A  1 326 ? -18.080 -6.139  -7.849   1.00 61.87  ? 627  SER   A OG  1 
ATOM   2584  N  N   . SER   A  1 327 ? -16.390 -5.163  -10.976  1.00 50.95  ? 628  SER   A N   1 
ATOM   2585  C  CA  . SER   A  1 327 ? -15.160 -4.722  -11.630  1.00 50.80  ? 628  SER   A CA  1 
ATOM   2586  C  C   . SER   A  1 327 ? -15.432 -3.709  -12.729  1.00 54.26  ? 628  SER   A C   1 
ATOM   2587  O  O   . SER   A  1 327 ? -14.499 -3.028  -13.169  1.00 59.03  ? 628  SER   A O   1 
ATOM   2588  C  CB  . SER   A  1 327 ? -14.397 -5.909  -12.223  1.00 44.95  ? 628  SER   A CB  1 
ATOM   2589  O  OG  . SER   A  1 327 ? -15.016 -6.374  -13.409  1.00 55.02  ? 628  SER   A OG  1 
ATOM   2590  N  N   . LEU   A  1 328 ? -16.686 -3.598  -13.170  1.00 49.60  ? 629  LEU   A N   1 
ATOM   2591  C  CA  . LEU   A  1 328 ? -17.078 -2.708  -14.262  1.00 49.41  ? 629  LEU   A CA  1 
ATOM   2592  C  C   . LEU   A  1 328 ? -16.339 -3.044  -15.552  1.00 47.77  ? 629  LEU   A C   1 
ATOM   2593  O  O   . LEU   A  1 328 ? -16.021 -2.160  -16.358  1.00 48.01  ? 629  LEU   A O   1 
ATOM   2594  C  CB  . LEU   A  1 328 ? -16.880 -1.242  -13.882  1.00 48.90  ? 629  LEU   A CB  1 
ATOM   2595  C  CG  . LEU   A  1 328 ? -17.716 -0.806  -12.678  1.00 45.28  ? 629  LEU   A CG  1 
ATOM   2596  C  CD1 . LEU   A  1 328 ? -17.738 0.698   -12.569  1.00 38.24  ? 629  LEU   A CD1 1 
ATOM   2597  C  CD2 . LEU   A  1 328 ? -19.126 -1.343  -12.808  1.00 43.33  ? 629  LEU   A CD2 1 
ATOM   2598  N  N   . TRP   A  1 329 ? -16.058 -4.331  -15.755  1.00 51.09  ? 630  TRP   A N   1 
ATOM   2599  C  CA  . TRP   A  1 329 ? -15.386 -4.734  -16.982  1.00 49.50  ? 630  TRP   A CA  1 
ATOM   2600  C  C   . TRP   A  1 329 ? -16.227 -4.376  -18.205  1.00 50.54  ? 630  TRP   A C   1 
ATOM   2601  O  O   . TRP   A  1 329 ? -15.683 -3.971  -19.233  1.00 54.95  ? 630  TRP   A O   1 
ATOM   2602  C  CB  . TRP   A  1 329 ? -15.056 -6.225  -16.951  1.00 41.98  ? 630  TRP   A CB  1 
ATOM   2603  C  CG  . TRP   A  1 329 ? -16.231 -7.155  -16.863  1.00 47.87  ? 630  TRP   A CG  1 
ATOM   2604  C  CD1 . TRP   A  1 329 ? -16.788 -7.664  -15.727  1.00 53.86  ? 630  TRP   A CD1 1 
ATOM   2605  C  CD2 . TRP   A  1 329 ? -16.963 -7.724  -17.955  1.00 49.41  ? 630  TRP   A CD2 1 
ATOM   2606  N  NE1 . TRP   A  1 329 ? -17.834 -8.500  -16.043  1.00 49.66  ? 630  TRP   A NE1 1 
ATOM   2607  C  CE2 . TRP   A  1 329 ? -17.964 -8.551  -17.404  1.00 51.82  ? 630  TRP   A CE2 1 
ATOM   2608  C  CE3 . TRP   A  1 329 ? -16.879 -7.607  -19.344  1.00 48.68  ? 630  TRP   A CE3 1 
ATOM   2609  C  CZ2 . TRP   A  1 329 ? -18.878 -9.254  -18.199  1.00 47.35  ? 630  TRP   A CZ2 1 
ATOM   2610  C  CZ3 . TRP   A  1 329 ? -17.785 -8.305  -20.128  1.00 47.49  ? 630  TRP   A CZ3 1 
ATOM   2611  C  CH2 . TRP   A  1 329 ? -18.764 -9.122  -19.554  1.00 45.15  ? 630  TRP   A CH2 1 
ATOM   2612  N  N   . LYS   A  1 330 ? -17.557 -4.484  -18.097  1.00 50.08  ? 631  LYS   A N   1 
ATOM   2613  C  CA  . LYS   A  1 330 ? -18.435 -4.110  -19.204  1.00 52.74  ? 631  LYS   A CA  1 
ATOM   2614  C  C   . LYS   A  1 330 ? -18.293 -2.638  -19.552  1.00 55.57  ? 631  LYS   A C   1 
ATOM   2615  O  O   . LYS   A  1 330 ? -18.137 -2.276  -20.728  1.00 52.21  ? 631  LYS   A O   1 
ATOM   2616  C  CB  . LYS   A  1 330 ? -19.890 -4.424  -18.864  1.00 46.54  ? 631  LYS   A CB  1 
ATOM   2617  C  CG  . LYS   A  1 330 ? -20.226 -5.887  -18.991  1.00 54.00  ? 631  LYS   A CG  1 
ATOM   2618  C  CD  . LYS   A  1 330 ? -21.683 -6.148  -18.707  1.00 53.97  ? 631  LYS   A CD  1 
ATOM   2619  C  CE  . LYS   A  1 330 ? -22.077 -7.512  -19.226  1.00 52.28  ? 631  LYS   A CE  1 
ATOM   2620  N  NZ  . LYS   A  1 330 ? -23.473 -7.846  -18.878  1.00 54.50  ? 631  LYS   A NZ  1 
ATOM   2621  N  N   . ASP   A  1 331 ? -18.371 -1.771  -18.537  1.00 53.77  ? 632  ASP   A N   1 
ATOM   2622  C  CA  . ASP   A  1 331 ? -18.253 -0.336  -18.775  1.00 48.83  ? 632  ASP   A CA  1 
ATOM   2623  C  C   . ASP   A  1 331 ? -16.904 -0.004  -19.395  1.00 47.07  ? 632  ASP   A C   1 
ATOM   2624  O  O   . ASP   A  1 331 ? -16.812 0.852   -20.285  1.00 41.02  ? 632  ASP   A O   1 
ATOM   2625  C  CB  . ASP   A  1 331 ? -18.440 0.443   -17.466  1.00 48.62  ? 632  ASP   A CB  1 
ATOM   2626  C  CG  . ASP   A  1 331 ? -19.599 -0.090  -16.611  1.00 40.98  ? 632  ASP   A CG  1 
ATOM   2627  O  OD1 . ASP   A  1 331 ? -19.502 -1.227  -16.112  1.00 38.91  ? 632  ASP   A OD1 1 
ATOM   2628  O  OD2 . ASP   A  1 331 ? -20.604 0.629   -16.438  1.00 43.55  ? 632  ASP   A OD2 1 
ATOM   2629  N  N   . GLN   A  1 332 ? -15.847 -0.688  -18.938  1.00 43.69  ? 633  GLN   A N   1 
ATOM   2630  C  CA  . GLN   A  1 332 ? -14.498 -0.407  -19.411  1.00 40.59  ? 633  GLN   A CA  1 
ATOM   2631  C  C   . GLN   A  1 332 ? -14.337 -0.789  -20.877  1.00 48.31  ? 633  GLN   A C   1 
ATOM   2632  O  O   . GLN   A  1 332 ? -13.879 0.018   -21.696  1.00 49.70  ? 633  GLN   A O   1 
ATOM   2633  C  CB  . GLN   A  1 332 ? -13.491 -1.161  -18.557  1.00 38.68  ? 633  GLN   A CB  1 
ATOM   2634  C  CG  . GLN   A  1 332 ? -12.445 -0.300  -17.906  1.00 47.46  ? 633  GLN   A CG  1 
ATOM   2635  C  CD  . GLN   A  1 332 ? -11.635 -1.087  -16.889  1.00 58.20  ? 633  GLN   A CD  1 
ATOM   2636  O  OE1 . GLN   A  1 332 ? -11.984 -2.218  -16.545  1.00 61.23  ? 633  GLN   A OE1 1 
ATOM   2637  N  NE2 . GLN   A  1 332 ? -10.554 -0.493  -16.402  1.00 65.38  ? 633  GLN   A NE2 1 
ATOM   2638  N  N   . ALA   A  1 333 ? -14.709 -2.023  -21.223  1.00 42.15  ? 634  ALA   A N   1 
ATOM   2639  C  CA  . ALA   A  1 333 ? -14.618 -2.462  -22.605  1.00 52.95  ? 634  ALA   A CA  1 
ATOM   2640  C  C   . ALA   A  1 333 ? -15.521 -1.638  -23.519  1.00 52.60  ? 634  ALA   A C   1 
ATOM   2641  O  O   . ALA   A  1 333 ? -15.176 -1.415  -24.684  1.00 52.67  ? 634  ALA   A O   1 
ATOM   2642  C  CB  . ALA   A  1 333 ? -14.958 -3.951  -22.694  1.00 54.34  ? 634  ALA   A CB  1 
ATOM   2643  N  N   . LEU   A  1 334 ? -16.661 -1.158  -23.011  1.00 51.67  ? 635  LEU   A N   1 
ATOM   2644  C  CA  . LEU   A  1 334 ? -17.545 -0.344  -23.844  1.00 44.33  ? 635  LEU   A CA  1 
ATOM   2645  C  C   . LEU   A  1 334 ? -16.888 0.975   -24.245  1.00 47.79  ? 635  LEU   A C   1 
ATOM   2646  O  O   . LEU   A  1 334 ? -17.001 1.400   -25.408  1.00 34.20  ? 635  LEU   A O   1 
ATOM   2647  C  CB  . LEU   A  1 334 ? -18.868 -0.089  -23.126  1.00 42.45  ? 635  LEU   A CB  1 
ATOM   2648  C  CG  . LEU   A  1 334 ? -19.889 0.821   -23.821  1.00 44.58  ? 635  LEU   A CG  1 
ATOM   2649  C  CD1 . LEU   A  1 334 ? -20.642 0.120   -24.952  1.00 38.89  ? 635  LEU   A CD1 1 
ATOM   2650  C  CD2 . LEU   A  1 334 ? -20.858 1.358   -22.803  1.00 45.85  ? 635  LEU   A CD2 1 
ATOM   2651  N  N   . VAL   A  1 335 ? -16.191 1.642   -23.310  1.00 43.09  ? 636  VAL   A N   1 
ATOM   2652  C  CA  . VAL   A  1 335 ? -15.536 2.901   -23.673  1.00 41.45  ? 636  VAL   A CA  1 
ATOM   2653  C  C   . VAL   A  1 335 ? -14.518 2.669   -24.789  1.00 45.73  ? 636  VAL   A C   1 
ATOM   2654  O  O   . VAL   A  1 335 ? -14.448 3.440   -25.760  1.00 36.27  ? 636  VAL   A O   1 
ATOM   2655  C  CB  . VAL   A  1 335 ? -14.886 3.580   -22.453  1.00 41.65  ? 636  VAL   A CB  1 
ATOM   2656  C  CG1 . VAL   A  1 335 ? -14.252 4.890   -22.890  1.00 36.02  ? 636  VAL   A CG1 1 
ATOM   2657  C  CG2 . VAL   A  1 335 ? -15.924 3.859   -21.338  1.00 33.45  ? 636  VAL   A CG2 1 
ATOM   2658  N  N   . GLU   A  1 336 ? -13.728 1.596   -24.685  1.00 40.86  ? 637  GLU   A N   1 
ATOM   2659  C  CA  . GLU   A  1 336 ? -12.708 1.345   -25.701  1.00 46.21  ? 637  GLU   A CA  1 
ATOM   2660  C  C   . GLU   A  1 336 ? -13.327 1.075   -27.072  1.00 47.63  ? 637  GLU   A C   1 
ATOM   2661  O  O   . GLU   A  1 336 ? -12.815 1.546   -28.097  1.00 45.63  ? 637  GLU   A O   1 
ATOM   2662  C  CB  . GLU   A  1 336 ? -11.812 0.181   -25.282  1.00 46.16  ? 637  GLU   A CB  1 
ATOM   2663  C  CG  . GLU   A  1 336 ? -11.072 0.407   -23.973  1.00 53.87  ? 637  GLU   A CG  1 
ATOM   2664  C  CD  . GLU   A  1 336 ? -10.042 1.518   -24.067  1.00 54.86  ? 637  GLU   A CD  1 
ATOM   2665  O  OE1 . GLU   A  1 336 ? -9.835  2.091   -25.159  1.00 50.06  ? 637  GLU   A OE1 1 
ATOM   2666  O  OE2 . GLU   A  1 336 ? -9.425  1.820   -23.033  1.00 49.32  ? 637  GLU   A OE2 1 
ATOM   2667  N  N   . ILE   A  1 337 ? -14.407 0.292   -27.114  1.00 50.72  ? 638  ILE   A N   1 
ATOM   2668  C  CA  . ILE   A  1 337 ? -15.094 0.043   -28.375  1.00 44.08  ? 638  ILE   A CA  1 
ATOM   2669  C  C   . ILE   A  1 337 ? -15.530 1.359   -28.993  1.00 46.26  ? 638  ILE   A C   1 
ATOM   2670  O  O   . ILE   A  1 337 ? -15.376 1.581   -30.199  1.00 44.38  ? 638  ILE   A O   1 
ATOM   2671  C  CB  . ILE   A  1 337 ? -16.282 -0.912  -28.154  1.00 40.48  ? 638  ILE   A CB  1 
ATOM   2672  C  CG1 . ILE   A  1 337 ? -15.767 -2.297  -27.796  1.00 43.37  ? 638  ILE   A CG1 1 
ATOM   2673  C  CG2 . ILE   A  1 337 ? -17.181 -1.012  -29.403  1.00 32.23  ? 638  ILE   A CG2 1 
ATOM   2674  C  CD1 . ILE   A  1 337 ? -16.814 -3.175  -27.178  1.00 46.68  ? 638  ILE   A CD1 1 
ATOM   2675  N  N   . ASN   A  1 338 ? -16.039 2.272   -28.171  1.00 41.27  ? 639  ASN   A N   1 
ATOM   2676  C  CA  . ASN   A  1 338 ? -16.542 3.523   -28.709  1.00 39.37  ? 639  ASN   A CA  1 
ATOM   2677  C  C   . ASN   A  1 338 ? -15.417 4.474   -29.099  1.00 41.84  ? 639  ASN   A C   1 
ATOM   2678  O  O   . ASN   A  1 338 ? -15.611 5.325   -29.973  1.00 40.28  ? 639  ASN   A O   1 
ATOM   2679  C  CB  . ASN   A  1 338 ? -17.507 4.144   -27.706  1.00 38.63  ? 639  ASN   A CB  1 
ATOM   2680  C  CG  . ASN   A  1 338 ? -18.892 3.576   -27.847  1.00 40.85  ? 639  ASN   A CG  1 
ATOM   2681  O  OD1 . ASN   A  1 338 ? -19.734 4.137   -28.545  1.00 47.16  ? 639  ASN   A OD1 1 
ATOM   2682  N  ND2 . ASN   A  1 338 ? -19.124 2.430   -27.235  1.00 47.36  ? 639  ASN   A ND2 1 
ATOM   2683  N  N   . ILE   A  1 339 ? -14.246 4.343   -28.472  1.00 38.38  ? 640  ILE   A N   1 
ATOM   2684  C  CA  . ILE   A  1 339 ? -13.068 5.070   -28.924  1.00 38.43  ? 640  ILE   A CA  1 
ATOM   2685  C  C   . ILE   A  1 339 ? -12.649 4.565   -30.298  1.00 45.96  ? 640  ILE   A C   1 
ATOM   2686  O  O   . ILE   A  1 339 ? -12.387 5.353   -31.216  1.00 42.25  ? 640  ILE   A O   1 
ATOM   2687  C  CB  . ILE   A  1 339 ? -11.922 4.937   -27.902  1.00 35.77  ? 640  ILE   A CB  1 
ATOM   2688  C  CG1 . ILE   A  1 339 ? -12.200 5.783   -26.655  1.00 41.95  ? 640  ILE   A CG1 1 
ATOM   2689  C  CG2 . ILE   A  1 339 ? -10.594 5.333   -28.525  1.00 36.82  ? 640  ILE   A CG2 1 
ATOM   2690  C  CD1 . ILE   A  1 339 ? -11.154 5.645   -25.588  1.00 40.45  ? 640  ILE   A CD1 1 
ATOM   2691  N  N   . ALA   A  1 340 ? -12.612 3.237   -30.450  1.00 47.25  ? 641  ALA   A N   1 
ATOM   2692  C  CA  . ALA   A  1 340 ? -12.219 2.601   -31.701  1.00 51.16  ? 641  ALA   A CA  1 
ATOM   2693  C  C   . ALA   A  1 340 ? -13.107 3.043   -32.863  1.00 48.16  ? 641  ALA   A C   1 
ATOM   2694  O  O   . ALA   A  1 340 ? -12.613 3.308   -33.970  1.00 43.06  ? 641  ALA   A O   1 
ATOM   2695  C  CB  . ALA   A  1 340 ? -12.264 1.078   -31.539  1.00 41.26  ? 641  ALA   A CB  1 
ATOM   2696  N  N   . VAL   A  1 341 ? -14.420 3.104   -32.628  1.00 33.76  ? 642  VAL   A N   1 
ATOM   2697  C  CA  . VAL   A  1 341 ? -15.367 3.492   -33.668  1.00 40.70  ? 642  VAL   A CA  1 
ATOM   2698  C  C   . VAL   A  1 341 ? -15.099 4.918   -34.124  1.00 38.73  ? 642  VAL   A C   1 
ATOM   2699  O  O   . VAL   A  1 341 ? -14.969 5.181   -35.322  1.00 42.18  ? 642  VAL   A O   1 
ATOM   2700  C  CB  . VAL   A  1 341 ? -16.813 3.309   -33.172  1.00 38.51  ? 642  VAL   A CB  1 
ATOM   2701  C  CG1 . VAL   A  1 341 ? -17.809 3.897   -34.164  1.00 38.05  ? 642  VAL   A CG1 1 
ATOM   2702  C  CG2 . VAL   A  1 341 ? -17.100 1.825   -32.963  1.00 32.86  ? 642  VAL   A CG2 1 
ATOM   2703  N  N   . LEU   A  1 342 ? -14.983 5.856   -33.178  1.00 40.21  ? 643  LEU   A N   1 
ATOM   2704  C  CA  . LEU   A  1 342 ? -14.740 7.252   -33.546  1.00 41.66  ? 643  LEU   A CA  1 
ATOM   2705  C  C   . LEU   A  1 342 ? -13.388 7.422   -34.232  1.00 48.57  ? 643  LEU   A C   1 
ATOM   2706  O  O   . LEU   A  1 342 ? -13.261 8.186   -35.195  1.00 43.77  ? 643  LEU   A O   1 
ATOM   2707  C  CB  . LEU   A  1 342 ? -14.828 8.164   -32.316  1.00 36.85  ? 643  LEU   A CB  1 
ATOM   2708  C  CG  . LEU   A  1 342 ? -16.219 8.340   -31.699  1.00 37.88  ? 643  LEU   A CG  1 
ATOM   2709  C  CD1 . LEU   A  1 342 ? -16.161 8.766   -30.210  1.00 39.70  ? 643  LEU   A CD1 1 
ATOM   2710  C  CD2 . LEU   A  1 342 ? -17.033 9.325   -32.482  1.00 28.58  ? 643  LEU   A CD2 1 
ATOM   2711  N  N   . TYR   A  1 343 ? -12.362 6.733   -33.737  1.00 52.71  ? 644  TYR   A N   1 
ATOM   2712  C  CA  . TYR   A  1 343 ? -11.033 6.866   -34.317  1.00 44.49  ? 644  TYR   A CA  1 
ATOM   2713  C  C   . TYR   A  1 343 ? -10.999 6.321   -35.734  1.00 52.50  ? 644  TYR   A C   1 
ATOM   2714  O  O   . TYR   A  1 343 ? -10.287 6.843   -36.603  1.00 50.86  ? 644  TYR   A O   1 
ATOM   2715  C  CB  . TYR   A  1 343 ? -10.029 6.125   -33.447  1.00 37.28  ? 644  TYR   A CB  1 
ATOM   2716  C  CG  . TYR   A  1 343 ? -8.677  5.917   -34.077  1.00 35.49  ? 644  TYR   A CG  1 
ATOM   2717  C  CD1 . TYR   A  1 343 ? -7.797  6.970   -34.212  1.00 38.22  ? 644  TYR   A CD1 1 
ATOM   2718  C  CD2 . TYR   A  1 343 ? -8.267  4.656   -34.505  1.00 37.48  ? 644  TYR   A CD2 1 
ATOM   2719  C  CE1 . TYR   A  1 343 ? -6.556  6.794   -34.764  1.00 47.49  ? 644  TYR   A CE1 1 
ATOM   2720  C  CE2 . TYR   A  1 343 ? -7.014  4.466   -35.058  1.00 46.46  ? 644  TYR   A CE2 1 
ATOM   2721  C  CZ  . TYR   A  1 343 ? -6.162  5.547   -35.192  1.00 50.27  ? 644  TYR   A CZ  1 
ATOM   2722  O  OH  . TYR   A  1 343 ? -4.902  5.398   -35.739  1.00 56.68  ? 644  TYR   A OH  1 
ATOM   2723  N  N   . SER   A  1 344 ? -11.752 5.256   -35.978  1.00 49.72  ? 645  SER   A N   1 
ATOM   2724  C  CA  . SER   A  1 344 ? -11.705 4.618   -37.279  1.00 44.74  ? 645  SER   A CA  1 
ATOM   2725  C  C   . SER   A  1 344 ? -12.371 5.494   -38.328  1.00 42.66  ? 645  SER   A C   1 
ATOM   2726  O  O   . SER   A  1 344 ? -11.785 5.762   -39.383  1.00 40.60  ? 645  SER   A O   1 
ATOM   2727  C  CB  . SER   A  1 344 ? -12.354 3.243   -37.195  1.00 39.29  ? 645  SER   A CB  1 
ATOM   2728  O  OG  . SER   A  1 344 ? -11.482 2.345   -36.538  1.00 45.82  ? 645  SER   A OG  1 
ATOM   2729  N  N   . PHE   A  1 345 ? -13.588 5.965   -38.046  1.00 36.99  ? 646  PHE   A N   1 
ATOM   2730  C  CA  . PHE   A  1 345 ? -14.277 6.865   -38.970  1.00 38.48  ? 646  PHE   A CA  1 
ATOM   2731  C  C   . PHE   A  1 345 ? -13.458 8.118   -39.248  1.00 44.84  ? 646  PHE   A C   1 
ATOM   2732  O  O   . PHE   A  1 345 ? -13.365 8.566   -40.398  1.00 48.09  ? 646  PHE   A O   1 
ATOM   2733  C  CB  . PHE   A  1 345 ? -15.651 7.249   -38.414  1.00 34.83  ? 646  PHE   A CB  1 
ATOM   2734  C  CG  . PHE   A  1 345 ? -16.732 6.255   -38.725  1.00 37.01  ? 646  PHE   A CG  1 
ATOM   2735  C  CD1 . PHE   A  1 345 ? -16.613 4.928   -38.316  1.00 38.15  ? 646  PHE   A CD1 1 
ATOM   2736  C  CD2 . PHE   A  1 345 ? -17.876 6.650   -39.420  1.00 32.40  ? 646  PHE   A CD2 1 
ATOM   2737  C  CE1 . PHE   A  1 345 ? -17.611 4.001   -38.597  1.00 38.47  ? 646  PHE   A CE1 1 
ATOM   2738  C  CE2 . PHE   A  1 345 ? -18.876 5.739   -39.707  1.00 28.77  ? 646  PHE   A CE2 1 
ATOM   2739  C  CZ  . PHE   A  1 345 ? -18.746 4.405   -39.298  1.00 40.26  ? 646  PHE   A CZ  1 
ATOM   2740  N  N   . GLN   A  1 346 ? -12.854 8.700   -38.207  1.00 44.24  ? 647  GLN   A N   1 
ATOM   2741  C  CA  . GLN   A  1 346 ? -12.088 9.928   -38.399  1.00 43.62  ? 647  GLN   A CA  1 
ATOM   2742  C  C   . GLN   A  1 346 ? -10.850 9.682   -39.253  1.00 47.08  ? 647  GLN   A C   1 
ATOM   2743  O  O   . GLN   A  1 346 ? -10.463 10.535  -40.059  1.00 49.08  ? 647  GLN   A O   1 
ATOM   2744  C  CB  . GLN   A  1 346 ? -11.702 10.519  -37.042  1.00 41.14  ? 647  GLN   A CB  1 
ATOM   2745  C  CG  . GLN   A  1 346 ? -12.811 11.313  -36.389  1.00 39.61  ? 647  GLN   A CG  1 
ATOM   2746  C  CD  . GLN   A  1 346 ? -12.598 11.499  -34.882  1.00 52.81  ? 647  GLN   A CD  1 
ATOM   2747  O  OE1 . GLN   A  1 346 ? -13.486 11.984  -34.180  1.00 52.26  ? 647  GLN   A OE1 1 
ATOM   2748  N  NE2 . GLN   A  1 346 ? -11.423 11.116  -34.389  1.00 55.26  ? 647  GLN   A NE2 1 
ATOM   2749  N  N   . SER   A  1 347 ? -10.206 8.527   -39.079  1.00 46.37  ? 648  SER   A N   1 
ATOM   2750  C  CA  . SER   A  1 347 ? -8.997  8.236   -39.831  1.00 42.47  ? 648  SER   A CA  1 
ATOM   2751  C  C   . SER   A  1 347 ? -9.312  8.053   -41.314  1.00 55.09  ? 648  SER   A C   1 
ATOM   2752  O  O   . SER   A  1 347 ? -8.595  8.574   -42.176  1.00 46.98  ? 648  SER   A O   1 
ATOM   2753  C  CB  . SER   A  1 347 ? -8.309  6.998   -39.250  1.00 42.38  ? 648  SER   A CB  1 
ATOM   2754  O  OG  . SER   A  1 347 ? -7.751  7.273   -37.968  1.00 50.99  ? 648  SER   A OG  1 
ATOM   2755  N  N   . ASP   A  1 348 ? -10.397 7.345   -41.626  1.00 53.33  ? 649  ASP   A N   1 
ATOM   2756  C  CA  . ASP   A  1 348 ? -10.878 7.211   -42.997  1.00 47.18  ? 649  ASP   A CA  1 
ATOM   2757  C  C   . ASP   A  1 348 ? -11.673 8.415   -43.477  1.00 42.49  ? 649  ASP   A C   1 
ATOM   2758  O  O   . ASP   A  1 348 ? -12.345 8.295   -44.500  1.00 50.10  ? 649  ASP   A O   1 
ATOM   2759  C  CB  . ASP   A  1 348 ? -11.751 5.962   -43.134  1.00 42.88  ? 649  ASP   A CB  1 
ATOM   2760  C  CG  . ASP   A  1 348 ? -10.970 4.687   -42.945  1.00 49.65  ? 649  ASP   A CG  1 
ATOM   2761  O  OD1 . ASP   A  1 348 ? -9.732  4.762   -42.781  1.00 45.56  ? 649  ASP   A OD1 1 
ATOM   2762  O  OD2 . ASP   A  1 348 ? -11.599 3.609   -42.956  1.00 56.52  ? 649  ASP   A OD2 1 
ATOM   2763  N  N   . LYS   A  1 349 ? -11.651 9.541   -42.760  1.00 44.11  ? 650  LYS   A N   1 
ATOM   2764  C  CA  . LYS   A  1 349 ? -12.347 10.764  -43.184  1.00 47.01  ? 650  LYS   A CA  1 
ATOM   2765  C  C   . LYS   A  1 349 ? -13.804 10.499  -43.579  1.00 42.69  ? 650  LYS   A C   1 
ATOM   2766  O  O   . LYS   A  1 349 ? -14.320 11.030  -44.565  1.00 47.77  ? 650  LYS   A O   1 
ATOM   2767  C  CB  . LYS   A  1 349 ? -11.583 11.450  -44.320  1.00 52.62  ? 650  LYS   A CB  1 
ATOM   2768  C  CG  . LYS   A  1 349 ? -10.174 11.882  -43.921  1.00 60.67  ? 650  LYS   A CG  1 
ATOM   2769  C  CD  . LYS   A  1 349 ? -9.222  11.824  -45.102  1.00 65.79  ? 650  LYS   A CD  1 
ATOM   2770  C  CE  . LYS   A  1 349 ? -8.738  13.201  -45.512  1.00 72.67  ? 650  LYS   A CE  1 
ATOM   2771  N  NZ  . LYS   A  1 349 ? -7.891  13.821  -44.456  1.00 81.99  ? 650  LYS   A NZ  1 
ATOM   2772  N  N   . VAL   A  1 350 ? -14.486 9.691   -42.777  1.00 48.13  ? 651  VAL   A N   1 
ATOM   2773  C  CA  . VAL   A  1 350 ? -15.919 9.449   -42.908  1.00 42.68  ? 651  VAL   A CA  1 
ATOM   2774  C  C   . VAL   A  1 350 ? -16.631 10.153  -41.752  1.00 41.60  ? 651  VAL   A C   1 
ATOM   2775  O  O   . VAL   A  1 350 ? -16.292 9.934   -40.581  1.00 45.23  ? 651  VAL   A O   1 
ATOM   2776  C  CB  . VAL   A  1 350 ? -16.218 7.937   -42.937  1.00 33.77  ? 651  VAL   A CB  1 
ATOM   2777  C  CG1 . VAL   A  1 350 ? -17.734 7.654   -42.873  1.00 30.51  ? 651  VAL   A CG1 1 
ATOM   2778  C  CG2 . VAL   A  1 350 ? -15.586 7.315   -44.165  1.00 43.40  ? 651  VAL   A CG2 1 
ATOM   2779  N  N   . THR   A  1 351 ? -17.618 10.990  -42.083  1.00 38.07  ? 652  THR   A N   1 
ATOM   2780  C  CA  . THR   A  1 351 ? -18.292 11.830  -41.102  1.00 33.76  ? 652  THR   A CA  1 
ATOM   2781  C  C   . THR   A  1 351 ? -18.841 11.015  -39.942  1.00 41.64  ? 652  THR   A C   1 
ATOM   2782  O  O   . THR   A  1 351 ? -19.522 10.003  -40.134  1.00 42.09  ? 652  THR   A O   1 
ATOM   2783  C  CB  . THR   A  1 351 ? -19.443 12.610  -41.737  1.00 39.34  ? 652  THR   A CB  1 
ATOM   2784  O  OG1 . THR   A  1 351 ? -18.979 13.372  -42.859  1.00 43.26  ? 652  THR   A OG1 1 
ATOM   2785  C  CG2 . THR   A  1 351 ? -20.073 13.562  -40.691  1.00 28.01  ? 652  THR   A CG2 1 
ATOM   2786  N  N   . ILE   A  1 352 ? -18.565 11.491  -38.729  1.00 39.55  ? 653  ILE   A N   1 
ATOM   2787  C  CA  . ILE   A  1 352 ? -19.155 10.941  -37.519  1.00 33.95  ? 653  ILE   A CA  1 
ATOM   2788  C  C   . ILE   A  1 352 ? -19.144 12.039  -36.470  1.00 39.05  ? 653  ILE   A C   1 
ATOM   2789  O  O   . ILE   A  1 352 ? -18.397 13.021  -36.579  1.00 38.32  ? 653  ILE   A O   1 
ATOM   2790  C  CB  . ILE   A  1 352 ? -18.386 9.684   -37.051  1.00 34.60  ? 653  ILE   A CB  1 
ATOM   2791  C  CG1 . ILE   A  1 352 ? -19.243 8.830   -36.105  1.00 29.71  ? 653  ILE   A CG1 1 
ATOM   2792  C  CG2 . ILE   A  1 352 ? -17.042 10.075  -36.435  1.00 35.47  ? 653  ILE   A CG2 1 
ATOM   2793  C  CD1 . ILE   A  1 352 ? -18.768 7.392   -36.038  1.00 28.14  ? 653  ILE   A CD1 1 
ATOM   2794  N  N   . VAL   A  1 353 ? -19.995 11.877  -35.453  1.00 36.24  ? 654  VAL   A N   1 
ATOM   2795  C  CA  . VAL   A  1 353 ? -20.068 12.793  -34.318  1.00 35.58  ? 654  VAL   A CA  1 
ATOM   2796  C  C   . VAL   A  1 353 ? -20.122 11.970  -33.037  1.00 39.50  ? 654  VAL   A C   1 
ATOM   2797  O  O   . VAL   A  1 353 ? -20.875 10.992  -32.951  1.00 29.91  ? 654  VAL   A O   1 
ATOM   2798  C  CB  . VAL   A  1 353 ? -21.286 13.736  -34.417  1.00 37.01  ? 654  VAL   A CB  1 
ATOM   2799  C  CG1 . VAL   A  1 353 ? -22.598 12.983  -34.249  1.00 31.44  ? 654  VAL   A CG1 1 
ATOM   2800  C  CG2 . VAL   A  1 353 ? -21.179 14.846  -33.409  1.00 35.97  ? 654  VAL   A CG2 1 
ATOM   2801  N  N   . ASP   A  1 354 ? -19.303 12.343  -32.055  1.00 42.39  ? 655  ASP   A N   1 
ATOM   2802  C  CA  . ASP   A  1 354 ? -19.362 11.659  -30.775  1.00 39.24  ? 655  ASP   A CA  1 
ATOM   2803  C  C   . ASP   A  1 354 ? -20.552 12.178  -29.974  1.00 37.81  ? 655  ASP   A C   1 
ATOM   2804  O  O   . ASP   A  1 354 ? -21.150 13.207  -30.297  1.00 32.74  ? 655  ASP   A O   1 
ATOM   2805  C  CB  . ASP   A  1 354 ? -18.065 11.844  -29.988  1.00 43.96  ? 655  ASP   A CB  1 
ATOM   2806  C  CG  . ASP   A  1 354 ? -17.758 13.301  -29.711  1.00 50.61  ? 655  ASP   A CG  1 
ATOM   2807  O  OD1 . ASP   A  1 354 ? -17.115 13.941  -30.575  1.00 56.81  ? 655  ASP   A OD1 1 
ATOM   2808  O  OD2 . ASP   A  1 354 ? -18.195 13.811  -28.650  1.00 42.50  ? 655  ASP   A OD2 1 
ATOM   2809  N  N   . HIS   A  1 355 ? -20.900 11.449  -28.912  1.00 37.51  ? 656  HIS   A N   1 
ATOM   2810  C  CA  . HIS   A  1 355 ? -22.099 11.818  -28.170  1.00 34.86  ? 656  HIS   A CA  1 
ATOM   2811  C  C   . HIS   A  1 355 ? -21.932 13.153  -27.456  1.00 31.58  ? 656  HIS   A C   1 
ATOM   2812  O  O   . HIS   A  1 355 ? -22.899 13.909  -27.333  1.00 38.51  ? 656  HIS   A O   1 
ATOM   2813  C  CB  . HIS   A  1 355 ? -22.484 10.701  -27.197  1.00 33.48  ? 656  HIS   A CB  1 
ATOM   2814  C  CG  . HIS   A  1 355 ? -21.350 10.192  -26.360  1.00 36.38  ? 656  HIS   A CG  1 
ATOM   2815  N  ND1 . HIS   A  1 355 ? -20.422 9.286   -26.832  1.00 40.67  ? 656  HIS   A ND1 1 
ATOM   2816  C  CD2 . HIS   A  1 355 ? -21.025 10.422  -25.066  1.00 34.29  ? 656  HIS   A CD2 1 
ATOM   2817  C  CE1 . HIS   A  1 355 ? -19.557 9.003   -25.873  1.00 35.05  ? 656  HIS   A CE1 1 
ATOM   2818  N  NE2 . HIS   A  1 355 ? -19.905 9.676   -24.790  1.00 37.69  ? 656  HIS   A NE2 1 
ATOM   2819  N  N   . HIS   A  1 356 ? -20.714 13.502  -27.053  1.00 27.57  ? 657  HIS   A N   1 
ATOM   2820  C  CA  . HIS   A  1 356 ? -20.506 14.797  -26.411  1.00 32.25  ? 657  HIS   A CA  1 
ATOM   2821  C  C   . HIS   A  1 356 ? -20.816 15.950  -27.349  1.00 39.82  ? 657  HIS   A C   1 
ATOM   2822  O  O   . HIS   A  1 356 ? -21.634 16.823  -27.029  1.00 43.00  ? 657  HIS   A O   1 
ATOM   2823  C  CB  . HIS   A  1 356 ? -19.085 14.881  -25.888  1.00 28.89  ? 657  HIS   A CB  1 
ATOM   2824  C  CG  . HIS   A  1 356 ? -18.776 13.802  -24.909  1.00 41.47  ? 657  HIS   A CG  1 
ATOM   2825  N  ND1 . HIS   A  1 356 ? -19.328 13.773  -23.648  1.00 37.81  ? 657  HIS   A ND1 1 
ATOM   2826  C  CD2 . HIS   A  1 356 ? -18.037 12.674  -25.026  1.00 40.58  ? 657  HIS   A CD2 1 
ATOM   2827  C  CE1 . HIS   A  1 356 ? -18.908 12.694  -23.017  1.00 40.12  ? 657  HIS   A CE1 1 
ATOM   2828  N  NE2 . HIS   A  1 356 ? -18.129 12.008  -23.834  1.00 36.15  ? 657  HIS   A NE2 1 
ATOM   2829  N  N   . SER   A  1 357 ? -20.169 15.977  -28.516  1.00 40.91  ? 658  SER   A N   1 
ATOM   2830  C  CA  A SER   A  1 357 ? -20.429 17.049  -29.468  0.61 38.32  ? 658  SER   A CA  1 
ATOM   2831  C  CA  B SER   A  1 357 ? -20.429 17.047  -29.470  0.39 38.82  ? 658  SER   A CA  1 
ATOM   2832  C  C   . SER   A  1 357 ? -21.905 17.092  -29.846  1.00 40.19  ? 658  SER   A C   1 
ATOM   2833  O  O   . SER   A  1 357 ? -22.527 18.161  -29.849  1.00 34.91  ? 658  SER   A O   1 
ATOM   2834  C  CB  A SER   A  1 357 ? -19.548 16.877  -30.714  0.61 39.54  ? 658  SER   A CB  1 
ATOM   2835  C  CB  B SER   A  1 357 ? -19.555 16.859  -30.712  0.39 39.25  ? 658  SER   A CB  1 
ATOM   2836  O  OG  A SER   A  1 357 ? -19.754 17.932  -31.647  0.61 40.13  ? 658  SER   A OG  1 
ATOM   2837  O  OG  B SER   A  1 357 ? -18.203 16.677  -30.343  0.39 36.80  ? 658  SER   A OG  1 
ATOM   2838  N  N   . ALA   A  1 358 ? -22.488 15.928  -30.147  1.00 43.41  ? 659  ALA   A N   1 
ATOM   2839  C  CA  . ALA   A  1 358 ? -23.874 15.885  -30.605  1.00 36.89  ? 659  ALA   A CA  1 
ATOM   2840  C  C   . ALA   A  1 358 ? -24.834 16.431  -29.555  1.00 39.95  ? 659  ALA   A C   1 
ATOM   2841  O  O   . ALA   A  1 358 ? -25.770 17.170  -29.893  1.00 40.54  ? 659  ALA   A O   1 
ATOM   2842  C  CB  . ALA   A  1 358 ? -24.255 14.452  -31.002  1.00 29.78  ? 659  ALA   A CB  1 
ATOM   2843  N  N   . THR   A  1 359 ? -24.641 16.069  -28.277  1.00 38.48  ? 660  THR   A N   1 
ATOM   2844  C  CA  . THR   A  1 359 ? -25.584 16.548  -27.267  1.00 32.00  ? 660  THR   A CA  1 
ATOM   2845  C  C   . THR   A  1 359 ? -25.400 18.039  -27.018  1.00 32.95  ? 660  THR   A C   1 
ATOM   2846  O  O   . THR   A  1 359 ? -26.381 18.788  -26.962  1.00 37.10  ? 660  THR   A O   1 
ATOM   2847  C  CB  . THR   A  1 359 ? -25.453 15.761  -25.961  1.00 34.91  ? 660  THR   A CB  1 
ATOM   2848  O  OG1 . THR   A  1 359 ? -24.094 15.770  -25.503  1.00 32.90  ? 660  THR   A OG1 1 
ATOM   2849  C  CG2 . THR   A  1 359 ? -25.946 14.338  -26.139  1.00 33.43  ? 660  THR   A CG2 1 
ATOM   2850  N  N   . GLU   A  1 360 ? -24.151 18.501  -26.919  1.00 36.05  ? 661  GLU   A N   1 
ATOM   2851  C  CA  . GLU   A  1 360 ? -23.930 19.935  -26.789  1.00 46.64  ? 661  GLU   A CA  1 
ATOM   2852  C  C   . GLU   A  1 360 ? -24.596 20.705  -27.930  1.00 41.28  ? 661  GLU   A C   1 
ATOM   2853  O  O   . GLU   A  1 360 ? -25.216 21.751  -27.709  1.00 42.06  ? 661  GLU   A O   1 
ATOM   2854  C  CB  . GLU   A  1 360 ? -22.440 20.244  -26.742  1.00 49.35  ? 661  GLU   A CB  1 
ATOM   2855  C  CG  . GLU   A  1 360 ? -22.180 21.715  -26.511  1.00 63.30  ? 661  GLU   A CG  1 
ATOM   2856  C  CD  . GLU   A  1 360 ? -20.727 22.092  -26.719  1.00 78.85  ? 661  GLU   A CD  1 
ATOM   2857  O  OE1 . GLU   A  1 360 ? -19.890 21.174  -26.876  1.00 83.35  ? 661  GLU   A OE1 1 
ATOM   2858  O  OE2 . GLU   A  1 360 ? -20.423 23.307  -26.722  1.00 82.33  ? 661  GLU   A OE2 1 
ATOM   2859  N  N   . SER   A  1 361 ? -24.503 20.190  -29.154  1.00 39.21  ? 662  SER   A N   1 
ATOM   2860  C  CA  . SER   A  1 361 ? -25.113 20.894  -30.276  1.00 40.74  ? 662  SER   A CA  1 
ATOM   2861  C  C   . SER   A  1 361 ? -26.629 20.908  -30.154  1.00 40.52  ? 662  SER   A C   1 
ATOM   2862  O  O   . SER   A  1 361 ? -27.275 21.927  -30.430  1.00 39.18  ? 662  SER   A O   1 
ATOM   2863  C  CB  . SER   A  1 361 ? -24.676 20.255  -31.589  1.00 39.00  ? 662  SER   A CB  1 
ATOM   2864  O  OG  . SER   A  1 361 ? -23.341 20.629  -31.895  1.00 45.42  ? 662  SER   A OG  1 
ATOM   2865  N  N   . PHE   A  1 362 ? -27.213 19.797  -29.710  1.00 39.05  ? 663  PHE   A N   1 
ATOM   2866  C  CA  . PHE   A  1 362 ? -28.659 19.761  -29.539  1.00 37.87  ? 663  PHE   A CA  1 
ATOM   2867  C  C   . PHE   A  1 362 ? -29.143 20.792  -28.511  1.00 36.25  ? 663  PHE   A C   1 
ATOM   2868  O  O   . PHE   A  1 362 ? -30.202 21.405  -28.700  1.00 38.82  ? 663  PHE   A O   1 
ATOM   2869  C  CB  . PHE   A  1 362 ? -29.118 18.360  -29.150  1.00 35.73  ? 663  PHE   A CB  1 
ATOM   2870  C  CG  . PHE   A  1 362 ? -30.576 18.287  -28.923  1.00 40.56  ? 663  PHE   A CG  1 
ATOM   2871  C  CD1 . PHE   A  1 362 ? -31.440 18.287  -30.001  1.00 28.81  ? 663  PHE   A CD1 1 
ATOM   2872  C  CD2 . PHE   A  1 362 ? -31.102 18.300  -27.624  1.00 32.73  ? 663  PHE   A CD2 1 
ATOM   2873  C  CE1 . PHE   A  1 362 ? -32.812 18.264  -29.814  1.00 29.15  ? 663  PHE   A CE1 1 
ATOM   2874  C  CE2 . PHE   A  1 362 ? -32.459 18.266  -27.430  1.00 35.44  ? 663  PHE   A CE2 1 
ATOM   2875  C  CZ  . PHE   A  1 362 ? -33.322 18.250  -28.525  1.00 46.06  ? 663  PHE   A CZ  1 
ATOM   2876  N  N   . ILE   A  1 363 ? -28.388 21.005  -27.423  1.00 36.49  ? 664  ILE   A N   1 
ATOM   2877  C  CA  . ILE   A  1 363 ? -28.764 22.041  -26.445  1.00 41.92  ? 664  ILE   A CA  1 
ATOM   2878  C  C   . ILE   A  1 363 ? -28.748 23.424  -27.095  1.00 44.12  ? 664  ILE   A C   1 
ATOM   2879  O  O   . ILE   A  1 363 ? -29.661 24.242  -26.903  1.00 40.77  ? 664  ILE   A O   1 
ATOM   2880  C  CB  . ILE   A  1 363 ? -27.838 21.999  -25.213  1.00 36.75  ? 664  ILE   A CB  1 
ATOM   2881  C  CG1 . ILE   A  1 363 ? -28.079 20.726  -24.402  1.00 35.91  ? 664  ILE   A CG1 1 
ATOM   2882  C  CG2 . ILE   A  1 363 ? -28.022 23.274  -24.331  1.00 28.37  ? 664  ILE   A CG2 1 
ATOM   2883  C  CD1 . ILE   A  1 363 ? -29.421 20.704  -23.749  1.00 36.69  ? 664  ILE   A CD1 1 
ATOM   2884  N  N   . LYS   A  1 364 ? -27.697 23.707  -27.865  1.00 40.74  ? 665  LYS   A N   1 
ATOM   2885  C  CA  . LYS   A  1 364 ? -27.651 24.952  -28.622  1.00 44.83  ? 665  LYS   A CA  1 
ATOM   2886  C  C   . LYS   A  1 364 ? -28.846 25.065  -29.561  1.00 42.53  ? 665  LYS   A C   1 
ATOM   2887  O  O   . LYS   A  1 364 ? -29.456 26.135  -29.679  1.00 41.00  ? 665  LYS   A O   1 
ATOM   2888  C  CB  . LYS   A  1 364 ? -26.336 25.036  -29.388  1.00 38.27  ? 665  LYS   A CB  1 
ATOM   2889  C  CG  . LYS   A  1 364 ? -25.158 25.522  -28.560  1.00 40.77  ? 665  LYS   A CG  1 
ATOM   2890  C  CD  . LYS   A  1 364 ? -23.850 25.118  -29.222  1.00 55.42  ? 665  LYS   A CD  1 
ATOM   2891  C  CE  . LYS   A  1 364 ? -22.650 25.899  -28.696  1.00 57.55  ? 665  LYS   A CE  1 
ATOM   2892  N  NZ  . LYS   A  1 364 ? -21.391 25.483  -29.404  1.00 53.50  ? 665  LYS   A NZ  1 
ATOM   2893  N  N   . HIS   A  1 365 ? -29.210 23.957  -30.212  1.00 43.23  ? 666  HIS   A N   1 
ATOM   2894  C  CA  . HIS   A  1 365 ? -30.352 23.950  -31.122  1.00 39.60  ? 666  HIS   A CA  1 
ATOM   2895  C  C   . HIS   A  1 365 ? -31.666 24.179  -30.376  1.00 41.11  ? 666  HIS   A C   1 
ATOM   2896  O  O   . HIS   A  1 365 ? -32.528 24.960  -30.825  1.00 30.44  ? 666  HIS   A O   1 
ATOM   2897  C  CB  . HIS   A  1 365 ? -30.377 22.620  -31.862  1.00 37.49  ? 666  HIS   A CB  1 
ATOM   2898  C  CG  . HIS   A  1 365 ? -31.664 22.343  -32.570  1.00 41.50  ? 666  HIS   A CG  1 
ATOM   2899  N  ND1 . HIS   A  1 365 ? -32.034 22.999  -33.723  1.00 40.22  ? 666  HIS   A ND1 1 
ATOM   2900  C  CD2 . HIS   A  1 365 ? -32.658 21.466  -32.300  1.00 40.03  ? 666  HIS   A CD2 1 
ATOM   2901  C  CE1 . HIS   A  1 365 ? -33.205 22.545  -34.128  1.00 32.56  ? 666  HIS   A CE1 1 
ATOM   2902  N  NE2 . HIS   A  1 365 ? -33.607 21.614  -33.283  1.00 37.60  ? 666  HIS   A NE2 1 
ATOM   2903  N  N   . MET   A  1 366 ? -31.834 23.499  -29.235  1.00 36.91  ? 667  MET   A N   1 
ATOM   2904  C  CA  . MET   A  1 366 ? -33.042 23.650  -28.439  1.00 39.21  ? 667  MET   A CA  1 
ATOM   2905  C  C   . MET   A  1 366 ? -33.263 25.107  -28.054  1.00 39.76  ? 667  MET   A C   1 
ATOM   2906  O  O   . MET   A  1 366 ? -34.330 25.678  -28.317  1.00 40.34  ? 667  MET   A O   1 
ATOM   2907  C  CB  . MET   A  1 366 ? -32.942 22.759  -27.199  1.00 47.64  ? 667  MET   A CB  1 
ATOM   2908  C  CG  . MET   A  1 366 ? -34.242 22.526  -26.491  1.00 47.26  ? 667  MET   A CG  1 
ATOM   2909  S  SD  . MET   A  1 366 ? -34.053 21.341  -25.138  1.00 48.64  ? 667  MET   A SD  1 
ATOM   2910  C  CE  . MET   A  1 366 ? -35.559 21.706  -24.238  1.00 45.81  ? 667  MET   A CE  1 
ATOM   2911  N  N   . GLU   A  1 367 ? -32.244 25.739  -27.464  1.00 47.49  ? 668  GLU   A N   1 
ATOM   2912  C  CA  . GLU   A  1 367 ? -32.379 27.138  -27.065  1.00 58.42  ? 668  GLU   A CA  1 
ATOM   2913  C  C   . GLU   A  1 367 ? -32.783 28.017  -28.246  1.00 52.00  ? 668  GLU   A C   1 
ATOM   2914  O  O   . GLU   A  1 367 ? -33.658 28.879  -28.117  1.00 52.72  ? 668  GLU   A O   1 
ATOM   2915  C  CB  . GLU   A  1 367 ? -31.077 27.629  -26.427  1.00 65.98  ? 668  GLU   A CB  1 
ATOM   2916  C  CG  . GLU   A  1 367 ? -30.849 27.098  -25.011  1.00 70.30  ? 668  GLU   A CG  1 
ATOM   2917  C  CD  . GLU   A  1 367 ? -29.399 27.200  -24.557  1.00 78.49  ? 668  GLU   A CD  1 
ATOM   2918  O  OE1 . GLU   A  1 367 ? -28.542 27.611  -25.374  1.00 83.59  ? 668  GLU   A OE1 1 
ATOM   2919  O  OE2 . GLU   A  1 367 ? -29.116 26.862  -23.385  1.00 75.68  ? 668  GLU   A OE2 1 
ATOM   2920  N  N   . ASN   A  1 368 ? -32.180 27.796  -29.409  1.00 46.39  ? 669  ASN   A N   1 
ATOM   2921  C  CA  . ASN   A  1 368 ? -32.526 28.590  -30.585  1.00 48.07  ? 669  ASN   A CA  1 
ATOM   2922  C  C   . ASN   A  1 368 ? -33.973 28.351  -31.016  1.00 45.90  ? 669  ASN   A C   1 
ATOM   2923  O  O   . ASN   A  1 368 ? -34.709 29.308  -31.299  1.00 45.62  ? 669  ASN   A O   1 
ATOM   2924  C  CB  . ASN   A  1 368 ? -31.554 28.272  -31.723  1.00 55.22  ? 669  ASN   A CB  1 
ATOM   2925  C  CG  . ASN   A  1 368 ? -31.800 29.116  -32.962  1.00 53.45  ? 669  ASN   A CG  1 
ATOM   2926  O  OD1 . ASN   A  1 368 ? -31.687 30.343  -32.928  1.00 61.91  ? 669  ASN   A OD1 1 
ATOM   2927  N  ND2 . ASN   A  1 368 ? -32.129 28.454  -34.069  1.00 44.04  ? 669  ASN   A ND2 1 
ATOM   2928  N  N   . GLU   A  1 369 ? -34.394 27.074  -31.080  1.00 40.18  ? 670  GLU   A N   1 
ATOM   2929  C  CA  . GLU   A  1 369 ? -35.791 26.741  -31.372  1.00 33.44  ? 670  GLU   A CA  1 
ATOM   2930  C  C   . GLU   A  1 369 ? -36.764 27.401  -30.386  1.00 40.59  ? 670  GLU   A C   1 
ATOM   2931  O  O   . GLU   A  1 369 ? -37.818 27.900  -30.789  1.00 40.67  ? 670  GLU   A O   1 
ATOM   2932  C  CB  . GLU   A  1 369 ? -35.975 25.221  -31.360  1.00 35.06  ? 670  GLU   A CB  1 
ATOM   2933  C  CG  . GLU   A  1 369 ? -35.300 24.496  -32.488  1.00 32.53  ? 670  GLU   A CG  1 
ATOM   2934  C  CD  . GLU   A  1 369 ? -35.973 24.783  -33.826  1.00 40.54  ? 670  GLU   A CD  1 
ATOM   2935  O  OE1 . GLU   A  1 369 ? -36.831 23.971  -34.254  1.00 42.74  ? 670  GLU   A OE1 1 
ATOM   2936  O  OE2 . GLU   A  1 369 ? -35.653 25.829  -34.428  1.00 39.72  ? 670  GLU   A OE2 1 
ATOM   2937  N  N   . TYR   A  1 370 ? -36.453 27.394  -29.087  1.00 33.01  ? 671  TYR   A N   1 
ATOM   2938  C  CA  . TYR   A  1 370 ? -37.297 28.148  -28.162  1.00 43.04  ? 671  TYR   A CA  1 
ATOM   2939  C  C   . TYR   A  1 370 ? -37.297 29.631  -28.517  1.00 41.81  ? 671  TYR   A C   1 
ATOM   2940  O  O   . TYR   A  1 370 ? -38.359 30.257  -28.564  1.00 43.44  ? 671  TYR   A O   1 
ATOM   2941  C  CB  . TYR   A  1 370 ? -36.856 27.918  -26.705  1.00 47.12  ? 671  TYR   A CB  1 
ATOM   2942  C  CG  . TYR   A  1 370 ? -37.476 26.673  -26.080  1.00 47.28  ? 671  TYR   A CG  1 
ATOM   2943  C  CD1 . TYR   A  1 370 ? -36.961 25.407  -26.345  1.00 47.70  ? 671  TYR   A CD1 1 
ATOM   2944  C  CD2 . TYR   A  1 370 ? -38.577 26.761  -25.226  1.00 49.28  ? 671  TYR   A CD2 1 
ATOM   2945  C  CE1 . TYR   A  1 370 ? -37.528 24.261  -25.788  1.00 49.08  ? 671  TYR   A CE1 1 
ATOM   2946  C  CE2 . TYR   A  1 370 ? -39.149 25.616  -24.660  1.00 45.33  ? 671  TYR   A CE2 1 
ATOM   2947  C  CZ  . TYR   A  1 370 ? -38.622 24.373  -24.949  1.00 49.16  ? 671  TYR   A CZ  1 
ATOM   2948  O  OH  . TYR   A  1 370 ? -39.184 23.245  -24.406  1.00 52.57  ? 671  TYR   A OH  1 
ATOM   2949  N  N   . ARG   A  1 371 ? -36.123 30.192  -28.823  1.00 50.14  ? 672  ARG   A N   1 
ATOM   2950  C  CA  . ARG   A  1 371 ? -36.008 31.605  -29.192  1.00 56.79  ? 672  ARG   A CA  1 
ATOM   2951  C  C   . ARG   A  1 371 ? -36.927 31.968  -30.356  1.00 55.59  ? 672  ARG   A C   1 
ATOM   2952  O  O   . ARG   A  1 371 ? -37.742 32.891  -30.259  1.00 55.26  ? 672  ARG   A O   1 
ATOM   2953  C  CB  . ARG   A  1 371 ? -34.557 31.940  -29.560  1.00 69.77  ? 672  ARG   A CB  1 
ATOM   2954  C  CG  . ARG   A  1 371 ? -33.817 32.842  -28.583  1.00 86.03  ? 672  ARG   A CG  1 
ATOM   2955  C  CD  . ARG   A  1 371 ? -33.275 32.078  -27.365  1.00 94.70  ? 672  ARG   A CD  1 
ATOM   2956  N  NE  . ARG   A  1 371 ? -34.269 31.935  -26.302  1.00 99.47  ? 672  ARG   A NE  1 
ATOM   2957  C  CZ  . ARG   A  1 371 ? -33.982 31.652  -25.033  1.00 98.10  ? 672  ARG   A CZ  1 
ATOM   2958  N  NH1 . ARG   A  1 371 ? -32.719 31.475  -24.651  1.00 95.76  ? 672  ARG   A NH1 1 
ATOM   2959  N  NH2 . ARG   A  1 371 ? -34.963 31.554  -24.142  1.00 95.76  ? 672  ARG   A NH2 1 
ATOM   2960  N  N   . CYS   A  1 372 ? -36.785 31.283  -31.488  1.00 54.28  ? 673  CYS   A N   1 
ATOM   2961  C  CA  . CYS   A  1 372 ? -37.439 31.741  -32.707  1.00 58.30  ? 673  CYS   A CA  1 
ATOM   2962  C  C   . CYS   A  1 372 ? -38.735 31.008  -33.020  1.00 55.21  ? 673  CYS   A C   1 
ATOM   2963  O  O   . CYS   A  1 372 ? -39.474 31.445  -33.903  1.00 50.40  ? 673  CYS   A O   1 
ATOM   2964  C  CB  . CYS   A  1 372 ? -36.486 31.605  -33.899  1.00 59.53  ? 673  CYS   A CB  1 
ATOM   2965  S  SG  . CYS   A  1 372 ? -36.163 29.891  -34.395  1.00 64.03  ? 673  CYS   A SG  1 
ATOM   2966  N  N   . ARG   A  1 373 ? -39.035 29.920  -32.320  1.00 54.30  ? 674  ARG   A N   1 
ATOM   2967  C  CA  . ARG   A  1 373 ? -40.175 29.087  -32.656  1.00 36.47  ? 674  ARG   A CA  1 
ATOM   2968  C  C   . ARG   A  1 373 ? -41.133 28.875  -31.493  1.00 45.05  ? 674  ARG   A C   1 
ATOM   2969  O  O   . ARG   A  1 373 ? -42.259 28.419  -31.721  1.00 47.93  ? 674  ARG   A O   1 
ATOM   2970  C  CB  . ARG   A  1 373 ? -39.692 27.722  -33.183  1.00 36.93  ? 674  ARG   A CB  1 
ATOM   2971  C  CG  . ARG   A  1 373 ? -40.731 26.948  -33.993  1.00 37.08  ? 674  ARG   A CG  1 
ATOM   2972  C  CD  . ARG   A  1 373 ? -40.254 25.560  -34.349  1.00 31.96  ? 674  ARG   A CD  1 
ATOM   2973  N  NE  . ARG   A  1 373 ? -41.291 24.853  -35.091  1.00 38.39  ? 674  ARG   A NE  1 
ATOM   2974  C  CZ  . ARG   A  1 373 ? -41.385 23.533  -35.177  1.00 39.36  ? 674  ARG   A CZ  1 
ATOM   2975  N  NH1 . ARG   A  1 373 ? -40.504 22.762  -34.556  1.00 42.73  ? 674  ARG   A NH1 1 
ATOM   2976  N  NH2 . ARG   A  1 373 ? -42.363 22.983  -35.882  1.00 34.44  ? 674  ARG   A NH2 1 
ATOM   2977  N  N   . GLY   A  1 374 ? -40.741 29.201  -30.263  1.00 41.15  ? 675  GLY   A N   1 
ATOM   2978  C  CA  . GLY   A  1 374 ? -41.632 29.012  -29.149  1.00 42.84  ? 675  GLY   A CA  1 
ATOM   2979  C  C   . GLY   A  1 374 ? -41.513 27.663  -28.486  1.00 49.89  ? 675  GLY   A C   1 
ATOM   2980  O  O   . GLY   A  1 374 ? -42.281 27.373  -27.555  1.00 50.50  ? 675  GLY   A O   1 
ATOM   2981  N  N   . GLY   A  1 375 ? -40.588 26.832  -28.941  1.00 45.27  ? 676  GLY   A N   1 
ATOM   2982  C  CA  . GLY   A  1 375 ? -40.320 25.575  -28.284  1.00 49.22  ? 676  GLY   A CA  1 
ATOM   2983  C  C   . GLY   A  1 375 ? -39.632 24.612  -29.232  1.00 54.49  ? 676  GLY   A C   1 
ATOM   2984  O  O   . GLY   A  1 375 ? -39.218 24.969  -30.341  1.00 54.62  ? 676  GLY   A O   1 
ATOM   2985  N  N   . CYS   A  1 376 ? -39.530 23.383  -28.764  1.00 51.06  ? 677  CYS   A N   1 
ATOM   2986  C  CA  . CYS   A  1 376 ? -38.841 22.326  -29.473  1.00 43.09  ? 677  CYS   A CA  1 
ATOM   2987  C  C   . CYS   A  1 376 ? -39.134 21.002  -28.786  1.00 45.09  ? 677  CYS   A C   1 
ATOM   2988  O  O   . CYS   A  1 376 ? -38.534 20.690  -27.754  1.00 43.11  ? 677  CYS   A O   1 
ATOM   2989  C  CB  . CYS   A  1 376 ? -37.345 22.596  -29.503  1.00 39.77  ? 677  CYS   A CB  1 
ATOM   2990  S  SG  . CYS   A  1 376 ? -36.408 21.192  -30.033  1.00 37.62  ? 677  CYS   A SG  1 
ATOM   2991  N  N   . PRO   A  1 377 ? -40.048 20.206  -29.320  1.00 43.11  ? 678  PRO   A N   1 
ATOM   2992  C  CA  . PRO   A  1 377 ? -40.414 18.959  -28.644  1.00 41.64  ? 678  PRO   A CA  1 
ATOM   2993  C  C   . PRO   A  1 377 ? -39.244 17.982  -28.656  1.00 47.69  ? 678  PRO   A C   1 
ATOM   2994  O  O   . PRO   A  1 377 ? -38.513 17.866  -29.644  1.00 47.42  ? 678  PRO   A O   1 
ATOM   2995  C  CB  . PRO   A  1 377 ? -41.599 18.445  -29.467  1.00 40.39  ? 678  PRO   A CB  1 
ATOM   2996  C  CG  . PRO   A  1 377 ? -41.344 19.022  -30.861  1.00 38.45  ? 678  PRO   A CG  1 
ATOM   2997  C  CD  . PRO   A  1 377 ? -40.698 20.363  -30.640  1.00 30.48  ? 678  PRO   A CD  1 
ATOM   2998  N  N   . ALA   A  1 378 ? -39.061 17.289  -27.536  1.00 41.76  ? 679  ALA   A N   1 
ATOM   2999  C  CA  . ALA   A  1 378 ? -37.856 16.502  -27.314  1.00 39.96  ? 679  ALA   A CA  1 
ATOM   3000  C  C   . ALA   A  1 378 ? -38.167 15.371  -26.349  1.00 36.10  ? 679  ALA   A C   1 
ATOM   3001  O  O   . ALA   A  1 378 ? -38.845 15.575  -25.339  1.00 33.18  ? 679  ALA   A O   1 
ATOM   3002  C  CB  . ALA   A  1 378 ? -36.713 17.359  -26.765  1.00 36.53  ? 679  ALA   A CB  1 
ATOM   3003  N  N   . ASP   A  1 379 ? -37.664 14.186  -26.676  1.00 34.93  ? 680  ASP   A N   1 
ATOM   3004  C  CA  . ASP   A  1 379 ? -37.926 12.943  -25.957  1.00 34.44  ? 680  ASP   A CA  1 
ATOM   3005  C  C   . ASP   A  1 379 ? -36.645 12.579  -25.209  1.00 39.41  ? 680  ASP   A C   1 
ATOM   3006  O  O   . ASP   A  1 379 ? -35.726 11.977  -25.783  1.00 40.37  ? 680  ASP   A O   1 
ATOM   3007  C  CB  . ASP   A  1 379 ? -38.351 11.853  -26.943  1.00 41.80  ? 680  ASP   A CB  1 
ATOM   3008  C  CG  . ASP   A  1 379 ? -38.901 10.604  -26.265  1.00 47.16  ? 680  ASP   A CG  1 
ATOM   3009  O  OD1 . ASP   A  1 379 ? -38.502 10.295  -25.116  1.00 47.25  ? 680  ASP   A OD1 1 
ATOM   3010  O  OD2 . ASP   A  1 379 ? -39.732 9.920   -26.912  1.00 46.03  ? 680  ASP   A OD2 1 
ATOM   3011  N  N   . TRP   A  1 380 ? -36.594 12.967  -23.926  1.00 36.12  ? 681  TRP   A N   1 
ATOM   3012  C  CA  . TRP   A  1 380 ? -35.400 12.786  -23.102  1.00 29.16  ? 681  TRP   A CA  1 
ATOM   3013  C  C   . TRP   A  1 380 ? -34.908 11.345  -23.131  1.00 28.52  ? 681  TRP   A C   1 
ATOM   3014  O  O   . TRP   A  1 380 ? -33.699 11.094  -23.151  1.00 30.93  ? 681  TRP   A O   1 
ATOM   3015  C  CB  . TRP   A  1 380 ? -35.721 13.217  -21.663  1.00 37.56  ? 681  TRP   A CB  1 
ATOM   3016  C  CG  . TRP   A  1 380 ? -34.556 13.344  -20.712  1.00 32.18  ? 681  TRP   A CG  1 
ATOM   3017  C  CD1 . TRP   A  1 380 ? -33.939 14.499  -20.327  1.00 32.15  ? 681  TRP   A CD1 1 
ATOM   3018  C  CD2 . TRP   A  1 380 ? -33.904 12.283  -19.993  1.00 33.00  ? 681  TRP   A CD2 1 
ATOM   3019  N  NE1 . TRP   A  1 380 ? -32.931 14.223  -19.425  1.00 35.22  ? 681  TRP   A NE1 1 
ATOM   3020  C  CE2 . TRP   A  1 380 ? -32.893 12.873  -19.200  1.00 32.90  ? 681  TRP   A CE2 1 
ATOM   3021  C  CE3 . TRP   A  1 380 ? -34.075 10.898  -19.942  1.00 34.14  ? 681  TRP   A CE3 1 
ATOM   3022  C  CZ2 . TRP   A  1 380 ? -32.055 12.122  -18.371  1.00 34.23  ? 681  TRP   A CZ2 1 
ATOM   3023  C  CZ3 . TRP   A  1 380 ? -33.242 10.148  -19.106  1.00 32.22  ? 681  TRP   A CZ3 1 
ATOM   3024  C  CH2 . TRP   A  1 380 ? -32.240 10.765  -18.344  1.00 33.32  ? 681  TRP   A CH2 1 
ATOM   3025  N  N   . VAL   A  1 381 ? -35.837 10.386  -23.109  1.00 30.08  ? 682  VAL   A N   1 
ATOM   3026  C  CA  . VAL   A  1 381 ? -35.506 8.968   -23.088  1.00 30.73  ? 682  VAL   A CA  1 
ATOM   3027  C  C   . VAL   A  1 381 ? -34.675 8.562   -24.302  1.00 34.74  ? 682  VAL   A C   1 
ATOM   3028  O  O   . VAL   A  1 381 ? -33.851 7.638   -24.217  1.00 33.87  ? 682  VAL   A O   1 
ATOM   3029  C  CB  . VAL   A  1 381 ? -36.816 8.164   -22.979  1.00 35.85  ? 682  VAL   A CB  1 
ATOM   3030  C  CG1 . VAL   A  1 381 ? -36.544 6.692   -22.964  1.00 36.05  ? 682  VAL   A CG1 1 
ATOM   3031  C  CG2 . VAL   A  1 381 ? -37.612 8.590   -21.722  1.00 33.86  ? 682  VAL   A CG2 1 
ATOM   3032  N  N   . TRP   A  1 382 ? -34.863 9.248   -25.440  1.00 38.23  ? 683  TRP   A N   1 
ATOM   3033  C  CA  . TRP   A  1 382 ? -34.090 9.037   -26.660  1.00 39.08  ? 683  TRP   A CA  1 
ATOM   3034  C  C   . TRP   A  1 382 ? -32.962 10.045  -26.850  1.00 34.71  ? 683  TRP   A C   1 
ATOM   3035  O  O   . TRP   A  1 382 ? -31.939 9.692   -27.445  1.00 38.70  ? 683  TRP   A O   1 
ATOM   3036  C  CB  . TRP   A  1 382 ? -35.011 9.083   -27.895  1.00 37.81  ? 683  TRP   A CB  1 
ATOM   3037  C  CG  . TRP   A  1 382 ? -35.819 7.845   -28.081  1.00 38.15  ? 683  TRP   A CG  1 
ATOM   3038  C  CD1 . TRP   A  1 382 ? -36.800 7.379   -27.261  1.00 38.72  ? 683  TRP   A CD1 1 
ATOM   3039  C  CD2 . TRP   A  1 382 ? -35.709 6.899   -29.152  1.00 43.41  ? 683  TRP   A CD2 1 
ATOM   3040  N  NE1 . TRP   A  1 382 ? -37.299 6.198   -27.744  1.00 38.55  ? 683  TRP   A NE1 1 
ATOM   3041  C  CE2 . TRP   A  1 382 ? -36.651 5.881   -28.905  1.00 48.55  ? 683  TRP   A CE2 1 
ATOM   3042  C  CE3 . TRP   A  1 382 ? -34.904 6.812   -30.290  1.00 47.03  ? 683  TRP   A CE3 1 
ATOM   3043  C  CZ2 . TRP   A  1 382 ? -36.817 4.791   -29.760  1.00 55.52  ? 683  TRP   A CZ2 1 
ATOM   3044  C  CZ3 . TRP   A  1 382 ? -35.069 5.726   -31.139  1.00 53.29  ? 683  TRP   A CZ3 1 
ATOM   3045  C  CH2 . TRP   A  1 382 ? -36.019 4.734   -30.870  1.00 53.64  ? 683  TRP   A CH2 1 
ATOM   3046  N  N   . ILE   A  1 383 ? -33.126 11.295  -26.388  1.00 27.54  ? 684  ILE   A N   1 
ATOM   3047  C  CA  . ILE   A  1 383 ? -32.078 12.303  -26.590  1.00 30.37  ? 684  ILE   A CA  1 
ATOM   3048  C  C   . ILE   A  1 383 ? -30.819 11.954  -25.792  1.00 38.43  ? 684  ILE   A C   1 
ATOM   3049  O  O   . ILE   A  1 383 ? -29.694 12.179  -26.257  1.00 36.78  ? 684  ILE   A O   1 
ATOM   3050  C  CB  . ILE   A  1 383 ? -32.599 13.707  -26.228  1.00 33.57  ? 684  ILE   A CB  1 
ATOM   3051  C  CG1 . ILE   A  1 383 ? -33.746 14.104  -27.146  1.00 36.95  ? 684  ILE   A CG1 1 
ATOM   3052  C  CG2 . ILE   A  1 383 ? -31.468 14.738  -26.270  1.00 28.26  ? 684  ILE   A CG2 1 
ATOM   3053  C  CD1 . ILE   A  1 383 ? -33.429 13.866  -28.602  1.00 47.68  ? 684  ILE   A CD1 1 
ATOM   3054  N  N   . VAL   A  1 384 ? -30.980 11.390  -24.593  1.00 35.83  ? 685  VAL   A N   1 
ATOM   3055  C  CA  . VAL   A  1 384 ? -29.812 11.082  -23.755  1.00 36.46  ? 685  VAL   A CA  1 
ATOM   3056  C  C   . VAL   A  1 384 ? -29.054 9.904   -24.360  1.00 37.71  ? 685  VAL   A C   1 
ATOM   3057  O  O   . VAL   A  1 384 ? -29.663 8.857   -24.638  1.00 32.54  ? 685  VAL   A O   1 
ATOM   3058  C  CB  . VAL   A  1 384 ? -30.253 10.786  -22.305  1.00 39.93  ? 685  VAL   A CB  1 
ATOM   3059  C  CG1 . VAL   A  1 384 ? -29.087 10.307  -21.450  1.00 26.71  ? 685  VAL   A CG1 1 
ATOM   3060  C  CG2 . VAL   A  1 384 ? -30.869 12.031  -21.691  1.00 42.34  ? 685  VAL   A CG2 1 
ATOM   3061  N  N   . PRO   A  1 385 ? -27.747 10.021  -24.584  1.00 42.83  ? 686  PRO   A N   1 
ATOM   3062  C  CA  . PRO   A  1 385 ? -26.979 8.919   -25.195  1.00 44.20  ? 686  PRO   A CA  1 
ATOM   3063  C  C   . PRO   A  1 385 ? -27.041 7.665   -24.341  1.00 47.17  ? 686  PRO   A C   1 
ATOM   3064  O  O   . PRO   A  1 385 ? -27.259 7.738   -23.123  1.00 42.86  ? 686  PRO   A O   1 
ATOM   3065  C  CB  . PRO   A  1 385 ? -25.547 9.474   -25.256  1.00 39.51  ? 686  PRO   A CB  1 
ATOM   3066  C  CG  . PRO   A  1 385 ? -25.687 10.941  -25.136  1.00 45.35  ? 686  PRO   A CG  1 
ATOM   3067  C  CD  . PRO   A  1 385 ? -26.904 11.192  -24.303  1.00 42.60  ? 686  PRO   A CD  1 
ATOM   3068  N  N   . PRO   A  1 386 ? -26.818 6.492   -24.935  1.00 41.83  ? 687  PRO   A N   1 
ATOM   3069  C  CA  . PRO   A  1 386 ? -26.933 5.235   -24.181  1.00 37.41  ? 687  PRO   A CA  1 
ATOM   3070  C  C   . PRO   A  1 386 ? -25.722 4.885   -23.325  1.00 36.71  ? 687  PRO   A C   1 
ATOM   3071  O  O   . PRO   A  1 386 ? -25.692 3.783   -22.762  1.00 41.47  ? 687  PRO   A O   1 
ATOM   3072  C  CB  . PRO   A  1 386 ? -27.116 4.203   -25.300  1.00 37.11  ? 687  PRO   A CB  1 
ATOM   3073  C  CG  . PRO   A  1 386 ? -26.286 4.779   -26.422  1.00 31.02  ? 687  PRO   A CG  1 
ATOM   3074  C  CD  . PRO   A  1 386 ? -26.460 6.265   -26.349  1.00 30.24  ? 687  PRO   A CD  1 
ATOM   3075  N  N   . MET   A  1 387 ? -24.718 5.760   -23.228  1.00 42.42  ? 688  MET   A N   1 
ATOM   3076  C  CA  . MET   A  1 387 ? -23.620 5.612   -22.278  1.00 39.28  ? 688  MET   A CA  1 
ATOM   3077  C  C   . MET   A  1 387 ? -23.274 6.993   -21.756  1.00 43.73  ? 688  MET   A C   1 
ATOM   3078  O  O   . MET   A  1 387 ? -23.556 7.999   -22.412  1.00 42.06  ? 688  MET   A O   1 
ATOM   3079  C  CB  . MET   A  1 387 ? -22.365 4.973   -22.901  1.00 43.30  ? 688  MET   A CB  1 
ATOM   3080  C  CG  . MET   A  1 387 ? -21.635 5.880   -23.905  1.00 50.24  ? 688  MET   A CG  1 
ATOM   3081  S  SD  . MET   A  1 387 ? -20.095 5.189   -24.587  1.00 45.09  ? 688  MET   A SD  1 
ATOM   3082  C  CE  . MET   A  1 387 ? -19.001 5.311   -23.166  1.00 50.04  ? 688  MET   A CE  1 
ATOM   3083  N  N   . SER   A  1 388 ? -22.674 7.037   -20.557  1.00 40.19  ? 689  SER   A N   1 
ATOM   3084  C  CA  . SER   A  1 388 ? -22.133 8.283   -19.999  1.00 34.80  ? 689  SER   A CA  1 
ATOM   3085  C  C   . SER   A  1 388 ? -23.194 9.377   -19.913  1.00 37.47  ? 689  SER   A C   1 
ATOM   3086  O  O   . SER   A  1 388 ? -22.911 10.555  -20.145  1.00 46.54  ? 689  SER   A O   1 
ATOM   3087  C  CB  . SER   A  1 388 ? -20.932 8.773   -20.814  1.00 30.88  ? 689  SER   A CB  1 
ATOM   3088  O  OG  . SER   A  1 388 ? -19.890 7.816   -20.780  1.00 41.87  ? 689  SER   A OG  1 
ATOM   3089  N  N   . GLY   A  1 389 ? -24.418 8.972   -19.564  1.00 34.72  ? 690  GLY   A N   1 
ATOM   3090  C  CA  . GLY   A  1 389 ? -25.571 9.851   -19.680  1.00 31.72  ? 690  GLY   A CA  1 
ATOM   3091  C  C   . GLY   A  1 389 ? -25.407 11.177  -18.961  1.00 44.41  ? 690  GLY   A C   1 
ATOM   3092  O  O   . GLY   A  1 389 ? -25.561 12.245  -19.563  1.00 41.38  ? 690  GLY   A O   1 
ATOM   3093  N  N   . SER   A  1 390 ? -25.092 11.135  -17.659  1.00 38.50  ? 691  SER   A N   1 
ATOM   3094  C  CA  . SER   A  1 390 ? -25.125 12.373  -16.895  1.00 37.06  ? 691  SER   A CA  1 
ATOM   3095  C  C   . SER   A  1 390 ? -23.902 13.256  -17.118  1.00 40.62  ? 691  SER   A C   1 
ATOM   3096  O  O   . SER   A  1 390 ? -23.877 14.375  -16.598  1.00 40.67  ? 691  SER   A O   1 
ATOM   3097  C  CB  . SER   A  1 390 ? -25.270 12.093  -15.394  1.00 35.94  ? 691  SER   A CB  1 
ATOM   3098  O  OG  . SER   A  1 390 ? -24.045 11.680  -14.850  1.00 31.70  ? 691  SER   A OG  1 
ATOM   3099  N  N   . ILE   A  1 391 ? -22.892 12.807  -17.857  1.00 42.13  ? 692  ILE   A N   1 
ATOM   3100  C  CA  . ILE   A  1 391 ? -21.785 13.714  -18.131  1.00 43.02  ? 692  ILE   A CA  1 
ATOM   3101  C  C   . ILE   A  1 391 ? -22.016 14.412  -19.467  1.00 37.14  ? 692  ILE   A C   1 
ATOM   3102  O  O   . ILE   A  1 391 ? -21.152 15.159  -19.945  1.00 33.86  ? 692  ILE   A O   1 
ATOM   3103  C  CB  . ILE   A  1 391 ? -20.418 13.013  -18.112  1.00 47.52  ? 692  ILE   A CB  1 
ATOM   3104  C  CG1 . ILE   A  1 391 ? -20.288 12.038  -19.257  1.00 40.37  ? 692  ILE   A CG1 1 
ATOM   3105  C  CG2 . ILE   A  1 391 ? -20.147 12.371  -16.751  1.00 38.93  ? 692  ILE   A CG2 1 
ATOM   3106  C  CD1 . ILE   A  1 391 ? -18.900 11.500  -19.389  1.00 43.71  ? 692  ILE   A CD1 1 
ATOM   3107  N  N   . THR   A  1 392 ? -23.207 14.193  -20.071  1.00 38.63  ? 693  THR   A N   1 
ATOM   3108  C  CA  . THR   A  1 392 ? -23.590 14.945  -21.245  1.00 41.69  ? 693  THR   A CA  1 
ATOM   3109  C  C   . THR   A  1 392 ? -24.646 15.968  -20.874  1.00 38.45  ? 693  THR   A C   1 
ATOM   3110  O  O   . THR   A  1 392 ? -25.488 15.703  -20.008  1.00 42.79  ? 693  THR   A O   1 
ATOM   3111  C  CB  . THR   A  1 392 ? -24.147 14.034  -22.341  1.00 43.60  ? 693  THR   A CB  1 
ATOM   3112  O  OG1 . THR   A  1 392 ? -25.329 13.380  -21.859  1.00 42.40  ? 693  THR   A OG1 1 
ATOM   3113  C  CG2 . THR   A  1 392 ? -23.114 13.001  -22.734  1.00 44.20  ? 693  THR   A CG2 1 
ATOM   3114  N  N   . PRO   A  1 393 ? -24.643 17.137  -21.523  1.00 37.46  ? 694  PRO   A N   1 
ATOM   3115  C  CA  . PRO   A  1 393 ? -25.488 18.235  -21.024  1.00 39.89  ? 694  PRO   A CA  1 
ATOM   3116  C  C   . PRO   A  1 393 ? -26.978 17.974  -21.162  1.00 39.90  ? 694  PRO   A C   1 
ATOM   3117  O  O   . PRO   A  1 393 ? -27.739 18.497  -20.343  1.00 35.02  ? 694  PRO   A O   1 
ATOM   3118  C  CB  . PRO   A  1 393 ? -25.038 19.436  -21.866  1.00 38.12  ? 694  PRO   A CB  1 
ATOM   3119  C  CG  . PRO   A  1 393 ? -24.533 18.809  -23.138  1.00 35.32  ? 694  PRO   A CG  1 
ATOM   3120  C  CD  . PRO   A  1 393 ? -23.874 17.532  -22.719  1.00 36.41  ? 694  PRO   A CD  1 
ATOM   3121  N  N   . VAL   A  1 394 ? -27.426 17.173  -22.144  1.00 43.04  ? 695  VAL   A N   1 
ATOM   3122  C  CA  . VAL   A  1 394 ? -28.864 16.942  -22.292  1.00 42.79  ? 695  VAL   A CA  1 
ATOM   3123  C  C   . VAL   A  1 394 ? -29.437 16.209  -21.075  1.00 36.59  ? 695  VAL   A C   1 
ATOM   3124  O  O   . VAL   A  1 394 ? -30.629 16.349  -20.768  1.00 30.05  ? 695  VAL   A O   1 
ATOM   3125  C  CB  . VAL   A  1 394 ? -29.186 16.183  -23.605  1.00 42.20  ? 695  VAL   A CB  1 
ATOM   3126  C  CG1 . VAL   A  1 394 ? -28.863 17.037  -24.845  1.00 40.76  ? 695  VAL   A CG1 1 
ATOM   3127  C  CG2 . VAL   A  1 394 ? -28.477 14.833  -23.668  1.00 25.99  ? 695  VAL   A CG2 1 
ATOM   3128  N  N   . PHE   A  1 395 ? -28.616 15.418  -20.370  1.00 38.99  ? 696  PHE   A N   1 
ATOM   3129  C  CA  . PHE   A  1 395 ? -29.110 14.708  -19.186  1.00 38.57  ? 696  PHE   A CA  1 
ATOM   3130  C  C   . PHE   A  1 395 ? -29.740 15.670  -18.183  1.00 45.52  ? 696  PHE   A C   1 
ATOM   3131  O  O   . PHE   A  1 395 ? -30.762 15.352  -17.562  1.00 37.78  ? 696  PHE   A O   1 
ATOM   3132  C  CB  . PHE   A  1 395 ? -27.984 13.907  -18.516  1.00 35.07  ? 696  PHE   A CB  1 
ATOM   3133  C  CG  . PHE   A  1 395 ? -28.409 13.176  -17.247  1.00 42.03  ? 696  PHE   A CG  1 
ATOM   3134  C  CD1 . PHE   A  1 395 ? -28.450 13.835  -16.024  1.00 41.18  ? 696  PHE   A CD1 1 
ATOM   3135  C  CD2 . PHE   A  1 395 ? -28.729 11.829  -17.276  1.00 35.53  ? 696  PHE   A CD2 1 
ATOM   3136  C  CE1 . PHE   A  1 395 ? -28.846 13.177  -14.861  1.00 42.77  ? 696  PHE   A CE1 1 
ATOM   3137  C  CE2 . PHE   A  1 395 ? -29.107 11.163  -16.122  1.00 42.58  ? 696  PHE   A CE2 1 
ATOM   3138  C  CZ  . PHE   A  1 395 ? -29.175 11.846  -14.907  1.00 36.04  ? 696  PHE   A CZ  1 
ATOM   3139  N  N   . HIS   A  1 396 ? -29.157 16.850  -18.025  1.00 46.07  ? 697  HIS   A N   1 
ATOM   3140  C  CA  . HIS   A  1 396 ? -29.600 17.798  -17.021  1.00 43.12  ? 697  HIS   A CA  1 
ATOM   3141  C  C   . HIS   A  1 396 ? -30.643 18.766  -17.542  1.00 42.75  ? 697  HIS   A C   1 
ATOM   3142  O  O   . HIS   A  1 396 ? -31.066 19.658  -16.795  1.00 36.18  ? 697  HIS   A O   1 
ATOM   3143  C  CB  . HIS   A  1 396 ? -28.392 18.555  -16.481  1.00 40.09  ? 697  HIS   A CB  1 
ATOM   3144  C  CG  . HIS   A  1 396 ? -27.277 17.649  -16.086  1.00 36.00  ? 697  HIS   A CG  1 
ATOM   3145  N  ND1 . HIS   A  1 396 ? -27.117 17.191  -14.799  1.00 35.55  ? 697  HIS   A ND1 1 
ATOM   3146  C  CD2 . HIS   A  1 396 ? -26.302 17.064  -16.819  1.00 40.79  ? 697  HIS   A CD2 1 
ATOM   3147  C  CE1 . HIS   A  1 396 ? -26.072 16.386  -14.748  1.00 41.12  ? 697  HIS   A CE1 1 
ATOM   3148  N  NE2 . HIS   A  1 396 ? -25.561 16.287  -15.961  1.00 35.02  ? 697  HIS   A NE2 1 
ATOM   3149  N  N   . GLN   A  1 397 ? -31.080 18.585  -18.787  1.00 46.63  ? 698  GLN   A N   1 
ATOM   3150  C  CA  . GLN   A  1 397 ? -31.960 19.516  -19.483  1.00 39.06  ? 698  GLN   A CA  1 
ATOM   3151  C  C   . GLN   A  1 397 ? -33.384 18.978  -19.473  1.00 39.46  ? 698  GLN   A C   1 
ATOM   3152  O  O   . GLN   A  1 397 ? -33.667 17.953  -20.103  1.00 36.48  ? 698  GLN   A O   1 
ATOM   3153  C  CB  . GLN   A  1 397 ? -31.498 19.713  -20.924  1.00 34.76  ? 698  GLN   A CB  1 
ATOM   3154  C  CG  . GLN   A  1 397 ? -32.481 20.545  -21.734  1.00 32.17  ? 698  GLN   A CG  1 
ATOM   3155  C  CD  . GLN   A  1 397 ? -32.486 21.979  -21.258  1.00 40.67  ? 698  GLN   A CD  1 
ATOM   3156  O  OE1 . GLN   A  1 397 ? -31.433 22.624  -21.217  1.00 38.95  ? 698  GLN   A OE1 1 
ATOM   3157  N  NE2 . GLN   A  1 397 ? -33.660 22.482  -20.867  1.00 36.95  ? 698  GLN   A NE2 1 
ATOM   3158  N  N   . GLU   A  1 398 ? -34.286 19.682  -18.794  1.00 32.98  ? 699  GLU   A N   1 
ATOM   3159  C  CA  . GLU   A  1 398 ? -35.699 19.345  -18.894  1.00 37.44  ? 699  GLU   A CA  1 
ATOM   3160  C  C   . GLU   A  1 398 ? -36.197 19.517  -20.329  1.00 35.16  ? 699  GLU   A C   1 
ATOM   3161  O  O   . GLU   A  1 398 ? -35.782 20.430  -21.047  1.00 31.05  ? 699  GLU   A O   1 
ATOM   3162  C  CB  . GLU   A  1 398 ? -36.529 20.216  -17.955  1.00 37.90  ? 699  GLU   A CB  1 
ATOM   3163  C  CG  . GLU   A  1 398 ? -36.397 19.845  -16.507  1.00 34.42  ? 699  GLU   A CG  1 
ATOM   3164  C  CD  . GLU   A  1 398 ? -37.264 20.700  -15.605  1.00 47.23  ? 699  GLU   A CD  1 
ATOM   3165  O  OE1 . GLU   A  1 398 ? -37.337 20.400  -14.392  1.00 49.71  ? 699  GLU   A OE1 1 
ATOM   3166  O  OE2 . GLU   A  1 398 ? -37.873 21.675  -16.100  1.00 48.27  ? 699  GLU   A OE2 1 
ATOM   3167  N  N   . MET   A  1 399 ? -37.114 18.642  -20.731  1.00 41.08  ? 700  MET   A N   1 
ATOM   3168  C  CA  . MET   A  1 399 ? -37.638 18.615  -22.089  1.00 42.26  ? 700  MET   A CA  1 
ATOM   3169  C  C   . MET   A  1 399 ? -39.132 18.348  -22.077  1.00 43.30  ? 700  MET   A C   1 
ATOM   3170  O  O   . MET   A  1 399 ? -39.617 17.505  -21.315  1.00 48.47  ? 700  MET   A O   1 
ATOM   3171  C  CB  . MET   A  1 399 ? -36.953 17.531  -22.926  1.00 43.38  ? 700  MET   A CB  1 
ATOM   3172  C  CG  . MET   A  1 399 ? -35.488 17.743  -23.151  1.00 41.63  ? 700  MET   A CG  1 
ATOM   3173  S  SD  . MET   A  1 399 ? -34.734 16.273  -23.860  1.00 40.98  ? 700  MET   A SD  1 
ATOM   3174  C  CE  . MET   A  1 399 ? -33.003 16.704  -23.633  1.00 30.50  ? 700  MET   A CE  1 
ATOM   3175  N  N   . LEU   A  1 400 ? -39.855 19.060  -22.924  1.00 35.02  ? 701  LEU   A N   1 
ATOM   3176  C  CA  . LEU   A  1 400 ? -41.268 18.788  -23.138  1.00 38.92  ? 701  LEU   A CA  1 
ATOM   3177  C  C   . LEU   A  1 400 ? -41.446 18.000  -24.428  1.00 44.91  ? 701  LEU   A C   1 
ATOM   3178  O  O   . LEU   A  1 400 ? -40.817 18.311  -25.447  1.00 37.62  ? 701  LEU   A O   1 
ATOM   3179  C  CB  . LEU   A  1 400 ? -42.071 20.081  -23.211  1.00 39.66  ? 701  LEU   A CB  1 
ATOM   3180  C  CG  . LEU   A  1 400 ? -42.166 20.888  -21.929  1.00 49.41  ? 701  LEU   A CG  1 
ATOM   3181  C  CD1 . LEU   A  1 400 ? -42.903 22.171  -22.238  1.00 50.99  ? 701  LEU   A CD1 1 
ATOM   3182  C  CD2 . LEU   A  1 400 ? -42.860 20.081  -20.843  1.00 51.73  ? 701  LEU   A CD2 1 
ATOM   3183  N  N   . ASN   A  1 401 ? -42.314 16.988  -24.382  1.00 41.56  ? 702  ASN   A N   1 
ATOM   3184  C  CA  . ASN   A  1 401 ? -42.541 16.105  -25.516  1.00 39.93  ? 702  ASN   A CA  1 
ATOM   3185  C  C   . ASN   A  1 401 ? -43.964 16.258  -26.023  1.00 44.37  ? 702  ASN   A C   1 
ATOM   3186  O  O   . ASN   A  1 401 ? -44.917 16.018  -25.281  1.00 42.99  ? 702  ASN   A O   1 
ATOM   3187  C  CB  . ASN   A  1 401 ? -42.273 14.642  -25.163  1.00 30.67  ? 702  ASN   A CB  1 
ATOM   3188  C  CG  . ASN   A  1 401 ? -42.017 13.827  -26.400  1.00 42.04  ? 702  ASN   A CG  1 
ATOM   3189  O  OD1 . ASN   A  1 401 ? -41.563 14.388  -27.380  1.00 42.26  ? 702  ASN   A OD1 1 
ATOM   3190  N  ND2 . ASN   A  1 401 ? -42.337 12.533  -26.391  1.00 35.77  ? 702  ASN   A ND2 1 
ATOM   3191  N  N   . TYR   A  1 402 ? -44.105 16.634  -27.293  1.00 36.20  ? 703  TYR   A N   1 
ATOM   3192  C  CA  . TYR   A  1 402 ? -45.415 16.696  -27.925  1.00 39.98  ? 703  TYR   A CA  1 
ATOM   3193  C  C   . TYR   A  1 402 ? -45.239 16.388  -29.407  1.00 41.51  ? 703  TYR   A C   1 
ATOM   3194  O  O   . TYR   A  1 402 ? -44.121 16.296  -29.910  1.00 45.95  ? 703  TYR   A O   1 
ATOM   3195  C  CB  . TYR   A  1 402 ? -46.106 18.049  -27.687  1.00 34.58  ? 703  TYR   A CB  1 
ATOM   3196  C  CG  . TYR   A  1 402 ? -45.193 19.238  -27.786  1.00 41.38  ? 703  TYR   A CG  1 
ATOM   3197  C  CD1 . TYR   A  1 402 ? -44.495 19.687  -26.678  1.00 32.99  ? 703  TYR   A CD1 1 
ATOM   3198  C  CD2 . TYR   A  1 402 ? -45.016 19.917  -29.002  1.00 36.51  ? 703  TYR   A CD2 1 
ATOM   3199  C  CE1 . TYR   A  1 402 ? -43.640 20.778  -26.765  1.00 34.67  ? 703  TYR   A CE1 1 
ATOM   3200  C  CE2 . TYR   A  1 402 ? -44.167 21.009  -29.100  1.00 33.60  ? 703  TYR   A CE2 1 
ATOM   3201  C  CZ  . TYR   A  1 402 ? -43.485 21.442  -27.971  1.00 42.54  ? 703  TYR   A CZ  1 
ATOM   3202  O  OH  . TYR   A  1 402 ? -42.642 22.526  -28.041  1.00 45.95  ? 703  TYR   A OH  1 
ATOM   3203  N  N   . ARG   A  1 403 ? -46.357 16.194  -30.098  1.00 40.34  ? 704  ARG   A N   1 
ATOM   3204  C  CA  . ARG   A  1 403 ? -46.337 15.703  -31.472  1.00 51.37  ? 704  ARG   A CA  1 
ATOM   3205  C  C   . ARG   A  1 403 ? -46.872 16.784  -32.406  1.00 46.10  ? 704  ARG   A C   1 
ATOM   3206  O  O   . ARG   A  1 403 ? -48.080 17.038  -32.444  1.00 45.85  ? 704  ARG   A O   1 
ATOM   3207  C  CB  . ARG   A  1 403 ? -47.131 14.406  -31.602  1.00 57.16  ? 704  ARG   A CB  1 
ATOM   3208  C  CG  . ARG   A  1 403 ? -47.181 13.876  -33.015  1.00 71.55  ? 704  ARG   A CG  1 
ATOM   3209  C  CD  . ARG   A  1 403 ? -47.541 12.398  -33.066  1.00 84.44  ? 704  ARG   A CD  1 
ATOM   3210  N  NE  . ARG   A  1 403 ? -46.455 11.544  -32.583  1.00 94.42  ? 704  ARG   A NE  1 
ATOM   3211  C  CZ  . ARG   A  1 403 ? -45.305 11.337  -33.227  1.00 97.66  ? 704  ARG   A CZ  1 
ATOM   3212  N  NH1 . ARG   A  1 403 ? -45.062 11.933  -34.387  1.00 100.97 ? 704  ARG   A NH1 1 
ATOM   3213  N  NH2 . ARG   A  1 403 ? -44.387 10.536  -32.704  1.00 96.67  ? 704  ARG   A NH2 1 
ATOM   3214  N  N   . LEU   A  1 404 ? -45.965 17.432  -33.130  1.00 38.49  ? 705  LEU   A N   1 
ATOM   3215  C  CA  . LEU   A  1 404 ? -46.313 18.357  -34.196  1.00 38.47  ? 705  LEU   A CA  1 
ATOM   3216  C  C   . LEU   A  1 404 ? -46.326 17.630  -35.535  1.00 43.09  ? 705  LEU   A C   1 
ATOM   3217  O  O   . LEU   A  1 404 ? -45.625 16.629  -35.736  1.00 43.89  ? 705  LEU   A O   1 
ATOM   3218  C  CB  . LEU   A  1 404 ? -45.325 19.518  -34.278  1.00 34.91  ? 705  LEU   A CB  1 
ATOM   3219  C  CG  . LEU   A  1 404 ? -45.020 20.309  -33.010  1.00 35.72  ? 705  LEU   A CG  1 
ATOM   3220  C  CD1 . LEU   A  1 404 ? -43.823 21.226  -33.274  1.00 38.92  ? 705  LEU   A CD1 1 
ATOM   3221  C  CD2 . LEU   A  1 404 ? -46.239 21.106  -32.599  1.00 36.64  ? 705  LEU   A CD2 1 
ATOM   3222  N  N   . THR   A  1 405 ? -47.115 18.158  -36.460  1.00 44.27  ? 706  THR   A N   1 
ATOM   3223  C  CA  . THR   A  1 405 ? -47.084 17.647  -37.822  1.00 42.72  ? 706  THR   A CA  1 
ATOM   3224  C  C   . THR   A  1 405 ? -46.632 18.740  -38.804  1.00 38.97  ? 706  THR   A C   1 
ATOM   3225  O  O   . THR   A  1 405 ? -46.787 19.935  -38.522  1.00 31.92  ? 706  THR   A O   1 
ATOM   3226  C  CB  . THR   A  1 405 ? -48.467 17.098  -38.194  1.00 40.76  ? 706  THR   A CB  1 
ATOM   3227  O  OG1 . THR   A  1 405 ? -48.406 16.441  -39.462  1.00 53.73  ? 706  THR   A OG1 1 
ATOM   3228  C  CG2 . THR   A  1 405 ? -49.505 18.203  -38.238  1.00 28.35  ? 706  THR   A CG2 1 
ATOM   3229  N  N   . PRO   A  1 406 ? -46.009 18.379  -39.945  1.00 37.72  ? 707  PRO   A N   1 
ATOM   3230  C  CA  . PRO   A  1 406 ? -45.596 17.071  -40.462  1.00 41.24  ? 707  PRO   A CA  1 
ATOM   3231  C  C   . PRO   A  1 406 ? -44.757 16.311  -39.469  1.00 36.32  ? 707  PRO   A C   1 
ATOM   3232  O  O   . PRO   A  1 406 ? -43.989 16.922  -38.735  1.00 34.53  ? 707  PRO   A O   1 
ATOM   3233  C  CB  . PRO   A  1 406 ? -44.761 17.418  -41.708  1.00 37.23  ? 707  PRO   A CB  1 
ATOM   3234  C  CG  . PRO   A  1 406 ? -45.228 18.731  -42.118  1.00 38.49  ? 707  PRO   A CG  1 
ATOM   3235  C  CD  . PRO   A  1 406 ? -45.626 19.465  -40.864  1.00 33.11  ? 707  PRO   A CD  1 
ATOM   3236  N  N   . SER   A  1 407 ? -44.900 14.996  -39.457  1.00 38.27  ? 708  SER   A N   1 
ATOM   3237  C  CA  . SER   A  1 407 ? -44.124 14.166  -38.559  1.00 41.46  ? 708  SER   A CA  1 
ATOM   3238  C  C   . SER   A  1 407 ? -43.666 12.917  -39.289  1.00 34.60  ? 708  SER   A C   1 
ATOM   3239  O  O   . SER   A  1 407 ? -44.266 12.510  -40.286  1.00 45.91  ? 708  SER   A O   1 
ATOM   3240  C  CB  . SER   A  1 407 ? -44.942 13.779  -37.333  1.00 46.49  ? 708  SER   A CB  1 
ATOM   3241  O  OG  . SER   A  1 407 ? -46.075 13.057  -37.742  1.00 54.09  ? 708  SER   A OG  1 
ATOM   3242  N  N   . PHE   A  1 408 ? -42.566 12.347  -38.809  1.00 27.68  ? 709  PHE   A N   1 
ATOM   3243  C  CA  . PHE   A  1 408 ? -42.213 10.970  -39.119  1.00 30.67  ? 709  PHE   A CA  1 
ATOM   3244  C  C   . PHE   A  1 408 ? -42.900 10.044  -38.125  1.00 37.21  ? 709  PHE   A C   1 
ATOM   3245  O  O   . PHE   A  1 408 ? -43.020 10.358  -36.936  1.00 46.43  ? 709  PHE   A O   1 
ATOM   3246  C  CB  . PHE   A  1 408 ? -40.699 10.755  -39.102  1.00 24.43  ? 709  PHE   A CB  1 
ATOM   3247  C  CG  . PHE   A  1 408 ? -39.994 11.385  -40.263  1.00 30.78  ? 709  PHE   A CG  1 
ATOM   3248  C  CD1 . PHE   A  1 408 ? -40.147 10.865  -41.550  1.00 34.40  ? 709  PHE   A CD1 1 
ATOM   3249  C  CD2 . PHE   A  1 408 ? -39.186 12.501  -40.081  1.00 24.25  ? 709  PHE   A CD2 1 
ATOM   3250  C  CE1 . PHE   A  1 408 ? -39.508 11.457  -42.640  1.00 32.77  ? 709  PHE   A CE1 1 
ATOM   3251  C  CE2 . PHE   A  1 408 ? -38.533 13.081  -41.154  1.00 34.16  ? 709  PHE   A CE2 1 
ATOM   3252  C  CZ  . PHE   A  1 408 ? -38.702 12.562  -42.447  1.00 32.55  ? 709  PHE   A CZ  1 
ATOM   3253  N  N   . GLU   A  1 409 ? -43.364 8.909   -38.629  1.00 37.76  ? 710  GLU   A N   1 
ATOM   3254  C  CA  . GLU   A  1 409 ? -44.254 8.015   -37.915  1.00 34.75  ? 710  GLU   A CA  1 
ATOM   3255  C  C   . GLU   A  1 409 ? -43.789 6.586   -38.135  1.00 43.34  ? 710  GLU   A C   1 
ATOM   3256  O  O   . GLU   A  1 409 ? -43.216 6.258   -39.176  1.00 40.73  ? 710  GLU   A O   1 
ATOM   3257  C  CB  . GLU   A  1 409 ? -45.703 8.162   -38.405  1.00 37.91  ? 710  GLU   A CB  1 
ATOM   3258  C  CG  . GLU   A  1 409 ? -46.344 9.525   -38.193  1.00 48.88  ? 710  GLU   A CG  1 
ATOM   3259  C  CD  . GLU   A  1 409 ? -46.704 9.789   -36.730  1.00 60.47  ? 710  GLU   A CD  1 
ATOM   3260  O  OE1 . GLU   A  1 409 ? -46.701 8.827   -35.921  1.00 60.66  ? 710  GLU   A OE1 1 
ATOM   3261  O  OE2 . GLU   A  1 409 ? -46.988 10.964  -36.393  1.00 58.91  ? 710  GLU   A OE2 1 
ATOM   3262  N  N   . TYR   A  1 410 ? -44.050 5.735   -37.151  1.00 47.39  ? 711  TYR   A N   1 
ATOM   3263  C  CA  . TYR   A  1 410 ? -43.850 4.312   -37.356  1.00 46.51  ? 711  TYR   A CA  1 
ATOM   3264  C  C   . TYR   A  1 410 ? -45.023 3.724   -38.118  1.00 45.42  ? 711  TYR   A C   1 
ATOM   3265  O  O   . TYR   A  1 410 ? -46.152 4.204   -38.033  1.00 43.99  ? 711  TYR   A O   1 
ATOM   3266  C  CB  . TYR   A  1 410 ? -43.710 3.570   -36.032  1.00 47.66  ? 711  TYR   A CB  1 
ATOM   3267  C  CG  . TYR   A  1 410 ? -42.601 4.056   -35.146  1.00 59.09  ? 711  TYR   A CG  1 
ATOM   3268  C  CD1 . TYR   A  1 410 ? -41.268 3.918   -35.515  1.00 64.47  ? 711  TYR   A CD1 1 
ATOM   3269  C  CD2 . TYR   A  1 410 ? -42.886 4.618   -33.910  1.00 69.46  ? 711  TYR   A CD2 1 
ATOM   3270  C  CE1 . TYR   A  1 410 ? -40.251 4.346   -34.681  1.00 71.19  ? 711  TYR   A CE1 1 
ATOM   3271  C  CE2 . TYR   A  1 410 ? -41.884 5.043   -33.070  1.00 75.14  ? 711  TYR   A CE2 1 
ATOM   3272  C  CZ  . TYR   A  1 410 ? -40.572 4.908   -33.457  1.00 75.21  ? 711  TYR   A CZ  1 
ATOM   3273  O  OH  . TYR   A  1 410 ? -39.587 5.339   -32.608  1.00 78.42  ? 711  TYR   A OH  1 
ATOM   3274  N  N   . GLN   A  1 411 ? -44.744 2.679   -38.871  1.00 47.73  ? 712  GLN   A N   1 
ATOM   3275  C  CA  . GLN   A  1 411 ? -45.790 1.908   -39.518  1.00 49.78  ? 712  GLN   A CA  1 
ATOM   3276  C  C   . GLN   A  1 411 ? -45.474 0.436   -39.314  1.00 36.04  ? 712  GLN   A C   1 
ATOM   3277  O  O   . GLN   A  1 411 ? -44.335 0.079   -38.996  1.00 39.21  ? 712  GLN   A O   1 
ATOM   3278  C  CB  . GLN   A  1 411 ? -45.908 2.259   -41.011  1.00 51.68  ? 712  GLN   A CB  1 
ATOM   3279  C  CG  . GLN   A  1 411 ? -44.639 2.086   -41.804  1.00 45.87  ? 712  GLN   A CG  1 
ATOM   3280  C  CD  . GLN   A  1 411 ? -44.773 2.633   -43.212  1.00 44.34  ? 712  GLN   A CD  1 
ATOM   3281  O  OE1 . GLN   A  1 411 ? -45.874 2.725   -43.760  1.00 45.00  ? 712  GLN   A OE1 1 
ATOM   3282  N  NE2 . GLN   A  1 411 ? -43.647 3.015   -43.796  1.00 35.75  ? 712  GLN   A NE2 1 
ATOM   3283  N  N   . PRO   A  1 412 ? -46.460 -0.436  -39.451  1.00 40.44  ? 713  PRO   A N   1 
ATOM   3284  C  CA  . PRO   A  1 412 ? -46.181 -1.867  -39.326  1.00 51.87  ? 713  PRO   A CA  1 
ATOM   3285  C  C   . PRO   A  1 412 ? -45.257 -2.358  -40.433  1.00 54.96  ? 713  PRO   A C   1 
ATOM   3286  O  O   . PRO   A  1 412 ? -45.135 -1.760  -41.508  1.00 46.73  ? 713  PRO   A O   1 
ATOM   3287  C  CB  . PRO   A  1 412 ? -47.566 -2.520  -39.414  1.00 56.26  ? 713  PRO   A CB  1 
ATOM   3288  C  CG  . PRO   A  1 412 ? -48.473 -1.481  -39.972  1.00 49.69  ? 713  PRO   A CG  1 
ATOM   3289  C  CD  . PRO   A  1 412 ? -47.897 -0.153  -39.602  1.00 45.93  ? 713  PRO   A CD  1 
ATOM   3290  N  N   . ASP   A  1 413 ? -44.572 -3.457  -40.128  1.00 58.50  ? 714  ASP   A N   1 
ATOM   3291  C  CA  . ASP   A  1 413 ? -43.672 -4.074  -41.084  1.00 60.06  ? 714  ASP   A CA  1 
ATOM   3292  C  C   . ASP   A  1 413 ? -44.453 -4.571  -42.294  1.00 61.83  ? 714  ASP   A C   1 
ATOM   3293  O  O   . ASP   A  1 413 ? -45.557 -5.108  -42.146  1.00 67.78  ? 714  ASP   A O   1 
ATOM   3294  C  CB  . ASP   A  1 413 ? -42.918 -5.232  -40.436  1.00 64.75  ? 714  ASP   A CB  1 
ATOM   3295  C  CG  . ASP   A  1 413 ? -41.875 -4.755  -39.469  1.00 65.69  ? 714  ASP   A CG  1 
ATOM   3296  O  OD1 . ASP   A  1 413 ? -41.597 -3.539  -39.470  1.00 66.60  ? 714  ASP   A OD1 1 
ATOM   3297  O  OD2 . ASP   A  1 413 ? -41.338 -5.581  -38.711  1.00 70.04  ? 714  ASP   A OD2 1 
ATOM   3298  N  N   . PRO   A  1 414 ? -43.904 -4.428  -43.499  1.00 58.17  ? 715  PRO   A N   1 
ATOM   3299  C  CA  . PRO   A  1 414 ? -44.702 -4.724  -44.698  1.00 50.29  ? 715  PRO   A CA  1 
ATOM   3300  C  C   . PRO   A  1 414 ? -45.187 -6.155  -44.752  1.00 48.46  ? 715  PRO   A C   1 
ATOM   3301  O  O   . PRO   A  1 414 ? -46.308 -6.411  -45.212  1.00 45.33  ? 715  PRO   A O   1 
ATOM   3302  C  CB  . PRO   A  1 414 ? -43.734 -4.415  -45.844  1.00 49.38  ? 715  PRO   A CB  1 
ATOM   3303  C  CG  . PRO   A  1 414 ? -42.672 -3.572  -45.256  1.00 48.51  ? 715  PRO   A CG  1 
ATOM   3304  C  CD  . PRO   A  1 414 ? -42.550 -3.957  -43.822  1.00 52.21  ? 715  PRO   A CD  1 
ATOM   3305  N  N   . TRP   A  1 415 ? -44.369 -7.103  -44.294  1.00 51.57  ? 716  TRP   A N   1 
ATOM   3306  C  CA  . TRP   A  1 415 ? -44.736 -8.510  -44.387  1.00 51.47  ? 716  TRP   A CA  1 
ATOM   3307  C  C   . TRP   A  1 415 ? -45.829 -8.908  -43.409  1.00 57.77  ? 716  TRP   A C   1 
ATOM   3308  O  O   . TRP   A  1 415 ? -46.383 -10.003 -43.549  1.00 64.11  ? 716  TRP   A O   1 
ATOM   3309  C  CB  . TRP   A  1 415 ? -43.513 -9.391  -44.169  1.00 49.86  ? 716  TRP   A CB  1 
ATOM   3310  C  CG  . TRP   A  1 415 ? -42.753 -9.113  -42.915  1.00 49.63  ? 716  TRP   A CG  1 
ATOM   3311  C  CD1 . TRP   A  1 415 ? -42.947 -9.694  -41.690  1.00 50.41  ? 716  TRP   A CD1 1 
ATOM   3312  C  CD2 . TRP   A  1 415 ? -41.643 -8.216  -42.764  1.00 42.57  ? 716  TRP   A CD2 1 
ATOM   3313  N  NE1 . TRP   A  1 415 ? -42.031 -9.204  -40.783  1.00 47.55  ? 716  TRP   A NE1 1 
ATOM   3314  C  CE2 . TRP   A  1 415 ? -41.221 -8.295  -41.415  1.00 48.69  ? 716  TRP   A CE2 1 
ATOM   3315  C  CE3 . TRP   A  1 415 ? -40.966 -7.358  -43.634  1.00 47.31  ? 716  TRP   A CE3 1 
ATOM   3316  C  CZ2 . TRP   A  1 415 ? -40.156 -7.546  -40.919  1.00 45.70  ? 716  TRP   A CZ2 1 
ATOM   3317  C  CZ3 . TRP   A  1 415 ? -39.911 -6.607  -43.140  1.00 51.87  ? 716  TRP   A CZ3 1 
ATOM   3318  C  CH2 . TRP   A  1 415 ? -39.517 -6.707  -41.790  1.00 54.31  ? 716  TRP   A CH2 1 
ATOM   3319  N  N   . ASN   A  1 416 ? -46.159 -8.060  -42.433  1.00 54.13  ? 717  ASN   A N   1 
ATOM   3320  C  CA  . ASN   A  1 416 ? -47.273 -8.341  -41.535  1.00 53.26  ? 717  ASN   A CA  1 
ATOM   3321  C  C   . ASN   A  1 416 ? -48.623 -7.959  -42.116  1.00 57.80  ? 717  ASN   A C   1 
ATOM   3322  O  O   . ASN   A  1 416 ? -49.650 -8.292  -41.525  1.00 66.07  ? 717  ASN   A O   1 
ATOM   3323  C  CB  . ASN   A  1 416 ? -47.071 -7.608  -40.216  1.00 45.61  ? 717  ASN   A CB  1 
ATOM   3324  C  CG  . ASN   A  1 416 ? -45.891 -8.140  -39.447  1.00 53.38  ? 717  ASN   A CG  1 
ATOM   3325  O  OD1 . ASN   A  1 416 ? -45.553 -9.320  -39.559  1.00 57.52  ? 717  ASN   A OD1 1 
ATOM   3326  N  ND2 . ASN   A  1 416 ? -45.244 -7.277  -38.675  1.00 54.62  ? 717  ASN   A ND2 1 
ATOM   3327  N  N   . THR   A  1 417 ? -48.651 -7.253  -43.239  1.00 57.58  ? 718  THR   A N   1 
ATOM   3328  C  CA  . THR   A  1 417 ? -49.903 -6.791  -43.822  1.00 58.50  ? 718  THR   A CA  1 
ATOM   3329  C  C   . THR   A  1 417 ? -49.996 -6.995  -45.323  1.00 61.66  ? 718  THR   A C   1 
ATOM   3330  O  O   . THR   A  1 417 ? -51.111 -6.958  -45.856  1.00 61.33  ? 718  THR   A O   1 
ATOM   3331  C  CB  . THR   A  1 417 ? -50.120 -5.303  -43.522  1.00 53.30  ? 718  THR   A CB  1 
ATOM   3332  O  OG1 . THR   A  1 417 ? -49.043 -4.551  -44.089  1.00 58.11  ? 718  THR   A OG1 1 
ATOM   3333  C  CG2 . THR   A  1 417 ? -50.174 -5.044  -42.013  1.00 44.72  ? 718  THR   A CG2 1 
ATOM   3334  N  N   . HIS   A  1 418 ? -48.882 -7.188  -46.023  1.00 60.72  ? 719  HIS   A N   1 
ATOM   3335  C  CA  . HIS   A  1 418 ? -48.946 -7.429  -47.455  1.00 61.67  ? 719  HIS   A CA  1 
ATOM   3336  C  C   . HIS   A  1 418 ? -49.547 -8.800  -47.724  1.00 68.19  ? 719  HIS   A C   1 
ATOM   3337  O  O   . HIS   A  1 418 ? -49.202 -9.786  -47.069  1.00 71.64  ? 719  HIS   A O   1 
ATOM   3338  C  CB  . HIS   A  1 418 ? -47.555 -7.336  -48.084  1.00 58.12  ? 719  HIS   A CB  1 
ATOM   3339  C  CG  . HIS   A  1 418 ? -47.535 -7.658  -49.544  1.00 53.43  ? 719  HIS   A CG  1 
ATOM   3340  N  ND1 . HIS   A  1 418 ? -47.899 -6.744  -50.510  1.00 52.13  ? 719  HIS   A ND1 1 
ATOM   3341  C  CD2 . HIS   A  1 418 ? -47.221 -8.798  -50.203  1.00 55.70  ? 719  HIS   A CD2 1 
ATOM   3342  C  CE1 . HIS   A  1 418 ? -47.800 -7.305  -51.702  1.00 57.33  ? 719  HIS   A CE1 1 
ATOM   3343  N  NE2 . HIS   A  1 418 ? -47.395 -8.553  -51.544  1.00 54.21  ? 719  HIS   A NE2 1 
ATOM   3344  N  N   . VAL   A  1 419 ? -50.471 -8.858  -48.678  1.00 73.09  ? 720  VAL   A N   1 
ATOM   3345  C  CA  . VAL   A  1 419 ? -51.009 -10.120 -49.163  1.00 78.89  ? 720  VAL   A CA  1 
ATOM   3346  C  C   . VAL   A  1 419 ? -50.474 -10.336 -50.571  1.00 75.78  ? 720  VAL   A C   1 
ATOM   3347  O  O   . VAL   A  1 419 ? -50.539 -9.435  -51.419  1.00 74.46  ? 720  VAL   A O   1 
ATOM   3348  C  CB  . VAL   A  1 419 ? -52.545 -10.153 -49.119  1.00 77.59  ? 720  VAL   A CB  1 
ATOM   3349  C  CG1 . VAL   A  1 419 ? -53.029 -11.595 -49.229  1.00 78.01  ? 720  VAL   A CG1 1 
ATOM   3350  C  CG2 . VAL   A  1 419 ? -53.044 -9.525  -47.832  1.00 70.95  ? 720  VAL   A CG2 1 
ATOM   3351  N  N   . TRP   A  1 420 ? -49.945 -11.530 -50.810  1.00 77.53  ? 721  TRP   A N   1 
ATOM   3352  C  CA  . TRP   A  1 420 ? -49.087 -11.781 -51.955  1.00 79.08  ? 721  TRP   A CA  1 
ATOM   3353  C  C   . TRP   A  1 420 ? -49.903 -12.089 -53.207  1.00 84.34  ? 721  TRP   A C   1 
ATOM   3354  O  O   . TRP   A  1 420 ? -50.854 -12.877 -53.163  1.00 85.79  ? 721  TRP   A O   1 
ATOM   3355  C  CB  . TRP   A  1 420 ? -48.132 -12.926 -51.623  1.00 70.57  ? 721  TRP   A CB  1 
ATOM   3356  C  CG  . TRP   A  1 420 ? -47.053 -12.490 -50.685  1.00 61.05  ? 721  TRP   A CG  1 
ATOM   3357  C  CD1 . TRP   A  1 420 ? -47.141 -12.347 -49.320  1.00 54.46  ? 721  TRP   A CD1 1 
ATOM   3358  C  CD2 . TRP   A  1 420 ? -45.730 -12.093 -51.044  1.00 57.23  ? 721  TRP   A CD2 1 
ATOM   3359  N  NE1 . TRP   A  1 420 ? -45.942 -11.905 -48.816  1.00 48.33  ? 721  TRP   A NE1 1 
ATOM   3360  C  CE2 . TRP   A  1 420 ? -45.061 -11.739 -49.852  1.00 54.52  ? 721  TRP   A CE2 1 
ATOM   3361  C  CE3 . TRP   A  1 420 ? -45.039 -12.016 -52.256  1.00 54.83  ? 721  TRP   A CE3 1 
ATOM   3362  C  CZ2 . TRP   A  1 420 ? -43.739 -11.313 -49.841  1.00 60.24  ? 721  TRP   A CZ2 1 
ATOM   3363  C  CZ3 . TRP   A  1 420 ? -43.735 -11.590 -52.246  1.00 59.38  ? 721  TRP   A CZ3 1 
ATOM   3364  C  CH2 . TRP   A  1 420 ? -43.093 -11.244 -51.045  1.00 59.12  ? 721  TRP   A CH2 1 
ATOM   3365  N  N   . LYS   A  1 421 ? -49.524 -11.452 -54.319  1.00 89.83  ? 722  LYS   A N   1 
ATOM   3366  C  CA  . LYS   A  1 421 ? -50.170 -11.637 -55.620  1.00 92.92  ? 722  LYS   A CA  1 
ATOM   3367  C  C   . LYS   A  1 421 ? -49.683 -12.901 -56.331  1.00 89.82  ? 722  LYS   A C   1 
ATOM   3368  O  O   . LYS   A  1 421 ? -50.467 -13.597 -56.981  1.00 90.10  ? 722  LYS   A O   1 
ATOM   3369  C  CB  . LYS   A  1 421 ? -49.920 -10.421 -56.526  1.00 95.70  ? 722  LYS   A CB  1 
ATOM   3370  C  CG  . LYS   A  1 421 ? -49.431 -9.166  -55.802  1.00 98.63  ? 722  LYS   A CG  1 
ATOM   3371  C  CD  . LYS   A  1 421 ? -50.565 -8.325  -55.231  1.00 96.10  ? 722  LYS   A CD  1 
ATOM   3372  C  CE  . LYS   A  1 421 ? -50.719 -7.032  -56.020  1.00 92.45  ? 722  LYS   A CE  1 
ATOM   3373  N  NZ  . LYS   A  1 421 ? -51.949 -6.287  -55.643  1.00 91.01  ? 722  LYS   A NZ  1 
ATOM   3374  N  N   . PHE   B  1 4   ? -56.478 -1.180  -19.013  1.00 73.81  ? 305  PHE   B N   1 
ATOM   3375  C  CA  . PHE   B  1 4   ? -55.393 -2.116  -18.708  1.00 73.58  ? 305  PHE   B CA  1 
ATOM   3376  C  C   . PHE   B  1 4   ? -54.250 -1.997  -19.714  1.00 62.99  ? 305  PHE   B C   1 
ATOM   3377  O  O   . PHE   B  1 4   ? -54.455 -2.168  -20.909  1.00 67.53  ? 305  PHE   B O   1 
ATOM   3378  C  CB  . PHE   B  1 4   ? -55.917 -3.547  -18.689  1.00 82.13  ? 305  PHE   B CB  1 
ATOM   3379  C  CG  . PHE   B  1 4   ? -57.345 -3.658  -18.253  1.00 90.45  ? 305  PHE   B CG  1 
ATOM   3380  C  CD1 . PHE   B  1 4   ? -57.681 -3.616  -16.905  1.00 90.69  ? 305  PHE   B CD1 1 
ATOM   3381  C  CD2 . PHE   B  1 4   ? -58.356 -3.805  -19.192  1.00 94.58  ? 305  PHE   B CD2 1 
ATOM   3382  C  CE1 . PHE   B  1 4   ? -59.000 -3.718  -16.497  1.00 93.68  ? 305  PHE   B CE1 1 
ATOM   3383  C  CE2 . PHE   B  1 4   ? -59.675 -3.907  -18.799  1.00 100.82 ? 305  PHE   B CE2 1 
ATOM   3384  C  CZ  . PHE   B  1 4   ? -60.000 -3.864  -17.443  1.00 101.11 ? 305  PHE   B CZ  1 
ATOM   3385  N  N   . LEU   B  1 5   ? -53.045 -1.736  -19.212  1.00 58.11  ? 306  LEU   B N   1 
ATOM   3386  C  CA  . LEU   B  1 5   ? -51.896 -1.369  -20.027  1.00 55.42  ? 306  LEU   B CA  1 
ATOM   3387  C  C   . LEU   B  1 5   ? -50.779 -2.393  -19.884  1.00 52.20  ? 306  LEU   B C   1 
ATOM   3388  O  O   . LEU   B  1 5   ? -50.558 -2.946  -18.807  1.00 56.21  ? 306  LEU   B O   1 
ATOM   3389  C  CB  . LEU   B  1 5   ? -51.381 0.016   -19.638  1.00 48.08  ? 306  LEU   B CB  1 
ATOM   3390  C  CG  . LEU   B  1 5   ? -52.506 1.046   -19.617  1.00 44.95  ? 306  LEU   B CG  1 
ATOM   3391  C  CD1 . LEU   B  1 5   ? -52.086 2.269   -18.868  1.00 44.33  ? 306  LEU   B CD1 1 
ATOM   3392  C  CD2 . LEU   B  1 5   ? -52.894 1.403   -21.035  1.00 44.47  ? 306  LEU   B CD2 1 
ATOM   3393  N  N   . LYS   B  1 6   ? -50.070 -2.623  -20.986  1.00 47.19  ? 307  LYS   B N   1 
ATOM   3394  C  CA  . LYS   B  1 6   ? -48.966 -3.568  -21.057  1.00 45.23  ? 307  LYS   B CA  1 
ATOM   3395  C  C   . LYS   B  1 6   ? -47.644 -2.821  -21.141  1.00 49.82  ? 307  LYS   B C   1 
ATOM   3396  O  O   . LYS   B  1 6   ? -47.563 -1.750  -21.750  1.00 53.54  ? 307  LYS   B O   1 
ATOM   3397  C  CB  . LYS   B  1 6   ? -49.094 -4.480  -22.279  1.00 47.77  ? 307  LYS   B CB  1 
ATOM   3398  C  CG  . LYS   B  1 6   ? -50.447 -5.117  -22.476  1.00 60.13  ? 307  LYS   B CG  1 
ATOM   3399  C  CD  . LYS   B  1 6   ? -50.383 -6.623  -22.273  1.00 74.24  ? 307  LYS   B CD  1 
ATOM   3400  C  CE  . LYS   B  1 6   ? -51.251 -7.372  -23.279  1.00 77.60  ? 307  LYS   B CE  1 
ATOM   3401  N  NZ  . LYS   B  1 6   ? -51.530 -8.750  -22.784  1.00 81.49  ? 307  LYS   B NZ  1 
ATOM   3402  N  N   . VAL   B  1 7   ? -46.605 -3.383  -20.531  1.00 46.36  ? 308  VAL   B N   1 
ATOM   3403  C  CA  . VAL   B  1 7   ? -45.243 -2.903  -20.723  1.00 42.57  ? 308  VAL   B CA  1 
ATOM   3404  C  C   . VAL   B  1 7   ? -44.421 -4.065  -21.249  1.00 46.62  ? 308  VAL   B C   1 
ATOM   3405  O  O   . VAL   B  1 7   ? -44.662 -5.222  -20.890  1.00 47.08  ? 308  VAL   B O   1 
ATOM   3406  C  CB  . VAL   B  1 7   ? -44.616 -2.328  -19.437  1.00 48.73  ? 308  VAL   B CB  1 
ATOM   3407  C  CG1 . VAL   B  1 7   ? -45.538 -1.302  -18.797  1.00 52.13  ? 308  VAL   B CG1 1 
ATOM   3408  C  CG2 . VAL   B  1 7   ? -44.255 -3.426  -18.473  1.00 45.57  ? 308  VAL   B CG2 1 
ATOM   3409  N  N   . LYS   B  1 8   ? -43.471 -3.764  -22.125  1.00 40.97  ? 309  LYS   B N   1 
ATOM   3410  C  CA  . LYS   B  1 8   ? -42.665 -4.798  -22.742  1.00 37.59  ? 309  LYS   B CA  1 
ATOM   3411  C  C   . LYS   B  1 8   ? -41.202 -4.504  -22.493  1.00 36.23  ? 309  LYS   B C   1 
ATOM   3412  O  O   . LYS   B  1 8   ? -40.773 -3.351  -22.564  1.00 50.07  ? 309  LYS   B O   1 
ATOM   3413  C  CB  . LYS   B  1 8   ? -42.939 -4.897  -24.252  1.00 46.22  ? 309  LYS   B CB  1 
ATOM   3414  C  CG  . LYS   B  1 8   ? -42.032 -5.852  -25.026  1.00 49.07  ? 309  LYS   B CG  1 
ATOM   3415  C  CD  . LYS   B  1 8   ? -42.437 -5.923  -26.506  1.00 54.18  ? 309  LYS   B CD  1 
ATOM   3416  C  CE  . LYS   B  1 8   ? -41.348 -6.548  -27.359  1.00 54.67  ? 309  LYS   B CE  1 
ATOM   3417  N  NZ  . LYS   B  1 8   ? -41.726 -6.590  -28.815  1.00 55.17  ? 309  LYS   B NZ  1 
ATOM   3418  N  N   . ASN   B  1 9   ? -40.444 -5.561  -22.210  1.00 38.42  ? 310  ASN   B N   1 
ATOM   3419  C  CA  . ASN   B  1 9   ? -38.988 -5.498  -22.187  1.00 46.45  ? 310  ASN   B CA  1 
ATOM   3420  C  C   . ASN   B  1 9   ? -38.454 -5.944  -23.547  1.00 50.04  ? 310  ASN   B C   1 
ATOM   3421  O  O   . ASN   B  1 9   ? -38.802 -7.025  -24.030  1.00 49.57  ? 310  ASN   B O   1 
ATOM   3422  C  CB  . ASN   B  1 9   ? -38.442 -6.378  -21.064  1.00 46.70  ? 310  ASN   B CB  1 
ATOM   3423  C  CG  . ASN   B  1 9   ? -36.944 -6.283  -20.935  1.00 50.39  ? 310  ASN   B CG  1 
ATOM   3424  O  OD1 . ASN   B  1 9   ? -36.208 -6.669  -21.855  1.00 50.89  ? 310  ASN   B OD1 1 
ATOM   3425  N  ND2 . ASN   B  1 9   ? -36.472 -5.779  -19.793  1.00 47.03  ? 310  ASN   B ND2 1 
ATOM   3426  N  N   . TRP   B  1 10  ? -37.629 -5.105  -24.176  1.00 53.72  ? 311  TRP   B N   1 
ATOM   3427  C  CA  . TRP   B  1 10  ? -37.223 -5.360  -25.556  1.00 51.53  ? 311  TRP   B CA  1 
ATOM   3428  C  C   . TRP   B  1 10  ? -35.967 -6.205  -25.657  1.00 53.92  ? 311  TRP   B C   1 
ATOM   3429  O  O   . TRP   B  1 10  ? -35.526 -6.504  -26.768  1.00 56.27  ? 311  TRP   B O   1 
ATOM   3430  C  CB  . TRP   B  1 10  ? -37.021 -4.046  -26.313  1.00 42.06  ? 311  TRP   B CB  1 
ATOM   3431  C  CG  . TRP   B  1 10  ? -38.291 -3.320  -26.514  1.00 36.39  ? 311  TRP   B CG  1 
ATOM   3432  C  CD1 . TRP   B  1 10  ? -38.879 -2.447  -25.648  1.00 33.41  ? 311  TRP   B CD1 1 
ATOM   3433  C  CD2 . TRP   B  1 10  ? -39.148 -3.391  -27.657  1.00 42.83  ? 311  TRP   B CD2 1 
ATOM   3434  N  NE1 . TRP   B  1 10  ? -40.052 -1.968  -26.177  1.00 41.90  ? 311  TRP   B NE1 1 
ATOM   3435  C  CE2 . TRP   B  1 10  ? -40.242 -2.536  -27.411  1.00 45.99  ? 311  TRP   B CE2 1 
ATOM   3436  C  CE3 . TRP   B  1 10  ? -39.095 -4.091  -28.868  1.00 54.34  ? 311  TRP   B CE3 1 
ATOM   3437  C  CZ2 . TRP   B  1 10  ? -41.279 -2.365  -28.327  1.00 48.70  ? 311  TRP   B CZ2 1 
ATOM   3438  C  CZ3 . TRP   B  1 10  ? -40.126 -3.922  -29.778  1.00 55.32  ? 311  TRP   B CZ3 1 
ATOM   3439  C  CH2 . TRP   B  1 10  ? -41.202 -3.062  -29.504  1.00 55.99  ? 311  TRP   B CH2 1 
ATOM   3440  N  N   . GLU   B  1 11  ? -35.396 -6.605  -24.528  1.00 54.68  ? 312  GLU   B N   1 
ATOM   3441  C  CA  . GLU   B  1 11  ? -34.291 -7.549  -24.506  1.00 48.81  ? 312  GLU   B CA  1 
ATOM   3442  C  C   . GLU   B  1 11  ? -34.791 -8.978  -24.320  1.00 51.43  ? 312  GLU   B C   1 
ATOM   3443  O  O   . GLU   B  1 11  ? -34.253 -9.909  -24.924  1.00 55.25  ? 312  GLU   B O   1 
ATOM   3444  C  CB  . GLU   B  1 11  ? -33.319 -7.163  -23.386  1.00 57.56  ? 312  GLU   B CB  1 
ATOM   3445  C  CG  . GLU   B  1 11  ? -31.888 -7.595  -23.613  1.00 70.36  ? 312  GLU   B CG  1 
ATOM   3446  C  CD  . GLU   B  1 11  ? -30.909 -6.895  -22.675  1.00 76.17  ? 312  GLU   B CD  1 
ATOM   3447  O  OE1 . GLU   B  1 11  ? -31.192 -6.802  -21.456  1.00 66.10  ? 312  GLU   B OE1 1 
ATOM   3448  O  OE2 . GLU   B  1 11  ? -29.856 -6.426  -23.170  1.00 85.46  ? 312  GLU   B OE2 1 
ATOM   3449  N  N   . THR   B  1 12  ? -35.840 -9.169  -23.522  1.00 49.00  ? 313  THR   B N   1 
ATOM   3450  C  CA  . THR   B  1 12  ? -36.351 -10.493 -23.195  1.00 49.72  ? 313  THR   B CA  1 
ATOM   3451  C  C   . THR   B  1 12  ? -37.693 -10.784 -23.839  1.00 52.78  ? 313  THR   B C   1 
ATOM   3452  O  O   . THR   B  1 12  ? -38.135 -11.937 -23.815  1.00 54.84  ? 313  THR   B O   1 
ATOM   3453  C  CB  . THR   B  1 12  ? -36.519 -10.648 -21.673  1.00 48.73  ? 313  THR   B CB  1 
ATOM   3454  O  OG1 . THR   B  1 12  ? -37.585 -9.799  -21.232  1.00 46.15  ? 313  THR   B OG1 1 
ATOM   3455  C  CG2 . THR   B  1 12  ? -35.253 -10.254 -20.938  1.00 48.07  ? 313  THR   B CG2 1 
ATOM   3456  N  N   . GLU   B  1 13  ? -38.360 -9.764  -24.372  1.00 55.75  ? 314  GLU   B N   1 
ATOM   3457  C  CA  . GLU   B  1 13  ? -39.732 -9.824  -24.875  1.00 57.34  ? 314  GLU   B CA  1 
ATOM   3458  C  C   . GLU   B  1 13  ? -40.752 -10.189 -23.795  1.00 54.57  ? 314  GLU   B C   1 
ATOM   3459  O  O   . GLU   B  1 13  ? -41.891 -10.539 -24.112  1.00 56.48  ? 314  GLU   B O   1 
ATOM   3460  C  CB  . GLU   B  1 13  ? -39.847 -10.772 -26.072  1.00 56.78  ? 314  GLU   B CB  1 
ATOM   3461  C  CG  . GLU   B  1 13  ? -39.546 -10.078 -27.385  1.00 68.28  ? 314  GLU   B CG  1 
ATOM   3462  C  CD  . GLU   B  1 13  ? -39.433 -11.044 -28.546  1.00 72.71  ? 314  GLU   B CD  1 
ATOM   3463  O  OE1 . GLU   B  1 13  ? -40.424 -11.197 -29.292  1.00 82.15  ? 314  GLU   B OE1 1 
ATOM   3464  O  OE2 . GLU   B  1 13  ? -38.355 -11.659 -28.695  1.00 63.60  ? 314  GLU   B OE2 1 
ATOM   3465  N  N   . VAL   B  1 14  ? -40.389 -10.084 -22.515  1.00 48.99  ? 315  VAL   B N   1 
ATOM   3466  C  CA  . VAL   B  1 14  ? -41.374 -10.262 -21.457  1.00 50.44  ? 315  VAL   B CA  1 
ATOM   3467  C  C   . VAL   B  1 14  ? -42.356 -9.095  -21.483  1.00 48.34  ? 315  VAL   B C   1 
ATOM   3468  O  O   . VAL   B  1 14  ? -41.958 -7.927  -21.578  1.00 49.26  ? 315  VAL   B O   1 
ATOM   3469  C  CB  . VAL   B  1 14  ? -40.673 -10.390 -20.097  1.00 58.00  ? 315  VAL   B CB  1 
ATOM   3470  C  CG1 . VAL   B  1 14  ? -41.673 -10.261 -18.957  1.00 59.56  ? 315  VAL   B CG1 1 
ATOM   3471  C  CG2 . VAL   B  1 14  ? -39.916 -11.712 -20.030  1.00 57.52  ? 315  VAL   B CG2 1 
ATOM   3472  N  N   . VAL   B  1 15  ? -43.649 -9.409  -21.442  1.00 50.14  ? 316  VAL   B N   1 
ATOM   3473  C  CA  . VAL   B  1 15  ? -44.718 -8.416  -21.422  1.00 50.51  ? 316  VAL   B CA  1 
ATOM   3474  C  C   . VAL   B  1 15  ? -45.490 -8.551  -20.114  1.00 62.27  ? 316  VAL   B C   1 
ATOM   3475  O  O   . VAL   B  1 15  ? -45.994 -9.637  -19.797  1.00 66.68  ? 316  VAL   B O   1 
ATOM   3476  C  CB  . VAL   B  1 15  ? -45.672 -8.584  -22.615  1.00 51.30  ? 316  VAL   B CB  1 
ATOM   3477  C  CG1 . VAL   B  1 15  ? -46.890 -7.671  -22.449  1.00 44.61  ? 316  VAL   B CG1 1 
ATOM   3478  C  CG2 . VAL   B  1 15  ? -44.943 -8.310  -23.929  1.00 49.71  ? 316  VAL   B CG2 1 
ATOM   3479  N  N   . LEU   B  1 16  ? -45.603 -7.448  -19.373  1.00 60.27  ? 317  LEU   B N   1 
ATOM   3480  C  CA  . LEU   B  1 16  ? -46.374 -7.384  -18.138  1.00 55.00  ? 317  LEU   B CA  1 
ATOM   3481  C  C   . LEU   B  1 16  ? -47.624 -6.537  -18.354  1.00 53.61  ? 317  LEU   B C   1 
ATOM   3482  O  O   . LEU   B  1 16  ? -47.682 -5.708  -19.267  1.00 60.99  ? 317  LEU   B O   1 
ATOM   3483  C  CB  . LEU   B  1 16  ? -45.530 -6.812  -16.992  1.00 49.12  ? 317  LEU   B CB  1 
ATOM   3484  C  CG  . LEU   B  1 16  ? -44.154 -7.465  -16.801  1.00 44.10  ? 317  LEU   B CG  1 
ATOM   3485  C  CD1 . LEU   B  1 16  ? -43.263 -6.636  -15.884  1.00 38.70  ? 317  LEU   B CD1 1 
ATOM   3486  C  CD2 . LEU   B  1 16  ? -44.293 -8.901  -16.292  1.00 40.93  ? 317  LEU   B CD2 1 
ATOM   3487  N  N   . THR   B  1 17  ? -48.636 -6.768  -17.515  1.00 45.15  ? 318  THR   B N   1 
ATOM   3488  C  CA  . THR   B  1 17  ? -49.959 -6.173  -17.684  1.00 44.51  ? 318  THR   B CA  1 
ATOM   3489  C  C   . THR   B  1 17  ? -50.352 -5.432  -16.418  1.00 52.01  ? 318  THR   B C   1 
ATOM   3490  O  O   . THR   B  1 17  ? -50.509 -6.047  -15.359  1.00 53.48  ? 318  THR   B O   1 
ATOM   3491  C  CB  . THR   B  1 17  ? -51.007 -7.232  -18.003  1.00 51.80  ? 318  THR   B CB  1 
ATOM   3492  O  OG1 . THR   B  1 17  ? -50.573 -7.993  -19.129  1.00 50.34  ? 318  THR   B OG1 1 
ATOM   3493  C  CG2 . THR   B  1 17  ? -52.338 -6.567  -18.331  1.00 58.22  ? 318  THR   B CG2 1 
ATOM   3494  N  N   . ASP   B  1 18  ? -50.554 -4.128  -16.542  1.00 47.40  ? 319  ASP   B N   1 
ATOM   3495  C  CA  . ASP   B  1 18  ? -50.716 -3.236  -15.404  1.00 43.50  ? 319  ASP   B CA  1 
ATOM   3496  C  C   . ASP   B  1 18  ? -52.190 -2.902  -15.220  1.00 49.74  ? 319  ASP   B C   1 
ATOM   3497  O  O   . ASP   B  1 18  ? -52.801 -2.278  -16.093  1.00 47.79  ? 319  ASP   B O   1 
ATOM   3498  C  CB  . ASP   B  1 18  ? -49.890 -1.971  -15.613  1.00 41.97  ? 319  ASP   B CB  1 
ATOM   3499  C  CG  . ASP   B  1 18  ? -49.793 -1.120  -14.359  1.00 44.98  ? 319  ASP   B CG  1 
ATOM   3500  O  OD1 . ASP   B  1 18  ? -50.830 -0.596  -13.907  1.00 38.76  ? 319  ASP   B OD1 1 
ATOM   3501  O  OD2 . ASP   B  1 18  ? -48.670 -0.974  -13.837  1.00 47.81  ? 319  ASP   B OD2 1 
ATOM   3502  N  N   . THR   B  1 19  ? -52.759 -3.340  -14.087  1.00 43.51  ? 320  THR   B N   1 
ATOM   3503  C  CA  . THR   B  1 19  ? -54.042 -2.858  -13.588  1.00 43.37  ? 320  THR   B CA  1 
ATOM   3504  C  C   . THR   B  1 19  ? -53.911 -1.961  -12.366  1.00 45.07  ? 320  THR   B C   1 
ATOM   3505  O  O   . THR   B  1 19  ? -54.856 -1.224  -12.062  1.00 44.66  ? 320  THR   B O   1 
ATOM   3506  C  CB  . THR   B  1 19  ? -54.965 -4.025  -13.190  1.00 47.81  ? 320  THR   B CB  1 
ATOM   3507  O  OG1 . THR   B  1 19  ? -54.244 -4.946  -12.362  1.00 49.58  ? 320  THR   B OG1 1 
ATOM   3508  C  CG2 . THR   B  1 19  ? -55.519 -4.750  -14.390  1.00 46.37  ? 320  THR   B CG2 1 
ATOM   3509  N  N   . LEU   B  1 20  ? -52.780 -2.011  -11.654  1.00 44.28  ? 321  LEU   B N   1 
ATOM   3510  C  CA  . LEU   B  1 20  ? -52.635 -1.226  -10.425  1.00 51.36  ? 321  LEU   B CA  1 
ATOM   3511  C  C   . LEU   B  1 20  ? -52.784 0.272   -10.665  1.00 51.34  ? 321  LEU   B C   1 
ATOM   3512  O  O   . LEU   B  1 20  ? -53.184 0.990   -9.745   1.00 43.45  ? 321  LEU   B O   1 
ATOM   3513  C  CB  . LEU   B  1 20  ? -51.281 -1.513  -9.758   1.00 46.24  ? 321  LEU   B CB  1 
ATOM   3514  C  CG  . LEU   B  1 20  ? -50.922 -0.813  -8.441   1.00 45.63  ? 321  LEU   B CG  1 
ATOM   3515  C  CD1 . LEU   B  1 20  ? -51.818 -1.261  -7.238   1.00 33.38  ? 321  LEU   B CD1 1 
ATOM   3516  C  CD2 . LEU   B  1 20  ? -49.443 -0.989  -8.121   1.00 35.78  ? 321  LEU   B CD2 1 
ATOM   3517  N  N   . HIS   B  1 21  ? -52.496 0.755   -11.880  1.00 44.55  ? 322  HIS   B N   1 
ATOM   3518  C  CA  . HIS   B  1 21  ? -52.592 2.184   -12.166  1.00 48.84  ? 322  HIS   B CA  1 
ATOM   3519  C  C   . HIS   B  1 21  ? -54.016 2.709   -12.058  1.00 47.88  ? 322  HIS   B C   1 
ATOM   3520  O  O   . HIS   B  1 21  ? -54.204 3.928   -12.056  1.00 44.78  ? 322  HIS   B O   1 
ATOM   3521  C  CB  . HIS   B  1 21  ? -52.100 2.491   -13.578  1.00 43.29  ? 322  HIS   B CB  1 
ATOM   3522  C  CG  . HIS   B  1 21  ? -53.087 2.100   -14.624  1.00 41.68  ? 322  HIS   B CG  1 
ATOM   3523  N  ND1 . HIS   B  1 21  ? -53.099 0.847   -15.199  1.00 42.70  ? 322  HIS   B ND1 1 
ATOM   3524  C  CD2 . HIS   B  1 21  ? -54.136 2.770   -15.152  1.00 42.70  ? 322  HIS   B CD2 1 
ATOM   3525  C  CE1 . HIS   B  1 21  ? -54.102 0.771   -16.052  1.00 46.32  ? 322  HIS   B CE1 1 
ATOM   3526  N  NE2 . HIS   B  1 21  ? -54.750 1.923   -16.038  1.00 47.74  ? 322  HIS   B NE2 1 
ATOM   3527  N  N   . LEU   B  1 22  ? -55.025 1.832   -12.039  1.00 43.68  ? 323  LEU   B N   1 
ATOM   3528  C  CA  . LEU   B  1 22  ? -56.391 2.296   -11.819  1.00 45.27  ? 323  LEU   B CA  1 
ATOM   3529  C  C   . LEU   B  1 22  ? -56.580 2.854   -10.416  1.00 54.11  ? 323  LEU   B C   1 
ATOM   3530  O  O   . LEU   B  1 22  ? -57.566 3.549   -10.160  1.00 62.09  ? 323  LEU   B O   1 
ATOM   3531  C  CB  . LEU   B  1 22  ? -57.394 1.168   -12.049  1.00 49.85  ? 323  LEU   B CB  1 
ATOM   3532  C  CG  . LEU   B  1 22  ? -57.318 0.373   -13.354  1.00 54.11  ? 323  LEU   B CG  1 
ATOM   3533  C  CD1 . LEU   B  1 22  ? -58.305 -0.779  -13.306  1.00 53.61  ? 323  LEU   B CD1 1 
ATOM   3534  C  CD2 . LEU   B  1 22  ? -57.597 1.267   -14.540  1.00 55.58  ? 323  LEU   B CD2 1 
ATOM   3535  N  N   . LYS   B  1 23  ? -55.663 2.562   -9.508   1.00 53.30  ? 324  LYS   B N   1 
ATOM   3536  C  CA  . LYS   B  1 23  ? -55.692 3.092   -8.157   1.00 47.09  ? 324  LYS   B CA  1 
ATOM   3537  C  C   . LYS   B  1 23  ? -54.931 4.406   -8.034   1.00 55.97  ? 324  LYS   B C   1 
ATOM   3538  O  O   . LYS   B  1 23  ? -54.756 4.909   -6.921   1.00 60.37  ? 324  LYS   B O   1 
ATOM   3539  C  CB  . LYS   B  1 23  ? -55.128 2.047   -7.188   1.00 44.28  ? 324  LYS   B CB  1 
ATOM   3540  C  CG  . LYS   B  1 23  ? -56.192 1.424   -6.277   1.00 50.17  ? 324  LYS   B CG  1 
ATOM   3541  C  CD  . LYS   B  1 23  ? -57.371 0.874   -7.073   1.00 55.78  ? 324  LYS   B CD  1 
ATOM   3542  C  CE  . LYS   B  1 23  ? -58.607 0.684   -6.192   1.00 69.76  ? 324  LYS   B CE  1 
ATOM   3543  N  NZ  . LYS   B  1 23  ? -58.260 0.454   -4.751   1.00 65.37  ? 324  LYS   B NZ  1 
ATOM   3544  N  N   . SER   B  1 24  ? -54.473 4.964   -9.150   1.00 55.20  ? 325  SER   B N   1 
ATOM   3545  C  CA  . SER   B  1 24  ? -53.709 6.203   -9.124   1.00 60.73  ? 325  SER   B CA  1 
ATOM   3546  C  C   . SER   B  1 24  ? -54.589 7.372   -8.686   1.00 64.67  ? 325  SER   B C   1 
ATOM   3547  O  O   . SER   B  1 24  ? -55.757 7.475   -9.074   1.00 67.70  ? 325  SER   B O   1 
ATOM   3548  C  CB  . SER   B  1 24  ? -53.111 6.468   -10.506  1.00 63.50  ? 325  SER   B CB  1 
ATOM   3549  O  OG  . SER   B  1 24  ? -52.482 7.732   -10.577  1.00 71.94  ? 325  SER   B OG  1 
ATOM   3550  N  N   . THR   B  1 25  ? -54.023 8.265   -7.880   1.00 64.52  ? 326  THR   B N   1 
ATOM   3551  C  CA  . THR   B  1 25  ? -54.809 9.349   -7.304   1.00 72.04  ? 326  THR   B CA  1 
ATOM   3552  C  C   . THR   B  1 25  ? -54.472 10.726  -7.852   1.00 70.58  ? 326  THR   B C   1 
ATOM   3553  O  O   . THR   B  1 25  ? -55.383 11.500  -8.154   1.00 78.22  ? 326  THR   B O   1 
ATOM   3554  C  CB  . THR   B  1 25  ? -54.655 9.365   -5.779   1.00 73.53  ? 326  THR   B CB  1 
ATOM   3555  O  OG1 . THR   B  1 25  ? -53.744 8.335   -5.367   1.00 69.09  ? 326  THR   B OG1 1 
ATOM   3556  C  CG2 . THR   B  1 25  ? -56.012 9.136   -5.131   1.00 79.56  ? 326  THR   B CG2 1 
ATOM   3557  N  N   . LEU   B  1 26  ? -53.198 11.058  -8.006   1.00 60.94  ? 327  LEU   B N   1 
ATOM   3558  C  CA  . LEU   B  1 26  ? -52.798 12.416  -8.340   1.00 58.70  ? 327  LEU   B CA  1 
ATOM   3559  C  C   . LEU   B  1 26  ? -52.304 12.520  -9.783   1.00 60.34  ? 327  LEU   B C   1 
ATOM   3560  O  O   . LEU   B  1 26  ? -51.912 11.530  -10.411  1.00 56.15  ? 327  LEU   B O   1 
ATOM   3561  C  CB  . LEU   B  1 26  ? -51.723 12.898  -7.365   1.00 56.56  ? 327  LEU   B CB  1 
ATOM   3562  C  CG  . LEU   B  1 26  ? -52.198 12.809  -5.906   1.00 67.95  ? 327  LEU   B CG  1 
ATOM   3563  C  CD1 . LEU   B  1 26  ? -51.751 11.513  -5.197   1.00 70.49  ? 327  LEU   B CD1 1 
ATOM   3564  C  CD2 . LEU   B  1 26  ? -51.743 14.031  -5.149   1.00 63.84  ? 327  LEU   B CD2 1 
ATOM   3565  N  N   . GLU   B  1 27  ? -52.341 13.748  -10.303  1.00 57.28  ? 328  GLU   B N   1 
ATOM   3566  C  CA  . GLU   B  1 27  ? -51.904 14.016  -11.668  1.00 57.73  ? 328  GLU   B CA  1 
ATOM   3567  C  C   . GLU   B  1 27  ? -50.398 13.827  -11.801  1.00 56.68  ? 328  GLU   B C   1 
ATOM   3568  O  O   . GLU   B  1 27  ? -49.629 14.159  -10.892  1.00 54.94  ? 328  GLU   B O   1 
ATOM   3569  C  CB  . GLU   B  1 27  ? -52.310 15.431  -12.085  1.00 45.08  ? 328  GLU   B CB  1 
ATOM   3570  C  CG  . GLU   B  1 27  ? -53.777 15.533  -12.499  1.00 50.30  ? 328  GLU   B CG  1 
ATOM   3571  C  CD  . GLU   B  1 27  ? -54.259 16.956  -12.739  1.00 56.32  ? 328  GLU   B CD  1 
ATOM   3572  O  OE1 . GLU   B  1 27  ? -55.475 17.128  -12.982  1.00 60.55  ? 328  GLU   B OE1 1 
ATOM   3573  O  OE2 . GLU   B  1 27  ? -53.437 17.898  -12.679  1.00 60.28  ? 328  GLU   B OE2 1 
ATOM   3574  N  N   . THR   B  1 28  ? -49.983 13.252  -12.936  1.00 49.84  ? 329  THR   B N   1 
ATOM   3575  C  CA  . THR   B  1 28  ? -48.564 13.105  -13.233  1.00 39.57  ? 329  THR   B CA  1 
ATOM   3576  C  C   . THR   B  1 28  ? -47.967 14.382  -13.788  1.00 33.36  ? 329  THR   B C   1 
ATOM   3577  O  O   . THR   B  1 28  ? -46.756 14.577  -13.680  1.00 42.76  ? 329  THR   B O   1 
ATOM   3578  C  CB  . THR   B  1 28  ? -48.309 11.982  -14.249  1.00 46.39  ? 329  THR   B CB  1 
ATOM   3579  O  OG1 . THR   B  1 28  ? -48.969 12.271  -15.501  1.00 41.23  ? 329  THR   B OG1 1 
ATOM   3580  C  CG2 . THR   B  1 28  ? -48.758 10.626  -13.703  1.00 44.35  ? 329  THR   B CG2 1 
ATOM   3581  N  N   . GLY   B  1 29  ? -48.792 15.250  -14.367  1.00 35.52  ? 330  GLY   B N   1 
ATOM   3582  C  CA  . GLY   B  1 29  ? -48.340 16.372  -15.153  1.00 38.86  ? 330  GLY   B CA  1 
ATOM   3583  C  C   . GLY   B  1 29  ? -48.580 16.207  -16.642  1.00 48.69  ? 330  GLY   B C   1 
ATOM   3584  O  O   . GLY   B  1 29  ? -48.675 17.212  -17.356  1.00 55.35  ? 330  GLY   B O   1 
ATOM   3585  N  N   . CYS   B  1 30  ? -48.711 14.977  -17.127  1.00 41.35  ? 331  CYS   B N   1 
ATOM   3586  C  CA  . CYS   B  1 30  ? -48.886 14.757  -18.552  1.00 45.04  ? 331  CYS   B CA  1 
ATOM   3587  C  C   . CYS   B  1 30  ? -50.345 14.944  -18.969  1.00 45.08  ? 331  CYS   B C   1 
ATOM   3588  O  O   . CYS   B  1 30  ? -51.262 14.993  -18.149  1.00 51.47  ? 331  CYS   B O   1 
ATOM   3589  C  CB  . CYS   B  1 30  ? -48.422 13.356  -18.944  1.00 32.58  ? 331  CYS   B CB  1 
ATOM   3590  S  SG  . CYS   B  1 30  ? -46.715 12.994  -18.544  1.00 36.67  ? 331  CYS   B SG  1 
ATOM   3591  N  N   . THR   B  1 31  ? -50.547 15.074  -20.276  1.00 48.70  ? 332  THR   B N   1 
ATOM   3592  C  CA  . THR   B  1 31  ? -51.865 14.990  -20.877  1.00 50.36  ? 332  THR   B CA  1 
ATOM   3593  C  C   . THR   B  1 31  ? -51.756 14.132  -22.130  1.00 54.75  ? 332  THR   B C   1 
ATOM   3594  O  O   . THR   B  1 31  ? -50.676 13.658  -22.501  1.00 54.37  ? 332  THR   B O   1 
ATOM   3595  C  CB  . THR   B  1 31  ? -52.432 16.379  -21.211  1.00 54.13  ? 332  THR   B CB  1 
ATOM   3596  O  OG1 . THR   B  1 31  ? -51.740 16.930  -22.346  1.00 47.57  ? 332  THR   B OG1 1 
ATOM   3597  C  CG2 . THR   B  1 31  ? -52.305 17.340  -19.993  1.00 49.35  ? 332  THR   B CG2 1 
ATOM   3598  N  N   . GLU   B  1 32  ? -52.890 13.944  -22.799  1.00 60.84  ? 333  GLU   B N   1 
ATOM   3599  C  CA  . GLU   B  1 32  ? -52.872 13.276  -24.089  1.00 63.43  ? 333  GLU   B CA  1 
ATOM   3600  C  C   . GLU   B  1 32  ? -52.004 14.013  -25.106  1.00 60.46  ? 333  GLU   B C   1 
ATOM   3601  O  O   . GLU   B  1 32  ? -51.566 13.395  -26.079  1.00 59.81  ? 333  GLU   B O   1 
ATOM   3602  C  CB  . GLU   B  1 32  ? -54.303 13.120  -24.615  1.00 71.02  ? 333  GLU   B CB  1 
ATOM   3603  C  CG  . GLU   B  1 32  ? -55.128 12.033  -23.923  1.00 77.52  ? 333  GLU   B CG  1 
ATOM   3604  C  CD  . GLU   B  1 32  ? -55.795 12.500  -22.633  1.00 88.17  ? 333  GLU   B CD  1 
ATOM   3605  O  OE1 . GLU   B  1 32  ? -55.429 13.576  -22.112  1.00 90.53  ? 333  GLU   B OE1 1 
ATOM   3606  O  OE2 . GLU   B  1 32  ? -56.696 11.786  -22.139  1.00 91.96  ? 333  GLU   B OE2 1 
ATOM   3607  N  N   . TYR   B  1 33  ? -51.704 15.302  -24.887  1.00 57.09  ? 334  TYR   B N   1 
ATOM   3608  C  CA  . TYR   B  1 33  ? -50.971 16.095  -25.868  1.00 56.44  ? 334  TYR   B CA  1 
ATOM   3609  C  C   . TYR   B  1 33  ? -49.581 16.551  -25.433  1.00 54.40  ? 334  TYR   B C   1 
ATOM   3610  O  O   . TYR   B  1 33  ? -48.833 17.062  -26.275  1.00 57.49  ? 334  TYR   B O   1 
ATOM   3611  C  CB  . TYR   B  1 33  ? -51.777 17.338  -26.264  1.00 59.33  ? 334  TYR   B CB  1 
ATOM   3612  C  CG  . TYR   B  1 33  ? -53.089 17.025  -26.911  1.00 61.52  ? 334  TYR   B CG  1 
ATOM   3613  C  CD1 . TYR   B  1 33  ? -53.163 16.696  -28.257  1.00 72.18  ? 334  TYR   B CD1 1 
ATOM   3614  C  CD2 . TYR   B  1 33  ? -54.259 17.055  -26.179  1.00 59.88  ? 334  TYR   B CD2 1 
ATOM   3615  C  CE1 . TYR   B  1 33  ? -54.373 16.408  -28.854  1.00 76.47  ? 334  TYR   B CE1 1 
ATOM   3616  C  CE2 . TYR   B  1 33  ? -55.466 16.768  -26.761  1.00 64.54  ? 334  TYR   B CE2 1 
ATOM   3617  C  CZ  . TYR   B  1 33  ? -55.520 16.449  -28.094  1.00 74.98  ? 334  TYR   B CZ  1 
ATOM   3618  O  OH  . TYR   B  1 33  ? -56.732 16.166  -28.665  1.00 85.40  ? 334  TYR   B OH  1 
ATOM   3619  N  N   . ILE   B  1 34  ? -49.215 16.427  -24.159  1.00 41.86  ? 335  ILE   B N   1 
ATOM   3620  C  CA  . ILE   B  1 34  ? -47.886 16.826  -23.710  1.00 42.76  ? 335  ILE   B CA  1 
ATOM   3621  C  C   . ILE   B  1 34  ? -47.424 15.828  -22.659  1.00 46.15  ? 335  ILE   B C   1 
ATOM   3622  O  O   . ILE   B  1 34  ? -48.155 15.543  -21.706  1.00 50.61  ? 335  ILE   B O   1 
ATOM   3623  C  CB  . ILE   B  1 34  ? -47.858 18.266  -23.149  1.00 49.26  ? 335  ILE   B CB  1 
ATOM   3624  C  CG1 . ILE   B  1 34  ? -48.524 19.250  -24.112  1.00 69.98  ? 335  ILE   B CG1 1 
ATOM   3625  C  CG2 . ILE   B  1 34  ? -46.444 18.749  -22.983  1.00 44.84  ? 335  ILE   B CG2 1 
ATOM   3626  C  CD1 . ILE   B  1 34  ? -49.462 20.247  -23.451  1.00 81.94  ? 335  ILE   B CD1 1 
ATOM   3627  N  N   . CYS   B  1 35  ? -46.229 15.274  -22.845  1.00 40.61  ? 336  CYS   B N   1 
ATOM   3628  C  CA  . CYS   B  1 35  ? -45.601 14.429  -21.840  1.00 38.90  ? 336  CYS   B CA  1 
ATOM   3629  C  C   . CYS   B  1 35  ? -44.581 15.255  -21.071  1.00 41.58  ? 336  CYS   B C   1 
ATOM   3630  O  O   . CYS   B  1 35  ? -43.786 15.987  -21.676  1.00 42.36  ? 336  CYS   B O   1 
ATOM   3631  C  CB  . CYS   B  1 35  ? -44.926 13.214  -22.466  1.00 34.64  ? 336  CYS   B CB  1 
ATOM   3632  S  SG  . CYS   B  1 35  ? -43.934 12.289  -21.277  1.00 38.15  ? 336  CYS   B SG  1 
ATOM   3633  N  N   . MET   B  1 36  ? -44.613 15.140  -19.740  1.00 37.00  ? 337  MET   B N   1 
ATOM   3634  C  CA  . MET   B  1 36  ? -43.720 15.893  -18.874  1.00 39.84  ? 337  MET   B CA  1 
ATOM   3635  C  C   . MET   B  1 36  ? -42.771 14.984  -18.103  1.00 35.97  ? 337  MET   B C   1 
ATOM   3636  O  O   . MET   B  1 36  ? -42.147 15.433  -17.141  1.00 40.93  ? 337  MET   B O   1 
ATOM   3637  C  CB  . MET   B  1 36  ? -44.519 16.758  -17.912  1.00 40.20  ? 337  MET   B CB  1 
ATOM   3638  C  CG  . MET   B  1 36  ? -45.159 17.948  -18.585  1.00 47.60  ? 337  MET   B CG  1 
ATOM   3639  S  SD  . MET   B  1 36  ? -45.751 19.088  -17.338  1.00 70.56  ? 337  MET   B SD  1 
ATOM   3640  C  CE  . MET   B  1 36  ? -46.638 20.222  -18.385  1.00 68.22  ? 337  MET   B CE  1 
ATOM   3641  N  N   . GLY   B  1 37  ? -42.588 13.740  -18.555  1.00 37.13  ? 338  GLY   B N   1 
ATOM   3642  C  CA  . GLY   B  1 37  ? -41.853 12.709  -17.831  1.00 40.52  ? 338  GLY   B CA  1 
ATOM   3643  C  C   . GLY   B  1 37  ? -40.394 13.014  -17.529  1.00 36.31  ? 338  GLY   B C   1 
ATOM   3644  O  O   . GLY   B  1 37  ? -39.765 12.227  -16.816  1.00 32.31  ? 338  GLY   B O   1 
ATOM   3645  N  N   . SER   B  1 38  ? -39.831 14.104  -18.059  1.00 37.61  ? 339  SER   B N   1 
ATOM   3646  C  CA  . SER   B  1 38  ? -38.461 14.508  -17.737  1.00 34.44  ? 339  SER   B CA  1 
ATOM   3647  C  C   . SER   B  1 38  ? -38.416 15.840  -16.995  1.00 38.94  ? 339  SER   B C   1 
ATOM   3648  O  O   . SER   B  1 38  ? -37.341 16.442  -16.859  1.00 39.46  ? 339  SER   B O   1 
ATOM   3649  C  CB  . SER   B  1 38  ? -37.609 14.584  -19.007  1.00 41.21  ? 339  SER   B CB  1 
ATOM   3650  O  OG  . SER   B  1 38  ? -37.887 15.755  -19.769  1.00 42.14  ? 339  SER   B OG  1 
ATOM   3651  N  N   . ILE   B  1 39  ? -39.576 16.341  -16.573  1.00 33.22  ? 340  ILE   B N   1 
ATOM   3652  C  CA  . ILE   B  1 39  ? -39.652 17.492  -15.679  1.00 42.79  ? 340  ILE   B CA  1 
ATOM   3653  C  C   . ILE   B  1 39  ? -39.399 17.031  -14.248  1.00 40.28  ? 340  ILE   B C   1 
ATOM   3654  O  O   . ILE   B  1 39  ? -39.906 15.986  -13.811  1.00 46.40  ? 340  ILE   B O   1 
ATOM   3655  C  CB  . ILE   B  1 39  ? -41.019 18.183  -15.813  1.00 43.53  ? 340  ILE   B CB  1 
ATOM   3656  C  CG1 . ILE   B  1 39  ? -41.246 18.627  -17.258  1.00 39.63  ? 340  ILE   B CG1 1 
ATOM   3657  C  CG2 . ILE   B  1 39  ? -41.121 19.369  -14.859  1.00 36.93  ? 340  ILE   B CG2 1 
ATOM   3658  C  CD1 . ILE   B  1 39  ? -40.362 19.785  -17.685  1.00 42.65  ? 340  ILE   B CD1 1 
ATOM   3659  N  N   . MET   B  1 40  ? -38.607 17.809  -13.509  1.00 40.85  ? 341  MET   B N   1 
ATOM   3660  C  CA  . MET   B  1 40  ? -38.240 17.420  -12.150  1.00 45.53  ? 341  MET   B CA  1 
ATOM   3661  C  C   . MET   B  1 40  ? -39.449 17.444  -11.205  1.00 45.95  ? 341  MET   B C   1 
ATOM   3662  O  O   . MET   B  1 40  ? -39.663 16.500  -10.438  1.00 39.04  ? 341  MET   B O   1 
ATOM   3663  C  CB  . MET   B  1 40  ? -37.133 18.337  -11.640  1.00 56.18  ? 341  MET   B CB  1 
ATOM   3664  C  CG  . MET   B  1 40  ? -36.680 18.016  -10.228  1.00 67.96  ? 341  MET   B CG  1 
ATOM   3665  S  SD  . MET   B  1 40  ? -35.498 16.668  -10.176  1.00 71.60  ? 341  MET   B SD  1 
ATOM   3666  C  CE  . MET   B  1 40  ? -34.172 17.304  -11.219  1.00 61.00  ? 341  MET   B CE  1 
ATOM   3667  N  N   . HIS   B  1 41  ? -40.253 18.516  -11.245  1.00 54.42  ? 342  HIS   B N   1 
ATOM   3668  C  CA  . HIS   B  1 41  ? -41.469 18.641  -10.430  1.00 54.48  ? 342  HIS   B CA  1 
ATOM   3669  C  C   . HIS   B  1 41  ? -42.639 18.993  -11.338  1.00 44.87  ? 342  HIS   B C   1 
ATOM   3670  O  O   . HIS   B  1 41  ? -43.064 20.152  -11.405  1.00 43.80  ? 342  HIS   B O   1 
ATOM   3671  C  CB  . HIS   B  1 41  ? -41.304 19.692  -9.329   1.00 51.47  ? 342  HIS   B CB  1 
ATOM   3672  C  CG  . HIS   B  1 41  ? -39.953 19.684  -8.689   1.00 58.11  ? 342  HIS   B CG  1 
ATOM   3673  N  ND1 . HIS   B  1 41  ? -39.531 18.673  -7.853   1.00 60.92  ? 342  HIS   B ND1 1 
ATOM   3674  C  CD2 . HIS   B  1 41  ? -38.924 20.562  -8.770   1.00 63.37  ? 342  HIS   B CD2 1 
ATOM   3675  C  CE1 . HIS   B  1 41  ? -38.298 18.927  -7.448   1.00 63.71  ? 342  HIS   B CE1 1 
ATOM   3676  N  NE2 . HIS   B  1 41  ? -37.908 20.069  -7.989   1.00 63.03  ? 342  HIS   B NE2 1 
ATOM   3677  N  N   . PRO   B  1 42  ? -43.193 18.017  -12.055  1.00 56.33  ? 343  PRO   B N   1 
ATOM   3678  C  CA  . PRO   B  1 42  ? -44.192 18.369  -13.080  1.00 57.20  ? 343  PRO   B CA  1 
ATOM   3679  C  C   . PRO   B  1 42  ? -45.513 18.859  -12.501  1.00 59.17  ? 343  PRO   B C   1 
ATOM   3680  O  O   . PRO   B  1 42  ? -46.131 19.754  -13.088  1.00 58.50  ? 343  PRO   B O   1 
ATOM   3681  C  CB  . PRO   B  1 42  ? -44.354 17.070  -13.882  1.00 50.10  ? 343  PRO   B CB  1 
ATOM   3682  C  CG  . PRO   B  1 42  ? -43.945 15.981  -12.953  1.00 53.98  ? 343  PRO   B CG  1 
ATOM   3683  C  CD  . PRO   B  1 42  ? -42.930 16.567  -11.992  1.00 59.30  ? 343  PRO   B CD  1 
ATOM   3684  N  N   . SER   B  1 43  ? -45.948 18.341  -11.352  1.00 60.76  ? 344  SER   B N   1 
ATOM   3685  C  CA  . SER   B  1 43  ? -47.276 18.614  -10.820  1.00 58.26  ? 344  SER   B CA  1 
ATOM   3686  C  C   . SER   B  1 43  ? -47.188 19.316  -9.469   1.00 58.06  ? 344  SER   B C   1 
ATOM   3687  O  O   . SER   B  1 43  ? -46.230 19.132  -8.712   1.00 53.45  ? 344  SER   B O   1 
ATOM   3688  C  CB  . SER   B  1 43  ? -48.083 17.308  -10.675  1.00 54.10  ? 344  SER   B CB  1 
ATOM   3689  O  OG  . SER   B  1 43  ? -49.481 17.547  -10.647  1.00 53.17  ? 344  SER   B OG  1 
ATOM   3690  N  N   . GLN   B  1 44  ? -48.195 20.140  -9.184   1.00 66.00  ? 345  GLN   B N   1 
ATOM   3691  C  CA  . GLN   B  1 44  ? -48.427 20.665  -7.842   1.00 70.50  ? 345  GLN   B CA  1 
ATOM   3692  C  C   . GLN   B  1 44  ? -49.736 20.157  -7.250   1.00 74.34  ? 345  GLN   B C   1 
ATOM   3693  O  O   . GLN   B  1 44  ? -50.192 20.690  -6.229   1.00 71.37  ? 345  GLN   B O   1 
ATOM   3694  C  CB  . GLN   B  1 44  ? -48.424 22.192  -7.849   1.00 68.40  ? 345  GLN   B CB  1 
ATOM   3695  C  CG  . GLN   B  1 44  ? -47.178 22.789  -8.442   1.00 71.01  ? 345  GLN   B CG  1 
ATOM   3696  C  CD  . GLN   B  1 44  ? -47.388 24.231  -8.836   1.00 77.03  ? 345  GLN   B CD  1 
ATOM   3697  O  OE1 . GLN   B  1 44  ? -47.549 24.545  -10.016  1.00 83.40  ? 345  GLN   B OE1 1 
ATOM   3698  N  NE2 . GLN   B  1 44  ? -47.402 25.119  -7.848   1.00 73.80  ? 345  GLN   B NE2 1 
ATOM   3699  N  N   . HIS   B  1 45  ? -50.352 19.147  -7.873   1.00 79.18  ? 346  HIS   B N   1 
ATOM   3700  C  CA  . HIS   B  1 45  ? -51.573 18.513  -7.384   1.00 80.54  ? 346  HIS   B CA  1 
ATOM   3701  C  C   . HIS   B  1 45  ? -51.324 17.843  -6.040   1.00 80.08  ? 346  HIS   B C   1 
ATOM   3702  O  O   . HIS   B  1 45  ? -50.654 16.808  -5.980   1.00 79.72  ? 346  HIS   B O   1 
ATOM   3703  C  CB  . HIS   B  1 45  ? -52.078 17.483  -8.402   1.00 77.11  ? 346  HIS   B CB  1 
ATOM   3704  C  CG  . HIS   B  1 45  ? -53.495 17.045  -8.181   1.00 78.85  ? 346  HIS   B CG  1 
ATOM   3705  N  ND1 . HIS   B  1 45  ? -53.963 15.813  -8.587   1.00 78.70  ? 346  HIS   B ND1 1 
ATOM   3706  C  CD2 . HIS   B  1 45  ? -54.549 17.679  -7.615   1.00 79.21  ? 346  HIS   B CD2 1 
ATOM   3707  C  CE1 . HIS   B  1 45  ? -55.242 15.705  -8.273   1.00 78.22  ? 346  HIS   B CE1 1 
ATOM   3708  N  NE2 . HIS   B  1 45  ? -55.622 16.823  -7.683   1.00 77.77  ? 346  HIS   B NE2 1 
ATOM   3709  N  N   . ALA   B  1 46  ? -51.841 18.429  -4.963   1.00 82.97  ? 347  ALA   B N   1 
ATOM   3710  C  CA  . ALA   B  1 46  ? -51.739 17.871  -3.621   1.00 78.04  ? 347  ALA   B CA  1 
ATOM   3711  C  C   . ALA   B  1 46  ? -53.064 17.236  -3.217   1.00 77.03  ? 347  ALA   B C   1 
ATOM   3712  O  O   . ALA   B  1 46  ? -54.119 17.526  -3.784   1.00 74.21  ? 347  ALA   B O   1 
ATOM   3713  C  CB  . ALA   B  1 46  ? -51.338 18.946  -2.607   1.00 74.44  ? 347  ALA   B CB  1 
ATOM   3714  N  N   . ARG   B  1 47  ? -52.999 16.347  -2.231   1.00 85.16  ? 348  ARG   B N   1 
ATOM   3715  C  CA  . ARG   B  1 47  ? -54.212 15.688  -1.766   1.00 92.80  ? 348  ARG   B CA  1 
ATOM   3716  C  C   . ARG   B  1 47  ? -55.007 16.538  -0.776   1.00 94.70  ? 348  ARG   B C   1 
ATOM   3717  O  O   . ARG   B  1 47  ? -56.183 16.243  -0.534   1.00 94.58  ? 348  ARG   B O   1 
ATOM   3718  C  CB  . ARG   B  1 47  ? -53.867 14.330  -1.141   1.00 92.79  ? 348  ARG   B CB  1 
ATOM   3719  C  CG  . ARG   B  1 47  ? -53.229 13.346  -2.107   1.00 89.46  ? 348  ARG   B CG  1 
ATOM   3720  C  CD  . ARG   B  1 47  ? -53.511 11.901  -1.729   1.00 96.74  ? 348  ARG   B CD  1 
ATOM   3721  N  NE  . ARG   B  1 47  ? -54.941 11.664  -1.539   1.00 108.70 ? 348  ARG   B NE  1 
ATOM   3722  C  CZ  . ARG   B  1 47  ? -55.540 10.492  -1.718   1.00 114.16 ? 348  ARG   B CZ  1 
ATOM   3723  N  NH1 . ARG   B  1 47  ? -54.841 9.451   -2.115   1.00 114.60 ? 348  ARG   B NH1 1 
ATOM   3724  N  NH2 . ARG   B  1 47  ? -56.844 10.360  -1.521   1.00 118.96 ? 348  ARG   B NH2 1 
ATOM   3725  N  N   . ARG   B  1 48  ? -54.412 17.601  -0.226   1.00 91.46  ? 349  ARG   B N   1 
ATOM   3726  C  CA  . ARG   B  1 48  ? -55.070 18.458  0.748    1.00 88.16  ? 349  ARG   B CA  1 
ATOM   3727  C  C   . ARG   B  1 48  ? -54.659 19.908  0.532    1.00 87.06  ? 349  ARG   B C   1 
ATOM   3728  O  O   . ARG   B  1 48  ? -53.499 20.168  0.187    1.00 86.99  ? 349  ARG   B O   1 
ATOM   3729  C  CB  . ARG   B  1 48  ? -54.717 18.015  2.169    1.00 85.38  ? 349  ARG   B CB  1 
ATOM   3730  C  CG  . ARG   B  1 48  ? -53.286 17.501  2.299    1.00 80.31  ? 349  ARG   B CG  1 
ATOM   3731  C  CD  . ARG   B  1 48  ? -52.775 17.652  3.709    1.00 79.64  ? 349  ARG   B CD  1 
ATOM   3732  N  NE  . ARG   B  1 48  ? -53.197 18.928  4.273    1.00 79.26  ? 349  ARG   B NE  1 
ATOM   3733  C  CZ  . ARG   B  1 48  ? -54.123 19.049  5.211    1.00 87.06  ? 349  ARG   B CZ  1 
ATOM   3734  N  NH1 . ARG   B  1 48  ? -54.705 17.964  5.700    1.00 89.00  ? 349  ARG   B NH1 1 
ATOM   3735  N  NH2 . ARG   B  1 48  ? -54.464 20.250  5.661    1.00 93.40  ? 349  ARG   B NH2 1 
ATOM   3736  N  N   . PRO   B  1 49  ? -55.571 20.862  0.718    1.00 93.23  ? 350  PRO   B N   1 
ATOM   3737  C  CA  . PRO   B  1 49  ? -55.221 22.280  0.531    1.00 103.04 ? 350  PRO   B CA  1 
ATOM   3738  C  C   . PRO   B  1 49  ? -54.133 22.799  1.466    1.00 115.92 ? 350  PRO   B C   1 
ATOM   3739  O  O   . PRO   B  1 49  ? -53.497 22.030  2.195    1.00 112.08 ? 350  PRO   B O   1 
ATOM   3740  C  CB  . PRO   B  1 49  ? -56.553 23.006  0.772    1.00 102.58 ? 350  PRO   B CB  1 
ATOM   3741  C  CG  . PRO   B  1 49  ? -57.444 22.001  1.437    1.00 102.17 ? 350  PRO   B CG  1 
ATOM   3742  C  CD  . PRO   B  1 49  ? -57.013 20.670  0.927    1.00 98.05  ? 350  PRO   B CD  1 
ATOM   3743  N  N   . GLU   B  1 50  ? -53.932 24.121  1.456    1.00 138.60 ? 351  GLU   B N   1 
ATOM   3744  C  CA  . GLU   B  1 50  ? -52.764 24.764  2.056    1.00 139.32 ? 351  GLU   B CA  1 
ATOM   3745  C  C   . GLU   B  1 50  ? -52.605 24.471  3.543    1.00 130.06 ? 351  GLU   B C   1 
ATOM   3746  O  O   . GLU   B  1 50  ? -51.753 23.665  3.932    1.00 129.41 ? 351  GLU   B O   1 
ATOM   3747  C  CB  . GLU   B  1 50  ? -52.825 26.281  1.840    1.00 147.70 ? 351  GLU   B CB  1 
ATOM   3748  C  CG  . GLU   B  1 50  ? -52.834 26.702  0.376    1.00 150.82 ? 351  GLU   B CG  1 
ATOM   3749  C  CD  . GLU   B  1 50  ? -51.939 27.894  0.103    1.00 151.73 ? 351  GLU   B CD  1 
ATOM   3750  O  OE1 . GLU   B  1 50  ? -51.411 28.472  1.077    1.00 151.08 ? 351  GLU   B OE1 1 
ATOM   3751  O  OE2 . GLU   B  1 50  ? -51.760 28.246  -1.084   1.00 151.73 ? 351  GLU   B OE2 1 
ATOM   3752  N  N   . ASP   B  1 51  ? -53.400 25.132  4.382    1.00 121.78 ? 352  ASP   B N   1 
ATOM   3753  C  CA  . ASP   B  1 51  ? -53.232 25.001  5.824    1.00 116.22 ? 352  ASP   B CA  1 
ATOM   3754  C  C   . ASP   B  1 51  ? -54.182 23.964  6.406    1.00 113.39 ? 352  ASP   B C   1 
ATOM   3755  O  O   . ASP   B  1 51  ? -54.485 22.960  5.751    1.00 104.55 ? 352  ASP   B O   1 
ATOM   3756  C  CB  . ASP   B  1 51  ? -53.435 26.350  6.512    1.00 115.67 ? 352  ASP   B CB  1 
ATOM   3757  C  CG  . ASP   B  1 51  ? -52.214 27.242  6.412    1.00 114.99 ? 352  ASP   B CG  1 
ATOM   3758  O  OD1 . ASP   B  1 51  ? -51.084 26.743  6.615    1.00 108.15 ? 352  ASP   B OD1 1 
ATOM   3759  O  OD2 . ASP   B  1 51  ? -52.389 28.446  6.125    1.00 119.57 ? 352  ASP   B OD2 1 
ATOM   3760  N  N   . VAL   B  1 52  ? -54.650 24.200  7.636    1.00 121.77 ? 353  VAL   B N   1 
ATOM   3761  C  CA  . VAL   B  1 52  ? -55.486 23.241  8.353    1.00 122.92 ? 353  VAL   B CA  1 
ATOM   3762  C  C   . VAL   B  1 52  ? -56.797 23.040  7.598    1.00 126.64 ? 353  VAL   B C   1 
ATOM   3763  O  O   . VAL   B  1 52  ? -57.622 23.957  7.485    1.00 130.92 ? 353  VAL   B O   1 
ATOM   3764  C  CB  . VAL   B  1 52  ? -55.722 23.680  9.813    1.00 117.93 ? 353  VAL   B CB  1 
ATOM   3765  C  CG1 . VAL   B  1 52  ? -56.156 25.138  9.887    1.00 122.59 ? 353  VAL   B CG1 1 
ATOM   3766  C  CG2 . VAL   B  1 52  ? -56.735 22.765  10.493   1.00 112.55 ? 353  VAL   B CG2 1 
ATOM   3767  N  N   . ALA   B  1 53  ? -56.981 21.832  7.066    1.00 110.53 ? 354  ALA   B N   1 
ATOM   3768  C  CA  . ALA   B  1 53  ? -58.115 21.516  6.213    1.00 91.23  ? 354  ALA   B CA  1 
ATOM   3769  C  C   . ALA   B  1 53  ? -59.387 21.333  7.033    1.00 78.90  ? 354  ALA   B C   1 
ATOM   3770  O  O   . ALA   B  1 53  ? -59.348 20.988  8.218    1.00 69.69  ? 354  ALA   B O   1 
ATOM   3771  C  CB  . ALA   B  1 53  ? -57.834 20.248  5.408    1.00 85.45  ? 354  ALA   B CB  1 
ATOM   3772  N  N   . THR   B  1 54  ? -60.524 21.567  6.386    1.00 70.33  ? 355  THR   B N   1 
ATOM   3773  C  CA  . THR   B  1 54  ? -61.794 21.303  7.040    1.00 71.09  ? 355  THR   B CA  1 
ATOM   3774  C  C   . THR   B  1 54  ? -62.074 19.802  7.053    1.00 67.83  ? 355  THR   B C   1 
ATOM   3775  O  O   . THR   B  1 54  ? -61.403 19.009  6.384    1.00 62.24  ? 355  THR   B O   1 
ATOM   3776  C  CB  . THR   B  1 54  ? -62.930 22.051  6.342    1.00 69.25  ? 355  THR   B CB  1 
ATOM   3777  O  OG1 . THR   B  1 54  ? -62.990 21.648  4.969    1.00 63.11  ? 355  THR   B OG1 1 
ATOM   3778  C  CG2 . THR   B  1 54  ? -62.708 23.552  6.420    1.00 64.73  ? 355  THR   B CG2 1 
ATOM   3779  N  N   . LYS   B  1 55  ? -63.101 19.416  7.816    1.00 63.24  ? 356  LYS   B N   1 
ATOM   3780  C  CA  . LYS   B  1 55  ? -63.386 17.996  8.009    1.00 64.66  ? 356  LYS   B CA  1 
ATOM   3781  C  C   . LYS   B  1 55  ? -63.689 17.290  6.692    1.00 64.06  ? 356  LYS   B C   1 
ATOM   3782  O  O   . LYS   B  1 55  ? -63.257 16.149  6.484    1.00 45.92  ? 356  LYS   B O   1 
ATOM   3783  C  CB  . LYS   B  1 55  ? -64.547 17.814  8.977    1.00 72.85  ? 356  LYS   B CB  1 
ATOM   3784  C  CG  . LYS   B  1 55  ? -64.812 16.362  9.301    1.00 73.81  ? 356  LYS   B CG  1 
ATOM   3785  C  CD  . LYS   B  1 55  ? -66.015 16.225  10.198   1.00 76.53  ? 356  LYS   B CD  1 
ATOM   3786  C  CE  . LYS   B  1 55  ? -66.241 14.774  10.554   1.00 77.84  ? 356  LYS   B CE  1 
ATOM   3787  N  NZ  . LYS   B  1 55  ? -67.378 14.615  11.499   1.00 77.15  ? 356  LYS   B NZ  1 
ATOM   3788  N  N   . ASP   B  1 56  ? -64.443 17.942  5.800    1.00 59.93  ? 357  ASP   B N   1 
ATOM   3789  C  CA  . ASP   B  1 56  ? -64.782 17.338  4.514    1.00 63.55  ? 357  ASP   B CA  1 
ATOM   3790  C  C   . ASP   B  1 56  ? -63.568 17.175  3.620    1.00 60.94  ? 357  ASP   B C   1 
ATOM   3791  O  O   . ASP   B  1 56  ? -63.654 16.460  2.617    1.00 61.36  ? 357  ASP   B O   1 
ATOM   3792  C  CB  . ASP   B  1 56  ? -65.862 18.159  3.785    1.00 68.57  ? 357  ASP   B CB  1 
ATOM   3793  C  CG  . ASP   B  1 56  ? -65.410 19.577  3.419    1.00 77.88  ? 357  ASP   B CG  1 
ATOM   3794  O  OD1 . ASP   B  1 56  ? -64.272 19.973  3.741    1.00 84.94  ? 357  ASP   B OD1 1 
ATOM   3795  O  OD2 . ASP   B  1 56  ? -66.209 20.309  2.798    1.00 82.96  ? 357  ASP   B OD2 1 
ATOM   3796  N  N   . GLN   B  1 57  ? -62.456 17.827  3.962    1.00 56.71  ? 358  GLN   B N   1 
ATOM   3797  C  CA  . GLN   B  1 57  ? -61.200 17.724  3.236    1.00 58.79  ? 358  GLN   B CA  1 
ATOM   3798  C  C   . GLN   B  1 57  ? -60.301 16.634  3.809    1.00 55.81  ? 358  GLN   B C   1 
ATOM   3799  O  O   . GLN   B  1 57  ? -59.757 15.816  3.057    1.00 50.43  ? 358  GLN   B O   1 
ATOM   3800  C  CB  . GLN   B  1 57  ? -60.479 19.077  3.246    1.00 63.24  ? 358  GLN   B CB  1 
ATOM   3801  C  CG  . GLN   B  1 57  ? -61.090 20.091  2.292    1.00 76.42  ? 358  GLN   B CG  1 
ATOM   3802  C  CD  . GLN   B  1 57  ? -60.687 21.513  2.606    1.00 80.55  ? 358  GLN   B CD  1 
ATOM   3803  O  OE1 . GLN   B  1 57  ? -59.840 21.757  3.467    1.00 78.10  ? 358  GLN   B OE1 1 
ATOM   3804  N  NE2 . GLN   B  1 57  ? -61.297 22.466  1.911    1.00 83.01  ? 358  GLN   B NE2 1 
ATOM   3805  N  N   . LEU   B  1 58  ? -60.141 16.594  5.133    1.00 51.64  ? 359  LEU   B N   1 
ATOM   3806  C  CA  . LEU   B  1 58  ? -59.220 15.613  5.695    1.00 51.75  ? 359  LEU   B CA  1 
ATOM   3807  C  C   . LEU   B  1 58  ? -59.848 14.224  5.772    1.00 48.30  ? 359  LEU   B C   1 
ATOM   3808  O  O   . LEU   B  1 58  ? -59.214 13.236  5.388    1.00 45.90  ? 359  LEU   B O   1 
ATOM   3809  C  CB  . LEU   B  1 58  ? -58.731 16.059  7.072    1.00 47.28  ? 359  LEU   B CB  1 
ATOM   3810  C  CG  . LEU   B  1 58  ? -57.716 15.074  7.664    1.00 45.22  ? 359  LEU   B CG  1 
ATOM   3811  C  CD1 . LEU   B  1 58  ? -56.572 14.897  6.692    1.00 37.21  ? 359  LEU   B CD1 1 
ATOM   3812  C  CD2 . LEU   B  1 58  ? -57.200 15.493  9.065    1.00 43.58  ? 359  LEU   B CD2 1 
ATOM   3813  N  N   . PHE   B  1 59  ? -61.085 14.121  6.266    1.00 53.28  ? 360  PHE   B N   1 
ATOM   3814  C  CA  . PHE   B  1 59  ? -61.665 12.799  6.503    1.00 51.07  ? 360  PHE   B CA  1 
ATOM   3815  C  C   . PHE   B  1 59  ? -61.644 11.880  5.287    1.00 51.82  ? 360  PHE   B C   1 
ATOM   3816  O  O   . PHE   B  1 59  ? -61.283 10.703  5.448    1.00 49.22  ? 360  PHE   B O   1 
ATOM   3817  C  CB  . PHE   B  1 59  ? -63.106 12.879  7.012    1.00 44.64  ? 360  PHE   B CB  1 
ATOM   3818  C  CG  . PHE   B  1 59  ? -63.665 11.527  7.368    1.00 61.86  ? 360  PHE   B CG  1 
ATOM   3819  C  CD1 . PHE   B  1 59  ? -63.463 10.997  8.639    1.00 61.66  ? 360  PHE   B CD1 1 
ATOM   3820  C  CD2 . PHE   B  1 59  ? -64.337 10.757  6.423    1.00 53.24  ? 360  PHE   B CD2 1 
ATOM   3821  C  CE1 . PHE   B  1 59  ? -63.944 9.749   8.971    1.00 62.86  ? 360  PHE   B CE1 1 
ATOM   3822  C  CE2 . PHE   B  1 59  ? -64.814 9.505   6.744    1.00 58.58  ? 360  PHE   B CE2 1 
ATOM   3823  C  CZ  . PHE   B  1 59  ? -64.619 8.999   8.024    1.00 64.50  ? 360  PHE   B CZ  1 
ATOM   3824  N  N   . PRO   B  1 60  ? -62.054 12.311  4.082    1.00 52.99  ? 361  PRO   B N   1 
ATOM   3825  C  CA  . PRO   B  1 60  ? -62.038 11.372  2.938    1.00 54.16  ? 361  PRO   B CA  1 
ATOM   3826  C  C   . PRO   B  1 60  ? -60.675 10.762  2.665    1.00 49.17  ? 361  PRO   B C   1 
ATOM   3827  O  O   . PRO   B  1 60  ? -60.591 9.564   2.355    1.00 47.35  ? 361  PRO   B O   1 
ATOM   3828  C  CB  . PRO   B  1 60  ? -62.517 12.239  1.768    1.00 42.98  ? 361  PRO   B CB  1 
ATOM   3829  C  CG  . PRO   B  1 60  ? -63.360 13.297  2.401    1.00 51.33  ? 361  PRO   B CG  1 
ATOM   3830  C  CD  . PRO   B  1 60  ? -62.705 13.590  3.734    1.00 50.61  ? 361  PRO   B CD  1 
ATOM   3831  N  N   . LEU   B  1 61  ? -59.603 11.557  2.771    1.00 52.56  ? 362  LEU   B N   1 
ATOM   3832  C  CA  . LEU   B  1 61  ? -58.249 11.011  2.676    1.00 49.95  ? 362  LEU   B CA  1 
ATOM   3833  C  C   . LEU   B  1 61  ? -57.985 9.994   3.786    1.00 55.57  ? 362  LEU   B C   1 
ATOM   3834  O  O   . LEU   B  1 61  ? -57.435 8.915   3.541    1.00 57.89  ? 362  LEU   B O   1 
ATOM   3835  C  CB  . LEU   B  1 61  ? -57.228 12.148  2.739    1.00 42.98  ? 362  LEU   B CB  1 
ATOM   3836  C  CG  . LEU   B  1 61  ? -57.445 13.342  1.806    1.00 48.39  ? 362  LEU   B CG  1 
ATOM   3837  C  CD1 . LEU   B  1 61  ? -56.550 14.500  2.181    1.00 46.17  ? 362  LEU   B CD1 1 
ATOM   3838  C  CD2 . LEU   B  1 61  ? -57.164 12.917  0.394    1.00 48.28  ? 362  LEU   B CD2 1 
ATOM   3839  N  N   . ALA   B  1 62  ? -58.367 10.328  5.022    1.00 55.22  ? 363  ALA   B N   1 
ATOM   3840  C  CA  . ALA   B  1 62  ? -58.183 9.400   6.135    1.00 52.27  ? 363  ALA   B CA  1 
ATOM   3841  C  C   . ALA   B  1 62  ? -58.935 8.096   5.893    1.00 50.13  ? 363  ALA   B C   1 
ATOM   3842  O  O   . ALA   B  1 62  ? -58.366 7.003   6.024    1.00 46.26  ? 363  ALA   B O   1 
ATOM   3843  C  CB  . ALA   B  1 62  ? -58.647 10.050  7.446    1.00 48.81  ? 363  ALA   B CB  1 
ATOM   3844  N  N   . LYS   B  1 63  ? -60.227 8.197   5.550    1.00 48.48  ? 364  LYS   B N   1 
ATOM   3845  C  CA  . LYS   B  1 63  ? -61.032 6.999   5.327    1.00 51.23  ? 364  LYS   B CA  1 
ATOM   3846  C  C   . LYS   B  1 63  ? -60.391 6.102   4.289    1.00 50.44  ? 364  LYS   B C   1 
ATOM   3847  O  O   . LYS   B  1 63  ? -60.431 4.874   4.408    1.00 55.58  ? 364  LYS   B O   1 
ATOM   3848  C  CB  . LYS   B  1 63  ? -62.449 7.374   4.892    1.00 55.23  ? 364  LYS   B CB  1 
ATOM   3849  C  CG  . LYS   B  1 63  ? -63.391 6.166   4.755    1.00 65.57  ? 364  LYS   B CG  1 
ATOM   3850  C  CD  . LYS   B  1 63  ? -64.421 6.346   3.639    1.00 71.82  ? 364  LYS   B CD  1 
ATOM   3851  C  CE  . LYS   B  1 63  ? -65.438 5.204   3.586    1.00 68.56  ? 364  LYS   B CE  1 
ATOM   3852  N  NZ  . LYS   B  1 63  ? -64.860 3.916   3.120    1.00 65.91  ? 364  LYS   B NZ  1 
ATOM   3853  N  N   . GLU   B  1 64  ? -59.766 6.704   3.280    1.00 46.23  ? 365  GLU   B N   1 
ATOM   3854  C  CA  . GLU   B  1 64  ? -59.172 5.934   2.198    1.00 52.05  ? 365  GLU   B CA  1 
ATOM   3855  C  C   . GLU   B  1 64  ? -57.940 5.164   2.676    1.00 46.35  ? 365  GLU   B C   1 
ATOM   3856  O  O   . GLU   B  1 64  ? -57.775 3.975   2.364    1.00 42.14  ? 365  GLU   B O   1 
ATOM   3857  C  CB  . GLU   B  1 64  ? -58.823 6.878   1.043    1.00 53.99  ? 365  GLU   B CB  1 
ATOM   3858  C  CG  . GLU   B  1 64  ? -58.496 6.179   -0.250   1.00 69.24  ? 365  GLU   B CG  1 
ATOM   3859  C  CD  . GLU   B  1 64  ? -57.129 6.558   -0.768   1.00 84.93  ? 365  GLU   B CD  1 
ATOM   3860  O  OE1 . GLU   B  1 64  ? -56.147 5.888   -0.373   1.00 88.98  ? 365  GLU   B OE1 1 
ATOM   3861  O  OE2 . GLU   B  1 64  ? -57.039 7.536   -1.551   1.00 88.43  ? 365  GLU   B OE2 1 
ATOM   3862  N  N   . PHE   B  1 65  ? -57.051 5.829   3.420    1.00 44.67  ? 366  PHE   B N   1 
ATOM   3863  C  CA  . PHE   B  1 65  ? -55.865 5.138   3.922    1.00 47.58  ? 366  PHE   B CA  1 
ATOM   3864  C  C   . PHE   B  1 65  ? -56.250 3.996   4.858    1.00 52.57  ? 366  PHE   B C   1 
ATOM   3865  O  O   . PHE   B  1 65  ? -55.707 2.888   4.755    1.00 53.29  ? 366  PHE   B O   1 
ATOM   3866  C  CB  . PHE   B  1 65  ? -54.935 6.115   4.634    1.00 45.64  ? 366  PHE   B CB  1 
ATOM   3867  C  CG  . PHE   B  1 65  ? -53.838 5.440   5.399    1.00 54.46  ? 366  PHE   B CG  1 
ATOM   3868  C  CD1 . PHE   B  1 65  ? -52.852 4.723   4.733    1.00 51.67  ? 366  PHE   B CD1 1 
ATOM   3869  C  CD2 . PHE   B  1 65  ? -53.805 5.495   6.785    1.00 57.52  ? 366  PHE   B CD2 1 
ATOM   3870  C  CE1 . PHE   B  1 65  ? -51.851 4.082   5.431    1.00 50.90  ? 366  PHE   B CE1 1 
ATOM   3871  C  CE2 . PHE   B  1 65  ? -52.796 4.864   7.494    1.00 54.91  ? 366  PHE   B CE2 1 
ATOM   3872  C  CZ  . PHE   B  1 65  ? -51.820 4.154   6.817    1.00 48.91  ? 366  PHE   B CZ  1 
ATOM   3873  N  N   . ILE   B  1 66  ? -57.188 4.254   5.779    1.00 51.86  ? 367  ILE   B N   1 
ATOM   3874  C  CA  . ILE   B  1 66  ? -57.624 3.228   6.728    1.00 51.76  ? 367  ILE   B CA  1 
ATOM   3875  C  C   . ILE   B  1 66  ? -58.293 2.071   5.986    1.00 50.87  ? 367  ILE   B C   1 
ATOM   3876  O  O   . ILE   B  1 66  ? -58.030 0.897   6.273    1.00 44.96  ? 367  ILE   B O   1 
ATOM   3877  C  CB  . ILE   B  1 66  ? -58.557 3.851   7.792    1.00 50.32  ? 367  ILE   B CB  1 
ATOM   3878  C  CG1 . ILE   B  1 66  ? -57.880 5.031   8.516    1.00 45.73  ? 367  ILE   B CG1 1 
ATOM   3879  C  CG2 . ILE   B  1 66  ? -59.064 2.794   8.774    1.00 47.99  ? 367  ILE   B CG2 1 
ATOM   3880  C  CD1 . ILE   B  1 66  ? -56.868 4.639   9.603    1.00 44.48  ? 367  ILE   B CD1 1 
ATOM   3881  N  N   . ASP   B  1 67  ? -59.160 2.385   5.014    1.00 53.80  ? 368  ASP   B N   1 
ATOM   3882  C  CA  . ASP   B  1 67  ? -59.721 1.358   4.133    1.00 57.63  ? 368  ASP   B CA  1 
ATOM   3883  C  C   . ASP   B  1 67  ? -58.616 0.537   3.470    1.00 49.25  ? 368  ASP   B C   1 
ATOM   3884  O  O   . ASP   B  1 67  ? -58.616 -0.699  3.532    1.00 46.84  ? 368  ASP   B O   1 
ATOM   3885  C  CB  . ASP   B  1 67  ? -60.613 2.003   3.066    1.00 58.44  ? 368  ASP   B CB  1 
ATOM   3886  C  CG  . ASP   B  1 67  ? -61.959 2.456   3.611    1.00 64.62  ? 368  ASP   B CG  1 
ATOM   3887  O  OD1 . ASP   B  1 67  ? -62.259 2.179   4.787    1.00 58.74  ? 368  ASP   B OD1 1 
ATOM   3888  O  OD2 . ASP   B  1 67  ? -62.722 3.089   2.852    1.00 69.82  ? 368  ASP   B OD2 1 
ATOM   3889  N  N   . GLN   B  1 68  ? -57.659 1.217   2.836    1.00 46.09  ? 369  GLN   B N   1 
ATOM   3890  C  CA  . GLN   B  1 68  ? -56.501 0.544   2.260    1.00 46.12  ? 369  GLN   B CA  1 
ATOM   3891  C  C   . GLN   B  1 68  ? -55.792 -0.345  3.283    1.00 52.24  ? 369  GLN   B C   1 
ATOM   3892  O  O   . GLN   B  1 68  ? -55.535 -1.525  3.017    1.00 50.43  ? 369  GLN   B O   1 
ATOM   3893  C  CB  . GLN   B  1 68  ? -55.546 1.592   1.688    1.00 45.99  ? 369  GLN   B CB  1 
ATOM   3894  C  CG  . GLN   B  1 68  ? -54.246 1.047   1.118    1.00 53.13  ? 369  GLN   B CG  1 
ATOM   3895  C  CD  . GLN   B  1 68  ? -53.330 2.159   0.610    1.00 66.27  ? 369  GLN   B CD  1 
ATOM   3896  O  OE1 . GLN   B  1 68  ? -52.100 2.069   0.710    1.00 62.93  ? 369  GLN   B OE1 1 
ATOM   3897  N  NE2 . GLN   B  1 68  ? -53.932 3.218   0.066    1.00 73.89  ? 369  GLN   B NE2 1 
ATOM   3898  N  N   . TYR   B  1 69  ? -55.484 0.198   4.469    1.00 54.58  ? 370  TYR   B N   1 
ATOM   3899  C  CA  . TYR   B  1 69  ? -54.713 -0.570  5.454    1.00 51.89  ? 370  TYR   B CA  1 
ATOM   3900  C  C   . TYR   B  1 69  ? -55.488 -1.776  5.978    1.00 47.51  ? 370  TYR   B C   1 
ATOM   3901  O  O   . TYR   B  1 69  ? -54.922 -2.865  6.139    1.00 50.17  ? 370  TYR   B O   1 
ATOM   3902  C  CB  . TYR   B  1 69  ? -54.279 0.301   6.636    1.00 39.19  ? 370  TYR   B CB  1 
ATOM   3903  C  CG  . TYR   B  1 69  ? -53.813 -0.546  7.801    1.00 40.72  ? 370  TYR   B CG  1 
ATOM   3904  C  CD1 . TYR   B  1 69  ? -52.574 -1.176  7.779    1.00 40.59  ? 370  TYR   B CD1 1 
ATOM   3905  C  CD2 . TYR   B  1 69  ? -54.638 -0.755  8.912    1.00 41.57  ? 370  TYR   B CD2 1 
ATOM   3906  C  CE1 . TYR   B  1 69  ? -52.160 -1.987  8.837    1.00 40.68  ? 370  TYR   B CE1 1 
ATOM   3907  C  CE2 . TYR   B  1 69  ? -54.224 -1.549  9.970    1.00 44.76  ? 370  TYR   B CE2 1 
ATOM   3908  C  CZ  . TYR   B  1 69  ? -52.989 -2.160  9.932    1.00 46.46  ? 370  TYR   B CZ  1 
ATOM   3909  O  OH  . TYR   B  1 69  ? -52.599 -2.956  10.991   1.00 55.16  ? 370  TYR   B OH  1 
ATOM   3910  N  N   . TYR   B  1 70  ? -56.770 -1.604  6.293    1.00 45.29  ? 371  TYR   B N   1 
ATOM   3911  C  CA  . TYR   B  1 70  ? -57.508 -2.771  6.757    1.00 48.11  ? 371  TYR   B CA  1 
ATOM   3912  C  C   . TYR   B  1 70  ? -57.722 -3.762  5.624    1.00 51.22  ? 371  TYR   B C   1 
ATOM   3913  O  O   . TYR   B  1 70  ? -57.703 -4.974  5.860    1.00 46.63  ? 371  TYR   B O   1 
ATOM   3914  C  CB  . TYR   B  1 70  ? -58.820 -2.354  7.421    1.00 54.67  ? 371  TYR   B CB  1 
ATOM   3915  C  CG  . TYR   B  1 70  ? -58.627 -2.068  8.902    1.00 58.50  ? 371  TYR   B CG  1 
ATOM   3916  C  CD1 . TYR   B  1 70  ? -58.698 -3.097  9.846    1.00 54.34  ? 371  TYR   B CD1 1 
ATOM   3917  C  CD2 . TYR   B  1 70  ? -58.338 -0.785  9.355    1.00 59.92  ? 371  TYR   B CD2 1 
ATOM   3918  C  CE1 . TYR   B  1 70  ? -58.503 -2.853  11.200   1.00 50.84  ? 371  TYR   B CE1 1 
ATOM   3919  C  CE2 . TYR   B  1 70  ? -58.143 -0.529  10.718   1.00 60.66  ? 371  TYR   B CE2 1 
ATOM   3920  C  CZ  . TYR   B  1 70  ? -58.224 -1.570  11.634   1.00 56.97  ? 371  TYR   B CZ  1 
ATOM   3921  O  OH  . TYR   B  1 70  ? -58.027 -1.319  12.979   1.00 51.54  ? 371  TYR   B OH  1 
ATOM   3922  N  N   . SER   B  1 71  ? -57.862 -3.270  4.383    1.00 56.21  ? 372  SER   B N   1 
ATOM   3923  C  CA  . SER   B  1 71  ? -57.877 -4.171  3.233    1.00 58.16  ? 372  SER   B CA  1 
ATOM   3924  C  C   . SER   B  1 71  ? -56.576 -4.960  3.138    1.00 47.24  ? 372  SER   B C   1 
ATOM   3925  O  O   . SER   B  1 71  ? -56.590 -6.163  2.851    1.00 48.89  ? 372  SER   B O   1 
ATOM   3926  C  CB  . SER   B  1 71  ? -58.129 -3.385  1.947    1.00 64.45  ? 372  SER   B CB  1 
ATOM   3927  O  OG  . SER   B  1 71  ? -59.457 -2.887  1.919    1.00 73.66  ? 372  SER   B OG  1 
ATOM   3928  N  N   . SER   B  1 72  ? -55.447 -4.308  3.414    1.00 41.51  ? 373  SER   B N   1 
ATOM   3929  C  CA  . SER   B  1 72  ? -54.156 -4.987  3.365    1.00 46.19  ? 373  SER   B CA  1 
ATOM   3930  C  C   . SER   B  1 72  ? -54.136 -6.232  4.238    1.00 52.27  ? 373  SER   B C   1 
ATOM   3931  O  O   . SER   B  1 72  ? -53.569 -7.258  3.845    1.00 54.03  ? 373  SER   B O   1 
ATOM   3932  C  CB  . SER   B  1 72  ? -53.049 -4.033  3.801    1.00 47.53  ? 373  SER   B CB  1 
ATOM   3933  O  OG  . SER   B  1 72  ? -52.854 -4.138  5.201    1.00 56.30  ? 373  SER   B OG  1 
ATOM   3934  N  N   . ILE   B  1 73  ? -54.755 -6.166  5.422    1.00 43.44  ? 374  ILE   B N   1 
ATOM   3935  C  CA  . ILE   B  1 73  ? -54.672 -7.240  6.404    1.00 43.67  ? 374  ILE   B CA  1 
ATOM   3936  C  C   . ILE   B  1 73  ? -55.922 -8.127  6.389    1.00 45.66  ? 374  ILE   B C   1 
ATOM   3937  O  O   . ILE   B  1 73  ? -56.203 -8.813  7.373    1.00 57.70  ? 374  ILE   B O   1 
ATOM   3938  C  CB  . ILE   B  1 73  ? -54.392 -6.694  7.818    1.00 50.91  ? 374  ILE   B CB  1 
ATOM   3939  C  CG1 . ILE   B  1 73  ? -55.542 -5.785  8.290    1.00 49.15  ? 374  ILE   B CG1 1 
ATOM   3940  C  CG2 . ILE   B  1 73  ? -53.049 -5.962  7.857    1.00 43.55  ? 374  ILE   B CG2 1 
ATOM   3941  C  CD1 . ILE   B  1 73  ? -55.332 -5.129  9.634    1.00 49.60  ? 374  ILE   B CD1 1 
ATOM   3942  N  N   . LYS   B  1 74  ? -56.668 -8.141  5.284    1.00 51.06  ? 375  LYS   B N   1 
ATOM   3943  C  CA  . LYS   B  1 74  ? -57.809 -9.048  5.116    1.00 67.56  ? 375  LYS   B CA  1 
ATOM   3944  C  C   . LYS   B  1 74  ? -58.846 -8.840  6.221    1.00 66.98  ? 375  LYS   B C   1 
ATOM   3945  O  O   . LYS   B  1 74  ? -59.417 -9.792  6.759    1.00 65.51  ? 375  LYS   B O   1 
ATOM   3946  C  CB  . LYS   B  1 74  ? -57.375 -10.519 5.059    1.00 74.34  ? 375  LYS   B CB  1 
ATOM   3947  C  CG  . LYS   B  1 74  ? -56.088 -10.797 4.301    1.00 72.36  ? 375  LYS   B CG  1 
ATOM   3948  C  CD  . LYS   B  1 74  ? -56.289 -10.746 2.812    1.00 71.36  ? 375  LYS   B CD  1 
ATOM   3949  C  CE  . LYS   B  1 74  ? -54.968 -10.491 2.096    1.00 69.03  ? 375  LYS   B CE  1 
ATOM   3950  N  NZ  . LYS   B  1 74  ? -55.216 -10.084 0.689    1.00 58.69  ? 375  LYS   B NZ  1 
ATOM   3951  N  N   . ARG   B  1 75  ? -59.064 -7.581  6.582    1.00 64.05  ? 376  ARG   B N   1 
ATOM   3952  C  CA  . ARG   B  1 75  ? -60.274 -7.190  7.284    1.00 71.22  ? 376  ARG   B CA  1 
ATOM   3953  C  C   . ARG   B  1 75  ? -61.168 -6.457  6.299    1.00 82.52  ? 376  ARG   B C   1 
ATOM   3954  O  O   . ARG   B  1 75  ? -61.676 -7.052  5.339    1.00 84.70  ? 376  ARG   B O   1 
ATOM   3955  C  CB  . ARG   B  1 75  ? -59.955 -6.302  8.477    1.00 65.78  ? 376  ARG   B CB  1 
ATOM   3956  C  CG  . ARG   B  1 75  ? -58.887 -6.884  9.356    1.00 67.33  ? 376  ARG   B CG  1 
ATOM   3957  C  CD  . ARG   B  1 75  ? -59.495 -7.853  10.323   1.00 86.22  ? 376  ARG   B CD  1 
ATOM   3958  N  NE  . ARG   B  1 75  ? -58.902 -9.176  10.214   1.00 93.18  ? 376  ARG   B NE  1 
ATOM   3959  C  CZ  . ARG   B  1 75  ? -59.081 -10.143 11.105   1.00 94.34  ? 376  ARG   B CZ  1 
ATOM   3960  N  NH1 . ARG   B  1 75  ? -58.494 -11.316 10.914   1.00 91.88  ? 376  ARG   B NH1 1 
ATOM   3961  N  NH2 . ARG   B  1 75  ? -59.840 -9.937  12.184   1.00 93.85  ? 376  ARG   B NH2 1 
ATOM   3962  N  N   . PHE   B  1 76  ? -61.301 -5.149  6.510    1.00 82.45  ? 377  PHE   B N   1 
ATOM   3963  C  CA  . PHE   B  1 76  ? -62.210 -4.289  5.766    1.00 78.85  ? 377  PHE   B CA  1 
ATOM   3964  C  C   . PHE   B  1 76  ? -63.646 -4.627  6.142    1.00 76.11  ? 377  PHE   B C   1 
ATOM   3965  O  O   . PHE   B  1 76  ? -64.152 -5.713  5.835    1.00 64.88  ? 377  PHE   B O   1 
ATOM   3966  C  CB  . PHE   B  1 76  ? -62.003 -4.379  4.248    1.00 76.83  ? 377  PHE   B CB  1 
ATOM   3967  C  CG  . PHE   B  1 76  ? -63.009 -3.589  3.474    1.00 76.60  ? 377  PHE   B CG  1 
ATOM   3968  C  CD1 . PHE   B  1 76  ? -62.834 -2.229  3.271    1.00 73.85  ? 377  PHE   B CD1 1 
ATOM   3969  C  CD2 . PHE   B  1 76  ? -64.159 -4.194  2.996    1.00 81.55  ? 377  PHE   B CD2 1 
ATOM   3970  C  CE1 . PHE   B  1 76  ? -63.782 -1.494  2.586    1.00 77.78  ? 377  PHE   B CE1 1 
ATOM   3971  C  CE2 . PHE   B  1 76  ? -65.113 -3.467  2.316    1.00 86.35  ? 377  PHE   B CE2 1 
ATOM   3972  C  CZ  . PHE   B  1 76  ? -64.923 -2.116  2.106    1.00 85.68  ? 377  PHE   B CZ  1 
ATOM   3973  N  N   . GLY   B  1 77  ? -64.311 -3.683  6.804    1.00 78.25  ? 378  GLY   B N   1 
ATOM   3974  C  CA  . GLY   B  1 77  ? -65.609 -3.923  7.377    1.00 78.58  ? 378  GLY   B CA  1 
ATOM   3975  C  C   . GLY   B  1 77  ? -65.578 -4.614  8.715    1.00 74.90  ? 378  GLY   B C   1 
ATOM   3976  O  O   . GLY   B  1 77  ? -66.628 -4.715  9.361    1.00 80.92  ? 378  GLY   B O   1 
ATOM   3977  N  N   . SER   B  1 78  ? -64.413 -5.092  9.155    1.00 65.47  ? 379  SER   B N   1 
ATOM   3978  C  CA  . SER   B  1 78  ? -64.308 -5.760  10.441   1.00 59.06  ? 379  SER   B CA  1 
ATOM   3979  C  C   . SER   B  1 78  ? -64.666 -4.791  11.564   1.00 64.02  ? 379  SER   B C   1 
ATOM   3980  O  O   . SER   B  1 78  ? -64.769 -3.575  11.372   1.00 61.10  ? 379  SER   B O   1 
ATOM   3981  C  CB  . SER   B  1 78  ? -62.897 -6.308  10.655   1.00 56.47  ? 379  SER   B CB  1 
ATOM   3982  O  OG  . SER   B  1 78  ? -61.971 -5.249  10.865   1.00 49.26  ? 379  SER   B OG  1 
ATOM   3983  N  N   . LYS   B  1 79  ? -64.855 -5.347  12.759   1.00 63.60  ? 380  LYS   B N   1 
ATOM   3984  C  CA  . LYS   B  1 79  ? -65.195 -4.499  13.891   1.00 63.41  ? 380  LYS   B CA  1 
ATOM   3985  C  C   . LYS   B  1 79  ? -64.105 -3.452  14.121   1.00 62.51  ? 380  LYS   B C   1 
ATOM   3986  O  O   . LYS   B  1 79  ? -64.393 -2.254  14.219   1.00 62.70  ? 380  LYS   B O   1 
ATOM   3987  C  CB  . LYS   B  1 79  ? -65.448 -5.361  15.135   1.00 57.51  ? 380  LYS   B CB  1 
ATOM   3988  C  CG  . LYS   B  1 79  ? -66.490 -4.770  16.095   1.00 76.86  ? 380  LYS   B CG  1 
ATOM   3989  C  CD  . LYS   B  1 79  ? -67.292 -5.842  16.875   1.00 80.40  ? 380  LYS   B CD  1 
ATOM   3990  C  CE  . LYS   B  1 79  ? -68.590 -6.220  16.152   1.00 83.65  ? 380  LYS   B CE  1 
ATOM   3991  N  NZ  . LYS   B  1 79  ? -69.586 -5.110  16.097   1.00 81.37  ? 380  LYS   B NZ  1 
ATOM   3992  N  N   . ALA   B  1 80  ? -62.836 -3.876  14.141   1.00 59.20  ? 381  ALA   B N   1 
ATOM   3993  C  CA  . ALA   B  1 80  ? -61.747 -2.933  14.387   1.00 53.55  ? 381  ALA   B CA  1 
ATOM   3994  C  C   . ALA   B  1 80  ? -61.641 -1.883  13.283   1.00 55.88  ? 381  ALA   B C   1 
ATOM   3995  O  O   . ALA   B  1 80  ? -61.151 -0.773  13.526   1.00 49.94  ? 381  ALA   B O   1 
ATOM   3996  C  CB  . ALA   B  1 80  ? -60.422 -3.683  14.530   1.00 50.63  ? 381  ALA   B CB  1 
ATOM   3997  N  N   . HIS   B  1 81  ? -62.083 -2.209  12.067   1.00 57.87  ? 382  HIS   B N   1 
ATOM   3998  C  CA  . HIS   B  1 81  ? -62.039 -1.228  10.984   1.00 60.04  ? 382  HIS   B CA  1 
ATOM   3999  C  C   . HIS   B  1 81  ? -63.125 -0.174  11.162   1.00 65.07  ? 382  HIS   B C   1 
ATOM   4000  O  O   . HIS   B  1 81  ? -62.868 1.030   11.028   1.00 57.78  ? 382  HIS   B O   1 
ATOM   4001  C  CB  . HIS   B  1 81  ? -62.186 -1.929  9.634    1.00 57.66  ? 382  HIS   B CB  1 
ATOM   4002  C  CG  . HIS   B  1 81  ? -62.199 -0.992  8.470    1.00 69.06  ? 382  HIS   B CG  1 
ATOM   4003  N  ND1 . HIS   B  1 81  ? -62.598 -1.379  7.211    1.00 74.58  ? 382  HIS   B ND1 1 
ATOM   4004  C  CD2 . HIS   B  1 81  ? -61.851 0.313   8.369    1.00 73.64  ? 382  HIS   B CD2 1 
ATOM   4005  C  CE1 . HIS   B  1 81  ? -62.500 -0.353  6.384    1.00 75.54  ? 382  HIS   B CE1 1 
ATOM   4006  N  NE2 . HIS   B  1 81  ? -62.051 0.687   7.062    1.00 72.51  ? 382  HIS   B NE2 1 
ATOM   4007  N  N   . MET   B  1 82  ? -64.349 -0.615  11.474   1.00 68.12  ? 383  MET   B N   1 
ATOM   4008  C  CA  . MET   B  1 82  ? -65.454 0.323   11.632   1.00 66.99  ? 383  MET   B CA  1 
ATOM   4009  C  C   . MET   B  1 82  ? -65.261 1.212   12.849   1.00 67.23  ? 383  MET   B C   1 
ATOM   4010  O  O   . MET   B  1 82  ? -65.696 2.370   12.843   1.00 61.45  ? 383  MET   B O   1 
ATOM   4011  C  CB  . MET   B  1 82  ? -66.782 -0.430  11.731   1.00 65.22  ? 383  MET   B CB  1 
ATOM   4012  C  CG  . MET   B  1 82  ? -67.131 -1.215  10.490   1.00 63.47  ? 383  MET   B CG  1 
ATOM   4013  S  SD  . MET   B  1 82  ? -66.856 -0.204  9.021    1.00 74.79  ? 383  MET   B SD  1 
ATOM   4014  C  CE  . MET   B  1 82  ? -68.213 0.954   9.216    1.00 80.02  ? 383  MET   B CE  1 
ATOM   4015  N  N   . GLU   B  1 83  ? -64.619 0.692   13.898   1.00 70.99  ? 384  GLU   B N   1 
ATOM   4016  C  CA  . GLU   B  1 83  ? -64.353 1.509   15.074   1.00 67.30  ? 384  GLU   B CA  1 
ATOM   4017  C  C   . GLU   B  1 83  ? -63.252 2.514   14.789   1.00 57.17  ? 384  GLU   B C   1 
ATOM   4018  O  O   . GLU   B  1 83  ? -63.283 3.643   15.296   1.00 52.24  ? 384  GLU   B O   1 
ATOM   4019  C  CB  . GLU   B  1 83  ? -63.968 0.628   16.258   1.00 71.81  ? 384  GLU   B CB  1 
ATOM   4020  C  CG  . GLU   B  1 83  ? -65.025 -0.368  16.657   1.00 81.83  ? 384  GLU   B CG  1 
ATOM   4021  C  CD  . GLU   B  1 83  ? -64.517 -1.349  17.683   1.00 88.87  ? 384  GLU   B CD  1 
ATOM   4022  O  OE1 . GLU   B  1 83  ? -63.396 -1.137  18.191   1.00 89.85  ? 384  GLU   B OE1 1 
ATOM   4023  O  OE2 . GLU   B  1 83  ? -65.233 -2.328  17.981   1.00 94.45  ? 384  GLU   B OE2 1 
ATOM   4024  N  N   . ARG   B  1 84  ? -62.265 2.113   13.987   1.00 55.27  ? 385  ARG   B N   1 
ATOM   4025  C  CA  . ARG   B  1 84  ? -61.203 3.034   13.611   1.00 55.57  ? 385  ARG   B CA  1 
ATOM   4026  C  C   . ARG   B  1 84  ? -61.757 4.219   12.823   1.00 60.79  ? 385  ARG   B C   1 
ATOM   4027  O  O   . ARG   B  1 84  ? -61.355 5.368   13.044   1.00 65.83  ? 385  ARG   B O   1 
ATOM   4028  C  CB  . ARG   B  1 84  ? -60.141 2.285   12.813   1.00 55.09  ? 385  ARG   B CB  1 
ATOM   4029  C  CG  . ARG   B  1 84  ? -58.876 3.067   12.592   1.00 51.56  ? 385  ARG   B CG  1 
ATOM   4030  C  CD  . ARG   B  1 84  ? -58.033 3.187   13.848   1.00 57.27  ? 385  ARG   B CD  1 
ATOM   4031  N  NE  . ARG   B  1 84  ? -56.846 3.987   13.571   1.00 60.38  ? 385  ARG   B NE  1 
ATOM   4032  C  CZ  . ARG   B  1 84  ? -56.678 5.240   13.978   1.00 59.68  ? 385  ARG   B CZ  1 
ATOM   4033  N  NH1 . ARG   B  1 84  ? -57.611 5.835   14.718   1.00 62.56  ? 385  ARG   B NH1 1 
ATOM   4034  N  NH2 . ARG   B  1 84  ? -55.565 5.886   13.667   1.00 49.34  ? 385  ARG   B NH2 1 
ATOM   4035  N  N   . LEU   B  1 85  ? -62.697 3.961   11.913   1.00 59.43  ? 386  LEU   B N   1 
ATOM   4036  C  CA  . LEU   B  1 85  ? -63.328 5.051   11.177   1.00 54.98  ? 386  LEU   B CA  1 
ATOM   4037  C  C   . LEU   B  1 85  ? -64.007 6.035   12.126   1.00 53.13  ? 386  LEU   B C   1 
ATOM   4038  O  O   . LEU   B  1 85  ? -63.818 7.253   12.018   1.00 53.99  ? 386  LEU   B O   1 
ATOM   4039  C  CB  . LEU   B  1 85  ? -64.321 4.482   10.161   1.00 54.62  ? 386  LEU   B CB  1 
ATOM   4040  C  CG  . LEU   B  1 85  ? -63.688 3.695   8.997    1.00 56.69  ? 386  LEU   B CG  1 
ATOM   4041  C  CD1 . LEU   B  1 85  ? -64.736 3.237   7.992    1.00 47.57  ? 386  LEU   B CD1 1 
ATOM   4042  C  CD2 . LEU   B  1 85  ? -62.593 4.497   8.295    1.00 54.60  ? 386  LEU   B CD2 1 
ATOM   4043  N  N   . GLU   B  1 86  ? -64.791 5.519   13.076   1.00 58.77  ? 387  GLU   B N   1 
ATOM   4044  C  CA  . GLU   B  1 86  ? -65.442 6.376   14.062   1.00 65.33  ? 387  GLU   B CA  1 
ATOM   4045  C  C   . GLU   B  1 86  ? -64.421 7.087   14.939   1.00 63.63  ? 387  GLU   B C   1 
ATOM   4046  O  O   . GLU   B  1 86  ? -64.626 8.241   15.336   1.00 64.49  ? 387  GLU   B O   1 
ATOM   4047  C  CB  . GLU   B  1 86  ? -66.395 5.549   14.923   1.00 75.85  ? 387  GLU   B CB  1 
ATOM   4048  C  CG  . GLU   B  1 86  ? -67.491 4.853   14.142   1.00 95.45  ? 387  GLU   B CG  1 
ATOM   4049  C  CD  . GLU   B  1 86  ? -68.063 3.655   14.879   1.00 113.87 ? 387  GLU   B CD  1 
ATOM   4050  O  OE1 . GLU   B  1 86  ? -68.003 3.637   16.130   1.00 120.10 ? 387  GLU   B OE1 1 
ATOM   4051  O  OE2 . GLU   B  1 86  ? -68.562 2.725   14.203   1.00 119.08 ? 387  GLU   B OE2 1 
ATOM   4052  N  N   . GLU   B  1 87  ? -63.313 6.414   15.254   1.00 61.38  ? 388  GLU   B N   1 
ATOM   4053  C  CA  . GLU   B  1 87  ? -62.269 7.053   16.046   1.00 66.57  ? 388  GLU   B CA  1 
ATOM   4054  C  C   . GLU   B  1 87  ? -61.608 8.186   15.263   1.00 63.37  ? 388  GLU   B C   1 
ATOM   4055  O  O   . GLU   B  1 87  ? -61.441 9.299   15.782   1.00 44.50  ? 388  GLU   B O   1 
ATOM   4056  C  CB  . GLU   B  1 87  ? -61.240 6.010   16.495   1.00 63.08  ? 388  GLU   B CB  1 
ATOM   4057  C  CG  . GLU   B  1 87  ? -60.326 6.473   17.611   1.00 59.44  ? 388  GLU   B CG  1 
ATOM   4058  C  CD  . GLU   B  1 87  ? -59.272 5.435   17.970   1.00 64.68  ? 388  GLU   B CD  1 
ATOM   4059  O  OE1 . GLU   B  1 87  ? -59.069 4.494   17.168   1.00 59.93  ? 388  GLU   B OE1 1 
ATOM   4060  O  OE2 . GLU   B  1 87  ? -58.650 5.561   19.053   1.00 65.49  ? 388  GLU   B OE2 1 
ATOM   4061  N  N   . VAL   B  1 88  ? -61.234 7.932   14.004   1.00 58.02  ? 389  VAL   B N   1 
ATOM   4062  C  CA  . VAL   B  1 88  ? -60.646 9.002   13.200   1.00 53.65  ? 389  VAL   B CA  1 
ATOM   4063  C  C   . VAL   B  1 88  ? -61.638 10.151  13.032   1.00 56.28  ? 389  VAL   B C   1 
ATOM   4064  O  O   . VAL   B  1 88  ? -61.264 11.328  13.097   1.00 55.75  ? 389  VAL   B O   1 
ATOM   4065  C  CB  . VAL   B  1 88  ? -60.159 8.459   11.848   1.00 54.83  ? 389  VAL   B CB  1 
ATOM   4066  C  CG1 . VAL   B  1 88  ? -59.852 9.615   10.881   1.00 40.76  ? 389  VAL   B CG1 1 
ATOM   4067  C  CG2 . VAL   B  1 88  ? -58.922 7.589   12.060   1.00 46.44  ? 389  VAL   B CG2 1 
ATOM   4068  N  N   . ASN   B  1 89  ? -62.922 9.832   12.864   1.00 56.57  ? 390  ASN   B N   1 
ATOM   4069  C  CA  . ASN   B  1 89  ? -63.919 10.878  12.662   1.00 57.15  ? 390  ASN   B CA  1 
ATOM   4070  C  C   . ASN   B  1 89  ? -64.105 11.730  13.914   1.00 64.11  ? 390  ASN   B C   1 
ATOM   4071  O  O   . ASN   B  1 89  ? -64.144 12.966  13.834   1.00 65.12  ? 390  ASN   B O   1 
ATOM   4072  C  CB  . ASN   B  1 89  ? -65.248 10.263  12.239   1.00 61.26  ? 390  ASN   B CB  1 
ATOM   4073  C  CG  . ASN   B  1 89  ? -66.248 11.312  11.806   1.00 71.44  ? 390  ASN   B CG  1 
ATOM   4074  O  OD1 . ASN   B  1 89  ? -66.934 11.921  12.634   1.00 72.16  ? 390  ASN   B OD1 1 
ATOM   4075  N  ND2 . ASN   B  1 89  ? -66.333 11.536  10.495   1.00 77.42  ? 390  ASN   B ND2 1 
ATOM   4076  N  N   . LYS   B  1 90  ? -64.257 11.088  15.078   1.00 57.96  ? 391  LYS   B N   1 
ATOM   4077  C  CA  . LYS   B  1 90  ? -64.373 11.842  16.318   1.00 56.31  ? 391  LYS   B CA  1 
ATOM   4078  C  C   . LYS   B  1 90  ? -63.137 12.697  16.539   1.00 52.31  ? 391  LYS   B C   1 
ATOM   4079  O  O   . LYS   B  1 90  ? -63.233 13.846  16.994   1.00 48.21  ? 391  LYS   B O   1 
ATOM   4080  C  CB  . LYS   B  1 90  ? -64.596 10.882  17.488   1.00 59.39  ? 391  LYS   B CB  1 
ATOM   4081  C  CG  . LYS   B  1 90  ? -64.084 11.376  18.827   1.00 69.80  ? 391  LYS   B CG  1 
ATOM   4082  C  CD  . LYS   B  1 90  ? -63.307 10.282  19.573   1.00 77.55  ? 391  LYS   B CD  1 
ATOM   4083  C  CE  . LYS   B  1 90  ? -61.788 10.419  19.384   1.00 74.76  ? 391  LYS   B CE  1 
ATOM   4084  N  NZ  . LYS   B  1 90  ? -61.201 11.563  20.153   1.00 76.17  ? 391  LYS   B NZ  1 
ATOM   4085  N  N   . GLU   B  1 91  ? -61.967 12.161  16.184   1.00 46.88  ? 392  GLU   B N   1 
ATOM   4086  C  CA  . GLU   B  1 91  ? -60.713 12.865  16.423   1.00 52.18  ? 392  GLU   B CA  1 
ATOM   4087  C  C   . GLU   B  1 91  ? -60.607 14.124  15.571   1.00 60.05  ? 392  GLU   B C   1 
ATOM   4088  O  O   . GLU   B  1 91  ? -60.178 15.176  16.059   1.00 57.20  ? 392  GLU   B O   1 
ATOM   4089  C  CB  . GLU   B  1 91  ? -59.542 11.929  16.155   1.00 46.58  ? 392  GLU   B CB  1 
ATOM   4090  C  CG  . GLU   B  1 91  ? -58.325 12.221  16.999   1.00 54.56  ? 392  GLU   B CG  1 
ATOM   4091  C  CD  . GLU   B  1 91  ? -57.341 11.082  16.978   1.00 61.59  ? 392  GLU   B CD  1 
ATOM   4092  O  OE1 . GLU   B  1 91  ? -56.145 11.334  17.233   1.00 64.38  ? 392  GLU   B OE1 1 
ATOM   4093  O  OE2 . GLU   B  1 91  ? -57.764 9.939   16.692   1.00 65.13  ? 392  GLU   B OE2 1 
ATOM   4094  N  N   . ILE   B  1 92  ? -60.993 14.042  14.295   1.00 64.66  ? 393  ILE   B N   1 
ATOM   4095  C  CA  . ILE   B  1 92  ? -60.936 15.225  13.443   1.00 62.71  ? 393  ILE   B CA  1 
ATOM   4096  C  C   . ILE   B  1 92  ? -61.961 16.250  13.902   1.00 60.89  ? 393  ILE   B C   1 
ATOM   4097  O  O   . ILE   B  1 92  ? -61.669 17.449  13.964   1.00 62.23  ? 393  ILE   B O   1 
ATOM   4098  C  CB  . ILE   B  1 92  ? -61.125 14.832  11.968   1.00 62.91  ? 393  ILE   B CB  1 
ATOM   4099  C  CG1 . ILE   B  1 92  ? -59.922 14.014  11.483   1.00 56.39  ? 393  ILE   B CG1 1 
ATOM   4100  C  CG2 . ILE   B  1 92  ? -61.304 16.066  11.101   1.00 66.03  ? 393  ILE   B CG2 1 
ATOM   4101  C  CD1 . ILE   B  1 92  ? -60.192 13.231  10.216   1.00 59.50  ? 393  ILE   B CD1 1 
ATOM   4102  N  N   . ASP   B  1 93  ? -63.164 15.789  14.261   1.00 66.37  ? 394  ASP   B N   1 
ATOM   4103  C  CA  . ASP   B  1 93  ? -64.173 16.655  14.870   1.00 67.21  ? 394  ASP   B CA  1 
ATOM   4104  C  C   . ASP   B  1 93  ? -63.621 17.450  16.049   1.00 76.33  ? 394  ASP   B C   1 
ATOM   4105  O  O   . ASP   B  1 93  ? -64.006 18.605  16.260   1.00 87.84  ? 394  ASP   B O   1 
ATOM   4106  C  CB  . ASP   B  1 93  ? -65.369 15.822  15.337   1.00 70.28  ? 394  ASP   B CB  1 
ATOM   4107  C  CG  . ASP   B  1 93  ? -66.342 15.525  14.228   1.00 79.39  ? 394  ASP   B CG  1 
ATOM   4108  O  OD1 . ASP   B  1 93  ? -66.389 16.312  13.262   1.00 85.71  ? 394  ASP   B OD1 1 
ATOM   4109  O  OD2 . ASP   B  1 93  ? -67.066 14.512  14.321   1.00 81.37  ? 394  ASP   B OD2 1 
ATOM   4110  N  N   . THR   B  1 94  ? -62.720 16.856  16.833   1.00 66.48  ? 395  THR   B N   1 
ATOM   4111  C  CA  . THR   B  1 94  ? -62.295 17.463  18.085   1.00 66.71  ? 395  THR   B CA  1 
ATOM   4112  C  C   . THR   B  1 94  ? -60.879 18.036  18.065   1.00 71.64  ? 395  THR   B C   1 
ATOM   4113  O  O   . THR   B  1 94  ? -60.495 18.713  19.026   1.00 80.66  ? 395  THR   B O   1 
ATOM   4114  C  CB  . THR   B  1 94  ? -62.417 16.439  19.229   1.00 66.94  ? 395  THR   B CB  1 
ATOM   4115  O  OG1 . THR   B  1 94  ? -61.746 15.229  18.860   1.00 72.77  ? 395  THR   B OG1 1 
ATOM   4116  C  CG2 . THR   B  1 94  ? -63.871 16.116  19.493   1.00 60.79  ? 395  THR   B CG2 1 
ATOM   4117  N  N   . THR   B  1 95  ? -60.087 17.780  17.022   1.00 64.95  ? 396  THR   B N   1 
ATOM   4118  C  CA  . THR   B  1 95  ? -58.756 18.381  16.917   1.00 57.83  ? 396  THR   B CA  1 
ATOM   4119  C  C   . THR   B  1 95  ? -58.395 18.865  15.516   1.00 58.95  ? 396  THR   B C   1 
ATOM   4120  O  O   . THR   B  1 95  ? -57.313 19.438  15.355   1.00 61.28  ? 396  THR   B O   1 
ATOM   4121  C  CB  . THR   B  1 95  ? -57.650 17.402  17.364   1.00 52.24  ? 396  THR   B CB  1 
ATOM   4122  O  OG1 . THR   B  1 95  ? -57.618 16.272  16.482   1.00 52.40  ? 396  THR   B OG1 1 
ATOM   4123  C  CG2 . THR   B  1 95  ? -57.845 16.923  18.793   1.00 43.51  ? 396  THR   B CG2 1 
ATOM   4124  N  N   . SER   B  1 96  ? -59.229 18.642  14.503   1.00 50.86  ? 397  SER   B N   1 
ATOM   4125  C  CA  . SER   B  1 96  ? -58.926 18.946  13.103   1.00 60.00  ? 397  SER   B CA  1 
ATOM   4126  C  C   . SER   B  1 96  ? -57.805 18.081  12.535   1.00 61.80  ? 397  SER   B C   1 
ATOM   4127  O  O   . SER   B  1 96  ? -57.277 18.393  11.454   1.00 67.11  ? 397  SER   B O   1 
ATOM   4128  C  CB  . SER   B  1 96  ? -58.573 20.424  12.886   1.00 61.08  ? 397  SER   B CB  1 
ATOM   4129  O  OG  . SER   B  1 96  ? -59.698 21.259  13.087   1.00 69.04  ? 397  SER   B OG  1 
ATOM   4130  N  N   . THR   B  1 97  ? -57.422 17.008  13.221   1.00 59.06  ? 398  THR   B N   1 
ATOM   4131  C  CA  . THR   B  1 97  ? -56.446 16.061  12.688   1.00 62.88  ? 398  THR   B CA  1 
ATOM   4132  C  C   . THR   B  1 97  ? -56.763 14.690  13.284   1.00 55.45  ? 398  THR   B C   1 
ATOM   4133  O  O   . THR   B  1 97  ? -57.825 14.495  13.883   1.00 51.93  ? 398  THR   B O   1 
ATOM   4134  C  CB  . THR   B  1 97  ? -55.018 16.552  12.975   1.00 57.90  ? 398  THR   B CB  1 
ATOM   4135  O  OG1 . THR   B  1 97  ? -54.084 15.830  12.174   1.00 53.18  ? 398  THR   B OG1 1 
ATOM   4136  C  CG2 . THR   B  1 97  ? -54.668 16.379  14.445   1.00 59.62  ? 398  THR   B CG2 1 
ATOM   4137  N  N   . TYR   B  1 98  ? -55.866 13.723  13.086   1.00 45.50  ? 399  TYR   B N   1 
ATOM   4138  C  CA  . TYR   B  1 98  ? -55.971 12.436  13.766   1.00 50.28  ? 399  TYR   B CA  1 
ATOM   4139  C  C   . TYR   B  1 98  ? -54.574 11.849  13.903   1.00 48.11  ? 399  TYR   B C   1 
ATOM   4140  O  O   . TYR   B  1 98  ? -53.606 12.373  13.349   1.00 45.50  ? 399  TYR   B O   1 
ATOM   4141  C  CB  . TYR   B  1 98  ? -56.923 11.479  13.037   1.00 51.25  ? 399  TYR   B CB  1 
ATOM   4142  C  CG  . TYR   B  1 98  ? -56.412 10.961  11.709   1.00 49.38  ? 399  TYR   B CG  1 
ATOM   4143  C  CD1 . TYR   B  1 98  ? -56.442 11.762  10.570   1.00 47.94  ? 399  TYR   B CD1 1 
ATOM   4144  C  CD2 . TYR   B  1 98  ? -55.928 9.658   11.587   1.00 49.72  ? 399  TYR   B CD2 1 
ATOM   4145  C  CE1 . TYR   B  1 98  ? -55.979 11.288  9.348    1.00 53.08  ? 399  TYR   B CE1 1 
ATOM   4146  C  CE2 . TYR   B  1 98  ? -55.469 9.177   10.376   1.00 46.73  ? 399  TYR   B CE2 1 
ATOM   4147  C  CZ  . TYR   B  1 98  ? -55.495 9.996   9.258    1.00 54.56  ? 399  TYR   B CZ  1 
ATOM   4148  O  OH  . TYR   B  1 98  ? -55.037 9.520   8.045    1.00 56.55  ? 399  TYR   B OH  1 
ATOM   4149  N  N   . GLN   B  1 99  ? -54.462 10.763  14.670   1.00 48.11  ? 400  GLN   B N   1 
ATOM   4150  C  CA  . GLN   B  1 99  ? -53.169 10.149  14.955   1.00 42.79  ? 400  GLN   B CA  1 
ATOM   4151  C  C   . GLN   B  1 99  ? -53.150 8.706   14.479   1.00 47.02  ? 400  GLN   B C   1 
ATOM   4152  O  O   . GLN   B  1 99  ? -54.124 7.969   14.657   1.00 54.64  ? 400  GLN   B O   1 
ATOM   4153  C  CB  . GLN   B  1 99  ? -52.835 10.204  16.455   1.00 39.31  ? 400  GLN   B CB  1 
ATOM   4154  C  CG  . GLN   B  1 99  ? -52.853 11.606  17.029   1.00 38.60  ? 400  GLN   B CG  1 
ATOM   4155  C  CD  . GLN   B  1 99  ? -51.760 12.477  16.452   1.00 50.02  ? 400  GLN   B CD  1 
ATOM   4156  O  OE1 . GLN   B  1 99  ? -50.628 12.033  16.256   1.00 55.08  ? 400  GLN   B OE1 1 
ATOM   4157  N  NE2 . GLN   B  1 99  ? -52.096 13.725  16.164   1.00 56.71  ? 400  GLN   B NE2 1 
ATOM   4158  N  N   . LEU   B  1 100 ? -52.035 8.306   13.876   1.00 49.91  ? 401  LEU   B N   1 
ATOM   4159  C  CA  . LEU   B  1 100 ? -51.916 6.965   13.322   1.00 48.65  ? 401  LEU   B CA  1 
ATOM   4160  C  C   . LEU   B  1 100 ? -51.534 5.990   14.419   1.00 45.80  ? 401  LEU   B C   1 
ATOM   4161  O  O   . LEU   B  1 100 ? -50.690 6.297   15.261   1.00 39.28  ? 401  LEU   B O   1 
ATOM   4162  C  CB  . LEU   B  1 100 ? -50.864 6.924   12.206   1.00 34.96  ? 401  LEU   B CB  1 
ATOM   4163  C  CG  . LEU   B  1 100 ? -51.164 7.749   10.964   1.00 39.99  ? 401  LEU   B CG  1 
ATOM   4164  C  CD1 . LEU   B  1 100 ? -50.056 7.596   9.950    1.00 38.87  ? 401  LEU   B CD1 1 
ATOM   4165  C  CD2 . LEU   B  1 100 ? -52.491 7.327   10.358   1.00 42.63  ? 401  LEU   B CD2 1 
ATOM   4166  N  N   . LYS   B  1 101 ? -52.159 4.815   14.405   1.00 42.48  ? 402  LYS   B N   1 
ATOM   4167  C  CA  . LYS   B  1 101 ? -51.665 3.710   15.208   1.00 44.62  ? 402  LYS   B CA  1 
ATOM   4168  C  C   . LYS   B  1 101 ? -50.260 3.324   14.759   1.00 43.77  ? 402  LYS   B C   1 
ATOM   4169  O  O   . LYS   B  1 101 ? -49.847 3.594   13.638   1.00 42.32  ? 402  LYS   B O   1 
ATOM   4170  C  CB  . LYS   B  1 101 ? -52.587 2.497   15.096   1.00 44.44  ? 402  LYS   B CB  1 
ATOM   4171  C  CG  . LYS   B  1 101 ? -54.001 2.734   15.560   1.00 51.71  ? 402  LYS   B CG  1 
ATOM   4172  C  CD  . LYS   B  1 101 ? -54.063 3.233   17.002   1.00 53.94  ? 402  LYS   B CD  1 
ATOM   4173  C  CE  . LYS   B  1 101 ? -55.502 3.210   17.522   1.00 64.65  ? 402  LYS   B CE  1 
ATOM   4174  N  NZ  . LYS   B  1 101 ? -55.696 4.027   18.766   1.00 72.09  ? 402  LYS   B NZ  1 
ATOM   4175  N  N   . ASP   B  1 102 ? -49.530 2.674   15.664   1.00 52.13  ? 403  ASP   B N   1 
ATOM   4176  C  CA  . ASP   B  1 102 ? -48.183 2.201   15.363   1.00 46.36  ? 403  ASP   B CA  1 
ATOM   4177  C  C   . ASP   B  1 102 ? -48.153 1.359   14.099   1.00 40.83  ? 403  ASP   B C   1 
ATOM   4178  O  O   . ASP   B  1 102 ? -47.285 1.542   13.237   1.00 42.49  ? 403  ASP   B O   1 
ATOM   4179  C  CB  . ASP   B  1 102 ? -47.647 1.382   16.536   1.00 57.25  ? 403  ASP   B CB  1 
ATOM   4180  C  CG  . ASP   B  1 102 ? -47.170 2.245   17.684   1.00 66.64  ? 403  ASP   B CG  1 
ATOM   4181  O  OD1 . ASP   B  1 102 ? -47.219 3.486   17.559   1.00 70.02  ? 403  ASP   B OD1 1 
ATOM   4182  O  OD2 . ASP   B  1 102 ? -46.735 1.678   18.709   1.00 72.26  ? 403  ASP   B OD2 1 
ATOM   4183  N  N   . THR   B  1 103 ? -49.072 0.398   13.992   1.00 43.60  ? 404  THR   B N   1 
ATOM   4184  C  CA  . THR   B  1 103 ? -49.093 -0.474  12.820   1.00 50.29  ? 404  THR   B CA  1 
ATOM   4185  C  C   . THR   B  1 103 ? -49.387 0.321   11.545   1.00 48.46  ? 404  THR   B C   1 
ATOM   4186  O  O   . THR   B  1 103 ? -48.799 0.063   10.492   1.00 45.42  ? 404  THR   B O   1 
ATOM   4187  C  CB  . THR   B  1 103 ? -50.126 -1.589  13.013   1.00 49.73  ? 404  THR   B CB  1 
ATOM   4188  O  OG1 . THR   B  1 103 ? -51.411 -1.026  13.312   1.00 52.21  ? 404  THR   B OG1 1 
ATOM   4189  C  CG2 . THR   B  1 103 ? -49.717 -2.493  14.137   1.00 53.92  ? 404  THR   B CG2 1 
ATOM   4190  N  N   . GLU   B  1 104 ? -50.290 1.296   11.630   1.00 46.88  ? 405  GLU   B N   1 
ATOM   4191  C  CA  . GLU   B  1 104 ? -50.614 2.115   10.475   1.00 43.77  ? 405  GLU   B CA  1 
ATOM   4192  C  C   . GLU   B  1 104 ? -49.410 2.928   10.033   1.00 49.89  ? 405  GLU   B C   1 
ATOM   4193  O  O   . GLU   B  1 104 ? -49.167 3.085   8.831    1.00 40.62  ? 405  GLU   B O   1 
ATOM   4194  C  CB  . GLU   B  1 104 ? -51.794 3.029   10.812   1.00 43.12  ? 405  GLU   B CB  1 
ATOM   4195  C  CG  . GLU   B  1 104 ? -53.032 2.270   11.263   1.00 45.58  ? 405  GLU   B CG  1 
ATOM   4196  C  CD  . GLU   B  1 104 ? -54.094 3.160   11.877   1.00 47.16  ? 405  GLU   B CD  1 
ATOM   4197  O  OE1 . GLU   B  1 104 ? -55.209 2.657   12.118   1.00 48.04  ? 405  GLU   B OE1 1 
ATOM   4198  O  OE2 . GLU   B  1 104 ? -53.817 4.355   12.125   1.00 46.84  ? 405  GLU   B OE2 1 
ATOM   4199  N  N   . LEU   B  1 105 ? -48.648 3.459   10.995   1.00 46.04  ? 406  LEU   B N   1 
ATOM   4200  C  CA  . LEU   B  1 105 ? -47.455 4.219   10.647   1.00 39.12  ? 406  LEU   B CA  1 
ATOM   4201  C  C   . LEU   B  1 105 ? -46.442 3.343   9.925    1.00 46.87  ? 406  LEU   B C   1 
ATOM   4202  O  O   . LEU   B  1 105 ? -45.806 3.783   8.957    1.00 39.25  ? 406  LEU   B O   1 
ATOM   4203  C  CB  . LEU   B  1 105 ? -46.822 4.828   11.895   1.00 44.15  ? 406  LEU   B CB  1 
ATOM   4204  C  CG  . LEU   B  1 105 ? -45.670 5.805   11.658   1.00 46.30  ? 406  LEU   B CG  1 
ATOM   4205  C  CD1 . LEU   B  1 105 ? -46.175 7.178   11.222   1.00 49.80  ? 406  LEU   B CD1 1 
ATOM   4206  C  CD2 . LEU   B  1 105 ? -44.804 5.922   12.905   1.00 34.85  ? 406  LEU   B CD2 1 
ATOM   4207  N  N   . ILE   B  1 106 ? -46.271 2.103   10.381   1.00 29.64  ? 407  ILE   B N   1 
ATOM   4208  C  CA  . ILE   B  1 106 ? -45.280 1.232   9.770    1.00 41.82  ? 407  ILE   B CA  1 
ATOM   4209  C  C   . ILE   B  1 106 ? -45.720 0.845   8.363    1.00 44.74  ? 407  ILE   B C   1 
ATOM   4210  O  O   . ILE   B  1 106 ? -44.929 0.886   7.417    1.00 48.01  ? 407  ILE   B O   1 
ATOM   4211  C  CB  . ILE   B  1 106 ? -45.043 0.001   10.654   1.00 37.60  ? 407  ILE   B CB  1 
ATOM   4212  C  CG1 . ILE   B  1 106 ? -44.243 0.416   11.885   1.00 34.92  ? 407  ILE   B CG1 1 
ATOM   4213  C  CG2 . ILE   B  1 106 ? -44.325 -1.101  9.883    1.00 35.01  ? 407  ILE   B CG2 1 
ATOM   4214  C  CD1 . ILE   B  1 106 ? -44.556 -0.424  13.081   1.00 38.18  ? 407  ILE   B CD1 1 
ATOM   4215  N  N   . TYR   B  1 107 ? -46.994 0.469   8.220    1.00 41.09  ? 408  TYR   B N   1 
ATOM   4216  C  CA  . TYR   B  1 107 ? -47.564 0.128   6.927    1.00 48.14  ? 408  TYR   B CA  1 
ATOM   4217  C  C   . TYR   B  1 107 ? -47.397 1.262   5.931    1.00 44.22  ? 408  TYR   B C   1 
ATOM   4218  O  O   . TYR   B  1 107 ? -47.109 1.030   4.748    1.00 37.36  ? 408  TYR   B O   1 
ATOM   4219  C  CB  . TYR   B  1 107 ? -49.045 -0.209  7.096    1.00 49.54  ? 408  TYR   B CB  1 
ATOM   4220  C  CG  . TYR   B  1 107 ? -49.784 -0.342  5.796    1.00 54.74  ? 408  TYR   B CG  1 
ATOM   4221  C  CD1 . TYR   B  1 107 ? -49.688 -1.505  5.036    1.00 59.09  ? 408  TYR   B CD1 1 
ATOM   4222  C  CD2 . TYR   B  1 107 ? -50.570 0.699   5.314    1.00 57.24  ? 408  TYR   B CD2 1 
ATOM   4223  C  CE1 . TYR   B  1 107 ? -50.364 -1.631  3.829    1.00 58.11  ? 408  TYR   B CE1 1 
ATOM   4224  C  CE2 . TYR   B  1 107 ? -51.245 0.588   4.116    1.00 52.75  ? 408  TYR   B CE2 1 
ATOM   4225  C  CZ  . TYR   B  1 107 ? -51.145 -0.580  3.375    1.00 59.58  ? 408  TYR   B CZ  1 
ATOM   4226  O  OH  . TYR   B  1 107 ? -51.829 -0.693  2.176    1.00 64.63  ? 408  TYR   B OH  1 
ATOM   4227  N  N   . GLY   B  1 108 ? -47.584 2.493   6.396    1.00 42.48  ? 409  GLY   B N   1 
ATOM   4228  C  CA  . GLY   B  1 108 ? -47.590 3.647   5.526    1.00 37.17  ? 409  GLY   B CA  1 
ATOM   4229  C  C   . GLY   B  1 108 ? -46.201 4.053   5.081    1.00 46.09  ? 409  GLY   B C   1 
ATOM   4230  O  O   . GLY   B  1 108 ? -46.005 4.426   3.917    1.00 43.06  ? 409  GLY   B O   1 
ATOM   4231  N  N   . ALA   B  1 109 ? -45.229 3.999   5.995    1.00 40.33  ? 410  ALA   B N   1 
ATOM   4232  C  CA  . ALA   B  1 109 ? -43.868 4.328   5.606    1.00 41.99  ? 410  ALA   B CA  1 
ATOM   4233  C  C   . ALA   B  1 109 ? -43.343 3.308   4.610    1.00 35.58  ? 410  ALA   B C   1 
ATOM   4234  O  O   . ALA   B  1 109 ? -42.696 3.670   3.626    1.00 35.58  ? 410  ALA   B O   1 
ATOM   4235  C  CB  . ALA   B  1 109 ? -42.967 4.406   6.838    1.00 34.67  ? 410  ALA   B CB  1 
ATOM   4236  N  N   . LYS   B  1 110 ? -43.607 2.028   4.856    1.00 32.71  ? 411  LYS   B N   1 
ATOM   4237  C  CA  . LYS   B  1 110 ? -43.129 1.000   3.947    1.00 37.64  ? 411  LYS   B CA  1 
ATOM   4238  C  C   . LYS   B  1 110 ? -43.801 1.127   2.588    1.00 42.00  ? 411  LYS   B C   1 
ATOM   4239  O  O   . LYS   B  1 110 ? -43.165 0.899   1.554    1.00 37.91  ? 411  LYS   B O   1 
ATOM   4240  C  CB  . LYS   B  1 110 ? -43.375 -0.385  4.545    1.00 35.01  ? 411  LYS   B CB  1 
ATOM   4241  C  CG  . LYS   B  1 110 ? -42.343 -0.808  5.563    1.00 39.41  ? 411  LYS   B CG  1 
ATOM   4242  C  CD  . LYS   B  1 110 ? -42.759 -2.107  6.252    1.00 37.63  ? 411  LYS   B CD  1 
ATOM   4243  C  CE  . LYS   B  1 110 ? -41.753 -2.500  7.323    1.00 35.57  ? 411  LYS   B CE  1 
ATOM   4244  N  NZ  . LYS   B  1 110 ? -41.961 -3.879  7.784    1.00 34.31  ? 411  LYS   B NZ  1 
ATOM   4245  N  N   . HIS   B  1 111 ? -45.071 1.525   2.563    1.00 45.50  ? 412  HIS   B N   1 
ATOM   4246  C  CA  . HIS   B  1 111 ? -45.737 1.634   1.272    1.00 39.56  ? 412  HIS   B CA  1 
ATOM   4247  C  C   . HIS   B  1 111 ? -45.365 2.916   0.542    1.00 47.45  ? 412  HIS   B C   1 
ATOM   4248  O  O   . HIS   B  1 111 ? -45.373 2.941   -0.700   1.00 44.92  ? 412  HIS   B O   1 
ATOM   4249  C  CB  . HIS   B  1 111 ? -47.252 1.503   1.438    1.00 30.78  ? 412  HIS   B CB  1 
ATOM   4250  C  CG  . HIS   B  1 111 ? -47.706 0.078   1.435    1.00 42.05  ? 412  HIS   B CG  1 
ATOM   4251  N  ND1 . HIS   B  1 111 ? -48.579 -0.427  0.496    1.00 50.23  ? 412  HIS   B ND1 1 
ATOM   4252  C  CD2 . HIS   B  1 111 ? -47.350 -0.969  2.217    1.00 43.78  ? 412  HIS   B CD2 1 
ATOM   4253  C  CE1 . HIS   B  1 111 ? -48.763 -1.717  0.717    1.00 51.40  ? 412  HIS   B CE1 1 
ATOM   4254  N  NE2 . HIS   B  1 111 ? -48.022 -2.072  1.751    1.00 45.68  ? 412  HIS   B NE2 1 
ATOM   4255  N  N   . ALA   B  1 112 ? -45.012 3.972   1.275    1.00 40.74  ? 413  ALA   B N   1 
ATOM   4256  C  CA  . ALA   B  1 112 ? -44.470 5.154   0.624    1.00 40.81  ? 413  ALA   B CA  1 
ATOM   4257  C  C   . ALA   B  1 112 ? -43.213 4.802   -0.162   1.00 41.97  ? 413  ALA   B C   1 
ATOM   4258  O  O   . ALA   B  1 112 ? -43.080 5.175   -1.331   1.00 33.38  ? 413  ALA   B O   1 
ATOM   4259  C  CB  . ALA   B  1 112 ? -44.174 6.230   1.655    1.00 38.33  ? 413  ALA   B CB  1 
ATOM   4260  N  N   . TRP   B  1 113 ? -42.286 4.066   0.472    1.00 33.91  ? 414  TRP   B N   1 
ATOM   4261  C  CA  . TRP   B  1 113 ? -41.080 3.607   -0.211   1.00 32.39  ? 414  TRP   B CA  1 
ATOM   4262  C  C   . TRP   B  1 113 ? -41.422 2.686   -1.383   1.00 37.68  ? 414  TRP   B C   1 
ATOM   4263  O  O   . TRP   B  1 113 ? -40.823 2.781   -2.457   1.00 40.26  ? 414  TRP   B O   1 
ATOM   4264  C  CB  . TRP   B  1 113 ? -40.162 2.885   0.778    1.00 30.14  ? 414  TRP   B CB  1 
ATOM   4265  C  CG  . TRP   B  1 113 ? -38.845 2.412   0.197    1.00 33.57  ? 414  TRP   B CG  1 
ATOM   4266  C  CD1 . TRP   B  1 113 ? -38.316 2.732   -1.026   1.00 32.52  ? 414  TRP   B CD1 1 
ATOM   4267  C  CD2 . TRP   B  1 113 ? -37.895 1.528   0.823    1.00 37.17  ? 414  TRP   B CD2 1 
ATOM   4268  N  NE1 . TRP   B  1 113 ? -37.107 2.103   -1.195   1.00 33.71  ? 414  TRP   B NE1 1 
ATOM   4269  C  CE2 . TRP   B  1 113 ? -36.830 1.358   -0.073   1.00 34.73  ? 414  TRP   B CE2 1 
ATOM   4270  C  CE3 . TRP   B  1 113 ? -37.850 0.865   2.051    1.00 34.95  ? 414  TRP   B CE3 1 
ATOM   4271  C  CZ2 . TRP   B  1 113 ? -35.727 0.553   0.228    1.00 40.76  ? 414  TRP   B CZ2 1 
ATOM   4272  C  CZ3 . TRP   B  1 113 ? -36.755 0.064   2.345    1.00 29.59  ? 414  TRP   B CZ3 1 
ATOM   4273  C  CH2 . TRP   B  1 113 ? -35.707 -0.073  1.451    1.00 33.89  ? 414  TRP   B CH2 1 
ATOM   4274  N  N   . ARG   B  1 114 ? -42.365 1.773   -1.180   1.00 34.17  ? 415  ARG   B N   1 
ATOM   4275  C  CA  . ARG   B  1 114 ? -42.760 0.861   -2.237   1.00 38.33  ? 415  ARG   B CA  1 
ATOM   4276  C  C   . ARG   B  1 114 ? -43.316 1.613   -3.446   1.00 44.36  ? 415  ARG   B C   1 
ATOM   4277  O  O   . ARG   B  1 114 ? -43.138 1.176   -4.593   1.00 45.85  ? 415  ARG   B O   1 
ATOM   4278  C  CB  . ARG   B  1 114 ? -43.784 -0.116  -1.668   1.00 34.13  ? 415  ARG   B CB  1 
ATOM   4279  C  CG  . ARG   B  1 114 ? -44.173 -1.204  -2.606   1.00 33.51  ? 415  ARG   B CG  1 
ATOM   4280  C  CD  . ARG   B  1 114 ? -45.407 -1.885  -2.118   1.00 38.10  ? 415  ARG   B CD  1 
ATOM   4281  N  NE  . ARG   B  1 114 ? -45.576 -3.148  -2.804   1.00 44.39  ? 415  ARG   B NE  1 
ATOM   4282  C  CZ  . ARG   B  1 114 ? -46.509 -4.037  -2.509   1.00 44.92  ? 415  ARG   B CZ  1 
ATOM   4283  N  NH1 . ARG   B  1 114 ? -46.560 -5.161  -3.206   1.00 31.90  ? 415  ARG   B NH1 1 
ATOM   4284  N  NH2 . ARG   B  1 114 ? -47.372 -3.806  -1.516   1.00 41.86  ? 415  ARG   B NH2 1 
ATOM   4285  N  N   . ASN   B  1 115 ? -43.949 2.759   -3.210   1.00 37.82  ? 416  ASN   B N   1 
ATOM   4286  C  CA  . ASN   B  1 115 ? -44.593 3.553   -4.243   1.00 40.18  ? 416  ASN   B CA  1 
ATOM   4287  C  C   . ASN   B  1 115 ? -43.656 4.554   -4.912   1.00 35.93  ? 416  ASN   B C   1 
ATOM   4288  O  O   . ASN   B  1 115 ? -44.102 5.286   -5.798   1.00 39.16  ? 416  ASN   B O   1 
ATOM   4289  C  CB  . ASN   B  1 115 ? -45.795 4.301   -3.650   1.00 33.81  ? 416  ASN   B CB  1 
ATOM   4290  C  CG  . ASN   B  1 115 ? -46.909 3.371   -3.216   1.00 39.65  ? 416  ASN   B CG  1 
ATOM   4291  O  OD1 . ASN   B  1 115 ? -46.939 2.204   -3.595   1.00 41.01  ? 416  ASN   B OD1 1 
ATOM   4292  N  ND2 . ASN   B  1 115 ? -47.839 3.890   -2.401   1.00 34.12  ? 416  ASN   B ND2 1 
ATOM   4293  N  N   . ALA   B  1 116 ? -42.382 4.612   -4.513   1.00 35.63  ? 417  ALA   B N   1 
ATOM   4294  C  CA  . ALA   B  1 116 ? -41.495 5.695   -4.942   1.00 37.97  ? 417  ALA   B CA  1 
ATOM   4295  C  C   . ALA   B  1 116 ? -40.988 5.377   -6.352   1.00 35.34  ? 417  ALA   B C   1 
ATOM   4296  O  O   . ALA   B  1 116 ? -39.993 4.671   -6.555   1.00 30.36  ? 417  ALA   B O   1 
ATOM   4297  C  CB  . ALA   B  1 116 ? -40.358 5.900   -3.946   1.00 34.25  ? 417  ALA   B CB  1 
ATOM   4298  N  N   . SER   B  1 117 ? -41.684 5.943   -7.336   1.00 33.54  ? 418  SER   B N   1 
ATOM   4299  C  CA  A SER   B  1 117 ? -41.449 5.559   -8.726   0.59 36.12  ? 418  SER   B CA  1 
ATOM   4300  C  CA  B SER   B  1 117 ? -41.451 5.575   -8.732   0.41 35.75  ? 418  SER   B CA  1 
ATOM   4301  C  C   . SER   B  1 117 ? -40.001 5.773   -9.143   1.00 36.64  ? 418  SER   B C   1 
ATOM   4302  O  O   . SER   B  1 117 ? -39.504 5.052   -10.012  1.00 41.23  ? 418  SER   B O   1 
ATOM   4303  C  CB  A SER   B  1 117 ? -42.388 6.341   -9.640   0.59 31.72  ? 418  SER   B CB  1 
ATOM   4304  C  CB  B SER   B  1 117 ? -42.365 6.393   -9.640   0.41 32.11  ? 418  SER   B CB  1 
ATOM   4305  O  OG  A SER   B  1 117 ? -42.164 7.733   -9.531   0.59 33.62  ? 418  SER   B OG  1 
ATOM   4306  O  OG  B SER   B  1 117 ? -43.695 5.917   -9.575   0.41 33.85  ? 418  SER   B OG  1 
ATOM   4307  N  N   . ARG   B  1 118 ? -39.309 6.736   -8.522   1.00 32.07  ? 419  ARG   B N   1 
ATOM   4308  C  CA  . ARG   B  1 118 ? -37.938 7.059   -8.883   1.00 34.23  ? 419  ARG   B CA  1 
ATOM   4309  C  C   . ARG   B  1 118 ? -36.886 6.175   -8.226   1.00 34.61  ? 419  ARG   B C   1 
ATOM   4310  O  O   . ARG   B  1 118 ? -35.709 6.320   -8.565   1.00 26.58  ? 419  ARG   B O   1 
ATOM   4311  C  CB  . ARG   B  1 118 ? -37.660 8.540   -8.575   1.00 28.96  ? 419  ARG   B CB  1 
ATOM   4312  C  CG  . ARG   B  1 118 ? -38.525 9.469   -9.428   1.00 33.50  ? 419  ARG   B CG  1 
ATOM   4313  C  CD  . ARG   B  1 118 ? -38.241 10.945  -9.257   1.00 35.24  ? 419  ARG   B CD  1 
ATOM   4314  N  NE  . ARG   B  1 118 ? -38.990 11.697  -10.266  1.00 40.87  ? 419  ARG   B NE  1 
ATOM   4315  C  CZ  . ARG   B  1 118 ? -39.031 13.024  -10.364  1.00 49.18  ? 419  ARG   B CZ  1 
ATOM   4316  N  NH1 . ARG   B  1 118 ? -38.369 13.778  -9.502   1.00 55.23  ? 419  ARG   B NH1 1 
ATOM   4317  N  NH2 . ARG   B  1 118 ? -39.746 13.602  -11.328  1.00 47.20  ? 419  ARG   B NH2 1 
ATOM   4318  N  N   . CYS   B  1 119 ? -37.257 5.254   -7.332   1.00 37.84  ? 420  CYS   B N   1 
ATOM   4319  C  CA  . CYS   B  1 119 ? -36.283 4.540   -6.509   1.00 30.26  ? 420  CYS   B CA  1 
ATOM   4320  C  C   . CYS   B  1 119 ? -35.989 3.170   -7.106   1.00 26.39  ? 420  CYS   B C   1 
ATOM   4321  O  O   . CYS   B  1 119 ? -36.880 2.319   -7.195   1.00 30.43  ? 420  CYS   B O   1 
ATOM   4322  C  CB  . CYS   B  1 119 ? -36.776 4.390   -5.065   1.00 36.76  ? 420  CYS   B CB  1 
ATOM   4323  S  SG  . CYS   B  1 119 ? -35.651 3.409   -4.030   1.00 34.12  ? 420  CYS   B SG  1 
ATOM   4324  N  N   . VAL   B  1 120 ? -34.723 2.941   -7.459   1.00 31.24  ? 421  VAL   B N   1 
ATOM   4325  C  CA  . VAL   B  1 120 ? -34.303 1.645   -7.993   1.00 33.62  ? 421  VAL   B CA  1 
ATOM   4326  C  C   . VAL   B  1 120 ? -34.125 0.598   -6.909   1.00 39.39  ? 421  VAL   B C   1 
ATOM   4327  O  O   . VAL   B  1 120 ? -34.053 -0.600  -7.227   1.00 31.58  ? 421  VAL   B O   1 
ATOM   4328  C  CB  . VAL   B  1 120 ? -32.992 1.786   -8.796   1.00 31.56  ? 421  VAL   B CB  1 
ATOM   4329  C  CG1 . VAL   B  1 120 ? -31.832 2.211   -7.879   1.00 28.54  ? 421  VAL   B CG1 1 
ATOM   4330  C  CG2 . VAL   B  1 120 ? -32.656 0.515   -9.534   1.00 34.80  ? 421  VAL   B CG2 1 
ATOM   4331  N  N   . GLY   B  1 121 ? -34.090 1.009   -5.632   1.00 36.19  ? 422  GLY   B N   1 
ATOM   4332  C  CA  . GLY   B  1 121 ? -33.787 0.142   -4.520   1.00 31.65  ? 422  GLY   B CA  1 
ATOM   4333  C  C   . GLY   B  1 121 ? -34.947 -0.616  -3.917   1.00 39.49  ? 422  GLY   B C   1 
ATOM   4334  O  O   . GLY   B  1 121 ? -34.728 -1.386  -2.980   1.00 35.71  ? 422  GLY   B O   1 
ATOM   4335  N  N   . ARG   B  1 122 ? -36.167 -0.462  -4.443   1.00 43.94  ? 423  ARG   B N   1 
ATOM   4336  C  CA  . ARG   B  1 122 ? -37.389 -0.882  -3.758   1.00 39.78  ? 423  ARG   B CA  1 
ATOM   4337  C  C   . ARG   B  1 122 ? -37.555 -2.390  -3.605   1.00 39.77  ? 423  ARG   B C   1 
ATOM   4338  O  O   . ARG   B  1 122 ? -38.568 -2.801  -3.028   1.00 42.79  ? 423  ARG   B O   1 
ATOM   4339  C  CB  . ARG   B  1 122 ? -38.617 -0.333  -4.476   1.00 35.65  ? 423  ARG   B CB  1 
ATOM   4340  C  CG  . ARG   B  1 122 ? -38.745 1.164   -4.440   1.00 25.46  ? 423  ARG   B CG  1 
ATOM   4341  C  CD  . ARG   B  1 122 ? -39.958 1.611   -5.242   1.00 50.35  ? 423  ARG   B CD  1 
ATOM   4342  N  NE  . ARG   B  1 122 ? -39.685 1.730   -6.680   1.00 45.13  ? 423  ARG   B NE  1 
ATOM   4343  C  CZ  . ARG   B  1 122 ? -40.629 1.803   -7.617   1.00 50.43  ? 423  ARG   B CZ  1 
ATOM   4344  N  NH1 . ARG   B  1 122 ? -41.919 1.735   -7.276   1.00 26.23  ? 423  ARG   B NH1 1 
ATOM   4345  N  NH2 . ARG   B  1 122 ? -40.287 1.937   -8.909   1.00 41.51  ? 423  ARG   B NH2 1 
ATOM   4346  N  N   . ILE   B  1 123 ? -36.625 -3.224  -4.079   1.00 37.52  ? 424  ILE   B N   1 
ATOM   4347  C  CA  . ILE   B  1 123 ? -36.731 -4.661  -3.829   1.00 37.20  ? 424  ILE   B CA  1 
ATOM   4348  C  C   . ILE   B  1 123 ? -36.828 -4.945  -2.322   1.00 43.47  ? 424  ILE   B C   1 
ATOM   4349  O  O   . ILE   B  1 123 ? -37.457 -5.930  -1.909   1.00 40.88  ? 424  ILE   B O   1 
ATOM   4350  C  CB  . ILE   B  1 123 ? -35.542 -5.397  -4.490   1.00 35.04  ? 424  ILE   B CB  1 
ATOM   4351  C  CG1 . ILE   B  1 123 ? -35.684 -6.918  -4.433   1.00 38.22  ? 424  ILE   B CG1 1 
ATOM   4352  C  CG2 . ILE   B  1 123 ? -34.236 -5.011  -3.848   1.00 39.44  ? 424  ILE   B CG2 1 
ATOM   4353  C  CD1 . ILE   B  1 123 ? -36.805 -7.489  -5.256   1.00 35.93  ? 424  ILE   B CD1 1 
ATOM   4354  N  N   . GLN   B  1 124 ? -36.269 -4.062  -1.487   1.00 46.12  ? 425  GLN   B N   1 
ATOM   4355  C  CA  . GLN   B  1 124 ? -36.216 -4.233  -0.037   1.00 52.74  ? 425  GLN   B CA  1 
ATOM   4356  C  C   . GLN   B  1 124 ? -37.327 -3.506  0.710    1.00 49.92  ? 425  GLN   B C   1 
ATOM   4357  O  O   . GLN   B  1 124 ? -37.242 -3.392  1.935    1.00 54.78  ? 425  GLN   B O   1 
ATOM   4358  C  CB  . GLN   B  1 124 ? -34.886 -3.721  0.505    1.00 57.18  ? 425  GLN   B CB  1 
ATOM   4359  C  CG  . GLN   B  1 124 ? -33.749 -3.760  -0.459   1.00 63.98  ? 425  GLN   B CG  1 
ATOM   4360  C  CD  . GLN   B  1 124 ? -32.885 -4.968  -0.228   1.00 72.97  ? 425  GLN   B CD  1 
ATOM   4361  O  OE1 . GLN   B  1 124 ? -33.014 -5.646  0.796    1.00 62.18  ? 425  GLN   B OE1 1 
ATOM   4362  N  NE2 . GLN   B  1 124 ? -31.993 -5.255  -1.181   1.00 85.88  ? 425  GLN   B NE2 1 
ATOM   4363  N  N   . TRP   B  1 125 ? -38.352 -3.008  0.011    1.00 41.21  ? 426  TRP   B N   1 
ATOM   4364  C  CA  . TRP   B  1 125 ? -39.262 -2.026  0.594    1.00 33.75  ? 426  TRP   B CA  1 
ATOM   4365  C  C   . TRP   B  1 125 ? -39.847 -2.490  1.928    1.00 44.26  ? 426  TRP   B C   1 
ATOM   4366  O  O   . TRP   B  1 125 ? -40.015 -1.685  2.847    1.00 50.62  ? 426  TRP   B O   1 
ATOM   4367  C  CB  . TRP   B  1 125 ? -40.396 -1.703  -0.384   1.00 41.04  ? 426  TRP   B CB  1 
ATOM   4368  C  CG  . TRP   B  1 125 ? -41.341 -2.844  -0.602   1.00 38.48  ? 426  TRP   B CG  1 
ATOM   4369  C  CD1 . TRP   B  1 125 ? -41.219 -3.831  -1.530   1.00 43.01  ? 426  TRP   B CD1 1 
ATOM   4370  C  CD2 . TRP   B  1 125 ? -42.562 -3.111  0.113    1.00 38.82  ? 426  TRP   B CD2 1 
ATOM   4371  N  NE1 . TRP   B  1 125 ? -42.279 -4.699  -1.437   1.00 47.10  ? 426  TRP   B NE1 1 
ATOM   4372  C  CE2 . TRP   B  1 125 ? -43.116 -4.282  -0.434   1.00 45.75  ? 426  TRP   B CE2 1 
ATOM   4373  C  CE3 . TRP   B  1 125 ? -43.234 -2.475  1.160    1.00 46.54  ? 426  TRP   B CE3 1 
ATOM   4374  C  CZ2 . TRP   B  1 125 ? -44.325 -4.829  0.025    1.00 37.33  ? 426  TRP   B CZ2 1 
ATOM   4375  C  CZ3 . TRP   B  1 125 ? -44.426 -3.029  1.625    1.00 50.16  ? 426  TRP   B CZ3 1 
ATOM   4376  C  CH2 . TRP   B  1 125 ? -44.956 -4.192  1.054    1.00 41.42  ? 426  TRP   B CH2 1 
ATOM   4377  N  N   . SER   B  1 126 ? -40.157 -3.779  2.054    1.00 38.48  ? 427  SER   B N   1 
ATOM   4378  C  CA  . SER   B  1 126 ? -40.847 -4.285  3.226    1.00 38.42  ? 427  SER   B CA  1 
ATOM   4379  C  C   . SER   B  1 126 ? -39.903 -4.615  4.383    1.00 45.56  ? 427  SER   B C   1 
ATOM   4380  O  O   . SER   B  1 126 ? -40.375 -5.041  5.449    1.00 43.11  ? 427  SER   B O   1 
ATOM   4381  C  CB  . SER   B  1 126 ? -41.645 -5.523  2.850    1.00 42.22  ? 427  SER   B CB  1 
ATOM   4382  O  OG  . SER   B  1 126 ? -40.798 -6.651  2.919    1.00 47.82  ? 427  SER   B OG  1 
ATOM   4383  N  N   . LYS   B  1 127 ? -38.594 -4.433  4.195    1.00 44.22  ? 428  LYS   B N   1 
ATOM   4384  C  CA  . LYS   B  1 127 ? -37.598 -4.679  5.228    1.00 52.91  ? 428  LYS   B CA  1 
ATOM   4385  C  C   . LYS   B  1 127 ? -37.045 -3.362  5.767    1.00 61.96  ? 428  LYS   B C   1 
ATOM   4386  O  O   . LYS   B  1 127 ? -35.839 -3.117  5.691    1.00 82.93  ? 428  LYS   B O   1 
ATOM   4387  C  CB  . LYS   B  1 127 ? -36.469 -5.536  4.661    1.00 58.72  ? 428  LYS   B CB  1 
ATOM   4388  C  CG  . LYS   B  1 127 ? -35.813 -6.412  5.684    1.00 75.18  ? 428  LYS   B CG  1 
ATOM   4389  C  CD  . LYS   B  1 127 ? -34.310 -6.213  5.732    1.00 83.79  ? 428  LYS   B CD  1 
ATOM   4390  C  CE  . LYS   B  1 127 ? -33.758 -6.774  7.040    1.00 86.58  ? 428  LYS   B CE  1 
ATOM   4391  N  NZ  . LYS   B  1 127 ? -32.329 -7.173  6.924    1.00 89.47  ? 428  LYS   B NZ  1 
ATOM   4392  N  N   . LEU   B  1 128 ? -37.909 -2.501  6.296    1.00 44.65  ? 429  LEU   B N   1 
ATOM   4393  C  CA  . LEU   B  1 128 ? -37.547 -1.137  6.660    1.00 40.93  ? 429  LEU   B CA  1 
ATOM   4394  C  C   . LEU   B  1 128 ? -37.713 -0.959  8.161    1.00 41.32  ? 429  LEU   B C   1 
ATOM   4395  O  O   . LEU   B  1 128 ? -38.750 -1.326  8.716    1.00 41.71  ? 429  LEU   B O   1 
ATOM   4396  C  CB  . LEU   B  1 128 ? -38.424 -0.122  5.932    1.00 26.80  ? 429  LEU   B CB  1 
ATOM   4397  C  CG  . LEU   B  1 128 ? -38.295 1.344   6.335    1.00 31.93  ? 429  LEU   B CG  1 
ATOM   4398  C  CD1 . LEU   B  1 128 ? -36.989 1.959   5.852    1.00 26.97  ? 429  LEU   B CD1 1 
ATOM   4399  C  CD2 . LEU   B  1 128 ? -39.487 2.142   5.817    1.00 32.16  ? 429  LEU   B CD2 1 
ATOM   4400  N  N   . GLN   B  1 129 ? -36.702 -0.404  8.814    1.00 39.92  ? 430  GLN   B N   1 
ATOM   4401  C  CA  . GLN   B  1 129 ? -36.814 -0.129  10.236   1.00 43.08  ? 430  GLN   B CA  1 
ATOM   4402  C  C   . GLN   B  1 129 ? -37.455 1.249   10.418   1.00 38.08  ? 430  GLN   B C   1 
ATOM   4403  O  O   . GLN   B  1 129 ? -37.029 2.229   9.794    1.00 47.18  ? 430  GLN   B O   1 
ATOM   4404  C  CB  . GLN   B  1 129 ? -35.443 -0.203  10.905   1.00 47.41  ? 430  GLN   B CB  1 
ATOM   4405  C  CG  . GLN   B  1 129 ? -35.499 -0.129  12.430   1.00 56.07  ? 430  GLN   B CG  1 
ATOM   4406  C  CD  . GLN   B  1 129 ? -36.361 -1.214  13.026   1.00 57.20  ? 430  GLN   B CD  1 
ATOM   4407  O  OE1 . GLN   B  1 129 ? -36.350 -2.358  12.572   1.00 55.85  ? 430  GLN   B OE1 1 
ATOM   4408  N  NE2 . GLN   B  1 129 ? -37.124 -0.858  14.046   1.00 66.65  ? 430  GLN   B NE2 1 
ATOM   4409  N  N   . VAL   B  1 130 ? -38.512 1.312   11.226   1.00 40.50  ? 431  VAL   B N   1 
ATOM   4410  C  CA  . VAL   B  1 130 ? -39.298 2.528   11.430   1.00 35.73  ? 431  VAL   B CA  1 
ATOM   4411  C  C   . VAL   B  1 130 ? -39.130 2.974   12.874   1.00 39.74  ? 431  VAL   B C   1 
ATOM   4412  O  O   . VAL   B  1 130 ? -39.512 2.252   13.800   1.00 41.08  ? 431  VAL   B O   1 
ATOM   4413  C  CB  . VAL   B  1 130 ? -40.785 2.308   11.112   1.00 36.85  ? 431  VAL   B CB  1 
ATOM   4414  C  CG1 . VAL   B  1 130 ? -41.562 3.597   11.354   1.00 27.58  ? 431  VAL   B CG1 1 
ATOM   4415  C  CG2 . VAL   B  1 130 ? -40.966 1.840   9.664    1.00 45.98  ? 431  VAL   B CG2 1 
ATOM   4416  N  N   . PHE   B  1 131 ? -38.599 4.172   13.065   1.00 43.25  ? 432  PHE   B N   1 
ATOM   4417  C  CA  . PHE   B  1 131 ? -38.442 4.772   14.383   1.00 34.16  ? 432  PHE   B CA  1 
ATOM   4418  C  C   . PHE   B  1 131 ? -39.513 5.835   14.552   1.00 42.45  ? 432  PHE   B C   1 
ATOM   4419  O  O   . PHE   B  1 131 ? -39.474 6.876   13.882   1.00 46.58  ? 432  PHE   B O   1 
ATOM   4420  C  CB  . PHE   B  1 131 ? -37.044 5.360   14.543   1.00 35.29  ? 432  PHE   B CB  1 
ATOM   4421  C  CG  . PHE   B  1 131 ? -35.972 4.329   14.502   1.00 36.14  ? 432  PHE   B CG  1 
ATOM   4422  C  CD1 . PHE   B  1 131 ? -35.977 3.276   15.412   1.00 28.48  ? 432  PHE   B CD1 1 
ATOM   4423  C  CD2 . PHE   B  1 131 ? -34.963 4.392   13.558   1.00 37.08  ? 432  PHE   B CD2 1 
ATOM   4424  C  CE1 . PHE   B  1 131 ? -34.995 2.292   15.361   1.00 33.33  ? 432  PHE   B CE1 1 
ATOM   4425  C  CE2 . PHE   B  1 131 ? -33.972 3.414   13.514   1.00 38.08  ? 432  PHE   B CE2 1 
ATOM   4426  C  CZ  . PHE   B  1 131 ? -33.984 2.366   14.411   1.00 34.59  ? 432  PHE   B CZ  1 
ATOM   4427  N  N   . ASP   B  1 132 ? -40.476 5.558   15.433   1.00 42.11  ? 433  ASP   B N   1 
ATOM   4428  C  CA  . ASP   B  1 132 ? -41.494 6.533   15.810   1.00 40.75  ? 433  ASP   B CA  1 
ATOM   4429  C  C   . ASP   B  1 132 ? -40.872 7.593   16.712   1.00 37.69  ? 433  ASP   B C   1 
ATOM   4430  O  O   . ASP   B  1 132 ? -40.452 7.296   17.828   1.00 40.26  ? 433  ASP   B O   1 
ATOM   4431  C  CB  . ASP   B  1 132 ? -42.654 5.839   16.513   1.00 31.43  ? 433  ASP   B CB  1 
ATOM   4432  C  CG  . ASP   B  1 132 ? -43.864 6.734   16.659   1.00 38.68  ? 433  ASP   B CG  1 
ATOM   4433  O  OD1 . ASP   B  1 132 ? -43.721 7.975   16.530   1.00 39.34  ? 433  ASP   B OD1 1 
ATOM   4434  O  OD2 . ASP   B  1 132 ? -44.965 6.201   16.901   1.00 43.76  ? 433  ASP   B OD2 1 
ATOM   4435  N  N   . ALA   B  1 133 ? -40.793 8.825   16.226   1.00 43.25  ? 434  ALA   B N   1 
ATOM   4436  C  CA  . ALA   B  1 133 ? -40.333 9.951   17.025   1.00 43.18  ? 434  ALA   B CA  1 
ATOM   4437  C  C   . ALA   B  1 133 ? -41.438 10.986  17.173   1.00 37.40  ? 434  ALA   B C   1 
ATOM   4438  O  O   . ALA   B  1 133 ? -41.168 12.179  17.306   1.00 31.58  ? 434  ALA   B O   1 
ATOM   4439  C  CB  . ALA   B  1 133 ? -39.090 10.589  16.403   1.00 28.75  ? 434  ALA   B CB  1 
ATOM   4440  N  N   . ARG   B  1 134 ? -42.691 10.543  17.126   1.00 29.87  ? 435  ARG   B N   1 
ATOM   4441  C  CA  . ARG   B  1 134 ? -43.797 11.484  17.155   1.00 41.36  ? 435  ARG   B CA  1 
ATOM   4442  C  C   . ARG   B  1 134 ? -44.013 12.102  18.529   1.00 47.40  ? 435  ARG   B C   1 
ATOM   4443  O  O   . ARG   B  1 134 ? -44.872 12.979  18.665   1.00 53.39  ? 435  ARG   B O   1 
ATOM   4444  C  CB  . ARG   B  1 134 ? -45.069 10.791  16.681   1.00 40.41  ? 435  ARG   B CB  1 
ATOM   4445  C  CG  . ARG   B  1 134 ? -45.145 10.647  15.178   1.00 43.64  ? 435  ARG   B CG  1 
ATOM   4446  C  CD  . ARG   B  1 134 ? -46.400 9.893   14.802   1.00 38.48  ? 435  ARG   B CD  1 
ATOM   4447  N  NE  . ARG   B  1 134 ? -46.427 8.587   15.451   1.00 36.03  ? 435  ARG   B NE  1 
ATOM   4448  C  CZ  . ARG   B  1 134 ? -47.494 7.803   15.492   1.00 32.59  ? 435  ARG   B CZ  1 
ATOM   4449  N  NH1 . ARG   B  1 134 ? -48.632 8.205   14.931   1.00 34.66  ? 435  ARG   B NH1 1 
ATOM   4450  N  NH2 . ARG   B  1 134 ? -47.428 6.621   16.092   1.00 32.33  ? 435  ARG   B NH2 1 
ATOM   4451  N  N   . ASP   B  1 135 ? -43.259 11.675  19.538   1.00 48.19  ? 436  ASP   B N   1 
ATOM   4452  C  CA  . ASP   B  1 135 ? -43.294 12.284  20.855   1.00 45.73  ? 436  ASP   B CA  1 
ATOM   4453  C  C   . ASP   B  1 135 ? -42.266 13.394  20.995   1.00 46.70  ? 436  ASP   B C   1 
ATOM   4454  O  O   . ASP   B  1 135 ? -42.203 14.025  22.056   1.00 39.95  ? 436  ASP   B O   1 
ATOM   4455  C  CB  . ASP   B  1 135 ? -43.071 11.218  21.933   1.00 42.69  ? 436  ASP   B CB  1 
ATOM   4456  C  CG  . ASP   B  1 135 ? -41.656 10.655  21.918   1.00 50.85  ? 436  ASP   B CG  1 
ATOM   4457  O  OD1 . ASP   B  1 135 ? -40.932 10.892  20.927   1.00 49.34  ? 436  ASP   B OD1 1 
ATOM   4458  O  OD2 . ASP   B  1 135 ? -41.264 9.976   22.891   1.00 47.73  ? 436  ASP   B OD2 1 
ATOM   4459  N  N   . CYS   B  1 136 ? -41.468 13.638  19.952   1.00 42.61  ? 437  CYS   B N   1 
ATOM   4460  C  CA  . CYS   B  1 136 ? -40.409 14.641  20.005   1.00 43.09  ? 437  CYS   B CA  1 
ATOM   4461  C  C   . CYS   B  1 136 ? -40.989 16.042  20.210   1.00 45.01  ? 437  CYS   B C   1 
ATOM   4462  O  O   . CYS   B  1 136 ? -42.059 16.366  19.688   1.00 46.19  ? 437  CYS   B O   1 
ATOM   4463  C  CB  . CYS   B  1 136 ? -39.593 14.587  18.715   1.00 40.75  ? 437  CYS   B CB  1 
ATOM   4464  S  SG  . CYS   B  1 136 ? -37.969 15.358  18.784   1.00 41.19  ? 437  CYS   B SG  1 
ATOM   4465  N  N   . THR   B  1 137 ? -40.289 16.878  20.999   1.00 38.77  ? 438  THR   B N   1 
ATOM   4466  C  CA  . THR   B  1 137 ? -40.724 18.261  21.186   1.00 39.94  ? 438  THR   B CA  1 
ATOM   4467  C  C   . THR   B  1 137 ? -39.676 19.335  20.892   1.00 34.81  ? 438  THR   B C   1 
ATOM   4468  O  O   . THR   B  1 137 ? -40.071 20.477  20.645   1.00 43.42  ? 438  THR   B O   1 
ATOM   4469  C  CB  . THR   B  1 137 ? -41.251 18.484  22.621   1.00 40.59  ? 438  THR   B CB  1 
ATOM   4470  O  OG1 . THR   B  1 137 ? -40.153 18.657  23.535   1.00 40.98  ? 438  THR   B OG1 1 
ATOM   4471  C  CG2 . THR   B  1 137 ? -42.117 17.313  23.077   1.00 37.80  ? 438  THR   B CG2 1 
ATOM   4472  N  N   . THR   B  1 138 ? -38.376 19.045  20.935   1.00 40.34  ? 439  THR   B N   1 
ATOM   4473  C  CA  . THR   B  1 138 ? -37.361 20.082  20.754   1.00 35.11  ? 439  THR   B CA  1 
ATOM   4474  C  C   . THR   B  1 138 ? -36.300 19.631  19.759   1.00 34.28  ? 439  THR   B C   1 
ATOM   4475  O  O   . THR   B  1 138 ? -36.164 18.444  19.454   1.00 43.04  ? 439  THR   B O   1 
ATOM   4476  C  CB  . THR   B  1 138 ? -36.634 20.446  22.059   1.00 40.66  ? 439  THR   B CB  1 
ATOM   4477  O  OG1 . THR   B  1 138 ? -35.724 19.383  22.390   1.00 43.55  ? 439  THR   B OG1 1 
ATOM   4478  C  CG2 . THR   B  1 138 ? -37.616 20.660  23.191   1.00 41.83  ? 439  THR   B CG2 1 
ATOM   4479  N  N   . ALA   B  1 139 ? -35.521 20.606  19.274   1.00 49.69  ? 440  ALA   B N   1 
ATOM   4480  C  CA  . ALA   B  1 139 ? -34.436 20.302  18.344   1.00 39.16  ? 440  ALA   B CA  1 
ATOM   4481  C  C   . ALA   B  1 139 ? -33.389 19.401  18.986   1.00 44.22  ? 440  ALA   B C   1 
ATOM   4482  O  O   . ALA   B  1 139 ? -32.780 18.571  18.292   1.00 41.76  ? 440  ALA   B O   1 
ATOM   4483  C  CB  . ALA   B  1 139 ? -33.798 21.593  17.823   1.00 35.16  ? 440  ALA   B CB  1 
ATOM   4484  N  N   . HIS   B  1 140 ? -33.170 19.538  20.305   1.00 45.68  ? 441  HIS   B N   1 
ATOM   4485  C  CA  . HIS   B  1 140 ? -32.311 18.595  21.028   1.00 43.11  ? 441  HIS   B CA  1 
ATOM   4486  C  C   . HIS   B  1 140 ? -32.857 17.176  20.935   1.00 38.74  ? 441  HIS   B C   1 
ATOM   4487  O  O   . HIS   B  1 140 ? -32.116 16.233  20.630   1.00 39.59  ? 441  HIS   B O   1 
ATOM   4488  C  CB  . HIS   B  1 140 ? -32.167 19.009  22.496   1.00 44.39  ? 441  HIS   B CB  1 
ATOM   4489  C  CG  . HIS   B  1 140 ? -31.083 20.015  22.753   1.00 43.77  ? 441  HIS   B CG  1 
ATOM   4490  N  ND1 . HIS   B  1 140 ? -31.311 21.374  22.756   1.00 43.43  ? 441  HIS   B ND1 1 
ATOM   4491  C  CD2 . HIS   B  1 140 ? -29.771 19.854  23.044   1.00 46.06  ? 441  HIS   B CD2 1 
ATOM   4492  C  CE1 . HIS   B  1 140 ? -30.183 22.007  23.027   1.00 45.35  ? 441  HIS   B CE1 1 
ATOM   4493  N  NE2 . HIS   B  1 140 ? -29.236 21.108  23.217   1.00 44.76  ? 441  HIS   B NE2 1 
ATOM   4494  N  N   . GLY   B  1 141 ? -34.153 17.002  21.211   1.00 38.27  ? 442  GLY   B N   1 
ATOM   4495  C  CA  . GLY   B  1 141 ? -34.774 15.713  20.970   1.00 32.70  ? 442  GLY   B CA  1 
ATOM   4496  C  C   . GLY   B  1 141 ? -34.565 15.215  19.548   1.00 46.05  ? 442  GLY   B C   1 
ATOM   4497  O  O   . GLY   B  1 141 ? -34.272 14.035  19.333   1.00 44.24  ? 442  GLY   B O   1 
ATOM   4498  N  N   . MET   B  1 142 ? -34.697 16.112  18.557   1.00 31.65  ? 443  MET   B N   1 
ATOM   4499  C  CA  . MET   B  1 142 ? -34.541 15.702  17.154   1.00 34.95  ? 443  MET   B CA  1 
ATOM   4500  C  C   . MET   B  1 142 ? -33.122 15.229  16.877   1.00 36.63  ? 443  MET   B C   1 
ATOM   4501  O  O   . MET   B  1 142 ? -32.914 14.267  16.134   1.00 39.00  ? 443  MET   B O   1 
ATOM   4502  C  CB  . MET   B  1 142 ? -34.881 16.856  16.207   1.00 30.94  ? 443  MET   B CB  1 
ATOM   4503  C  CG  . MET   B  1 142 ? -36.332 17.235  16.107   1.00 39.00  ? 443  MET   B CG  1 
ATOM   4504  S  SD  . MET   B  1 142 ? -36.481 18.685  15.040   1.00 44.40  ? 443  MET   B SD  1 
ATOM   4505  C  CE  . MET   B  1 142 ? -36.459 17.924  13.397   1.00 43.33  ? 443  MET   B CE  1 
ATOM   4506  N  N   . PHE   B  1 143 ? -32.136 15.909  17.468   1.00 38.63  ? 444  PHE   B N   1 
ATOM   4507  C  CA  . PHE   B  1 143 ? -30.747 15.496  17.342   1.00 35.01  ? 444  PHE   B CA  1 
ATOM   4508  C  C   . PHE   B  1 143 ? -30.528 14.122  17.953   1.00 42.45  ? 444  PHE   B C   1 
ATOM   4509  O  O   . PHE   B  1 143 ? -29.860 13.266  17.355   1.00 40.17  ? 444  PHE   B O   1 
ATOM   4510  C  CB  . PHE   B  1 143 ? -29.847 16.543  17.999   1.00 35.33  ? 444  PHE   B CB  1 
ATOM   4511  C  CG  . PHE   B  1 143 ? -28.412 16.127  18.123   1.00 40.36  ? 444  PHE   B CG  1 
ATOM   4512  C  CD1 . PHE   B  1 143 ? -27.617 15.972  16.998   1.00 39.53  ? 444  PHE   B CD1 1 
ATOM   4513  C  CD2 . PHE   B  1 143 ? -27.851 15.903  19.375   1.00 34.06  ? 444  PHE   B CD2 1 
ATOM   4514  C  CE1 . PHE   B  1 143 ? -26.293 15.604  17.119   1.00 41.28  ? 444  PHE   B CE1 1 
ATOM   4515  C  CE2 . PHE   B  1 143 ? -26.533 15.518  19.501   1.00 34.62  ? 444  PHE   B CE2 1 
ATOM   4516  C  CZ  . PHE   B  1 143 ? -25.749 15.374  18.371   1.00 41.87  ? 444  PHE   B CZ  1 
ATOM   4517  N  N   . ASN   B  1 144 ? -31.088 13.890  19.144   1.00 45.99  ? 445  ASN   B N   1 
ATOM   4518  C  CA  . ASN   B  1 144 ? -30.965 12.580  19.778   1.00 43.98  ? 445  ASN   B CA  1 
ATOM   4519  C  C   . ASN   B  1 144 ? -31.527 11.483  18.869   1.00 43.80  ? 445  ASN   B C   1 
ATOM   4520  O  O   . ASN   B  1 144 ? -30.868 10.463  18.625   1.00 38.52  ? 445  ASN   B O   1 
ATOM   4521  C  CB  . ASN   B  1 144 ? -31.665 12.593  21.145   1.00 44.05  ? 445  ASN   B CB  1 
ATOM   4522  C  CG  . ASN   B  1 144 ? -31.491 11.286  21.911   1.00 50.99  ? 445  ASN   B CG  1 
ATOM   4523  O  OD1 . ASN   B  1 144 ? -32.454 10.713  22.442   1.00 47.09  ? 445  ASN   B OD1 1 
ATOM   4524  N  ND2 . ASN   B  1 144 ? -30.256 10.808  21.969   1.00 52.79  ? 445  ASN   B ND2 1 
ATOM   4525  N  N   . TYR   B  1 145 ? -32.735 11.691  18.333   1.00 39.84  ? 446  TYR   B N   1 
ATOM   4526  C  CA  . TYR   B  1 145 ? -33.336 10.678  17.464   1.00 43.05  ? 446  TYR   B CA  1 
ATOM   4527  C  C   . TYR   B  1 145 ? -32.487 10.433  16.219   1.00 38.15  ? 446  TYR   B C   1 
ATOM   4528  O  O   . TYR   B  1 145 ? -32.291 9.282   15.804   1.00 36.34  ? 446  TYR   B O   1 
ATOM   4529  C  CB  . TYR   B  1 145 ? -34.745 11.101  17.069   1.00 44.66  ? 446  TYR   B CB  1 
ATOM   4530  C  CG  . TYR   B  1 145 ? -35.828 10.597  17.989   1.00 38.77  ? 446  TYR   B CG  1 
ATOM   4531  C  CD1 . TYR   B  1 145 ? -36.165 9.252   18.014   1.00 32.07  ? 446  TYR   B CD1 1 
ATOM   4532  C  CD2 . TYR   B  1 145 ? -36.533 11.469  18.812   1.00 40.68  ? 446  TYR   B CD2 1 
ATOM   4533  C  CE1 . TYR   B  1 145 ? -37.157 8.783   18.830   1.00 31.86  ? 446  TYR   B CE1 1 
ATOM   4534  C  CE2 . TYR   B  1 145 ? -37.544 11.002  19.631   1.00 30.26  ? 446  TYR   B CE2 1 
ATOM   4535  C  CZ  . TYR   B  1 145 ? -37.845 9.646   19.630   1.00 35.56  ? 446  TYR   B CZ  1 
ATOM   4536  O  OH  . TYR   B  1 145 ? -38.834 9.141   20.446   1.00 45.24  ? 446  TYR   B OH  1 
ATOM   4537  N  N   . ILE   B  1 146 ? -31.934 11.501  15.647   1.00 33.49  ? 447  ILE   B N   1 
ATOM   4538  C  CA  . ILE   B  1 146 ? -31.168 11.378  14.412   1.00 42.53  ? 447  ILE   B CA  1 
ATOM   4539  C  C   . ILE   B  1 146 ? -29.861 10.631  14.663   1.00 44.72  ? 447  ILE   B C   1 
ATOM   4540  O  O   . ILE   B  1 146 ? -29.433 9.805   13.844   1.00 42.50  ? 447  ILE   B O   1 
ATOM   4541  C  CB  . ILE   B  1 146 ? -30.958 12.780  13.818   1.00 42.03  ? 447  ILE   B CB  1 
ATOM   4542  C  CG1 . ILE   B  1 146 ? -32.293 13.296  13.260   1.00 38.03  ? 447  ILE   B CG1 1 
ATOM   4543  C  CG2 . ILE   B  1 146 ? -29.843 12.789  12.784   1.00 34.94  ? 447  ILE   B CG2 1 
ATOM   4544  C  CD1 . ILE   B  1 146 ? -32.253 14.699  12.697   1.00 34.24  ? 447  ILE   B CD1 1 
ATOM   4545  N  N   . CYS   B  1 147 ? -29.240 10.862  15.825   1.00 32.40  ? 448  CYS   B N   1 
ATOM   4546  C  CA  . CYS   B  1 147 ? -28.014 10.155  16.160   1.00 31.35  ? 448  CYS   B CA  1 
ATOM   4547  C  C   . CYS   B  1 147 ? -28.256 8.663   16.285   1.00 39.96  ? 448  CYS   B C   1 
ATOM   4548  O  O   . CYS   B  1 147 ? -27.449 7.856   15.794   1.00 38.30  ? 448  CYS   B O   1 
ATOM   4549  C  CB  . CYS   B  1 147 ? -27.423 10.698  17.461   1.00 41.80  ? 448  CYS   B CB  1 
ATOM   4550  S  SG  . CYS   B  1 147 ? -26.582 12.266  17.292   1.00 40.95  ? 448  CYS   B SG  1 
ATOM   4551  N  N   . ASN   B  1 148 ? -29.342 8.277   16.969   1.00 38.31  ? 449  ASN   B N   1 
ATOM   4552  C  CA  . ASN   B  1 148 ? -29.669 6.859   17.084   1.00 36.73  ? 449  ASN   B CA  1 
ATOM   4553  C  C   . ASN   B  1 148 ? -29.942 6.267   15.703   1.00 36.33  ? 449  ASN   B C   1 
ATOM   4554  O  O   . ASN   B  1 148 ? -29.471 5.169   15.383   1.00 34.00  ? 449  ASN   B O   1 
ATOM   4555  C  CB  . ASN   B  1 148 ? -30.870 6.645   18.011   1.00 29.99  ? 449  ASN   B CB  1 
ATOM   4556  C  CG  . ASN   B  1 148 ? -30.647 7.225   19.448   1.00 46.35  ? 449  ASN   B CG  1 
ATOM   4557  O  OD1 . ASN   B  1 148 ? -29.521 7.359   19.912   1.00 31.42  ? 449  ASN   B OD1 1 
ATOM   4558  N  ND2 . ASN   B  1 148 ? -31.734 7.567   20.125   1.00 34.49  ? 449  ASN   B ND2 1 
ATOM   4559  N  N   . HIS   B  1 149 ? -30.692 6.994   14.868   1.00 36.57  ? 450  HIS   B N   1 
ATOM   4560  C  CA  . HIS   B  1 149 ? -30.929 6.556   13.493   1.00 37.84  ? 450  HIS   B CA  1 
ATOM   4561  C  C   . HIS   B  1 149 ? -29.610 6.270   12.785   1.00 30.35  ? 450  HIS   B C   1 
ATOM   4562  O  O   . HIS   B  1 149 ? -29.372 5.156   12.305   1.00 30.48  ? 450  HIS   B O   1 
ATOM   4563  C  CB  . HIS   B  1 149 ? -31.743 7.615   12.732   1.00 36.45  ? 450  HIS   B CB  1 
ATOM   4564  C  CG  . HIS   B  1 149 ? -32.059 7.244   11.306   1.00 38.11  ? 450  HIS   B CG  1 
ATOM   4565  N  ND1 . HIS   B  1 149 ? -33.328 7.352   10.774   1.00 42.00  ? 450  HIS   B ND1 1 
ATOM   4566  C  CD2 . HIS   B  1 149 ? -31.274 6.774   10.305   1.00 37.06  ? 450  HIS   B CD2 1 
ATOM   4567  C  CE1 . HIS   B  1 149 ? -33.310 6.960   9.510    1.00 41.73  ? 450  HIS   B CE1 1 
ATOM   4568  N  NE2 . HIS   B  1 149 ? -32.078 6.599   9.203    1.00 40.60  ? 450  HIS   B NE2 1 
ATOM   4569  N  N   . VAL   B  1 150 ? -28.726 7.267   12.752   1.00 33.57  ? 451  VAL   B N   1 
ATOM   4570  C  CA  . VAL   B  1 150 ? -27.456 7.116   12.055   1.00 28.79  ? 451  VAL   B CA  1 
ATOM   4571  C  C   . VAL   B  1 150 ? -26.680 5.913   12.574   1.00 42.90  ? 451  VAL   B C   1 
ATOM   4572  O  O   . VAL   B  1 150 ? -26.104 5.148   11.788   1.00 34.36  ? 451  VAL   B O   1 
ATOM   4573  C  CB  . VAL   B  1 150 ? -26.657 8.422   12.160   1.00 29.28  ? 451  VAL   B CB  1 
ATOM   4574  C  CG1 . VAL   B  1 150 ? -25.229 8.236   11.682   1.00 29.90  ? 451  VAL   B CG1 1 
ATOM   4575  C  CG2 . VAL   B  1 150 ? -27.369 9.507   11.337   1.00 28.75  ? 451  VAL   B CG2 1 
ATOM   4576  N  N   . LYS   B  1 151 ? -26.676 5.706   13.901   1.00 43.26  ? 452  LYS   B N   1 
ATOM   4577  C  CA  . LYS   B  1 151 ? -25.899 4.611   14.481   1.00 37.24  ? 452  LYS   B CA  1 
ATOM   4578  C  C   . LYS   B  1 151 ? -26.505 3.262   14.128   1.00 37.56  ? 452  LYS   B C   1 
ATOM   4579  O  O   . LYS   B  1 151 ? -25.787 2.336   13.737   1.00 38.66  ? 452  LYS   B O   1 
ATOM   4580  C  CB  . LYS   B  1 151 ? -25.794 4.761   16.001   1.00 41.98  ? 452  LYS   B CB  1 
ATOM   4581  C  CG  . LYS   B  1 151 ? -24.856 3.764   16.666   1.00 32.46  ? 452  LYS   B CG  1 
ATOM   4582  C  CD  . LYS   B  1 151 ? -24.623 4.146   18.151   1.00 38.84  ? 452  LYS   B CD  1 
ATOM   4583  C  CE  . LYS   B  1 151 ? -23.547 3.284   18.805   1.00 34.48  ? 452  LYS   B CE  1 
ATOM   4584  N  NZ  . LYS   B  1 151 ? -23.162 3.823   20.158   1.00 46.84  ? 452  LYS   B NZ  1 
ATOM   4585  N  N   . TYR   B  1 152 ? -27.824 3.124   14.292   1.00 34.27  ? 453  TYR   B N   1 
ATOM   4586  C  CA  . TYR   B  1 152 ? -28.500 1.900   13.876   1.00 36.10  ? 453  TYR   B CA  1 
ATOM   4587  C  C   . TYR   B  1 152 ? -28.281 1.632   12.386   1.00 36.18  ? 453  TYR   B C   1 
ATOM   4588  O  O   . TYR   B  1 152 ? -27.903 0.521   11.990   1.00 34.81  ? 453  TYR   B O   1 
ATOM   4589  C  CB  . TYR   B  1 152 ? -29.998 1.996   14.185   1.00 37.84  ? 453  TYR   B CB  1 
ATOM   4590  C  CG  . TYR   B  1 152 ? -30.773 0.820   13.646   1.00 40.59  ? 453  TYR   B CG  1 
ATOM   4591  C  CD1 . TYR   B  1 152 ? -31.260 0.814   12.333   1.00 41.34  ? 453  TYR   B CD1 1 
ATOM   4592  C  CD2 . TYR   B  1 152 ? -30.974 -0.309  14.423   1.00 35.65  ? 453  TYR   B CD2 1 
ATOM   4593  C  CE1 . TYR   B  1 152 ? -31.943 -0.279  11.833   1.00 41.57  ? 453  TYR   B CE1 1 
ATOM   4594  C  CE2 . TYR   B  1 152 ? -31.667 -1.399  13.936   1.00 38.80  ? 453  TYR   B CE2 1 
ATOM   4595  C  CZ  . TYR   B  1 152 ? -32.146 -1.378  12.639   1.00 44.55  ? 453  TYR   B CZ  1 
ATOM   4596  O  OH  . TYR   B  1 152 ? -32.829 -2.466  12.153   1.00 53.39  ? 453  TYR   B OH  1 
ATOM   4597  N  N   . ALA   B  1 153 ? -28.514 2.649   11.553   1.00 28.75  ? 454  ALA   B N   1 
ATOM   4598  C  CA  . ALA   B  1 153 ? -28.468 2.483   10.090   1.00 38.96  ? 454  ALA   B CA  1 
ATOM   4599  C  C   . ALA   B  1 153 ? -27.079 2.069   9.610    1.00 35.69  ? 454  ALA   B C   1 
ATOM   4600  O  O   . ALA   B  1 153 ? -26.941 1.154   8.789    1.00 39.24  ? 454  ALA   B O   1 
ATOM   4601  C  CB  . ALA   B  1 153 ? -28.892 3.786   9.408    1.00 27.64  ? 454  ALA   B CB  1 
ATOM   4602  N  N   . THR   B  1 154 ? -26.041 2.750   10.108   1.00 37.44  ? 455  THR   B N   1 
ATOM   4603  C  CA  . THR   B  1 154 ? -24.661 2.475   9.720    1.00 35.58  ? 455  THR   B CA  1 
ATOM   4604  C  C   . THR   B  1 154 ? -24.236 1.067   10.117   1.00 40.03  ? 455  THR   B C   1 
ATOM   4605  O  O   . THR   B  1 154 ? -23.641 0.338   9.317    1.00 34.03  ? 455  THR   B O   1 
ATOM   4606  C  CB  . THR   B  1 154 ? -23.747 3.518   10.360   1.00 37.78  ? 455  THR   B CB  1 
ATOM   4607  O  OG1 . THR   B  1 154 ? -24.152 4.825   9.940    1.00 30.10  ? 455  THR   B OG1 1 
ATOM   4608  C  CG2 . THR   B  1 154 ? -22.280 3.280   10.006   1.00 31.69  ? 455  THR   B CG2 1 
ATOM   4609  N  N   . ASN   B  1 155 ? -24.501 0.671   11.366   1.00 48.65  ? 456  ASN   B N   1 
ATOM   4610  C  CA  . ASN   B  1 155 ? -24.265 -0.714  11.801   1.00 43.37  ? 456  ASN   B CA  1 
ATOM   4611  C  C   . ASN   B  1 155 ? -22.844 -1.177  11.457   1.00 42.98  ? 456  ASN   B C   1 
ATOM   4612  O  O   . ASN   B  1 155 ? -22.624 -2.278  10.941   1.00 35.35  ? 456  ASN   B O   1 
ATOM   4613  C  CB  . ASN   B  1 155 ? -25.318 -1.648  11.189   1.00 40.31  ? 456  ASN   B CB  1 
ATOM   4614  C  CG  . ASN   B  1 155 ? -25.341 -3.020  11.842   1.00 47.95  ? 456  ASN   B CG  1 
ATOM   4615  O  OD1 . ASN   B  1 155 ? -25.116 -3.154  13.055   1.00 41.76  ? 456  ASN   B OD1 1 
ATOM   4616  N  ND2 . ASN   B  1 155 ? -25.611 -4.049  11.044   1.00 39.86  ? 456  ASN   B ND2 1 
ATOM   4617  N  N   . LYS   B  1 156 ? -21.872 -0.297  11.700   1.00 42.57  ? 457  LYS   B N   1 
ATOM   4618  C  CA  . LYS   B  1 156 ? -20.459 -0.583  11.454   1.00 45.22  ? 457  LYS   B CA  1 
ATOM   4619  C  C   . LYS   B  1 156 ? -20.196 -1.034  10.016   1.00 43.45  ? 457  LYS   B C   1 
ATOM   4620  O  O   . LYS   B  1 156 ? -19.372 -1.916  9.762    1.00 45.77  ? 457  LYS   B O   1 
ATOM   4621  C  CB  . LYS   B  1 156 ? -19.933 -1.620  12.449   1.00 36.19  ? 457  LYS   B CB  1 
ATOM   4622  C  CG  . LYS   B  1 156 ? -19.756 -1.067  13.873   1.00 36.64  ? 457  LYS   B CG  1 
ATOM   4623  C  CD  . LYS   B  1 156 ? -19.415 -2.213  14.844   1.00 40.07  ? 457  LYS   B CD  1 
ATOM   4624  C  CE  . LYS   B  1 156 ? -19.138 -1.721  16.249   1.00 57.73  ? 457  LYS   B CE  1 
ATOM   4625  N  NZ  . LYS   B  1 156 ? -18.863 -2.908  17.121   1.00 65.92  ? 457  LYS   B NZ  1 
ATOM   4626  N  N   . GLY   B  1 157 ? -20.898 -0.417  9.057    1.00 46.69  ? 458  GLY   B N   1 
ATOM   4627  C  CA  . GLY   B  1 157 ? -20.695 -0.678  7.645    1.00 34.96  ? 458  GLY   B CA  1 
ATOM   4628  C  C   . GLY   B  1 157 ? -21.665 -1.668  7.040    1.00 40.96  ? 458  GLY   B C   1 
ATOM   4629  O  O   . GLY   B  1 157 ? -21.850 -1.657  5.825    1.00 45.75  ? 458  GLY   B O   1 
ATOM   4630  N  N   . ASN   B  1 158 ? -22.278 -2.531  7.846    1.00 42.57  ? 459  ASN   B N   1 
ATOM   4631  C  CA  . ASN   B  1 158 ? -23.330 -3.416  7.352    1.00 42.62  ? 459  ASN   B CA  1 
ATOM   4632  C  C   . ASN   B  1 158 ? -24.669 -2.673  7.382    1.00 47.01  ? 459  ASN   B C   1 
ATOM   4633  O  O   . ASN   B  1 158 ? -25.527 -2.902  8.245    1.00 46.04  ? 459  ASN   B O   1 
ATOM   4634  C  CB  . ASN   B  1 158 ? -23.369 -4.693  8.178    1.00 43.14  ? 459  ASN   B CB  1 
ATOM   4635  C  CG  . ASN   B  1 158 ? -24.405 -5.672  7.672    1.00 53.45  ? 459  ASN   B CG  1 
ATOM   4636  O  OD1 . ASN   B  1 158 ? -24.797 -5.628  6.506    1.00 61.48  ? 459  ASN   B OD1 1 
ATOM   4637  N  ND2 . ASN   B  1 158 ? -24.864 -6.554  8.544    1.00 57.19  ? 459  ASN   B ND2 1 
ATOM   4638  N  N   . LEU   B  1 159 ? -24.864 -1.789  6.391    1.00 35.93  ? 460  LEU   B N   1 
ATOM   4639  C  CA  . LEU   B  1 159 ? -25.936 -0.796  6.478    1.00 36.41  ? 460  LEU   B CA  1 
ATOM   4640  C  C   . LEU   B  1 159 ? -27.310 -1.453  6.529    1.00 45.15  ? 460  LEU   B C   1 
ATOM   4641  O  O   . LEU   B  1 159 ? -27.533 -2.537  5.977    1.00 42.65  ? 460  LEU   B O   1 
ATOM   4642  C  CB  . LEU   B  1 159 ? -25.897 0.187   5.301    1.00 30.39  ? 460  LEU   B CB  1 
ATOM   4643  C  CG  . LEU   B  1 159 ? -24.536 0.839   5.050    1.00 46.03  ? 460  LEU   B CG  1 
ATOM   4644  C  CD1 . LEU   B  1 159 ? -24.594 1.924   3.991    1.00 49.22  ? 460  LEU   B CD1 1 
ATOM   4645  C  CD2 . LEU   B  1 159 ? -23.966 1.378   6.338    1.00 43.20  ? 460  LEU   B CD2 1 
ATOM   4646  N  N   . ARG   B  1 160 ? -28.239 -0.767  7.195    1.00 28.84  ? 461  ARG   B N   1 
ATOM   4647  C  CA  . ARG   B  1 160 ? -29.616 -1.215  7.332    1.00 31.78  ? 461  ARG   B CA  1 
ATOM   4648  C  C   . ARG   B  1 160 ? -30.534 -0.054  7.009    1.00 29.85  ? 461  ARG   B C   1 
ATOM   4649  O  O   . ARG   B  1 160 ? -30.211 1.095   7.297    1.00 36.25  ? 461  ARG   B O   1 
ATOM   4650  C  CB  . ARG   B  1 160 ? -29.920 -1.715  8.773    1.00 31.97  ? 461  ARG   B CB  1 
ATOM   4651  C  CG  . ARG   B  1 160 ? -29.137 -2.922  9.204    1.00 44.47  ? 461  ARG   B CG  1 
ATOM   4652  C  CD  . ARG   B  1 160 ? -29.452 -3.294  10.675   1.00 43.00  ? 461  ARG   B CD  1 
ATOM   4653  N  NE  . ARG   B  1 160 ? -28.808 -2.399  11.635   1.00 37.87  ? 461  ARG   B NE  1 
ATOM   4654  C  CZ  . ARG   B  1 160 ? -28.604 -2.719  12.912   1.00 43.70  ? 461  ARG   B CZ  1 
ATOM   4655  N  NH1 . ARG   B  1 160 ? -29.006 -3.894  13.360   1.00 32.31  ? 461  ARG   B NH1 1 
ATOM   4656  N  NH2 . ARG   B  1 160 ? -27.995 -1.878  13.732   1.00 39.11  ? 461  ARG   B NH2 1 
ATOM   4657  N  N   . SER   B  1 161 ? -31.695 -0.345  6.436    1.00 39.50  ? 462  SER   B N   1 
ATOM   4658  C  CA  . SER   B  1 161 ? -32.569 0.741   5.998    1.00 43.39  ? 462  SER   B CA  1 
ATOM   4659  C  C   . SER   B  1 161 ? -33.414 1.278   7.150    1.00 40.82  ? 462  SER   B C   1 
ATOM   4660  O  O   . SER   B  1 161 ? -33.961 0.511   7.951    1.00 35.24  ? 462  SER   B O   1 
ATOM   4661  C  CB  . SER   B  1 161 ? -33.470 0.274   4.857    1.00 39.54  ? 462  SER   B CB  1 
ATOM   4662  O  OG  . SER   B  1 161 ? -32.654 -0.142  3.783    1.00 44.49  ? 462  SER   B OG  1 
ATOM   4663  N  N   . ALA   B  1 162 ? -33.556 2.602   7.219    1.00 35.07  ? 463  ALA   B N   1 
ATOM   4664  C  CA  . ALA   B  1 162 ? -34.336 3.136   8.327    1.00 31.34  ? 463  ALA   B CA  1 
ATOM   4665  C  C   . ALA   B  1 162 ? -34.977 4.460   7.962    1.00 32.12  ? 463  ALA   B C   1 
ATOM   4666  O  O   . ALA   B  1 162 ? -34.493 5.198   7.091    1.00 30.07  ? 463  ALA   B O   1 
ATOM   4667  C  CB  . ALA   B  1 162 ? -33.482 3.312   9.587    1.00 31.10  ? 463  ALA   B CB  1 
ATOM   4668  N  N   . ILE   B  1 163 ? -36.066 4.756   8.672    1.00 36.07  ? 464  ILE   B N   1 
ATOM   4669  C  CA  . ILE   B  1 163 ? -36.715 6.062   8.641    1.00 35.42  ? 464  ILE   B CA  1 
ATOM   4670  C  C   . ILE   B  1 163 ? -37.097 6.438   10.080   1.00 41.36  ? 464  ILE   B C   1 
ATOM   4671  O  O   . ILE   B  1 163 ? -37.492 5.577   10.875   1.00 36.36  ? 464  ILE   B O   1 
ATOM   4672  C  CB  . ILE   B  1 163 ? -37.947 6.067   7.711    1.00 29.53  ? 464  ILE   B CB  1 
ATOM   4673  C  CG1 . ILE   B  1 163 ? -38.530 7.473   7.581    1.00 29.20  ? 464  ILE   B CG1 1 
ATOM   4674  C  CG2 . ILE   B  1 163 ? -39.025 5.109   8.219    1.00 29.91  ? 464  ILE   B CG2 1 
ATOM   4675  C  CD1 . ILE   B  1 163 ? -39.685 7.574   6.534    1.00 25.44  ? 464  ILE   B CD1 1 
ATOM   4676  N  N   . THR   B  1 164 ? -36.948 7.724   10.416   1.00 38.03  ? 465  THR   B N   1 
ATOM   4677  C  CA  . THR   B  1 164 ? -37.349 8.284   11.702   1.00 35.76  ? 465  THR   B CA  1 
ATOM   4678  C  C   . THR   B  1 164 ? -38.422 9.328   11.436   1.00 35.36  ? 465  THR   B C   1 
ATOM   4679  O  O   . THR   B  1 164 ? -38.172 10.296  10.709   1.00 39.35  ? 465  THR   B O   1 
ATOM   4680  C  CB  . THR   B  1 164 ? -36.167 8.923   12.437   1.00 34.07  ? 465  THR   B CB  1 
ATOM   4681  O  OG1 . THR   B  1 164 ? -35.250 7.906   12.847   1.00 38.96  ? 465  THR   B OG1 1 
ATOM   4682  C  CG2 . THR   B  1 164 ? -36.657 9.724   13.658   1.00 33.55  ? 465  THR   B CG2 1 
ATOM   4683  N  N   . ILE   B  1 165 ? -39.605 9.143   12.020   1.00 32.08  ? 466  ILE   B N   1 
ATOM   4684  C  CA  . ILE   B  1 165 ? -40.757 9.974   11.694   1.00 33.18  ? 466  ILE   B CA  1 
ATOM   4685  C  C   . ILE   B  1 165 ? -41.076 10.889  12.875   1.00 41.63  ? 466  ILE   B C   1 
ATOM   4686  O  O   . ILE   B  1 165 ? -41.448 10.430  13.964   1.00 43.32  ? 466  ILE   B O   1 
ATOM   4687  C  CB  . ILE   B  1 165 ? -41.965 9.120   11.288   1.00 39.53  ? 466  ILE   B CB  1 
ATOM   4688  C  CG1 . ILE   B  1 165 ? -41.572 8.147   10.166   1.00 32.01  ? 466  ILE   B CG1 1 
ATOM   4689  C  CG2 . ILE   B  1 165 ? -43.089 10.012  10.820   1.00 43.70  ? 466  ILE   B CG2 1 
ATOM   4690  C  CD1 . ILE   B  1 165 ? -42.684 7.202   9.750    1.00 29.31  ? 466  ILE   B CD1 1 
ATOM   4691  N  N   . PHE   B  1 166 ? -40.942 12.183  12.645   1.00 46.11  ? 467  PHE   B N   1 
ATOM   4692  C  CA  . PHE   B  1 166 ? -41.187 13.225  13.627   1.00 33.40  ? 467  PHE   B CA  1 
ATOM   4693  C  C   . PHE   B  1 166 ? -42.627 13.699  13.535   1.00 38.37  ? 467  PHE   B C   1 
ATOM   4694  O  O   . PHE   B  1 166 ? -43.347 13.332  12.607   1.00 46.61  ? 467  PHE   B O   1 
ATOM   4695  C  CB  . PHE   B  1 166 ? -40.206 14.364  13.387   1.00 36.72  ? 467  PHE   B CB  1 
ATOM   4696  C  CG  . PHE   B  1 166 ? -38.797 14.020  13.742   1.00 38.33  ? 467  PHE   B CG  1 
ATOM   4697  C  CD1 . PHE   B  1 166 ? -38.405 13.931  15.073   1.00 40.48  ? 467  PHE   B CD1 1 
ATOM   4698  C  CD2 . PHE   B  1 166 ? -37.871 13.760  12.749   1.00 30.68  ? 467  PHE   B CD2 1 
ATOM   4699  C  CE1 . PHE   B  1 166 ? -37.106 13.603  15.402   1.00 39.22  ? 467  PHE   B CE1 1 
ATOM   4700  C  CE2 . PHE   B  1 166 ? -36.563 13.438  13.066   1.00 35.00  ? 467  PHE   B CE2 1 
ATOM   4701  C  CZ  . PHE   B  1 166 ? -36.173 13.350  14.389   1.00 37.12  ? 467  PHE   B CZ  1 
ATOM   4702  N  N   . PRO   B  1 167 ? -43.095 14.511  14.493   1.00 37.37  ? 468  PRO   B N   1 
ATOM   4703  C  CA  . PRO   B  1 167 ? -44.534 14.795  14.566   1.00 35.78  ? 468  PRO   B CA  1 
ATOM   4704  C  C   . PRO   B  1 167 ? -45.074 15.448  13.302   1.00 35.29  ? 468  PRO   B C   1 
ATOM   4705  O  O   . PRO   B  1 167 ? -44.434 16.306  12.692   1.00 36.98  ? 468  PRO   B O   1 
ATOM   4706  C  CB  . PRO   B  1 167 ? -44.646 15.741  15.762   1.00 34.49  ? 468  PRO   B CB  1 
ATOM   4707  C  CG  . PRO   B  1 167 ? -43.459 15.417  16.593   1.00 37.43  ? 468  PRO   B CG  1 
ATOM   4708  C  CD  . PRO   B  1 167 ? -42.377 15.175  15.595   1.00 37.36  ? 468  PRO   B CD  1 
ATOM   4709  N  N   . GLN   B  1 168 ? -46.287 15.050  12.945   1.00 38.66  ? 469  GLN   B N   1 
ATOM   4710  C  CA  . GLN   B  1 168 ? -46.935 15.500  11.730   1.00 42.30  ? 469  GLN   B CA  1 
ATOM   4711  C  C   . GLN   B  1 168 ? -47.230 16.994  11.776   1.00 50.45  ? 469  GLN   B C   1 
ATOM   4712  O  O   . GLN   B  1 168 ? -47.274 17.627  12.837   1.00 52.19  ? 469  GLN   B O   1 
ATOM   4713  C  CB  . GLN   B  1 168 ? -48.232 14.739  11.522   1.00 31.44  ? 469  GLN   B CB  1 
ATOM   4714  C  CG  . GLN   B  1 168 ? -49.250 15.034  12.589   1.00 34.10  ? 469  GLN   B CG  1 
ATOM   4715  C  CD  . GLN   B  1 168 ? -50.199 13.891  12.751   1.00 35.95  ? 469  GLN   B CD  1 
ATOM   4716  O  OE1 . GLN   B  1 168 ? -49.795 12.723  12.794   1.00 37.44  ? 469  GLN   B OE1 1 
ATOM   4717  N  NE2 . GLN   B  1 168 ? -51.482 14.208  12.795   1.00 36.70  ? 469  GLN   B NE2 1 
ATOM   4718  N  N   . ARG   B  1 169 ? -47.441 17.553  10.590   1.00 47.88  ? 470  ARG   B N   1 
ATOM   4719  C  CA  . ARG   B  1 169 ? -47.795 18.957  10.460   1.00 44.41  ? 470  ARG   B CA  1 
ATOM   4720  C  C   . ARG   B  1 169 ? -49.197 19.188  11.007   1.00 42.50  ? 470  ARG   B C   1 
ATOM   4721  O  O   . ARG   B  1 169 ? -50.109 18.394  10.758   1.00 43.73  ? 470  ARG   B O   1 
ATOM   4722  C  CB  . ARG   B  1 169 ? -47.702 19.369  8.993    1.00 54.32  ? 470  ARG   B CB  1 
ATOM   4723  C  CG  . ARG   B  1 169 ? -48.168 20.773  8.729    1.00 61.91  ? 470  ARG   B CG  1 
ATOM   4724  C  CD  . ARG   B  1 169 ? -47.991 21.099  7.287    1.00 56.35  ? 470  ARG   B CD  1 
ATOM   4725  N  NE  . ARG   B  1 169 ? -46.599 21.358  6.960    1.00 53.35  ? 470  ARG   B NE  1 
ATOM   4726  C  CZ  . ARG   B  1 169 ? -46.060 21.055  5.787    1.00 63.02  ? 470  ARG   B CZ  1 
ATOM   4727  N  NH1 . ARG   B  1 169 ? -46.801 20.459  4.863    1.00 59.86  ? 470  ARG   B NH1 1 
ATOM   4728  N  NH2 . ARG   B  1 169 ? -44.785 21.325  5.543    1.00 71.13  ? 470  ARG   B NH2 1 
ATOM   4729  N  N   . THR   B  1 170 ? -49.369 20.259  11.781   1.00 39.39  ? 471  THR   B N   1 
ATOM   4730  C  CA  . THR   B  1 170 ? -50.676 20.515  12.372   1.00 45.56  ? 471  THR   B CA  1 
ATOM   4731  C  C   . THR   B  1 170 ? -51.318 21.712  11.692   1.00 58.51  ? 471  THR   B C   1 
ATOM   4732  O  O   . THR   B  1 170 ? -52.267 21.556  10.918   1.00 68.21  ? 471  THR   B O   1 
ATOM   4733  C  CB  . THR   B  1 170 ? -50.580 20.753  13.890   1.00 50.77  ? 471  THR   B CB  1 
ATOM   4734  O  OG1 . THR   B  1 170 ? -49.676 21.837  14.164   1.00 58.49  ? 471  THR   B OG1 1 
ATOM   4735  C  CG2 . THR   B  1 170 ? -50.094 19.501  14.613   1.00 44.22  ? 471  THR   B CG2 1 
ATOM   4736  N  N   . ASP   B  1 171 ? -50.807 22.908  11.970   1.00 61.86  ? 472  ASP   B N   1 
ATOM   4737  C  CA  . ASP   B  1 171 ? -51.354 24.128  11.405   1.00 66.96  ? 472  ASP   B CA  1 
ATOM   4738  C  C   . ASP   B  1 171 ? -50.453 24.760  10.356   1.00 64.62  ? 472  ASP   B C   1 
ATOM   4739  O  O   . ASP   B  1 171 ? -50.894 25.683  9.663    1.00 73.85  ? 472  ASP   B O   1 
ATOM   4740  C  CB  . ASP   B  1 171 ? -51.649 25.147  12.521   1.00 73.95  ? 472  ASP   B CB  1 
ATOM   4741  C  CG  . ASP   B  1 171 ? -50.405 25.867  13.010   1.00 75.80  ? 472  ASP   B CG  1 
ATOM   4742  O  OD1 . ASP   B  1 171 ? -49.307 25.285  12.953   1.00 78.24  ? 472  ASP   B OD1 1 
ATOM   4743  O  OD2 . ASP   B  1 171 ? -50.528 27.028  13.451   1.00 77.29  ? 472  ASP   B OD2 1 
ATOM   4744  N  N   . GLY   B  1 172 ? -49.218 24.288  10.208   1.00 58.01  ? 473  GLY   B N   1 
ATOM   4745  C  CA  . GLY   B  1 172 ? -48.287 24.824  9.239    1.00 55.42  ? 473  GLY   B CA  1 
ATOM   4746  C  C   . GLY   B  1 172 ? -47.273 25.794  9.811    1.00 60.35  ? 473  GLY   B C   1 
ATOM   4747  O  O   . GLY   B  1 172 ? -46.213 25.993  9.207    1.00 61.16  ? 473  GLY   B O   1 
ATOM   4748  N  N   . LYS   B  1 173 ? -47.572 26.409  10.951   1.00 63.10  ? 474  LYS   B N   1 
ATOM   4749  C  CA  . LYS   B  1 173 ? -46.632 27.285  11.630   1.00 71.77  ? 474  LYS   B CA  1 
ATOM   4750  C  C   . LYS   B  1 173 ? -45.857 26.564  12.727   1.00 75.92  ? 474  LYS   B C   1 
ATOM   4751  O  O   . LYS   B  1 173 ? -45.203 27.221  13.542   1.00 75.65  ? 474  LYS   B O   1 
ATOM   4752  C  CB  . LYS   B  1 173 ? -47.368 28.495  12.212   1.00 79.20  ? 474  LYS   B CB  1 
ATOM   4753  C  CG  . LYS   B  1 173 ? -48.053 29.369  11.168   1.00 85.67  ? 474  LYS   B CG  1 
ATOM   4754  C  CD  . LYS   B  1 173 ? -48.592 30.652  11.781   1.00 93.65  ? 474  LYS   B CD  1 
ATOM   4755  C  CE  . LYS   B  1 173 ? -49.815 30.399  12.654   1.00 96.67  ? 474  LYS   B CE  1 
ATOM   4756  N  NZ  . LYS   B  1 173 ? -51.063 30.299  11.844   1.00 95.72  ? 474  LYS   B NZ  1 
ATOM   4757  N  N   . HIS   B  1 174 ? -45.924 25.230  12.771   1.00 71.43  ? 475  HIS   B N   1 
ATOM   4758  C  CA  . HIS   B  1 174 ? -45.267 24.438  13.803   1.00 67.51  ? 475  HIS   B CA  1 
ATOM   4759  C  C   . HIS   B  1 174 ? -44.589 23.222  13.195   1.00 62.75  ? 475  HIS   B C   1 
ATOM   4760  O  O   . HIS   B  1 174 ? -44.498 22.174  13.838   1.00 63.32  ? 475  HIS   B O   1 
ATOM   4761  C  CB  . HIS   B  1 174 ? -46.255 24.001  14.883   1.00 70.83  ? 475  HIS   B CB  1 
ATOM   4762  C  CG  . HIS   B  1 174 ? -46.916 25.137  15.592   1.00 75.10  ? 475  HIS   B CG  1 
ATOM   4763  N  ND1 . HIS   B  1 174 ? -48.220 25.510  15.346   1.00 78.32  ? 475  HIS   B ND1 1 
ATOM   4764  C  CD2 . HIS   B  1 174 ? -46.452 25.990  16.533   1.00 76.99  ? 475  HIS   B CD2 1 
ATOM   4765  C  CE1 . HIS   B  1 174 ? -48.530 26.545  16.105   1.00 79.66  ? 475  HIS   B CE1 1 
ATOM   4766  N  NE2 . HIS   B  1 174 ? -47.474 26.856  16.834   1.00 80.01  ? 475  HIS   B NE2 1 
ATOM   4767  N  N   . ASP   B  1 175 ? -44.129 23.344  11.952   1.00 50.26  ? 476  ASP   B N   1 
ATOM   4768  C  CA  . ASP   B  1 175 ? -43.517 22.213  11.270   1.00 48.09  ? 476  ASP   B CA  1 
ATOM   4769  C  C   . ASP   B  1 175 ? -42.234 21.792  11.966   1.00 42.37  ? 476  ASP   B C   1 
ATOM   4770  O  O   . ASP   B  1 175 ? -41.457 22.626  12.429   1.00 47.18  ? 476  ASP   B O   1 
ATOM   4771  C  CB  . ASP   B  1 175 ? -43.172 22.551  9.811    1.00 47.12  ? 476  ASP   B CB  1 
ATOM   4772  C  CG  . ASP   B  1 175 ? -44.385 22.719  8.922    1.00 47.31  ? 476  ASP   B CG  1 
ATOM   4773  O  OD1 . ASP   B  1 175 ? -45.529 22.644  9.412    1.00 51.89  ? 476  ASP   B OD1 1 
ATOM   4774  O  OD2 . ASP   B  1 175 ? -44.170 22.947  7.716    1.00 51.59  ? 476  ASP   B OD2 1 
ATOM   4775  N  N   . PHE   B  1 176 ? -42.000 20.489  12.000   1.00 38.25  ? 477  PHE   B N   1 
ATOM   4776  C  CA  . PHE   B  1 176 ? -40.676 19.953  12.264   1.00 44.38  ? 477  PHE   B CA  1 
ATOM   4777  C  C   . PHE   B  1 176 ? -39.937 19.832  10.937   1.00 43.46  ? 477  PHE   B C   1 
ATOM   4778  O  O   . PHE   B  1 176 ? -40.501 19.342  9.951    1.00 45.35  ? 477  PHE   B O   1 
ATOM   4779  C  CB  . PHE   B  1 176 ? -40.775 18.601  12.975   1.00 41.56  ? 477  PHE   B CB  1 
ATOM   4780  C  CG  . PHE   B  1 176 ? -41.206 18.720  14.392   1.00 45.27  ? 477  PHE   B CG  1 
ATOM   4781  C  CD1 . PHE   B  1 176 ? -42.508 19.088  14.704   1.00 48.20  ? 477  PHE   B CD1 1 
ATOM   4782  C  CD2 . PHE   B  1 176 ? -40.314 18.490  15.418   1.00 46.35  ? 477  PHE   B CD2 1 
ATOM   4783  C  CE1 . PHE   B  1 176 ? -42.912 19.224  16.025   1.00 46.94  ? 477  PHE   B CE1 1 
ATOM   4784  C  CE2 . PHE   B  1 176 ? -40.713 18.634  16.738   1.00 44.44  ? 477  PHE   B CE2 1 
ATOM   4785  C  CZ  . PHE   B  1 176 ? -42.010 18.998  17.037   1.00 39.19  ? 477  PHE   B CZ  1 
ATOM   4786  N  N   . ARG   B  1 177 ? -38.694 20.312  10.901   1.00 42.12  ? 478  ARG   B N   1 
ATOM   4787  C  CA  . ARG   B  1 177 ? -37.883 20.228  9.692    1.00 46.86  ? 478  ARG   B CA  1 
ATOM   4788  C  C   . ARG   B  1 177 ? -36.434 19.905  10.028   1.00 47.49  ? 478  ARG   B C   1 
ATOM   4789  O  O   . ARG   B  1 177 ? -35.842 20.529  10.916   1.00 51.41  ? 478  ARG   B O   1 
ATOM   4790  C  CB  . ARG   B  1 177 ? -37.931 21.540  8.892    1.00 41.43  ? 478  ARG   B CB  1 
ATOM   4791  C  CG  . ARG   B  1 177 ? -39.288 21.894  8.329    1.00 44.04  ? 478  ARG   B CG  1 
ATOM   4792  C  CD  . ARG   B  1 177 ? -39.748 20.883  7.283    1.00 46.92  ? 478  ARG   B CD  1 
ATOM   4793  N  NE  . ARG   B  1 177 ? -38.841 20.746  6.151    1.00 40.82  ? 478  ARG   B NE  1 
ATOM   4794  C  CZ  . ARG   B  1 177 ? -38.934 21.449  5.022    1.00 46.81  ? 478  ARG   B CZ  1 
ATOM   4795  N  NH1 . ARG   B  1 177 ? -39.882 22.365  4.874    1.00 46.61  ? 478  ARG   B NH1 1 
ATOM   4796  N  NH2 . ARG   B  1 177 ? -38.076 21.233  4.035    1.00 38.16  ? 478  ARG   B NH2 1 
ATOM   4797  N  N   . VAL   B  1 178 ? -35.870 18.934  9.315    1.00 39.46  ? 479  VAL   B N   1 
ATOM   4798  C  CA  . VAL   B  1 178 ? -34.425 18.874  9.136    1.00 38.72  ? 479  VAL   B CA  1 
ATOM   4799  C  C   . VAL   B  1 178 ? -34.088 19.863  8.028    1.00 43.92  ? 479  VAL   B C   1 
ATOM   4800  O  O   . VAL   B  1 178 ? -34.666 19.808  6.941    1.00 45.02  ? 479  VAL   B O   1 
ATOM   4801  C  CB  . VAL   B  1 178 ? -33.955 17.459  8.773    1.00 36.03  ? 479  VAL   B CB  1 
ATOM   4802  C  CG1 . VAL   B  1 178 ? -32.451 17.451  8.584    1.00 32.57  ? 479  VAL   B CG1 1 
ATOM   4803  C  CG2 . VAL   B  1 178 ? -34.362 16.461  9.838    1.00 40.13  ? 479  VAL   B CG2 1 
ATOM   4804  N  N   . TRP   B  1 179 ? -33.203 20.809  8.315    1.00 51.07  ? 480  TRP   B N   1 
ATOM   4805  C  CA  . TRP   B  1 179 ? -32.874 21.772  7.275    1.00 45.86  ? 480  TRP   B CA  1 
ATOM   4806  C  C   . TRP   B  1 179 ? -31.846 21.213  6.312    1.00 44.10  ? 480  TRP   B C   1 
ATOM   4807  O  O   . TRP   B  1 179 ? -31.821 21.624  5.152    1.00 41.64  ? 480  TRP   B O   1 
ATOM   4808  C  CB  . TRP   B  1 179 ? -32.396 23.095  7.883    1.00 45.43  ? 480  TRP   B CB  1 
ATOM   4809  C  CG  . TRP   B  1 179 ? -33.550 23.937  8.361    1.00 44.16  ? 480  TRP   B CG  1 
ATOM   4810  C  CD1 . TRP   B  1 179 ? -34.708 23.482  8.939    1.00 38.90  ? 480  TRP   B CD1 1 
ATOM   4811  C  CD2 . TRP   B  1 179 ? -33.690 25.364  8.259    1.00 44.11  ? 480  TRP   B CD2 1 
ATOM   4812  N  NE1 . TRP   B  1 179 ? -35.545 24.536  9.211    1.00 37.38  ? 480  TRP   B NE1 1 
ATOM   4813  C  CE2 . TRP   B  1 179 ? -34.946 25.700  8.806    1.00 38.01  ? 480  TRP   B CE2 1 
ATOM   4814  C  CE3 . TRP   B  1 179 ? -32.876 26.388  7.759    1.00 50.53  ? 480  TRP   B CE3 1 
ATOM   4815  C  CZ2 . TRP   B  1 179 ? -35.404 27.015  8.873    1.00 41.23  ? 480  TRP   B CZ2 1 
ATOM   4816  C  CZ3 . TRP   B  1 179 ? -33.333 27.698  7.829    1.00 48.52  ? 480  TRP   B CZ3 1 
ATOM   4817  C  CH2 . TRP   B  1 179 ? -34.584 27.997  8.380    1.00 46.46  ? 480  TRP   B CH2 1 
ATOM   4818  N  N   . ASN   B  1 180 ? -31.013 20.274  6.762    1.00 40.66  ? 481  ASN   B N   1 
ATOM   4819  C  CA  . ASN   B  1 180 ? -30.114 19.585  5.851    1.00 38.09  ? 481  ASN   B CA  1 
ATOM   4820  C  C   . ASN   B  1 180 ? -30.923 18.827  4.812    1.00 45.32  ? 481  ASN   B C   1 
ATOM   4821  O  O   . ASN   B  1 180 ? -32.021 18.339  5.103    1.00 42.14  ? 481  ASN   B O   1 
ATOM   4822  C  CB  . ASN   B  1 180 ? -29.218 18.613  6.612    1.00 37.90  ? 481  ASN   B CB  1 
ATOM   4823  C  CG  . ASN   B  1 180 ? -28.467 19.277  7.754    1.00 40.80  ? 481  ASN   B CG  1 
ATOM   4824  O  OD1 . ASN   B  1 180 ? -29.066 19.795  8.700    1.00 33.69  ? 481  ASN   B OD1 1 
ATOM   4825  N  ND2 . ASN   B  1 180 ? -27.139 19.252  7.675    1.00 44.98  ? 481  ASN   B ND2 1 
ATOM   4826  N  N   . SER   B  1 181 ? -30.383 18.724  3.588    1.00 38.80  ? 482  SER   B N   1 
ATOM   4827  C  CA  . SER   B  1 181 ? -31.077 17.923  2.581    1.00 31.17  ? 482  SER   B CA  1 
ATOM   4828  C  C   . SER   B  1 181 ? -30.772 16.442  2.759    1.00 31.79  ? 482  SER   B C   1 
ATOM   4829  O  O   . SER   B  1 181 ? -31.649 15.596  2.547    1.00 34.51  ? 482  SER   B O   1 
ATOM   4830  C  CB  . SER   B  1 181 ? -30.726 18.405  1.159    1.00 36.21  ? 482  SER   B CB  1 
ATOM   4831  O  OG  . SER   B  1 181 ? -29.329 18.561  0.984    1.00 36.11  ? 482  SER   B OG  1 
ATOM   4832  N  N   . GLN   B  1 182 ? -29.548 16.107  3.169    1.00 32.67  ? 483  GLN   B N   1 
ATOM   4833  C  CA  . GLN   B  1 182 ? -29.243 14.789  3.707    1.00 37.28  ? 483  GLN   B CA  1 
ATOM   4834  C  C   . GLN   B  1 182 ? -28.586 14.952  5.074    1.00 42.77  ? 483  GLN   B C   1 
ATOM   4835  O  O   . GLN   B  1 182 ? -27.963 15.978  5.355    1.00 53.01  ? 483  GLN   B O   1 
ATOM   4836  C  CB  . GLN   B  1 182 ? -28.324 13.984  2.800    1.00 33.03  ? 483  GLN   B CB  1 
ATOM   4837  C  CG  . GLN   B  1 182 ? -28.912 13.608  1.446    1.00 44.37  ? 483  GLN   B CG  1 
ATOM   4838  C  CD  . GLN   B  1 182 ? -27.816 13.329  0.415    1.00 48.58  ? 483  GLN   B CD  1 
ATOM   4839  O  OE1 . GLN   B  1 182 ? -26.956 12.460  0.613    1.00 45.26  ? 483  GLN   B OE1 1 
ATOM   4840  N  NE2 . GLN   B  1 182 ? -27.810 14.105  -0.659   1.00 50.75  ? 483  GLN   B NE2 1 
ATOM   4841  N  N   . LEU   B  1 183 ? -28.726 13.933  5.925    1.00 33.25  ? 484  LEU   B N   1 
ATOM   4842  C  CA  . LEU   B  1 183 ? -28.161 14.021  7.274    1.00 37.56  ? 484  LEU   B CA  1 
ATOM   4843  C  C   . LEU   B  1 183 ? -26.664 14.272  7.222    1.00 41.54  ? 484  LEU   B C   1 
ATOM   4844  O  O   . LEU   B  1 183 ? -26.128 15.053  8.013    1.00 38.44  ? 484  LEU   B O   1 
ATOM   4845  C  CB  . LEU   B  1 183 ? -28.459 12.746  8.060    1.00 30.18  ? 484  LEU   B CB  1 
ATOM   4846  C  CG  . LEU   B  1 183 ? -29.954 12.469  8.187    1.00 32.58  ? 484  LEU   B CG  1 
ATOM   4847  C  CD1 . LEU   B  1 183 ? -30.216 11.206  8.972    1.00 35.05  ? 484  LEU   B CD1 1 
ATOM   4848  C  CD2 . LEU   B  1 183 ? -30.687 13.674  8.787    1.00 27.75  ? 484  LEU   B CD2 1 
ATOM   4849  N  N   . ILE   B  1 184 ? -25.978 13.647  6.270    1.00 34.56  ? 485  ILE   B N   1 
ATOM   4850  C  CA  . ILE   B  1 184 ? -24.532 13.772  6.119    1.00 39.54  ? 485  ILE   B CA  1 
ATOM   4851  C  C   . ILE   B  1 184 ? -24.241 14.285  4.710    1.00 42.55  ? 485  ILE   B C   1 
ATOM   4852  O  O   . ILE   B  1 184 ? -24.551 13.608  3.721    1.00 38.76  ? 485  ILE   B O   1 
ATOM   4853  C  CB  . ILE   B  1 184 ? -23.824 12.437  6.398    1.00 42.29  ? 485  ILE   B CB  1 
ATOM   4854  C  CG1 . ILE   B  1 184 ? -23.921 12.113  7.902    1.00 42.11  ? 485  ILE   B CG1 1 
ATOM   4855  C  CG2 . ILE   B  1 184 ? -22.377 12.465  5.963    1.00 34.17  ? 485  ILE   B CG2 1 
ATOM   4856  C  CD1 . ILE   B  1 184 ? -23.891 10.653  8.177    1.00 36.41  ? 485  ILE   B CD1 1 
ATOM   4857  N  N   . ARG   B  1 185 ? -23.689 15.501  4.625    1.00 45.23  ? 486  ARG   B N   1 
ATOM   4858  C  CA  . ARG   B  1 185 ? -23.170 16.089  3.390    1.00 40.83  ? 486  ARG   B CA  1 
ATOM   4859  C  C   . ARG   B  1 185 ? -21.945 16.937  3.721    1.00 46.12  ? 486  ARG   B C   1 
ATOM   4860  O  O   . ARG   B  1 185 ? -21.708 17.305  4.880    1.00 43.40  ? 486  ARG   B O   1 
ATOM   4861  C  CB  . ARG   B  1 185 ? -24.207 16.966  2.667    1.00 37.03  ? 486  ARG   B CB  1 
ATOM   4862  C  CG  . ARG   B  1 185 ? -25.442 16.231  2.186    1.00 40.71  ? 486  ARG   B CG  1 
ATOM   4863  C  CD  . ARG   B  1 185 ? -26.185 16.981  1.060    1.00 50.98  ? 486  ARG   B CD  1 
ATOM   4864  N  NE  . ARG   B  1 185 ? -25.492 16.863  -0.223   1.00 57.94  ? 486  ARG   B NE  1 
ATOM   4865  C  CZ  . ARG   B  1 185 ? -25.936 17.364  -1.370   1.00 54.17  ? 486  ARG   B CZ  1 
ATOM   4866  N  NH1 . ARG   B  1 185 ? -27.080 18.026  -1.420   1.00 42.44  ? 486  ARG   B NH1 1 
ATOM   4867  N  NH2 . ARG   B  1 185 ? -25.227 17.201  -2.473   1.00 64.65  ? 486  ARG   B NH2 1 
ATOM   4868  N  N   . TYR   B  1 186 ? -21.166 17.251  2.693    1.00 37.19  ? 487  TYR   B N   1 
ATOM   4869  C  CA  . TYR   B  1 186 ? -19.981 18.073  2.870    1.00 43.42  ? 487  TYR   B CA  1 
ATOM   4870  C  C   . TYR   B  1 186 ? -20.281 19.528  2.541    1.00 46.76  ? 487  TYR   B C   1 
ATOM   4871  O  O   . TYR   B  1 186 ? -21.151 19.837  1.726    1.00 46.69  ? 487  TYR   B O   1 
ATOM   4872  C  CB  . TYR   B  1 186 ? -18.825 17.575  1.998    1.00 41.26  ? 487  TYR   B CB  1 
ATOM   4873  C  CG  . TYR   B  1 186 ? -18.381 16.171  2.324    1.00 49.32  ? 487  TYR   B CG  1 
ATOM   4874  C  CD1 . TYR   B  1 186 ? -17.869 15.856  3.580    1.00 45.52  ? 487  TYR   B CD1 1 
ATOM   4875  C  CD2 . TYR   B  1 186 ? -18.465 15.161  1.380    1.00 47.42  ? 487  TYR   B CD2 1 
ATOM   4876  C  CE1 . TYR   B  1 186 ? -17.460 14.574  3.880    1.00 49.01  ? 487  TYR   B CE1 1 
ATOM   4877  C  CE2 . TYR   B  1 186 ? -18.059 13.870  1.675    1.00 49.60  ? 487  TYR   B CE2 1 
ATOM   4878  C  CZ  . TYR   B  1 186 ? -17.557 13.581  2.924    1.00 50.15  ? 487  TYR   B CZ  1 
ATOM   4879  O  OH  . TYR   B  1 186 ? -17.153 12.298  3.222    1.00 49.31  ? 487  TYR   B OH  1 
ATOM   4880  N  N   . ALA   B  1 187 ? -19.541 20.424  3.187    1.00 52.63  ? 488  ALA   B N   1 
ATOM   4881  C  CA  . ALA   B  1 187 ? -19.736 21.851  3.003    1.00 51.49  ? 488  ALA   B CA  1 
ATOM   4882  C  C   . ALA   B  1 187 ? -19.244 22.304  1.631    1.00 54.81  ? 488  ALA   B C   1 
ATOM   4883  O  O   . ALA   B  1 187 ? -18.427 21.650  0.975    1.00 58.13  ? 488  ALA   B O   1 
ATOM   4884  C  CB  . ALA   B  1 187 ? -19.002 22.638  4.089    1.00 41.03  ? 488  ALA   B CB  1 
ATOM   4885  N  N   . GLY   B  1 188 ? -19.762 23.447  1.204    1.00 53.60  ? 489  GLY   B N   1 
ATOM   4886  C  CA  . GLY   B  1 188 ? -19.242 24.125  0.033    1.00 57.42  ? 489  GLY   B CA  1 
ATOM   4887  C  C   . GLY   B  1 188 ? -18.972 25.581  0.339    1.00 56.55  ? 489  GLY   B C   1 
ATOM   4888  O  O   . GLY   B  1 188 ? -19.824 26.268  0.910    1.00 59.90  ? 489  GLY   B O   1 
ATOM   4889  N  N   . TYR   B  1 189 ? -17.793 26.066  -0.029   1.00 53.18  ? 490  TYR   B N   1 
ATOM   4890  C  CA  . TYR   B  1 189 ? -17.360 27.409  0.328    1.00 58.46  ? 490  TYR   B CA  1 
ATOM   4891  C  C   . TYR   B  1 189 ? -17.057 28.191  -0.938   1.00 68.55  ? 490  TYR   B C   1 
ATOM   4892  O  O   . TYR   B  1 189 ? -16.348 27.698  -1.825   1.00 65.51  ? 490  TYR   B O   1 
ATOM   4893  C  CB  . TYR   B  1 189 ? -16.125 27.372  1.231    1.00 58.56  ? 490  TYR   B CB  1 
ATOM   4894  C  CG  . TYR   B  1 189 ? -16.223 26.438  2.424    1.00 61.76  ? 490  TYR   B CG  1 
ATOM   4895  C  CD1 . TYR   B  1 189 ? -16.965 26.779  3.551    1.00 63.51  ? 490  TYR   B CD1 1 
ATOM   4896  C  CD2 . TYR   B  1 189 ? -15.554 25.222  2.430    1.00 63.86  ? 490  TYR   B CD2 1 
ATOM   4897  C  CE1 . TYR   B  1 189 ? -17.038 25.930  4.651    1.00 66.05  ? 490  TYR   B CE1 1 
ATOM   4898  C  CE2 . TYR   B  1 189 ? -15.627 24.366  3.520    1.00 65.76  ? 490  TYR   B CE2 1 
ATOM   4899  C  CZ  . TYR   B  1 189 ? -16.360 24.726  4.628    1.00 64.65  ? 490  TYR   B CZ  1 
ATOM   4900  O  OH  . TYR   B  1 189 ? -16.429 23.866  5.700    1.00 62.46  ? 490  TYR   B OH  1 
ATOM   4901  N  N   . LYS   B  1 190 ? -17.588 29.407  -1.015   1.00 74.75  ? 491  LYS   B N   1 
ATOM   4902  C  CA  . LYS   B  1 190 ? -17.356 30.278  -2.161   1.00 77.42  ? 491  LYS   B CA  1 
ATOM   4903  C  C   . LYS   B  1 190 ? -16.028 31.003  -1.962   1.00 79.62  ? 491  LYS   B C   1 
ATOM   4904  O  O   . LYS   B  1 190 ? -15.911 31.864  -1.088   1.00 85.59  ? 491  LYS   B O   1 
ATOM   4905  C  CB  . LYS   B  1 190 ? -18.516 31.257  -2.318   1.00 80.65  ? 491  LYS   B CB  1 
ATOM   4906  C  CG  . LYS   B  1 190 ? -18.812 31.634  -3.764   1.00 88.52  ? 491  LYS   B CG  1 
ATOM   4907  C  CD  . LYS   B  1 190 ? -19.093 30.400  -4.621   1.00 89.47  ? 491  LYS   B CD  1 
ATOM   4908  C  CE  . LYS   B  1 190 ? -19.296 30.772  -6.081   1.00 91.32  ? 491  LYS   B CE  1 
ATOM   4909  N  NZ  . LYS   B  1 190 ? -18.153 31.563  -6.623   1.00 92.24  ? 491  LYS   B NZ  1 
ATOM   4910  N  N   . GLN   B  1 191 ? -15.024 30.656  -2.768   1.00 82.39  ? 492  GLN   B N   1 
ATOM   4911  C  CA  . GLN   B  1 191 ? -13.696 31.237  -2.618   1.00 89.87  ? 492  GLN   B CA  1 
ATOM   4912  C  C   . GLN   B  1 191 ? -13.662 32.679  -3.132   1.00 90.53  ? 492  GLN   B C   1 
ATOM   4913  O  O   . GLN   B  1 191 ? -14.485 33.077  -3.962   1.00 89.77  ? 492  GLN   B O   1 
ATOM   4914  C  CB  . GLN   B  1 191 ? -12.652 30.397  -3.357   1.00 88.71  ? 492  GLN   B CB  1 
ATOM   4915  C  CG  . GLN   B  1 191 ? -12.492 28.962  -2.858   1.00 86.96  ? 492  GLN   B CG  1 
ATOM   4916  C  CD  . GLN   B  1 191 ? -11.763 28.850  -1.524   1.00 90.23  ? 492  GLN   B CD  1 
ATOM   4917  O  OE1 . GLN   B  1 191 ? -11.964 29.653  -0.614   1.00 90.29  ? 492  GLN   B OE1 1 
ATOM   4918  N  NE2 . GLN   B  1 191 ? -10.913 27.839  -1.406   1.00 91.52  ? 492  GLN   B NE2 1 
ATOM   4919  N  N   . PRO   B  1 192 ? -12.713 33.486  -2.644   1.00 89.53  ? 493  PRO   B N   1 
ATOM   4920  C  CA  . PRO   B  1 192 ? -12.657 34.889  -3.088   1.00 91.32  ? 493  PRO   B CA  1 
ATOM   4921  C  C   . PRO   B  1 192 ? -12.366 35.045  -4.574   1.00 94.29  ? 493  PRO   B C   1 
ATOM   4922  O  O   . PRO   B  1 192 ? -12.871 35.984  -5.205   1.00 88.68  ? 493  PRO   B O   1 
ATOM   4923  C  CB  . PRO   B  1 192 ? -11.543 35.486  -2.213   1.00 86.05  ? 493  PRO   B CB  1 
ATOM   4924  C  CG  . PRO   B  1 192 ? -10.741 34.316  -1.734   1.00 80.38  ? 493  PRO   B CG  1 
ATOM   4925  C  CD  . PRO   B  1 192 ? -11.712 33.193  -1.600   1.00 83.56  ? 493  PRO   B CD  1 
ATOM   4926  N  N   . ASP   B  1 193 ? -11.579 34.146  -5.157   1.00 97.71  ? 494  ASP   B N   1 
ATOM   4927  C  CA  . ASP   B  1 193 ? -11.269 34.173  -6.579   1.00 96.18  ? 494  ASP   B CA  1 
ATOM   4928  C  C   . ASP   B  1 193 ? -12.406 33.661  -7.451   1.00 92.84  ? 494  ASP   B C   1 
ATOM   4929  O  O   . ASP   B  1 193 ? -12.228 33.521  -8.669   1.00 98.32  ? 494  ASP   B O   1 
ATOM   4930  C  CB  . ASP   B  1 193 ? -10.003 33.356  -6.846   1.00 98.80  ? 494  ASP   B CB  1 
ATOM   4931  C  CG  . ASP   B  1 193 ? -10.000 32.031  -6.103   1.00 96.83  ? 494  ASP   B CG  1 
ATOM   4932  O  OD1 . ASP   B  1 193 ? -10.538 31.044  -6.656   1.00 89.45  ? 494  ASP   B OD1 1 
ATOM   4933  O  OD2 . ASP   B  1 193 ? -9.465  31.985  -4.966   1.00 97.05  ? 494  ASP   B OD2 1 
ATOM   4934  N  N   . GLY   B  1 194 ? -13.570 33.362  -6.874   1.00 79.18  ? 495  GLY   B N   1 
ATOM   4935  C  CA  . GLY   B  1 194 ? -14.719 32.953  -7.639   1.00 61.79  ? 495  GLY   B CA  1 
ATOM   4936  C  C   . GLY   B  1 194 ? -14.902 31.459  -7.786   1.00 61.38  ? 495  GLY   B C   1 
ATOM   4937  O  O   . GLY   B  1 194 ? -16.000 31.021  -8.143   1.00 64.69  ? 495  GLY   B O   1 
ATOM   4938  N  N   . SER   B  1 195 ? -13.864 30.663  -7.537   1.00 70.83  ? 496  SER   B N   1 
ATOM   4939  C  CA  . SER   B  1 195 ? -13.988 29.210  -7.547   1.00 77.39  ? 496  SER   B CA  1 
ATOM   4940  C  C   . SER   B  1 195 ? -14.777 28.739  -6.320   1.00 79.38  ? 496  SER   B C   1 
ATOM   4941  O  O   . SER   B  1 195 ? -15.285 29.536  -5.525   1.00 76.77  ? 496  SER   B O   1 
ATOM   4942  C  CB  . SER   B  1 195 ? -12.609 28.560  -7.596   1.00 82.14  ? 496  SER   B CB  1 
ATOM   4943  O  OG  . SER   B  1 195 ? -11.764 29.078  -6.580   1.00 86.45  ? 496  SER   B OG  1 
ATOM   4944  N  N   . THR   B  1 196 ? -14.876 27.420  -6.159   1.00 79.49  ? 497  THR   B N   1 
ATOM   4945  C  CA  . THR   B  1 196 ? -15.679 26.836  -5.090   1.00 78.64  ? 497  THR   B CA  1 
ATOM   4946  C  C   . THR   B  1 196 ? -14.955 25.653  -4.463   1.00 72.52  ? 497  THR   B C   1 
ATOM   4947  O  O   . THR   B  1 196 ? -14.566 24.719  -5.168   1.00 75.48  ? 497  THR   B O   1 
ATOM   4948  C  CB  . THR   B  1 196 ? -17.044 26.389  -5.620   1.00 83.72  ? 497  THR   B CB  1 
ATOM   4949  O  OG1 . THR   B  1 196 ? -17.729 27.510  -6.200   1.00 80.63  ? 497  THR   B OG1 1 
ATOM   4950  C  CG2 . THR   B  1 196 ? -17.878 25.814  -4.488   1.00 85.92  ? 497  THR   B CG2 1 
ATOM   4951  N  N   . LEU   B  1 197 ? -14.792 25.691  -3.141   1.00 69.99  ? 498  LEU   B N   1 
ATOM   4952  C  CA  . LEU   B  1 197 ? -14.148 24.621  -2.385   1.00 68.16  ? 498  LEU   B CA  1 
ATOM   4953  C  C   . LEU   B  1 197 ? -15.199 23.758  -1.700   1.00 65.41  ? 498  LEU   B C   1 
ATOM   4954  O  O   . LEU   B  1 197 ? -16.179 24.274  -1.151   1.00 60.20  ? 498  LEU   B O   1 
ATOM   4955  C  CB  . LEU   B  1 197 ? -13.179 25.191  -1.337   1.00 65.95  ? 498  LEU   B CB  1 
ATOM   4956  C  CG  . LEU   B  1 197 ? -12.708 24.253  -0.213   1.00 59.10  ? 498  LEU   B CG  1 
ATOM   4957  C  CD1 . LEU   B  1 197 ? -11.867 23.087  -0.728   1.00 55.84  ? 498  LEU   B CD1 1 
ATOM   4958  C  CD2 . LEU   B  1 197 ? -11.944 25.017  0.861    1.00 62.43  ? 498  LEU   B CD2 1 
ATOM   4959  N  N   . GLY   B  1 198 ? -14.981 22.439  -1.725   1.00 70.41  ? 499  GLY   B N   1 
ATOM   4960  C  CA  . GLY   B  1 198 ? -15.943 21.484  -1.194   1.00 66.63  ? 499  GLY   B CA  1 
ATOM   4961  C  C   . GLY   B  1 198 ? -17.017 21.067  -2.186   1.00 63.12  ? 499  GLY   B C   1 
ATOM   4962  O  O   . GLY   B  1 198 ? -16.721 20.798  -3.352   1.00 65.58  ? 499  GLY   B O   1 
ATOM   4963  N  N   . ASP   B  1 199 ? -18.280 21.022  -1.737   1.00 56.79  ? 500  ASP   B N   1 
ATOM   4964  C  CA  . ASP   B  1 199 ? -19.388 20.594  -2.578   1.00 47.07  ? 500  ASP   B CA  1 
ATOM   4965  C  C   . ASP   B  1 199 ? -20.197 21.810  -3.013   1.00 51.51  ? 500  ASP   B C   1 
ATOM   4966  O  O   . ASP   B  1 199 ? -20.865 22.436  -2.164   1.00 43.59  ? 500  ASP   B O   1 
ATOM   4967  C  CB  . ASP   B  1 199 ? -20.274 19.606  -1.827   1.00 46.63  ? 500  ASP   B CB  1 
ATOM   4968  C  CG  . ASP   B  1 199 ? -21.309 18.937  -2.719   1.00 53.25  ? 500  ASP   B CG  1 
ATOM   4969  O  OD1 . ASP   B  1 199 ? -21.642 19.489  -3.800   1.00 60.15  ? 500  ASP   B OD1 1 
ATOM   4970  O  OD2 . ASP   B  1 199 ? -21.799 17.849  -2.328   1.00 40.71  ? 500  ASP   B OD2 1 
ATOM   4971  N  N   . PRO   B  1 200 ? -20.191 22.173  -4.309   1.00 43.78  ? 501  PRO   B N   1 
ATOM   4972  C  CA  . PRO   B  1 200 ? -20.913 23.388  -4.737   1.00 42.16  ? 501  PRO   B CA  1 
ATOM   4973  C  C   . PRO   B  1 200 ? -22.402 23.372  -4.422   1.00 43.14  ? 501  PRO   B C   1 
ATOM   4974  O  O   . PRO   B  1 200 ? -22.980 24.435  -4.158   1.00 48.79  ? 501  PRO   B O   1 
ATOM   4975  C  CB  . PRO   B  1 200 ? -20.647 23.433  -6.253   1.00 43.00  ? 501  PRO   B CB  1 
ATOM   4976  C  CG  . PRO   B  1 200 ? -19.319 22.773  -6.416   1.00 40.04  ? 501  PRO   B CG  1 
ATOM   4977  C  CD  . PRO   B  1 200 ? -19.334 21.634  -5.379   1.00 42.66  ? 501  PRO   B CD  1 
ATOM   4978  N  N   . ALA   B  1 201 ? -23.035 22.197  -4.405   1.00 37.89  ? 502  ALA   B N   1 
ATOM   4979  C  CA  . ALA   B  1 201 ? -24.467 22.126  -4.131   1.00 37.27  ? 502  ALA   B CA  1 
ATOM   4980  C  C   . ALA   B  1 201 ? -24.826 22.725  -2.774   1.00 53.35  ? 502  ALA   B C   1 
ATOM   4981  O  O   . ALA   B  1 201 ? -25.909 23.298  -2.608   1.00 53.47  ? 502  ALA   B O   1 
ATOM   4982  C  CB  . ALA   B  1 201 ? -24.929 20.673  -4.203   1.00 36.62  ? 502  ALA   B CB  1 
ATOM   4983  N  N   . ASN   B  1 202 ? -23.932 22.623  -1.803   1.00 48.34  ? 503  ASN   B N   1 
ATOM   4984  C  CA  . ASN   B  1 202 ? -24.259 23.005  -0.442   1.00 53.97  ? 503  ASN   B CA  1 
ATOM   4985  C  C   . ASN   B  1 202 ? -23.710 24.363  -0.074   1.00 60.62  ? 503  ASN   B C   1 
ATOM   4986  O  O   . ASN   B  1 202 ? -23.717 24.716  1.105    1.00 57.42  ? 503  ASN   B O   1 
ATOM   4987  C  CB  . ASN   B  1 202 ? -23.754 21.937  0.523    1.00 41.91  ? 503  ASN   B CB  1 
ATOM   4988  C  CG  . ASN   B  1 202 ? -24.339 20.588  0.212    1.00 38.52  ? 503  ASN   B CG  1 
ATOM   4989  O  OD1 . ASN   B  1 202 ? -25.542 20.477  -0.054   1.00 44.82  ? 503  ASN   B OD1 1 
ATOM   4990  N  ND2 . ASN   B  1 202 ? -23.498 19.552  0.211    1.00 41.99  ? 503  ASN   B ND2 1 
ATOM   4991  N  N   . VAL   B  1 203 ? -23.240 25.135  -1.060   1.00 63.43  ? 504  VAL   B N   1 
ATOM   4992  C  CA  . VAL   B  1 203 ? -22.693 26.460  -0.779   1.00 59.03  ? 504  VAL   B CA  1 
ATOM   4993  C  C   . VAL   B  1 203 ? -23.695 27.285  0.018    1.00 58.29  ? 504  VAL   B C   1 
ATOM   4994  O  O   . VAL   B  1 203 ? -23.339 27.950  1.004    1.00 57.35  ? 504  VAL   B O   1 
ATOM   4995  C  CB  . VAL   B  1 203 ? -22.288 27.164  -2.092   1.00 59.06  ? 504  VAL   B CB  1 
ATOM   4996  C  CG1 . VAL   B  1 203 ? -22.046 28.643  -1.855   1.00 44.07  ? 504  VAL   B CG1 1 
ATOM   4997  C  CG2 . VAL   B  1 203 ? -21.034 26.515  -2.692   1.00 48.22  ? 504  VAL   B CG2 1 
ATOM   4998  N  N   . GLN   B  1 204 ? -24.971 27.223  -0.369   1.00 50.27  ? 505  GLN   B N   1 
ATOM   4999  C  CA  . GLN   B  1 204 ? -25.966 28.090  0.246    1.00 54.06  ? 505  GLN   B CA  1 
ATOM   5000  C  C   . GLN   B  1 204 ? -26.354 27.597  1.634    1.00 61.57  ? 505  GLN   B C   1 
ATOM   5001  O  O   . GLN   B  1 204 ? -26.538 28.401  2.554    1.00 64.80  ? 505  GLN   B O   1 
ATOM   5002  C  CB  . GLN   B  1 204 ? -27.200 28.191  -0.646   1.00 54.40  ? 505  GLN   B CB  1 
ATOM   5003  C  CG  . GLN   B  1 204 ? -28.233 29.182  -0.138   1.00 64.08  ? 505  GLN   B CG  1 
ATOM   5004  C  CD  . GLN   B  1 204 ? -29.618 28.936  -0.702   1.00 72.39  ? 505  GLN   B CD  1 
ATOM   5005  O  OE1 . GLN   B  1 204 ? -29.890 27.874  -1.265   1.00 77.32  ? 505  GLN   B OE1 1 
ATOM   5006  N  NE2 . GLN   B  1 204 ? -30.502 29.919  -0.557   1.00 74.97  ? 505  GLN   B NE2 1 
ATOM   5007  N  N   . PHE   B  1 205 ? -26.501 26.284  1.802    1.00 60.57  ? 506  PHE   B N   1 
ATOM   5008  C  CA  . PHE   B  1 205 ? -26.752 25.745  3.130    1.00 50.79  ? 506  PHE   B CA  1 
ATOM   5009  C  C   . PHE   B  1 205 ? -25.539 25.932  4.034    1.00 54.24  ? 506  PHE   B C   1 
ATOM   5010  O  O   . PHE   B  1 205 ? -25.685 26.235  5.229    1.00 49.24  ? 506  PHE   B O   1 
ATOM   5011  C  CB  . PHE   B  1 205 ? -27.132 24.272  3.036    1.00 42.61  ? 506  PHE   B CB  1 
ATOM   5012  C  CG  . PHE   B  1 205 ? -27.496 23.657  4.364    1.00 48.56  ? 506  PHE   B CG  1 
ATOM   5013  C  CD1 . PHE   B  1 205 ? -28.707 23.958  4.969    1.00 48.79  ? 506  PHE   B CD1 1 
ATOM   5014  C  CD2 . PHE   B  1 205 ? -26.629 22.782  5.006    1.00 48.71  ? 506  PHE   B CD2 1 
ATOM   5015  C  CE1 . PHE   B  1 205 ? -29.057 23.398  6.185    1.00 49.99  ? 506  PHE   B CE1 1 
ATOM   5016  C  CE2 . PHE   B  1 205 ? -26.974 22.215  6.231    1.00 54.57  ? 506  PHE   B CE2 1 
ATOM   5017  C  CZ  . PHE   B  1 205 ? -28.191 22.526  6.820    1.00 52.02  ? 506  PHE   B CZ  1 
ATOM   5018  N  N   . THR   B  1 206 ? -24.333 25.753  3.484    1.00 43.73  ? 507  THR   B N   1 
ATOM   5019  C  CA  . THR   B  1 206 ? -23.129 26.029  4.260    1.00 46.15  ? 507  THR   B CA  1 
ATOM   5020  C  C   . THR   B  1 206 ? -23.113 27.474  4.737    1.00 58.71  ? 507  THR   B C   1 
ATOM   5021  O  O   . THR   B  1 206 ? -22.748 27.751  5.885    1.00 58.76  ? 507  THR   B O   1 
ATOM   5022  C  CB  . THR   B  1 206 ? -21.882 25.720  3.436    1.00 48.38  ? 507  THR   B CB  1 
ATOM   5023  O  OG1 . THR   B  1 206 ? -21.907 24.346  3.038    1.00 52.58  ? 507  THR   B OG1 1 
ATOM   5024  C  CG2 . THR   B  1 206 ? -20.623 25.986  4.241    1.00 45.95  ? 507  THR   B CG2 1 
ATOM   5025  N  N   . GLU   B  1 207 ? -23.543 28.407  3.883    1.00 63.45  ? 508  GLU   B N   1 
ATOM   5026  C  CA  . GLU   B  1 207 ? -23.602 29.808  4.296    1.00 65.41  ? 508  GLU   B CA  1 
ATOM   5027  C  C   . GLU   B  1 207 ? -24.553 30.000  5.476    1.00 58.15  ? 508  GLU   B C   1 
ATOM   5028  O  O   . GLU   B  1 207 ? -24.230 30.718  6.427    1.00 51.19  ? 508  GLU   B O   1 
ATOM   5029  C  CB  . GLU   B  1 207 ? -24.010 30.696  3.118    1.00 67.78  ? 508  GLU   B CB  1 
ATOM   5030  C  CG  . GLU   B  1 207 ? -22.847 31.119  2.234    1.00 84.80  ? 508  GLU   B CG  1 
ATOM   5031  C  CD  . GLU   B  1 207 ? -23.298 31.706  0.902    1.00 98.01  ? 508  GLU   B CD  1 
ATOM   5032  O  OE1 . GLU   B  1 207 ? -24.470 32.134  0.805    1.00 102.51 ? 508  GLU   B OE1 1 
ATOM   5033  O  OE2 . GLU   B  1 207 ? -22.480 31.728  -0.047   1.00 99.45  ? 508  GLU   B OE2 1 
ATOM   5034  N  N   . ILE   B  1 208 ? -25.732 29.365  5.430    1.00 54.30  ? 509  ILE   B N   1 
ATOM   5035  C  CA  . ILE   B  1 208 ? -26.696 29.508  6.522    1.00 54.58  ? 509  ILE   B CA  1 
ATOM   5036  C  C   . ILE   B  1 208 ? -26.089 29.009  7.825    1.00 55.90  ? 509  ILE   B C   1 
ATOM   5037  O  O   . ILE   B  1 208 ? -26.208 29.651  8.876    1.00 58.14  ? 509  ILE   B O   1 
ATOM   5038  C  CB  . ILE   B  1 208 ? -27.998 28.759  6.197    1.00 55.07  ? 509  ILE   B CB  1 
ATOM   5039  C  CG1 . ILE   B  1 208 ? -28.617 29.265  4.901    1.00 54.46  ? 509  ILE   B CG1 1 
ATOM   5040  C  CG2 . ILE   B  1 208 ? -28.993 28.908  7.338    1.00 59.55  ? 509  ILE   B CG2 1 
ATOM   5041  C  CD1 . ILE   B  1 208 ? -29.864 28.491  4.497    1.00 47.76  ? 509  ILE   B CD1 1 
ATOM   5042  N  N   . CYS   B  1 209 ? -25.418 27.859  7.769    1.00 55.69  ? 510  CYS   B N   1 
ATOM   5043  C  CA  . CYS   B  1 209 ? -24.753 27.320  8.945    1.00 51.96  ? 510  CYS   B CA  1 
ATOM   5044  C  C   . CYS   B  1 209 ? -23.723 28.297  9.488    1.00 55.83  ? 510  CYS   B C   1 
ATOM   5045  O  O   . CYS   B  1 209 ? -23.700 28.579  10.695   1.00 55.52  ? 510  CYS   B O   1 
ATOM   5046  C  CB  . CYS   B  1 209 ? -24.109 25.979  8.604    1.00 51.23  ? 510  CYS   B CB  1 
ATOM   5047  S  SG  . CYS   B  1 209 ? -25.304 24.702  8.116    1.00 56.35  ? 510  CYS   B SG  1 
ATOM   5048  N  N   . ILE   B  1 210 ? -22.860 28.828  8.610    1.00 61.26  ? 511  ILE   B N   1 
ATOM   5049  C  CA  . ILE   B  1 210 ? -21.869 29.811  9.049    1.00 65.30  ? 511  ILE   B CA  1 
ATOM   5050  C  C   . ILE   B  1 210 ? -22.570 31.030  9.626    1.00 69.26  ? 511  ILE   B C   1 
ATOM   5051  O  O   . ILE   B  1 210 ? -22.206 31.533  10.696   1.00 67.70  ? 511  ILE   B O   1 
ATOM   5052  C  CB  . ILE   B  1 210 ? -20.924 30.200  7.896    1.00 62.83  ? 511  ILE   B CB  1 
ATOM   5053  C  CG1 . ILE   B  1 210 ? -20.322 28.975  7.229    1.00 64.86  ? 511  ILE   B CG1 1 
ATOM   5054  C  CG2 . ILE   B  1 210 ? -19.775 31.017  8.419    1.00 62.10  ? 511  ILE   B CG2 1 
ATOM   5055  C  CD1 . ILE   B  1 210 ? -19.522 29.319  5.989    1.00 61.24  ? 511  ILE   B CD1 1 
ATOM   5056  N  N   . GLN   B  1 211 ? -23.610 31.495  8.941    1.00 70.19  ? 512  GLN   B N   1 
ATOM   5057  C  CA  . GLN   B  1 211 ? -24.477 32.586  9.361    1.00 79.83  ? 512  GLN   B CA  1 
ATOM   5058  C  C   . GLN   B  1 211 ? -25.281 32.261  10.617   1.00 78.92  ? 512  GLN   B C   1 
ATOM   5059  O  O   . GLN   B  1 211 ? -25.959 33.146  11.139   1.00 83.11  ? 512  GLN   B O   1 
ATOM   5060  C  CB  . GLN   B  1 211 ? -25.409 32.934  8.206    1.00 90.92  ? 512  GLN   B CB  1 
ATOM   5061  C  CG  . GLN   B  1 211 ? -26.177 34.216  8.324    1.00 102.97 ? 512  GLN   B CG  1 
ATOM   5062  C  CD  . GLN   B  1 211 ? -26.968 34.479  7.073    1.00 110.51 ? 512  GLN   B CD  1 
ATOM   5063  O  OE1 . GLN   B  1 211 ? -26.416 34.476  5.974    1.00 107.04 ? 512  GLN   B OE1 1 
ATOM   5064  N  NE2 . GLN   B  1 211 ? -28.275 34.671  7.222    1.00 116.98 ? 512  GLN   B NE2 1 
ATOM   5065  N  N   . GLN   B  1 212 ? -25.226 31.030  11.116   1.00 71.39  ? 513  GLN   B N   1 
ATOM   5066  C  CA  . GLN   B  1 212 ? -25.876 30.677  12.369   1.00 65.15  ? 513  GLN   B CA  1 
ATOM   5067  C  C   . GLN   B  1 212 ? -24.886 30.419  13.484   1.00 65.62  ? 513  GLN   B C   1 
ATOM   5068  O  O   . GLN   B  1 212 ? -25.291 30.006  14.572   1.00 70.72  ? 513  GLN   B O   1 
ATOM   5069  C  CB  . GLN   B  1 212 ? -26.765 29.448  12.183   1.00 67.98  ? 513  GLN   B CB  1 
ATOM   5070  C  CG  . GLN   B  1 212 ? -28.067 29.753  11.487   1.00 68.28  ? 513  GLN   B CG  1 
ATOM   5071  C  CD  . GLN   B  1 212 ? -28.846 30.814  12.225   1.00 74.15  ? 513  GLN   B CD  1 
ATOM   5072  O  OE1 . GLN   B  1 212 ? -29.333 31.766  11.626   1.00 80.86  ? 513  GLN   B OE1 1 
ATOM   5073  N  NE2 . GLN   B  1 212 ? -28.953 30.662  13.538   1.00 70.86  ? 513  GLN   B NE2 1 
ATOM   5074  N  N   . GLY   B  1 213 ? -23.603 30.664  13.247   1.00 64.75  ? 514  GLY   B N   1 
ATOM   5075  C  CA  . GLY   B  1 213 ? -22.574 30.475  14.244   1.00 58.03  ? 514  GLY   B CA  1 
ATOM   5076  C  C   . GLY   B  1 213 ? -21.678 29.279  14.018   1.00 60.23  ? 514  GLY   B C   1 
ATOM   5077  O  O   . GLY   B  1 213 ? -20.768 29.057  14.826   1.00 62.56  ? 514  GLY   B O   1 
ATOM   5078  N  N   . TRP   B  1 214 ? -21.903 28.489  12.967   1.00 53.44  ? 515  TRP   B N   1 
ATOM   5079  C  CA  . TRP   B  1 214 ? -21.015 27.366  12.700   1.00 57.29  ? 515  TRP   B CA  1 
ATOM   5080  C  C   . TRP   B  1 214 ? -19.635 27.886  12.306   1.00 62.44  ? 515  TRP   B C   1 
ATOM   5081  O  O   . TRP   B  1 214 ? -19.512 28.814  11.496   1.00 57.44  ? 515  TRP   B O   1 
ATOM   5082  C  CB  . TRP   B  1 214 ? -21.598 26.467  11.605   1.00 51.83  ? 515  TRP   B CB  1 
ATOM   5083  C  CG  . TRP   B  1 214 ? -20.825 25.185  11.377   1.00 59.69  ? 515  TRP   B CG  1 
ATOM   5084  C  CD1 . TRP   B  1 214 ? -20.600 24.196  12.287   1.00 62.30  ? 515  TRP   B CD1 1 
ATOM   5085  C  CD2 . TRP   B  1 214 ? -20.201 24.751  10.154   1.00 59.40  ? 515  TRP   B CD2 1 
ATOM   5086  N  NE1 . TRP   B  1 214 ? -19.863 23.182  11.717   1.00 62.81  ? 515  TRP   B NE1 1 
ATOM   5087  C  CE2 . TRP   B  1 214 ? -19.603 23.499  10.411   1.00 59.17  ? 515  TRP   B CE2 1 
ATOM   5088  C  CE3 . TRP   B  1 214 ? -20.087 25.300  8.875    1.00 63.77  ? 515  TRP   B CE3 1 
ATOM   5089  C  CZ2 . TRP   B  1 214 ? -18.906 22.786  9.436    1.00 61.40  ? 515  TRP   B CZ2 1 
ATOM   5090  C  CZ3 . TRP   B  1 214 ? -19.385 24.589  7.903    1.00 65.17  ? 515  TRP   B CZ3 1 
ATOM   5091  C  CH2 . TRP   B  1 214 ? -18.802 23.349  8.193    1.00 62.80  ? 515  TRP   B CH2 1 
ATOM   5092  N  N   . LYS   B  1 215 ? -18.595 27.304  12.905   1.00 59.60  ? 516  LYS   B N   1 
ATOM   5093  C  CA  . LYS   B  1 215 ? -17.220 27.629  12.550   1.00 67.66  ? 516  LYS   B CA  1 
ATOM   5094  C  C   . LYS   B  1 215 ? -16.740 26.626  11.517   1.00 74.54  ? 516  LYS   B C   1 
ATOM   5095  O  O   . LYS   B  1 215 ? -16.447 25.470  11.847   1.00 84.73  ? 516  LYS   B O   1 
ATOM   5096  C  CB  . LYS   B  1 215 ? -16.303 27.606  13.768   1.00 71.92  ? 516  LYS   B CB  1 
ATOM   5097  C  CG  . LYS   B  1 215 ? -16.833 28.403  14.932   1.00 81.40  ? 516  LYS   B CG  1 
ATOM   5098  C  CD  . LYS   B  1 215 ? -17.165 29.824  14.506   1.00 84.67  ? 516  LYS   B CD  1 
ATOM   5099  C  CE  . LYS   B  1 215 ? -17.570 30.678  15.693   1.00 79.78  ? 516  LYS   B CE  1 
ATOM   5100  N  NZ  . LYS   B  1 215 ? -17.690 32.097  15.300   1.00 78.56  ? 516  LYS   B NZ  1 
ATOM   5101  N  N   . PRO   B  1 216 ? -16.661 27.023  10.260   1.00 69.01  ? 517  PRO   B N   1 
ATOM   5102  C  CA  . PRO   B  1 216 ? -16.241 26.099  9.226    1.00 67.68  ? 517  PRO   B CA  1 
ATOM   5103  C  C   . PRO   B  1 216 ? -14.756 25.817  9.343    1.00 64.51  ? 517  PRO   B C   1 
ATOM   5104  O  O   . PRO   B  1 216 ? -13.957 26.745  9.526    1.00 60.81  ? 517  PRO   B O   1 
ATOM   5105  C  CB  . PRO   B  1 216 ? -16.564 26.856  7.932    1.00 72.88  ? 517  PRO   B CB  1 
ATOM   5106  C  CG  . PRO   B  1 216 ? -16.436 28.301  8.318    1.00 72.14  ? 517  PRO   B CG  1 
ATOM   5107  C  CD  . PRO   B  1 216 ? -16.899 28.383  9.748    1.00 69.81  ? 517  PRO   B CD  1 
ATOM   5108  N  N   . PRO   B  1 217 ? -14.348 24.548  9.267    1.00 66.73  ? 518  PRO   B N   1 
ATOM   5109  C  CA  . PRO   B  1 217 ? -12.919 24.252  9.079    1.00 68.94  ? 518  PRO   B CA  1 
ATOM   5110  C  C   . PRO   B  1 217 ? -12.418 24.610  7.685    1.00 68.50  ? 518  PRO   B C   1 
ATOM   5111  O  O   . PRO   B  1 217 ? -11.201 24.597  7.460    1.00 68.19  ? 518  PRO   B O   1 
ATOM   5112  C  CB  . PRO   B  1 217 ? -12.833 22.739  9.332    1.00 69.61  ? 518  PRO   B CB  1 
ATOM   5113  C  CG  . PRO   B  1 217 ? -14.153 22.352  9.954    1.00 66.48  ? 518  PRO   B CG  1 
ATOM   5114  C  CD  . PRO   B  1 217 ? -15.153 23.328  9.433    1.00 64.25  ? 518  PRO   B CD  1 
ATOM   5115  N  N   . ARG   B  1 218 ? -13.326 24.918  6.758    1.00 67.91  ? 519  ARG   B N   1 
ATOM   5116  C  CA  . ARG   B  1 218 ? -13.013 25.388  5.407    1.00 73.99  ? 519  ARG   B CA  1 
ATOM   5117  C  C   . ARG   B  1 218 ? -12.076 24.420  4.674    1.00 79.16  ? 519  ARG   B C   1 
ATOM   5118  O  O   . ARG   B  1 218 ? -10.961 24.761  4.270    1.00 82.25  ? 519  ARG   B O   1 
ATOM   5119  C  CB  . ARG   B  1 218 ? -12.451 26.815  5.441    1.00 74.82  ? 519  ARG   B CB  1 
ATOM   5120  C  CG  . ARG   B  1 218 ? -13.440 27.856  5.997    1.00 74.25  ? 519  ARG   B CG  1 
ATOM   5121  C  CD  . ARG   B  1 218 ? -13.185 29.263  5.448    1.00 78.95  ? 519  ARG   B CD  1 
ATOM   5122  N  NE  . ARG   B  1 218 ? -14.086 29.615  4.343    1.00 83.72  ? 519  ARG   B NE  1 
ATOM   5123  C  CZ  . ARG   B  1 218 ? -15.095 30.482  4.440    1.00 80.42  ? 519  ARG   B CZ  1 
ATOM   5124  N  NH1 . ARG   B  1 218 ? -15.865 30.736  3.385    1.00 72.35  ? 519  ARG   B NH1 1 
ATOM   5125  N  NH2 . ARG   B  1 218 ? -15.333 31.103  5.594    1.00 81.23  ? 519  ARG   B NH2 1 
ATOM   5126  N  N   . GLY   B  1 219 ? -12.578 23.195  4.493    1.00 76.78  ? 520  GLY   B N   1 
ATOM   5127  C  CA  . GLY   B  1 219 ? -11.893 22.152  3.747    1.00 70.15  ? 520  GLY   B CA  1 
ATOM   5128  C  C   . GLY   B  1 219 ? -12.709 21.587  2.594    1.00 69.13  ? 520  GLY   B C   1 
ATOM   5129  O  O   . GLY   B  1 219 ? -13.781 22.105  2.265    1.00 62.31  ? 520  GLY   B O   1 
ATOM   5130  N  N   . ARG   B  1 220 ? -12.215 20.521  1.963    1.00 69.31  ? 521  ARG   B N   1 
ATOM   5131  C  CA  . ARG   B  1 220 ? -12.901 19.951  0.813    1.00 62.73  ? 521  ARG   B CA  1 
ATOM   5132  C  C   . ARG   B  1 220 ? -13.972 18.948  1.210    1.00 67.90  ? 521  ARG   B C   1 
ATOM   5133  O  O   . ARG   B  1 220 ? -14.940 18.765  0.463    1.00 66.34  ? 521  ARG   B O   1 
ATOM   5134  C  CB  . ARG   B  1 220 ? -11.888 19.292  -0.130   1.00 62.13  ? 521  ARG   B CB  1 
ATOM   5135  C  CG  . ARG   B  1 220 ? -12.461 18.838  -1.457   1.00 58.68  ? 521  ARG   B CG  1 
ATOM   5136  C  CD  . ARG   B  1 220 ? -11.744 19.518  -2.616   1.00 72.96  ? 521  ARG   B CD  1 
ATOM   5137  N  NE  . ARG   B  1 220 ? -12.161 18.991  -3.913   1.00 77.34  ? 521  ARG   B NE  1 
ATOM   5138  C  CZ  . ARG   B  1 220 ? -11.533 18.011  -4.558   1.00 80.67  ? 521  ARG   B CZ  1 
ATOM   5139  N  NH1 . ARG   B  1 220 ? -10.450 17.450  -4.034   1.00 82.57  ? 521  ARG   B NH1 1 
ATOM   5140  N  NH2 . ARG   B  1 220 ? -11.987 17.595  -5.731   1.00 82.87  ? 521  ARG   B NH2 1 
ATOM   5141  N  N   . PHE   B  1 221 ? -13.830 18.310  2.385    1.00 72.51  ? 522  PHE   B N   1 
ATOM   5142  C  CA  . PHE   B  1 221 ? -14.799 17.339  2.902    1.00 66.17  ? 522  PHE   B CA  1 
ATOM   5143  C  C   . PHE   B  1 221 ? -15.081 17.663  4.378    1.00 71.11  ? 522  PHE   B C   1 
ATOM   5144  O  O   . PHE   B  1 221 ? -14.657 16.945  5.291    1.00 75.50  ? 522  PHE   B O   1 
ATOM   5145  C  CB  . PHE   B  1 221 ? -14.291 15.902  2.724    1.00 63.49  ? 522  PHE   B CB  1 
ATOM   5146  C  CG  . PHE   B  1 221 ? -14.007 15.533  1.294    1.00 68.72  ? 522  PHE   B CG  1 
ATOM   5147  C  CD1 . PHE   B  1 221 ? -14.948 15.766  0.302    1.00 72.14  ? 522  PHE   B CD1 1 
ATOM   5148  C  CD2 . PHE   B  1 221 ? -12.796 14.969  0.937    1.00 67.45  ? 522  PHE   B CD2 1 
ATOM   5149  C  CE1 . PHE   B  1 221 ? -14.687 15.441  -1.021   1.00 71.37  ? 522  PHE   B CE1 1 
ATOM   5150  C  CE2 . PHE   B  1 221 ? -12.535 14.642  -0.384   1.00 73.00  ? 522  PHE   B CE2 1 
ATOM   5151  C  CZ  . PHE   B  1 221 ? -13.483 14.885  -1.364   1.00 69.73  ? 522  PHE   B CZ  1 
ATOM   5152  N  N   . ASP   B  1 222 ? -15.805 18.761  4.606    1.00 61.96  ? 523  ASP   B N   1 
ATOM   5153  C  CA  . ASP   B  1 222 ? -16.233 19.170  5.939    1.00 53.34  ? 523  ASP   B CA  1 
ATOM   5154  C  C   . ASP   B  1 222 ? -17.666 18.692  6.151    1.00 51.11  ? 523  ASP   B C   1 
ATOM   5155  O  O   . ASP   B  1 222 ? -18.597 19.233  5.548    1.00 48.60  ? 523  ASP   B O   1 
ATOM   5156  C  CB  . ASP   B  1 222 ? -16.141 20.689  6.103    1.00 54.84  ? 523  ASP   B CB  1 
ATOM   5157  C  CG  . ASP   B  1 222 ? -14.700 21.197  6.209    1.00 62.11  ? 523  ASP   B CG  1 
ATOM   5158  O  OD1 . ASP   B  1 222 ? -13.790 20.388  6.494    1.00 64.84  ? 523  ASP   B OD1 1 
ATOM   5159  O  OD2 . ASP   B  1 222 ? -14.476 22.416  6.020    1.00 59.37  ? 523  ASP   B OD2 1 
ATOM   5160  N  N   . VAL   B  1 223 ? -17.850 17.689  7.021    1.00 56.16  ? 524  VAL   B N   1 
ATOM   5161  C  CA  . VAL   B  1 223 ? -19.202 17.257  7.374    1.00 43.40  ? 524  VAL   B CA  1 
ATOM   5162  C  C   . VAL   B  1 223 ? -19.974 18.442  7.927    1.00 39.68  ? 524  VAL   B C   1 
ATOM   5163  O  O   . VAL   B  1 223 ? -19.501 19.145  8.825    1.00 44.40  ? 524  VAL   B O   1 
ATOM   5164  C  CB  . VAL   B  1 223 ? -19.170 16.107  8.395    1.00 49.41  ? 524  VAL   B CB  1 
ATOM   5165  C  CG1 . VAL   B  1 223 ? -20.600 15.659  8.726    1.00 34.64  ? 524  VAL   B CG1 1 
ATOM   5166  C  CG2 . VAL   B  1 223 ? -18.316 14.930  7.894    1.00 38.51  ? 524  VAL   B CG2 1 
ATOM   5167  N  N   . LEU   B  1 224 ? -21.155 18.683  7.379    1.00 43.08  ? 525  LEU   B N   1 
ATOM   5168  C  CA  . LEU   B  1 224 ? -21.951 19.822  7.806    1.00 45.19  ? 525  LEU   B CA  1 
ATOM   5169  C  C   . LEU   B  1 224 ? -22.626 19.528  9.143    1.00 40.76  ? 525  LEU   B C   1 
ATOM   5170  O  O   . LEU   B  1 224 ? -22.888 18.370  9.468    1.00 44.32  ? 525  LEU   B O   1 
ATOM   5171  C  CB  . LEU   B  1 224 ? -23.007 20.154  6.757    1.00 47.10  ? 525  LEU   B CB  1 
ATOM   5172  C  CG  . LEU   B  1 224 ? -22.511 20.833  5.479    1.00 49.40  ? 525  LEU   B CG  1 
ATOM   5173  C  CD1 . LEU   B  1 224 ? -23.453 20.517  4.349    1.00 35.71  ? 525  LEU   B CD1 1 
ATOM   5174  C  CD2 . LEU   B  1 224 ? -22.419 22.337  5.703    1.00 56.96  ? 525  LEU   B CD2 1 
ATOM   5175  N  N   . PRO   B  1 225 ? -22.914 20.557  9.937    1.00 43.79  ? 526  PRO   B N   1 
ATOM   5176  C  CA  . PRO   B  1 225 ? -23.687 20.344  11.162   1.00 37.47  ? 526  PRO   B CA  1 
ATOM   5177  C  C   . PRO   B  1 225 ? -25.136 20.074  10.810   1.00 43.73  ? 526  PRO   B C   1 
ATOM   5178  O  O   . PRO   B  1 225 ? -25.616 20.458  9.744    1.00 52.08  ? 526  PRO   B O   1 
ATOM   5179  C  CB  . PRO   B  1 225 ? -23.548 21.676  11.901   1.00 41.45  ? 526  PRO   B CB  1 
ATOM   5180  C  CG  . PRO   B  1 225 ? -23.453 22.670  10.784   1.00 46.69  ? 526  PRO   B CG  1 
ATOM   5181  C  CD  . PRO   B  1 225 ? -22.641 21.989  9.707    1.00 41.96  ? 526  PRO   B CD  1 
ATOM   5182  N  N   . LEU   B  1 226 ? -25.836 19.395  11.711   1.00 40.79  ? 527  LEU   B N   1 
ATOM   5183  C  CA  . LEU   B  1 226 ? -27.288 19.355  11.601   1.00 45.73  ? 527  LEU   B CA  1 
ATOM   5184  C  C   . LEU   B  1 226 ? -27.871 20.728  11.911   1.00 38.44  ? 527  LEU   B C   1 
ATOM   5185  O  O   . LEU   B  1 226 ? -27.306 21.501  12.682   1.00 42.91  ? 527  LEU   B O   1 
ATOM   5186  C  CB  . LEU   B  1 226 ? -27.881 18.315  12.547   1.00 38.96  ? 527  LEU   B CB  1 
ATOM   5187  C  CG  . LEU   B  1 226 ? -27.519 16.893  12.140   1.00 43.02  ? 527  LEU   B CG  1 
ATOM   5188  C  CD1 . LEU   B  1 226 ? -27.991 15.911  13.180   1.00 34.87  ? 527  LEU   B CD1 1 
ATOM   5189  C  CD2 . LEU   B  1 226 ? -28.085 16.541  10.749   1.00 30.71  ? 527  LEU   B CD2 1 
ATOM   5190  N  N   . LEU   B  1 227 ? -28.989 21.042  11.262   1.00 41.88  ? 528  LEU   B N   1 
ATOM   5191  C  CA  . LEU   B  1 227 ? -29.728 22.287  11.473   1.00 36.57  ? 528  LEU   B CA  1 
ATOM   5192  C  C   . LEU   B  1 227 ? -31.180 21.863  11.616   1.00 41.33  ? 528  LEU   B C   1 
ATOM   5193  O  O   . LEU   B  1 227 ? -31.860 21.641  10.611   1.00 41.96  ? 528  LEU   B O   1 
ATOM   5194  C  CB  . LEU   B  1 227 ? -29.553 23.272  10.322   1.00 40.54  ? 528  LEU   B CB  1 
ATOM   5195  C  CG  . LEU   B  1 227 ? -29.323 24.778  10.568   1.00 47.20  ? 528  LEU   B CG  1 
ATOM   5196  C  CD1 . LEU   B  1 227 ? -30.082 25.642  9.564    1.00 38.48  ? 528  LEU   B CD1 1 
ATOM   5197  C  CD2 . LEU   B  1 227 ? -29.609 25.231  12.001   1.00 44.16  ? 528  LEU   B CD2 1 
ATOM   5198  N  N   . LEU   B  1 228 ? -31.640 21.732  12.861   1.00 48.61  ? 529  LEU   B N   1 
ATOM   5199  C  CA  . LEU   B  1 228 ? -32.886 21.047  13.180   1.00 44.61  ? 529  LEU   B CA  1 
ATOM   5200  C  C   . LEU   B  1 228 ? -33.931 22.033  13.679   1.00 47.91  ? 529  LEU   B C   1 
ATOM   5201  O  O   . LEU   B  1 228 ? -33.641 22.878  14.541   1.00 42.58  ? 529  LEU   B O   1 
ATOM   5202  C  CB  . LEU   B  1 228 ? -32.644 19.961  14.229   1.00 41.92  ? 529  LEU   B CB  1 
ATOM   5203  C  CG  . LEU   B  1 228 ? -31.542 18.978  13.833   1.00 43.17  ? 529  LEU   B CG  1 
ATOM   5204  C  CD1 . LEU   B  1 228 ? -31.455 17.889  14.863   1.00 31.70  ? 529  LEU   B CD1 1 
ATOM   5205  C  CD2 . LEU   B  1 228 ? -31.802 18.364  12.439   1.00 30.99  ? 529  LEU   B CD2 1 
ATOM   5206  N  N   . GLN   B  1 229 ? -35.153 21.902  13.157   1.00 41.20  ? 530  GLN   B N   1 
ATOM   5207  C  CA  . GLN   B  1 229 ? -36.262 22.782  13.501   1.00 42.10  ? 530  GLN   B CA  1 
ATOM   5208  C  C   . GLN   B  1 229 ? -37.393 21.968  14.114   1.00 40.56  ? 530  GLN   B C   1 
ATOM   5209  O  O   . GLN   B  1 229 ? -37.973 21.103  13.447   1.00 38.64  ? 530  GLN   B O   1 
ATOM   5210  C  CB  . GLN   B  1 229 ? -36.761 23.531  12.271   1.00 44.65  ? 530  GLN   B CB  1 
ATOM   5211  C  CG  . GLN   B  1 229 ? -38.053 24.271  12.496   1.00 50.87  ? 530  GLN   B CG  1 
ATOM   5212  C  CD  . GLN   B  1 229 ? -38.665 24.737  11.197   1.00 58.88  ? 530  GLN   B CD  1 
ATOM   5213  O  OE1 . GLN   B  1 229 ? -37.962 24.997  10.226   1.00 52.70  ? 530  GLN   B OE1 1 
ATOM   5214  N  NE2 . GLN   B  1 229 ? -39.984 24.828  11.169   1.00 68.01  ? 530  GLN   B NE2 1 
ATOM   5215  N  N   . ALA   B  1 230 ? -37.705 22.260  15.379   1.00 43.04  ? 531  ALA   B N   1 
ATOM   5216  C  CA  . ALA   B  1 230 ? -38.796 21.640  16.120   1.00 34.29  ? 531  ALA   B CA  1 
ATOM   5217  C  C   . ALA   B  1 230 ? -39.933 22.631  16.310   1.00 41.42  ? 531  ALA   B C   1 
ATOM   5218  O  O   . ALA   B  1 230 ? -39.704 23.798  16.647   1.00 42.93  ? 531  ALA   B O   1 
ATOM   5219  C  CB  . ALA   B  1 230 ? -38.331 21.151  17.504   1.00 34.35  ? 531  ALA   B CB  1 
ATOM   5220  N  N   . ASN   B  1 231 ? -41.154 22.151  16.089   1.00 45.44  ? 532  ASN   B N   1 
ATOM   5221  C  CA  . ASN   B  1 231 ? -42.389 22.881  16.373   1.00 51.37  ? 532  ASN   B CA  1 
ATOM   5222  C  C   . ASN   B  1 231 ? -42.358 24.340  15.900   1.00 53.44  ? 532  ASN   B C   1 
ATOM   5223  O  O   . ASN   B  1 231 ? -42.787 25.257  16.599   1.00 48.01  ? 532  ASN   B O   1 
ATOM   5224  C  CB  . ASN   B  1 231 ? -42.719 22.813  17.854   1.00 52.90  ? 532  ASN   B CB  1 
ATOM   5225  C  CG  . ASN   B  1 231 ? -44.180 23.028  18.103   1.00 64.38  ? 532  ASN   B CG  1 
ATOM   5226  O  OD1 . ASN   B  1 231 ? -45.021 22.458  17.402   1.00 69.17  ? 532  ASN   B OD1 1 
ATOM   5227  N  ND2 . ASN   B  1 231 ? -44.503 23.880  19.069   1.00 61.61  ? 532  ASN   B ND2 1 
ATOM   5228  N  N   . GLY   B  1 232 ? -41.858 24.554  14.682   1.00 53.38  ? 533  GLY   B N   1 
ATOM   5229  C  CA  . GLY   B  1 232 ? -41.872 25.871  14.078   1.00 48.73  ? 533  GLY   B CA  1 
ATOM   5230  C  C   . GLY   B  1 232 ? -40.868 26.868  14.616   1.00 56.59  ? 533  GLY   B C   1 
ATOM   5231  O  O   . GLY   B  1 232 ? -40.727 27.952  14.032   1.00 62.83  ? 533  GLY   B O   1 
ATOM   5232  N  N   . ASN   B  1 233 ? -40.163 26.552  15.699   1.00 57.13  ? 534  ASN   B N   1 
ATOM   5233  C  CA  . ASN   B  1 233 ? -39.191 27.480  16.257   1.00 57.69  ? 534  ASN   B CA  1 
ATOM   5234  C  C   . ASN   B  1 233 ? -37.966 27.587  15.343   1.00 51.67  ? 534  ASN   B C   1 
ATOM   5235  O  O   . ASN   B  1 233 ? -37.811 26.847  14.368   1.00 55.23  ? 534  ASN   B O   1 
ATOM   5236  C  CB  . ASN   B  1 233 ? -38.783 27.034  17.664   1.00 60.55  ? 534  ASN   B CB  1 
ATOM   5237  C  CG  . ASN   B  1 233 ? -39.982 26.810  18.582   1.00 59.98  ? 534  ASN   B CG  1 
ATOM   5238  O  OD1 . ASN   B  1 233 ? -40.780 27.711  18.817   1.00 66.84  ? 534  ASN   B OD1 1 
ATOM   5239  N  ND2 . ASN   B  1 233 ? -40.121 25.595  19.080   1.00 58.38  ? 534  ASN   B ND2 1 
ATOM   5240  N  N   . ASP   B  1 234 ? -37.083 28.526  15.675   1.00 52.48  ? 535  ASP   B N   1 
ATOM   5241  C  CA  . ASP   B  1 234 ? -35.854 28.706  14.915   1.00 54.63  ? 535  ASP   B CA  1 
ATOM   5242  C  C   . ASP   B  1 234 ? -35.027 27.417  14.922   1.00 56.41  ? 535  ASP   B C   1 
ATOM   5243  O  O   . ASP   B  1 234 ? -35.077 26.636  15.877   1.00 59.49  ? 535  ASP   B O   1 
ATOM   5244  C  CB  . ASP   B  1 234 ? -35.025 29.854  15.493   1.00 64.09  ? 535  ASP   B CB  1 
ATOM   5245  C  CG  . ASP   B  1 234 ? -35.631 31.230  15.222   1.00 67.07  ? 535  ASP   B CG  1 
ATOM   5246  O  OD1 . ASP   B  1 234 ? -36.664 31.321  14.523   1.00 64.88  ? 535  ASP   B OD1 1 
ATOM   5247  O  OD2 . ASP   B  1 234 ? -35.059 32.225  15.719   1.00 68.73  ? 535  ASP   B OD2 1 
ATOM   5248  N  N   . PRO   B  1 235 ? -34.278 27.152  13.856   1.00 52.87  ? 536  PRO   B N   1 
ATOM   5249  C  CA  . PRO   B  1 235 ? -33.425 25.960  13.840   1.00 47.42  ? 536  PRO   B CA  1 
ATOM   5250  C  C   . PRO   B  1 235 ? -32.195 26.127  14.724   1.00 47.38  ? 536  PRO   B C   1 
ATOM   5251  O  O   . PRO   B  1 235 ? -31.753 27.236  15.028   1.00 54.79  ? 536  PRO   B O   1 
ATOM   5252  C  CB  . PRO   B  1 235 ? -33.043 25.810  12.357   1.00 45.99  ? 536  PRO   B CB  1 
ATOM   5253  C  CG  . PRO   B  1 235 ? -33.267 27.136  11.756   1.00 42.32  ? 536  PRO   B CG  1 
ATOM   5254  C  CD  . PRO   B  1 235 ? -34.386 27.779  12.528   1.00 45.80  ? 536  PRO   B CD  1 
ATOM   5255  N  N   . GLU   B  1 236 ? -31.630 24.986  15.123   1.00 45.11  ? 537  GLU   B N   1 
ATOM   5256  C  CA  . GLU   B  1 236 ? -30.480 24.936  16.017   1.00 48.55  ? 537  GLU   B CA  1 
ATOM   5257  C  C   . GLU   B  1 236 ? -29.389 24.043  15.427   1.00 46.75  ? 537  GLU   B C   1 
ATOM   5258  O  O   . GLU   B  1 236 ? -29.669 22.931  14.974   1.00 47.67  ? 537  GLU   B O   1 
ATOM   5259  C  CB  . GLU   B  1 236 ? -30.904 24.413  17.415   1.00 46.07  ? 537  GLU   B CB  1 
ATOM   5260  C  CG  . GLU   B  1 236 ? -32.103 25.162  18.020   1.00 53.15  ? 537  GLU   B CG  1 
ATOM   5261  C  CD  . GLU   B  1 236 ? -32.487 24.694  19.430   1.00 58.17  ? 537  GLU   B CD  1 
ATOM   5262  O  OE1 . GLU   B  1 236 ? -31.606 24.192  20.171   1.00 54.27  ? 537  GLU   B OE1 1 
ATOM   5263  O  OE2 . GLU   B  1 236 ? -33.679 24.835  19.791   1.00 56.09  ? 537  GLU   B OE2 1 
ATOM   5264  N  N   . LEU   B  1 237 ? -28.143 24.524  15.453   1.00 41.26  ? 538  LEU   B N   1 
ATOM   5265  C  CA  . LEU   B  1 237 ? -27.011 23.736  14.982   1.00 46.48  ? 538  LEU   B CA  1 
ATOM   5266  C  C   . LEU   B  1 237 ? -26.612 22.654  15.993   1.00 49.23  ? 538  LEU   B C   1 
ATOM   5267  O  O   . LEU   B  1 237 ? -26.636 22.878  17.207   1.00 47.15  ? 538  LEU   B O   1 
ATOM   5268  C  CB  . LEU   B  1 237 ? -25.818 24.657  14.687   1.00 39.92  ? 538  LEU   B CB  1 
ATOM   5269  C  CG  . LEU   B  1 237 ? -25.994 25.575  13.463   1.00 49.79  ? 538  LEU   B CG  1 
ATOM   5270  C  CD1 . LEU   B  1 237 ? -24.933 26.657  13.383   1.00 52.13  ? 538  LEU   B CD1 1 
ATOM   5271  C  CD2 . LEU   B  1 237 ? -26.027 24.765  12.165   1.00 44.41  ? 538  LEU   B CD2 1 
ATOM   5272  N  N   . PHE   B  1 238 ? -26.250 21.471  15.477   1.00 45.26  ? 539  PHE   B N   1 
ATOM   5273  C  CA  . PHE   B  1 238 ? -25.661 20.375  16.244   1.00 46.84  ? 539  PHE   B CA  1 
ATOM   5274  C  C   . PHE   B  1 238 ? -24.585 19.705  15.401   1.00 53.61  ? 539  PHE   B C   1 
ATOM   5275  O  O   . PHE   B  1 238 ? -24.795 19.466  14.213   1.00 50.53  ? 539  PHE   B O   1 
ATOM   5276  C  CB  . PHE   B  1 238 ? -26.695 19.306  16.628   1.00 41.62  ? 539  PHE   B CB  1 
ATOM   5277  C  CG  . PHE   B  1 238 ? -27.848 19.831  17.414   1.00 47.71  ? 539  PHE   B CG  1 
ATOM   5278  C  CD1 . PHE   B  1 238 ? -28.951 20.384  16.771   1.00 46.82  ? 539  PHE   B CD1 1 
ATOM   5279  C  CD2 . PHE   B  1 238 ? -27.838 19.763  18.804   1.00 41.86  ? 539  PHE   B CD2 1 
ATOM   5280  C  CE1 . PHE   B  1 238 ? -30.020 20.871  17.497   1.00 47.96  ? 539  PHE   B CE1 1 
ATOM   5281  C  CE2 . PHE   B  1 238 ? -28.908 20.247  19.546   1.00 44.82  ? 539  PHE   B CE2 1 
ATOM   5282  C  CZ  . PHE   B  1 238 ? -29.999 20.800  18.904   1.00 47.75  ? 539  PHE   B CZ  1 
ATOM   5283  N  N   . GLN   B  1 239 ? -23.449 19.369  16.009   1.00 62.50  ? 540  GLN   B N   1 
ATOM   5284  C  CA  . GLN   B  1 239 ? -22.397 18.630  15.312   1.00 57.87  ? 540  GLN   B CA  1 
ATOM   5285  C  C   . GLN   B  1 239 ? -22.591 17.134  15.549   1.00 46.93  ? 540  GLN   B C   1 
ATOM   5286  O  O   . GLN   B  1 239 ? -22.585 16.681  16.701   1.00 38.87  ? 540  GLN   B O   1 
ATOM   5287  C  CB  . GLN   B  1 239 ? -21.013 19.071  15.786   1.00 59.61  ? 540  GLN   B CB  1 
ATOM   5288  C  CG  . GLN   B  1 239 ? -19.886 18.152  15.327   1.00 69.22  ? 540  GLN   B CG  1 
ATOM   5289  C  CD  . GLN   B  1 239 ? -19.001 17.675  16.479   1.00 84.07  ? 540  GLN   B CD  1 
ATOM   5290  O  OE1 . GLN   B  1 239 ? -19.492 17.247  17.538   1.00 86.15  ? 540  GLN   B OE1 1 
ATOM   5291  N  NE2 . GLN   B  1 239 ? -17.688 17.737  16.272   1.00 82.91  ? 540  GLN   B NE2 1 
ATOM   5292  N  N   . ILE   B  1 240 ? -22.775 16.372  14.473   1.00 35.21  ? 541  ILE   B N   1 
ATOM   5293  C  CA  . ILE   B  1 240 ? -22.911 14.912  14.626   1.00 35.90  ? 541  ILE   B CA  1 
ATOM   5294  C  C   . ILE   B  1 240 ? -21.598 14.354  15.154   1.00 40.40  ? 541  ILE   B C   1 
ATOM   5295  O  O   . ILE   B  1 240 ? -20.519 14.721  14.646   1.00 41.79  ? 541  ILE   B O   1 
ATOM   5296  C  CB  . ILE   B  1 240 ? -23.281 14.243  13.296   1.00 43.01  ? 541  ILE   B CB  1 
ATOM   5297  C  CG1 . ILE   B  1 240 ? -24.508 14.895  12.667   1.00 41.68  ? 541  ILE   B CG1 1 
ATOM   5298  C  CG2 . ILE   B  1 240 ? -23.533 12.758  13.491   1.00 35.39  ? 541  ILE   B CG2 1 
ATOM   5299  C  CD1 . ILE   B  1 240 ? -24.873 14.274  11.372   1.00 40.17  ? 541  ILE   B CD1 1 
ATOM   5300  N  N   . PRO   B  1 241 ? -21.611 13.518  16.185   1.00 41.27  ? 542  PRO   B N   1 
ATOM   5301  C  CA  . PRO   B  1 241 ? -20.370 12.954  16.671   1.00 46.99  ? 542  PRO   B CA  1 
ATOM   5302  C  C   . PRO   B  1 241 ? -19.668 12.217  15.549   1.00 45.85  ? 542  PRO   B C   1 
ATOM   5303  O  O   . PRO   B  1 241 ? -20.270 11.360  14.878   1.00 40.21  ? 542  PRO   B O   1 
ATOM   5304  C  CB  . PRO   B  1 241 ? -20.818 12.004  17.794   1.00 50.86  ? 542  PRO   B CB  1 
ATOM   5305  C  CG  . PRO   B  1 241 ? -22.094 12.579  18.277   1.00 45.22  ? 542  PRO   B CG  1 
ATOM   5306  C  CD  . PRO   B  1 241 ? -22.758 13.162  17.041   1.00 46.96  ? 542  PRO   B CD  1 
ATOM   5307  N  N   . PRO   B  1 242 ? -18.402 12.555  15.303   1.00 48.05  ? 543  PRO   B N   1 
ATOM   5308  C  CA  . PRO   B  1 242 ? -17.708 12.035  14.118   1.00 45.35  ? 543  PRO   B CA  1 
ATOM   5309  C  C   . PRO   B  1 242 ? -17.635 10.524  14.090   1.00 59.55  ? 543  PRO   B C   1 
ATOM   5310  O  O   . PRO   B  1 242 ? -17.666 9.922   13.000   1.00 50.31  ? 543  PRO   B O   1 
ATOM   5311  C  CB  . PRO   B  1 242 ? -16.315 12.666  14.241   1.00 42.36  ? 543  PRO   B CB  1 
ATOM   5312  C  CG  . PRO   B  1 242 ? -16.493 13.827  15.177   1.00 45.13  ? 543  PRO   B CG  1 
ATOM   5313  C  CD  . PRO   B  1 242 ? -17.524 13.392  16.135   1.00 44.04  ? 543  PRO   B CD  1 
ATOM   5314  N  N   . GLU   B  1 243 ? -17.567 9.894   15.270   1.00 37.73  ? 544  GLU   B N   1 
ATOM   5315  C  CA  . GLU   B  1 243 ? -17.485 8.446   15.367   1.00 43.31  ? 544  GLU   B CA  1 
ATOM   5316  C  C   . GLU   B  1 243 ? -18.752 7.768   14.877   1.00 42.03  ? 544  GLU   B C   1 
ATOM   5317  O  O   . GLU   B  1 243 ? -18.760 6.543   14.715   1.00 43.09  ? 544  GLU   B O   1 
ATOM   5318  C  CB  . GLU   B  1 243 ? -17.180 8.023   16.823   1.00 40.06  ? 544  GLU   B CB  1 
ATOM   5319  C  CG  . GLU   B  1 243 ? -18.267 8.355   17.823   1.00 43.18  ? 544  GLU   B CG  1 
ATOM   5320  C  CD  . GLU   B  1 243 ? -18.045 9.693   18.491   1.00 50.50  ? 544  GLU   B CD  1 
ATOM   5321  O  OE1 . GLU   B  1 243 ? -17.238 10.474  17.952   1.00 51.91  ? 544  GLU   B OE1 1 
ATOM   5322  O  OE2 . GLU   B  1 243 ? -18.646 9.955   19.563   1.00 63.34  ? 544  GLU   B OE2 1 
ATOM   5323  N  N   . LEU   B  1 244 ? -19.818 8.532   14.664   1.00 45.62  ? 545  LEU   B N   1 
ATOM   5324  C  CA  . LEU   B  1 244 ? -21.032 8.029   14.051   1.00 33.78  ? 545  LEU   B CA  1 
ATOM   5325  C  C   . LEU   B  1 244 ? -21.064 8.231   12.541   1.00 41.69  ? 545  LEU   B C   1 
ATOM   5326  O  O   . LEU   B  1 244 ? -21.960 7.679   11.898   1.00 42.24  ? 545  LEU   B O   1 
ATOM   5327  C  CB  . LEU   B  1 244 ? -22.260 8.703   14.659   1.00 35.91  ? 545  LEU   B CB  1 
ATOM   5328  C  CG  . LEU   B  1 244 ? -22.547 8.536   16.154   1.00 40.24  ? 545  LEU   B CG  1 
ATOM   5329  C  CD1 . LEU   B  1 244 ? -23.757 9.356   16.515   1.00 37.90  ? 545  LEU   B CD1 1 
ATOM   5330  C  CD2 . LEU   B  1 244 ? -22.752 7.074   16.510   1.00 38.12  ? 545  LEU   B CD2 1 
ATOM   5331  N  N   . VAL   B  1 245 ? -20.128 8.997   11.972   1.00 36.64  ? 546  VAL   B N   1 
ATOM   5332  C  CA  . VAL   B  1 245 ? -20.142 9.343   10.536   1.00 44.91  ? 546  VAL   B CA  1 
ATOM   5333  C  C   . VAL   B  1 245 ? -19.083 8.486   9.854    1.00 34.02  ? 546  VAL   B C   1 
ATOM   5334  O  O   . VAL   B  1 245 ? -17.905 8.842   9.800    1.00 37.67  ? 546  VAL   B O   1 
ATOM   5335  C  CB  . VAL   B  1 245 ? -19.895 10.832  10.294   1.00 42.89  ? 546  VAL   B CB  1 
ATOM   5336  C  CG1 . VAL   B  1 245 ? -19.844 11.131  8.792    1.00 39.15  ? 546  VAL   B CG1 1 
ATOM   5337  C  CG2 . VAL   B  1 245 ? -20.972 11.663  10.965   1.00 48.59  ? 546  VAL   B CG2 1 
ATOM   5338  N  N   . LEU   B  1 246 ? -19.509 7.338   9.338    1.00 35.53  ? 547  LEU   B N   1 
ATOM   5339  C  CA  . LEU   B  1 246 ? -18.596 6.432   8.655    1.00 40.02  ? 547  LEU   B CA  1 
ATOM   5340  C  C   . LEU   B  1 246 ? -18.196 7.024   7.305    1.00 44.29  ? 547  LEU   B C   1 
ATOM   5341  O  O   . LEU   B  1 246 ? -19.046 7.521   6.569    1.00 46.19  ? 547  LEU   B O   1 
ATOM   5342  C  CB  . LEU   B  1 246 ? -19.261 5.071   8.464    1.00 37.89  ? 547  LEU   B CB  1 
ATOM   5343  C  CG  . LEU   B  1 246 ? -18.444 3.992   7.765    1.00 44.26  ? 547  LEU   B CG  1 
ATOM   5344  C  CD1 . LEU   B  1 246 ? -17.129 3.826   8.482    1.00 51.17  ? 547  LEU   B CD1 1 
ATOM   5345  C  CD2 . LEU   B  1 246 ? -19.217 2.704   7.786    1.00 45.13  ? 547  LEU   B CD2 1 
ATOM   5346  N  N   . GLU   B  1 247 ? -16.900 6.999   7.002    1.00 45.68  ? 548  GLU   B N   1 
ATOM   5347  C  CA  . GLU   B  1 247 ? -16.371 7.521   5.748    1.00 42.77  ? 548  GLU   B CA  1 
ATOM   5348  C  C   . GLU   B  1 247 ? -15.437 6.500   5.115    1.00 46.70  ? 548  GLU   B C   1 
ATOM   5349  O  O   . GLU   B  1 247 ? -14.769 5.726   5.807    1.00 56.68  ? 548  GLU   B O   1 
ATOM   5350  C  CB  . GLU   B  1 247 ? -15.622 8.838   5.952    1.00 44.92  ? 548  GLU   B CB  1 
ATOM   5351  C  CG  . GLU   B  1 247 ? -16.496 10.010  6.380    1.00 48.09  ? 548  GLU   B CG  1 
ATOM   5352  C  CD  . GLU   B  1 247 ? -15.683 11.256  6.650    1.00 51.58  ? 548  GLU   B CD  1 
ATOM   5353  O  OE1 . GLU   B  1 247 ? -14.684 11.161  7.390    1.00 58.83  ? 548  GLU   B OE1 1 
ATOM   5354  O  OE2 . GLU   B  1 247 ? -16.019 12.327  6.110    1.00 55.55  ? 548  GLU   B OE2 1 
ATOM   5355  N  N   . VAL   B  1 248 ? -15.386 6.515   3.788    1.00 47.07  ? 549  VAL   B N   1 
ATOM   5356  C  CA  . VAL   B  1 248 ? -14.591 5.576   3.014    1.00 47.13  ? 549  VAL   B CA  1 
ATOM   5357  C  C   . VAL   B  1 248 ? -13.572 6.384   2.221    1.00 57.40  ? 549  VAL   B C   1 
ATOM   5358  O  O   . VAL   B  1 248 ? -13.956 7.235   1.414    1.00 66.81  ? 549  VAL   B O   1 
ATOM   5359  C  CB  . VAL   B  1 248 ? -15.462 4.722   2.076    1.00 51.72  ? 549  VAL   B CB  1 
ATOM   5360  C  CG1 . VAL   B  1 248 ? -14.601 3.789   1.217    1.00 47.18  ? 549  VAL   B CG1 1 
ATOM   5361  C  CG2 . VAL   B  1 248 ? -16.497 3.926   2.878    1.00 47.47  ? 549  VAL   B CG2 1 
ATOM   5362  N  N   . PRO   B  1 249 ? -12.269 6.178   2.420    1.00 53.67  ? 550  PRO   B N   1 
ATOM   5363  C  CA  . PRO   B  1 249 ? -11.281 6.849   1.563    1.00 46.87  ? 550  PRO   B CA  1 
ATOM   5364  C  C   . PRO   B  1 249 ? -11.167 6.120   0.231    1.00 56.87  ? 550  PRO   B C   1 
ATOM   5365  O  O   . PRO   B  1 249 ? -11.056 4.892   0.193    1.00 65.36  ? 550  PRO   B O   1 
ATOM   5366  C  CB  . PRO   B  1 249 ? -9.983  6.759   2.371    1.00 48.26  ? 550  PRO   B CB  1 
ATOM   5367  C  CG  . PRO   B  1 249 ? -10.165 5.525   3.226    1.00 54.94  ? 550  PRO   B CG  1 
ATOM   5368  C  CD  . PRO   B  1 249 ? -11.641 5.412   3.516    1.00 55.06  ? 550  PRO   B CD  1 
ATOM   5369  N  N   . ILE   B  1 250 ? -11.207 6.876   -0.865   1.00 49.17  ? 551  ILE   B N   1 
ATOM   5370  C  CA  . ILE   B  1 250 ? -11.277 6.285   -2.201   1.00 49.34  ? 551  ILE   B CA  1 
ATOM   5371  C  C   . ILE   B  1 250 ? -9.869  6.000   -2.697   1.00 51.06  ? 551  ILE   B C   1 
ATOM   5372  O  O   . ILE   B  1 250 ? -9.047  6.914   -2.822   1.00 52.84  ? 551  ILE   B O   1 
ATOM   5373  C  CB  . ILE   B  1 250 ? -12.025 7.190   -3.196   1.00 49.20  ? 551  ILE   B CB  1 
ATOM   5374  C  CG1 . ILE   B  1 250 ? -13.337 7.718   -2.595   1.00 42.91  ? 551  ILE   B CG1 1 
ATOM   5375  C  CG2 . ILE   B  1 250 ? -12.277 6.422   -4.509   1.00 39.36  ? 551  ILE   B CG2 1 
ATOM   5376  C  CD1 . ILE   B  1 250 ? -14.278 6.644   -2.135   1.00 36.92  ? 551  ILE   B CD1 1 
ATOM   5377  N  N   . ARG   B  1 251 ? -9.604  4.733   -3.008   1.00 52.75  ? 552  ARG   B N   1 
ATOM   5378  C  CA  . ARG   B  1 251 ? -8.380  4.318   -3.683   1.00 56.05  ? 552  ARG   B CA  1 
ATOM   5379  C  C   . ARG   B  1 251 ? -8.728  3.425   -4.871   1.00 50.39  ? 552  ARG   B C   1 
ATOM   5380  O  O   . ARG   B  1 251 ? -9.864  2.966   -5.021   1.00 46.31  ? 552  ARG   B O   1 
ATOM   5381  C  CB  . ARG   B  1 251 ? -7.431  3.592   -2.724   1.00 59.83  ? 552  ARG   B CB  1 
ATOM   5382  C  CG  . ARG   B  1 251 ? -8.041  2.404   -2.048   1.00 60.00  ? 552  ARG   B CG  1 
ATOM   5383  C  CD  . ARG   B  1 251 ? -8.737  2.798   -0.759   1.00 58.19  ? 552  ARG   B CD  1 
ATOM   5384  N  NE  . ARG   B  1 251 ? -9.070  1.615   0.023    1.00 61.84  ? 552  ARG   B NE  1 
ATOM   5385  C  CZ  . ARG   B  1 251 ? -9.943  1.599   1.024    1.00 57.72  ? 552  ARG   B CZ  1 
ATOM   5386  N  NH1 . ARG   B  1 251 ? -10.179 0.466   1.663    1.00 59.68  ? 552  ARG   B NH1 1 
ATOM   5387  N  NH2 . ARG   B  1 251 ? -10.591 2.702   1.370    1.00 52.73  ? 552  ARG   B NH2 1 
ATOM   5388  N  N   . HIS   B  1 252 ? -7.719  3.161   -5.723   1.00 50.17  ? 553  HIS   B N   1 
ATOM   5389  C  CA  . HIS   B  1 252 ? -7.956  2.420   -6.956   1.00 50.92  ? 553  HIS   B CA  1 
ATOM   5390  C  C   . HIS   B  1 252 ? -7.189  1.109   -6.955   1.00 56.21  ? 553  HIS   B C   1 
ATOM   5391  O  O   . HIS   B  1 252 ? -6.027  1.068   -6.533   1.00 63.43  ? 553  HIS   B O   1 
ATOM   5392  C  CB  . HIS   B  1 252 ? -7.541  3.227   -8.186   1.00 47.28  ? 553  HIS   B CB  1 
ATOM   5393  C  CG  . HIS   B  1 252 ? -8.084  2.690   -9.470   1.00 59.97  ? 553  HIS   B CG  1 
ATOM   5394  N  ND1 . HIS   B  1 252 ? -7.425  1.736   -10.215  1.00 63.97  ? 553  HIS   B ND1 1 
ATOM   5395  C  CD2 . HIS   B  1 252 ? -9.219  2.981   -10.147  1.00 57.81  ? 553  HIS   B CD2 1 
ATOM   5396  C  CE1 . HIS   B  1 252 ? -8.132  1.460   -11.295  1.00 61.30  ? 553  HIS   B CE1 1 
ATOM   5397  N  NE2 . HIS   B  1 252 ? -9.228  2.198   -11.275  1.00 60.53  ? 553  HIS   B NE2 1 
ATOM   5398  N  N   . PRO   B  1 253 ? -7.813  0.024   -7.417   1.00 49.87  ? 554  PRO   B N   1 
ATOM   5399  C  CA  . PRO   B  1 253 ? -7.162  -1.292  -7.337   1.00 51.47  ? 554  PRO   B CA  1 
ATOM   5400  C  C   . PRO   B  1 253 ? -5.933  -1.442  -8.217   1.00 58.30  ? 554  PRO   B C   1 
ATOM   5401  O  O   . PRO   B  1 253 ? -5.174  -2.394  -8.003   1.00 61.13  ? 554  PRO   B O   1 
ATOM   5402  C  CB  . PRO   B  1 253 ? -8.275  -2.267  -7.758   1.00 54.54  ? 554  PRO   B CB  1 
ATOM   5403  C  CG  . PRO   B  1 253 ? -9.330  -1.425  -8.393   1.00 58.28  ? 554  PRO   B CG  1 
ATOM   5404  C  CD  . PRO   B  1 253 ? -9.240  -0.074  -7.761   1.00 46.35  ? 554  PRO   B CD  1 
ATOM   5405  N  N   . LYS   B  1 254 ? -5.704  -0.550  -9.184   1.00 65.06  ? 555  LYS   B N   1 
ATOM   5406  C  CA  . LYS   B  1 254 ? -4.532  -0.598  -10.057  1.00 67.71  ? 555  LYS   B CA  1 
ATOM   5407  C  C   . LYS   B  1 254 ? -3.718  0.685   -10.036  1.00 66.46  ? 555  LYS   B C   1 
ATOM   5408  O  O   . LYS   B  1 254 ? -2.485  0.635   -10.022  1.00 68.08  ? 555  LYS   B O   1 
ATOM   5409  C  CB  . LYS   B  1 254 ? -4.946  -0.907  -11.510  1.00 76.56  ? 555  LYS   B CB  1 
ATOM   5410  C  CG  . LYS   B  1 254 ? -5.014  -2.395  -11.836  1.00 85.41  ? 555  LYS   B CG  1 
ATOM   5411  C  CD  . LYS   B  1 254 ? -3.862  -3.164  -11.173  1.00 93.16  ? 555  LYS   B CD  1 
ATOM   5412  C  CE  . LYS   B  1 254 ? -3.194  -4.141  -12.129  1.00 93.99  ? 555  LYS   B CE  1 
ATOM   5413  N  NZ  . LYS   B  1 254 ? -4.167  -5.098  -12.726  1.00 93.13  ? 555  LYS   B NZ  1 
ATOM   5414  N  N   . PHE   B  1 255 ? -4.382  1.834   -10.035  1.00 68.63  ? 556  PHE   B N   1 
ATOM   5415  C  CA  . PHE   B  1 255 ? -3.724  3.136   -10.043  1.00 66.76  ? 556  PHE   B CA  1 
ATOM   5416  C  C   . PHE   B  1 255 ? -3.332  3.475   -8.616   1.00 65.80  ? 556  PHE   B C   1 
ATOM   5417  O  O   . PHE   B  1 255 ? -4.156  3.951   -7.831   1.00 61.19  ? 556  PHE   B O   1 
ATOM   5418  C  CB  . PHE   B  1 255 ? -4.650  4.203   -10.618  1.00 67.65  ? 556  PHE   B CB  1 
ATOM   5419  C  CG  . PHE   B  1 255 ? -5.074  3.948   -12.039  1.00 61.21  ? 556  PHE   B CG  1 
ATOM   5420  C  CD1 . PHE   B  1 255 ? -4.246  3.266   -12.906  1.00 59.77  ? 556  PHE   B CD1 1 
ATOM   5421  C  CD2 . PHE   B  1 255 ? -6.303  4.400   -12.503  1.00 61.64  ? 556  PHE   B CD2 1 
ATOM   5422  C  CE1 . PHE   B  1 255 ? -4.633  3.034   -14.216  1.00 58.70  ? 556  PHE   B CE1 1 
ATOM   5423  C  CE2 . PHE   B  1 255 ? -6.699  4.179   -13.803  1.00 51.67  ? 556  PHE   B CE2 1 
ATOM   5424  C  CZ  . PHE   B  1 255 ? -5.861  3.492   -14.662  1.00 56.51  ? 556  PHE   B CZ  1 
ATOM   5425  N  N   . GLU   B  1 256 ? -2.066  3.230   -8.278   1.00 72.30  ? 557  GLU   B N   1 
ATOM   5426  C  CA  . GLU   B  1 256 ? -1.569  3.564   -6.950   1.00 75.97  ? 557  GLU   B CA  1 
ATOM   5427  C  C   . GLU   B  1 256 ? -1.631  5.055   -6.677   1.00 78.44  ? 557  GLU   B C   1 
ATOM   5428  O  O   . GLU   B  1 256 ? -1.676  5.461   -5.511   1.00 85.77  ? 557  GLU   B O   1 
ATOM   5429  C  CB  . GLU   B  1 256 ? -0.137  3.068   -6.785   1.00 81.70  ? 557  GLU   B CB  1 
ATOM   5430  C  CG  . GLU   B  1 256 ? -0.009  1.572   -6.913   1.00 91.39  ? 557  GLU   B CG  1 
ATOM   5431  C  CD  . GLU   B  1 256 ? 1.084   1.017   -6.042   1.00 104.68 ? 557  GLU   B CD  1 
ATOM   5432  O  OE1 . GLU   B  1 256 ? 1.904   1.813   -5.540   1.00 110.48 ? 557  GLU   B OE1 1 
ATOM   5433  O  OE2 . GLU   B  1 256 ? 1.115   -0.214  -5.850   1.00 110.16 ? 557  GLU   B OE2 1 
ATOM   5434  N  N   . TRP   B  1 257 ? -1.640  5.877   -7.720   1.00 69.99  ? 558  TRP   B N   1 
ATOM   5435  C  CA  . TRP   B  1 257 ? -1.720  7.316   -7.550   1.00 65.45  ? 558  TRP   B CA  1 
ATOM   5436  C  C   . TRP   B  1 257 ? -3.119  7.794   -7.204   1.00 63.76  ? 558  TRP   B C   1 
ATOM   5437  O  O   . TRP   B  1 257 ? -3.277  8.960   -6.822   1.00 69.84  ? 558  TRP   B O   1 
ATOM   5438  C  CB  . TRP   B  1 257 ? -1.252  8.014   -8.826   1.00 71.54  ? 558  TRP   B CB  1 
ATOM   5439  C  CG  . TRP   B  1 257 ? -1.916  7.505   -10.068  1.00 69.72  ? 558  TRP   B CG  1 
ATOM   5440  C  CD1 . TRP   B  1 257 ? -1.418  6.588   -10.950  1.00 75.23  ? 558  TRP   B CD1 1 
ATOM   5441  C  CD2 . TRP   B  1 257 ? -3.195  7.889   -10.570  1.00 63.46  ? 558  TRP   B CD2 1 
ATOM   5442  N  NE1 . TRP   B  1 257 ? -2.311  6.377   -11.971  1.00 73.42  ? 558  TRP   B NE1 1 
ATOM   5443  C  CE2 . TRP   B  1 257 ? -3.409  7.168   -11.764  1.00 66.78  ? 558  TRP   B CE2 1 
ATOM   5444  C  CE3 . TRP   B  1 257 ? -4.177  8.781   -10.135  1.00 61.24  ? 558  TRP   B CE3 1 
ATOM   5445  C  CZ2 . TRP   B  1 257 ? -4.567  7.303   -12.517  1.00 68.14  ? 558  TRP   B CZ2 1 
ATOM   5446  C  CZ3 . TRP   B  1 257 ? -5.334  8.911   -10.883  1.00 60.96  ? 558  TRP   B CZ3 1 
ATOM   5447  C  CH2 . TRP   B  1 257 ? -5.518  8.179   -12.062  1.00 64.80  ? 558  TRP   B CH2 1 
ATOM   5448  N  N   . PHE   B  1 258 ? -4.135  6.941   -7.343   1.00 56.54  ? 559  PHE   B N   1 
ATOM   5449  C  CA  . PHE   B  1 258 ? -5.491  7.397   -7.070   1.00 59.11  ? 559  PHE   B CA  1 
ATOM   5450  C  C   . PHE   B  1 258 ? -5.647  7.831   -5.619   1.00 58.36  ? 559  PHE   B C   1 
ATOM   5451  O  O   . PHE   B  1 258 ? -6.256  8.869   -5.341   1.00 56.99  ? 559  PHE   B O   1 
ATOM   5452  C  CB  . PHE   B  1 258 ? -6.508  6.313   -7.396   1.00 57.15  ? 559  PHE   B CB  1 
ATOM   5453  C  CG  . PHE   B  1 258 ? -7.849  6.860   -7.761   1.00 59.20  ? 559  PHE   B CG  1 
ATOM   5454  C  CD1 . PHE   B  1 258 ? -8.694  7.380   -6.788   1.00 51.84  ? 559  PHE   B CD1 1 
ATOM   5455  C  CD2 . PHE   B  1 258 ? -8.252  6.901   -9.087   1.00 61.45  ? 559  PHE   B CD2 1 
ATOM   5456  C  CE1 . PHE   B  1 258 ? -9.923  7.916   -7.130   1.00 52.41  ? 559  PHE   B CE1 1 
ATOM   5457  C  CE2 . PHE   B  1 258 ? -9.479  7.423   -9.435   1.00 64.37  ? 559  PHE   B CE2 1 
ATOM   5458  C  CZ  . PHE   B  1 258 ? -10.322 7.930   -8.456   1.00 58.13  ? 559  PHE   B CZ  1 
ATOM   5459  N  N   . LYS   B  1 259 ? -5.107  7.053   -4.681   1.00 60.03  ? 560  LYS   B N   1 
ATOM   5460  C  CA  . LYS   B  1 259 ? -5.250  7.423   -3.275   1.00 67.19  ? 560  LYS   B CA  1 
ATOM   5461  C  C   . LYS   B  1 259 ? -4.751  8.841   -3.033   1.00 69.95  ? 560  LYS   B C   1 
ATOM   5462  O  O   . LYS   B  1 259 ? -5.333  9.574   -2.226   1.00 49.89  ? 560  LYS   B O   1 
ATOM   5463  C  CB  . LYS   B  1 259 ? -4.507  6.425   -2.382   1.00 71.13  ? 560  LYS   B CB  1 
ATOM   5464  C  CG  . LYS   B  1 259 ? -3.016  6.302   -2.676   1.00 75.41  ? 560  LYS   B CG  1 
ATOM   5465  C  CD  . LYS   B  1 259 ? -2.333  5.340   -1.717   1.00 74.58  ? 560  LYS   B CD  1 
ATOM   5466  C  CE  . LYS   B  1 259 ? -0.829  5.318   -1.933   1.00 77.55  ? 560  LYS   B CE  1 
ATOM   5467  N  NZ  . LYS   B  1 259 ? -0.421  4.682   -3.219   1.00 71.24  ? 560  LYS   B NZ  1 
ATOM   5468  N  N   . ASP   B  1 260 ? -3.728  9.267   -3.781   1.00 63.56  ? 561  ASP   B N   1 
ATOM   5469  C  CA  . ASP   B  1 260 ? -3.126  10.580  -3.594   1.00 63.84  ? 561  ASP   B CA  1 
ATOM   5470  C  C   . ASP   B  1 260 ? -4.029  11.721  -4.042   1.00 59.12  ? 561  ASP   B C   1 
ATOM   5471  O  O   . ASP   B  1 260 ? -3.702  12.880  -3.769   1.00 66.31  ? 561  ASP   B O   1 
ATOM   5472  C  CB  . ASP   B  1 260 ? -1.789  10.642  -4.329   1.00 79.81  ? 561  ASP   B CB  1 
ATOM   5473  C  CG  . ASP   B  1 260 ? -0.886  9.475   -3.984   1.00 90.43  ? 561  ASP   B CG  1 
ATOM   5474  O  OD1 . ASP   B  1 260 ? -1.060  8.910   -2.879   1.00 89.77  ? 561  ASP   B OD1 1 
ATOM   5475  O  OD2 . ASP   B  1 260 ? -0.013  9.123   -4.817   1.00 96.02  ? 561  ASP   B OD2 1 
ATOM   5476  N  N   . LEU   B  1 261 ? -5.149  11.433  -4.712   1.00 56.77  ? 562  LEU   B N   1 
ATOM   5477  C  CA  . LEU   B  1 261 ? -6.126  12.480  -5.002   1.00 62.67  ? 562  LEU   B CA  1 
ATOM   5478  C  C   . LEU   B  1 261 ? -6.813  12.973  -3.735   1.00 62.98  ? 562  LEU   B C   1 
ATOM   5479  O  O   . LEU   B  1 261 ? -7.486  14.009  -3.772   1.00 63.93  ? 562  LEU   B O   1 
ATOM   5480  C  CB  . LEU   B  1 261 ? -7.178  11.983  -6.007   1.00 47.70  ? 562  LEU   B CB  1 
ATOM   5481  C  CG  . LEU   B  1 261 ? -6.720  11.562  -7.411   1.00 59.12  ? 562  LEU   B CG  1 
ATOM   5482  C  CD1 . LEU   B  1 261 ? -7.830  10.818  -8.185   1.00 54.33  ? 562  LEU   B CD1 1 
ATOM   5483  C  CD2 . LEU   B  1 261 ? -6.251  12.764  -8.215   1.00 62.02  ? 562  LEU   B CD2 1 
ATOM   5484  N  N   . GLY   B  1 262 ? -6.657  12.250  -2.629   1.00 59.70  ? 563  GLY   B N   1 
ATOM   5485  C  CA  . GLY   B  1 262 ? -7.203  12.660  -1.346   1.00 66.55  ? 563  GLY   B CA  1 
ATOM   5486  C  C   . GLY   B  1 262 ? -8.710  12.752  -1.333   1.00 66.21  ? 563  GLY   B C   1 
ATOM   5487  O  O   . GLY   B  1 262 ? -9.268  13.697  -0.763   1.00 70.42  ? 563  GLY   B O   1 
ATOM   5488  N  N   . LEU   B  1 263 ? -9.381  11.797  -1.964   1.00 61.47  ? 564  LEU   B N   1 
ATOM   5489  C  CA  . LEU   B  1 263 ? -10.829 11.777  -2.044   1.00 56.79  ? 564  LEU   B CA  1 
ATOM   5490  C  C   . LEU   B  1 263 ? -11.403 10.803  -1.021   1.00 50.46  ? 564  LEU   B C   1 
ATOM   5491  O  O   . LEU   B  1 263 ? -10.848 9.723   -0.792   1.00 48.94  ? 564  LEU   B O   1 
ATOM   5492  C  CB  . LEU   B  1 263 ? -11.288 11.382  -3.451   1.00 57.04  ? 564  LEU   B CB  1 
ATOM   5493  C  CG  . LEU   B  1 263 ? -10.958 12.377  -4.561   1.00 62.62  ? 564  LEU   B CG  1 
ATOM   5494  C  CD1 . LEU   B  1 263 ? -11.369 11.809  -5.905   1.00 61.82  ? 564  LEU   B CD1 1 
ATOM   5495  C  CD2 . LEU   B  1 263 ? -11.644 13.707  -4.318   1.00 64.16  ? 564  LEU   B CD2 1 
ATOM   5496  N  N   . LYS   B  1 264 ? -12.527 11.189  -0.421   1.00 50.19  ? 565  LYS   B N   1 
ATOM   5497  C  CA  . LYS   B  1 264 ? -13.326 10.285  0.392    1.00 49.46  ? 565  LYS   B CA  1 
ATOM   5498  C  C   . LYS   B  1 264 ? -14.795 10.610  0.173    1.00 52.21  ? 565  LYS   B C   1 
ATOM   5499  O  O   . LYS   B  1 264 ? -15.143 11.679  -0.335   1.00 61.46  ? 565  LYS   B O   1 
ATOM   5500  C  CB  . LYS   B  1 264 ? -12.971 10.382  1.883    1.00 41.89  ? 565  LYS   B CB  1 
ATOM   5501  C  CG  . LYS   B  1 264 ? -13.145 11.757  2.486    1.00 54.52  ? 565  LYS   B CG  1 
ATOM   5502  C  CD  . LYS   B  1 264 ? -12.814 11.751  3.997    1.00 62.56  ? 565  LYS   B CD  1 
ATOM   5503  C  CE  . LYS   B  1 264 ? -12.498 13.155  4.495    1.00 69.27  ? 565  LYS   B CE  1 
ATOM   5504  N  NZ  . LYS   B  1 264 ? -11.768 13.142  5.792    1.00 76.23  ? 565  LYS   B NZ  1 
ATOM   5505  N  N   . TRP   B  1 265 ? -15.659 9.664   0.537    1.00 39.60  ? 566  TRP   B N   1 
ATOM   5506  C  CA  . TRP   B  1 265 ? -17.087 9.922   0.617    1.00 34.89  ? 566  TRP   B CA  1 
ATOM   5507  C  C   . TRP   B  1 265 ? -17.608 9.266   1.889    1.00 44.84  ? 566  TRP   B C   1 
ATOM   5508  O  O   . TRP   B  1 265 ? -16.896 8.502   2.551    1.00 49.52  ? 566  TRP   B O   1 
ATOM   5509  C  CB  . TRP   B  1 265 ? -17.845 9.415   -0.622   1.00 33.43  ? 566  TRP   B CB  1 
ATOM   5510  C  CG  . TRP   B  1 265 ? -19.137 10.167  -0.857   1.00 35.75  ? 566  TRP   B CG  1 
ATOM   5511  C  CD1 . TRP   B  1 265 ? -20.410 9.691   -0.683   1.00 38.32  ? 566  TRP   B CD1 1 
ATOM   5512  C  CD2 . TRP   B  1 265 ? -19.276 11.535  -1.279   1.00 38.21  ? 566  TRP   B CD2 1 
ATOM   5513  N  NE1 . TRP   B  1 265 ? -21.331 10.673  -0.989   1.00 39.69  ? 566  TRP   B NE1 1 
ATOM   5514  C  CE2 . TRP   B  1 265 ? -20.661 11.813  -1.354   1.00 37.54  ? 566  TRP   B CE2 1 
ATOM   5515  C  CE3 . TRP   B  1 265 ? -18.367 12.545  -1.607   1.00 36.77  ? 566  TRP   B CE3 1 
ATOM   5516  C  CZ2 . TRP   B  1 265 ? -21.153 13.059  -1.740   1.00 31.74  ? 566  TRP   B CZ2 1 
ATOM   5517  C  CZ3 . TRP   B  1 265 ? -18.859 13.785  -1.972   1.00 41.23  ? 566  TRP   B CZ3 1 
ATOM   5518  C  CH2 . TRP   B  1 265 ? -20.238 14.030  -2.037   1.00 39.76  ? 566  TRP   B CH2 1 
ATOM   5519  N  N   . TYR   B  1 266 ? -18.849 9.587   2.246    1.00 38.66  ? 567  TYR   B N   1 
ATOM   5520  C  CA  . TYR   B  1 266 ? -19.464 9.001   3.430    1.00 44.30  ? 567  TYR   B CA  1 
ATOM   5521  C  C   . TYR   B  1 266 ? -20.263 7.763   3.046    1.00 48.70  ? 567  TYR   B C   1 
ATOM   5522  O  O   . TYR   B  1 266 ? -20.637 7.568   1.884    1.00 41.49  ? 567  TYR   B O   1 
ATOM   5523  C  CB  . TYR   B  1 266 ? -20.363 10.015  4.146    1.00 40.54  ? 567  TYR   B CB  1 
ATOM   5524  C  CG  . TYR   B  1 266 ? -21.286 10.768  3.212    1.00 41.66  ? 567  TYR   B CG  1 
ATOM   5525  C  CD1 . TYR   B  1 266 ? -20.889 11.956  2.616    1.00 40.31  ? 567  TYR   B CD1 1 
ATOM   5526  C  CD2 . TYR   B  1 266 ? -22.552 10.285  2.926    1.00 49.08  ? 567  TYR   B CD2 1 
ATOM   5527  C  CE1 . TYR   B  1 266 ? -21.738 12.648  1.760    1.00 47.15  ? 567  TYR   B CE1 1 
ATOM   5528  C  CE2 . TYR   B  1 266 ? -23.404 10.961  2.079    1.00 51.43  ? 567  TYR   B CE2 1 
ATOM   5529  C  CZ  . TYR   B  1 266 ? -22.997 12.140  1.492    1.00 50.87  ? 567  TYR   B CZ  1 
ATOM   5530  O  OH  . TYR   B  1 266 ? -23.860 12.807  0.646    1.00 51.18  ? 567  TYR   B OH  1 
ATOM   5531  N  N   . GLY   B  1 267 ? -20.526 6.921   4.046    1.00 45.22  ? 568  GLY   B N   1 
ATOM   5532  C  CA  . GLY   B  1 267 ? -21.166 5.646   3.795    1.00 33.02  ? 568  GLY   B CA  1 
ATOM   5533  C  C   . GLY   B  1 267 ? -22.679 5.662   3.786    1.00 33.66  ? 568  GLY   B C   1 
ATOM   5534  O  O   . GLY   B  1 267 ? -23.300 4.770   3.198    1.00 31.52  ? 568  GLY   B O   1 
ATOM   5535  N  N   . LEU   B  1 268 ? -23.297 6.659   4.419    1.00 35.49  ? 569  LEU   B N   1 
ATOM   5536  C  CA  . LEU   B  1 268 ? -24.726 6.576   4.686    1.00 35.00  ? 569  LEU   B CA  1 
ATOM   5537  C  C   . LEU   B  1 268 ? -25.496 7.638   3.909    1.00 35.37  ? 569  LEU   B C   1 
ATOM   5538  O  O   . LEU   B  1 268 ? -25.435 8.828   4.268    1.00 30.26  ? 569  LEU   B O   1 
ATOM   5539  C  CB  . LEU   B  1 268 ? -24.992 6.709   6.193    1.00 38.06  ? 569  LEU   B CB  1 
ATOM   5540  C  CG  . LEU   B  1 268 ? -26.456 6.547   6.590    1.00 40.42  ? 569  LEU   B CG  1 
ATOM   5541  C  CD1 . LEU   B  1 268 ? -26.924 5.139   6.294    1.00 45.67  ? 569  LEU   B CD1 1 
ATOM   5542  C  CD2 . LEU   B  1 268 ? -26.687 6.874   8.042    1.00 45.77  ? 569  LEU   B CD2 1 
ATOM   5543  N  N   . PRO   B  1 269 ? -26.250 7.269   2.845    1.00 34.03  ? 570  PRO   B N   1 
ATOM   5544  C  CA  . PRO   B  1 269 ? -27.103 8.262   2.179    1.00 32.84  ? 570  PRO   B CA  1 
ATOM   5545  C  C   . PRO   B  1 269 ? -28.424 8.375   2.915    1.00 27.33  ? 570  PRO   B C   1 
ATOM   5546  O  O   . PRO   B  1 269 ? -29.174 7.397   3.001    1.00 28.23  ? 570  PRO   B O   1 
ATOM   5547  C  CB  . PRO   B  1 269 ? -27.273 7.691   0.759    1.00 26.41  ? 570  PRO   B CB  1 
ATOM   5548  C  CG  . PRO   B  1 269 ? -27.227 6.181   0.954    1.00 37.55  ? 570  PRO   B CG  1 
ATOM   5549  C  CD  . PRO   B  1 269 ? -26.374 5.933   2.230    1.00 39.04  ? 570  PRO   B CD  1 
ATOM   5550  N  N   . ALA   B  1 270 ? -28.731 9.544   3.459    1.00 31.81  ? 571  ALA   B N   1 
ATOM   5551  C  CA  . ALA   B  1 270 ? -29.902 9.686   4.322    1.00 31.89  ? 571  ALA   B CA  1 
ATOM   5552  C  C   . ALA   B  1 270 ? -30.688 10.922  3.903    1.00 34.74  ? 571  ALA   B C   1 
ATOM   5553  O  O   . ALA   B  1 270 ? -30.340 12.042  4.290    1.00 42.39  ? 571  ALA   B O   1 
ATOM   5554  C  CB  . ALA   B  1 270 ? -29.480 9.752   5.794    1.00 28.64  ? 571  ALA   B CB  1 
ATOM   5555  N  N   . VAL   B  1 271 ? -31.759 10.731  3.131    1.00 36.29  ? 572  VAL   B N   1 
ATOM   5556  C  CA  . VAL   B  1 271 ? -32.481 11.866  2.560    1.00 30.73  ? 572  VAL   B CA  1 
ATOM   5557  C  C   . VAL   B  1 271 ? -33.365 12.477  3.638    1.00 34.21  ? 572  VAL   B C   1 
ATOM   5558  O  O   . VAL   B  1 271 ? -34.144 11.772  4.287    1.00 35.91  ? 572  VAL   B O   1 
ATOM   5559  C  CB  . VAL   B  1 271 ? -33.309 11.434  1.339    1.00 27.42  ? 572  VAL   B CB  1 
ATOM   5560  C  CG1 . VAL   B  1 271 ? -34.219 12.568  0.920    1.00 27.03  ? 572  VAL   B CG1 1 
ATOM   5561  C  CG2 . VAL   B  1 271 ? -32.395 11.057  0.159    1.00 29.20  ? 572  VAL   B CG2 1 
ATOM   5562  N  N   . SER   B  1 272 ? -33.255 13.798  3.832    1.00 35.89  ? 573  SER   B N   1 
ATOM   5563  C  CA  . SER   B  1 272 ? -33.873 14.425  4.995    1.00 35.45  ? 573  SER   B CA  1 
ATOM   5564  C  C   . SER   B  1 272 ? -34.694 15.667  4.681    1.00 36.93  ? 573  SER   B C   1 
ATOM   5565  O  O   . SER   B  1 272 ? -35.117 16.358  5.614    1.00 39.63  ? 573  SER   B O   1 
ATOM   5566  C  CB  . SER   B  1 272 ? -32.815 14.769  6.054    1.00 29.83  ? 573  SER   B CB  1 
ATOM   5567  O  OG  . SER   B  1 272 ? -31.915 15.779  5.622    1.00 29.89  ? 573  SER   B OG  1 
ATOM   5568  N  N   . ASN   B  1 273 ? -34.958 15.968  3.411    1.00 45.69  ? 574  ASN   B N   1 
ATOM   5569  C  CA  . ASN   B  1 273 ? -35.752 17.145  3.075    1.00 42.85  ? 574  ASN   B CA  1 
ATOM   5570  C  C   . ASN   B  1 273 ? -37.099 16.799  2.468    1.00 31.47  ? 574  ASN   B C   1 
ATOM   5571  O  O   . ASN   B  1 273 ? -37.793 17.692  1.987    1.00 34.63  ? 574  ASN   B O   1 
ATOM   5572  C  CB  . ASN   B  1 273 ? -34.986 18.064  2.125    1.00 45.99  ? 574  ASN   B CB  1 
ATOM   5573  C  CG  . ASN   B  1 273 ? -34.529 17.360  0.864    1.00 43.23  ? 574  ASN   B CG  1 
ATOM   5574  O  OD1 . ASN   B  1 273 ? -34.851 16.199  0.625    1.00 46.01  ? 574  ASN   B OD1 1 
ATOM   5575  N  ND2 . ASN   B  1 273 ? -33.758 18.065  0.055    1.00 39.54  ? 574  ASN   B ND2 1 
ATOM   5576  N  N   . MET   B  1 274 ? -37.495 15.538  2.474    1.00 34.39  ? 575  MET   B N   1 
ATOM   5577  C  CA  . MET   B  1 274 ? -38.721 15.166  1.788    1.00 36.43  ? 575  MET   B CA  1 
ATOM   5578  C  C   . MET   B  1 274 ? -39.872 15.071  2.781    1.00 41.82  ? 575  MET   B C   1 
ATOM   5579  O  O   . MET   B  1 274 ? -39.670 15.006  3.992    1.00 39.62  ? 575  MET   B O   1 
ATOM   5580  C  CB  . MET   B  1 274 ? -38.528 13.853  1.020    1.00 31.63  ? 575  MET   B CB  1 
ATOM   5581  C  CG  . MET   B  1 274 ? -37.807 14.074  -0.326   1.00 35.35  ? 575  MET   B CG  1 
ATOM   5582  S  SD  . MET   B  1 274 ? -37.709 12.605  -1.363   1.00 44.59  ? 575  MET   B SD  1 
ATOM   5583  C  CE  . MET   B  1 274 ? -39.214 12.746  -2.339   1.00 33.30  ? 575  MET   B CE  1 
ATOM   5584  N  N   . LEU   B  1 275 ? -41.089 15.107  2.245    1.00 32.95  ? 576  LEU   B N   1 
ATOM   5585  C  CA  . LEU   B  1 275 ? -42.316 15.055  3.020    1.00 30.38  ? 576  LEU   B CA  1 
ATOM   5586  C  C   . LEU   B  1 275 ? -42.957 13.689  2.833    1.00 33.78  ? 576  LEU   B C   1 
ATOM   5587  O  O   . LEU   B  1 275 ? -43.013 13.177  1.718    1.00 41.35  ? 576  LEU   B O   1 
ATOM   5588  C  CB  . LEU   B  1 275 ? -43.279 16.169  2.586    1.00 37.69  ? 576  LEU   B CB  1 
ATOM   5589  C  CG  . LEU   B  1 275 ? -44.625 16.328  3.299    1.00 42.33  ? 576  LEU   B CG  1 
ATOM   5590  C  CD1 . LEU   B  1 275 ? -45.126 17.748  3.168    1.00 41.81  ? 576  LEU   B CD1 1 
ATOM   5591  C  CD2 . LEU   B  1 275 ? -45.669 15.359  2.745    1.00 36.72  ? 576  LEU   B CD2 1 
ATOM   5592  N  N   . LEU   B  1 276 ? -43.433 13.097  3.918    1.00 32.25  ? 577  LEU   B N   1 
ATOM   5593  C  CA  . LEU   B  1 276 ? -44.101 11.806  3.879    1.00 30.66  ? 577  LEU   B CA  1 
ATOM   5594  C  C   . LEU   B  1 276 ? -45.577 12.016  4.175    1.00 34.08  ? 577  LEU   B C   1 
ATOM   5595  O  O   . LEU   B  1 276 ? -45.934 12.568  5.223    1.00 43.36  ? 577  LEU   B O   1 
ATOM   5596  C  CB  . LEU   B  1 276 ? -43.470 10.825  4.870    1.00 33.97  ? 577  LEU   B CB  1 
ATOM   5597  C  CG  . LEU   B  1 276 ? -44.294 9.605   5.287    1.00 35.28  ? 577  LEU   B CG  1 
ATOM   5598  C  CD1 . LEU   B  1 276 ? -44.464 8.642   4.142    1.00 35.73  ? 577  LEU   B CD1 1 
ATOM   5599  C  CD2 . LEU   B  1 276 ? -43.662 8.895   6.493    1.00 27.35  ? 577  LEU   B CD2 1 
ATOM   5600  N  N   . GLU   B  1 277 ? -46.425 11.573  3.253    1.00 38.01  ? 578  GLU   B N   1 
ATOM   5601  C  CA  . GLU   B  1 277 ? -47.862 11.795  3.308    1.00 38.65  ? 578  GLU   B CA  1 
ATOM   5602  C  C   . GLU   B  1 277 ? -48.556 10.452  3.502    1.00 43.17  ? 578  GLU   B C   1 
ATOM   5603  O  O   . GLU   B  1 277 ? -48.379 9.535   2.689    1.00 31.25  ? 578  GLU   B O   1 
ATOM   5604  C  CB  . GLU   B  1 277 ? -48.347 12.493  2.033    1.00 47.13  ? 578  GLU   B CB  1 
ATOM   5605  C  CG  . GLU   B  1 277 ? -49.820 12.851  2.033    1.00 53.83  ? 578  GLU   B CG  1 
ATOM   5606  C  CD  . GLU   B  1 277 ? -50.653 11.790  1.357    1.00 65.46  ? 578  GLU   B CD  1 
ATOM   5607  O  OE1 . GLU   B  1 277 ? -50.070 10.988  0.594    1.00 70.01  ? 578  GLU   B OE1 1 
ATOM   5608  O  OE2 . GLU   B  1 277 ? -51.878 11.746  1.587    1.00 65.42  ? 578  GLU   B OE2 1 
ATOM   5609  N  N   . ILE   B  1 278 ? -49.327 10.331  4.592    1.00 39.24  ? 579  ILE   B N   1 
ATOM   5610  C  CA  . ILE   B  1 278 ? -50.099 9.126   4.884    1.00 37.70  ? 579  ILE   B CA  1 
ATOM   5611  C  C   . ILE   B  1 278 ? -51.508 9.543   5.290    1.00 43.09  ? 579  ILE   B C   1 
ATOM   5612  O  O   . ILE   B  1 278 ? -51.681 10.335  6.223    1.00 42.15  ? 579  ILE   B O   1 
ATOM   5613  C  CB  . ILE   B  1 278 ? -49.449 8.279   5.987    1.00 38.66  ? 579  ILE   B CB  1 
ATOM   5614  C  CG1 . ILE   B  1 278 ? -48.012 7.938   5.609    1.00 36.93  ? 579  ILE   B CG1 1 
ATOM   5615  C  CG2 . ILE   B  1 278 ? -50.257 7.041   6.229    1.00 32.78  ? 579  ILE   B CG2 1 
ATOM   5616  C  CD1 . ILE   B  1 278 ? -47.212 7.368   6.729    1.00 36.16  ? 579  ILE   B CD1 1 
ATOM   5617  N  N   . GLY   B  1 279 ? -52.505 9.027   4.581    1.00 42.87  ? 580  GLY   B N   1 
ATOM   5618  C  CA  . GLY   B  1 279 ? -53.901 9.344   4.813    1.00 40.10  ? 580  GLY   B CA  1 
ATOM   5619  C  C   . GLY   B  1 279 ? -54.215 10.792  5.109    1.00 42.65  ? 580  GLY   B C   1 
ATOM   5620  O  O   . GLY   B  1 279 ? -54.943 11.081  6.065    1.00 45.13  ? 580  GLY   B O   1 
ATOM   5621  N  N   . GLY   B  1 280 ? -53.678 11.711  4.307    1.00 40.97  ? 581  GLY   B N   1 
ATOM   5622  C  CA  . GLY   B  1 280 ? -53.881 13.133  4.527    1.00 49.69  ? 581  GLY   B CA  1 
ATOM   5623  C  C   . GLY   B  1 280 ? -52.944 13.775  5.535    1.00 48.69  ? 581  GLY   B C   1 
ATOM   5624  O  O   . GLY   B  1 280 ? -52.855 15.012  5.576    1.00 44.44  ? 581  GLY   B O   1 
ATOM   5625  N  N   . LEU   B  1 281 ? -52.242 12.985  6.343    1.00 40.64  ? 582  LEU   B N   1 
ATOM   5626  C  CA  . LEU   B  1 281 ? -51.283 13.524  7.295    1.00 43.59  ? 582  LEU   B CA  1 
ATOM   5627  C  C   . LEU   B  1 281 ? -49.959 13.814  6.604    1.00 46.71  ? 582  LEU   B C   1 
ATOM   5628  O  O   . LEU   B  1 281 ? -49.551 13.110  5.676    1.00 46.28  ? 582  LEU   B O   1 
ATOM   5629  C  CB  . LEU   B  1 281 ? -51.068 12.549  8.452    1.00 36.47  ? 582  LEU   B CB  1 
ATOM   5630  C  CG  . LEU   B  1 281 ? -52.336 12.090  9.182    1.00 37.15  ? 582  LEU   B CG  1 
ATOM   5631  C  CD1 . LEU   B  1 281 ? -51.980 11.196  10.367   1.00 38.14  ? 582  LEU   B CD1 1 
ATOM   5632  C  CD2 . LEU   B  1 281 ? -53.162 13.292  9.617    1.00 34.65  ? 582  LEU   B CD2 1 
ATOM   5633  N  N   . GLU   B  1 282 ? -49.288 14.863  7.067    1.00 42.14  ? 583  GLU   B N   1 
ATOM   5634  C  CA  . GLU   B  1 282 ? -48.062 15.354  6.444    1.00 43.12  ? 583  GLU   B CA  1 
ATOM   5635  C  C   . GLU   B  1 282 ? -46.939 15.338  7.470    1.00 50.84  ? 583  GLU   B C   1 
ATOM   5636  O  O   . GLU   B  1 282 ? -46.920 16.159  8.395    1.00 52.58  ? 583  GLU   B O   1 
ATOM   5637  C  CB  . GLU   B  1 282 ? -48.247 16.762  5.896    1.00 43.59  ? 583  GLU   B CB  1 
ATOM   5638  C  CG  . GLU   B  1 282 ? -49.341 16.887  4.872    1.00 56.79  ? 583  GLU   B CG  1 
ATOM   5639  C  CD  . GLU   B  1 282 ? -49.298 18.226  4.198    1.00 63.62  ? 583  GLU   B CD  1 
ATOM   5640  O  OE1 . GLU   B  1 282 ? -49.240 18.261  2.947    1.00 68.59  ? 583  GLU   B OE1 1 
ATOM   5641  O  OE2 . GLU   B  1 282 ? -49.296 19.242  4.928    1.00 61.02  ? 583  GLU   B OE2 1 
ATOM   5642  N  N   . PHE   B  1 283 ? -45.994 14.424  7.290    1.00 45.84  ? 584  PHE   B N   1 
ATOM   5643  C  CA  . PHE   B  1 283 ? -44.825 14.328  8.149    1.00 35.51  ? 584  PHE   B CA  1 
ATOM   5644  C  C   . PHE   B  1 283 ? -43.679 15.070  7.460    1.00 42.81  ? 584  PHE   B C   1 
ATOM   5645  O  O   . PHE   B  1 283 ? -42.966 14.523  6.612    1.00 43.66  ? 584  PHE   B O   1 
ATOM   5646  C  CB  . PHE   B  1 283 ? -44.512 12.872  8.431    1.00 36.18  ? 584  PHE   B CB  1 
ATOM   5647  C  CG  . PHE   B  1 283 ? -45.634 12.138  9.145    1.00 44.58  ? 584  PHE   B CG  1 
ATOM   5648  C  CD1 . PHE   B  1 283 ? -45.739 12.170  10.534   1.00 36.21  ? 584  PHE   B CD1 1 
ATOM   5649  C  CD2 . PHE   B  1 283 ? -46.570 11.394  8.422    1.00 42.29  ? 584  PHE   B CD2 1 
ATOM   5650  C  CE1 . PHE   B  1 283 ? -46.763 11.472  11.198   1.00 31.52  ? 584  PHE   B CE1 1 
ATOM   5651  C  CE2 . PHE   B  1 283 ? -47.589 10.702  9.060    1.00 39.87  ? 584  PHE   B CE2 1 
ATOM   5652  C  CZ  . PHE   B  1 283 ? -47.695 10.741  10.460   1.00 39.98  ? 584  PHE   B CZ  1 
ATOM   5653  N  N   . SER   B  1 284 ? -43.535 16.351  7.813    1.00 36.21  ? 585  SER   B N   1 
ATOM   5654  C  CA  . SER   B  1 284 ? -42.550 17.239  7.210    1.00 31.05  ? 585  SER   B CA  1 
ATOM   5655  C  C   . SER   B  1 284 ? -41.116 16.886  7.569    1.00 34.62  ? 585  SER   B C   1 
ATOM   5656  O  O   . SER   B  1 284 ? -40.192 17.429  6.955    1.00 38.22  ? 585  SER   B O   1 
ATOM   5657  C  CB  . SER   B  1 284 ? -42.839 18.679  7.620    1.00 38.09  ? 585  SER   B CB  1 
ATOM   5658  O  OG  . SER   B  1 284 ? -43.063 18.784  9.024    1.00 49.66  ? 585  SER   B OG  1 
ATOM   5659  N  N   . ALA   B  1 285 ? -40.896 16.010  8.544    1.00 42.18  ? 586  ALA   B N   1 
ATOM   5660  C  CA  . ALA   B  1 285 ? -39.545 15.611  8.923    1.00 37.62  ? 586  ALA   B CA  1 
ATOM   5661  C  C   . ALA   B  1 285 ? -39.543 14.103  9.110    1.00 34.59  ? 586  ALA   B C   1 
ATOM   5662  O  O   . ALA   B  1 285 ? -40.108 13.585  10.083   1.00 35.74  ? 586  ALA   B O   1 
ATOM   5663  C  CB  . ALA   B  1 285 ? -39.079 16.334  10.184   1.00 47.43  ? 586  ALA   B CB  1 
ATOM   5664  N  N   . CYS   B  1 286 ? -38.901 13.413  8.178    1.00 35.49  ? 587  CYS   B N   1 
ATOM   5665  C  CA  . CYS   B  1 286 ? -38.921 11.963  8.091    1.00 31.85  ? 587  CYS   B CA  1 
ATOM   5666  C  C   . CYS   B  1 286 ? -37.642 11.449  7.437    1.00 38.25  ? 587  CYS   B C   1 
ATOM   5667  O  O   . CYS   B  1 286 ? -37.713 10.766  6.399    1.00 42.01  ? 587  CYS   B O   1 
ATOM   5668  C  CB  . CYS   B  1 286 ? -40.129 11.515  7.273    1.00 38.71  ? 587  CYS   B CB  1 
ATOM   5669  S  SG  . CYS   B  1 286 ? -40.114 12.241  5.563    1.00 34.15  ? 587  CYS   B SG  1 
ATOM   5670  N  N   . PRO   B  1 287 ? -36.465 11.738  7.996    1.00 43.43  ? 588  PRO   B N   1 
ATOM   5671  C  CA  . PRO   B  1 287 ? -35.223 11.302  7.341    1.00 37.07  ? 588  PRO   B CA  1 
ATOM   5672  C  C   . PRO   B  1 287 ? -35.181 9.789   7.165    1.00 38.79  ? 588  PRO   B C   1 
ATOM   5673  O  O   . PRO   B  1 287 ? -35.514 9.025   8.084    1.00 32.87  ? 588  PRO   B O   1 
ATOM   5674  C  CB  . PRO   B  1 287 ? -34.127 11.799  8.287    1.00 39.13  ? 588  PRO   B CB  1 
ATOM   5675  C  CG  . PRO   B  1 287 ? -34.821 12.086  9.605    1.00 37.94  ? 588  PRO   B CG  1 
ATOM   5676  C  CD  . PRO   B  1 287 ? -36.214 12.442  9.277    1.00 43.22  ? 588  PRO   B CD  1 
ATOM   5677  N  N   . PHE   B  1 288 ? -34.787 9.357   5.956    1.00 30.27  ? 589  PHE   B N   1 
ATOM   5678  C  CA  . PHE   B  1 288 ? -34.711 7.944   5.601    1.00 26.64  ? 589  PHE   B CA  1 
ATOM   5679  C  C   . PHE   B  1 288 ? -33.381 7.647   4.916    1.00 28.75  ? 589  PHE   B C   1 
ATOM   5680  O  O   . PHE   B  1 288 ? -32.780 8.505   4.270    1.00 31.74  ? 589  PHE   B O   1 
ATOM   5681  C  CB  . PHE   B  1 288 ? -35.887 7.499   4.700    1.00 29.21  ? 589  PHE   B CB  1 
ATOM   5682  C  CG  . PHE   B  1 288 ? -36.018 8.288   3.397    1.00 35.68  ? 589  PHE   B CG  1 
ATOM   5683  C  CD1 . PHE   B  1 288 ? -35.318 7.911   2.249    1.00 39.04  ? 589  PHE   B CD1 1 
ATOM   5684  C  CD2 . PHE   B  1 288 ? -36.871 9.380   3.322    1.00 32.83  ? 589  PHE   B CD2 1 
ATOM   5685  C  CE1 . PHE   B  1 288 ? -35.459 8.631   1.032    1.00 29.96  ? 589  PHE   B CE1 1 
ATOM   5686  C  CE2 . PHE   B  1 288 ? -37.011 10.112  2.137    1.00 39.23  ? 589  PHE   B CE2 1 
ATOM   5687  C  CZ  . PHE   B  1 288 ? -36.310 9.728   0.982    1.00 31.90  ? 589  PHE   B CZ  1 
ATOM   5688  N  N   . SER   B  1 289 ? -32.928 6.415   5.054    1.00 29.34  ? 590  SER   B N   1 
ATOM   5689  C  CA  . SER   B  1 289 ? -31.591 6.098   4.618    1.00 27.92  ? 590  SER   B CA  1 
ATOM   5690  C  C   . SER   B  1 289 ? -31.552 4.654   4.146    1.00 28.36  ? 590  SER   B C   1 
ATOM   5691  O  O   . SER   B  1 289 ? -32.353 3.819   4.572    1.00 25.46  ? 590  SER   B O   1 
ATOM   5692  C  CB  . SER   B  1 289 ? -30.572 6.340   5.744    1.00 34.86  ? 590  SER   B CB  1 
ATOM   5693  O  OG  . SER   B  1 289 ? -30.760 5.437   6.813    1.00 36.89  ? 590  SER   B OG  1 
ATOM   5694  N  N   . GLY   B  1 290 ? -30.641 4.380   3.219    1.00 37.39  ? 591  GLY   B N   1 
ATOM   5695  C  CA  . GLY   B  1 290 ? -30.426 3.019   2.783    1.00 32.53  ? 591  GLY   B CA  1 
ATOM   5696  C  C   . GLY   B  1 290 ? -28.949 2.814   2.574    1.00 43.96  ? 591  GLY   B C   1 
ATOM   5697  O  O   . GLY   B  1 290 ? -28.164 3.015   3.504    1.00 46.68  ? 591  GLY   B O   1 
ATOM   5698  N  N   . TRP   B  1 291 ? -28.553 2.443   1.357    1.00 38.48  ? 592  TRP   B N   1 
ATOM   5699  C  CA  . TRP   B  1 291 ? -27.148 2.407   1.017    1.00 37.79  ? 592  TRP   B CA  1 
ATOM   5700  C  C   . TRP   B  1 291 ? -26.992 2.854   -0.437   1.00 39.34  ? 592  TRP   B C   1 
ATOM   5701  O  O   . TRP   B  1 291 ? -27.950 2.891   -1.210   1.00 34.82  ? 592  TRP   B O   1 
ATOM   5702  C  CB  . TRP   B  1 291 ? -26.566 1.022   1.275    1.00 37.85  ? 592  TRP   B CB  1 
ATOM   5703  C  CG  . TRP   B  1 291 ? -27.351 -0.042  0.635    1.00 42.92  ? 592  TRP   B CG  1 
ATOM   5704  C  CD1 . TRP   B  1 291 ? -27.309 -0.408  -0.683   1.00 38.31  ? 592  TRP   B CD1 1 
ATOM   5705  C  CD2 . TRP   B  1 291 ? -28.319 -0.889  1.257    1.00 43.09  ? 592  TRP   B CD2 1 
ATOM   5706  N  NE1 . TRP   B  1 291 ? -28.191 -1.430  -0.915   1.00 39.75  ? 592  TRP   B NE1 1 
ATOM   5707  C  CE2 . TRP   B  1 291 ? -28.826 -1.746  0.255    1.00 44.96  ? 592  TRP   B CE2 1 
ATOM   5708  C  CE3 . TRP   B  1 291 ? -28.814 -1.007  2.561    1.00 50.41  ? 592  TRP   B CE3 1 
ATOM   5709  C  CZ2 . TRP   B  1 291 ? -29.793 -2.718  0.520    1.00 52.69  ? 592  TRP   B CZ2 1 
ATOM   5710  C  CZ3 . TRP   B  1 291 ? -29.780 -1.975  2.825    1.00 51.93  ? 592  TRP   B CZ3 1 
ATOM   5711  C  CH2 . TRP   B  1 291 ? -30.255 -2.819  1.808    1.00 57.41  ? 592  TRP   B CH2 1 
ATOM   5712  N  N   . TYR   B  1 292 ? -25.778 3.250   -0.778   1.00 27.44  ? 593  TYR   B N   1 
ATOM   5713  C  CA  . TYR   B  1 292 ? -25.498 3.864   -2.065   1.00 38.21  ? 593  TYR   B CA  1 
ATOM   5714  C  C   . TYR   B  1 292 ? -25.464 2.844   -3.197   1.00 41.31  ? 593  TYR   B C   1 
ATOM   5715  O  O   . TYR   B  1 292 ? -25.000 1.712   -3.034   1.00 41.01  ? 593  TYR   B O   1 
ATOM   5716  C  CB  . TYR   B  1 292 ? -24.150 4.567   -2.034   1.00 32.90  ? 593  TYR   B CB  1 
ATOM   5717  C  CG  . TYR   B  1 292 ? -24.198 5.994   -1.616   1.00 39.19  ? 593  TYR   B CG  1 
ATOM   5718  C  CD1 . TYR   B  1 292 ? -24.983 6.901   -2.310   1.00 43.11  ? 593  TYR   B CD1 1 
ATOM   5719  C  CD2 . TYR   B  1 292 ? -23.438 6.451   -0.545   1.00 37.73  ? 593  TYR   B CD2 1 
ATOM   5720  C  CE1 . TYR   B  1 292 ? -25.019 8.226   -1.957   1.00 35.08  ? 593  TYR   B CE1 1 
ATOM   5721  C  CE2 . TYR   B  1 292 ? -23.464 7.778   -0.179   1.00 37.85  ? 593  TYR   B CE2 1 
ATOM   5722  C  CZ  . TYR   B  1 292 ? -24.254 8.660   -0.892   1.00 39.81  ? 593  TYR   B CZ  1 
ATOM   5723  O  OH  . TYR   B  1 292 ? -24.281 9.982   -0.552   1.00 45.44  ? 593  TYR   B OH  1 
ATOM   5724  N  N   . MET   B  1 293 ? -25.963 3.264   -4.351   1.00 43.16  ? 594  MET   B N   1 
ATOM   5725  C  CA  . MET   B  1 293 ? -25.510 2.708   -5.614   1.00 32.25  ? 594  MET   B CA  1 
ATOM   5726  C  C   . MET   B  1 293 ? -24.240 3.457   -5.996   1.00 29.71  ? 594  MET   B C   1 
ATOM   5727  O  O   . MET   B  1 293 ? -24.178 4.681   -5.867   1.00 31.94  ? 594  MET   B O   1 
ATOM   5728  C  CB  . MET   B  1 293 ? -26.596 2.850   -6.683   1.00 30.59  ? 594  MET   B CB  1 
ATOM   5729  C  CG  . MET   B  1 293 ? -26.302 2.084   -7.958   1.00 34.96  ? 594  MET   B CG  1 
ATOM   5730  S  SD  . MET   B  1 293 ? -27.797 1.879   -8.924   1.00 38.33  ? 594  MET   B SD  1 
ATOM   5731  C  CE  . MET   B  1 293 ? -28.094 3.548   -9.495   1.00 36.49  ? 594  MET   B CE  1 
ATOM   5732  N  N   . GLY   B  1 294 ? -23.213 2.722   -6.436   1.00 35.40  ? 595  GLY   B N   1 
ATOM   5733  C  CA  . GLY   B  1 294 ? -21.912 3.339   -6.669   1.00 35.61  ? 595  GLY   B CA  1 
ATOM   5734  C  C   . GLY   B  1 294 ? -21.957 4.580   -7.545   1.00 37.05  ? 595  GLY   B C   1 
ATOM   5735  O  O   . GLY   B  1 294 ? -21.202 5.532   -7.326   1.00 33.43  ? 595  GLY   B O   1 
ATOM   5736  N  N   . THR   B  1 295 ? -22.851 4.591   -8.545   1.00 33.62  ? 596  THR   B N   1 
ATOM   5737  C  CA  . THR   B  1 295 ? -22.878 5.689   -9.511   1.00 35.76  ? 596  THR   B CA  1 
ATOM   5738  C  C   . THR   B  1 295 ? -23.297 7.008   -8.885   1.00 38.84  ? 596  THR   B C   1 
ATOM   5739  O  O   . THR   B  1 295 ? -22.881 8.068   -9.362   1.00 35.13  ? 596  THR   B O   1 
ATOM   5740  C  CB  . THR   B  1 295 ? -23.823 5.363   -10.658  1.00 37.01  ? 596  THR   B CB  1 
ATOM   5741  O  OG1 . THR   B  1 295 ? -25.077 4.941   -10.119  1.00 30.71  ? 596  THR   B OG1 1 
ATOM   5742  C  CG2 . THR   B  1 295 ? -23.232 4.275   -11.565  1.00 36.32  ? 596  THR   B CG2 1 
ATOM   5743  N  N   . GLU   B  1 296 ? -24.126 6.970   -7.833   1.00 41.97  ? 597  GLU   B N   1 
ATOM   5744  C  CA  . GLU   B  1 296 ? -24.529 8.205   -7.162   1.00 41.42  ? 597  GLU   B CA  1 
ATOM   5745  C  C   . GLU   B  1 296 ? -23.310 9.001   -6.715   1.00 46.67  ? 597  GLU   B C   1 
ATOM   5746  O  O   . GLU   B  1 296 ? -23.236 10.218  -6.927   1.00 47.14  ? 597  GLU   B O   1 
ATOM   5747  C  CB  . GLU   B  1 296 ? -25.425 7.892   -5.960   1.00 42.47  ? 597  GLU   B CB  1 
ATOM   5748  C  CG  . GLU   B  1 296 ? -26.744 7.208   -6.287   1.00 44.37  ? 597  GLU   B CG  1 
ATOM   5749  C  CD  . GLU   B  1 296 ? -27.555 6.874   -5.025   1.00 44.17  ? 597  GLU   B CD  1 
ATOM   5750  O  OE1 . GLU   B  1 296 ? -28.222 7.788   -4.485   1.00 39.74  ? 597  GLU   B OE1 1 
ATOM   5751  O  OE2 . GLU   B  1 296 ? -27.530 5.702   -4.599   1.00 29.86  ? 597  GLU   B OE2 1 
ATOM   5752  N  N   . ILE   B  1 297 ? -22.336 8.313   -6.108   1.00 36.16  ? 598  ILE   B N   1 
ATOM   5753  C  CA  . ILE   B  1 297 ? -21.079 8.942   -5.714   1.00 32.69  ? 598  ILE   B CA  1 
ATOM   5754  C  C   . ILE   B  1 297 ? -20.188 9.198   -6.928   1.00 43.55  ? 598  ILE   B C   1 
ATOM   5755  O  O   . ILE   B  1 297 ? -19.727 10.323  -7.149   1.00 48.55  ? 598  ILE   B O   1 
ATOM   5756  C  CB  . ILE   B  1 297 ? -20.342 8.054   -4.702   1.00 33.52  ? 598  ILE   B CB  1 
ATOM   5757  C  CG1 . ILE   B  1 297 ? -21.207 7.795   -3.468   1.00 37.99  ? 598  ILE   B CG1 1 
ATOM   5758  C  CG2 . ILE   B  1 297 ? -19.008 8.685   -4.360   1.00 32.16  ? 598  ILE   B CG2 1 
ATOM   5759  C  CD1 . ILE   B  1 297 ? -20.670 6.656   -2.580   1.00 43.22  ? 598  ILE   B CD1 1 
ATOM   5760  N  N   . GLY   B  1 298 ? -19.892 8.136   -7.701   1.00 38.12  ? 599  GLY   B N   1 
ATOM   5761  C  CA  . GLY   B  1 298 ? -18.821 8.190   -8.688   1.00 48.61  ? 599  GLY   B CA  1 
ATOM   5762  C  C   . GLY   B  1 298 ? -19.187 8.845   -10.009  1.00 38.27  ? 599  GLY   B C   1 
ATOM   5763  O  O   . GLY   B  1 298 ? -18.339 9.482   -10.635  1.00 40.50  ? 599  GLY   B O   1 
ATOM   5764  N  N   . VAL   B  1 299 ? -20.441 8.728   -10.432  1.00 35.56  ? 600  VAL   B N   1 
ATOM   5765  C  CA  . VAL   B  1 299 ? -20.907 9.459   -11.603  1.00 44.03  ? 600  VAL   B CA  1 
ATOM   5766  C  C   . VAL   B  1 299 ? -21.355 10.871  -11.228  1.00 48.36  ? 600  VAL   B C   1 
ATOM   5767  O  O   . VAL   B  1 299 ? -20.808 11.862  -11.730  1.00 51.42  ? 600  VAL   B O   1 
ATOM   5768  C  CB  . VAL   B  1 299 ? -22.033 8.679   -12.298  1.00 43.64  ? 600  VAL   B CB  1 
ATOM   5769  C  CG1 . VAL   B  1 299 ? -22.481 9.439   -13.520  1.00 46.13  ? 600  VAL   B CG1 1 
ATOM   5770  C  CG2 . VAL   B  1 299 ? -21.551 7.283   -12.690  1.00 40.59  ? 600  VAL   B CG2 1 
ATOM   5771  N  N   . ARG   B  1 300 ? -22.350 10.985  -10.332  1.00 42.73  ? 601  ARG   B N   1 
ATOM   5772  C  CA  . ARG   B  1 300 ? -23.031 12.263  -10.081  1.00 46.08  ? 601  ARG   B CA  1 
ATOM   5773  C  C   . ARG   B  1 300 ? -22.280 13.152  -9.083   1.00 46.22  ? 601  ARG   B C   1 
ATOM   5774  O  O   . ARG   B  1 300 ? -22.038 14.334  -9.356   1.00 42.89  ? 601  ARG   B O   1 
ATOM   5775  C  CB  . ARG   B  1 300 ? -24.456 12.021  -9.569   1.00 35.06  ? 601  ARG   B CB  1 
ATOM   5776  C  CG  . ARG   B  1 300 ? -25.350 11.208  -10.466  1.00 40.14  ? 601  ARG   B CG  1 
ATOM   5777  C  CD  . ARG   B  1 300 ? -25.482 11.860  -11.841  1.00 43.25  ? 601  ARG   B CD  1 
ATOM   5778  N  NE  . ARG   B  1 300 ? -25.908 13.254  -11.748  1.00 46.49  ? 601  ARG   B NE  1 
ATOM   5779  C  CZ  . ARG   B  1 300 ? -27.164 13.648  -11.568  1.00 41.44  ? 601  ARG   B CZ  1 
ATOM   5780  N  NH1 . ARG   B  1 300 ? -28.137 12.755  -11.445  1.00 43.83  ? 601  ARG   B NH1 1 
ATOM   5781  N  NH2 . ARG   B  1 300 ? -27.444 14.940  -11.503  1.00 43.97  ? 601  ARG   B NH2 1 
ATOM   5782  N  N   . ASP   B  1 301 ? -21.952 12.620  -7.901   1.00 43.59  ? 602  ASP   B N   1 
ATOM   5783  C  CA  . ASP   B  1 301 ? -21.325 13.452  -6.871   1.00 49.61  ? 602  ASP   B CA  1 
ATOM   5784  C  C   . ASP   B  1 301 ? -19.934 13.902  -7.294   1.00 41.04  ? 602  ASP   B C   1 
ATOM   5785  O  O   . ASP   B  1 301 ? -19.574 15.071  -7.131   1.00 44.58  ? 602  ASP   B O   1 
ATOM   5786  C  CB  . ASP   B  1 301 ? -21.252 12.703  -5.535   1.00 49.26  ? 602  ASP   B CB  1 
ATOM   5787  C  CG  . ASP   B  1 301 ? -22.611 12.502  -4.898   1.00 52.03  ? 602  ASP   B CG  1 
ATOM   5788  O  OD1 . ASP   B  1 301 ? -23.457 13.423  -4.953   1.00 53.16  ? 602  ASP   B OD1 1 
ATOM   5789  O  OD2 . ASP   B  1 301 ? -22.832 11.406  -4.344   1.00 51.93  ? 602  ASP   B OD2 1 
ATOM   5790  N  N   . TYR   B  1 302 ? -19.143 12.995  -7.848   1.00 48.88  ? 603  TYR   B N   1 
ATOM   5791  C  CA  . TYR   B  1 302 ? -17.779 13.343  -8.216   1.00 48.43  ? 603  TYR   B CA  1 
ATOM   5792  C  C   . TYR   B  1 302 ? -17.676 14.013  -9.587   1.00 47.12  ? 603  TYR   B C   1 
ATOM   5793  O  O   . TYR   B  1 302 ? -16.791 14.852  -9.785   1.00 44.57  ? 603  TYR   B O   1 
ATOM   5794  C  CB  . TYR   B  1 302 ? -16.908 12.090  -8.179   1.00 56.47  ? 603  TYR   B CB  1 
ATOM   5795  C  CG  . TYR   B  1 302 ? -16.440 11.715  -6.786   1.00 60.85  ? 603  TYR   B CG  1 
ATOM   5796  C  CD1 . TYR   B  1 302 ? -16.518 12.620  -5.738   1.00 59.19  ? 603  TYR   B CD1 1 
ATOM   5797  C  CD2 . TYR   B  1 302 ? -15.901 10.461  -6.530   1.00 60.14  ? 603  TYR   B CD2 1 
ATOM   5798  C  CE1 . TYR   B  1 302 ? -16.081 12.281  -4.481   1.00 61.23  ? 603  TYR   B CE1 1 
ATOM   5799  C  CE2 . TYR   B  1 302 ? -15.461 10.115  -5.273   1.00 57.74  ? 603  TYR   B CE2 1 
ATOM   5800  C  CZ  . TYR   B  1 302 ? -15.551 11.027  -4.255   1.00 60.94  ? 603  TYR   B CZ  1 
ATOM   5801  O  OH  . TYR   B  1 302 ? -15.109 10.673  -3.003   1.00 67.43  ? 603  TYR   B OH  1 
ATOM   5802  N  N   . CYS   B  1 303 ? -18.547 13.674  -10.545  1.00 44.44  ? 604  CYS   B N   1 
ATOM   5803  C  CA  . CYS   B  1 303 ? -18.296 14.085  -11.919  1.00 54.00  ? 604  CYS   B CA  1 
ATOM   5804  C  C   . CYS   B  1 303 ? -19.275 15.095  -12.500  1.00 54.06  ? 604  CYS   B C   1 
ATOM   5805  O  O   . CYS   B  1 303 ? -18.979 15.641  -13.568  1.00 52.78  ? 604  CYS   B O   1 
ATOM   5806  C  CB  . CYS   B  1 303 ? -18.239 12.862  -12.843  1.00 56.97  ? 604  CYS   B CB  1 
ATOM   5807  S  SG  . CYS   B  1 303 ? -16.757 11.885  -12.565  1.00 56.82  ? 604  CYS   B SG  1 
ATOM   5808  N  N   . ASP   B  1 304 ? -20.415 15.372  -11.855  1.00 51.57  ? 605  ASP   B N   1 
ATOM   5809  C  CA  . ASP   B  1 304 ? -21.267 16.460  -12.332  1.00 54.61  ? 605  ASP   B CA  1 
ATOM   5810  C  C   . ASP   B  1 304 ? -20.470 17.760  -12.390  1.00 62.33  ? 605  ASP   B C   1 
ATOM   5811  O  O   . ASP   B  1 304 ? -19.596 18.009  -11.552  1.00 64.80  ? 605  ASP   B O   1 
ATOM   5812  C  CB  . ASP   B  1 304 ? -22.494 16.645  -11.433  1.00 57.97  ? 605  ASP   B CB  1 
ATOM   5813  C  CG  . ASP   B  1 304 ? -23.685 15.817  -11.876  1.00 57.55  ? 605  ASP   B CG  1 
ATOM   5814  O  OD1 . ASP   B  1 304 ? -23.503 14.888  -12.701  1.00 63.40  ? 605  ASP   B OD1 1 
ATOM   5815  O  OD2 . ASP   B  1 304 ? -24.809 16.107  -11.397  1.00 52.86  ? 605  ASP   B OD2 1 
ATOM   5816  N  N   . ASN   B  1 305 ? -20.764 18.587  -13.400  1.00 58.83  ? 606  ASN   B N   1 
ATOM   5817  C  CA  . ASN   B  1 305 ? -20.054 19.858  -13.534  1.00 57.96  ? 606  ASN   B CA  1 
ATOM   5818  C  C   . ASN   B  1 305 ? -20.330 20.784  -12.352  1.00 63.40  ? 606  ASN   B C   1 
ATOM   5819  O  O   . ASN   B  1 305 ? -19.426 21.482  -11.876  1.00 66.15  ? 606  ASN   B O   1 
ATOM   5820  C  CB  . ASN   B  1 305 ? -20.428 20.538  -14.847  1.00 47.79  ? 606  ASN   B CB  1 
ATOM   5821  C  CG  . ASN   B  1 305 ? -19.493 20.161  -15.977  1.00 54.76  ? 606  ASN   B CG  1 
ATOM   5822  O  OD1 . ASN   B  1 305 ? -18.368 20.658  -16.054  1.00 64.63  ? 606  ASN   B OD1 1 
ATOM   5823  N  ND2 . ASN   B  1 305 ? -19.943 19.268  -16.852  1.00 43.02  ? 606  ASN   B ND2 1 
ATOM   5824  N  N   . SER   B  1 306 ? -21.572 20.802  -11.861  1.00 63.29  ? 607  SER   B N   1 
ATOM   5825  C  CA  . SER   B  1 306 ? -21.957 21.616  -10.713  1.00 57.85  ? 607  SER   B CA  1 
ATOM   5826  C  C   . SER   B  1 306 ? -21.598 20.969  -9.379   1.00 54.70  ? 607  SER   B C   1 
ATOM   5827  O  O   . SER   B  1 306 ? -22.003 21.469  -8.322   1.00 60.76  ? 607  SER   B O   1 
ATOM   5828  C  CB  . SER   B  1 306 ? -23.458 21.904  -10.755  1.00 55.12  ? 607  SER   B CB  1 
ATOM   5829  O  OG  . SER   B  1 306 ? -23.846 22.429  -12.007  1.00 67.35  ? 607  SER   B OG  1 
ATOM   5830  N  N   . ARG   B  1 307 ? -20.856 19.867  -9.401   1.00 51.78  ? 608  ARG   B N   1 
ATOM   5831  C  CA  . ARG   B  1 307 ? -20.491 19.183  -8.171   1.00 53.38  ? 608  ARG   B CA  1 
ATOM   5832  C  C   . ARG   B  1 307 ? -18.972 19.139  -8.013   1.00 57.86  ? 608  ARG   B C   1 
ATOM   5833  O  O   . ARG   B  1 307 ? -18.313 20.177  -8.113   1.00 62.93  ? 608  ARG   B O   1 
ATOM   5834  C  CB  . ARG   B  1 307 ? -21.111 17.787  -8.146   1.00 47.05  ? 608  ARG   B CB  1 
ATOM   5835  C  CG  . ARG   B  1 307 ? -22.635 17.799  -8.118   1.00 44.91  ? 608  ARG   B CG  1 
ATOM   5836  C  CD  . ARG   B  1 307 ? -23.206 18.476  -6.869   1.00 50.55  ? 608  ARG   B CD  1 
ATOM   5837  N  NE  . ARG   B  1 307 ? -22.849 17.793  -5.619   1.00 47.66  ? 608  ARG   B NE  1 
ATOM   5838  C  CZ  . ARG   B  1 307 ? -23.337 16.611  -5.233   1.00 47.96  ? 608  ARG   B CZ  1 
ATOM   5839  N  NH1 . ARG   B  1 307 ? -24.201 15.953  -6.005   1.00 46.50  ? 608  ARG   B NH1 1 
ATOM   5840  N  NH2 . ARG   B  1 307 ? -22.948 16.072  -4.075   1.00 35.61  ? 608  ARG   B NH2 1 
ATOM   5841  N  N   . TYR   B  1 308 ? -18.394 17.966  -7.755   1.00 58.51  ? 609  TYR   B N   1 
ATOM   5842  C  CA  . TYR   B  1 308 ? -16.968 17.952  -7.468   1.00 51.87  ? 609  TYR   B CA  1 
ATOM   5843  C  C   . TYR   B  1 308 ? -16.112 18.044  -8.719   1.00 56.57  ? 609  TYR   B C   1 
ATOM   5844  O  O   . TYR   B  1 308 ? -14.957 18.466  -8.612   1.00 63.00  ? 609  TYR   B O   1 
ATOM   5845  C  CB  . TYR   B  1 308 ? -16.589 16.724  -6.650   1.00 51.50  ? 609  TYR   B CB  1 
ATOM   5846  C  CG  . TYR   B  1 308 ? -16.734 17.001  -5.175   1.00 60.66  ? 609  TYR   B CG  1 
ATOM   5847  C  CD1 . TYR   B  1 308 ? -17.944 16.785  -4.527   1.00 53.82  ? 609  TYR   B CD1 1 
ATOM   5848  C  CD2 . TYR   B  1 308 ? -15.677 17.529  -4.438   1.00 70.05  ? 609  TYR   B CD2 1 
ATOM   5849  C  CE1 . TYR   B  1 308 ? -18.097 17.055  -3.188   1.00 56.87  ? 609  TYR   B CE1 1 
ATOM   5850  C  CE2 . TYR   B  1 308 ? -15.819 17.802  -3.082   1.00 67.03  ? 609  TYR   B CE2 1 
ATOM   5851  C  CZ  . TYR   B  1 308 ? -17.036 17.560  -2.471   1.00 59.22  ? 609  TYR   B CZ  1 
ATOM   5852  O  OH  . TYR   B  1 308 ? -17.215 17.818  -1.144   1.00 50.54  ? 609  TYR   B OH  1 
ATOM   5853  N  N   . ASN   B  1 309 ? -16.640 17.661  -9.892   1.00 45.42  ? 610  ASN   B N   1 
ATOM   5854  C  CA  . ASN   B  1 309 ? -16.032 18.028  -11.178  1.00 47.14  ? 610  ASN   B CA  1 
ATOM   5855  C  C   . ASN   B  1 309 ? -14.596 17.517  -11.304  1.00 46.36  ? 610  ASN   B C   1 
ATOM   5856  O  O   . ASN   B  1 309 ? -13.696 18.233  -11.751  1.00 50.67  ? 610  ASN   B O   1 
ATOM   5857  C  CB  . ASN   B  1 309 ? -16.088 19.548  -11.370  1.00 48.18  ? 610  ASN   B CB  1 
ATOM   5858  C  CG  . ASN   B  1 309 ? -15.852 19.973  -12.808  1.00 52.61  ? 610  ASN   B CG  1 
ATOM   5859  O  OD1 . ASN   B  1 309 ? -15.936 19.164  -13.726  1.00 50.43  ? 610  ASN   B OD1 1 
ATOM   5860  N  ND2 . ASN   B  1 309 ? -15.568 21.252  -13.005  1.00 53.79  ? 610  ASN   B ND2 1 
ATOM   5861  N  N   . ILE   B  1 310 ? -14.367 16.269  -10.899  1.00 48.76  ? 611  ILE   B N   1 
ATOM   5862  C  CA  . ILE   B  1 310 ? -12.994 15.786  -10.768  1.00 55.88  ? 611  ILE   B CA  1 
ATOM   5863  C  C   . ILE   B  1 310 ? -12.486 15.146  -12.058  1.00 59.11  ? 611  ILE   B C   1 
ATOM   5864  O  O   . ILE   B  1 310 ? -11.375 14.601  -12.084  1.00 60.17  ? 611  ILE   B O   1 
ATOM   5865  C  CB  . ILE   B  1 310 ? -12.867 14.799  -9.592   1.00 59.22  ? 611  ILE   B CB  1 
ATOM   5866  C  CG1 . ILE   B  1 310 ? -13.443 13.432  -9.957   1.00 56.38  ? 611  ILE   B CG1 1 
ATOM   5867  C  CG2 . ILE   B  1 310 ? -13.588 15.329  -8.367   1.00 62.30  ? 611  ILE   B CG2 1 
ATOM   5868  C  CD1 . ILE   B  1 310 ? -13.206 12.397  -8.891   1.00 39.75  ? 611  ILE   B CD1 1 
ATOM   5869  N  N   . LEU   B  1 311 ? -13.276 15.220  -13.140  1.00 53.29  ? 612  LEU   B N   1 
ATOM   5870  C  CA  . LEU   B  1 311 ? -12.936 14.482  -14.357  1.00 50.40  ? 612  LEU   B CA  1 
ATOM   5871  C  C   . LEU   B  1 311 ? -11.575 14.901  -14.909  1.00 50.31  ? 612  LEU   B C   1 
ATOM   5872  O  O   . LEU   B  1 311 ? -10.722 14.048  -15.174  1.00 60.36  ? 612  LEU   B O   1 
ATOM   5873  C  CB  . LEU   B  1 311 ? -14.030 14.650  -15.418  1.00 41.20  ? 612  LEU   B CB  1 
ATOM   5874  C  CG  . LEU   B  1 311 ? -15.243 13.721  -15.317  1.00 39.31  ? 612  LEU   B CG  1 
ATOM   5875  C  CD1 . LEU   B  1 311 ? -16.323 14.092  -16.301  1.00 41.21  ? 612  LEU   B CD1 1 
ATOM   5876  C  CD2 . LEU   B  1 311 ? -14.866 12.252  -15.450  1.00 39.16  ? 612  LEU   B CD2 1 
ATOM   5877  N  N   . GLU   B  1 312 ? -11.339 16.210  -15.072  1.00 54.22  ? 613  GLU   B N   1 
ATOM   5878  C  CA  . GLU   B  1 312 ? -10.072 16.658  -15.657  1.00 64.91  ? 613  GLU   B CA  1 
ATOM   5879  C  C   . GLU   B  1 312 ? -8.886  16.168  -14.839  1.00 70.91  ? 613  GLU   B C   1 
ATOM   5880  O  O   . GLU   B  1 312 ? -7.898  15.673  -15.394  1.00 66.96  ? 613  GLU   B O   1 
ATOM   5881  C  CB  . GLU   B  1 312 ? -10.026 18.184  -15.773  1.00 74.40  ? 613  GLU   B CB  1 
ATOM   5882  C  CG  . GLU   B  1 312 ? -11.306 18.822  -16.252  1.00 82.22  ? 613  GLU   B CG  1 
ATOM   5883  C  CD  . GLU   B  1 312 ? -12.205 19.248  -15.098  1.00 86.75  ? 613  GLU   B CD  1 
ATOM   5884  O  OE1 . GLU   B  1 312 ? -12.204 20.452  -14.762  1.00 88.42  ? 613  GLU   B OE1 1 
ATOM   5885  O  OE2 . GLU   B  1 312 ? -12.902 18.380  -14.521  1.00 83.35  ? 613  GLU   B OE2 1 
ATOM   5886  N  N   . GLU   B  1 313 ? -8.977  16.288  -13.509  1.00 75.69  ? 614  GLU   B N   1 
ATOM   5887  C  CA  . GLU   B  1 313 ? -7.859  15.913  -12.652  1.00 78.18  ? 614  GLU   B CA  1 
ATOM   5888  C  C   . GLU   B  1 313 ? -7.552  14.427  -12.755  1.00 77.83  ? 614  GLU   B C   1 
ATOM   5889  O  O   . GLU   B  1 313 ? -6.384  14.030  -12.816  1.00 83.41  ? 614  GLU   B O   1 
ATOM   5890  C  CB  . GLU   B  1 313 ? -8.152  16.305  -11.207  1.00 85.58  ? 614  GLU   B CB  1 
ATOM   5891  C  CG  . GLU   B  1 313 ? -7.268  17.419  -10.679  1.00 102.16 ? 614  GLU   B CG  1 
ATOM   5892  C  CD  . GLU   B  1 313 ? -6.505  17.017  -9.420   1.00 109.32 ? 614  GLU   B CD  1 
ATOM   5893  O  OE1 . GLU   B  1 313 ? -6.518  15.816  -9.075   1.00 108.99 ? 614  GLU   B OE1 1 
ATOM   5894  O  OE2 . GLU   B  1 313 ? -5.891  17.899  -8.778   1.00 111.30 ? 614  GLU   B OE2 1 
ATOM   5895  N  N   . VAL   B  1 314 ? -8.585  13.587  -12.774  1.00 71.50  ? 615  VAL   B N   1 
ATOM   5896  C  CA  . VAL   B  1 314 ? -8.344  12.163  -12.968  1.00 64.77  ? 615  VAL   B CA  1 
ATOM   5897  C  C   . VAL   B  1 314 ? -7.839  11.904  -14.380  1.00 61.12  ? 615  VAL   B C   1 
ATOM   5898  O  O   . VAL   B  1 314 ? -6.932  11.090  -14.590  1.00 60.59  ? 615  VAL   B O   1 
ATOM   5899  C  CB  . VAL   B  1 314 ? -9.610  11.351  -12.650  1.00 58.14  ? 615  VAL   B CB  1 
ATOM   5900  C  CG1 . VAL   B  1 314 ? -9.410  9.884   -12.996  1.00 53.97  ? 615  VAL   B CG1 1 
ATOM   5901  C  CG2 . VAL   B  1 314 ? -9.972  11.507  -11.170  1.00 51.09  ? 615  VAL   B CG2 1 
ATOM   5902  N  N   . ALA   B  1 315 ? -8.385  12.614  -15.367  1.00 61.64  ? 616  ALA   B N   1 
ATOM   5903  C  CA  . ALA   B  1 315 ? -7.959  12.388  -16.744  1.00 63.35  ? 616  ALA   B CA  1 
ATOM   5904  C  C   . ALA   B  1 315 ? -6.498  12.781  -16.936  1.00 51.23  ? 616  ALA   B C   1 
ATOM   5905  O  O   . ALA   B  1 315 ? -5.723  12.023  -17.523  1.00 52.36  ? 616  ALA   B O   1 
ATOM   5906  C  CB  . ALA   B  1 315 ? -8.870  13.140  -17.716  1.00 63.15  ? 616  ALA   B CB  1 
ATOM   5907  N  N   . LYS   B  1 316 ? -6.096  13.947  -16.408  1.00 65.82  ? 617  LYS   B N   1 
ATOM   5908  C  CA  . LYS   B  1 316 ? -4.691  14.355  -16.456  1.00 66.14  ? 617  LYS   B CA  1 
ATOM   5909  C  C   . LYS   B  1 316 ? -3.794  13.305  -15.817  1.00 65.07  ? 617  LYS   B C   1 
ATOM   5910  O  O   . LYS   B  1 316 ? -2.767  12.922  -16.384  1.00 60.64  ? 617  LYS   B O   1 
ATOM   5911  C  CB  . LYS   B  1 316 ? -4.495  15.708  -15.760  1.00 74.09  ? 617  LYS   B CB  1 
ATOM   5912  C  CG  . LYS   B  1 316 ? -5.100  16.912  -16.482  1.00 83.13  ? 617  LYS   B CG  1 
ATOM   5913  C  CD  . LYS   B  1 316 ? -4.978  18.190  -15.651  1.00 86.41  ? 617  LYS   B CD  1 
ATOM   5914  C  CE  . LYS   B  1 316 ? -5.487  17.962  -14.235  1.00 92.06  ? 617  LYS   B CE  1 
ATOM   5915  N  NZ  . LYS   B  1 316 ? -5.739  19.202  -13.442  1.00 93.62  ? 617  LYS   B NZ  1 
ATOM   5916  N  N   . LYS   B  1 317 ? -4.166  12.829  -14.627  1.00 68.15  ? 618  LYS   B N   1 
ATOM   5917  C  CA  . LYS   B  1 317 ? -3.364  11.801  -13.975  1.00 71.83  ? 618  LYS   B CA  1 
ATOM   5918  C  C   . LYS   B  1 317 ? -3.250  10.544  -14.828  1.00 75.82  ? 618  LYS   B C   1 
ATOM   5919  O  O   . LYS   B  1 317 ? -2.257  9.819   -14.718  1.00 78.18  ? 618  LYS   B O   1 
ATOM   5920  C  CB  . LYS   B  1 317 ? -3.949  11.468  -12.598  1.00 75.62  ? 618  LYS   B CB  1 
ATOM   5921  C  CG  . LYS   B  1 317 ? -3.540  12.432  -11.470  1.00 79.80  ? 618  LYS   B CG  1 
ATOM   5922  C  CD  . LYS   B  1 317 ? -2.077  12.235  -11.086  1.00 88.68  ? 618  LYS   B CD  1 
ATOM   5923  C  CE  . LYS   B  1 317 ? -1.333  13.557  -10.954  1.00 99.41  ? 618  LYS   B CE  1 
ATOM   5924  N  NZ  . LYS   B  1 317 ? -1.904  14.412  -9.880   1.00 104.57 ? 618  LYS   B NZ  1 
ATOM   5925  N  N   . MET   B  1 318 ? -4.223  10.290  -15.699  1.00 70.96  ? 619  MET   B N   1 
ATOM   5926  C  CA  . MET   B  1 318 ? -4.223  9.092   -16.526  1.00 70.89  ? 619  MET   B CA  1 
ATOM   5927  C  C   . MET   B  1 318 ? -3.503  9.274   -17.857  1.00 71.59  ? 619  MET   B C   1 
ATOM   5928  O  O   . MET   B  1 318 ? -3.370  8.294   -18.595  1.00 67.13  ? 619  MET   B O   1 
ATOM   5929  C  CB  . MET   B  1 318 ? -5.664  8.629   -16.788  1.00 69.42  ? 619  MET   B CB  1 
ATOM   5930  C  CG  . MET   B  1 318 ? -6.357  8.006   -15.580  1.00 64.70  ? 619  MET   B CG  1 
ATOM   5931  S  SD  . MET   B  1 318 ? -8.095  7.583   -15.874  1.00 66.54  ? 619  MET   B SD  1 
ATOM   5932  C  CE  . MET   B  1 318 ? -7.951  6.411   -17.230  1.00 63.64  ? 619  MET   B CE  1 
ATOM   5933  N  N   . ASN   B  1 319 ? -3.043  10.488  -18.174  1.00 73.02  ? 620  ASN   B N   1 
ATOM   5934  C  CA  . ASN   B  1 319 ? -2.356  10.808  -19.427  1.00 84.22  ? 620  ASN   B CA  1 
ATOM   5935  C  C   . ASN   B  1 319 ? -3.272  10.556  -20.628  1.00 82.59  ? 620  ASN   B C   1 
ATOM   5936  O  O   . ASN   B  1 319 ? -3.032  9.694   -21.477  1.00 79.55  ? 620  ASN   B O   1 
ATOM   5937  C  CB  . ASN   B  1 319 ? -1.048  10.020  -19.558  1.00 94.28  ? 620  ASN   B CB  1 
ATOM   5938  C  CG  . ASN   B  1 319 ? -0.125  10.242  -18.387  1.00 103.14 ? 620  ASN   B CG  1 
ATOM   5939  O  OD1 . ASN   B  1 319 ? 0.429   11.327  -18.226  1.00 112.48 ? 620  ASN   B OD1 1 
ATOM   5940  N  ND2 . ASN   B  1 319 ? 0.046   9.217   -17.556  1.00 101.54 ? 620  ASN   B ND2 1 
ATOM   5941  N  N   . LEU   B  1 320 ? -4.335  11.348  -20.674  1.00 79.94  ? 621  LEU   B N   1 
ATOM   5942  C  CA  . LEU   B  1 320 ? -5.391  11.182  -21.654  1.00 73.74  ? 621  LEU   B CA  1 
ATOM   5943  C  C   . LEU   B  1 320 ? -5.392  12.352  -22.621  1.00 80.79  ? 621  LEU   B C   1 
ATOM   5944  O  O   . LEU   B  1 320 ? -5.123  13.493  -22.234  1.00 83.94  ? 621  LEU   B O   1 
ATOM   5945  C  CB  . LEU   B  1 320 ? -6.752  11.068  -20.974  1.00 69.76  ? 621  LEU   B CB  1 
ATOM   5946  C  CG  . LEU   B  1 320 ? -6.989  9.771   -20.207  1.00 64.48  ? 621  LEU   B CG  1 
ATOM   5947  C  CD1 . LEU   B  1 320 ? -8.292  9.853   -19.428  1.00 54.42  ? 621  LEU   B CD1 1 
ATOM   5948  C  CD2 . LEU   B  1 320 ? -6.988  8.590   -21.171  1.00 50.77  ? 621  LEU   B CD2 1 
ATOM   5949  N  N   . ASP   B  1 321 ? -5.690  12.048  -23.883  1.00 79.94  ? 622  ASP   B N   1 
ATOM   5950  C  CA  . ASP   B  1 321 ? -5.837  13.048  -24.928  1.00 83.54  ? 622  ASP   B CA  1 
ATOM   5951  C  C   . ASP   B  1 321 ? -7.034  13.935  -24.619  1.00 73.81  ? 622  ASP   B C   1 
ATOM   5952  O  O   . ASP   B  1 321 ? -8.160  13.613  -25.012  1.00 78.36  ? 622  ASP   B O   1 
ATOM   5953  C  CB  . ASP   B  1 321 ? -5.995  12.342  -26.282  1.00 99.95  ? 622  ASP   B CB  1 
ATOM   5954  C  CG  . ASP   B  1 321 ? -6.076  13.304  -27.448  1.00 110.33 ? 622  ASP   B CG  1 
ATOM   5955  O  OD1 . ASP   B  1 321 ? -6.133  14.525  -27.207  1.00 113.54 ? 622  ASP   B OD1 1 
ATOM   5956  O  OD2 . ASP   B  1 321 ? -6.078  12.831  -28.611  1.00 112.21 ? 622  ASP   B OD2 1 
ATOM   5957  N  N   . MET   B  1 322 ? -6.811  15.054  -23.929  1.00 65.41  ? 623  MET   B N   1 
ATOM   5958  C  CA  . MET   B  1 322 ? -7.904  15.900  -23.466  1.00 67.84  ? 623  MET   B CA  1 
ATOM   5959  C  C   . MET   B  1 322 ? -8.145  17.104  -24.370  1.00 71.73  ? 623  MET   B C   1 
ATOM   5960  O  O   . MET   B  1 322 ? -8.766  18.078  -23.933  1.00 75.27  ? 623  MET   B O   1 
ATOM   5961  C  CB  . MET   B  1 322 ? -7.655  16.371  -22.028  1.00 60.19  ? 623  MET   B CB  1 
ATOM   5962  C  CG  . MET   B  1 322 ? -7.502  15.259  -21.022  1.00 62.25  ? 623  MET   B CG  1 
ATOM   5963  S  SD  . MET   B  1 322 ? -7.078  15.861  -19.359  1.00 77.83  ? 623  MET   B SD  1 
ATOM   5964  C  CE  . MET   B  1 322 ? -8.486  16.905  -18.977  1.00 71.90  ? 623  MET   B CE  1 
ATOM   5965  N  N   . ARG   B  1 323 ? -7.692  17.058  -25.624  1.00 71.72  ? 624  ARG   B N   1 
ATOM   5966  C  CA  . ARG   B  1 323 ? -7.878  18.209  -26.494  1.00 71.86  ? 624  ARG   B CA  1 
ATOM   5967  C  C   . ARG   B  1 323 ? -9.170  18.156  -27.300  1.00 66.28  ? 624  ARG   B C   1 
ATOM   5968  O  O   . ARG   B  1 323 ? -9.593  19.191  -27.821  1.00 77.30  ? 624  ARG   B O   1 
ATOM   5969  C  CB  . ARG   B  1 323 ? -6.679  18.373  -27.438  1.00 87.67  ? 624  ARG   B CB  1 
ATOM   5970  C  CG  . ARG   B  1 323 ? -6.492  17.242  -28.431  1.00 96.33  ? 624  ARG   B CG  1 
ATOM   5971  C  CD  . ARG   B  1 323 ? -5.303  17.462  -29.358  1.00 101.87 ? 624  ARG   B CD  1 
ATOM   5972  N  NE  . ARG   B  1 323 ? -5.734  18.006  -30.640  1.00 107.73 ? 624  ARG   B NE  1 
ATOM   5973  C  CZ  . ARG   B  1 323 ? -5.830  19.304  -30.890  1.00 111.68 ? 624  ARG   B CZ  1 
ATOM   5974  N  NH1 . ARG   B  1 323 ? -5.510  20.168  -29.939  1.00 115.15 ? 624  ARG   B NH1 1 
ATOM   5975  N  NH2 . ARG   B  1 323 ? -6.236  19.736  -32.078  1.00 108.91 ? 624  ARG   B NH2 1 
ATOM   5976  N  N   . LYS   B  1 324 ? -9.816  16.999  -27.421  1.00 65.82  ? 625  LYS   B N   1 
ATOM   5977  C  CA  . LYS   B  1 324 ? -11.121 16.949  -28.071  1.00 71.70  ? 625  LYS   B CA  1 
ATOM   5978  C  C   . LYS   B  1 324 ? -12.015 15.945  -27.349  1.00 69.55  ? 625  LYS   B C   1 
ATOM   5979  O  O   . LYS   B  1 324 ? -11.541 15.060  -26.632  1.00 75.05  ? 625  LYS   B O   1 
ATOM   5980  C  CB  . LYS   B  1 324 ? -10.994 16.607  -29.570  1.00 72.77  ? 625  LYS   B CB  1 
ATOM   5981  C  CG  . LYS   B  1 324 ? -11.918 17.426  -30.490  1.00 84.53  ? 625  LYS   B CG  1 
ATOM   5982  C  CD  . LYS   B  1 324 ? -13.366 16.888  -30.499  1.00 90.04  ? 625  LYS   B CD  1 
ATOM   5983  C  CE  . LYS   B  1 324 ? -14.342 17.751  -31.318  1.00 91.79  ? 625  LYS   B CE  1 
ATOM   5984  N  NZ  . LYS   B  1 324 ? -14.319 17.458  -32.789  1.00 86.88  ? 625  LYS   B NZ  1 
ATOM   5985  N  N   . THR   B  1 325 ? -13.328 16.108  -27.530  1.00 63.14  ? 626  THR   B N   1 
ATOM   5986  C  CA  . THR   B  1 325 ? -14.288 15.177  -26.936  1.00 55.21  ? 626  THR   B CA  1 
ATOM   5987  C  C   . THR   B  1 325 ? -14.111 13.756  -27.465  1.00 52.12  ? 626  THR   B C   1 
ATOM   5988  O  O   . THR   B  1 325 ? -14.255 12.789  -26.708  1.00 47.31  ? 626  THR   B O   1 
ATOM   5989  C  CB  . THR   B  1 325 ? -15.719 15.636  -27.217  1.00 57.49  ? 626  THR   B CB  1 
ATOM   5990  O  OG1 . THR   B  1 325 ? -15.870 15.871  -28.624  1.00 72.66  ? 626  THR   B OG1 1 
ATOM   5991  C  CG2 . THR   B  1 325 ? -16.046 16.897  -26.467  1.00 51.61  ? 626  THR   B CG2 1 
ATOM   5992  N  N   . SER   B  1 326 ? -13.832 13.608  -28.772  1.00 57.56  ? 627  SER   B N   1 
ATOM   5993  C  CA  . SER   B  1 326 ? -13.964 12.314  -29.440  1.00 46.74  ? 627  SER   B CA  1 
ATOM   5994  C  C   . SER   B  1 326 ? -12.954 11.290  -28.956  1.00 53.68  ? 627  SER   B C   1 
ATOM   5995  O  O   . SER   B  1 326 ? -13.115 10.106  -29.265  1.00 54.64  ? 627  SER   B O   1 
ATOM   5996  C  CB  . SER   B  1 326 ? -13.830 12.457  -30.971  1.00 51.31  ? 627  SER   B CB  1 
ATOM   5997  O  OG  . SER   B  1 326 ? -13.352 13.733  -31.331  1.00 63.63  ? 627  SER   B OG  1 
ATOM   5998  N  N   . SER   B  1 327 ? -11.899 11.711  -28.246  1.00 48.31  ? 628  SER   B N   1 
ATOM   5999  C  CA  . SER   B  1 327 ? -11.053 10.754  -27.534  1.00 53.19  ? 628  SER   B CA  1 
ATOM   6000  C  C   . SER   B  1 327 ? -11.780 10.061  -26.381  1.00 46.87  ? 628  SER   B C   1 
ATOM   6001  O  O   . SER   B  1 327 ? -11.254 9.091   -25.835  1.00 55.07  ? 628  SER   B O   1 
ATOM   6002  C  CB  . SER   B  1 327 ? -9.818  11.446  -26.974  1.00 57.09  ? 628  SER   B CB  1 
ATOM   6003  O  OG  . SER   B  1 327 ? -10.189 12.300  -25.908  1.00 54.92  ? 628  SER   B OG  1 
ATOM   6004  N  N   . LEU   B  1 328 ? -12.958 10.533  -25.997  1.00 46.94  ? 629  LEU   B N   1 
ATOM   6005  C  CA  . LEU   B  1 328 ? -13.743 9.932   -24.912  1.00 44.84  ? 629  LEU   B CA  1 
ATOM   6006  C  C   . LEU   B  1 328 ? -12.959 9.876   -23.595  1.00 49.10  ? 629  LEU   B C   1 
ATOM   6007  O  O   . LEU   B  1 328 ? -13.126 8.947   -22.796  1.00 43.87  ? 629  LEU   B O   1 
ATOM   6008  C  CB  . LEU   B  1 328 ? -14.247 8.535   -25.304  1.00 42.94  ? 629  LEU   B CB  1 
ATOM   6009  C  CG  . LEU   B  1 328 ? -15.115 8.416   -26.566  1.00 44.56  ? 629  LEU   B CG  1 
ATOM   6010  C  CD1 . LEU   B  1 328 ? -15.952 7.156   -26.552  1.00 41.57  ? 629  LEU   B CD1 1 
ATOM   6011  C  CD2 . LEU   B  1 328 ? -16.007 9.631   -26.776  1.00 42.02  ? 629  LEU   B CD2 1 
ATOM   6012  N  N   . TRP   B  1 329 ? -12.091 10.867  -23.356  1.00 45.31  ? 630  TRP   B N   1 
ATOM   6013  C  CA  . TRP   B  1 329 ? -11.313 10.879  -22.122  1.00 51.49  ? 630  TRP   B CA  1 
ATOM   6014  C  C   . TRP   B  1 329 ? -12.219 10.986  -20.892  1.00 52.28  ? 630  TRP   B C   1 
ATOM   6015  O  O   . TRP   B  1 329 ? -11.970 10.338  -19.867  1.00 48.68  ? 630  TRP   B O   1 
ATOM   6016  C  CB  . TRP   B  1 329 ? -10.287 12.017  -22.154  1.00 56.45  ? 630  TRP   B CB  1 
ATOM   6017  C  CG  . TRP   B  1 329 ? -10.857 13.404  -22.286  1.00 58.25  ? 630  TRP   B CG  1 
ATOM   6018  C  CD1 . TRP   B  1 329 ? -11.123 14.069  -23.439  1.00 57.75  ? 630  TRP   B CD1 1 
ATOM   6019  C  CD2 . TRP   B  1 329 ? -11.211 14.298  -21.219  1.00 62.98  ? 630  TRP   B CD2 1 
ATOM   6020  N  NE1 . TRP   B  1 329 ? -11.624 15.319  -23.166  1.00 59.57  ? 630  TRP   B NE1 1 
ATOM   6021  C  CE2 . TRP   B  1 329 ? -11.690 15.485  -21.808  1.00 63.68  ? 630  TRP   B CE2 1 
ATOM   6022  C  CE3 . TRP   B  1 329 ? -11.170 14.210  -19.826  1.00 60.14  ? 630  TRP   B CE3 1 
ATOM   6023  C  CZ2 . TRP   B  1 329 ? -12.133 16.571  -21.049  1.00 58.82  ? 630  TRP   B CZ2 1 
ATOM   6024  C  CZ3 . TRP   B  1 329 ? -11.598 15.289  -19.076  1.00 55.80  ? 630  TRP   B CZ3 1 
ATOM   6025  C  CH2 . TRP   B  1 329 ? -12.070 16.454  -19.688  1.00 51.56  ? 630  TRP   B CH2 1 
ATOM   6026  N  N   . LYS   B  1 330 ? -13.283 11.783  -20.984  1.00 46.34  ? 631  LYS   B N   1 
ATOM   6027  C  CA  . LYS   B  1 330 ? -14.232 11.885  -19.886  1.00 42.95  ? 631  LYS   B CA  1 
ATOM   6028  C  C   . LYS   B  1 330 ? -14.829 10.526  -19.545  1.00 54.03  ? 631  LYS   B C   1 
ATOM   6029  O  O   . LYS   B  1 330 ? -14.898 10.141  -18.367  1.00 39.43  ? 631  LYS   B O   1 
ATOM   6030  C  CB  . LYS   B  1 330 ? -15.337 12.874  -20.248  1.00 40.59  ? 631  LYS   B CB  1 
ATOM   6031  C  CG  . LYS   B  1 330 ? -14.909 14.328  -20.173  1.00 49.05  ? 631  LYS   B CG  1 
ATOM   6032  C  CD  . LYS   B  1 330 ? -16.084 15.244  -20.438  1.00 49.07  ? 631  LYS   B CD  1 
ATOM   6033  C  CE  . LYS   B  1 330 ? -15.723 16.679  -20.151  1.00 52.94  ? 631  LYS   B CE  1 
ATOM   6034  N  NZ  . LYS   B  1 330 ? -16.910 17.529  -20.396  1.00 64.71  ? 631  LYS   B NZ  1 
ATOM   6035  N  N   . ASP   B  1 331 ? -15.272 9.787   -20.571  1.00 50.35  ? 632  ASP   B N   1 
ATOM   6036  C  CA  . ASP   B  1 331 ? -15.895 8.486   -20.356  1.00 43.49  ? 632  ASP   B CA  1 
ATOM   6037  C  C   . ASP   B  1 331 ? -14.925 7.509   -19.713  1.00 48.70  ? 632  ASP   B C   1 
ATOM   6038  O  O   . ASP   B  1 331 ? -15.325 6.677   -18.883  1.00 48.97  ? 632  ASP   B O   1 
ATOM   6039  C  CB  . ASP   B  1 331 ? -16.400 7.906   -21.685  1.00 38.74  ? 632  ASP   B CB  1 
ATOM   6040  C  CG  . ASP   B  1 331 ? -17.173 8.910   -22.503  1.00 38.89  ? 632  ASP   B CG  1 
ATOM   6041  O  OD1 . ASP   B  1 331 ? -16.533 9.837   -23.032  1.00 39.56  ? 632  ASP   B OD1 1 
ATOM   6042  O  OD2 . ASP   B  1 331 ? -18.408 8.773   -22.629  1.00 37.31  ? 632  ASP   B OD2 1 
ATOM   6043  N  N   . GLN   B  1 332 ? -13.650 7.589   -20.103  1.00 46.28  ? 633  GLN   B N   1 
ATOM   6044  C  CA  . GLN   B  1 332 ? -12.637 6.664   -19.609  1.00 54.63  ? 633  GLN   B CA  1 
ATOM   6045  C  C   . GLN   B  1 332 ? -12.318 6.928   -18.147  1.00 51.87  ? 633  GLN   B C   1 
ATOM   6046  O  O   . GLN   B  1 332 ? -12.243 5.995   -17.337  1.00 45.73  ? 633  GLN   B O   1 
ATOM   6047  C  CB  . GLN   B  1 332 ? -11.373 6.787   -20.455  1.00 60.48  ? 633  GLN   B CB  1 
ATOM   6048  C  CG  . GLN   B  1 332 ? -10.982 5.508   -21.132  1.00 66.14  ? 633  GLN   B CG  1 
ATOM   6049  C  CD  . GLN   B  1 332 ? -9.777  5.680   -22.019  1.00 70.22  ? 633  GLN   B CD  1 
ATOM   6050  O  OE1 . GLN   B  1 332 ? -9.520  6.767   -22.546  1.00 70.83  ? 633  GLN   B OE1 1 
ATOM   6051  N  NE2 . GLN   B  1 332 ? -9.019  4.611   -22.184  1.00 75.63  ? 633  GLN   B NE2 1 
ATOM   6052  N  N   . ALA   B  1 333 ? -12.086 8.195   -17.805  1.00 53.65  ? 634  ALA   B N   1 
ATOM   6053  C  CA  . ALA   B  1 333 ? -11.876 8.557   -16.415  1.00 49.72  ? 634  ALA   B CA  1 
ATOM   6054  C  C   . ALA   B  1 333 ? -13.092 8.197   -15.590  1.00 48.04  ? 634  ALA   B C   1 
ATOM   6055  O  O   . ALA   B  1 333 ? -12.962 7.671   -14.476  1.00 45.64  ? 634  ALA   B O   1 
ATOM   6056  C  CB  . ALA   B  1 333 ? -11.567 10.049  -16.297  1.00 47.05  ? 634  ALA   B CB  1 
ATOM   6057  N  N   . LEU   B  1 334 ? -14.285 8.446   -16.141  1.00 47.49  ? 635  LEU   B N   1 
ATOM   6058  C  CA  . LEU   B  1 334 ? -15.514 8.179   -15.406  1.00 49.53  ? 635  LEU   B CA  1 
ATOM   6059  C  C   . LEU   B  1 334 ? -15.585 6.723   -14.975  1.00 50.89  ? 635  LEU   B C   1 
ATOM   6060  O  O   . LEU   B  1 334 ? -15.977 6.419   -13.842  1.00 51.74  ? 635  LEU   B O   1 
ATOM   6061  C  CB  . LEU   B  1 334 ? -16.722 8.546   -16.259  1.00 48.07  ? 635  LEU   B CB  1 
ATOM   6062  C  CG  . LEU   B  1 334 ? -18.061 8.250   -15.598  1.00 47.39  ? 635  LEU   B CG  1 
ATOM   6063  C  CD1 . LEU   B  1 334 ? -18.297 9.243   -14.479  1.00 42.01  ? 635  LEU   B CD1 1 
ATOM   6064  C  CD2 . LEU   B  1 334 ? -19.186 8.292   -16.613  1.00 42.60  ? 635  LEU   B CD2 1 
ATOM   6065  N  N   . VAL   B  1 335 ? -15.171 5.811   -15.855  1.00 49.14  ? 636  VAL   B N   1 
ATOM   6066  C  CA  . VAL   B  1 335 ? -15.219 4.394   -15.525  1.00 45.45  ? 636  VAL   B CA  1 
ATOM   6067  C  C   . VAL   B  1 335 ? -14.239 4.074   -14.403  1.00 47.65  ? 636  VAL   B C   1 
ATOM   6068  O  O   . VAL   B  1 335 ? -14.581 3.361   -13.452  1.00 51.50  ? 636  VAL   B O   1 
ATOM   6069  C  CB  . VAL   B  1 335 ? -14.956 3.539   -16.777  1.00 38.97  ? 636  VAL   B CB  1 
ATOM   6070  C  CG1 . VAL   B  1 335 ? -14.742 2.103   -16.387  1.00 41.13  ? 636  VAL   B CG1 1 
ATOM   6071  C  CG2 . VAL   B  1 335 ? -16.130 3.628   -17.728  1.00 37.52  ? 636  VAL   B CG2 1 
ATOM   6072  N  N   . GLU   B  1 336 ? -13.017 4.606   -14.485  1.00 42.72  ? 637  GLU   B N   1 
ATOM   6073  C  CA  . GLU   B  1 336 ? -12.019 4.330   -13.460  1.00 49.48  ? 637  GLU   B CA  1 
ATOM   6074  C  C   . GLU   B  1 336 ? -12.462 4.837   -12.089  1.00 50.37  ? 637  GLU   B C   1 
ATOM   6075  O  O   . GLU   B  1 336 ? -12.216 4.183   -11.066  1.00 47.98  ? 637  GLU   B O   1 
ATOM   6076  C  CB  . GLU   B  1 336 ? -10.685 4.952   -13.852  1.00 45.03  ? 637  GLU   B CB  1 
ATOM   6077  C  CG  . GLU   B  1 336 ? -10.058 4.336   -15.096  1.00 49.07  ? 637  GLU   B CG  1 
ATOM   6078  C  CD  . GLU   B  1 336 ? -9.842  2.819   -15.011  1.00 55.88  ? 637  GLU   B CD  1 
ATOM   6079  O  OE1 . GLU   B  1 336 ? -9.796  2.245   -13.902  1.00 57.75  ? 637  GLU   B OE1 1 
ATOM   6080  O  OE2 . GLU   B  1 336 ? -9.705  2.192   -16.077  1.00 57.47  ? 637  GLU   B OE2 1 
ATOM   6081  N  N   . ILE   B  1 337 ? -13.116 5.998   -12.048  1.00 47.00  ? 638  ILE   B N   1 
ATOM   6082  C  CA  . ILE   B  1 337 ? -13.584 6.548   -10.779  1.00 45.04  ? 638  ILE   B CA  1 
ATOM   6083  C  C   . ILE   B  1 337 ? -14.607 5.618   -10.143  1.00 45.30  ? 638  ILE   B C   1 
ATOM   6084  O  O   . ILE   B  1 337 ? -14.596 5.388   -8.928   1.00 45.74  ? 638  ILE   B O   1 
ATOM   6085  C  CB  . ILE   B  1 337 ? -14.150 7.961   -11.007  1.00 42.71  ? 638  ILE   B CB  1 
ATOM   6086  C  CG1 . ILE   B  1 337 ? -13.015 8.909   -11.406  1.00 44.76  ? 638  ILE   B CG1 1 
ATOM   6087  C  CG2 . ILE   B  1 337 ? -14.864 8.476   -9.780   1.00 43.77  ? 638  ILE   B CG2 1 
ATOM   6088  C  CD1 . ILE   B  1 337 ? -13.503 10.173  -12.052  1.00 48.12  ? 638  ILE   B CD1 1 
ATOM   6089  N  N   . ASN   B  1 338 ? -15.491 5.049   -10.958  1.00 44.40  ? 639  ASN   B N   1 
ATOM   6090  C  CA  . ASN   B  1 338 ? -16.525 4.179   -10.426  1.00 46.40  ? 639  ASN   B CA  1 
ATOM   6091  C  C   . ASN   B  1 338 ? -15.982 2.813   -10.050  1.00 46.61  ? 639  ASN   B C   1 
ATOM   6092  O  O   . ASN   B  1 338 ? -16.480 2.202   -9.095   1.00 45.82  ? 639  ASN   B O   1 
ATOM   6093  C  CB  . ASN   B  1 338 ? -17.667 4.070   -11.431  1.00 47.04  ? 639  ASN   B CB  1 
ATOM   6094  C  CG  . ASN   B  1 338 ? -18.543 5.306   -11.417  1.00 47.69  ? 639  ASN   B CG  1 
ATOM   6095  O  OD1 . ASN   B  1 338 ? -19.530 5.375   -10.679  1.00 42.89  ? 639  ASN   B OD1 1 
ATOM   6096  N  ND2 . ASN   B  1 338 ? -18.159 6.308   -12.200  1.00 46.16  ? 639  ASN   B ND2 1 
ATOM   6097  N  N   . ILE   B  1 339 ? -14.969 2.328   -10.775  1.00 40.95  ? 640  ILE   B N   1 
ATOM   6098  C  CA  . ILE   B  1 339 ? -14.225 1.161   -10.311  1.00 43.16  ? 640  ILE   B CA  1 
ATOM   6099  C  C   . ILE   B  1 339 ? -13.629 1.430   -8.933   1.00 53.87  ? 640  ILE   B C   1 
ATOM   6100  O  O   . ILE   B  1 339 ? -13.624 0.558   -8.057   1.00 59.27  ? 640  ILE   B O   1 
ATOM   6101  C  CB  . ILE   B  1 339 ? -13.130 0.781   -11.320  1.00 39.86  ? 640  ILE   B CB  1 
ATOM   6102  C  CG1 . ILE   B  1 339 ? -13.740 0.230   -12.611  1.00 39.58  ? 640  ILE   B CG1 1 
ATOM   6103  C  CG2 . ILE   B  1 339 ? -12.162 -0.220  -10.715  1.00 41.29  ? 640  ILE   B CG2 1 
ATOM   6104  C  CD1 . ILE   B  1 339 ? -12.704 -0.319  -13.534  1.00 41.22  ? 640  ILE   B CD1 1 
ATOM   6105  N  N   . ALA   B  1 340 ? -13.130 2.648   -8.721   1.00 52.57  ? 641  ALA   B N   1 
ATOM   6106  C  CA  . ALA   B  1 340 ? -12.412 2.970   -7.495   1.00 46.88  ? 641  ALA   B CA  1 
ATOM   6107  C  C   . ALA   B  1 340 ? -13.366 3.110   -6.308   1.00 47.27  ? 641  ALA   B C   1 
ATOM   6108  O  O   . ALA   B  1 340 ? -13.086 2.603   -5.213   1.00 49.44  ? 641  ALA   B O   1 
ATOM   6109  C  CB  . ALA   B  1 340 ? -11.597 4.249   -7.700   1.00 43.73  ? 641  ALA   B CB  1 
ATOM   6110  N  N   . VAL   B  1 341 ? -14.490 3.801   -6.505   1.00 44.84  ? 642  VAL   B N   1 
ATOM   6111  C  CA  . VAL   B  1 341 ? -15.466 3.969   -5.430   1.00 46.01  ? 642  VAL   B CA  1 
ATOM   6112  C  C   . VAL   B  1 341 ? -15.953 2.606   -4.948   1.00 50.66  ? 642  VAL   B C   1 
ATOM   6113  O  O   . VAL   B  1 341 ? -15.923 2.303   -3.746   1.00 42.40  ? 642  VAL   B O   1 
ATOM   6114  C  CB  . VAL   B  1 341 ? -16.628 4.862   -5.904   1.00 41.03  ? 642  VAL   B CB  1 
ATOM   6115  C  CG1 . VAL   B  1 341 ? -17.852 4.664   -5.043   1.00 35.50  ? 642  VAL   B CG1 1 
ATOM   6116  C  CG2 . VAL   B  1 341 ? -16.204 6.336   -5.923   1.00 40.07  ? 642  VAL   B CG2 1 
ATOM   6117  N  N   . LEU   B  1 342 ? -16.371 1.751   -5.890   1.00 41.47  ? 643  LEU   B N   1 
ATOM   6118  C  CA  . LEU   B  1 342 ? -16.816 0.398   -5.558   1.00 40.43  ? 643  LEU   B CA  1 
ATOM   6119  C  C   . LEU   B  1 342 ? -15.746 -0.371  -4.793   1.00 48.84  ? 643  LEU   B C   1 
ATOM   6120  O  O   . LEU   B  1 342 ? -16.007 -0.914  -3.712   1.00 52.26  ? 643  LEU   B O   1 
ATOM   6121  C  CB  . LEU   B  1 342 ? -17.194 -0.359  -6.837   1.00 41.31  ? 643  LEU   B CB  1 
ATOM   6122  C  CG  . LEU   B  1 342 ? -18.492 0.079   -7.525   1.00 43.83  ? 643  LEU   B CG  1 
ATOM   6123  C  CD1 . LEU   B  1 342 ? -18.685 -0.587  -8.917   1.00 34.12  ? 643  LEU   B CD1 1 
ATOM   6124  C  CD2 . LEU   B  1 342 ? -19.685 -0.188  -6.609   1.00 32.84  ? 643  LEU   B CD2 1 
ATOM   6125  N  N   . TYR   B  1 343 ? -14.536 -0.452  -5.358   1.00 50.09  ? 644  TYR   B N   1 
ATOM   6126  C  CA  . TYR   B  1 343 ? -13.456 -1.200  -4.723   1.00 55.21  ? 644  TYR   B CA  1 
ATOM   6127  C  C   . TYR   B  1 343 ? -13.179 -0.707  -3.302   1.00 58.85  ? 644  TYR   B C   1 
ATOM   6128  O  O   . TYR   B  1 343 ? -12.799 -1.498  -2.429   1.00 57.18  ? 644  TYR   B O   1 
ATOM   6129  C  CB  . TYR   B  1 343 ? -12.206 -1.109  -5.596   1.00 41.05  ? 644  TYR   B CB  1 
ATOM   6130  C  CG  . TYR   B  1 343 ? -10.906 -1.513  -4.934   1.00 43.31  ? 644  TYR   B CG  1 
ATOM   6131  C  CD1 . TYR   B  1 343 ? -10.552 -2.847  -4.810   1.00 47.66  ? 644  TYR   B CD1 1 
ATOM   6132  C  CD2 . TYR   B  1 343 ? -10.010 -0.552  -4.474   1.00 47.70  ? 644  TYR   B CD2 1 
ATOM   6133  C  CE1 . TYR   B  1 343 ? -9.363  -3.213  -4.227   1.00 54.71  ? 644  TYR   B CE1 1 
ATOM   6134  C  CE2 . TYR   B  1 343 ? -8.816  -0.909  -3.894   1.00 53.73  ? 644  TYR   B CE2 1 
ATOM   6135  C  CZ  . TYR   B  1 343 ? -8.497  -2.241  -3.764   1.00 58.40  ? 644  TYR   B CZ  1 
ATOM   6136  O  OH  . TYR   B  1 343 ? -7.306  -2.608  -3.171   1.00 58.06  ? 644  TYR   B OH  1 
ATOM   6137  N  N   . SER   B  1 344 ? -13.402 0.579   -3.040   1.00 55.43  ? 645  SER   B N   1 
ATOM   6138  C  CA  . SER   B  1 344 ? -13.070 1.130   -1.733   1.00 45.43  ? 645  SER   B CA  1 
ATOM   6139  C  C   . SER   B  1 344 ? -14.125 0.767   -0.694   1.00 48.23  ? 645  SER   B C   1 
ATOM   6140  O  O   . SER   B  1 344 ? -13.794 0.292   0.399    1.00 54.17  ? 645  SER   B O   1 
ATOM   6141  C  CB  . SER   B  1 344 ? -12.895 2.641   -1.846   1.00 40.65  ? 645  SER   B CB  1 
ATOM   6142  O  OG  . SER   B  1 344 ? -11.767 2.934   -2.651   1.00 52.32  ? 645  SER   B OG  1 
ATOM   6143  N  N   . PHE   B  1 345 ? -15.399 0.991   -1.019   1.00 43.18  ? 646  PHE   B N   1 
ATOM   6144  C  CA  . PHE   B  1 345 ? -16.479 0.548   -0.145   1.00 44.75  ? 646  PHE   B CA  1 
ATOM   6145  C  C   . PHE   B  1 345 ? -16.390 -0.948  0.146    1.00 51.44  ? 646  PHE   B C   1 
ATOM   6146  O  O   . PHE   B  1 345 ? -16.593 -1.370  1.286    1.00 54.78  ? 646  PHE   B O   1 
ATOM   6147  C  CB  . PHE   B  1 345 ? -17.839 0.905   -0.756   1.00 37.03  ? 646  PHE   B CB  1 
ATOM   6148  C  CG  . PHE   B  1 345 ? -18.273 2.314   -0.476   1.00 39.02  ? 646  PHE   B CG  1 
ATOM   6149  C  CD1 . PHE   B  1 345 ? -17.512 3.390   -0.915   1.00 39.01  ? 646  PHE   B CD1 1 
ATOM   6150  C  CD2 . PHE   B  1 345 ? -19.430 2.569   0.244    1.00 36.13  ? 646  PHE   B CD2 1 
ATOM   6151  C  CE1 . PHE   B  1 345 ? -17.907 4.701   -0.641   1.00 34.29  ? 646  PHE   B CE1 1 
ATOM   6152  C  CE2 . PHE   B  1 345 ? -19.831 3.872   0.513    1.00 35.34  ? 646  PHE   B CE2 1 
ATOM   6153  C  CZ  . PHE   B  1 345 ? -19.067 4.936   0.071    1.00 33.98  ? 646  PHE   B CZ  1 
ATOM   6154  N  N   . GLN   B  1 346 ? -16.073 -1.766  -0.862   1.00 46.60  ? 647  GLN   B N   1 
ATOM   6155  C  CA  . GLN   B  1 346 ? -16.026 -3.210  -0.639   1.00 48.62  ? 647  GLN   B CA  1 
ATOM   6156  C  C   . GLN   B  1 346 ? -14.821 -3.607  0.198    1.00 57.73  ? 647  GLN   B C   1 
ATOM   6157  O  O   . GLN   B  1 346 ? -14.915 -4.523  1.024    1.00 59.87  ? 647  GLN   B O   1 
ATOM   6158  C  CB  . GLN   B  1 346 ? -16.008 -3.960  -1.969   1.00 45.58  ? 647  GLN   B CB  1 
ATOM   6159  C  CG  . GLN   B  1 346 ? -17.294 -3.801  -2.769   1.00 48.71  ? 647  GLN   B CG  1 
ATOM   6160  C  CD  . GLN   B  1 346 ? -17.191 -4.335  -4.190   1.00 50.42  ? 647  GLN   B CD  1 
ATOM   6161  O  OE1 . GLN   B  1 346 ? -16.115 -4.728  -4.647   1.00 50.83  ? 647  GLN   B OE1 1 
ATOM   6162  N  NE2 . GLN   B  1 346 ? -18.316 -4.349  -4.893   1.00 48.74  ? 647  GLN   B NE2 1 
ATOM   6163  N  N   . SER   B  1 347 ? -13.687 -2.935  -0.005   1.00 56.44  ? 648  SER   B N   1 
ATOM   6164  C  CA  . SER   B  1 347 ? -12.502 -3.230  0.789    1.00 51.04  ? 648  SER   B CA  1 
ATOM   6165  C  C   . SER   B  1 347 ? -12.735 -2.913  2.258    1.00 51.28  ? 648  SER   B C   1 
ATOM   6166  O  O   . SER   B  1 347 ? -12.194 -3.591  3.136    1.00 51.39  ? 648  SER   B O   1 
ATOM   6167  C  CB  . SER   B  1 347 ? -11.298 -2.447  0.267    1.00 47.49  ? 648  SER   B CB  1 
ATOM   6168  O  OG  . SER   B  1 347 ? -10.954 -2.869  -1.041   1.00 63.83  ? 648  SER   B OG  1 
ATOM   6169  N  N   . ASP   B  1 348 ? -13.514 -1.874  2.541    1.00 50.76  ? 649  ASP   B N   1 
ATOM   6170  C  CA  . ASP   B  1 348 ? -13.810 -1.478  3.906    1.00 50.10  ? 649  ASP   B CA  1 
ATOM   6171  C  C   . ASP   B  1 348 ? -15.084 -2.123  4.424    1.00 53.11  ? 649  ASP   B C   1 
ATOM   6172  O  O   . ASP   B  1 348 ? -15.598 -1.701  5.457    1.00 45.60  ? 649  ASP   B O   1 
ATOM   6173  C  CB  . ASP   B  1 348 ? -13.903 0.040   4.003    1.00 39.20  ? 649  ASP   B CB  1 
ATOM   6174  C  CG  . ASP   B  1 348 ? -12.554 0.709   3.858    1.00 51.08  ? 649  ASP   B CG  1 
ATOM   6175  O  OD1 . ASP   B  1 348 ? -11.545 -0.019  3.750    1.00 46.37  ? 649  ASP   B OD1 1 
ATOM   6176  O  OD2 . ASP   B  1 348 ? -12.498 1.958   3.850    1.00 51.61  ? 649  ASP   B OD2 1 
ATOM   6177  N  N   . LYS   B  1 349 ? -15.587 -3.137  3.719    1.00 59.42  ? 650  LYS   B N   1 
ATOM   6178  C  CA  . LYS   B  1 349 ? -16.814 -3.856  4.059    1.00 62.12  ? 650  LYS   B CA  1 
ATOM   6179  C  C   . LYS   B  1 349 ? -17.942 -2.898  4.446    1.00 63.89  ? 650  LYS   B C   1 
ATOM   6180  O  O   . LYS   B  1 349 ? -18.625 -3.066  5.455    1.00 70.74  ? 650  LYS   B O   1 
ATOM   6181  C  CB  . LYS   B  1 349 ? -16.548 -4.891  5.150    1.00 60.50  ? 650  LYS   B CB  1 
ATOM   6182  C  CG  . LYS   B  1 349 ? -15.456 -5.886  4.756    1.00 71.42  ? 650  LYS   B CG  1 
ATOM   6183  C  CD  . LYS   B  1 349 ? -15.193 -6.956  5.815    1.00 77.93  ? 650  LYS   B CD  1 
ATOM   6184  C  CE  . LYS   B  1 349 ? -16.155 -8.142  5.695    1.00 86.91  ? 650  LYS   B CE  1 
ATOM   6185  N  NZ  . LYS   B  1 349 ? -15.961 -8.948  4.449    1.00 92.43  ? 650  LYS   B NZ  1 
ATOM   6186  N  N   . VAL   B  1 350 ? -18.142 -1.882  3.611    1.00 48.77  ? 651  VAL   B N   1 
ATOM   6187  C  CA  . VAL   B  1 350 ? -19.280 -0.974  3.713    1.00 43.57  ? 651  VAL   B CA  1 
ATOM   6188  C  C   . VAL   B  1 350 ? -20.252 -1.294  2.581    1.00 44.75  ? 651  VAL   B C   1 
ATOM   6189  O  O   . VAL   B  1 350 ? -19.854 -1.350  1.406    1.00 41.79  ? 651  VAL   B O   1 
ATOM   6190  C  CB  . VAL   B  1 350 ? -18.831 0.494   3.658    1.00 39.12  ? 651  VAL   B CB  1 
ATOM   6191  C  CG1 . VAL   B  1 350 ? -20.026 1.415   3.740    1.00 39.27  ? 651  VAL   B CG1 1 
ATOM   6192  C  CG2 . VAL   B  1 350 ? -17.831 0.789   4.769    1.00 46.23  ? 651  VAL   B CG2 1 
ATOM   6193  N  N   . THR   B  1 351 ? -21.522 -1.506  2.934    1.00 33.21  ? 652  THR   B N   1 
ATOM   6194  C  CA  . THR   B  1 351 ? -22.531 -1.874  1.953    1.00 34.00  ? 652  THR   B CA  1 
ATOM   6195  C  C   . THR   B  1 351 ? -22.544 -0.894  0.793    1.00 40.46  ? 652  THR   B C   1 
ATOM   6196  O  O   . THR   B  1 351 ? -22.570 0.325   0.993    1.00 42.50  ? 652  THR   B O   1 
ATOM   6197  C  CB  . THR   B  1 351 ? -23.916 -1.914  2.584    1.00 37.07  ? 652  THR   B CB  1 
ATOM   6198  O  OG1 . THR   B  1 351 ? -23.861 -2.611  3.831    1.00 48.18  ? 652  THR   B OG1 1 
ATOM   6199  C  CG2 . THR   B  1 351 ? -24.871 -2.646  1.649    1.00 32.83  ? 652  THR   B CG2 1 
ATOM   6200  N  N   . ILE   B  1 352 ? -22.516 -1.445  -0.421   1.00 40.46  ? 653  ILE   B N   1 
ATOM   6201  C  CA  . ILE   B  1 352 ? -22.656 -0.670  -1.652   1.00 39.21  ? 653  ILE   B CA  1 
ATOM   6202  C  C   . ILE   B  1 352 ? -23.089 -1.651  -2.724   1.00 40.56  ? 653  ILE   B C   1 
ATOM   6203  O  O   . ILE   B  1 352 ? -22.821 -2.855  -2.625   1.00 40.32  ? 653  ILE   B O   1 
ATOM   6204  C  CB  . ILE   B  1 352 ? -21.335 0.041   -2.038   1.00 37.23  ? 653  ILE   B CB  1 
ATOM   6205  C  CG1 . ILE   B  1 352 ? -21.579 1.152   -3.056   1.00 38.47  ? 653  ILE   B CG1 1 
ATOM   6206  C  CG2 . ILE   B  1 352 ? -20.347 -0.953  -2.624   1.00 32.49  ? 653  ILE   B CG2 1 
ATOM   6207  C  CD1 . ILE   B  1 352 ? -20.353 2.025   -3.307   1.00 37.64  ? 653  ILE   B CD1 1 
ATOM   6208  N  N   . VAL   B  1 353 ? -23.785 -1.147  -3.740   1.00 42.22  ? 654  VAL   B N   1 
ATOM   6209  C  CA  . VAL   B  1 353 ? -24.229 -1.970  -4.864   1.00 48.02  ? 654  VAL   B CA  1 
ATOM   6210  C  C   . VAL   B  1 353 ? -23.875 -1.261  -6.169   1.00 41.07  ? 654  VAL   B C   1 
ATOM   6211  O  O   . VAL   B  1 353 ? -24.076 -0.047  -6.288   1.00 41.86  ? 654  VAL   B O   1 
ATOM   6212  C  CB  . VAL   B  1 353 ? -25.740 -2.276  -4.787   1.00 45.43  ? 654  VAL   B CB  1 
ATOM   6213  C  CG1 . VAL   B  1 353 ? -26.552 -0.990  -4.646   1.00 36.05  ? 654  VAL   B CG1 1 
ATOM   6214  C  CG2 . VAL   B  1 353 ? -26.179 -3.043  -6.026   1.00 52.99  ? 654  VAL   B CG2 1 
ATOM   6215  N  N   . ASP   B  1 354 ? -23.317 -2.009  -7.133   1.00 43.16  ? 655  ASP   B N   1 
ATOM   6216  C  CA  . ASP   B  1 354 ? -23.035 -1.438  -8.453   1.00 35.74  ? 655  ASP   B CA  1 
ATOM   6217  C  C   . ASP   B  1 354 ? -24.323 -1.291  -9.267   1.00 40.41  ? 655  ASP   B C   1 
ATOM   6218  O  O   . ASP   B  1 354 ? -25.386 -1.804  -8.907   1.00 42.21  ? 655  ASP   B O   1 
ATOM   6219  C  CB  . ASP   B  1 354 ? -22.001 -2.274  -9.228   1.00 39.44  ? 655  ASP   B CB  1 
ATOM   6220  C  CG  . ASP   B  1 354 ? -22.552 -3.593  -9.726   1.00 46.65  ? 655  ASP   B CG  1 
ATOM   6221  O  OD1 . ASP   B  1 354 ? -23.347 -3.598  -10.677  1.00 51.41  ? 655  ASP   B OD1 1 
ATOM   6222  O  OD2 . ASP   B  1 354 ? -22.177 -4.644  -9.180   1.00 54.78  ? 655  ASP   B OD2 1 
ATOM   6223  N  N   . HIS   B  1 355 ? -24.226 -0.571  -10.394  1.00 36.01  ? 656  HIS   B N   1 
ATOM   6224  C  CA  . HIS   B  1 355 ? -25.441 -0.311  -11.146  1.00 32.85  ? 656  HIS   B CA  1 
ATOM   6225  C  C   . HIS   B  1 355 ? -25.939 -1.552  -11.897  1.00 39.61  ? 656  HIS   B C   1 
ATOM   6226  O  O   . HIS   B  1 355 ? -27.145 -1.667  -12.141  1.00 47.85  ? 656  HIS   B O   1 
ATOM   6227  C  CB  . HIS   B  1 355 ? -25.225 0.864   -12.092  1.00 38.11  ? 656  HIS   B CB  1 
ATOM   6228  C  CG  . HIS   B  1 355 ? -23.960 0.779   -12.874  1.00 40.85  ? 656  HIS   B CG  1 
ATOM   6229  N  ND1 . HIS   B  1 355 ? -22.727 1.046   -12.320  1.00 42.30  ? 656  HIS   B ND1 1 
ATOM   6230  C  CD2 . HIS   B  1 355 ? -23.732 0.462   -14.169  1.00 34.85  ? 656  HIS   B CD2 1 
ATOM   6231  C  CE1 . HIS   B  1 355 ? -21.793 0.899   -13.241  1.00 41.40  ? 656  HIS   B CE1 1 
ATOM   6232  N  NE2 . HIS   B  1 355 ? -22.377 0.545   -14.370  1.00 42.54  ? 656  HIS   B NE2 1 
ATOM   6233  N  N   . HIS   B  1 356 ? -25.059 -2.499  -12.243  1.00 33.30  ? 657  HIS   B N   1 
ATOM   6234  C  CA  . HIS   B  1 356 ? -25.530 -3.724  -12.898  1.00 41.78  ? 657  HIS   B CA  1 
ATOM   6235  C  C   . HIS   B  1 356 ? -26.346 -4.575  -11.928  1.00 36.73  ? 657  HIS   B C   1 
ATOM   6236  O  O   . HIS   B  1 356 ? -27.465 -5.004  -12.239  1.00 33.31  ? 657  HIS   B O   1 
ATOM   6237  C  CB  . HIS   B  1 356 ? -24.354 -4.548  -13.461  1.00 39.46  ? 657  HIS   B CB  1 
ATOM   6238  C  CG  . HIS   B  1 356 ? -23.374 -3.748  -14.271  1.00 42.74  ? 657  HIS   B CG  1 
ATOM   6239  N  ND1 . HIS   B  1 356 ? -23.650 -3.300  -15.546  1.00 37.34  ? 657  HIS   B ND1 1 
ATOM   6240  C  CD2 . HIS   B  1 356 ? -22.126 -3.303  -13.977  1.00 40.15  ? 657  HIS   B CD2 1 
ATOM   6241  C  CE1 . HIS   B  1 356 ? -22.621 -2.602  -15.994  1.00 41.02  ? 657  HIS   B CE1 1 
ATOM   6242  N  NE2 . HIS   B  1 356 ? -21.680 -2.596  -15.068  1.00 42.21  ? 657  HIS   B NE2 1 
ATOM   6243  N  N   . SER   B  1 357 ? -25.786 -4.841  -10.749  1.00 45.67  ? 658  SER   B N   1 
ATOM   6244  C  CA  . SER   B  1 357 ? -26.517 -5.602  -9.742   1.00 50.41  ? 658  SER   B CA  1 
ATOM   6245  C  C   . SER   B  1 357 ? -27.822 -4.908  -9.361   1.00 35.40  ? 658  SER   B C   1 
ATOM   6246  O  O   . SER   B  1 357 ? -28.873 -5.552  -9.265   1.00 33.19  ? 658  SER   B O   1 
ATOM   6247  C  CB  . SER   B  1 357 ? -25.632 -5.815  -8.515   1.00 53.66  ? 658  SER   B CB  1 
ATOM   6248  O  OG  . SER   B  1 357 ? -26.119 -6.887  -7.736   1.00 62.53  ? 658  SER   B OG  1 
ATOM   6249  N  N   . ALA   B  1 358 ? -27.789 -3.587  -9.187   1.00 34.23  ? 659  ALA   B N   1 
ATOM   6250  C  CA  . ALA   B  1 358 ? -28.976 -2.897  -8.689   1.00 36.83  ? 659  ALA   B CA  1 
ATOM   6251  C  C   . ALA   B  1 358 ? -30.087 -2.868  -9.731   1.00 42.39  ? 659  ALA   B C   1 
ATOM   6252  O  O   . ALA   B  1 358 ? -31.264 -3.059  -9.395   1.00 38.04  ? 659  ALA   B O   1 
ATOM   6253  C  CB  . ALA   B  1 358 ? -28.617 -1.479  -8.250   1.00 29.79  ? 659  ALA   B CB  1 
ATOM   6254  N  N   . THR   B  1 359 ? -29.744 -2.626  -11.003  1.00 41.26  ? 660  THR   B N   1 
ATOM   6255  C  CA  . THR   B  1 359 ? -30.786 -2.596  -12.028  1.00 35.35  ? 660  THR   B CA  1 
ATOM   6256  C  C   . THR   B  1 359 ? -31.353 -3.990  -12.278  1.00 35.59  ? 660  THR   B C   1 
ATOM   6257  O  O   . THR   B  1 359 ? -32.564 -4.145  -12.463  1.00 40.50  ? 660  THR   B O   1 
ATOM   6258  C  CB  . THR   B  1 359 ? -30.261 -1.981  -13.321  1.00 37.72  ? 660  THR   B CB  1 
ATOM   6259  O  OG1 . THR   B  1 359 ? -29.085 -2.680  -13.760  1.00 43.81  ? 660  THR   B OG1 1 
ATOM   6260  C  CG2 . THR   B  1 359 ? -29.955 -0.508  -13.112  1.00 29.89  ? 660  THR   B CG2 1 
ATOM   6261  N  N   . GLU   B  1 360 ? -30.504 -5.018  -12.263  1.00 30.26  ? 661  GLU   B N   1 
ATOM   6262  C  CA  . GLU   B  1 360 ? -31.000 -6.390  -12.358  1.00 32.10  ? 661  GLU   B CA  1 
ATOM   6263  C  C   . GLU   B  1 360 ? -32.003 -6.694  -11.242  1.00 43.91  ? 661  GLU   B C   1 
ATOM   6264  O  O   . GLU   B  1 360 ? -33.068 -7.276  -11.489  1.00 45.39  ? 661  GLU   B O   1 
ATOM   6265  C  CB  . GLU   B  1 360 ? -29.825 -7.359  -12.305  1.00 37.17  ? 661  GLU   B CB  1 
ATOM   6266  C  CG  . GLU   B  1 360 ? -30.227 -8.807  -12.330  1.00 56.61  ? 661  GLU   B CG  1 
ATOM   6267  C  CD  . GLU   B  1 360 ? -29.026 -9.746  -12.275  1.00 78.17  ? 661  GLU   B CD  1 
ATOM   6268  O  OE1 . GLU   B  1 360 ? -27.980 -9.366  -11.696  1.00 81.65  ? 661  GLU   B OE1 1 
ATOM   6269  O  OE2 . GLU   B  1 360 ? -29.129 -10.865 -12.825  1.00 85.23  ? 661  GLU   B OE2 1 
ATOM   6270  N  N   . SER   B  1 361 ? -31.668 -6.313  -9.999   1.00 36.06  ? 662  SER   B N   1 
ATOM   6271  C  CA  A SER   B  1 361 ? -32.589 -6.524  -8.887   0.50 36.45  ? 662  SER   B CA  1 
ATOM   6272  C  CA  B SER   B  1 361 ? -32.591 -6.518  -8.884   0.50 36.46  ? 662  SER   B CA  1 
ATOM   6273  C  C   . SER   B  1 361 ? -33.921 -5.828  -9.138   1.00 33.94  ? 662  SER   B C   1 
ATOM   6274  O  O   . SER   B  1 361 ? -34.983 -6.396  -8.865   1.00 37.59  ? 662  SER   B O   1 
ATOM   6275  C  CB  A SER   B  1 361 ? -31.961 -6.029  -7.578   0.50 38.50  ? 662  SER   B CB  1 
ATOM   6276  C  CB  B SER   B  1 361 ? -31.980 -5.999  -7.581   0.50 38.50  ? 662  SER   B CB  1 
ATOM   6277  O  OG  A SER   B  1 361 ? -30.752 -6.717  -7.275   0.50 30.73  ? 662  SER   B OG  1 
ATOM   6278  O  OG  B SER   B  1 361 ? -32.294 -4.628  -7.385   0.50 34.93  ? 662  SER   B OG  1 
ATOM   6279  N  N   . PHE   B  1 362 ? -33.884 -4.600  -9.664   1.00 31.34  ? 663  PHE   B N   1 
ATOM   6280  C  CA  . PHE   B  1 362 ? -35.127 -3.866  -9.883   1.00 34.77  ? 663  PHE   B CA  1 
ATOM   6281  C  C   . PHE   B  1 362 ? -36.026 -4.559  -10.910  1.00 41.57  ? 663  PHE   B C   1 
ATOM   6282  O  O   . PHE   B  1 362 ? -37.247 -4.632  -10.718  1.00 47.92  ? 663  PHE   B O   1 
ATOM   6283  C  CB  . PHE   B  1 362 ? -34.848 -2.418  -10.295  1.00 31.43  ? 663  PHE   B CB  1 
ATOM   6284  C  CG  . PHE   B  1 362 ? -36.098 -1.623  -10.467  1.00 39.39  ? 663  PHE   B CG  1 
ATOM   6285  C  CD1 . PHE   B  1 362 ? -36.836 -1.210  -9.359   1.00 39.83  ? 663  PHE   B CD1 1 
ATOM   6286  C  CD2 . PHE   B  1 362 ? -36.606 -1.377  -11.736  1.00 43.49  ? 663  PHE   B CD2 1 
ATOM   6287  C  CE1 . PHE   B  1 362 ? -38.033 -0.509  -9.513   1.00 32.22  ? 663  PHE   B CE1 1 
ATOM   6288  C  CE2 . PHE   B  1 362 ? -37.790 -0.678  -11.897  1.00 47.34  ? 663  PHE   B CE2 1 
ATOM   6289  C  CZ  . PHE   B  1 362 ? -38.505 -0.239  -10.785  1.00 40.48  ? 663  PHE   B CZ  1 
ATOM   6290  N  N   . ILE   B  1 363 ? -35.451 -5.065  -12.007  1.00 42.93  ? 664  ILE   B N   1 
ATOM   6291  C  CA  . ILE   B  1 363 ? -36.242 -5.843  -12.963  1.00 41.36  ? 664  ILE   B CA  1 
ATOM   6292  C  C   . ILE   B  1 363 ? -36.962 -6.981  -12.242  1.00 44.36  ? 664  ILE   B C   1 
ATOM   6293  O  O   . ILE   B  1 363 ? -38.166 -7.196  -12.426  1.00 37.46  ? 664  ILE   B O   1 
ATOM   6294  C  CB  . ILE   B  1 363 ? -35.353 -6.383  -14.098  1.00 35.29  ? 664  ILE   B CB  1 
ATOM   6295  C  CG1 . ILE   B  1 363 ? -34.766 -5.243  -14.950  1.00 47.62  ? 664  ILE   B CG1 1 
ATOM   6296  C  CG2 . ILE   B  1 363 ? -36.142 -7.384  -14.920  1.00 32.17  ? 664  ILE   B CG2 1 
ATOM   6297  C  CD1 . ILE   B  1 363 ? -35.771 -4.524  -15.864  1.00 47.28  ? 664  ILE   B CD1 1 
ATOM   6298  N  N   . LYS   B  1 364 ? -36.227 -7.716  -11.397  1.00 35.85  ? 665  LYS   B N   1 
ATOM   6299  C  CA  . LYS   B  1 364 ? -36.835 -8.773  -10.588  1.00 43.91  ? 665  LYS   B CA  1 
ATOM   6300  C  C   . LYS   B  1 364 ? -37.933 -8.226  -9.671   1.00 45.32  ? 665  LYS   B C   1 
ATOM   6301  O  O   . LYS   B  1 364 ? -39.019 -8.816  -9.574   1.00 48.62  ? 665  LYS   B O   1 
ATOM   6302  C  CB  . LYS   B  1 364 ? -35.758 -9.493  -9.781   1.00 45.74  ? 665  LYS   B CB  1 
ATOM   6303  C  CG  . LYS   B  1 364 ? -36.293 -10.341 -8.639   1.00 57.36  ? 665  LYS   B CG  1 
ATOM   6304  C  CD  . LYS   B  1 364 ? -36.103 -11.832 -8.895   1.00 74.15  ? 665  LYS   B CD  1 
ATOM   6305  C  CE  . LYS   B  1 364 ? -37.084 -12.373 -9.932   1.00 84.31  ? 665  LYS   B CE  1 
ATOM   6306  N  NZ  . LYS   B  1 364 ? -38.516 -12.310 -9.503   1.00 84.57  ? 665  LYS   B NZ  1 
ATOM   6307  N  N   . HIS   B  1 365 ? -37.675 -7.103  -8.994   1.00 41.90  ? 666  HIS   B N   1 
ATOM   6308  C  CA  . HIS   B  1 365 ? -38.724 -6.482  -8.186   1.00 38.82  ? 666  HIS   B CA  1 
ATOM   6309  C  C   . HIS   B  1 365 ? -39.954 -6.192  -9.045   1.00 47.94  ? 666  HIS   B C   1 
ATOM   6310  O  O   . HIS   B  1 365 ? -41.088 -6.512  -8.661   1.00 43.34  ? 666  HIS   B O   1 
ATOM   6311  C  CB  . HIS   B  1 365 ? -38.192 -5.203  -7.527   1.00 34.70  ? 666  HIS   B CB  1 
ATOM   6312  C  CG  . HIS   B  1 365 ? -39.226 -4.426  -6.762   1.00 33.26  ? 666  HIS   B CG  1 
ATOM   6313  N  ND1 . HIS   B  1 365 ? -39.946 -4.965  -5.715   1.00 37.25  ? 666  HIS   B ND1 1 
ATOM   6314  C  CD2 . HIS   B  1 365 ? -39.653 -3.146  -6.889   1.00 35.09  ? 666  HIS   B CD2 1 
ATOM   6315  C  CE1 . HIS   B  1 365 ? -40.774 -4.051  -5.235   1.00 33.23  ? 666  HIS   B CE1 1 
ATOM   6316  N  NE2 . HIS   B  1 365 ? -40.615 -2.937  -5.928   1.00 36.25  ? 666  HIS   B NE2 1 
ATOM   6317  N  N   . MET   B  1 366 ? -39.735 -5.616  -10.237  1.00 48.19  ? 667  MET   B N   1 
ATOM   6318  C  CA  . MET   B  1 366 ? -40.831 -5.367  -11.172  1.00 45.09  ? 667  MET   B CA  1 
ATOM   6319  C  C   . MET   B  1 366 ? -41.642 -6.630  -11.435  1.00 37.35  ? 667  MET   B C   1 
ATOM   6320  O  O   . MET   B  1 366 ? -42.871 -6.624  -11.301  1.00 41.44  ? 667  MET   B O   1 
ATOM   6321  C  CB  . MET   B  1 366 ? -40.285 -4.800  -12.482  1.00 44.92  ? 667  MET   B CB  1 
ATOM   6322  C  CG  . MET   B  1 366 ? -40.258 -3.297  -12.522  1.00 49.24  ? 667  MET   B CG  1 
ATOM   6323  S  SD  . MET   B  1 366 ? -40.004 -2.632  -14.195  1.00 50.62  ? 667  MET   B SD  1 
ATOM   6324  C  CE  . MET   B  1 366 ? -41.585 -2.927  -14.960  1.00 51.60  ? 667  MET   B CE  1 
ATOM   6325  N  N   . GLU   B  1 367 ? -40.976 -7.720  -11.835  1.00 36.66  ? 668  GLU   B N   1 
ATOM   6326  C  CA  A GLU   B  1 367 ? -41.674 -8.982  -12.055  0.46 45.65  ? 668  GLU   B CA  1 
ATOM   6327  C  CA  B GLU   B  1 367 ? -41.706 -8.965  -12.065  0.54 45.45  ? 668  GLU   B CA  1 
ATOM   6328  C  C   . GLU   B  1 367 ? -42.521 -9.348  -10.839  1.00 47.70  ? 668  GLU   B C   1 
ATOM   6329  O  O   . GLU   B  1 367 ? -43.698 -9.704  -10.958  1.00 43.93  ? 668  GLU   B O   1 
ATOM   6330  C  CB  A GLU   B  1 367 ? -40.640 -10.067 -12.366  0.46 51.69  ? 668  GLU   B CB  1 
ATOM   6331  C  CB  B GLU   B  1 367 ? -40.775 -10.122 -12.433  0.54 51.66  ? 668  GLU   B CB  1 
ATOM   6332  C  CG  A GLU   B  1 367 ? -41.143 -11.496 -12.400  0.46 54.58  ? 668  GLU   B CG  1 
ATOM   6333  C  CG  B GLU   B  1 367 ? -39.402 -9.763  -12.916  0.54 54.78  ? 668  GLU   B CG  1 
ATOM   6334  C  CD  A GLU   B  1 367 ? -40.003 -12.512 -12.386  0.46 54.74  ? 668  GLU   B CD  1 
ATOM   6335  C  CD  B GLU   B  1 367 ? -39.240 -9.905  -14.416  0.54 52.58  ? 668  GLU   B CD  1 
ATOM   6336  O  OE1 A GLU   B  1 367 ? -38.826 -12.110 -12.511  0.46 51.52  ? 668  GLU   B OE1 1 
ATOM   6337  O  OE1 B GLU   B  1 367 ? -39.574 -8.946  -15.150  0.54 46.06  ? 668  GLU   B OE1 1 
ATOM   6338  O  OE2 A GLU   B  1 367 ? -40.282 -13.719 -12.241  0.46 59.96  ? 668  GLU   B OE2 1 
ATOM   6339  O  OE2 B GLU   B  1 367 ? -38.771 -10.976 -14.851  0.54 35.96  ? 668  GLU   B OE2 1 
ATOM   6340  N  N   . ASN   B  1 368 ? -41.923 -9.259  -9.650   1.00 53.39  ? 669  ASN   B N   1 
ATOM   6341  C  CA  . ASN   B  1 368 ? -42.653 -9.584  -8.426   1.00 46.81  ? 669  ASN   B CA  1 
ATOM   6342  C  C   . ASN   B  1 368 ? -43.894 -8.710  -8.280   1.00 43.87  ? 669  ASN   B C   1 
ATOM   6343  O  O   . ASN   B  1 368 ? -45.004 -9.216  -8.081   1.00 43.30  ? 669  ASN   B O   1 
ATOM   6344  C  CB  . ASN   B  1 368 ? -41.736 -9.432  -7.213   1.00 47.51  ? 669  ASN   B CB  1 
ATOM   6345  C  CG  . ASN   B  1 368 ? -40.640 -10.475 -7.174   1.00 49.20  ? 669  ASN   B CG  1 
ATOM   6346  O  OD1 . ASN   B  1 368 ? -40.800 -11.576 -7.706   1.00 58.06  ? 669  ASN   B OD1 1 
ATOM   6347  N  ND2 . ASN   B  1 368 ? -39.517 -10.136 -6.540   1.00 46.82  ? 669  ASN   B ND2 1 
ATOM   6348  N  N   . GLU   B  1 369 ? -43.730 -7.394  -8.426   1.00 41.19  ? 670  GLU   B N   1 
ATOM   6349  C  CA  . GLU   B  1 369 ? -44.832 -6.474  -8.159   1.00 42.75  ? 670  GLU   B CA  1 
ATOM   6350  C  C   . GLU   B  1 369 ? -46.004 -6.705  -9.105   1.00 50.89  ? 670  GLU   B C   1 
ATOM   6351  O  O   . GLU   B  1 369 ? -47.163 -6.730  -8.672   1.00 50.74  ? 670  GLU   B O   1 
ATOM   6352  C  CB  . GLU   B  1 369 ? -44.340 -5.028  -8.242   1.00 30.99  ? 670  GLU   B CB  1 
ATOM   6353  C  CG  . GLU   B  1 369 ? -43.416 -4.646  -7.116   1.00 38.31  ? 670  GLU   B CG  1 
ATOM   6354  C  CD  . GLU   B  1 369 ? -44.170 -4.440  -5.794   1.00 42.71  ? 670  GLU   B CD  1 
ATOM   6355  O  OE1 . GLU   B  1 369 ? -44.224 -3.282  -5.313   1.00 42.73  ? 670  GLU   B OE1 1 
ATOM   6356  O  OE2 . GLU   B  1 369 ? -44.721 -5.430  -5.268   1.00 39.07  ? 670  GLU   B OE2 1 
ATOM   6357  N  N   . TYR   B  1 370 ? -45.728 -6.858  -10.410  1.00 48.64  ? 671  TYR   B N   1 
ATOM   6358  C  CA  . TYR   B  1 370 ? -46.811 -7.143  -11.343  1.00 38.87  ? 671  TYR   B CA  1 
ATOM   6359  C  C   . TYR   B  1 370 ? -47.491 -8.451  -10.975  1.00 47.04  ? 671  TYR   B C   1 
ATOM   6360  O  O   . TYR   B  1 370 ? -48.725 -8.546  -10.977  1.00 58.95  ? 671  TYR   B O   1 
ATOM   6361  C  CB  . TYR   B  1 370 ? -46.289 -7.173  -12.795  1.00 37.15  ? 671  TYR   B CB  1 
ATOM   6362  C  CG  . TYR   B  1 370 ? -46.258 -5.787  -13.417  1.00 40.92  ? 671  TYR   B CG  1 
ATOM   6363  C  CD1 . TYR   B  1 370 ? -45.187 -4.934  -13.204  1.00 39.99  ? 671  TYR   B CD1 1 
ATOM   6364  C  CD2 . TYR   B  1 370 ? -47.324 -5.319  -14.175  1.00 43.00  ? 671  TYR   B CD2 1 
ATOM   6365  C  CE1 . TYR   B  1 370 ? -45.168 -3.667  -13.735  1.00 37.09  ? 671  TYR   B CE1 1 
ATOM   6366  C  CE2 . TYR   B  1 370 ? -47.314 -4.045  -14.715  1.00 36.92  ? 671  TYR   B CE2 1 
ATOM   6367  C  CZ  . TYR   B  1 370 ? -46.237 -3.225  -14.486  1.00 42.15  ? 671  TYR   B CZ  1 
ATOM   6368  O  OH  . TYR   B  1 370 ? -46.224 -1.952  -15.013  1.00 48.71  ? 671  TYR   B OH  1 
ATOM   6369  N  N   . ARG   B  1 371 ? -46.694 -9.459  -10.613  1.00 44.34  ? 672  ARG   B N   1 
ATOM   6370  C  CA  . ARG   B  1 371 ? -47.216 -10.798 -10.336  1.00 51.47  ? 672  ARG   B CA  1 
ATOM   6371  C  C   . ARG   B  1 371 ? -48.228 -10.798 -9.188   1.00 53.90  ? 672  ARG   B C   1 
ATOM   6372  O  O   . ARG   B  1 371 ? -49.207 -11.549 -9.219   1.00 58.28  ? 672  ARG   B O   1 
ATOM   6373  C  CB  . ARG   B  1 371 ? -46.038 -11.723 -10.036  1.00 63.01  ? 672  ARG   B CB  1 
ATOM   6374  C  CG  . ARG   B  1 371 ? -46.343 -13.136 -9.602   1.00 74.67  ? 672  ARG   B CG  1 
ATOM   6375  C  CD  . ARG   B  1 371 ? -45.038 -13.924 -9.674   1.00 89.09  ? 672  ARG   B CD  1 
ATOM   6376  N  NE  . ARG   B  1 371 ? -44.560 -13.983 -11.060  1.00 101.09 ? 672  ARG   B NE  1 
ATOM   6377  C  CZ  . ARG   B  1 371 ? -43.284 -14.071 -11.433  1.00 102.84 ? 672  ARG   B CZ  1 
ATOM   6378  N  NH1 . ARG   B  1 371 ? -42.316 -14.100 -10.524  1.00 104.02 ? 672  ARG   B NH1 1 
ATOM   6379  N  NH2 . ARG   B  1 371 ? -42.977 -14.121 -12.727  1.00 98.70  ? 672  ARG   B NH2 1 
ATOM   6380  N  N   . CYS   B  1 372 ? -48.026 -9.958  -8.173   1.00 47.35  ? 673  CYS   B N   1 
ATOM   6381  C  CA  . CYS   B  1 372 ? -48.885 -10.012 -6.994   1.00 61.98  ? 673  CYS   B CA  1 
ATOM   6382  C  C   . CYS   B  1 372 ? -49.678 -8.741  -6.726   1.00 61.93  ? 673  CYS   B C   1 
ATOM   6383  O  O   . CYS   B  1 372 ? -50.687 -8.808  -6.021   1.00 64.83  ? 673  CYS   B O   1 
ATOM   6384  C  CB  . CYS   B  1 372 ? -48.060 -10.343 -5.742   1.00 62.68  ? 673  CYS   B CB  1 
ATOM   6385  S  SG  . CYS   B  1 372 ? -47.129 -8.939  -5.146   1.00 75.76  ? 673  CYS   B SG  1 
ATOM   6386  N  N   . ARG   B  1 373 ? -49.261 -7.597  -7.259   1.00 56.51  ? 674  ARG   B N   1 
ATOM   6387  C  CA  . ARG   B  1 373 ? -49.937 -6.331  -7.020   1.00 46.68  ? 674  ARG   B CA  1 
ATOM   6388  C  C   . ARG   B  1 373 ? -50.634 -5.794  -8.258   1.00 49.64  ? 674  ARG   B C   1 
ATOM   6389  O  O   . ARG   B  1 373 ? -51.405 -4.836  -8.146   1.00 44.17  ? 674  ARG   B O   1 
ATOM   6390  C  CB  . ARG   B  1 373 ? -48.927 -5.287  -6.507   1.00 46.40  ? 674  ARG   B CB  1 
ATOM   6391  C  CG  . ARG   B  1 373 ? -49.504 -4.116  -5.739   1.00 42.17  ? 674  ARG   B CG  1 
ATOM   6392  C  CD  . ARG   B  1 373 ? -48.400 -3.149  -5.306   1.00 44.41  ? 674  ARG   B CD  1 
ATOM   6393  N  NE  . ARG   B  1 373 ? -48.928 -2.060  -4.492   1.00 42.76  ? 674  ARG   B NE  1 
ATOM   6394  C  CZ  . ARG   B  1 373 ? -48.325 -0.892  -4.288   1.00 46.33  ? 674  ARG   B CZ  1 
ATOM   6395  N  NH1 . ARG   B  1 373 ? -47.149 -0.632  -4.845   1.00 41.14  ? 674  ARG   B NH1 1 
ATOM   6396  N  NH2 . ARG   B  1 373 ? -48.908 0.024   -3.514   1.00 45.13  ? 674  ARG   B NH2 1 
ATOM   6397  N  N   . GLY   B  1 374 ? -50.384 -6.384  -9.429   1.00 52.40  ? 675  GLY   B N   1 
ATOM   6398  C  CA  . GLY   B  1 374 ? -50.955 -5.895  -10.670  1.00 55.10  ? 675  GLY   B CA  1 
ATOM   6399  C  C   . GLY   B  1 374 ? -50.249 -4.710  -11.286  1.00 52.79  ? 675  GLY   B C   1 
ATOM   6400  O  O   . GLY   B  1 374 ? -50.877 -3.947  -12.031  1.00 48.60  ? 675  GLY   B O   1 
ATOM   6401  N  N   . GLY   B  1 375 ? -48.953 -4.533  -11.010  1.00 45.95  ? 676  GLY   B N   1 
ATOM   6402  C  CA  . GLY   B  1 375 ? -48.232 -3.356  -11.467  1.00 45.09  ? 676  GLY   B CA  1 
ATOM   6403  C  C   . GLY   B  1 375 ? -47.208 -2.814  -10.492  1.00 52.16  ? 676  GLY   B C   1 
ATOM   6404  O  O   . GLY   B  1 375 ? -47.141 -3.216  -9.330   1.00 53.38  ? 676  GLY   B O   1 
ATOM   6405  N  N   . CYS   B  1 376 ? -46.390 -1.882  -10.984  1.00 49.64  ? 677  CYS   B N   1 
ATOM   6406  C  CA  . CYS   B  1 376 ? -45.326 -1.253  -10.218  1.00 38.71  ? 677  CYS   B CA  1 
ATOM   6407  C  C   . CYS   B  1 376 ? -44.981 0.080   -10.861  1.00 38.37  ? 677  CYS   B C   1 
ATOM   6408  O  O   . CYS   B  1 376 ? -44.470 0.092   -11.991  1.00 43.98  ? 677  CYS   B O   1 
ATOM   6409  C  CB  . CYS   B  1 376 ? -44.083 -2.147  -10.167  1.00 32.75  ? 677  CYS   B CB  1 
ATOM   6410  S  SG  . CYS   B  1 376 ? -42.654 -1.331  -9.448   1.00 37.14  ? 677  CYS   B SG  1 
ATOM   6411  N  N   . PRO   B  1 377 ? -45.244 1.211   -10.198  1.00 30.59  ? 678  PRO   B N   1 
ATOM   6412  C  CA  . PRO   B  1 377 ? -44.935 2.508   -10.811  1.00 29.26  ? 678  PRO   B CA  1 
ATOM   6413  C  C   . PRO   B  1 377 ? -43.436 2.756   -10.845  1.00 35.08  ? 678  PRO   B C   1 
ATOM   6414  O  O   . PRO   B  1 377 ? -42.716 2.507   -9.876   1.00 27.80  ? 678  PRO   B O   1 
ATOM   6415  C  CB  . PRO   B  1 377 ? -45.657 3.509   -9.899   1.00 39.76  ? 678  PRO   B CB  1 
ATOM   6416  C  CG  . PRO   B  1 377 ? -45.630 2.842   -8.530   1.00 32.85  ? 678  PRO   B CG  1 
ATOM   6417  C  CD  . PRO   B  1 377 ? -45.794 1.368   -8.833   1.00 38.56  ? 678  PRO   B CD  1 
ATOM   6418  N  N   . ALA   B  1 378 ? -42.953 3.248   -11.984  1.00 39.86  ? 679  ALA   B N   1 
ATOM   6419  C  CA  . ALA   B  1 378 ? -41.514 3.382   -12.139  1.00 35.01  ? 679  ALA   B CA  1 
ATOM   6420  C  C   . ALA   B  1 378 ? -41.202 4.446   -13.182  1.00 38.19  ? 679  ALA   B C   1 
ATOM   6421  O  O   . ALA   B  1 378 ? -41.809 4.476   -14.260  1.00 35.09  ? 679  ALA   B O   1 
ATOM   6422  C  CB  . ALA   B  1 378 ? -40.879 2.031   -12.510  1.00 26.75  ? 679  ALA   B CB  1 
ATOM   6423  N  N   . ASP   B  1 379 ? -40.227 5.290   -12.850  1.00 35.41  ? 680  ASP   B N   1 
ATOM   6424  C  CA  . ASP   B  1 379 ? -39.870 6.478   -13.620  1.00 37.04  ? 680  ASP   B CA  1 
ATOM   6425  C  C   . ASP   B  1 379 ? -38.581 6.154   -14.377  1.00 38.39  ? 680  ASP   B C   1 
ATOM   6426  O  O   . ASP   B  1 379 ? -37.488 6.167   -13.798  1.00 31.87  ? 680  ASP   B O   1 
ATOM   6427  C  CB  . ASP   B  1 379 ? -39.731 7.675   -12.681  1.00 34.67  ? 680  ASP   B CB  1 
ATOM   6428  C  CG  . ASP   B  1 379 ? -39.434 8.989   -13.405  1.00 45.20  ? 680  ASP   B CG  1 
ATOM   6429  O  OD1 . ASP   B  1 379 ? -38.763 8.990   -14.459  1.00 50.16  ? 680  ASP   B OD1 1 
ATOM   6430  O  OD2 . ASP   B  1 379 ? -39.854 10.047  -12.888  1.00 46.80  ? 680  ASP   B OD2 1 
ATOM   6431  N  N   . TRP   B  1 380 ? -38.719 5.858   -15.683  1.00 36.63  ? 681  TRP   B N   1 
ATOM   6432  C  CA  . TRP   B  1 380 ? -37.572 5.440   -16.495  1.00 33.35  ? 681  TRP   B CA  1 
ATOM   6433  C  C   . TRP   B  1 380 ? -36.419 6.438   -16.408  1.00 31.79  ? 681  TRP   B C   1 
ATOM   6434  O  O   . TRP   B  1 380 ? -35.252 6.046   -16.277  1.00 29.13  ? 681  TRP   B O   1 
ATOM   6435  C  CB  . TRP   B  1 380 ? -38.017 5.257   -17.946  1.00 31.94  ? 681  TRP   B CB  1 
ATOM   6436  C  CG  . TRP   B  1 380 ? -37.063 4.475   -18.828  1.00 38.04  ? 681  TRP   B CG  1 
ATOM   6437  C  CD1 . TRP   B  1 380 ? -37.142 3.148   -19.144  1.00 36.63  ? 681  TRP   B CD1 1 
ATOM   6438  C  CD2 . TRP   B  1 380 ? -35.916 4.985   -19.529  1.00 38.51  ? 681  TRP   B CD2 1 
ATOM   6439  N  NE1 . TRP   B  1 380 ? -36.115 2.802   -19.990  1.00 37.74  ? 681  TRP   B NE1 1 
ATOM   6440  C  CE2 . TRP   B  1 380 ? -35.341 3.906   -20.230  1.00 40.14  ? 681  TRP   B CE2 1 
ATOM   6441  C  CE3 . TRP   B  1 380 ? -35.312 6.244   -19.618  1.00 39.51  ? 681  TRP   B CE3 1 
ATOM   6442  C  CZ2 . TRP   B  1 380 ? -34.197 4.051   -21.020  1.00 45.38  ? 681  TRP   B CZ2 1 
ATOM   6443  C  CZ3 . TRP   B  1 380 ? -34.168 6.384   -20.407  1.00 37.55  ? 681  TRP   B CZ3 1 
ATOM   6444  C  CH2 . TRP   B  1 380 ? -33.624 5.294   -21.091  1.00 38.91  ? 681  TRP   B CH2 1 
ATOM   6445  N  N   . VAL   B  1 381 ? -36.731 7.735   -16.448  1.00 38.43  ? 682  VAL   B N   1 
ATOM   6446  C  CA  . VAL   B  1 381 ? -35.703 8.773   -16.467  1.00 36.45  ? 682  VAL   B CA  1 
ATOM   6447  C  C   . VAL   B  1 381 ? -34.802 8.712   -15.241  1.00 38.93  ? 682  VAL   B C   1 
ATOM   6448  O  O   . VAL   B  1 381 ? -33.610 9.039   -15.326  1.00 37.12  ? 682  VAL   B O   1 
ATOM   6449  C  CB  . VAL   B  1 381 ? -36.366 10.151  -16.595  1.00 29.89  ? 682  VAL   B CB  1 
ATOM   6450  C  CG1 . VAL   B  1 381 ? -35.338 11.229  -16.393  1.00 34.80  ? 682  VAL   B CG1 1 
ATOM   6451  C  CG2 . VAL   B  1 381 ? -37.050 10.280  -17.958  1.00 31.22  ? 682  VAL   B CG2 1 
ATOM   6452  N  N   . TRP   B  1 382 ? -35.345 8.296   -14.091  1.00 37.42  ? 683  TRP   B N   1 
ATOM   6453  C  CA  . TRP   B  1 382 ? -34.606 8.230   -12.833  1.00 37.58  ? 683  TRP   B CA  1 
ATOM   6454  C  C   . TRP   B  1 382 ? -34.075 6.841   -12.521  1.00 39.86  ? 683  TRP   B C   1 
ATOM   6455  O  O   . TRP   B  1 382 ? -33.079 6.721   -11.803  1.00 40.76  ? 683  TRP   B O   1 
ATOM   6456  C  CB  . TRP   B  1 382 ? -35.489 8.699   -11.671  1.00 27.54  ? 683  TRP   B CB  1 
ATOM   6457  C  CG  . TRP   B  1 382 ? -35.565 10.193  -11.524  1.00 40.24  ? 683  TRP   B CG  1 
ATOM   6458  C  CD1 . TRP   B  1 382 ? -36.131 11.078  -12.399  1.00 46.57  ? 683  TRP   B CD1 1 
ATOM   6459  C  CD2 . TRP   B  1 382 ? -35.070 10.978  -10.424  1.00 44.87  ? 683  TRP   B CD2 1 
ATOM   6460  N  NE1 . TRP   B  1 382 ? -35.999 12.366  -11.924  1.00 46.98  ? 683  TRP   B NE1 1 
ATOM   6461  C  CE2 . TRP   B  1 382 ? -35.356 12.330  -10.712  1.00 45.90  ? 683  TRP   B CE2 1 
ATOM   6462  C  CE3 . TRP   B  1 382 ? -34.407 10.668  -9.230   1.00 45.38  ? 683  TRP   B CE3 1 
ATOM   6463  C  CZ2 . TRP   B  1 382 ? -35.002 13.373  -9.847   1.00 49.17  ? 683  TRP   B CZ2 1 
ATOM   6464  C  CZ3 . TRP   B  1 382 ? -34.050 11.712  -8.368   1.00 48.28  ? 683  TRP   B CZ3 1 
ATOM   6465  C  CH2 . TRP   B  1 382 ? -34.353 13.047  -8.684   1.00 44.02  ? 683  TRP   B CH2 1 
ATOM   6466  N  N   . ILE   B  1 383 ? -34.710 5.796   -13.055  1.00 36.21  ? 684  ILE   B N   1 
ATOM   6467  C  CA  . ILE   B  1 383 ? -34.295 4.429   -12.764  1.00 32.50  ? 684  ILE   B CA  1 
ATOM   6468  C  C   . ILE   B  1 383 ? -33.048 4.046   -13.557  1.00 36.75  ? 684  ILE   B C   1 
ATOM   6469  O  O   . ILE   B  1 383 ? -32.166 3.352   -13.035  1.00 39.06  ? 684  ILE   B O   1 
ATOM   6470  C  CB  . ILE   B  1 383 ? -35.455 3.455   -13.034  1.00 29.12  ? 684  ILE   B CB  1 
ATOM   6471  C  CG1 . ILE   B  1 383 ? -36.602 3.666   -12.039  1.00 33.12  ? 684  ILE   B CG1 1 
ATOM   6472  C  CG2 . ILE   B  1 383 ? -34.968 2.018   -13.017  1.00 35.00  ? 684  ILE   B CG2 1 
ATOM   6473  C  CD1 . ILE   B  1 383 ? -36.262 3.318   -10.614  1.00 36.20  ? 684  ILE   B CD1 1 
ATOM   6474  N  N   . VAL   B  1 384 ? -32.953 4.461   -14.825  1.00 41.25  ? 685  VAL   B N   1 
ATOM   6475  C  CA  . VAL   B  1 384 ? -31.776 4.105   -15.638  1.00 30.08  ? 685  VAL   B CA  1 
ATOM   6476  C  C   . VAL   B  1 384 ? -30.552 4.819   -15.082  1.00 32.71  ? 685  VAL   B C   1 
ATOM   6477  O  O   . VAL   B  1 384 ? -30.590 6.051   -14.914  1.00 37.78  ? 685  VAL   B O   1 
ATOM   6478  C  CB  . VAL   B  1 384 ? -31.988 4.483   -17.122  1.00 35.18  ? 685  VAL   B CB  1 
ATOM   6479  C  CG1 . VAL   B  1 384 ? -30.679 4.327   -17.874  1.00 27.86  ? 685  VAL   B CG1 1 
ATOM   6480  C  CG2 . VAL   B  1 384 ? -33.042 3.612   -17.787  1.00 27.46  ? 685  VAL   B CG2 1 
ATOM   6481  N  N   . PRO   B  1 385 ? -29.449 4.121   -14.828  1.00 33.09  ? 686  PRO   B N   1 
ATOM   6482  C  CA  . PRO   B  1 385 ? -28.286 4.764   -14.199  1.00 33.60  ? 686  PRO   B CA  1 
ATOM   6483  C  C   . PRO   B  1 385 ? -27.684 5.813   -15.116  1.00 39.96  ? 686  PRO   B C   1 
ATOM   6484  O  O   . PRO   B  1 385 ? -27.957 5.831   -16.326  1.00 43.84  ? 686  PRO   B O   1 
ATOM   6485  C  CB  . PRO   B  1 385 ? -27.306 3.598   -13.957  1.00 29.29  ? 686  PRO   B CB  1 
ATOM   6486  C  CG  . PRO   B  1 385 ? -28.110 2.369   -14.100  1.00 31.70  ? 686  PRO   B CG  1 
ATOM   6487  C  CD  . PRO   B  1 385 ? -29.225 2.692   -15.062  1.00 29.06  ? 686  PRO   B CD  1 
ATOM   6488  N  N   . PRO   B  1 386 ? -26.882 6.722   -14.566  1.00 41.37  ? 687  PRO   B N   1 
ATOM   6489  C  CA  . PRO   B  1 386 ? -26.304 7.818   -15.356  1.00 39.53  ? 687  PRO   B CA  1 
ATOM   6490  C  C   . PRO   B  1 386 ? -25.003 7.492   -16.074  1.00 41.33  ? 687  PRO   B C   1 
ATOM   6491  O  O   . PRO   B  1 386 ? -24.425 8.395   -16.695  1.00 39.91  ? 687  PRO   B O   1 
ATOM   6492  C  CB  . PRO   B  1 386 ? -26.075 8.889   -14.284  1.00 42.27  ? 687  PRO   B CB  1 
ATOM   6493  C  CG  . PRO   B  1 386 ? -25.740 8.070   -13.062  1.00 36.99  ? 687  PRO   B CG  1 
ATOM   6494  C  CD  . PRO   B  1 386 ? -26.715 6.938   -13.118  1.00 35.20  ? 687  PRO   B CD  1 
ATOM   6495  N  N   . MET   B  1 387 ? -24.503 6.256   -15.994  1.00 43.60  ? 688  MET   B N   1 
ATOM   6496  C  CA  . MET   B  1 387 ? -23.512 5.775   -16.954  1.00 40.00  ? 688  MET   B CA  1 
ATOM   6497  C  C   . MET   B  1 387 ? -23.961 4.419   -17.494  1.00 42.82  ? 688  MET   B C   1 
ATOM   6498  O  O   . MET   B  1 387 ? -24.746 3.695   -16.864  1.00 40.62  ? 688  MET   B O   1 
ATOM   6499  C  CB  . MET   B  1 387 ? -22.087 5.671   -16.359  1.00 36.60  ? 688  MET   B CB  1 
ATOM   6500  C  CG  . MET   B  1 387 ? -21.889 4.604   -15.268  1.00 42.59  ? 688  MET   B CG  1 
ATOM   6501  S  SD  . MET   B  1 387 ? -20.209 4.545   -14.566  1.00 52.53  ? 688  MET   B SD  1 
ATOM   6502  C  CE  . MET   B  1 387 ? -19.277 3.774   -15.896  1.00 59.55  ? 688  MET   B CE  1 
ATOM   6503  N  N   . SER   B  1 388 ? -23.481 4.108   -18.699  1.00 43.35  ? 689  SER   B N   1 
ATOM   6504  C  CA  . SER   B  1 388 ? -23.638 2.785   -19.297  1.00 31.90  ? 689  SER   B CA  1 
ATOM   6505  C  C   . SER   B  1 388 ? -25.102 2.349   -19.358  1.00 34.18  ? 689  SER   B C   1 
ATOM   6506  O  O   . SER   B  1 388 ? -25.430 1.172   -19.199  1.00 42.85  ? 689  SER   B O   1 
ATOM   6507  C  CB  . SER   B  1 388 ? -22.792 1.767   -18.539  1.00 46.88  ? 689  SER   B CB  1 
ATOM   6508  O  OG  . SER   B  1 388 ? -21.479 2.244   -18.381  1.00 48.44  ? 689  SER   B OG  1 
ATOM   6509  N  N   . GLY   B  1 389 ? -25.989 3.304   -19.623  1.00 31.42  ? 690  GLY   B N   1 
ATOM   6510  C  CA  . GLY   B  1 389 ? -27.411 3.031   -19.501  1.00 36.38  ? 690  GLY   B CA  1 
ATOM   6511  C  C   . GLY   B  1 389 ? -27.864 1.799   -20.260  1.00 38.75  ? 690  GLY   B C   1 
ATOM   6512  O  O   . GLY   B  1 389 ? -28.520 0.912   -19.701  1.00 38.08  ? 690  GLY   B O   1 
ATOM   6513  N  N   . SER   B  1 390 ? -27.511 1.715   -21.547  1.00 34.21  ? 691  SER   B N   1 
ATOM   6514  C  CA  . SER   B  1 390 ? -28.096 0.664   -22.358  1.00 31.47  ? 691  SER   B CA  1 
ATOM   6515  C  C   . SER   B  1 390 ? -27.470 -0.706  -22.117  1.00 38.49  ? 691  SER   B C   1 
ATOM   6516  O  O   . SER   B  1 390 ? -28.025 -1.698  -22.585  1.00 39.55  ? 691  SER   B O   1 
ATOM   6517  C  CB  . SER   B  1 390 ? -28.020 1.030   -23.849  1.00 38.30  ? 691  SER   B CB  1 
ATOM   6518  O  OG  . SER   B  1 390 ? -26.742 0.782   -24.360  1.00 37.30  ? 691  SER   B OG  1 
ATOM   6519  N  N   . ILE   B  1 391 ? -26.362 -0.807  -21.387  1.00 43.56  ? 692  ILE   B N   1 
ATOM   6520  C  CA  . ILE   B  1 391 ? -25.886 -2.138  -21.023  1.00 51.00  ? 692  ILE   B CA  1 
ATOM   6521  C  C   . ILE   B  1 391 ? -26.453 -2.558  -19.667  1.00 51.09  ? 692  ILE   B C   1 
ATOM   6522  O  O   . ILE   B  1 391 ? -26.025 -3.567  -19.100  1.00 49.55  ? 692  ILE   B O   1 
ATOM   6523  C  CB  . ILE   B  1 391 ? -24.349 -2.249  -21.021  1.00 55.05  ? 692  ILE   B CB  1 
ATOM   6524  C  CG1 . ILE   B  1 391 ? -23.733 -1.293  -20.020  1.00 52.69  ? 692  ILE   B CG1 1 
ATOM   6525  C  CG2 . ILE   B  1 391 ? -23.769 -2.045  -22.433  1.00 52.56  ? 692  ILE   B CG2 1 
ATOM   6526  C  CD1 . ILE   B  1 391 ? -22.313 -1.622  -19.683  1.00 52.32  ? 692  ILE   B CD1 1 
ATOM   6527  N  N   . THR   B  1 392 ? -27.430 -1.799  -19.130  1.00 51.73  ? 693  THR   B N   1 
ATOM   6528  C  CA  . THR   B  1 392 ? -28.150 -2.325  -17.972  1.00 47.14  ? 693  THR   B CA  1 
ATOM   6529  C  C   . THR   B  1 392 ? -29.548 -2.760  -18.407  1.00 43.00  ? 693  THR   B C   1 
ATOM   6530  O  O   . THR   B  1 392 ? -30.077 -2.243  -19.387  1.00 40.45  ? 693  THR   B O   1 
ATOM   6531  C  CB  . THR   B  1 392 ? -28.270 -1.318  -16.812  1.00 48.27  ? 693  THR   B CB  1 
ATOM   6532  O  OG1 . THR   B  1 392 ? -29.071 -0.193  -17.202  1.00 50.78  ? 693  THR   B OG1 1 
ATOM   6533  C  CG2 . THR   B  1 392 ? -26.887 -0.828  -16.338  1.00 38.06  ? 693  THR   B CG2 1 
ATOM   6534  N  N   . PRO   B  1 393 ? -30.172 -3.723  -17.722  1.00 44.48  ? 694  PRO   B N   1 
ATOM   6535  C  CA  . PRO   B  1 393 ? -31.459 -4.239  -18.216  1.00 41.20  ? 694  PRO   B CA  1 
ATOM   6536  C  C   . PRO   B  1 393 ? -32.605 -3.248  -18.133  1.00 46.10  ? 694  PRO   B C   1 
ATOM   6537  O  O   . PRO   B  1 393 ? -33.590 -3.427  -18.859  1.00 49.29  ? 694  PRO   B O   1 
ATOM   6538  C  CB  . PRO   B  1 393 ? -31.725 -5.458  -17.321  1.00 42.12  ? 694  PRO   B CB  1 
ATOM   6539  C  CG  . PRO   B  1 393 ? -30.897 -5.212  -16.091  1.00 41.70  ? 694  PRO   B CG  1 
ATOM   6540  C  CD  . PRO   B  1 393 ? -29.654 -4.532  -16.608  1.00 39.36  ? 694  PRO   B CD  1 
ATOM   6541  N  N   . VAL   B  1 394 ? -32.531 -2.223  -17.281  1.00 48.72  ? 695  VAL   B N   1 
ATOM   6542  C  CA  . VAL   B  1 394 ? -33.683 -1.334  -17.160  1.00 43.40  ? 695  VAL   B CA  1 
ATOM   6543  C  C   . VAL   B  1 394 ? -33.792 -0.416  -18.362  1.00 32.67  ? 695  VAL   B C   1 
ATOM   6544  O  O   . VAL   B  1 394 ? -34.888 0.069   -18.675  1.00 32.33  ? 695  VAL   B O   1 
ATOM   6545  C  CB  . VAL   B  1 394 ? -33.642 -0.506  -15.856  1.00 39.44  ? 695  VAL   B CB  1 
ATOM   6546  C  CG1 . VAL   B  1 394 ? -33.848 -1.387  -14.660  1.00 39.13  ? 695  VAL   B CG1 1 
ATOM   6547  C  CG2 . VAL   B  1 394 ? -32.354 0.275   -15.750  1.00 33.72  ? 695  VAL   B CG2 1 
ATOM   6548  N  N   . PHE   B  1 395 ? -32.672 -0.117  -19.024  1.00 30.71  ? 696  PHE   B N   1 
ATOM   6549  C  CA  . PHE   B  1 395 ? -32.739 0.677   -20.260  1.00 38.57  ? 696  PHE   B CA  1 
ATOM   6550  C  C   . PHE   B  1 395 ? -33.755 0.110   -21.250  1.00 32.35  ? 696  PHE   B C   1 
ATOM   6551  O  O   . PHE   B  1 395 ? -34.537 0.858   -21.853  1.00 29.71  ? 696  PHE   B O   1 
ATOM   6552  C  CB  . PHE   B  1 395 ? -31.364 0.752   -20.920  1.00 36.24  ? 696  PHE   B CB  1 
ATOM   6553  C  CG  . PHE   B  1 395 ? -31.344 1.547   -22.206  1.00 35.42  ? 696  PHE   B CG  1 
ATOM   6554  C  CD1 . PHE   B  1 395 ? -31.664 0.950   -23.407  1.00 34.62  ? 696  PHE   B CD1 1 
ATOM   6555  C  CD2 . PHE   B  1 395 ? -30.972 2.882   -22.201  1.00 32.62  ? 696  PHE   B CD2 1 
ATOM   6556  C  CE1 . PHE   B  1 395 ? -31.640 1.679   -24.605  1.00 42.01  ? 696  PHE   B CE1 1 
ATOM   6557  C  CE2 . PHE   B  1 395 ? -30.941 3.617   -23.366  1.00 41.53  ? 696  PHE   B CE2 1 
ATOM   6558  C  CZ  . PHE   B  1 395 ? -31.275 3.009   -24.588  1.00 41.25  ? 696  PHE   B CZ  1 
ATOM   6559  N  N   . HIS   B  1 396 ? -33.771 -1.210  -21.405  1.00 32.53  ? 697  HIS   B N   1 
ATOM   6560  C  CA  . HIS   B  1 396 ? -34.604 -1.903  -22.375  1.00 36.26  ? 697  HIS   B CA  1 
ATOM   6561  C  C   . HIS   B  1 396 ? -35.979 -2.279  -21.833  1.00 36.78  ? 697  HIS   B C   1 
ATOM   6562  O  O   . HIS   B  1 396 ? -36.695 -3.042  -22.489  1.00 41.83  ? 697  HIS   B O   1 
ATOM   6563  C  CB  . HIS   B  1 396 ? -33.860 -3.145  -22.861  1.00 34.68  ? 697  HIS   B CB  1 
ATOM   6564  C  CG  . HIS   B  1 396 ? -32.459 -2.851  -23.298  1.00 41.93  ? 697  HIS   B CG  1 
ATOM   6565  N  ND1 . HIS   B  1 396 ? -32.152 -2.416  -24.569  1.00 46.15  ? 697  HIS   B ND1 1 
ATOM   6566  C  CD2 . HIS   B  1 396 ? -31.288 -2.885  -22.618  1.00 44.03  ? 697  HIS   B CD2 1 
ATOM   6567  C  CE1 . HIS   B  1 396 ? -30.849 -2.213  -24.658  1.00 47.64  ? 697  HIS   B CE1 1 
ATOM   6568  N  NE2 . HIS   B  1 396 ? -30.303 -2.487  -23.485  1.00 45.82  ? 697  HIS   B NE2 1 
ATOM   6569  N  N   . GLN   B  1 397 ? -36.380 -1.731  -20.686  1.00 39.08  ? 698  GLN   B N   1 
ATOM   6570  C  CA  . GLN   B  1 397 ? -37.637 -2.071  -20.018  1.00 37.52  ? 698  GLN   B CA  1 
ATOM   6571  C  C   . GLN   B  1 397 ? -38.614 -0.897  -20.066  1.00 36.09  ? 698  GLN   B C   1 
ATOM   6572  O  O   . GLN   B  1 397 ? -38.375 0.135   -19.431  1.00 42.05  ? 698  GLN   B O   1 
ATOM   6573  C  CB  . GLN   B  1 397 ? -37.365 -2.468  -18.569  1.00 41.67  ? 698  GLN   B CB  1 
ATOM   6574  C  CG  . GLN   B  1 397 ? -38.614 -2.735  -17.755  1.00 40.39  ? 698  GLN   B CG  1 
ATOM   6575  C  CD  . GLN   B  1 397 ? -39.220 -4.054  -18.112  1.00 33.33  ? 698  GLN   B CD  1 
ATOM   6576  O  OE1 . GLN   B  1 397 ? -38.553 -5.095  -18.016  1.00 31.60  ? 698  GLN   B OE1 1 
ATOM   6577  N  NE2 . GLN   B  1 397 ? -40.477 -4.030  -18.572  1.00 32.20  ? 698  GLN   B NE2 1 
ATOM   6578  N  N   . GLU   B  1 398 ? -39.728 -1.068  -20.788  1.00 30.49  ? 699  GLU   B N   1 
ATOM   6579  C  CA  . GLU   B  1 398 ? -40.811 -0.095  -20.729  1.00 30.29  ? 699  GLU   B CA  1 
ATOM   6580  C  C   . GLU   B  1 398 ? -41.348 0.016   -19.296  1.00 46.34  ? 699  GLU   B C   1 
ATOM   6581  O  O   . GLU   B  1 398 ? -41.450 -0.983  -18.577  1.00 30.01  ? 699  GLU   B O   1 
ATOM   6582  C  CB  . GLU   B  1 398 ? -41.923 -0.503  -21.685  1.00 35.82  ? 699  GLU   B CB  1 
ATOM   6583  C  CG  . GLU   B  1 398 ? -41.516 -0.376  -23.174  1.00 39.08  ? 699  GLU   B CG  1 
ATOM   6584  C  CD  . GLU   B  1 398 ? -42.650 -0.683  -24.131  1.00 48.08  ? 699  GLU   B CD  1 
ATOM   6585  O  OE1 . GLU   B  1 398 ? -42.507 -0.377  -25.350  1.00 40.07  ? 699  GLU   B OE1 1 
ATOM   6586  O  OE2 . GLU   B  1 398 ? -43.684 -1.227  -23.665  1.00 49.65  ? 699  GLU   B OE2 1 
ATOM   6587  N  N   . MET   B  1 399 ? -41.696 1.236   -18.878  1.00 37.56  ? 700  MET   B N   1 
ATOM   6588  C  CA  . MET   B  1 399 ? -42.215 1.462   -17.534  1.00 38.17  ? 700  MET   B CA  1 
ATOM   6589  C  C   . MET   B  1 399 ? -43.415 2.402   -17.567  1.00 44.10  ? 700  MET   B C   1 
ATOM   6590  O  O   . MET   B  1 399 ? -43.461 3.339   -18.367  1.00 57.32  ? 700  MET   B O   1 
ATOM   6591  C  CB  . MET   B  1 399 ? -41.133 2.040   -16.620  1.00 34.63  ? 700  MET   B CB  1 
ATOM   6592  C  CG  . MET   B  1 399 ? -40.042 1.056   -16.228  1.00 34.56  ? 700  MET   B CG  1 
ATOM   6593  S  SD  . MET   B  1 399 ? -38.544 1.909   -15.675  1.00 33.56  ? 700  MET   B SD  1 
ATOM   6594  C  CE  . MET   B  1 399 ? -37.322 0.663   -16.076  1.00 27.59  ? 700  MET   B CE  1 
ATOM   6595  N  N   . LEU   B  1 400 ? -44.396 2.133   -16.709  1.00 34.15  ? 701  LEU   B N   1 
ATOM   6596  C  CA  . LEU   B  1 400 ? -45.543 3.012   -16.511  1.00 35.35  ? 701  LEU   B CA  1 
ATOM   6597  C  C   . LEU   B  1 400 ? -45.357 3.800   -15.226  1.00 41.05  ? 701  LEU   B C   1 
ATOM   6598  O  O   . LEU   B  1 400 ? -45.065 3.218   -14.179  1.00 38.16  ? 701  LEU   B O   1 
ATOM   6599  C  CB  . LEU   B  1 400 ? -46.845 2.218   -16.428  1.00 33.80  ? 701  LEU   B CB  1 
ATOM   6600  C  CG  . LEU   B  1 400 ? -47.343 1.537   -17.689  1.00 41.48  ? 701  LEU   B CG  1 
ATOM   6601  C  CD1 . LEU   B  1 400 ? -48.650 0.806   -17.420  1.00 45.45  ? 701  LEU   B CD1 1 
ATOM   6602  C  CD2 . LEU   B  1 400 ? -47.497 2.567   -18.791  1.00 39.57  ? 701  LEU   B CD2 1 
ATOM   6603  N  N   . ASN   B  1 401 ? -45.517 5.113   -15.300  1.00 44.62  ? 702  ASN   B N   1 
ATOM   6604  C  CA  . ASN   B  1 401 ? -45.373 5.967   -14.132  1.00 40.67  ? 702  ASN   B CA  1 
ATOM   6605  C  C   . ASN   B  1 401 ? -46.734 6.491   -13.701  1.00 44.08  ? 702  ASN   B C   1 
ATOM   6606  O  O   . ASN   B  1 401 ? -47.507 6.970   -14.538  1.00 35.90  ? 702  ASN   B O   1 
ATOM   6607  C  CB  . ASN   B  1 401 ? -44.420 7.135   -14.391  1.00 41.93  ? 702  ASN   B CB  1 
ATOM   6608  C  CG  . ASN   B  1 401 ? -43.844 7.674   -13.105  1.00 40.48  ? 702  ASN   B CG  1 
ATOM   6609  O  OD1 . ASN   B  1 401 ? -43.964 7.030   -12.090  1.00 40.62  ? 702  ASN   B OD1 1 
ATOM   6610  N  ND2 . ASN   B  1 401 ? -43.237 8.846   -13.138  1.00 37.28  ? 702  ASN   B ND2 1 
ATOM   6611  N  N   . TYR   B  1 402 ? -47.019 6.397   -12.395  1.00 44.97  ? 703  TYR   B N   1 
ATOM   6612  C  CA  . TYR   B  1 402 ? -48.257 6.913   -11.819  1.00 29.13  ? 703  TYR   B CA  1 
ATOM   6613  C  C   . TYR   B  1 402 ? -48.062 7.057   -10.312  1.00 35.28  ? 703  TYR   B C   1 
ATOM   6614  O  O   . TYR   B  1 402 ? -47.165 6.453   -9.724   1.00 32.31  ? 703  TYR   B O   1 
ATOM   6615  C  CB  . TYR   B  1 402 ? -49.462 6.016   -12.146  1.00 30.09  ? 703  TYR   B CB  1 
ATOM   6616  C  CG  . TYR   B  1 402 ? -49.230 4.514   -11.992  1.00 45.61  ? 703  TYR   B CG  1 
ATOM   6617  C  CD1 . TYR   B  1 402 ? -48.787 3.739   -13.067  1.00 39.85  ? 703  TYR   B CD1 1 
ATOM   6618  C  CD2 . TYR   B  1 402 ? -49.486 3.864   -10.777  1.00 35.99  ? 703  TYR   B CD2 1 
ATOM   6619  C  CE1 . TYR   B  1 402 ? -48.586 2.368   -12.931  1.00 37.41  ? 703  TYR   B CE1 1 
ATOM   6620  C  CE2 . TYR   B  1 402 ? -49.284 2.502   -10.632  1.00 33.70  ? 703  TYR   B CE2 1 
ATOM   6621  C  CZ  . TYR   B  1 402 ? -48.844 1.750   -11.715  1.00 41.25  ? 703  TYR   B CZ  1 
ATOM   6622  O  OH  . TYR   B  1 402 ? -48.645 0.385   -11.581  1.00 41.24  ? 703  TYR   B OH  1 
ATOM   6623  N  N   . ARG   B  1 403 ? -48.909 7.878   -9.703   1.00 38.51  ? 704  ARG   B N   1 
ATOM   6624  C  CA  . ARG   B  1 403 ? -48.690 8.378   -8.348   1.00 44.00  ? 704  ARG   B CA  1 
ATOM   6625  C  C   . ARG   B  1 403 ? -49.655 7.689   -7.387   1.00 46.54  ? 704  ARG   B C   1 
ATOM   6626  O  O   . ARG   B  1 403 ? -50.860 7.972   -7.389   1.00 47.05  ? 704  ARG   B O   1 
ATOM   6627  C  CB  . ARG   B  1 403 ? -48.848 9.894   -8.311   1.00 46.02  ? 704  ARG   B CB  1 
ATOM   6628  C  CG  . ARG   B  1 403 ? -47.941 10.609  -9.303   1.00 45.02  ? 704  ARG   B CG  1 
ATOM   6629  C  CD  . ARG   B  1 403 ? -47.154 11.674  -8.609   1.00 54.02  ? 704  ARG   B CD  1 
ATOM   6630  N  NE  . ARG   B  1 403 ? -47.892 12.929  -8.556   1.00 58.48  ? 704  ARG   B NE  1 
ATOM   6631  C  CZ  . ARG   B  1 403 ? -47.933 13.721  -7.494   1.00 55.83  ? 704  ARG   B CZ  1 
ATOM   6632  N  NH1 . ARG   B  1 403 ? -47.303 13.362  -6.384   1.00 50.98  ? 704  ARG   B NH1 1 
ATOM   6633  N  NH2 . ARG   B  1 403 ? -48.617 14.858  -7.542   1.00 62.70  ? 704  ARG   B NH2 1 
ATOM   6634  N  N   . LEU   B  1 404 ? -49.115 6.777   -6.583   1.00 43.93  ? 705  LEU   B N   1 
ATOM   6635  C  CA  . LEU   B  1 404 ? -49.863 6.058   -5.560   1.00 41.19  ? 705  LEU   B CA  1 
ATOM   6636  C  C   . LEU   B  1 404 ? -49.617 6.676   -4.192   1.00 44.32  ? 705  LEU   B C   1 
ATOM   6637  O  O   . LEU   B  1 404 ? -48.579 7.290   -3.945   1.00 49.53  ? 705  LEU   B O   1 
ATOM   6638  C  CB  . LEU   B  1 404 ? -49.470 4.581   -5.528   1.00 29.55  ? 705  LEU   B CB  1 
ATOM   6639  C  CG  . LEU   B  1 404 ? -49.781 3.745   -6.776   1.00 38.43  ? 705  LEU   B CG  1 
ATOM   6640  C  CD1 . LEU   B  1 404 ? -49.312 2.301   -6.549   1.00 34.23  ? 705  LEU   B CD1 1 
ATOM   6641  C  CD2 . LEU   B  1 404 ? -51.270 3.795   -7.154   1.00 31.81  ? 705  LEU   B CD2 1 
ATOM   6642  N  N   . THR   B  1 405 ? -50.580 6.484   -3.295   1.00 49.26  ? 706  THR   B N   1 
ATOM   6643  C  CA  . THR   B  1 405 ? -50.499 6.987   -1.941   1.00 39.58  ? 706  THR   B CA  1 
ATOM   6644  C  C   . THR   B  1 405 ? -50.592 5.822   -0.958   1.00 46.04  ? 706  THR   B C   1 
ATOM   6645  O  O   . THR   B  1 405 ? -51.300 4.837   -1.227   1.00 43.93  ? 706  THR   B O   1 
ATOM   6646  C  CB  . THR   B  1 405 ? -51.617 8.010   -1.677   1.00 45.79  ? 706  THR   B CB  1 
ATOM   6647  O  OG1 . THR   B  1 405 ? -51.232 8.898   -0.621   1.00 51.39  ? 706  THR   B OG1 1 
ATOM   6648  C  CG2 . THR   B  1 405 ? -52.909 7.318   -1.288   1.00 43.99  ? 706  THR   B CG2 1 
ATOM   6649  N  N   . PRO   B  1 406 ? -49.855 5.871   0.180    1.00 42.23  ? 707  PRO   B N   1 
ATOM   6650  C  CA  . PRO   B  1 406 ? -48.932 6.897   0.701    1.00 41.11  ? 707  PRO   B CA  1 
ATOM   6651  C  C   . PRO   B  1 406 ? -47.703 7.172   -0.163   1.00 38.63  ? 707  PRO   B C   1 
ATOM   6652  O  O   . PRO   B  1 406 ? -47.307 6.314   -0.947   1.00 48.78  ? 707  PRO   B O   1 
ATOM   6653  C  CB  . PRO   B  1 406 ? -48.484 6.314   2.056    1.00 41.50  ? 707  PRO   B CB  1 
ATOM   6654  C  CG  . PRO   B  1 406 ? -49.527 5.324   2.401    1.00 43.26  ? 707  PRO   B CG  1 
ATOM   6655  C  CD  . PRO   B  1 406 ? -50.004 4.750   1.122    1.00 39.08  ? 707  PRO   B CD  1 
ATOM   6656  N  N   . SER   B  1 407 ? -47.086 8.342   -0.004   1.00 31.77  ? 708  SER   B N   1 
ATOM   6657  C  CA  . SER   B  1 407 ? -45.947 8.686   -0.844   1.00 38.95  ? 708  SER   B CA  1 
ATOM   6658  C  C   . SER   B  1 407 ? -44.973 9.582   -0.096   1.00 40.05  ? 708  SER   B C   1 
ATOM   6659  O  O   . SER   B  1 407 ? -45.313 10.220  0.903    1.00 42.01  ? 708  SER   B O   1 
ATOM   6660  C  CB  . SER   B  1 407 ? -46.388 9.400   -2.132   1.00 46.78  ? 708  SER   B CB  1 
ATOM   6661  O  OG  . SER   B  1 407 ? -46.989 10.646  -1.822   1.00 55.50  ? 708  SER   B OG  1 
ATOM   6662  N  N   . PHE   B  1 408 ? -43.749 9.623   -0.613   1.00 47.10  ? 709  PHE   B N   1 
ATOM   6663  C  CA  . PHE   B  1 408 ? -42.815 10.694  -0.319   1.00 38.81  ? 709  PHE   B CA  1 
ATOM   6664  C  C   . PHE   B  1 408 ? -42.979 11.784  -1.374   1.00 41.35  ? 709  PHE   B C   1 
ATOM   6665  O  O   . PHE   B  1 408 ? -43.144 11.489  -2.562   1.00 41.58  ? 709  PHE   B O   1 
ATOM   6666  C  CB  . PHE   B  1 408 ? -41.380 10.167  -0.296   1.00 33.15  ? 709  PHE   B CB  1 
ATOM   6667  C  CG  . PHE   B  1 408 ? -41.109 9.183   0.822    1.00 38.28  ? 709  PHE   B CG  1 
ATOM   6668  C  CD1 . PHE   B  1 408 ? -40.892 9.629   2.128    1.00 32.63  ? 709  PHE   B CD1 1 
ATOM   6669  C  CD2 . PHE   B  1 408 ? -41.059 7.816   0.566    1.00 35.04  ? 709  PHE   B CD2 1 
ATOM   6670  C  CE1 . PHE   B  1 408 ? -40.634 8.717   3.153    1.00 35.58  ? 709  PHE   B CE1 1 
ATOM   6671  C  CE2 . PHE   B  1 408 ? -40.802 6.898   1.587    1.00 32.86  ? 709  PHE   B CE2 1 
ATOM   6672  C  CZ  . PHE   B  1 408 ? -40.592 7.354   2.891    1.00 33.13  ? 709  PHE   B CZ  1 
ATOM   6673  N  N   . GLU   B  1 409 ? -42.957 13.042  -0.924   1.00 35.39  ? 710  GLU   B N   1 
ATOM   6674  C  CA  . GLU   B  1 409 ? -43.156 14.218  -1.754   1.00 32.66  ? 710  GLU   B CA  1 
ATOM   6675  C  C   . GLU   B  1 409 ? -42.018 15.201  -1.537   1.00 37.35  ? 710  GLU   B C   1 
ATOM   6676  O  O   . GLU   B  1 409 ? -41.364 15.204  -0.498   1.00 47.73  ? 710  GLU   B O   1 
ATOM   6677  C  CB  . GLU   B  1 409 ? -44.484 14.934  -1.438   1.00 32.82  ? 710  GLU   B CB  1 
ATOM   6678  C  CG  . GLU   B  1 409 ? -45.744 14.096  -1.636   1.00 40.89  ? 710  GLU   B CG  1 
ATOM   6679  C  CD  . GLU   B  1 409 ? -45.983 13.654  -3.101   1.00 53.02  ? 710  GLU   B CD  1 
ATOM   6680  O  OE1 . GLU   B  1 409 ? -45.440 14.281  -4.054   1.00 50.84  ? 710  GLU   B OE1 1 
ATOM   6681  O  OE2 . GLU   B  1 409 ? -46.729 12.666  -3.287   1.00 49.05  ? 710  GLU   B OE2 1 
ATOM   6682  N  N   . TYR   B  1 410 ? -41.805 16.062  -2.517   1.00 35.09  ? 711  TYR   B N   1 
ATOM   6683  C  CA  . TYR   B  1 410 ? -40.921 17.191  -2.309   1.00 35.74  ? 711  TYR   B CA  1 
ATOM   6684  C  C   . TYR   B  1 410 ? -41.651 18.280  -1.536   1.00 37.97  ? 711  TYR   B C   1 
ATOM   6685  O  O   . TYR   B  1 410 ? -42.883 18.310  -1.466   1.00 44.80  ? 711  TYR   B O   1 
ATOM   6686  C  CB  . TYR   B  1 410 ? -40.425 17.772  -3.640   1.00 43.35  ? 711  TYR   B CB  1 
ATOM   6687  C  CG  . TYR   B  1 410 ? -39.768 16.769  -4.542   1.00 53.19  ? 711  TYR   B CG  1 
ATOM   6688  C  CD1 . TYR   B  1 410 ? -38.483 16.321  -4.290   1.00 61.19  ? 711  TYR   B CD1 1 
ATOM   6689  C  CD2 . TYR   B  1 410 ? -40.437 16.261  -5.650   1.00 66.47  ? 711  TYR   B CD2 1 
ATOM   6690  C  CE1 . TYR   B  1 410 ? -37.881 15.392  -5.117   1.00 70.58  ? 711  TYR   B CE1 1 
ATOM   6691  C  CE2 . TYR   B  1 410 ? -39.846 15.338  -6.481   1.00 72.22  ? 711  TYR   B CE2 1 
ATOM   6692  C  CZ  . TYR   B  1 410 ? -38.564 14.904  -6.213   1.00 75.98  ? 711  TYR   B CZ  1 
ATOM   6693  O  OH  . TYR   B  1 410 ? -37.963 13.979  -7.041   1.00 77.03  ? 711  TYR   B OH  1 
ATOM   6694  N  N   . GLN   B  1 411 ? -40.869 19.186  -0.959   1.00 35.04  ? 712  GLN   B N   1 
ATOM   6695  C  CA  . GLN   B  1 411 ? -41.394 20.323  -0.218   1.00 32.95  ? 712  GLN   B CA  1 
ATOM   6696  C  C   . GLN   B  1 411 ? -40.402 21.464  -0.359   1.00 35.57  ? 712  GLN   B C   1 
ATOM   6697  O  O   . GLN   B  1 411 ? -39.225 21.234  -0.658   1.00 34.92  ? 712  GLN   B O   1 
ATOM   6698  C  CB  . GLN   B  1 411 ? -41.639 19.974  1.261    1.00 34.62  ? 712  GLN   B CB  1 
ATOM   6699  C  CG  . GLN   B  1 411 ? -40.402 19.569  2.043    1.00 32.65  ? 712  GLN   B CG  1 
ATOM   6700  C  CD  . GLN   B  1 411 ? -40.713 19.073  3.473    1.00 37.83  ? 712  GLN   B CD  1 
ATOM   6701  O  OE1 . GLN   B  1 411 ? -41.729 19.431  4.082    1.00 46.04  ? 712  GLN   B OE1 1 
ATOM   6702  N  NE2 . GLN   B  1 411 ? -39.827 18.247  4.001    1.00 34.79  ? 712  GLN   B NE2 1 
ATOM   6703  N  N   . PRO   B  1 412 ? -40.848 22.703  -0.193   1.00 46.73  ? 713  PRO   B N   1 
ATOM   6704  C  CA  . PRO   B  1 412 ? -39.923 23.829  -0.325   1.00 54.10  ? 713  PRO   B CA  1 
ATOM   6705  C  C   . PRO   B  1 412 ? -38.872 23.797  0.771    1.00 49.41  ? 713  PRO   B C   1 
ATOM   6706  O  O   . PRO   B  1 412 ? -39.130 23.355  1.892    1.00 48.43  ? 713  PRO   B O   1 
ATOM   6707  C  CB  . PRO   B  1 412 ? -40.831 25.058  -0.183   1.00 59.48  ? 713  PRO   B CB  1 
ATOM   6708  C  CG  . PRO   B  1 412 ? -42.247 24.543  -0.298   1.00 50.37  ? 713  PRO   B CG  1 
ATOM   6709  C  CD  . PRO   B  1 412 ? -42.211 23.138  0.164    1.00 47.12  ? 713  PRO   B CD  1 
ATOM   6710  N  N   . ASP   B  1 413 ? -37.671 24.253  0.424    1.00 50.33  ? 714  ASP   B N   1 
ATOM   6711  C  CA  . ASP   B  1 413 ? -36.636 24.471  1.422    1.00 56.71  ? 714  ASP   B CA  1 
ATOM   6712  C  C   . ASP   B  1 413 ? -37.174 25.373  2.531    1.00 59.32  ? 714  ASP   B C   1 
ATOM   6713  O  O   . ASP   B  1 413 ? -37.764 26.423  2.237    1.00 56.78  ? 714  ASP   B O   1 
ATOM   6714  C  CB  . ASP   B  1 413 ? -35.400 25.117  0.795    1.00 61.62  ? 714  ASP   B CB  1 
ATOM   6715  C  CG  . ASP   B  1 413 ? -34.681 24.198  -0.169   1.00 64.78  ? 714  ASP   B CG  1 
ATOM   6716  O  OD1 . ASP   B  1 413 ? -34.648 22.972  0.077    1.00 63.00  ? 714  ASP   B OD1 1 
ATOM   6717  O  OD2 . ASP   B  1 413 ? -34.142 24.708  -1.175   1.00 69.75  ? 714  ASP   B OD2 1 
ATOM   6718  N  N   . PRO   B  1 414 ? -36.981 25.016  3.804    1.00 61.04  ? 715  PRO   B N   1 
ATOM   6719  C  CA  . PRO   B  1 414 ? -37.621 25.792  4.877    1.00 53.63  ? 715  PRO   B CA  1 
ATOM   6720  C  C   . PRO   B  1 414 ? -37.157 27.238  4.941    1.00 58.16  ? 715  PRO   B C   1 
ATOM   6721  O  O   . PRO   B  1 414 ? -37.896 28.078  5.461    1.00 69.17  ? 715  PRO   B O   1 
ATOM   6722  C  CB  . PRO   B  1 414 ? -37.252 25.015  6.150    1.00 52.81  ? 715  PRO   B CB  1 
ATOM   6723  C  CG  . PRO   B  1 414 ? -36.026 24.272  5.815    1.00 56.87  ? 715  PRO   B CG  1 
ATOM   6724  C  CD  . PRO   B  1 414 ? -36.092 23.967  4.325    1.00 58.84  ? 715  PRO   B CD  1 
ATOM   6725  N  N   . TRP   B  1 415 ? -35.987 27.575  4.403    1.00 53.88  ? 716  TRP   B N   1 
ATOM   6726  C  CA  . TRP   B  1 415 ? -35.534 28.955  4.525    1.00 61.69  ? 716  TRP   B CA  1 
ATOM   6727  C  C   . TRP   B  1 415 ? -36.162 29.892  3.505    1.00 65.47  ? 716  TRP   B C   1 
ATOM   6728  O  O   . TRP   B  1 415 ? -35.943 31.104  3.598    1.00 62.76  ? 716  TRP   B O   1 
ATOM   6729  C  CB  . TRP   B  1 415 ? -34.016 29.044  4.413    1.00 62.67  ? 716  TRP   B CB  1 
ATOM   6730  C  CG  . TRP   B  1 415 ? -33.477 28.466  3.171    1.00 62.04  ? 716  TRP   B CG  1 
ATOM   6731  C  CD1 . TRP   B  1 415 ? -33.360 29.084  1.962    1.00 62.45  ? 716  TRP   B CD1 1 
ATOM   6732  C  CD2 . TRP   B  1 415 ? -32.963 27.144  3.002    1.00 59.51  ? 716  TRP   B CD2 1 
ATOM   6733  N  NE1 . TRP   B  1 415 ? -32.802 28.228  1.047    1.00 59.83  ? 716  TRP   B NE1 1 
ATOM   6734  C  CE2 . TRP   B  1 415 ? -32.549 27.028  1.659    1.00 58.09  ? 716  TRP   B CE2 1 
ATOM   6735  C  CE3 . TRP   B  1 415 ? -32.813 26.045  3.856    1.00 48.69  ? 716  TRP   B CE3 1 
ATOM   6736  C  CZ2 . TRP   B  1 415 ? -31.992 25.860  1.148    1.00 53.77  ? 716  TRP   B CZ2 1 
ATOM   6737  C  CZ3 . TRP   B  1 415 ? -32.266 24.886  3.349    1.00 51.14  ? 716  TRP   B CZ3 1 
ATOM   6738  C  CH2 . TRP   B  1 415 ? -31.859 24.803  2.004    1.00 51.75  ? 716  TRP   B CH2 1 
ATOM   6739  N  N   . ASN   B  1 416 ? -36.917 29.375  2.533    1.00 69.11  ? 717  ASN   B N   1 
ATOM   6740  C  CA  . ASN   B  1 416 ? -37.748 30.243  1.707    1.00 69.96  ? 717  ASN   B CA  1 
ATOM   6741  C  C   . ASN   B  1 416 ? -39.041 30.611  2.411    1.00 73.71  ? 717  ASN   B C   1 
ATOM   6742  O  O   . ASN   B  1 416 ? -39.698 31.583  2.019    1.00 72.43  ? 717  ASN   B O   1 
ATOM   6743  C  CB  . ASN   B  1 416 ? -38.076 29.572  0.371    1.00 60.56  ? 717  ASN   B CB  1 
ATOM   6744  C  CG  . ASN   B  1 416 ? -36.839 29.164  -0.392   1.00 58.46  ? 717  ASN   B CG  1 
ATOM   6745  O  OD1 . ASN   B  1 416 ? -35.810 29.843  -0.339   1.00 62.77  ? 717  ASN   B OD1 1 
ATOM   6746  N  ND2 . ASN   B  1 416 ? -36.930 28.048  -1.113   1.00 51.56  ? 717  ASN   B ND2 1 
ATOM   6747  N  N   . THR   B  1 417 ? -39.392 29.869  3.463    1.00 74.19  ? 718  THR   B N   1 
ATOM   6748  C  CA  . THR   B  1 417 ? -40.698 29.951  4.090    1.00 78.84  ? 718  THR   B CA  1 
ATOM   6749  C  C   . THR   B  1 417 ? -40.670 30.400  5.548    1.00 79.50  ? 718  THR   B C   1 
ATOM   6750  O  O   . THR   B  1 417 ? -41.679 30.931  6.025    1.00 81.41  ? 718  THR   B O   1 
ATOM   6751  C  CB  . THR   B  1 417 ? -41.397 28.582  3.999    1.00 81.31  ? 718  THR   B CB  1 
ATOM   6752  O  OG1 . THR   B  1 417 ? -40.589 27.684  3.224    1.00 76.73  ? 718  THR   B OG1 1 
ATOM   6753  C  CG2 . THR   B  1 417 ? -42.755 28.716  3.332    1.00 83.03  ? 718  THR   B CG2 1 
ATOM   6754  N  N   . HIS   B  1 418 ? -39.551 30.242  6.255    1.00 81.83  ? 719  HIS   B N   1 
ATOM   6755  C  CA  . HIS   B  1 418 ? -39.551 30.359  7.710    1.00 86.03  ? 719  HIS   B CA  1 
ATOM   6756  C  C   . HIS   B  1 418 ? -39.462 31.814  8.157    1.00 92.31  ? 719  HIS   B C   1 
ATOM   6757  O  O   . HIS   B  1 418 ? -38.592 32.563  7.701    1.00 94.18  ? 719  HIS   B O   1 
ATOM   6758  C  CB  . HIS   B  1 418 ? -38.395 29.557  8.313    1.00 83.06  ? 719  HIS   B CB  1 
ATOM   6759  C  CG  . HIS   B  1 418 ? -38.296 29.674  9.802    1.00 78.05  ? 719  HIS   B CG  1 
ATOM   6760  N  ND1 . HIS   B  1 418 ? -37.250 30.315  10.431   1.00 77.22  ? 719  HIS   B ND1 1 
ATOM   6761  C  CD2 . HIS   B  1 418 ? -39.127 29.254  10.786   1.00 75.75  ? 719  HIS   B CD2 1 
ATOM   6762  C  CE1 . HIS   B  1 418 ? -37.438 30.280  11.739   1.00 77.77  ? 719  HIS   B CE1 1 
ATOM   6763  N  NE2 . HIS   B  1 418 ? -38.570 29.643  11.981   1.00 77.51  ? 719  HIS   B NE2 1 
ATOM   6764  N  N   . VAL   B  1 419 ? -40.358 32.202  9.063    1.00 96.49  ? 720  VAL   B N   1 
ATOM   6765  C  CA  . VAL   B  1 419 ? -40.339 33.523  9.683    1.00 99.68  ? 720  VAL   B CA  1 
ATOM   6766  C  C   . VAL   B  1 419 ? -39.540 33.422  10.981   1.00 97.62  ? 720  VAL   B C   1 
ATOM   6767  O  O   . VAL   B  1 419 ? -39.971 32.768  11.936   1.00 101.64 ? 720  VAL   B O   1 
ATOM   6768  C  CB  . VAL   B  1 419 ? -41.761 34.042  9.939    1.00 100.10 ? 720  VAL   B CB  1 
ATOM   6769  C  CG1 . VAL   B  1 419 ? -42.262 34.842  8.743    1.00 97.54  ? 720  VAL   B CG1 1 
ATOM   6770  C  CG2 . VAL   B  1 419 ? -42.711 32.874  10.246   1.00 97.30  ? 720  VAL   B CG2 1 
ATOM   6771  N  N   . TRP   B  1 420 ? -38.376 34.071  11.020   1.00 92.43  ? 721  TRP   B N   1 
ATOM   6772  C  CA  . TRP   B  1 420 ? -37.469 33.961  12.156   1.00 90.27  ? 721  TRP   B CA  1 
ATOM   6773  C  C   . TRP   B  1 420 ? -37.955 34.803  13.335   1.00 94.25  ? 721  TRP   B C   1 
ATOM   6774  O  O   . TRP   B  1 420 ? -38.847 35.649  13.212   1.00 92.19  ? 721  TRP   B O   1 
ATOM   6775  C  CB  . TRP   B  1 420 ? -36.056 34.390  11.762   1.00 87.58  ? 721  TRP   B CB  1 
ATOM   6776  C  CG  . TRP   B  1 420 ? -35.372 33.454  10.804   1.00 89.11  ? 721  TRP   B CG  1 
ATOM   6777  C  CD1 . TRP   B  1 420 ? -35.691 33.245  9.490    1.00 89.62  ? 721  TRP   B CD1 1 
ATOM   6778  C  CD2 . TRP   B  1 420 ? -34.241 32.612  11.079   1.00 83.18  ? 721  TRP   B CD2 1 
ATOM   6779  N  NE1 . TRP   B  1 420 ? -34.838 32.321  8.935    1.00 85.78  ? 721  TRP   B NE1 1 
ATOM   6780  C  CE2 . TRP   B  1 420 ? -33.937 31.919  9.886    1.00 81.90  ? 721  TRP   B CE2 1 
ATOM   6781  C  CE3 . TRP   B  1 420 ? -33.461 32.375  12.215   1.00 75.97  ? 721  TRP   B CE3 1 
ATOM   6782  C  CZ2 . TRP   B  1 420 ? -32.885 31.009  9.797    1.00 77.48  ? 721  TRP   B CZ2 1 
ATOM   6783  C  CZ3 . TRP   B  1 420 ? -32.418 31.472  12.127   1.00 74.99  ? 721  TRP   B CZ3 1 
ATOM   6784  C  CH2 . TRP   B  1 420 ? -32.140 30.799  10.925   1.00 77.68  ? 721  TRP   B CH2 1 
ATOM   6785  N  N   . LYS   B  1 421 ? -37.344 34.562  14.494   1.00 99.00  ? 722  LYS   B N   1 
ATOM   6786  C  CA  . LYS   B  1 421 ? -37.694 35.279  15.721   1.00 98.69  ? 722  LYS   B CA  1 
ATOM   6787  C  C   . LYS   B  1 421 ? -36.540 35.313  16.718   1.00 97.29  ? 722  LYS   B C   1 
ATOM   6788  O  O   . LYS   B  1 421 ? -35.444 35.781  16.408   1.00 96.40  ? 722  LYS   B O   1 
ATOM   6789  C  CB  . LYS   B  1 421 ? -38.931 34.649  16.368   1.00 96.34  ? 722  LYS   B CB  1 
ATOM   6790  C  CG  . LYS   B  1 421 ? -39.093 33.158  16.097   1.00 93.97  ? 722  LYS   B CG  1 
ATOM   6791  C  CD  . LYS   B  1 421 ? -40.547 32.727  16.246   1.00 93.02  ? 722  LYS   B CD  1 
ATOM   6792  C  CE  . LYS   B  1 421 ? -40.936 31.697  15.190   1.00 89.55  ? 722  LYS   B CE  1 
ATOM   6793  N  NZ  . LYS   B  1 421 ? -42.410 31.447  15.155   1.00 86.52  ? 722  LYS   B NZ  1 
ATOM   6794  N  N   . ARG   C  1 3   ? 0.025   43.494  -62.443  1.00 113.39 ? 304  ARG   C N   1 
ATOM   6795  C  CA  . ARG   C  1 3   ? 0.251   43.567  -63.881  1.00 117.04 ? 304  ARG   C CA  1 
ATOM   6796  C  C   . ARG   C  1 3   ? 1.656   44.100  -64.154  1.00 109.86 ? 304  ARG   C C   1 
ATOM   6797  O  O   . ARG   C  1 3   ? 1.850   44.930  -65.043  1.00 115.48 ? 304  ARG   C O   1 
ATOM   6798  C  CB  . ARG   C  1 3   ? -0.811  44.458  -64.542  1.00 125.47 ? 304  ARG   C CB  1 
ATOM   6799  C  CG  . ARG   C  1 3   ? -0.997  44.285  -66.055  1.00 126.91 ? 304  ARG   C CG  1 
ATOM   6800  C  CD  . ARG   C  1 3   ? -2.464  44.007  -66.398  1.00 134.09 ? 304  ARG   C CD  1 
ATOM   6801  N  NE  . ARG   C  1 3   ? -2.861  44.505  -67.718  1.00 139.57 ? 304  ARG   C NE  1 
ATOM   6802  C  CZ  . ARG   C  1 3   ? -3.796  45.434  -67.920  1.00 144.13 ? 304  ARG   C CZ  1 
ATOM   6803  N  NH1 . ARG   C  1 3   ? -4.441  45.968  -66.889  1.00 147.30 ? 304  ARG   C NH1 1 
ATOM   6804  N  NH2 . ARG   C  1 3   ? -4.093  45.828  -69.154  1.00 141.76 ? 304  ARG   C NH2 1 
ATOM   6805  N  N   . PHE   C  1 4   ? 2.635   43.617  -63.391  1.00 95.54  ? 305  PHE   C N   1 
ATOM   6806  C  CA  . PHE   C  1 4   ? 3.980   44.175  -63.460  1.00 86.10  ? 305  PHE   C CA  1 
ATOM   6807  C  C   . PHE   C  1 4   ? 4.944   43.293  -62.673  1.00 75.77  ? 305  PHE   C C   1 
ATOM   6808  O  O   . PHE   C  1 4   ? 4.539   42.501  -61.818  1.00 77.28  ? 305  PHE   C O   1 
ATOM   6809  C  CB  . PHE   C  1 4   ? 4.012   45.615  -62.930  1.00 95.06  ? 305  PHE   C CB  1 
ATOM   6810  C  CG  . PHE   C  1 4   ? 3.952   45.714  -61.425  1.00 106.15 ? 305  PHE   C CG  1 
ATOM   6811  C  CD1 . PHE   C  1 4   ? 2.850   45.239  -60.722  1.00 110.20 ? 305  PHE   C CD1 1 
ATOM   6812  C  CD2 . PHE   C  1 4   ? 4.997   46.288  -60.715  1.00 105.61 ? 305  PHE   C CD2 1 
ATOM   6813  C  CE1 . PHE   C  1 4   ? 2.797   45.325  -59.341  1.00 108.47 ? 305  PHE   C CE1 1 
ATOM   6814  C  CE2 . PHE   C  1 4   ? 4.949   46.377  -59.337  1.00 106.23 ? 305  PHE   C CE2 1 
ATOM   6815  C  CZ  . PHE   C  1 4   ? 3.847   45.895  -58.649  1.00 107.76 ? 305  PHE   C CZ  1 
ATOM   6816  N  N   . LEU   C  1 5   ? 6.232   43.448  -62.981  1.00 63.69  ? 306  LEU   C N   1 
ATOM   6817  C  CA  . LEU   C  1 5   ? 7.313   42.693  -62.351  1.00 54.58  ? 306  LEU   C CA  1 
ATOM   6818  C  C   . LEU   C  1 5   ? 8.568   43.537  -62.447  1.00 53.56  ? 306  LEU   C C   1 
ATOM   6819  O  O   . LEU   C  1 5   ? 9.058   43.790  -63.549  1.00 65.38  ? 306  LEU   C O   1 
ATOM   6820  C  CB  . LEU   C  1 5   ? 7.552   41.340  -63.027  1.00 49.03  ? 306  LEU   C CB  1 
ATOM   6821  C  CG  . LEU   C  1 5   ? 6.576   40.193  -62.796  1.00 49.87  ? 306  LEU   C CG  1 
ATOM   6822  C  CD1 . LEU   C  1 5   ? 6.959   39.015  -63.664  1.00 47.85  ? 306  LEU   C CD1 1 
ATOM   6823  C  CD2 . LEU   C  1 5   ? 6.560   39.811  -61.323  1.00 40.86  ? 306  LEU   C CD2 1 
ATOM   6824  N  N   . LYS   C  1 6   ? 9.094   43.953  -61.311  1.00 48.96  ? 307  LYS   C N   1 
ATOM   6825  C  CA  . LYS   C  1 6   ? 10.226  44.856  -61.302  1.00 46.83  ? 307  LYS   C CA  1 
ATOM   6826  C  C   . LYS   C  1 6   ? 11.527  44.079  -61.201  1.00 49.63  ? 307  LYS   C C   1 
ATOM   6827  O  O   . LYS   C  1 6   ? 11.586  42.997  -60.608  1.00 50.88  ? 307  LYS   C O   1 
ATOM   6828  C  CB  . LYS   C  1 6   ? 10.114  45.843  -60.144  1.00 54.89  ? 307  LYS   C CB  1 
ATOM   6829  C  CG  . LYS   C  1 6   ? 8.932   46.803  -60.234  1.00 63.30  ? 307  LYS   C CG  1 
ATOM   6830  C  CD  . LYS   C  1 6   ? 8.758   47.568  -58.917  1.00 73.19  ? 307  LYS   C CD  1 
ATOM   6831  C  CE  . LYS   C  1 6   ? 7.694   48.655  -59.002  1.00 74.00  ? 307  LYS   C CE  1 
ATOM   6832  N  NZ  . LYS   C  1 6   ? 8.062   49.693  -60.004  1.00 72.90  ? 307  LYS   C NZ  1 
ATOM   6833  N  N   . VAL   C  1 7   ? 12.568  44.633  -61.808  1.00 43.21  ? 308  VAL   C N   1 
ATOM   6834  C  CA  . VAL   C  1 7   ? 13.928  44.150  -61.625  1.00 41.86  ? 308  VAL   C CA  1 
ATOM   6835  C  C   . VAL   C  1 7   ? 14.749  45.316  -61.108  1.00 43.97  ? 308  VAL   C C   1 
ATOM   6836  O  O   . VAL   C  1 7   ? 14.439  46.479  -61.380  1.00 44.63  ? 308  VAL   C O   1 
ATOM   6837  C  CB  . VAL   C  1 7   ? 14.543  43.578  -62.923  1.00 50.27  ? 308  VAL   C CB  1 
ATOM   6838  C  CG1 . VAL   C  1 7   ? 13.604  42.557  -63.559  1.00 49.28  ? 308  VAL   C CG1 1 
ATOM   6839  C  CG2 . VAL   C  1 7   ? 14.885  44.696  -63.896  1.00 49.37  ? 308  VAL   C CG2 1 
ATOM   6840  N  N   . LYS   C  1 8   ? 15.786  45.003  -60.337  1.00 39.19  ? 309  LYS   C N   1 
ATOM   6841  C  CA  . LYS   C  1 8   ? 16.588  46.022  -59.684  1.00 39.41  ? 309  LYS   C CA  1 
ATOM   6842  C  C   . LYS   C  1 8   ? 18.051  45.749  -59.953  1.00 32.84  ? 309  LYS   C C   1 
ATOM   6843  O  O   . LYS   C  1 8   ? 18.475  44.595  -59.965  1.00 45.96  ? 309  LYS   C O   1 
ATOM   6844  C  CB  . LYS   C  1 8   ? 16.340  46.052  -58.161  1.00 42.51  ? 309  LYS   C CB  1 
ATOM   6845  C  CG  . LYS   C  1 8   ? 17.255  46.991  -57.376  1.00 49.10  ? 309  LYS   C CG  1 
ATOM   6846  C  CD  . LYS   C  1 8   ? 16.857  47.076  -55.894  1.00 54.92  ? 309  LYS   C CD  1 
ATOM   6847  C  CE  . LYS   C  1 8   ? 17.819  47.945  -55.091  1.00 59.23  ? 309  LYS   C CE  1 
ATOM   6848  N  NZ  . LYS   C  1 8   ? 17.605  47.827  -53.609  1.00 54.60  ? 309  LYS   C NZ  1 
ATOM   6849  N  N   . ASN   C  1 9   ? 18.821  46.818  -60.140  1.00 43.20  ? 310  ASN   C N   1 
ATOM   6850  C  CA  . ASN   C  1 9   ? 20.276  46.752  -60.215  1.00 48.44  ? 310  ASN   C CA  1 
ATOM   6851  C  C   . ASN   C  1 9   ? 20.835  47.219  -58.874  1.00 48.71  ? 310  ASN   C C   1 
ATOM   6852  O  O   . ASN   C  1 9   ? 20.532  48.331  -58.435  1.00 53.23  ? 310  ASN   C O   1 
ATOM   6853  C  CB  . ASN   C  1 9   ? 20.793  47.612  -61.373  1.00 43.76  ? 310  ASN   C CB  1 
ATOM   6854  C  CG  . ASN   C  1 9   ? 22.307  47.577  -61.501  1.00 51.34  ? 310  ASN   C CG  1 
ATOM   6855  O  OD1 . ASN   C  1 9   ? 23.037  47.902  -60.558  1.00 57.43  ? 310  ASN   C OD1 1 
ATOM   6856  N  ND2 . ASN   C  1 9   ? 22.790  47.175  -62.670  1.00 46.36  ? 310  ASN   C ND2 1 
ATOM   6857  N  N   . TRP   C  1 10  ? 21.647  46.378  -58.221  1.00 49.29  ? 311  TRP   C N   1 
ATOM   6858  C  CA  . TRP   C  1 10  ? 22.043  46.650  -56.835  1.00 49.12  ? 311  TRP   C CA  1 
ATOM   6859  C  C   . TRP   C  1 10  ? 23.278  47.538  -56.714  1.00 53.57  ? 311  TRP   C C   1 
ATOM   6860  O  O   . TRP   C  1 10  ? 23.592  47.976  -55.603  1.00 62.57  ? 311  TRP   C O   1 
ATOM   6861  C  CB  . TRP   C  1 10  ? 22.257  45.336  -56.059  1.00 35.10  ? 311  TRP   C CB  1 
ATOM   6862  C  CG  . TRP   C  1 10  ? 20.979  44.589  -55.852  1.00 36.92  ? 311  TRP   C CG  1 
ATOM   6863  C  CD1 . TRP   C  1 10  ? 20.374  43.735  -56.735  1.00 39.33  ? 311  TRP   C CD1 1 
ATOM   6864  C  CD2 . TRP   C  1 10  ? 20.122  44.644  -54.702  1.00 42.79  ? 311  TRP   C CD2 1 
ATOM   6865  N  NE1 . TRP   C  1 10  ? 19.202  43.246  -56.203  1.00 42.57  ? 311  TRP   C NE1 1 
ATOM   6866  C  CE2 . TRP   C  1 10  ? 19.024  43.789  -54.956  1.00 43.61  ? 311  TRP   C CE2 1 
ATOM   6867  C  CE3 . TRP   C  1 10  ? 20.182  45.320  -53.479  1.00 48.75  ? 311  TRP   C CE3 1 
ATOM   6868  C  CZ2 . TRP   C  1 10  ? 17.990  43.605  -54.037  1.00 47.33  ? 311  TRP   C CZ2 1 
ATOM   6869  C  CZ3 . TRP   C  1 10  ? 19.151  45.137  -52.565  1.00 47.77  ? 311  TRP   C CZ3 1 
ATOM   6870  C  CH2 . TRP   C  1 10  ? 18.075  44.282  -52.846  1.00 47.76  ? 311  TRP   C CH2 1 
ATOM   6871  N  N   . GLU   C  1 11  ? 23.975  47.817  -57.818  1.00 53.09  ? 312  GLU   C N   1 
ATOM   6872  C  CA  . GLU   C  1 11  ? 24.983  48.873  -57.850  1.00 45.12  ? 312  GLU   C CA  1 
ATOM   6873  C  C   . GLU   C  1 11  ? 24.336  50.250  -57.897  1.00 46.91  ? 312  GLU   C C   1 
ATOM   6874  O  O   . GLU   C  1 11  ? 24.738  51.163  -57.174  1.00 58.08  ? 312  GLU   C O   1 
ATOM   6875  C  CB  . GLU   C  1 11  ? 25.883  48.721  -59.076  1.00 54.61  ? 312  GLU   C CB  1 
ATOM   6876  C  CG  . GLU   C  1 11  ? 27.074  47.815  -58.935  1.00 67.42  ? 312  GLU   C CG  1 
ATOM   6877  C  CD  . GLU   C  1 11  ? 28.011  47.932  -60.137  1.00 74.37  ? 312  GLU   C CD  1 
ATOM   6878  O  OE1 . GLU   C  1 11  ? 27.651  47.457  -61.236  1.00 69.25  ? 312  GLU   C OE1 1 
ATOM   6879  O  OE2 . GLU   C  1 11  ? 29.102  48.521  -59.985  1.00 78.72  ? 312  GLU   C OE2 1 
ATOM   6880  N  N   . THR   C  1 12  ? 23.349  50.425  -58.774  1.00 46.51  ? 313  THR   C N   1 
ATOM   6881  C  CA  . THR   C  1 12  ? 22.822  51.743  -59.088  1.00 45.76  ? 313  THR   C CA  1 
ATOM   6882  C  C   . THR   C  1 12  ? 21.452  51.998  -58.484  1.00 53.41  ? 313  THR   C C   1 
ATOM   6883  O  O   . THR   C  1 12  ? 21.000  53.147  -58.483  1.00 56.34  ? 313  THR   C O   1 
ATOM   6884  C  CB  . THR   C  1 12  ? 22.740  51.922  -60.612  1.00 55.57  ? 313  THR   C CB  1 
ATOM   6885  O  OG1 . THR   C  1 12  ? 21.556  51.281  -61.107  1.00 50.79  ? 313  THR   C OG1 1 
ATOM   6886  C  CG2 . THR   C  1 12  ? 23.943  51.281  -61.279  1.00 54.04  ? 313  THR   C CG2 1 
ATOM   6887  N  N   . GLU   C  1 13  ? 20.778  50.957  -58.005  1.00 54.53  ? 314  GLU   C N   1 
ATOM   6888  C  CA  . GLU   C  1 13  ? 19.406  50.986  -57.505  1.00 54.35  ? 314  GLU   C CA  1 
ATOM   6889  C  C   . GLU   C  1 13  ? 18.380  51.338  -58.578  1.00 51.44  ? 314  GLU   C C   1 
ATOM   6890  O  O   . GLU   C  1 13  ? 17.217  51.604  -58.248  1.00 42.16  ? 314  GLU   C O   1 
ATOM   6891  C  CB  . GLU   C  1 13  ? 19.264  51.922  -56.304  1.00 57.92  ? 314  GLU   C CB  1 
ATOM   6892  C  CG  . GLU   C  1 13  ? 20.126  51.489  -55.146  1.00 67.23  ? 314  GLU   C CG  1 
ATOM   6893  C  CD  . GLU   C  1 13  ? 19.934  52.359  -53.925  1.00 72.88  ? 314  GLU   C CD  1 
ATOM   6894  O  OE1 . GLU   C  1 13  ? 18.824  52.331  -53.350  1.00 76.40  ? 314  GLU   C OE1 1 
ATOM   6895  O  OE2 . GLU   C  1 13  ? 20.891  53.077  -53.558  1.00 71.48  ? 314  GLU   C OE2 1 
ATOM   6896  N  N   . VAL   C  1 14  ? 18.762  51.321  -59.862  1.00 43.06  ? 315  VAL   C N   1 
ATOM   6897  C  CA  . VAL   C  1 14  ? 17.764  51.477  -60.907  1.00 47.96  ? 315  VAL   C CA  1 
ATOM   6898  C  C   . VAL   C  1 14  ? 16.794  50.307  -60.825  1.00 53.84  ? 315  VAL   C C   1 
ATOM   6899  O  O   . VAL   C  1 14  ? 17.204  49.147  -60.691  1.00 59.89  ? 315  VAL   C O   1 
ATOM   6900  C  CB  . VAL   C  1 14  ? 18.449  51.580  -62.280  1.00 55.59  ? 315  VAL   C CB  1 
ATOM   6901  C  CG1 . VAL   C  1 14  ? 17.468  51.274  -63.424  1.00 55.48  ? 315  VAL   C CG1 1 
ATOM   6902  C  CG2 . VAL   C  1 14  ? 19.061  52.960  -62.446  1.00 54.63  ? 315  VAL   C CG2 1 
ATOM   6903  N  N   . VAL   C  1 15  ? 15.497  50.608  -60.834  1.00 51.37  ? 316  VAL   C N   1 
ATOM   6904  C  CA  . VAL   C  1 15  ? 14.458  49.588  -60.916  1.00 52.69  ? 316  VAL   C CA  1 
ATOM   6905  C  C   . VAL   C  1 15  ? 13.763  49.720  -62.267  1.00 61.45  ? 316  VAL   C C   1 
ATOM   6906  O  O   . VAL   C  1 15  ? 13.357  50.824  -62.655  1.00 67.49  ? 316  VAL   C O   1 
ATOM   6907  C  CB  . VAL   C  1 15  ? 13.441  49.699  -59.769  1.00 45.64  ? 316  VAL   C CB  1 
ATOM   6908  C  CG1 . VAL   C  1 15  ? 12.342  48.636  -59.924  1.00 37.72  ? 316  VAL   C CG1 1 
ATOM   6909  C  CG2 . VAL   C  1 15  ? 14.130  49.554  -58.408  1.00 36.76  ? 316  VAL   C CG2 1 
ATOM   6910  N  N   . LEU   C  1 16  ? 13.625  48.602  -62.982  1.00 55.86  ? 317  LEU   C N   1 
ATOM   6911  C  CA  . LEU   C  1 16  ? 12.865  48.556  -64.225  1.00 51.57  ? 317  LEU   C CA  1 
ATOM   6912  C  C   . LEU   C  1 16  ? 11.606  47.724  -64.025  1.00 51.31  ? 317  LEU   C C   1 
ATOM   6913  O  O   . LEU   C  1 16  ? 11.565  46.824  -63.182  1.00 53.48  ? 317  LEU   C O   1 
ATOM   6914  C  CB  . LEU   C  1 16  ? 13.698  47.982  -65.371  1.00 45.40  ? 317  LEU   C CB  1 
ATOM   6915  C  CG  . LEU   C  1 16  ? 15.069  48.632  -65.565  1.00 40.54  ? 317  LEU   C CG  1 
ATOM   6916  C  CD1 . LEU   C  1 16  ? 15.921  47.826  -66.537  1.00 36.13  ? 317  LEU   C CD1 1 
ATOM   6917  C  CD2 . LEU   C  1 16  ? 14.915  50.083  -66.022  1.00 39.18  ? 317  LEU   C CD2 1 
ATOM   6918  N  N   . THR   C  1 17  ? 10.575  48.037  -64.803  1.00 45.65  ? 318  THR   C N   1 
ATOM   6919  C  CA  . THR   C  1 17  ? 9.243   47.474  -64.626  1.00 44.94  ? 318  THR   C CA  1 
ATOM   6920  C  C   . THR   C  1 17  ? 8.856   46.732  -65.896  1.00 47.50  ? 318  THR   C C   1 
ATOM   6921  O  O   . THR   C  1 17  ? 8.673   47.347  -66.949  1.00 53.28  ? 318  THR   C O   1 
ATOM   6922  C  CB  . THR   C  1 17  ? 8.232   48.570  -64.315  1.00 53.11  ? 318  THR   C CB  1 
ATOM   6923  O  OG1 . THR   C  1 17  ? 8.889   49.608  -63.578  1.00 53.98  ? 318  THR   C OG1 1 
ATOM   6924  C  CG2 . THR   C  1 17  ? 7.077   48.004  -63.499  1.00 55.21  ? 318  THR   C CG2 1 
ATOM   6925  N  N   . ASP   C  1 18  ? 8.700   45.424  -65.785  1.00 41.72  ? 319  ASP   C N   1 
ATOM   6926  C  CA  . ASP   C  1 18  ? 8.542   44.549  -66.931  1.00 40.93  ? 319  ASP   C CA  1 
ATOM   6927  C  C   . ASP   C  1 18  ? 7.074   44.216  -67.127  1.00 46.75  ? 319  ASP   C C   1 
ATOM   6928  O  O   . ASP   C  1 18  ? 6.434   43.667  -66.223  1.00 42.30  ? 319  ASP   C O   1 
ATOM   6929  C  CB  . ASP   C  1 18  ? 9.358   43.277  -66.732  1.00 43.31  ? 319  ASP   C CB  1 
ATOM   6930  C  CG  . ASP   C  1 18  ? 9.468   42.446  -67.992  1.00 41.89  ? 319  ASP   C CG  1 
ATOM   6931  O  OD1 . ASP   C  1 18  ? 8.421   42.079  -68.553  1.00 43.20  ? 319  ASP   C OD1 1 
ATOM   6932  O  OD2 . ASP   C  1 18  ? 10.608  42.146  -68.403  1.00 42.65  ? 319  ASP   C OD2 1 
ATOM   6933  N  N   . THR   C  1 19  ? 6.549   44.555  -68.311  1.00 42.77  ? 320  THR   C N   1 
ATOM   6934  C  CA  . THR   C  1 19  ? 5.272   44.047  -68.792  1.00 45.36  ? 320  THR   C CA  1 
ATOM   6935  C  C   . THR   C  1 19  ? 5.394   43.210  -70.060  1.00 48.14  ? 320  THR   C C   1 
ATOM   6936  O  O   . THR   C  1 19  ? 4.455   42.475  -70.384  1.00 44.24  ? 320  THR   C O   1 
ATOM   6937  C  CB  . THR   C  1 19  ? 4.293   45.199  -69.066  1.00 49.13  ? 320  THR   C CB  1 
ATOM   6938  O  OG1 . THR   C  1 19  ? 4.904   46.157  -69.947  1.00 50.25  ? 320  THR   C OG1 1 
ATOM   6939  C  CG2 . THR   C  1 19  ? 3.886   45.886  -67.764  1.00 40.07  ? 320  THR   C CG2 1 
ATOM   6940  N  N   . LEU   C  1 20  ? 6.516   43.295  -70.779  1.00 50.53  ? 321  LEU   C N   1 
ATOM   6941  C  CA  . LEU   C  1 20  ? 6.689   42.502  -71.995  1.00 50.80  ? 321  LEU   C CA  1 
ATOM   6942  C  C   . LEU   C  1 20  ? 6.493   41.011  -71.735  1.00 50.63  ? 321  LEU   C C   1 
ATOM   6943  O  O   . LEU   C  1 20  ? 5.979   40.296  -72.602  1.00 38.21  ? 321  LEU   C O   1 
ATOM   6944  C  CB  . LEU   C  1 20  ? 8.070   42.764  -72.591  1.00 43.31  ? 321  LEU   C CB  1 
ATOM   6945  C  CG  . LEU   C  1 20  ? 8.470   41.963  -73.827  1.00 41.61  ? 321  LEU   C CG  1 
ATOM   6946  C  CD1 . LEU   C  1 20  ? 7.515   42.248  -75.025  1.00 35.78  ? 321  LEU   C CD1 1 
ATOM   6947  C  CD2 . LEU   C  1 20  ? 9.923   42.261  -74.177  1.00 35.26  ? 321  LEU   C CD2 1 
ATOM   6948  N  N   . HIS   C  1 21  ? 6.851   40.535  -70.536  1.00 46.89  ? 322  HIS   C N   1 
ATOM   6949  C  CA  . HIS   C  1 21  ? 6.719   39.120  -70.203  1.00 47.50  ? 322  HIS   C CA  1 
ATOM   6950  C  C   . HIS   C  1 21  ? 5.288   38.613  -70.332  1.00 45.42  ? 322  HIS   C C   1 
ATOM   6951  O  O   . HIS   C  1 21  ? 5.079   37.400  -70.412  1.00 49.97  ? 322  HIS   C O   1 
ATOM   6952  C  CB  . HIS   C  1 21  ? 7.191   38.863  -68.768  1.00 48.44  ? 322  HIS   C CB  1 
ATOM   6953  C  CG  . HIS   C  1 21  ? 6.176   39.264  -67.745  1.00 38.99  ? 322  HIS   C CG  1 
ATOM   6954  N  ND1 . HIS   C  1 21  ? 6.162   40.513  -67.166  1.00 41.45  ? 322  HIS   C ND1 1 
ATOM   6955  C  CD2 . HIS   C  1 21  ? 5.095   38.611  -67.260  1.00 39.43  ? 322  HIS   C CD2 1 
ATOM   6956  C  CE1 . HIS   C  1 21  ? 5.134   40.602  -66.343  1.00 48.59  ? 322  HIS   C CE1 1 
ATOM   6957  N  NE2 . HIS   C  1 21  ? 4.467   39.462  -66.386  1.00 49.18  ? 322  HIS   C NE2 1 
ATOM   6958  N  N   . LEU   C  1 22  ? 4.291   39.496  -70.301  1.00 41.55  ? 323  LEU   C N   1 
ATOM   6959  C  CA  . LEU   C  1 22  ? 2.929   39.020  -70.507  1.00 48.03  ? 323  LEU   C CA  1 
ATOM   6960  C  C   . LEU   C  1 22  ? 2.713   38.461  -71.912  1.00 49.53  ? 323  LEU   C C   1 
ATOM   6961  O  O   . LEU   C  1 22  ? 1.724   37.761  -72.134  1.00 53.11  ? 323  LEU   C O   1 
ATOM   6962  C  CB  . LEU   C  1 22  ? 1.932   40.144  -70.202  1.00 52.81  ? 323  LEU   C CB  1 
ATOM   6963  C  CG  . LEU   C  1 22  ? 1.990   40.562  -68.725  1.00 55.74  ? 323  LEU   C CG  1 
ATOM   6964  C  CD1 . LEU   C  1 22  ? 1.293   41.883  -68.460  1.00 53.15  ? 323  LEU   C CD1 1 
ATOM   6965  C  CD2 . LEU   C  1 22  ? 1.396   39.476  -67.847  1.00 58.25  ? 323  LEU   C CD2 1 
ATOM   6966  N  N   . LYS   C  1 23  ? 3.632   38.707  -72.840  1.00 49.10  ? 324  LYS   C N   1 
ATOM   6967  C  CA  . LYS   C  1 23  ? 3.594   38.116  -74.172  1.00 49.69  ? 324  LYS   C CA  1 
ATOM   6968  C  C   . LYS   C  1 23  ? 4.331   36.789  -74.257  1.00 57.51  ? 324  LYS   C C   1 
ATOM   6969  O  O   . LYS   C  1 23  ? 4.456   36.243  -75.358  1.00 61.19  ? 324  LYS   C O   1 
ATOM   6970  C  CB  . LYS   C  1 23  ? 4.206   39.072  -75.204  1.00 39.90  ? 324  LYS   C CB  1 
ATOM   6971  C  CG  . LYS   C  1 23  ? 3.491   40.381  -75.359  1.00 48.96  ? 324  LYS   C CG  1 
ATOM   6972  C  CD  . LYS   C  1 23  ? 2.691   40.418  -76.639  1.00 62.70  ? 324  LYS   C CD  1 
ATOM   6973  C  CE  . LYS   C  1 23  ? 1.319   39.810  -76.461  1.00 69.40  ? 324  LYS   C CE  1 
ATOM   6974  N  NZ  . LYS   C  1 23  ? 0.468   40.127  -77.644  1.00 70.29  ? 324  LYS   C NZ  1 
ATOM   6975  N  N   . SER   C  1 24  ? 4.851   36.279  -73.141  1.00 56.15  ? 325  SER   C N   1 
ATOM   6976  C  CA  . SER   C  1 24  ? 5.582   35.019  -73.153  1.00 59.47  ? 325  SER   C CA  1 
ATOM   6977  C  C   . SER   C  1 24  ? 4.706   33.896  -73.704  1.00 59.07  ? 325  SER   C C   1 
ATOM   6978  O  O   . SER   C  1 24  ? 3.512   33.807  -73.402  1.00 58.26  ? 325  SER   C O   1 
ATOM   6979  C  CB  . SER   C  1 24  ? 6.055   34.685  -71.735  1.00 61.49  ? 325  SER   C CB  1 
ATOM   6980  O  OG  . SER   C  1 24  ? 6.545   33.362  -71.649  1.00 63.38  ? 325  SER   C OG  1 
ATOM   6981  N  N   . THR   C  1 25  ? 5.296   33.032  -74.524  1.00 63.51  ? 326  THR   C N   1 
ATOM   6982  C  CA  . THR   C  1 25  ? 4.501   31.999  -75.177  1.00 73.20  ? 326  THR   C CA  1 
ATOM   6983  C  C   . THR   C  1 25  ? 4.722   30.608  -74.597  1.00 74.47  ? 326  THR   C C   1 
ATOM   6984  O  O   . THR   C  1 25  ? 3.745   29.929  -74.263  1.00 84.49  ? 326  THR   C O   1 
ATOM   6985  C  CB  . THR   C  1 25  ? 4.750   32.013  -76.701  1.00 72.41  ? 326  THR   C CB  1 
ATOM   6986  O  OG1 . THR   C  1 25  ? 5.998   32.655  -76.992  1.00 72.13  ? 326  THR   C OG1 1 
ATOM   6987  C  CG2 . THR   C  1 25  ? 3.634   32.764  -77.415  1.00 70.22  ? 326  THR   C CG2 1 
ATOM   6988  N  N   . LEU   C  1 26  ? 5.966   30.162  -74.423  1.00 64.84  ? 327  LEU   C N   1 
ATOM   6989  C  CA  . LEU   C  1 26  ? 6.206   28.787  -74.003  1.00 65.67  ? 327  LEU   C CA  1 
ATOM   6990  C  C   . LEU   C  1 26  ? 6.926   28.710  -72.652  1.00 63.33  ? 327  LEU   C C   1 
ATOM   6991  O  O   . LEU   C  1 26  ? 7.511   29.682  -72.162  1.00 50.54  ? 327  LEU   C O   1 
ATOM   6992  C  CB  . LEU   C  1 26  ? 6.983   27.989  -75.066  1.00 70.29  ? 327  LEU   C CB  1 
ATOM   6993  C  CG  . LEU   C  1 26  ? 7.841   28.511  -76.233  1.00 73.58  ? 327  LEU   C CG  1 
ATOM   6994  C  CD1 . LEU   C  1 26  ? 8.115   27.344  -77.154  1.00 64.71  ? 327  LEU   C CD1 1 
ATOM   6995  C  CD2 . LEU   C  1 26  ? 7.253   29.646  -77.059  1.00 76.48  ? 327  LEU   C CD2 1 
ATOM   6996  N  N   . GLU   C  1 27  ? 6.857   27.519  -72.054  1.00 60.62  ? 328  GLU   C N   1 
ATOM   6997  C  CA  . GLU   C  1 27  ? 7.340   27.299  -70.697  1.00 54.87  ? 328  GLU   C CA  1 
ATOM   6998  C  C   . GLU   C  1 27  ? 8.846   27.516  -70.596  1.00 51.68  ? 328  GLU   C C   1 
ATOM   6999  O  O   . GLU   C  1 27  ? 9.600   27.302  -71.551  1.00 54.58  ? 328  GLU   C O   1 
ATOM   7000  C  CB  . GLU   C  1 27  ? 6.967   25.888  -70.233  1.00 50.96  ? 328  GLU   C CB  1 
ATOM   7001  C  CG  . GLU   C  1 27  ? 5.479   25.733  -69.892  1.00 53.54  ? 328  GLU   C CG  1 
ATOM   7002  C  CD  . GLU   C  1 27  ? 5.071   24.297  -69.583  1.00 63.74  ? 328  GLU   C CD  1 
ATOM   7003  O  OE1 . GLU   C  1 27  ? 5.954   23.411  -69.549  1.00 69.73  ? 328  GLU   C OE1 1 
ATOM   7004  O  OE2 . GLU   C  1 27  ? 3.863   24.055  -69.376  1.00 65.69  ? 328  GLU   C OE2 1 
ATOM   7005  N  N   . THR   C  1 28  ? 9.273   27.989  -69.425  1.00 49.32  ? 329  THR   C N   1 
ATOM   7006  C  CA  . THR   C  1 28  ? 10.690  28.118  -69.111  1.00 40.96  ? 329  THR   C CA  1 
ATOM   7007  C  C   . THR   C  1 28  ? 11.274  26.838  -68.554  1.00 37.29  ? 329  THR   C C   1 
ATOM   7008  O  O   . THR   C  1 28  ? 12.487  26.641  -68.651  1.00 44.98  ? 329  THR   C O   1 
ATOM   7009  C  CB  . THR   C  1 28  ? 10.935  29.229  -68.083  1.00 43.18  ? 329  THR   C CB  1 
ATOM   7010  O  OG1 . THR   C  1 28  ? 10.168  28.969  -66.891  1.00 42.00  ? 329  THR   C OG1 1 
ATOM   7011  C  CG2 . THR   C  1 28  ? 10.593  30.594  -68.652  1.00 42.13  ? 329  THR   C CG2 1 
ATOM   7012  N  N   . GLY   C  1 29  ? 10.439  25.968  -67.990  1.00 40.88  ? 330  GLY   C N   1 
ATOM   7013  C  CA  . GLY   C  1 29  ? 10.882  24.826  -67.229  1.00 47.14  ? 330  GLY   C CA  1 
ATOM   7014  C  C   . GLY   C  1 29  ? 10.690  24.981  -65.734  1.00 52.98  ? 330  GLY   C C   1 
ATOM   7015  O  O   . GLY   C  1 29  ? 10.534  23.976  -65.034  1.00 51.78  ? 330  GLY   C O   1 
ATOM   7016  N  N   . CYS   C  1 30  ? 10.660  26.215  -65.238  1.00 51.57  ? 331  CYS   C N   1 
ATOM   7017  C  CA  . CYS   C  1 30  ? 10.451  26.475  -63.824  1.00 43.17  ? 331  CYS   C CA  1 
ATOM   7018  C  C   . CYS   C  1 30  ? 8.983   26.292  -63.448  1.00 49.02  ? 331  CYS   C C   1 
ATOM   7019  O  O   . CYS   C  1 30  ? 8.092   26.281  -64.300  1.00 49.84  ? 331  CYS   C O   1 
ATOM   7020  C  CB  . CYS   C  1 30  ? 10.900  27.891  -63.474  1.00 32.88  ? 331  CYS   C CB  1 
ATOM   7021  S  SG  . CYS   C  1 30  ? 12.609  28.271  -63.917  1.00 38.33  ? 331  CYS   C SG  1 
ATOM   7022  N  N   . THR   C  1 31  ? 8.740   26.122  -62.146  1.00 45.78  ? 332  THR   C N   1 
ATOM   7023  C  CA  . THR   C  1 31  ? 7.414   26.259  -61.565  1.00 43.27  ? 332  THR   C CA  1 
ATOM   7024  C  C   . THR   C  1 31  ? 7.523   27.079  -60.289  1.00 47.15  ? 332  THR   C C   1 
ATOM   7025  O  O   . THR   C  1 31  ? 8.617   27.439  -59.847  1.00 54.97  ? 332  THR   C O   1 
ATOM   7026  C  CB  . THR   C  1 31  ? 6.764   24.904  -61.249  1.00 48.62  ? 332  THR   C CB  1 
ATOM   7027  O  OG1 . THR   C  1 31  ? 7.445   24.278  -60.149  1.00 43.53  ? 332  THR   C OG1 1 
ATOM   7028  C  CG2 . THR   C  1 31  ? 6.776   23.981  -62.471  1.00 48.46  ? 332  THR   C CG2 1 
ATOM   7029  N  N   . GLU   C  1 32  ? 6.368   27.350  -59.677  1.00 47.52  ? 333  GLU   C N   1 
ATOM   7030  C  CA  . GLU   C  1 32  ? 6.346   27.964  -58.356  1.00 47.30  ? 333  GLU   C CA  1 
ATOM   7031  C  C   . GLU   C  1 32  ? 7.252   27.228  -57.373  1.00 50.51  ? 333  GLU   C C   1 
ATOM   7032  O  O   . GLU   C  1 32  ? 7.812   27.852  -56.465  1.00 44.90  ? 333  GLU   C O   1 
ATOM   7033  C  CB  . GLU   C  1 32  ? 4.910   28.004  -57.816  1.00 58.38  ? 333  GLU   C CB  1 
ATOM   7034  C  CG  . GLU   C  1 32  ? 4.054   29.144  -58.366  1.00 74.83  ? 333  GLU   C CG  1 
ATOM   7035  C  CD  . GLU   C  1 32  ? 3.342   28.812  -59.684  1.00 89.69  ? 333  GLU   C CD  1 
ATOM   7036  O  OE1 . GLU   C  1 32  ? 2.185   29.261  -59.849  1.00 98.41  ? 333  GLU   C OE1 1 
ATOM   7037  O  OE2 . GLU   C  1 32  ? 3.924   28.117  -60.550  1.00 85.16  ? 333  GLU   C OE2 1 
ATOM   7038  N  N   . TYR   C  1 33  ? 7.438   25.914  -57.543  1.00 45.77  ? 334  TYR   C N   1 
ATOM   7039  C  CA  . TYR   C  1 33  ? 8.166   25.128  -56.553  1.00 54.39  ? 334  TYR   C CA  1 
ATOM   7040  C  C   . TYR   C  1 33  ? 9.563   24.703  -56.981  1.00 56.73  ? 334  TYR   C C   1 
ATOM   7041  O  O   . TYR   C  1 33  ? 10.276  24.097  -56.172  1.00 62.95  ? 334  TYR   C O   1 
ATOM   7042  C  CB  . TYR   C  1 33  ? 7.363   23.878  -56.165  1.00 52.67  ? 334  TYR   C CB  1 
ATOM   7043  C  CG  . TYR   C  1 33  ? 6.041   24.194  -55.535  1.00 59.52  ? 334  TYR   C CG  1 
ATOM   7044  C  CD1 . TYR   C  1 33  ? 5.904   24.255  -54.152  1.00 71.04  ? 334  TYR   C CD1 1 
ATOM   7045  C  CD2 . TYR   C  1 33  ? 4.927   24.443  -56.317  1.00 59.08  ? 334  TYR   C CD2 1 
ATOM   7046  C  CE1 . TYR   C  1 33  ? 4.684   24.550  -53.567  1.00 73.88  ? 334  TYR   C CE1 1 
ATOM   7047  C  CE2 . TYR   C  1 33  ? 3.713   24.740  -55.748  1.00 63.60  ? 334  TYR   C CE2 1 
ATOM   7048  C  CZ  . TYR   C  1 33  ? 3.595   24.789  -54.378  1.00 73.85  ? 334  TYR   C CZ  1 
ATOM   7049  O  OH  . TYR   C  1 33  ? 2.379   25.082  -53.827  1.00 84.68  ? 334  TYR   C OH  1 
ATOM   7050  N  N   . ILE   C  1 34  ? 9.986   24.993  -58.207  1.00 48.63  ? 335  ILE   C N   1 
ATOM   7051  C  CA  . ILE   C  1 34  ? 11.322  24.589  -58.625  1.00 49.92  ? 335  ILE   C CA  1 
ATOM   7052  C  C   . ILE   C  1 34  ? 11.814  25.527  -59.726  1.00 47.25  ? 335  ILE   C C   1 
ATOM   7053  O  O   . ILE   C  1 34  ? 11.077  25.844  -60.665  1.00 48.85  ? 335  ILE   C O   1 
ATOM   7054  C  CB  . ILE   C  1 34  ? 11.331  23.115  -59.076  1.00 58.23  ? 335  ILE   C CB  1 
ATOM   7055  C  CG1 . ILE   C  1 34  ? 12.759  22.638  -59.310  1.00 59.06  ? 335  ILE   C CG1 1 
ATOM   7056  C  CG2 . ILE   C  1 34  ? 10.508  22.927  -60.341  1.00 66.83  ? 335  ILE   C CG2 1 
ATOM   7057  C  CD1 . ILE   C  1 34  ? 12.886  21.151  -59.237  1.00 64.01  ? 335  ILE   C CD1 1 
ATOM   7058  N  N   . CYS   C  1 35  ? 13.058  25.991  -59.593  1.00 35.79  ? 336  CYS   C N   1 
ATOM   7059  C  CA  . CYS   C  1 35  ? 13.696  26.829  -60.600  1.00 36.35  ? 336  CYS   C CA  1 
ATOM   7060  C  C   . CYS   C  1 35  ? 14.709  25.989  -61.361  1.00 39.91  ? 336  CYS   C C   1 
ATOM   7061  O  O   . CYS   C  1 35  ? 15.504  25.262  -60.754  1.00 44.10  ? 336  CYS   C O   1 
ATOM   7062  C  CB  . CYS   C  1 35  ? 14.385  28.044  -59.976  1.00 31.32  ? 336  CYS   C CB  1 
ATOM   7063  S  SG  . CYS   C  1 35  ? 15.372  29.026  -61.146  1.00 36.25  ? 336  CYS   C SG  1 
ATOM   7064  N  N   . MET   C  1 36  ? 14.664  26.083  -62.685  1.00 30.36  ? 337  MET   C N   1 
ATOM   7065  C  CA  . MET   C  1 36  ? 15.584  25.375  -63.564  1.00 35.65  ? 337  MET   C CA  1 
ATOM   7066  C  C   . MET   C  1 36  ? 16.486  26.336  -64.329  1.00 37.49  ? 337  MET   C C   1 
ATOM   7067  O  O   . MET   C  1 36  ? 16.992  26.004  -65.402  1.00 44.33  ? 337  MET   C O   1 
ATOM   7068  C  CB  . MET   C  1 36  ? 14.807  24.471  -64.519  1.00 37.97  ? 337  MET   C CB  1 
ATOM   7069  C  CG  . MET   C  1 36  ? 14.065  23.341  -63.802  1.00 49.82  ? 337  MET   C CG  1 
ATOM   7070  S  SD  . MET   C  1 36  ? 13.479  22.104  -64.959  1.00 63.97  ? 337  MET   C SD  1 
ATOM   7071  C  CE  . MET   C  1 36  ? 12.629  21.001  -63.845  1.00 66.84  ? 337  MET   C CE  1 
ATOM   7072  N  N   . GLY   C  1 37  ? 16.729  27.515  -63.759  1.00 38.26  ? 338  GLY   C N   1 
ATOM   7073  C  CA  . GLY   C  1 37  ? 17.498  28.556  -64.418  1.00 39.82  ? 338  GLY   C CA  1 
ATOM   7074  C  C   . GLY   C  1 37  ? 18.930  28.194  -64.774  1.00 36.36  ? 338  GLY   C C   1 
ATOM   7075  O  O   . GLY   C  1 37  ? 19.543  28.918  -65.566  1.00 36.18  ? 338  GLY   C O   1 
ATOM   7076  N  N   . SER   C  1 38  ? 19.489  27.122  -64.214  1.00 34.81  ? 339  SER   C N   1 
ATOM   7077  C  CA  . SER   C  1 38  ? 20.828  26.683  -64.596  1.00 34.18  ? 339  SER   C CA  1 
ATOM   7078  C  C   . SER   C  1 38  ? 20.813  25.365  -65.365  1.00 40.15  ? 339  SER   C C   1 
ATOM   7079  O  O   . SER   C  1 38  ? 21.871  24.751  -65.548  1.00 44.53  ? 339  SER   C O   1 
ATOM   7080  C  CB  . SER   C  1 38  ? 21.719  26.550  -63.362  1.00 42.08  ? 339  SER   C CB  1 
ATOM   7081  O  OG  . SER   C  1 38  ? 21.385  25.381  -62.623  1.00 35.80  ? 339  SER   C OG  1 
ATOM   7082  N  N   . ILE   C  1 39  ? 19.643  24.895  -65.782  1.00 38.88  ? 340  ILE   C N   1 
ATOM   7083  C  CA  . ILE   C  1 39  ? 19.554  23.758  -66.693  1.00 45.25  ? 340  ILE   C CA  1 
ATOM   7084  C  C   . ILE   C  1 39  ? 19.766  24.258  -68.125  1.00 39.21  ? 340  ILE   C C   1 
ATOM   7085  O  O   . ILE   C  1 39  ? 19.192  25.277  -68.530  1.00 40.24  ? 340  ILE   C O   1 
ATOM   7086  C  CB  . ILE   C  1 39  ? 18.195  23.061  -66.538  1.00 45.90  ? 340  ILE   C CB  1 
ATOM   7087  C  CG1 . ILE   C  1 39  ? 17.974  22.641  -65.090  1.00 46.01  ? 340  ILE   C CG1 1 
ATOM   7088  C  CG2 . ILE   C  1 39  ? 18.116  21.858  -67.461  1.00 45.70  ? 340  ILE   C CG2 1 
ATOM   7089  C  CD1 . ILE   C  1 39  ? 18.892  21.528  -64.666  1.00 46.82  ? 340  ILE   C CD1 1 
ATOM   7090  N  N   . MET   C  1 40  ? 20.585  23.548  -68.907  1.00 43.25  ? 341  MET   C N   1 
ATOM   7091  C  CA  . MET   C  1 40  ? 20.885  24.073  -70.241  1.00 45.38  ? 341  MET   C CA  1 
ATOM   7092  C  C   . MET   C  1 40  ? 19.689  23.946  -71.187  1.00 45.94  ? 341  MET   C C   1 
ATOM   7093  O  O   . MET   C  1 40  ? 19.395  24.879  -71.943  1.00 42.82  ? 341  MET   C O   1 
ATOM   7094  C  CB  . MET   C  1 40  ? 22.106  23.401  -70.850  1.00 52.84  ? 341  MET   C CB  1 
ATOM   7095  C  CG  . MET   C  1 40  ? 22.448  24.065  -72.190  1.00 65.91  ? 341  MET   C CG  1 
ATOM   7096  S  SD  . MET   C  1 40  ? 24.145  23.887  -72.737  1.00 76.97  ? 341  MET   C SD  1 
ATOM   7097  C  CE  . MET   C  1 40  ? 25.034  24.206  -71.196  1.00 64.71  ? 341  MET   C CE  1 
ATOM   7098  N  N   . HIS   C  1 41  ? 18.981  22.810  -71.156  1.00 49.99  ? 342  HIS   C N   1 
ATOM   7099  C  CA  . HIS   C  1 41  ? 17.783  22.580  -71.967  1.00 47.26  ? 342  HIS   C CA  1 
ATOM   7100  C  C   . HIS   C  1 41  ? 16.622  22.252  -71.038  1.00 39.07  ? 342  HIS   C C   1 
ATOM   7101  O  O   . HIS   C  1 41  ? 16.166  21.102  -70.975  1.00 38.19  ? 342  HIS   C O   1 
ATOM   7102  C  CB  . HIS   C  1 41  ? 17.983  21.446  -72.969  1.00 48.20  ? 342  HIS   C CB  1 
ATOM   7103  C  CG  . HIS   C  1 41  ? 19.353  21.393  -73.558  1.00 65.01  ? 342  HIS   C CG  1 
ATOM   7104  N  ND1 . HIS   C  1 41  ? 19.881  22.417  -74.315  1.00 68.94  ? 342  HIS   C ND1 1 
ATOM   7105  C  CD2 . HIS   C  1 41  ? 20.305  20.431  -73.507  1.00 72.13  ? 342  HIS   C CD2 1 
ATOM   7106  C  CE1 . HIS   C  1 41  ? 21.102  22.091  -74.700  1.00 72.06  ? 342  HIS   C CE1 1 
ATOM   7107  N  NE2 . HIS   C  1 41  ? 21.383  20.890  -74.223  1.00 73.31  ? 342  HIS   C NE2 1 
ATOM   7108  N  N   . PRO   C  1 42  ? 16.085  23.240  -70.332  1.00 44.90  ? 343  PRO   C N   1 
ATOM   7109  C  CA  . PRO   C  1 42  ? 15.071  22.909  -69.316  1.00 53.50  ? 343  PRO   C CA  1 
ATOM   7110  C  C   . PRO   C  1 42  ? 13.758  22.421  -69.908  1.00 54.37  ? 343  PRO   C C   1 
ATOM   7111  O  O   . PRO   C  1 42  ? 13.138  21.518  -69.333  1.00 49.40  ? 343  PRO   C O   1 
ATOM   7112  C  CB  . PRO   C  1 42  ? 14.903  24.218  -68.525  1.00 53.56  ? 343  PRO   C CB  1 
ATOM   7113  C  CG  . PRO   C  1 42  ? 15.555  25.319  -69.375  1.00 52.93  ? 343  PRO   C CG  1 
ATOM   7114  C  CD  . PRO   C  1 42  ? 16.181  24.686  -70.603  1.00 45.08  ? 343  PRO   C CD  1 
ATOM   7115  N  N   . SER   C  1 43  ? 13.331  22.945  -71.056  1.00 58.71  ? 344  SER   C N   1 
ATOM   7116  C  CA  . SER   C  1 43  ? 11.992  22.687  -71.564  1.00 57.15  ? 344  SER   C CA  1 
ATOM   7117  C  C   . SER   C  1 43  ? 12.038  21.983  -72.911  1.00 60.85  ? 344  SER   C C   1 
ATOM   7118  O  O   . SER   C  1 43  ? 12.939  22.214  -73.727  1.00 49.74  ? 344  SER   C O   1 
ATOM   7119  C  CB  . SER   C  1 43  ? 11.196  23.989  -71.701  1.00 53.21  ? 344  SER   C CB  1 
ATOM   7120  O  OG  . SER   C  1 43  ? 9.807   23.720  -71.803  1.00 53.22  ? 344  SER   C OG  1 
ATOM   7121  N  N   . GLN   C  1 44  ? 11.043  21.123  -73.133  1.00 67.15  ? 345  GLN   C N   1 
ATOM   7122  C  CA  . GLN   C  1 44  ? 10.770  20.551  -74.445  1.00 74.46  ? 345  GLN   C CA  1 
ATOM   7123  C  C   . GLN   C  1 44  ? 9.483   21.089  -75.061  1.00 71.11  ? 345  GLN   C C   1 
ATOM   7124  O  O   . GLN   C  1 44  ? 9.062   20.596  -76.112  1.00 61.10  ? 345  GLN   C O   1 
ATOM   7125  C  CB  . GLN   C  1 44  ? 10.689  19.030  -74.363  1.00 78.29  ? 345  GLN   C CB  1 
ATOM   7126  C  CG  . GLN   C  1 44  ? 11.861  18.372  -73.692  1.00 79.47  ? 345  GLN   C CG  1 
ATOM   7127  C  CD  . GLN   C  1 44  ? 11.617  16.895  -73.503  1.00 82.91  ? 345  GLN   C CD  1 
ATOM   7128  O  OE1 . GLN   C  1 44  ? 11.288  16.446  -72.404  1.00 86.74  ? 345  GLN   C OE1 1 
ATOM   7129  N  NE2 . GLN   C  1 44  ? 11.755  16.127  -74.583  1.00 80.41  ? 345  GLN   C NE2 1 
ATOM   7130  N  N   . HIS   C  1 45  ? 8.847   22.077  -74.423  1.00 70.83  ? 346  HIS   C N   1 
ATOM   7131  C  CA  . HIS   C  1 45  ? 7.636   22.717  -74.932  1.00 73.24  ? 346  HIS   C CA  1 
ATOM   7132  C  C   . HIS   C  1 45  ? 7.880   23.353  -76.295  1.00 71.57  ? 346  HIS   C C   1 
ATOM   7133  O  O   . HIS   C  1 45  ? 8.536   24.395  -76.383  1.00 60.89  ? 346  HIS   C O   1 
ATOM   7134  C  CB  . HIS   C  1 45  ? 7.141   23.784  -73.949  1.00 69.03  ? 346  HIS   C CB  1 
ATOM   7135  C  CG  . HIS   C  1 45  ? 5.730   24.231  -74.191  1.00 71.71  ? 346  HIS   C CG  1 
ATOM   7136  N  ND1 . HIS   C  1 45  ? 5.221   25.402  -73.670  1.00 72.89  ? 346  HIS   C ND1 1 
ATOM   7137  C  CD2 . HIS   C  1 45  ? 4.717   23.659  -74.884  1.00 72.19  ? 346  HIS   C CD2 1 
ATOM   7138  C  CE1 . HIS   C  1 45  ? 3.957   25.532  -74.033  1.00 73.03  ? 346  HIS   C CE1 1 
ATOM   7139  N  NE2 . HIS   C  1 45  ? 3.627   24.487  -74.771  1.00 71.49  ? 346  HIS   C NE2 1 
ATOM   7140  N  N   . ALA   C  1 46  ? 7.359   22.738  -77.356  1.00 80.65  ? 347  ALA   C N   1 
ATOM   7141  C  CA  . ALA   C  1 46  ? 7.470   23.250  -78.713  1.00 74.76  ? 347  ALA   C CA  1 
ATOM   7142  C  C   . ALA   C  1 46  ? 6.125   23.802  -79.170  1.00 76.25  ? 347  ALA   C C   1 
ATOM   7143  O  O   . ALA   C  1 46  ? 5.065   23.393  -78.684  1.00 74.13  ? 347  ALA   C O   1 
ATOM   7144  C  CB  . ALA   C  1 46  ? 7.954   22.165  -79.682  1.00 71.52  ? 347  ALA   C CB  1 
ATOM   7145  N  N   . ARG   C  1 47  ? 6.174   24.745  -80.108  1.00 80.49  ? 348  ARG   C N   1 
ATOM   7146  C  CA  . ARG   C  1 47  ? 4.951   25.405  -80.548  1.00 82.14  ? 348  ARG   C CA  1 
ATOM   7147  C  C   . ARG   C  1 47  ? 4.149   24.577  -81.557  1.00 85.49  ? 348  ARG   C C   1 
ATOM   7148  O  O   . ARG   C  1 47  ? 2.931   24.763  -81.654  1.00 82.81  ? 348  ARG   C O   1 
ATOM   7149  C  CB  . ARG   C  1 47  ? 5.292   26.789  -81.105  1.00 76.20  ? 348  ARG   C CB  1 
ATOM   7150  C  CG  . ARG   C  1 47  ? 5.353   27.866  -80.025  1.00 71.73  ? 348  ARG   C CG  1 
ATOM   7151  C  CD  . ARG   C  1 47  ? 6.271   29.019  -80.392  1.00 74.23  ? 348  ARG   C CD  1 
ATOM   7152  N  NE  . ARG   C  1 47  ? 5.899   29.640  -81.657  1.00 85.80  ? 348  ARG   C NE  1 
ATOM   7153  C  CZ  . ARG   C  1 47  ? 4.895   30.498  -81.800  1.00 87.85  ? 348  ARG   C CZ  1 
ATOM   7154  N  NH1 . ARG   C  1 47  ? 4.159   30.830  -80.740  1.00 86.22  ? 348  ARG   C NH1 1 
ATOM   7155  N  NH2 . ARG   C  1 47  ? 4.627   31.017  -83.001  1.00 79.40  ? 348  ARG   C NH2 1 
ATOM   7156  N  N   . ARG   C  1 48  ? 4.786   23.652  -82.285  1.00 86.18  ? 349  ARG   C N   1 
ATOM   7157  C  CA  . ARG   C  1 48  ? 4.067   22.736  -83.175  1.00 84.07  ? 349  ARG   C CA  1 
ATOM   7158  C  C   . ARG   C  1 48  ? 4.615   21.320  -83.032  1.00 85.80  ? 349  ARG   C C   1 
ATOM   7159  O  O   . ARG   C  1 48  ? 5.832   21.137  -82.882  1.00 84.90  ? 349  ARG   C O   1 
ATOM   7160  C  CB  . ARG   C  1 48  ? 4.150   23.189  -84.643  1.00 75.38  ? 349  ARG   C CB  1 
ATOM   7161  C  CG  . ARG   C  1 48  ? 5.415   23.955  -84.993  1.00 65.32  ? 349  ARG   C CG  1 
ATOM   7162  C  CD  . ARG   C  1 48  ? 6.312   23.151  -85.904  1.00 68.55  ? 349  ARG   C CD  1 
ATOM   7163  N  NE  . ARG   C  1 48  ? 5.726   22.964  -87.229  1.00 67.87  ? 349  ARG   C NE  1 
ATOM   7164  C  CZ  . ARG   C  1 48  ? 5.051   21.882  -87.600  1.00 83.57  ? 349  ARG   C CZ  1 
ATOM   7165  N  NH1 . ARG   C  1 48  ? 4.870   20.884  -86.743  1.00 90.33  ? 349  ARG   C NH1 1 
ATOM   7166  N  NH2 . ARG   C  1 48  ? 4.557   21.795  -88.829  1.00 89.83  ? 349  ARG   C NH2 1 
ATOM   7167  N  N   . PRO   C  1 49  ? 3.742   20.307  -83.061  1.00 95.71  ? 350  PRO   C N   1 
ATOM   7168  C  CA  . PRO   C  1 49  ? 4.180   18.917  -82.842  1.00 105.59 ? 350  PRO   C CA  1 
ATOM   7169  C  C   . PRO   C  1 49  ? 5.209   18.360  -83.825  1.00 116.83 ? 350  PRO   C C   1 
ATOM   7170  O  O   . PRO   C  1 49  ? 5.781   19.083  -84.648  1.00 117.73 ? 350  PRO   C O   1 
ATOM   7171  C  CB  . PRO   C  1 49  ? 2.864   18.121  -82.923  1.00 105.37 ? 350  PRO   C CB  1 
ATOM   7172  C  CG  . PRO   C  1 49  ? 1.818   19.088  -83.421  1.00 104.55 ? 350  PRO   C CG  1 
ATOM   7173  C  CD  . PRO   C  1 49  ? 2.280   20.438  -82.997  1.00 100.97 ? 350  PRO   C CD  1 
ATOM   7174  N  N   . GLU   C  1 50  ? 5.426   17.043  -83.734  1.00 124.99 ? 351  GLU   C N   1 
ATOM   7175  C  CA  . GLU   C  1 50  ? 6.545   16.336  -84.355  1.00 126.44 ? 351  GLU   C CA  1 
ATOM   7176  C  C   . GLU   C  1 50  ? 6.717   16.623  -85.841  1.00 121.83 ? 351  GLU   C C   1 
ATOM   7177  O  O   . GLU   C  1 50  ? 7.723   17.209  -86.255  1.00 116.84 ? 351  GLU   C O   1 
ATOM   7178  C  CB  . GLU   C  1 50  ? 6.383   14.822  -84.161  1.00 131.62 ? 351  GLU   C CB  1 
ATOM   7179  C  CG  . GLU   C  1 50  ? 6.209   14.380  -82.714  1.00 134.06 ? 351  GLU   C CG  1 
ATOM   7180  C  CD  . GLU   C  1 50  ? 7.060   13.172  -82.360  1.00 135.25 ? 351  GLU   C CD  1 
ATOM   7181  O  OE1 . GLU   C  1 50  ? 7.521   12.471  -83.287  1.00 135.27 ? 351  GLU   C OE1 1 
ATOM   7182  O  OE2 . GLU   C  1 50  ? 7.273   12.930  -81.151  1.00 134.97 ? 351  GLU   C OE2 1 
ATOM   7183  N  N   . ASP   C  1 51  ? 5.747   16.203  -86.650  1.00 121.35 ? 352  ASP   C N   1 
ATOM   7184  C  CA  . ASP   C  1 51  ? 5.874   16.151  -88.093  1.00 122.15 ? 352  ASP   C CA  1 
ATOM   7185  C  C   . ASP   C  1 51  ? 4.993   17.223  -88.739  1.00 122.25 ? 352  ASP   C C   1 
ATOM   7186  O  O   . ASP   C  1 51  ? 4.741   18.275  -88.122  1.00 121.40 ? 352  ASP   C O   1 
ATOM   7187  C  CB  . ASP   C  1 51  ? 5.551   14.737  -88.564  1.00 123.63 ? 352  ASP   C CB  1 
ATOM   7188  C  CG  . ASP   C  1 51  ? 6.791   13.919  -88.844  1.00 122.80 ? 352  ASP   C CG  1 
ATOM   7189  O  OD1 . ASP   C  1 51  ? 7.914   14.431  -88.635  1.00 117.61 ? 352  ASP   C OD1 1 
ATOM   7190  O  OD2 . ASP   C  1 51  ? 6.637   12.760  -89.281  1.00 127.38 ? 352  ASP   C OD2 1 
ATOM   7191  N  N   . VAL   C  1 52  ? 4.533   16.960  -89.965  1.00 121.63 ? 353  VAL   C N   1 
ATOM   7192  C  CA  . VAL   C  1 52  ? 3.745   17.929  -90.720  1.00 117.16 ? 353  VAL   C CA  1 
ATOM   7193  C  C   . VAL   C  1 52  ? 2.431   18.186  -89.992  1.00 112.42 ? 353  VAL   C C   1 
ATOM   7194  O  O   . VAL   C  1 52  ? 1.613   17.275  -89.805  1.00 116.94 ? 353  VAL   C O   1 
ATOM   7195  C  CB  . VAL   C  1 52  ? 3.530   17.440  -92.158  1.00 113.97 ? 353  VAL   C CB  1 
ATOM   7196  C  CG1 . VAL   C  1 52  ? 3.135   15.966  -92.175  1.00 117.88 ? 353  VAL   C CG1 1 
ATOM   7197  C  CG2 . VAL   C  1 52  ? 2.492   18.295  -92.868  1.00 110.43 ? 353  VAL   C CG2 1 
ATOM   7198  N  N   . ALA   C  1 53  ? 2.224   19.437  -89.579  1.00 98.17  ? 354  ALA   C N   1 
ATOM   7199  C  CA  . ALA   C  1 53  ? 1.119   19.795  -88.701  1.00 81.59  ? 354  ALA   C CA  1 
ATOM   7200  C  C   . ALA   C  1 53  ? -0.178  19.967  -89.480  1.00 74.70  ? 354  ALA   C C   1 
ATOM   7201  O  O   . ALA   C  1 53  ? -0.179  20.291  -90.671  1.00 67.80  ? 354  ALA   C O   1 
ATOM   7202  C  CB  . ALA   C  1 53  ? 1.435   21.085  -87.941  1.00 74.61  ? 354  ALA   C CB  1 
ATOM   7203  N  N   . THR   C  1 54  ? -1.292  19.744  -88.787  1.00 71.27  ? 355  THR   C N   1 
ATOM   7204  C  CA  . THR   C  1 54  ? -2.598  20.001  -89.372  1.00 73.00  ? 355  THR   C CA  1 
ATOM   7205  C  C   . THR   C  1 54  ? -2.814  21.508  -89.528  1.00 67.70  ? 355  THR   C C   1 
ATOM   7206  O  O   . THR   C  1 54  ? -2.015  22.330  -89.069  1.00 65.06  ? 355  THR   C O   1 
ATOM   7207  C  CB  . THR   C  1 54  ? -3.701  19.392  -88.505  1.00 72.68  ? 355  THR   C CB  1 
ATOM   7208  O  OG1 . THR   C  1 54  ? -3.560  19.862  -87.157  1.00 72.17  ? 355  THR   C OG1 1 
ATOM   7209  C  CG2 . THR   C  1 54  ? -3.608  17.886  -88.514  1.00 67.34  ? 355  THR   C CG2 1 
ATOM   7210  N  N   . LYS   C  1 55  ? -3.929  21.872  -90.171  1.00 59.91  ? 356  LYS   C N   1 
ATOM   7211  C  CA  . LYS   C  1 55  ? -4.241  23.289  -90.342  1.00 60.41  ? 356  LYS   C CA  1 
ATOM   7212  C  C   . LYS   C  1 55  ? -4.441  23.985  -88.998  1.00 60.64  ? 356  LYS   C C   1 
ATOM   7213  O  O   . LYS   C  1 55  ? -3.881  25.061  -88.761  1.00 45.19  ? 356  LYS   C O   1 
ATOM   7214  C  CB  . LYS   C  1 55  ? -5.480  23.471  -91.212  1.00 68.71  ? 356  LYS   C CB  1 
ATOM   7215  C  CG  . LYS   C  1 55  ? -5.627  24.897  -91.728  1.00 69.17  ? 356  LYS   C CG  1 
ATOM   7216  C  CD  . LYS   C  1 55  ? -5.979  24.892  -93.189  1.00 66.87  ? 356  LYS   C CD  1 
ATOM   7217  C  CE  . LYS   C  1 55  ? -7.475  24.991  -93.400  1.00 70.91  ? 356  LYS   C CE  1 
ATOM   7218  N  NZ  . LYS   C  1 55  ? -7.885  26.389  -93.727  1.00 70.78  ? 356  LYS   C NZ  1 
ATOM   7219  N  N   . ASP   C  1 56  ? -5.251  23.393  -88.109  1.00 54.06  ? 357  ASP   C N   1 
ATOM   7220  C  CA  . ASP   C  1 56  ? -5.529  24.027  -86.824  1.00 63.90  ? 357  ASP   C CA  1 
ATOM   7221  C  C   . ASP   C  1 56  ? -4.304  24.084  -85.931  1.00 57.27  ? 357  ASP   C C   1 
ATOM   7222  O  O   . ASP   C  1 56  ? -4.331  24.804  -84.934  1.00 58.28  ? 357  ASP   C O   1 
ATOM   7223  C  CB  . ASP   C  1 56  ? -6.674  23.318  -86.088  1.00 73.77  ? 357  ASP   C CB  1 
ATOM   7224  C  CG  . ASP   C  1 56  ? -6.331  21.896  -85.676  1.00 83.10  ? 357  ASP   C CG  1 
ATOM   7225  O  OD1 . ASP   C  1 56  ? -5.700  21.168  -86.466  1.00 91.14  ? 357  ASP   C OD1 1 
ATOM   7226  O  OD2 . ASP   C  1 56  ? -6.710  21.498  -84.557  1.00 90.54  ? 357  ASP   C OD2 1 
ATOM   7227  N  N   . GLN   C  1 57  ? -3.238  23.356  -86.271  1.00 53.10  ? 358  GLN   C N   1 
ATOM   7228  C  CA  . GLN   C  1 57  ? -1.974  23.477  -85.561  1.00 54.73  ? 358  GLN   C CA  1 
ATOM   7229  C  C   . GLN   C  1 57  ? -1.132  24.621  -86.103  1.00 60.41  ? 358  GLN   C C   1 
ATOM   7230  O  O   . GLN   C  1 57  ? -0.668  25.478  -85.341  1.00 64.71  ? 358  GLN   C O   1 
ATOM   7231  C  CB  . GLN   C  1 57  ? -1.202  22.160  -85.642  1.00 60.95  ? 358  GLN   C CB  1 
ATOM   7232  C  CG  . GLN   C  1 57  ? -1.624  21.144  -84.596  1.00 70.82  ? 358  GLN   C CG  1 
ATOM   7233  C  CD  . GLN   C  1 57  ? -1.240  19.733  -84.974  1.00 76.56  ? 358  GLN   C CD  1 
ATOM   7234  O  OE1 . GLN   C  1 57  ? -0.351  19.518  -85.800  1.00 75.48  ? 358  GLN   C OE1 1 
ATOM   7235  N  NE2 . GLN   C  1 57  ? -1.917  18.759  -84.379  1.00 77.13  ? 358  GLN   C NE2 1 
ATOM   7236  N  N   . LEU   C  1 58  ? -0.923  24.656  -87.416  1.00 66.57  ? 359  LEU   C N   1 
ATOM   7237  C  CA  . LEU   C  1 58  ? 0.014   25.626  -87.967  1.00 62.16  ? 359  LEU   C CA  1 
ATOM   7238  C  C   . LEU   C  1 58  ? -0.604  27.013  -88.133  1.00 57.37  ? 359  LEU   C C   1 
ATOM   7239  O  O   . LEU   C  1 58  ? 0.081   28.020  -87.921  1.00 51.65  ? 359  LEU   C O   1 
ATOM   7240  C  CB  . LEU   C  1 58  ? 0.560   25.132  -89.303  1.00 56.50  ? 359  LEU   C CB  1 
ATOM   7241  C  CG  . LEU   C  1 58  ? 1.574   26.111  -89.890  1.00 50.47  ? 359  LEU   C CG  1 
ATOM   7242  C  CD1 . LEU   C  1 58  ? 2.751   26.222  -88.924  1.00 37.66  ? 359  LEU   C CD1 1 
ATOM   7243  C  CD2 . LEU   C  1 58  ? 2.022   25.756  -91.340  1.00 44.62  ? 359  LEU   C CD2 1 
ATOM   7244  N  N   . PHE   C  1 59  ? -1.878  27.101  -88.522  1.00 57.56  ? 360  PHE   C N   1 
ATOM   7245  C  CA  . PHE   C  1 59  ? -2.446  28.422  -88.784  1.00 53.53  ? 360  PHE   C CA  1 
ATOM   7246  C  C   . PHE   C  1 59  ? -2.438  29.342  -87.572  1.00 52.24  ? 360  PHE   C C   1 
ATOM   7247  O  O   . PHE   C  1 59  ? -2.099  30.528  -87.738  1.00 51.16  ? 360  PHE   C O   1 
ATOM   7248  C  CB  . PHE   C  1 59  ? -3.868  28.323  -89.335  1.00 44.45  ? 360  PHE   C CB  1 
ATOM   7249  C  CG  . PHE   C  1 59  ? -4.430  29.666  -89.725  1.00 58.40  ? 360  PHE   C CG  1 
ATOM   7250  C  CD1 . PHE   C  1 59  ? -4.100  30.237  -90.955  1.00 57.69  ? 360  PHE   C CD1 1 
ATOM   7251  C  CD2 . PHE   C  1 59  ? -5.242  30.383  -88.849  1.00 56.27  ? 360  PHE   C CD2 1 
ATOM   7252  C  CE1 . PHE   C  1 59  ? -4.599  31.474  -91.321  1.00 58.91  ? 360  PHE   C CE1 1 
ATOM   7253  C  CE2 . PHE   C  1 59  ? -5.736  31.627  -89.201  1.00 60.95  ? 360  PHE   C CE2 1 
ATOM   7254  C  CZ  . PHE   C  1 59  ? -5.415  32.174  -90.443  1.00 63.97  ? 360  PHE   C CZ  1 
ATOM   7255  N  N   . PRO   C  1 60  ? -2.834  28.903  -86.364  1.00 53.19  ? 361  PRO   C N   1 
ATOM   7256  C  CA  . PRO   C  1 60  ? -2.816  29.829  -85.215  1.00 43.17  ? 361  PRO   C CA  1 
ATOM   7257  C  C   . PRO   C  1 60  ? -1.463  30.467  -84.987  1.00 47.51  ? 361  PRO   C C   1 
ATOM   7258  O  O   . PRO   C  1 60  ? -1.388  31.653  -84.629  1.00 50.71  ? 361  PRO   C O   1 
ATOM   7259  C  CB  . PRO   C  1 60  ? -3.237  28.925  -84.051  1.00 52.47  ? 361  PRO   C CB  1 
ATOM   7260  C  CG  . PRO   C  1 60  ? -4.143  27.928  -84.683  1.00 54.30  ? 361  PRO   C CG  1 
ATOM   7261  C  CD  . PRO   C  1 60  ? -3.488  27.627  -86.014  1.00 52.65  ? 361  PRO   C CD  1 
ATOM   7262  N  N   . LEU   C  1 61  ? -0.385  29.707  -85.213  1.00 45.63  ? 362  LEU   C N   1 
ATOM   7263  C  CA  . LEU   C  1 61  ? 0.962   30.263  -85.120  1.00 36.88  ? 362  LEU   C CA  1 
ATOM   7264  C  C   . LEU   C  1 61  ? 1.229   31.272  -86.241  1.00 43.22  ? 362  LEU   C C   1 
ATOM   7265  O  O   . LEU   C  1 61  ? 1.816   32.333  -86.000  1.00 35.85  ? 362  LEU   C O   1 
ATOM   7266  C  CB  . LEU   C  1 61  ? 1.987   29.126  -85.146  1.00 36.15  ? 362  LEU   C CB  1 
ATOM   7267  C  CG  . LEU   C  1 61  ? 1.775   28.066  -84.059  1.00 45.66  ? 362  LEU   C CG  1 
ATOM   7268  C  CD1 . LEU   C  1 61  ? 2.664   26.870  -84.256  1.00 39.61  ? 362  LEU   C CD1 1 
ATOM   7269  C  CD2 . LEU   C  1 61  ? 2.017   28.686  -82.688  1.00 42.81  ? 362  LEU   C CD2 1 
ATOM   7270  N  N   . ALA   C  1 62  ? 0.807   30.960  -87.473  1.00 46.29  ? 363  ALA   C N   1 
ATOM   7271  C  CA  . ALA   C  1 62  ? 0.989   31.906  -88.571  1.00 47.33  ? 363  ALA   C CA  1 
ATOM   7272  C  C   . ALA   C  1 62  ? 0.254   33.209  -88.288  1.00 48.30  ? 363  ALA   C C   1 
ATOM   7273  O  O   . ALA   C  1 62  ? 0.836   34.299  -88.372  1.00 40.65  ? 363  ALA   C O   1 
ATOM   7274  C  CB  . ALA   C  1 62  ? 0.507   31.285  -89.884  1.00 49.33  ? 363  ALA   C CB  1 
ATOM   7275  N  N   . LYS   C  1 63  ? -1.030  33.106  -87.924  1.00 50.22  ? 364  LYS   C N   1 
ATOM   7276  C  CA  . LYS   C  1 63  ? -1.811  34.290  -87.588  1.00 54.32  ? 364  LYS   C CA  1 
ATOM   7277  C  C   . LYS   C  1 63  ? -1.132  35.114  -86.503  1.00 58.02  ? 364  LYS   C C   1 
ATOM   7278  O  O   . LYS   C  1 63  ? -1.116  36.348  -86.566  1.00 57.28  ? 364  LYS   C O   1 
ATOM   7279  C  CB  . LYS   C  1 63  ? -3.215  33.880  -87.145  1.00 61.03  ? 364  LYS   C CB  1 
ATOM   7280  C  CG  . LYS   C  1 63  ? -4.154  35.054  -86.947  1.00 66.05  ? 364  LYS   C CG  1 
ATOM   7281  C  CD  . LYS   C  1 63  ? -5.348  34.680  -86.100  1.00 69.27  ? 364  LYS   C CD  1 
ATOM   7282  C  CE  . LYS   C  1 63  ? -6.328  35.835  -86.007  1.00 64.23  ? 364  LYS   C CE  1 
ATOM   7283  N  NZ  . LYS   C  1 63  ? -5.660  37.091  -85.575  1.00 56.06  ? 364  LYS   C NZ  1 
ATOM   7284  N  N   . GLU   C  1 64  ? -0.555  34.446  -85.505  1.00 56.68  ? 365  GLU   C N   1 
ATOM   7285  C  CA  . GLU   C  1 64  ? 0.141   35.158  -84.436  1.00 60.71  ? 365  GLU   C CA  1 
ATOM   7286  C  C   . GLU   C  1 64  ? 1.305   35.991  -84.982  1.00 47.83  ? 365  GLU   C C   1 
ATOM   7287  O  O   . GLU   C  1 64  ? 1.446   37.176  -84.657  1.00 39.89  ? 365  GLU   C O   1 
ATOM   7288  C  CB  . GLU   C  1 64  ? 0.625   34.150  -83.391  1.00 64.77  ? 365  GLU   C CB  1 
ATOM   7289  C  CG  . GLU   C  1 64  ? 1.498   34.714  -82.278  1.00 77.99  ? 365  GLU   C CG  1 
ATOM   7290  C  CD  . GLU   C  1 64  ? 2.018   33.605  -81.364  1.00 92.63  ? 365  GLU   C CD  1 
ATOM   7291  O  OE1 . GLU   C  1 64  ? 1.671   33.589  -80.155  1.00 95.34  ? 365  GLU   C OE1 1 
ATOM   7292  O  OE2 . GLU   C  1 64  ? 2.750   32.727  -81.878  1.00 96.09  ? 365  GLU   C OE2 1 
ATOM   7293  N  N   . PHE   C  1 65  ? 2.142   35.396  -85.829  1.00 48.90  ? 366  PHE   C N   1 
ATOM   7294  C  CA  . PHE   C  1 65  ? 3.313   36.118  -86.312  1.00 48.39  ? 366  PHE   C CA  1 
ATOM   7295  C  C   . PHE   C  1 65  ? 2.925   37.264  -87.246  1.00 48.90  ? 366  PHE   C C   1 
ATOM   7296  O  O   . PHE   C  1 65  ? 3.463   38.373  -87.137  1.00 44.55  ? 366  PHE   C O   1 
ATOM   7297  C  CB  . PHE   C  1 65  ? 4.268   35.162  -87.010  1.00 48.66  ? 366  PHE   C CB  1 
ATOM   7298  C  CG  . PHE   C  1 65  ? 5.389   35.857  -87.687  1.00 54.69  ? 366  PHE   C CG  1 
ATOM   7299  C  CD1 . PHE   C  1 65  ? 6.366   36.507  -86.939  1.00 48.81  ? 366  PHE   C CD1 1 
ATOM   7300  C  CD2 . PHE   C  1 65  ? 5.449   35.907  -89.072  1.00 48.58  ? 366  PHE   C CD2 1 
ATOM   7301  C  CE1 . PHE   C  1 65  ? 7.393   37.172  -87.563  1.00 50.06  ? 366  PHE   C CE1 1 
ATOM   7302  C  CE2 . PHE   C  1 65  ? 6.477   36.567  -89.705  1.00 48.94  ? 366  PHE   C CE2 1 
ATOM   7303  C  CZ  . PHE   C  1 65  ? 7.449   37.202  -88.963  1.00 50.03  ? 366  PHE   C CZ  1 
ATOM   7304  N  N   . ILE   C  1 66  ? 1.997   37.009  -88.174  1.00 48.70  ? 367  ILE   C N   1 
ATOM   7305  C  CA  . ILE   C  1 66  ? 1.580   38.039  -89.126  1.00 52.86  ? 367  ILE   C CA  1 
ATOM   7306  C  C   . ILE   C  1 66  ? 0.931   39.205  -88.390  1.00 53.65  ? 367  ILE   C C   1 
ATOM   7307  O  O   . ILE   C  1 66  ? 1.169   40.376  -88.716  1.00 43.11  ? 367  ILE   C O   1 
ATOM   7308  C  CB  . ILE   C  1 66  ? 0.631   37.429  -90.179  1.00 53.86  ? 367  ILE   C CB  1 
ATOM   7309  C  CG1 . ILE   C  1 66  ? 1.303   36.261  -90.911  1.00 47.66  ? 367  ILE   C CG1 1 
ATOM   7310  C  CG2 . ILE   C  1 66  ? 0.114   38.493  -91.142  1.00 56.23  ? 367  ILE   C CG2 1 
ATOM   7311  C  CD1 . ILE   C  1 66  ? 2.456   36.659  -91.812  1.00 50.16  ? 367  ILE   C CD1 1 
ATOM   7312  N  N   . ASP   C  1 67  ? 0.102   38.898  -87.384  1.00 57.35  ? 368  ASP   C N   1 
ATOM   7313  C  CA  . ASP   C  1 67  ? -0.496  39.932  -86.542  1.00 59.42  ? 368  ASP   C CA  1 
ATOM   7314  C  C   . ASP   C  1 67  ? 0.582   40.773  -85.868  1.00 56.04  ? 368  ASP   C C   1 
ATOM   7315  O  O   . ASP   C  1 67  ? 0.557   42.010  -85.927  1.00 47.09  ? 368  ASP   C O   1 
ATOM   7316  C  CB  . ASP   C  1 67  ? -1.403  39.291  -85.487  1.00 60.79  ? 368  ASP   C CB  1 
ATOM   7317  C  CG  . ASP   C  1 67  ? -2.721  38.786  -86.057  1.00 66.33  ? 368  ASP   C CG  1 
ATOM   7318  O  OD1 . ASP   C  1 67  ? -3.048  39.092  -87.225  1.00 71.30  ? 368  ASP   C OD1 1 
ATOM   7319  O  OD2 . ASP   C  1 67  ? -3.441  38.076  -85.326  1.00 70.61  ? 368  ASP   C OD2 1 
ATOM   7320  N  N   . GLN   C  1 68  ? 1.541   40.104  -85.224  1.00 36.31  ? 369  GLN   C N   1 
ATOM   7321  C  CA  . GLN   C  1 68  ? 2.694   40.782  -84.643  1.00 42.09  ? 369  GLN   C CA  1 
ATOM   7322  C  C   . GLN   C  1 68  ? 3.410   41.653  -85.670  1.00 49.76  ? 369  GLN   C C   1 
ATOM   7323  O  O   . GLN   C  1 68  ? 3.596   42.857  -85.459  1.00 47.00  ? 369  GLN   C O   1 
ATOM   7324  C  CB  . GLN   C  1 68  ? 3.640   39.734  -84.043  1.00 49.77  ? 369  GLN   C CB  1 
ATOM   7325  C  CG  . GLN   C  1 68  ? 4.949   40.258  -83.439  1.00 55.06  ? 369  GLN   C CG  1 
ATOM   7326  C  CD  . GLN   C  1 68  ? 5.857   39.125  -82.932  1.00 63.68  ? 369  GLN   C CD  1 
ATOM   7327  O  OE1 . GLN   C  1 68  ? 5.379   38.083  -82.479  1.00 70.41  ? 369  GLN   C OE1 1 
ATOM   7328  N  NE2 . GLN   C  1 68  ? 7.168   39.330  -83.017  1.00 64.10  ? 369  GLN   C NE2 1 
ATOM   7329  N  N   . TYR   C  1 69  ? 3.793   41.064  -86.807  1.00 50.63  ? 370  TYR   C N   1 
ATOM   7330  C  CA  . TYR   C  1 69  ? 4.550   41.816  -87.808  1.00 50.69  ? 370  TYR   C CA  1 
ATOM   7331  C  C   . TYR   C  1 69  ? 3.765   43.015  -88.322  1.00 44.95  ? 370  TYR   C C   1 
ATOM   7332  O  O   . TYR   C  1 69  ? 4.314   44.118  -88.462  1.00 45.64  ? 370  TYR   C O   1 
ATOM   7333  C  CB  . TYR   C  1 69  ? 4.944   40.927  -88.990  1.00 49.44  ? 370  TYR   C CB  1 
ATOM   7334  C  CG  . TYR   C  1 69  ? 5.417   41.753  -90.162  1.00 42.87  ? 370  TYR   C CG  1 
ATOM   7335  C  CD1 . TYR   C  1 69  ? 6.673   42.342  -90.151  1.00 44.92  ? 370  TYR   C CD1 1 
ATOM   7336  C  CD2 . TYR   C  1 69  ? 4.588   41.990  -91.256  1.00 43.79  ? 370  TYR   C CD2 1 
ATOM   7337  C  CE1 . TYR   C  1 69  ? 7.102   43.124  -91.217  1.00 47.36  ? 370  TYR   C CE1 1 
ATOM   7338  C  CE2 . TYR   C  1 69  ? 5.015   42.763  -92.327  1.00 52.23  ? 370  TYR   C CE2 1 
ATOM   7339  C  CZ  . TYR   C  1 69  ? 6.271   43.323  -92.300  1.00 52.21  ? 370  TYR   C CZ  1 
ATOM   7340  O  OH  . TYR   C  1 69  ? 6.692   44.097  -93.351  1.00 51.48  ? 370  TYR   C OH  1 
ATOM   7341  N  N   . TYR   C  1 70  ? 2.485   42.816  -88.640  1.00 38.11  ? 371  TYR   C N   1 
ATOM   7342  C  CA  . TYR   C  1 70  ? 1.708   43.944  -89.124  1.00 45.23  ? 371  TYR   C CA  1 
ATOM   7343  C  C   . TYR   C  1 70  ? 1.463   44.959  -88.022  1.00 52.53  ? 371  TYR   C C   1 
ATOM   7344  O  O   . TYR   C  1 70  ? 1.424   46.159  -88.303  1.00 40.59  ? 371  TYR   C O   1 
ATOM   7345  C  CB  . TYR   C  1 70  ? 0.405   43.468  -89.764  1.00 51.05  ? 371  TYR   C CB  1 
ATOM   7346  C  CG  . TYR   C  1 70  ? 0.597   43.226  -91.244  1.00 52.38  ? 371  TYR   C CG  1 
ATOM   7347  C  CD1 . TYR   C  1 70  ? 0.433   44.263  -92.160  1.00 46.70  ? 371  TYR   C CD1 1 
ATOM   7348  C  CD2 . TYR   C  1 70  ? 0.997   41.983  -91.724  1.00 54.02  ? 371  TYR   C CD2 1 
ATOM   7349  C  CE1 . TYR   C  1 70  ? 0.637   44.065  -93.511  1.00 47.61  ? 371  TYR   C CE1 1 
ATOM   7350  C  CE2 . TYR   C  1 70  ? 1.195   41.773  -93.098  1.00 56.14  ? 371  TYR   C CE2 1 
ATOM   7351  C  CZ  . TYR   C  1 70  ? 1.014   42.826  -93.978  1.00 51.25  ? 371  TYR   C CZ  1 
ATOM   7352  O  OH  . TYR   C  1 70  ? 1.209   42.651  -95.323  1.00 55.18  ? 371  TYR   C OH  1 
ATOM   7353  N  N   . SER   C  1 71  ? 1.335   44.510  -86.763  1.00 54.55  ? 372  SER   C N   1 
ATOM   7354  C  CA  . SER   C  1 71  ? 1.306   45.463  -85.658  1.00 55.28  ? 372  SER   C CA  1 
ATOM   7355  C  C   . SER   C  1 71  ? 2.612   46.244  -85.586  1.00 49.83  ? 372  SER   C C   1 
ATOM   7356  O  O   . SER   C  1 71  ? 2.602   47.472  -85.451  1.00 55.88  ? 372  SER   C O   1 
ATOM   7357  C  CB  . SER   C  1 71  ? 1.033   44.747  -84.333  1.00 65.45  ? 372  SER   C CB  1 
ATOM   7358  O  OG  . SER   C  1 71  ? -0.282  44.215  -84.303  1.00 74.47  ? 372  SER   C OG  1 
ATOM   7359  N  N   . SER   C  1 72  ? 3.745   45.552  -85.732  1.00 40.68  ? 373  SER   C N   1 
ATOM   7360  C  CA  . SER   C  1 72  ? 5.049   46.205  -85.666  1.00 40.62  ? 373  SER   C CA  1 
ATOM   7361  C  C   . SER   C  1 72  ? 5.177   47.381  -86.635  1.00 49.25  ? 373  SER   C C   1 
ATOM   7362  O  O   . SER   C  1 72  ? 5.925   48.325  -86.350  1.00 51.37  ? 373  SER   C O   1 
ATOM   7363  C  CB  . SER   C  1 72  ? 6.154   45.187  -85.941  1.00 41.39  ? 373  SER   C CB  1 
ATOM   7364  O  OG  . SER   C  1 72  ? 6.645   45.332  -87.261  1.00 55.44  ? 373  SER   C OG  1 
ATOM   7365  N  N   . ILE   C  1 73  ? 4.474   47.354  -87.773  1.00 42.55  ? 374  ILE   C N   1 
ATOM   7366  C  CA  . ILE   C  1 73  ? 4.636   48.395  -88.790  1.00 45.33  ? 374  ILE   C CA  1 
ATOM   7367  C  C   . ILE   C  1 73  ? 3.425   49.330  -88.847  1.00 45.39  ? 374  ILE   C C   1 
ATOM   7368  O  O   . ILE   C  1 73  ? 3.201   49.992  -89.862  1.00 54.46  ? 374  ILE   C O   1 
ATOM   7369  C  CB  . ILE   C  1 73  ? 4.953   47.803  -90.180  1.00 43.07  ? 374  ILE   C CB  1 
ATOM   7370  C  CG1 . ILE   C  1 73  ? 3.778   46.974  -90.720  1.00 45.18  ? 374  ILE   C CG1 1 
ATOM   7371  C  CG2 . ILE   C  1 73  ? 6.215   46.971  -90.124  1.00 39.44  ? 374  ILE   C CG2 1 
ATOM   7372  C  CD1 . ILE   C  1 73  ? 3.958   46.479  -92.171  1.00 45.66  ? 374  ILE   C CD1 1 
ATOM   7373  N  N   . LYS   C  1 74  ? 2.651   49.414  -87.769  1.00 50.52  ? 375  LYS   C N   1 
ATOM   7374  C  CA  . LYS   C  1 74  ? 1.540   50.358  -87.652  1.00 61.44  ? 375  LYS   C CA  1 
ATOM   7375  C  C   . LYS   C  1 74  ? 0.464   50.112  -88.709  1.00 64.81  ? 375  LYS   C C   1 
ATOM   7376  O  O   . LYS   C  1 74  ? -0.224  51.044  -89.143  1.00 60.84  ? 375  LYS   C O   1 
ATOM   7377  C  CB  . LYS   C  1 74  ? 2.035   51.810  -87.716  1.00 68.83  ? 375  LYS   C CB  1 
ATOM   7378  C  CG  . LYS   C  1 74  ? 3.234   52.096  -86.823  1.00 73.76  ? 375  LYS   C CG  1 
ATOM   7379  C  CD  . LYS   C  1 74  ? 2.860   53.000  -85.652  1.00 78.33  ? 375  LYS   C CD  1 
ATOM   7380  C  CE  . LYS   C  1 74  ? 3.987   53.103  -84.631  1.00 72.99  ? 375  LYS   C CE  1 
ATOM   7381  N  NZ  . LYS   C  1 74  ? 4.334   51.781  -84.029  1.00 65.92  ? 375  LYS   C NZ  1 
ATOM   7382  N  N   . ARG   C  1 75  ? 0.320   48.866  -89.148  1.00 65.52  ? 376  ARG   C N   1 
ATOM   7383  C  CA  . ARG   C  1 75  ? -0.814  48.474  -89.968  1.00 69.31  ? 376  ARG   C CA  1 
ATOM   7384  C  C   . ARG   C  1 75  ? -1.803  47.733  -89.083  1.00 84.43  ? 376  ARG   C C   1 
ATOM   7385  O  O   . ARG   C  1 75  ? -2.383  48.337  -88.174  1.00 93.20  ? 376  ARG   C O   1 
ATOM   7386  C  CB  . ARG   C  1 75  ? -0.344  47.638  -91.153  1.00 67.25  ? 376  ARG   C CB  1 
ATOM   7387  C  CG  . ARG   C  1 75  ? 0.517   48.457  -92.115  1.00 63.08  ? 376  ARG   C CG  1 
ATOM   7388  C  CD  . ARG   C  1 75  ? -0.331  49.562  -92.740  1.00 85.15  ? 376  ARG   C CD  1 
ATOM   7389  N  NE  . ARG   C  1 75  ? 0.441   50.660  -93.321  1.00 94.63  ? 376  ARG   C NE  1 
ATOM   7390  C  CZ  . ARG   C  1 75  ? 0.847   51.727  -92.635  1.00 94.41  ? 376  ARG   C CZ  1 
ATOM   7391  N  NH1 . ARG   C  1 75  ? 1.536   52.687  -93.237  1.00 87.21  ? 376  ARG   C NH1 1 
ATOM   7392  N  NH2 . ARG   C  1 75  ? 0.570   51.829  -91.342  1.00 98.83  ? 376  ARG   C NH2 1 
ATOM   7393  N  N   . PHE   C  1 76  ? -1.973  46.431  -89.308  1.00 83.80  ? 377  PHE   C N   1 
ATOM   7394  C  CA  . PHE   C  1 76  ? -2.886  45.595  -88.527  1.00 84.39  ? 377  PHE   C CA  1 
ATOM   7395  C  C   . PHE   C  1 76  ? -4.345  45.950  -88.792  1.00 81.00  ? 377  PHE   C C   1 
ATOM   7396  O  O   . PHE   C  1 76  ? -4.808  47.059  -88.490  1.00 70.16  ? 377  PHE   C O   1 
ATOM   7397  C  CB  . PHE   C  1 76  ? -2.612  45.663  -87.016  1.00 87.57  ? 377  PHE   C CB  1 
ATOM   7398  C  CG  . PHE   C  1 76  ? -3.583  44.844  -86.198  1.00 88.87  ? 377  PHE   C CG  1 
ATOM   7399  C  CD1 . PHE   C  1 76  ? -3.360  43.491  -85.975  1.00 85.99  ? 377  PHE   C CD1 1 
ATOM   7400  C  CD2 . PHE   C  1 76  ? -4.735  45.415  -85.686  1.00 90.98  ? 377  PHE   C CD2 1 
ATOM   7401  C  CE1 . PHE   C  1 76  ? -4.263  42.730  -85.249  1.00 82.49  ? 377  PHE   C CE1 1 
ATOM   7402  C  CE2 . PHE   C  1 76  ? -5.642  44.659  -84.965  1.00 90.52  ? 377  PHE   C CE2 1 
ATOM   7403  C  CZ  . PHE   C  1 76  ? -5.404  43.316  -84.745  1.00 87.18  ? 377  PHE   C CZ  1 
ATOM   7404  N  N   . GLY   C  1 77  ? -5.093  44.980  -89.309  1.00 76.43  ? 378  GLY   C N   1 
ATOM   7405  C  CA  . GLY   C  1 77  ? -6.401  45.242  -89.846  1.00 70.49  ? 378  GLY   C CA  1 
ATOM   7406  C  C   . GLY   C  1 77  ? -6.374  45.901  -91.202  1.00 65.63  ? 378  GLY   C C   1 
ATOM   7407  O  O   . GLY   C  1 77  ? -7.421  45.965  -91.860  1.00 70.70  ? 378  GLY   C O   1 
ATOM   7408  N  N   . SER   C  1 78  ? -5.209  46.387  -91.637  1.00 60.63  ? 379  SER   C N   1 
ATOM   7409  C  CA  . SER   C  1 78  ? -5.074  47.043  -92.925  1.00 62.17  ? 379  SER   C CA  1 
ATOM   7410  C  C   . SER   C  1 78  ? -5.423  46.074  -94.043  1.00 65.32  ? 379  SER   C C   1 
ATOM   7411  O  O   . SER   C  1 78  ? -5.476  44.854  -93.859  1.00 64.52  ? 379  SER   C O   1 
ATOM   7412  C  CB  . SER   C  1 78  ? -3.653  47.580  -93.123  1.00 50.26  ? 379  SER   C CB  1 
ATOM   7413  O  OG  . SER   C  1 78  ? -2.712  46.540  -93.336  1.00 48.00  ? 379  SER   C OG  1 
ATOM   7414  N  N   . LYS   C  1 79  ? -5.684  46.644  -95.215  1.00 64.67  ? 380  LYS   C N   1 
ATOM   7415  C  CA  . LYS   C  1 79  ? -5.928  45.823  -96.389  1.00 69.44  ? 380  LYS   C CA  1 
ATOM   7416  C  C   . LYS   C  1 79  ? -4.876  44.721  -96.503  1.00 66.76  ? 380  LYS   C C   1 
ATOM   7417  O  O   . LYS   C  1 79  ? -5.212  43.536  -96.585  1.00 69.81  ? 380  LYS   C O   1 
ATOM   7418  C  CB  . LYS   C  1 79  ? -5.955  46.716  -97.633  1.00 69.44  ? 380  LYS   C CB  1 
ATOM   7419  C  CG  . LYS   C  1 79  ? -6.885  46.232  -98.728  1.00 81.52  ? 380  LYS   C CG  1 
ATOM   7420  C  CD  . LYS   C  1 79  ? -7.739  47.372  -99.286  1.00 87.64  ? 380  LYS   C CD  1 
ATOM   7421  C  CE  . LYS   C  1 79  ? -8.974  47.614  -98.420  1.00 91.02  ? 380  LYS   C CE  1 
ATOM   7422  N  NZ  . LYS   C  1 79  ? -10.042 46.581  -98.602  1.00 87.50  ? 380  LYS   C NZ  1 
ATOM   7423  N  N   . ALA   C  1 80  ? -3.592  45.090  -96.429  1.00 61.40  ? 381  ALA   C N   1 
ATOM   7424  C  CA  . ALA   C  1 80  ? -2.531  44.120  -96.683  1.00 57.25  ? 381  ALA   C CA  1 
ATOM   7425  C  C   . ALA   C  1 80  ? -2.494  43.033  -95.614  1.00 56.56  ? 381  ALA   C C   1 
ATOM   7426  O  O   . ALA   C  1 80  ? -2.185  41.872  -95.909  1.00 51.05  ? 381  ALA   C O   1 
ATOM   7427  C  CB  . ALA   C  1 80  ? -1.182  44.833  -96.774  1.00 53.90  ? 381  ALA   C CB  1 
ATOM   7428  N  N   . HIS   C  1 81  ? -2.807  43.386  -94.369  1.00 57.35  ? 382  HIS   C N   1 
ATOM   7429  C  CA  . HIS   C  1 81  ? -2.812  42.393  -93.297  1.00 60.79  ? 382  HIS   C CA  1 
ATOM   7430  C  C   . HIS   C  1 81  ? -3.908  41.351  -93.518  1.00 64.75  ? 382  HIS   C C   1 
ATOM   7431  O  O   . HIS   C  1 81  ? -3.647  40.142  -93.474  1.00 63.60  ? 382  HIS   C O   1 
ATOM   7432  C  CB  . HIS   C  1 81  ? -2.985  43.096  -91.950  1.00 62.74  ? 382  HIS   C CB  1 
ATOM   7433  C  CG  . HIS   C  1 81  ? -2.931  42.176  -90.772  1.00 73.68  ? 382  HIS   C CG  1 
ATOM   7434  N  ND1 . HIS   C  1 81  ? -3.221  42.597  -89.494  1.00 76.62  ? 382  HIS   C ND1 1 
ATOM   7435  C  CD2 . HIS   C  1 81  ? -2.611  40.863  -90.672  1.00 75.72  ? 382  HIS   C CD2 1 
ATOM   7436  C  CE1 . HIS   C  1 81  ? -3.088  41.585  -88.656  1.00 75.63  ? 382  HIS   C CE1 1 
ATOM   7437  N  NE2 . HIS   C  1 81  ? -2.717  40.521  -89.345  1.00 74.47  ? 382  HIS   C NE2 1 
ATOM   7438  N  N   . MET   C  1 82  ? -5.145  41.806  -93.770  1.00 61.74  ? 383  MET   C N   1 
ATOM   7439  C  CA  . MET   C  1 82  ? -6.252  40.879  -93.998  1.00 59.28  ? 383  MET   C CA  1 
ATOM   7440  C  C   . MET   C  1 82  ? -6.028  40.044  -95.246  1.00 60.37  ? 383  MET   C C   1 
ATOM   7441  O  O   . MET   C  1 82  ? -6.437  38.877  -95.298  1.00 59.13  ? 383  MET   C O   1 
ATOM   7442  C  CB  . MET   C  1 82  ? -7.574  41.638  -94.111  1.00 56.75  ? 383  MET   C CB  1 
ATOM   7443  C  CG  . MET   C  1 82  ? -7.990  42.353  -92.866  1.00 60.24  ? 383  MET   C CG  1 
ATOM   7444  S  SD  . MET   C  1 82  ? -7.560  41.320  -91.470  1.00 70.00  ? 383  MET   C SD  1 
ATOM   7445  C  CE  . MET   C  1 82  ? -8.290  42.232  -90.114  1.00 87.14  ? 383  MET   C CE  1 
ATOM   7446  N  N   . GLU   C  1 83  ? -5.393  40.632  -96.260  1.00 63.06  ? 384  GLU   C N   1 
ATOM   7447  C  CA  . GLU   C  1 83  ? -5.022  39.886  -97.455  1.00 58.89  ? 384  GLU   C CA  1 
ATOM   7448  C  C   . GLU   C  1 83  ? -3.989  38.828  -97.116  1.00 55.14  ? 384  GLU   C C   1 
ATOM   7449  O  O   . GLU   C  1 83  ? -4.137  37.653  -97.471  1.00 57.09  ? 384  GLU   C O   1 
ATOM   7450  C  CB  . GLU   C  1 83  ? -4.469  40.843  -98.512  1.00 62.85  ? 384  GLU   C CB  1 
ATOM   7451  C  CG  . GLU   C  1 83  ? -5.270  40.949  -99.772  1.00 72.90  ? 384  GLU   C CG  1 
ATOM   7452  C  CD  . GLU   C  1 83  ? -5.356  42.381  -100.256 1.00 84.21  ? 384  GLU   C CD  1 
ATOM   7453  O  OE1 . GLU   C  1 83  ? -4.366  43.126  -100.097 1.00 85.22  ? 384  GLU   C OE1 1 
ATOM   7454  O  OE2 . GLU   C  1 83  ? -6.424  42.770  -100.774 1.00 90.67  ? 384  GLU   C OE2 1 
ATOM   7455  N  N   . ARG   C  1 84  ? -2.930  39.239  -96.420  1.00 54.21  ? 385  ARG   C N   1 
ATOM   7456  C  CA  . ARG   C  1 84  ? -1.878  38.310  -96.035  1.00 51.33  ? 385  ARG   C CA  1 
ATOM   7457  C  C   . ARG   C  1 84  ? -2.438  37.159  -95.205  1.00 56.58  ? 385  ARG   C C   1 
ATOM   7458  O  O   . ARG   C  1 84  ? -2.021  36.005  -95.364  1.00 58.63  ? 385  ARG   C O   1 
ATOM   7459  C  CB  . ARG   C  1 84  ? -0.796  39.070  -95.272  1.00 47.67  ? 385  ARG   C CB  1 
ATOM   7460  C  CG  . ARG   C  1 84  ? 0.444   38.277  -95.024  1.00 51.91  ? 385  ARG   C CG  1 
ATOM   7461  C  CD  . ARG   C  1 84  ? 1.218   38.033  -96.301  1.00 50.46  ? 385  ARG   C CD  1 
ATOM   7462  N  NE  . ARG   C  1 84  ? 2.415   37.271  -95.975  1.00 55.48  ? 385  ARG   C NE  1 
ATOM   7463  C  CZ  . ARG   C  1 84  ? 2.622   36.008  -96.326  1.00 56.16  ? 385  ARG   C CZ  1 
ATOM   7464  N  NH1 . ARG   C  1 84  ? 1.726   35.358  -97.066  1.00 62.02  ? 385  ARG   C NH1 1 
ATOM   7465  N  NH2 . ARG   C  1 84  ? 3.744   35.406  -95.959  1.00 46.07  ? 385  ARG   C NH2 1 
ATOM   7466  N  N   . LEU   C  1 85  ? -3.398  37.452  -94.326  1.00 60.23  ? 386  LEU   C N   1 
ATOM   7467  C  CA  . LEU   C  1 85  ? -4.060  36.393  -93.572  1.00 53.39  ? 386  LEU   C CA  1 
ATOM   7468  C  C   . LEU   C  1 85  ? -4.727  35.392  -94.508  1.00 56.03  ? 386  LEU   C C   1 
ATOM   7469  O  O   . LEU   C  1 85  ? -4.490  34.182  -94.415  1.00 56.45  ? 386  LEU   C O   1 
ATOM   7470  C  CB  . LEU   C  1 85  ? -5.075  37.005  -92.604  1.00 55.46  ? 386  LEU   C CB  1 
ATOM   7471  C  CG  . LEU   C  1 85  ? -4.725  36.962  -91.109  1.00 55.45  ? 386  LEU   C CG  1 
ATOM   7472  C  CD1 . LEU   C  1 85  ? -3.228  36.899  -90.901  1.00 51.55  ? 386  LEU   C CD1 1 
ATOM   7473  C  CD2 . LEU   C  1 85  ? -5.324  38.159  -90.375  1.00 57.68  ? 386  LEU   C CD2 1 
ATOM   7474  N  N   . GLU   C  1 86  ? -5.562  35.885  -95.432  1.00 51.51  ? 387  GLU   C N   1 
ATOM   7475  C  CA  . GLU   C  1 86  ? -6.227  34.991  -96.370  1.00 61.14  ? 387  GLU   C CA  1 
ATOM   7476  C  C   . GLU   C  1 86  ? -5.222  34.244  -97.235  1.00 58.12  ? 387  GLU   C C   1 
ATOM   7477  O  O   . GLU   C  1 86  ? -5.456  33.085  -97.600  1.00 52.73  ? 387  GLU   C O   1 
ATOM   7478  C  CB  . GLU   C  1 86  ? -7.208  35.776  -97.246  1.00 71.41  ? 387  GLU   C CB  1 
ATOM   7479  C  CG  . GLU   C  1 86  ? -8.405  36.357  -96.492  1.00 91.10  ? 387  GLU   C CG  1 
ATOM   7480  C  CD  . GLU   C  1 86  ? -9.484  35.322  -96.209  1.00 105.39 ? 387  GLU   C CD  1 
ATOM   7481  O  OE1 . GLU   C  1 86  ? -10.038 35.325  -95.088  1.00 111.64 ? 387  GLU   C OE1 1 
ATOM   7482  O  OE2 . GLU   C  1 86  ? -9.779  34.507  -97.110  1.00 108.61 ? 387  GLU   C OE2 1 
ATOM   7483  N  N   . GLU   C  1 87  ? -4.095  34.881  -97.559  1.00 56.40  ? 388  GLU   C N   1 
ATOM   7484  C  CA  . GLU   C  1 87  ? -3.105  34.233  -98.410  1.00 62.49  ? 388  GLU   C CA  1 
ATOM   7485  C  C   . GLU   C  1 87  ? -2.438  33.077  -97.674  1.00 56.43  ? 388  GLU   C C   1 
ATOM   7486  O  O   . GLU   C  1 87  ? -2.379  31.952  -98.186  1.00 48.14  ? 388  GLU   C O   1 
ATOM   7487  C  CB  . GLU   C  1 87  ? -2.075  35.259  -98.891  1.00 60.69  ? 388  GLU   C CB  1 
ATOM   7488  C  CG  . GLU   C  1 87  ? -1.018  34.703  -99.820  1.00 47.46  ? 388  GLU   C CG  1 
ATOM   7489  C  CD  . GLU   C  1 87  ? -0.011  35.753  -100.242 1.00 60.17  ? 388  GLU   C CD  1 
ATOM   7490  O  OE1 . GLU   C  1 87  ? 0.112   36.775  -99.535  1.00 63.40  ? 388  GLU   C OE1 1 
ATOM   7491  O  OE2 . GLU   C  1 87  ? 0.659   35.562  -101.285 1.00 66.12  ? 388  GLU   C OE2 1 
ATOM   7492  N  N   . VAL   C  1 88  ? -1.945  33.332  -96.459  1.00 54.85  ? 389  VAL   C N   1 
ATOM   7493  C  CA  . VAL   C  1 88  ? -1.382  32.246  -95.665  1.00 54.98  ? 389  VAL   C CA  1 
ATOM   7494  C  C   . VAL   C  1 88  ? -2.416  31.145  -95.463  1.00 55.36  ? 389  VAL   C C   1 
ATOM   7495  O  O   . VAL   C  1 88  ? -2.087  29.951  -95.500  1.00 48.72  ? 389  VAL   C O   1 
ATOM   7496  C  CB  . VAL   C  1 88  ? -0.843  32.789  -94.330  1.00 52.72  ? 389  VAL   C CB  1 
ATOM   7497  C  CG1 . VAL   C  1 88  ? -0.527  31.645  -93.370  1.00 50.96  ? 389  VAL   C CG1 1 
ATOM   7498  C  CG2 . VAL   C  1 88  ? 0.388   33.643  -94.584  1.00 47.88  ? 389  VAL   C CG2 1 
ATOM   7499  N  N   . ASN   C  1 89  ? -3.683  31.521  -95.298  1.00 59.94  ? 390  ASN   C N   1 
ATOM   7500  C  CA  . ASN   C  1 89  ? -4.729  30.526  -95.101  1.00 62.81  ? 390  ASN   C CA  1 
ATOM   7501  C  C   . ASN   C  1 89  ? -4.780  29.552  -96.273  1.00 62.92  ? 390  ASN   C C   1 
ATOM   7502  O  O   . ASN   C  1 89  ? -4.543  28.351  -96.102  1.00 58.17  ? 390  ASN   C O   1 
ATOM   7503  C  CB  . ASN   C  1 89  ? -6.079  31.209  -94.896  1.00 64.98  ? 390  ASN   C CB  1 
ATOM   7504  C  CG  . ASN   C  1 89  ? -7.066  30.325  -94.164  1.00 74.23  ? 390  ASN   C CG  1 
ATOM   7505  O  OD1 . ASN   C  1 89  ? -7.639  29.397  -94.742  1.00 72.43  ? 390  ASN   C OD1 1 
ATOM   7506  N  ND2 . ASN   C  1 89  ? -7.266  30.604  -92.876  1.00 84.51  ? 390  ASN   C ND2 1 
ATOM   7507  N  N   . LYS   C  1 90  ? -5.055  30.059  -97.483  1.00 57.81  ? 391  LYS   C N   1 
ATOM   7508  C  CA  . LYS   C  1 90  ? -5.132  29.179  -98.643  1.00 57.84  ? 391  LYS   C CA  1 
ATOM   7509  C  C   . LYS   C  1 90  ? -3.827  28.427  -98.857  1.00 47.16  ? 391  LYS   C C   1 
ATOM   7510  O  O   . LYS   C  1 90  ? -3.838  27.262  -99.273  1.00 68.77  ? 391  LYS   C O   1 
ATOM   7511  C  CB  . LYS   C  1 90  ? -5.508  29.985  -99.890  1.00 68.68  ? 391  LYS   C CB  1 
ATOM   7512  C  CG  . LYS   C  1 90  ? -7.017  30.187  -100.013 1.00 87.24  ? 391  LYS   C CG  1 
ATOM   7513  C  CD  . LYS   C  1 90  ? -7.408  31.221  -101.062 1.00 95.77  ? 391  LYS   C CD  1 
ATOM   7514  C  CE  . LYS   C  1 90  ? -8.920  31.414  -101.070 1.00 102.50 ? 391  LYS   C CE  1 
ATOM   7515  N  NZ  . LYS   C  1 90  ? -9.347  32.491  -102.002 1.00 106.54 ? 391  LYS   C NZ  1 
ATOM   7516  N  N   . GLU   C  1 91  ? -2.694  29.068  -98.562  1.00 51.79  ? 392  GLU   C N   1 
ATOM   7517  C  CA  . GLU   C  1 91  ? -1.398  28.417  -98.735  1.00 59.87  ? 392  GLU   C CA  1 
ATOM   7518  C  C   . GLU   C  1 91  ? -1.272  27.185  -97.851  1.00 59.56  ? 392  GLU   C C   1 
ATOM   7519  O  O   . GLU   C  1 91  ? -0.675  26.181  -98.252  1.00 53.58  ? 392  GLU   C O   1 
ATOM   7520  C  CB  . GLU   C  1 91  ? -0.274  29.405  -98.438  1.00 59.21  ? 392  GLU   C CB  1 
ATOM   7521  C  CG  . GLU   C  1 91  ? 0.847   29.367  -99.459  1.00 58.52  ? 392  GLU   C CG  1 
ATOM   7522  C  CD  . GLU   C  1 91  ? 1.809   30.519  -99.295  1.00 63.67  ? 392  GLU   C CD  1 
ATOM   7523  O  OE1 . GLU   C  1 91  ? 3.018   30.309  -99.523  1.00 66.49  ? 392  GLU   C OE1 1 
ATOM   7524  O  OE2 . GLU   C  1 91  ? 1.356   31.628  -98.929  1.00 57.40  ? 392  GLU   C OE2 1 
ATOM   7525  N  N   . ILE   C  1 92  ? -1.821  27.243  -96.641  1.00 63.96  ? 393  ILE   C N   1 
ATOM   7526  C  CA  . ILE   C  1 92  ? -1.781  26.071  -95.779  1.00 63.07  ? 393  ILE   C CA  1 
ATOM   7527  C  C   . ILE   C  1 92  ? -2.729  24.998  -96.300  1.00 63.89  ? 393  ILE   C C   1 
ATOM   7528  O  O   . ILE   C  1 92  ? -2.356  23.822  -96.380  1.00 66.43  ? 393  ILE   C O   1 
ATOM   7529  C  CB  . ILE   C  1 92  ? -2.082  26.471  -94.323  1.00 66.55  ? 393  ILE   C CB  1 
ATOM   7530  C  CG1 . ILE   C  1 92  ? -0.919  27.300  -93.757  1.00 53.65  ? 393  ILE   C CG1 1 
ATOM   7531  C  CG2 . ILE   C  1 92  ? -2.332  25.237  -93.473  1.00 70.21  ? 393  ILE   C CG2 1 
ATOM   7532  C  CD1 . ILE   C  1 92  ? -1.316  28.197  -92.590  1.00 54.52  ? 393  ILE   C CD1 1 
ATOM   7533  N  N   . ASP   C  1 93  ? -3.951  25.392  -96.711  1.00 67.35  ? 394  ASP   C N   1 
ATOM   7534  C  CA  . ASP   C  1 93  ? -4.926  24.455  -97.288  1.00 62.38  ? 394  ASP   C CA  1 
ATOM   7535  C  C   . ASP   C  1 93  ? -4.380  23.711  -98.505  1.00 72.13  ? 394  ASP   C C   1 
ATOM   7536  O  O   . ASP   C  1 93  ? -4.836  22.603  -98.810  1.00 81.08  ? 394  ASP   C O   1 
ATOM   7537  C  CB  . ASP   C  1 93  ? -6.207  25.179  -97.724  1.00 57.18  ? 394  ASP   C CB  1 
ATOM   7538  C  CG  . ASP   C  1 93  ? -6.926  25.865  -96.597  1.00 69.36  ? 394  ASP   C CG  1 
ATOM   7539  O  OD1 . ASP   C  1 93  ? -6.265  26.553  -95.816  1.00 80.27  ? 394  ASP   C OD1 1 
ATOM   7540  O  OD2 . ASP   C  1 93  ? -8.164  25.753  -96.497  1.00 76.77  ? 394  ASP   C OD2 1 
ATOM   7541  N  N   . THR   C  1 94  ? -3.444  24.313  -99.240  1.00 67.47  ? 395  THR   C N   1 
ATOM   7542  C  CA  . THR   C  1 94  ? -3.012  23.740  -100.504 1.00 72.80  ? 395  THR   C CA  1 
ATOM   7543  C  C   . THR   C  1 94  ? -1.608  23.144  -100.473 1.00 74.60  ? 395  THR   C C   1 
ATOM   7544  O  O   . THR   C  1 94  ? -1.265  22.376  -101.379 1.00 84.75  ? 395  THR   C O   1 
ATOM   7545  C  CB  . THR   C  1 94  ? -3.109  24.797  -101.619 1.00 68.93  ? 395  THR   C CB  1 
ATOM   7546  O  OG1 . THR   C  1 94  ? -2.284  25.920  -101.295 1.00 74.72  ? 395  THR   C OG1 1 
ATOM   7547  C  CG2 . THR   C  1 94  ? -4.535  25.285  -101.751 1.00 60.55  ? 395  THR   C CG2 1 
ATOM   7548  N  N   . THR   C  1 95  ? -0.793  23.462  -99.456  1.00 61.16  ? 396  THR   C N   1 
ATOM   7549  C  CA  . THR   C  1 95  ? 0.541   22.882  -99.336  1.00 55.25  ? 396  THR   C CA  1 
ATOM   7550  C  C   . THR   C  1 95  ? 0.892   22.422  -97.924  1.00 60.53  ? 396  THR   C C   1 
ATOM   7551  O  O   . THR   C  1 95  ? 2.008   21.932  -97.722  1.00 58.78  ? 396  THR   C O   1 
ATOM   7552  C  CB  . THR   C  1 95  ? 1.637   23.878  -99.779  1.00 52.00  ? 396  THR   C CB  1 
ATOM   7553  O  OG1 . THR   C  1 95  ? 1.926   24.785  -98.699  1.00 58.87  ? 396  THR   C OG1 1 
ATOM   7554  C  CG2 . THR   C  1 95  ? 1.229   24.673  -100.978 1.00 42.84  ? 396  THR   C CG2 1 
ATOM   7555  N  N   . SER   C  1 96  ? 0.015   22.600  -96.939  1.00 60.77  ? 397  SER   C N   1 
ATOM   7556  C  CA  . SER   C  1 96  ? 0.292   22.274  -95.543  1.00 66.03  ? 397  SER   C CA  1 
ATOM   7557  C  C   . SER   C  1 96  ? 1.407   23.120  -94.933  1.00 64.54  ? 397  SER   C C   1 
ATOM   7558  O  O   . SER   C  1 96  ? 1.855   22.821  -93.817  1.00 67.62  ? 397  SER   C O   1 
ATOM   7559  C  CB  . SER   C  1 96  ? 0.629   20.788  -95.354  1.00 67.35  ? 397  SER   C CB  1 
ATOM   7560  O  OG  . SER   C  1 96  ? -0.522  19.978  -95.496  1.00 69.72  ? 397  SER   C OG  1 
ATOM   7561  N  N   . THR   C  1 97  ? 1.870   24.165  -95.618  1.00 57.55  ? 398  THR   C N   1 
ATOM   7562  C  CA  . THR   C  1 97  ? 2.835   25.098  -95.038  1.00 55.00  ? 398  THR   C CA  1 
ATOM   7563  C  C   . THR   C  1 97  ? 2.539   26.490  -95.598  1.00 52.22  ? 398  THR   C C   1 
ATOM   7564  O  O   . THR   C  1 97  ? 1.459   26.733  -96.149  1.00 46.60  ? 398  THR   C O   1 
ATOM   7565  C  CB  . THR   C  1 97  ? 4.269   24.609  -95.299  1.00 52.37  ? 398  THR   C CB  1 
ATOM   7566  O  OG1 . THR   C  1 97  ? 5.194   25.391  -94.538  1.00 53.60  ? 398  THR   C OG1 1 
ATOM   7567  C  CG2 . THR   C  1 97  ? 4.630   24.694  -96.797  1.00 49.43  ? 398  THR   C CG2 1 
ATOM   7568  N  N   . TYR   C  1 98  ? 3.478   27.423  -95.427  1.00 48.32  ? 399  TYR   C N   1 
ATOM   7569  C  CA  . TYR   C  1 98  ? 3.367   28.712  -96.104  1.00 45.71  ? 399  TYR   C CA  1 
ATOM   7570  C  C   . TYR   C  1 98  ? 4.740   29.368  -96.189  1.00 45.68  ? 399  TYR   C C   1 
ATOM   7571  O  O   . TYR   C  1 98  ? 5.704   28.942  -95.546  1.00 47.91  ? 399  TYR   C O   1 
ATOM   7572  C  CB  . TYR   C  1 98  ? 2.348   29.631  -95.418  1.00 42.14  ? 399  TYR   C CB  1 
ATOM   7573  C  CG  . TYR   C  1 98  ? 2.827   30.268  -94.146  1.00 44.30  ? 399  TYR   C CG  1 
ATOM   7574  C  CD1 . TYR   C  1 98  ? 2.697   29.611  -92.925  1.00 44.18  ? 399  TYR   C CD1 1 
ATOM   7575  C  CD2 . TYR   C  1 98  ? 3.383   31.540  -94.155  1.00 40.19  ? 399  TYR   C CD2 1 
ATOM   7576  C  CE1 . TYR   C  1 98  ? 3.132   30.197  -91.758  1.00 50.47  ? 399  TYR   C CE1 1 
ATOM   7577  C  CE2 . TYR   C  1 98  ? 3.810   32.133  -92.999  1.00 47.27  ? 399  TYR   C CE2 1 
ATOM   7578  C  CZ  . TYR   C  1 98  ? 3.681   31.460  -91.804  1.00 52.33  ? 399  TYR   C CZ  1 
ATOM   7579  O  OH  . TYR   C  1 98  ? 4.114   32.055  -90.652  1.00 59.60  ? 399  TYR   C OH  1 
ATOM   7580  N  N   . GLN   C  1 99  ? 4.817   30.415  -97.007  1.00 46.90  ? 400  GLN   C N   1 
ATOM   7581  C  CA  . GLN   C  1 99  ? 6.082   31.058  -97.347  1.00 44.14  ? 400  GLN   C CA  1 
ATOM   7582  C  C   . GLN   C  1 99  ? 6.067   32.496  -96.863  1.00 40.85  ? 400  GLN   C C   1 
ATOM   7583  O  O   . GLN   C  1 99  ? 5.057   33.192  -96.994  1.00 44.28  ? 400  GLN   C O   1 
ATOM   7584  C  CB  . GLN   C  1 99  ? 6.348   31.023  -98.879  1.00 37.33  ? 400  GLN   C CB  1 
ATOM   7585  C  CG  . GLN   C  1 99  ? 6.351   29.627  -99.492  1.00 41.89  ? 400  GLN   C CG  1 
ATOM   7586  C  CD  . GLN   C  1 99  ? 7.396   28.698  -98.876  1.00 55.26  ? 400  GLN   C CD  1 
ATOM   7587  O  OE1 . GLN   C  1 99  ? 8.563   29.060  -98.711  1.00 53.87  ? 400  GLN   C OE1 1 
ATOM   7588  N  NE2 . GLN   C  1 99  ? 6.970   27.486  -98.534  1.00 62.49  ? 400  GLN   C NE2 1 
ATOM   7589  N  N   . LEU   C  1 100 ? 7.191   32.938  -96.311  1.00 45.61  ? 401  LEU   C N   1 
ATOM   7590  C  CA  . LEU   C  1 100 ? 7.297   34.284  -95.762  1.00 46.95  ? 401  LEU   C CA  1 
ATOM   7591  C  C   . LEU   C  1 100 ? 7.721   35.260  -96.846  1.00 41.59  ? 401  LEU   C C   1 
ATOM   7592  O  O   . LEU   C  1 100 ? 8.625   34.966  -97.630  1.00 39.67  ? 401  LEU   C O   1 
ATOM   7593  C  CB  . LEU   C  1 100 ? 8.314   34.334  -94.609  1.00 42.22  ? 401  LEU   C CB  1 
ATOM   7594  C  CG  . LEU   C  1 100 ? 8.048   33.526  -93.346  1.00 43.94  ? 401  LEU   C CG  1 
ATOM   7595  C  CD1 . LEU   C  1 100 ? 9.184   33.707  -92.341  1.00 49.02  ? 401  LEU   C CD1 1 
ATOM   7596  C  CD2 . LEU   C  1 100 ? 6.749   33.949  -92.724  1.00 31.70  ? 401  LEU   C CD2 1 
ATOM   7597  N  N   . LYS   C  1 101 ? 7.071   36.424  -96.873  1.00 38.79  ? 402  LYS   C N   1 
ATOM   7598  C  CA  . LYS   C  1 101 ? 7.583   37.559  -97.627  1.00 36.32  ? 402  LYS   C CA  1 
ATOM   7599  C  C   . LYS   C  1 101 ? 8.983   37.928  -97.137  1.00 40.00  ? 402  LYS   C C   1 
ATOM   7600  O  O   . LYS   C  1 101 ? 9.377   37.616  -96.013  1.00 38.31  ? 402  LYS   C O   1 
ATOM   7601  C  CB  . LYS   C  1 101 ? 6.671   38.777  -97.477  1.00 37.13  ? 402  LYS   C CB  1 
ATOM   7602  C  CG  . LYS   C  1 101 ? 5.250   38.595  -97.919  1.00 43.97  ? 402  LYS   C CG  1 
ATOM   7603  C  CD  . LYS   C  1 101 ? 5.155   38.055  -99.337  1.00 47.99  ? 402  LYS   C CD  1 
ATOM   7604  C  CE  . LYS   C  1 101 ? 3.710   37.982  -99.815  1.00 51.13  ? 402  LYS   C CE  1 
ATOM   7605  N  NZ  . LYS   C  1 101 ? 3.516   36.902  -100.839 1.00 61.12  ? 402  LYS   C NZ  1 
ATOM   7606  N  N   . ASP   C  1 102 ? 9.727   38.630  -97.994  1.00 45.97  ? 403  ASP   C N   1 
ATOM   7607  C  CA  . ASP   C  1 102 ? 11.096  39.019  -97.671  1.00 39.31  ? 403  ASP   C CA  1 
ATOM   7608  C  C   . ASP   C  1 102 ? 11.147  39.913  -96.442  1.00 40.64  ? 403  ASP   C C   1 
ATOM   7609  O  O   . ASP   C  1 102 ? 12.024  39.755  -95.586  1.00 46.23  ? 403  ASP   C O   1 
ATOM   7610  C  CB  . ASP   C  1 102 ? 11.721  39.744  -98.863  1.00 49.44  ? 403  ASP   C CB  1 
ATOM   7611  C  CG  . ASP   C  1 102 ? 12.035  38.809  -100.024 1.00 59.64  ? 403  ASP   C CG  1 
ATOM   7612  O  OD1 . ASP   C  1 102 ? 11.753  37.597  -99.908  1.00 60.40  ? 403  ASP   C OD1 1 
ATOM   7613  O  OD2 . ASP   C  1 102 ? 12.580  39.284  -101.048 1.00 62.82  ? 403  ASP   C OD2 1 
ATOM   7614  N  N   . THR   C  1 103 ? 10.233  40.880  -96.363  1.00 42.71  ? 404  THR   C N   1 
ATOM   7615  C  CA  . THR   C  1 103 ? 10.125  41.733  -95.187  1.00 48.07  ? 404  THR   C CA  1 
ATOM   7616  C  C   . THR   C  1 103 ? 9.881   40.905  -93.926  1.00 47.09  ? 404  THR   C C   1 
ATOM   7617  O  O   . THR   C  1 103 ? 10.566  41.076  -92.916  1.00 43.10  ? 404  THR   C O   1 
ATOM   7618  C  CB  . THR   C  1 103 ? 8.998   42.746  -95.395  1.00 48.12  ? 404  THR   C CB  1 
ATOM   7619  O  OG1 . THR   C  1 103 ? 7.772   42.054  -95.671  1.00 49.69  ? 404  THR   C OG1 1 
ATOM   7620  C  CG2 . THR   C  1 103 ? 9.315   43.641  -96.567  1.00 41.90  ? 404  THR   C CG2 1 
ATOM   7621  N  N   . GLU   C  1 104 ? 8.913   39.988  -93.980  1.00 46.82  ? 405  GLU   C N   1 
ATOM   7622  C  CA  . GLU   C  1 104 ? 8.610   39.136  -92.836  1.00 40.33  ? 405  GLU   C CA  1 
ATOM   7623  C  C   . GLU   C  1 104 ? 9.818   38.300  -92.420  1.00 45.59  ? 405  GLU   C C   1 
ATOM   7624  O  O   . GLU   C  1 104 ? 10.078  38.120  -91.223  1.00 42.68  ? 405  GLU   C O   1 
ATOM   7625  C  CB  . GLU   C  1 104 ? 7.424   38.232  -93.180  1.00 40.22  ? 405  GLU   C CB  1 
ATOM   7626  C  CG  . GLU   C  1 104 ? 6.223   38.977  -93.717  1.00 44.31  ? 405  GLU   C CG  1 
ATOM   7627  C  CD  . GLU   C  1 104 ? 5.143   38.051  -94.231  1.00 47.97  ? 405  GLU   C CD  1 
ATOM   7628  O  OE1 . GLU   C  1 104 ? 3.988   38.498  -94.369  1.00 45.37  ? 405  GLU   C OE1 1 
ATOM   7629  O  OE2 . GLU   C  1 104 ? 5.453   36.875  -94.499  1.00 49.34  ? 405  GLU   C OE2 1 
ATOM   7630  N  N   . LEU   C  1 105 ? 10.558  37.765  -93.400  1.00 44.22  ? 406  LEU   C N   1 
ATOM   7631  C  CA  . LEU   C  1 105 ? 11.757  36.991  -93.097  1.00 37.30  ? 406  LEU   C CA  1 
ATOM   7632  C  C   . LEU   C  1 105 ? 12.798  37.854  -92.390  1.00 42.88  ? 406  LEU   C C   1 
ATOM   7633  O  O   . LEU   C  1 105 ? 13.415  37.417  -91.410  1.00 41.31  ? 406  LEU   C O   1 
ATOM   7634  C  CB  . LEU   C  1 105 ? 12.349  36.386  -94.379  1.00 37.65  ? 406  LEU   C CB  1 
ATOM   7635  C  CG  . LEU   C  1 105 ? 13.561  35.459  -94.204  1.00 35.93  ? 406  LEU   C CG  1 
ATOM   7636  C  CD1 . LEU   C  1 105 ? 13.122  34.069  -93.771  1.00 35.64  ? 406  LEU   C CD1 1 
ATOM   7637  C  CD2 . LEU   C  1 105 ? 14.433  35.368  -95.467  1.00 36.95  ? 406  LEU   C CD2 1 
ATOM   7638  N  N   . ILE   C  1 106 ? 13.024  39.074  -92.889  1.00 37.75  ? 407  ILE   C N   1 
ATOM   7639  C  CA  . ILE   C  1 106 ? 14.034  39.936  -92.287  1.00 40.11  ? 407  ILE   C CA  1 
ATOM   7640  C  C   . ILE   C  1 106 ? 13.622  40.324  -90.871  1.00 47.42  ? 407  ILE   C C   1 
ATOM   7641  O  O   . ILE   C  1 106 ? 14.451  40.363  -89.952  1.00 44.54  ? 407  ILE   C O   1 
ATOM   7642  C  CB  . ILE   C  1 106 ? 14.265  41.176  -93.166  1.00 35.97  ? 407  ILE   C CB  1 
ATOM   7643  C  CG1 . ILE   C  1 106 ? 15.109  40.810  -94.385  1.00 28.06  ? 407  ILE   C CG1 1 
ATOM   7644  C  CG2 . ILE   C  1 106 ? 14.878  42.316  -92.334  1.00 31.96  ? 407  ILE   C CG2 1 
ATOM   7645  C  CD1 . ILE   C  1 106 ? 14.920  41.791  -95.598  1.00 31.47  ? 407  ILE   C CD1 1 
ATOM   7646  N  N   . TYR   C  1 107 ? 12.331  40.597  -90.684  1.00 45.89  ? 408  TYR   C N   1 
ATOM   7647  C  CA  . TYR   C  1 107 ? 11.791  40.965  -89.386  1.00 42.39  ? 408  TYR   C CA  1 
ATOM   7648  C  C   . TYR   C  1 107 ? 11.932  39.821  -88.391  1.00 45.22  ? 408  TYR   C C   1 
ATOM   7649  O  O   . TYR   C  1 107 ? 12.352  40.023  -87.244  1.00 41.75  ? 408  TYR   C O   1 
ATOM   7650  C  CB  . TYR   C  1 107 ? 10.322  41.361  -89.554  1.00 40.03  ? 408  TYR   C CB  1 
ATOM   7651  C  CG  . TYR   C  1 107 ? 9.562   41.546  -88.257  1.00 47.66  ? 408  TYR   C CG  1 
ATOM   7652  C  CD1 . TYR   C  1 107 ? 9.593   42.755  -87.577  1.00 49.02  ? 408  TYR   C CD1 1 
ATOM   7653  C  CD2 . TYR   C  1 107 ? 8.799   40.508  -87.721  1.00 49.05  ? 408  TYR   C CD2 1 
ATOM   7654  C  CE1 . TYR   C  1 107 ? 8.886   42.926  -86.390  1.00 56.32  ? 408  TYR   C CE1 1 
ATOM   7655  C  CE2 . TYR   C  1 107 ? 8.096   40.664  -86.552  1.00 47.86  ? 408  TYR   C CE2 1 
ATOM   7656  C  CZ  . TYR   C  1 107 ? 8.139   41.875  -85.883  1.00 57.65  ? 408  TYR   C CZ  1 
ATOM   7657  O  OH  . TYR   C  1 107 ? 7.431   42.031  -84.708  1.00 65.72  ? 408  TYR   C OH  1 
ATOM   7658  N  N   . GLY   C  1 108 ? 11.584  38.611  -88.824  1.00 41.01  ? 409  GLY   C N   1 
ATOM   7659  C  CA  . GLY   C  1 108 ? 11.674  37.460  -87.947  1.00 32.40  ? 409  GLY   C CA  1 
ATOM   7660  C  C   . GLY   C  1 108 ? 13.090  37.161  -87.489  1.00 44.48  ? 409  GLY   C C   1 
ATOM   7661  O  O   . GLY   C  1 108 ? 13.320  36.855  -86.312  1.00 43.77  ? 409  GLY   C O   1 
ATOM   7662  N  N   . ALA   C  1 109 ? 14.057  37.228  -88.407  1.00 42.07  ? 410  ALA   C N   1 
ATOM   7663  C  CA  . ALA   C  1 109 ? 15.432  36.955  -88.013  1.00 38.91  ? 410  ALA   C CA  1 
ATOM   7664  C  C   . ALA   C  1 109 ? 15.915  37.986  -87.000  1.00 32.62  ? 410  ALA   C C   1 
ATOM   7665  O  O   . ALA   C  1 109 ? 16.620  37.645  -86.048  1.00 34.19  ? 410  ALA   C O   1 
ATOM   7666  C  CB  . ALA   C  1 109 ? 16.356  36.934  -89.234  1.00 30.16  ? 410  ALA   C CB  1 
ATOM   7667  N  N   . LYS   C  1 110 ? 15.560  39.251  -87.197  1.00 30.28  ? 411  LYS   C N   1 
ATOM   7668  C  CA  . LYS   C  1 110 ? 16.087  40.270  -86.313  1.00 36.46  ? 411  LYS   C CA  1 
ATOM   7669  C  C   . LYS   C  1 110 ? 15.460  40.147  -84.935  1.00 41.70  ? 411  LYS   C C   1 
ATOM   7670  O  O   . LYS   C  1 110 ? 16.106  40.457  -83.929  1.00 37.78  ? 411  LYS   C O   1 
ATOM   7671  C  CB  . LYS   C  1 110 ? 15.861  41.658  -86.902  1.00 40.89  ? 411  LYS   C CB  1 
ATOM   7672  C  CG  . LYS   C  1 110 ? 16.704  41.942  -88.144  1.00 42.36  ? 411  LYS   C CG  1 
ATOM   7673  C  CD  . LYS   C  1 110 ? 16.478  43.357  -88.668  1.00 34.49  ? 411  LYS   C CD  1 
ATOM   7674  C  CE  . LYS   C  1 110 ? 17.515  43.717  -89.727  1.00 41.55  ? 411  LYS   C CE  1 
ATOM   7675  N  NZ  . LYS   C  1 110 ? 17.451  45.150  -90.123  1.00 41.86  ? 411  LYS   C NZ  1 
ATOM   7676  N  N   . HIS   C  1 111 ? 14.234  39.644  -84.870  1.00 41.14  ? 412  HIS   C N   1 
ATOM   7677  C  CA  . HIS   C  1 111 ? 13.549  39.537  -83.594  1.00 40.10  ? 412  HIS   C CA  1 
ATOM   7678  C  C   . HIS   C  1 111 ? 13.897  38.247  -82.855  1.00 49.78  ? 412  HIS   C C   1 
ATOM   7679  O  O   . HIS   C  1 111 ? 13.837  38.213  -81.616  1.00 46.32  ? 412  HIS   C O   1 
ATOM   7680  C  CB  . HIS   C  1 111 ? 12.044  39.684  -83.819  1.00 33.34  ? 412  HIS   C CB  1 
ATOM   7681  C  CG  . HIS   C  1 111 ? 11.616  41.112  -83.882  1.00 40.42  ? 412  HIS   C CG  1 
ATOM   7682  N  ND1 . HIS   C  1 111 ? 10.829  41.698  -82.916  1.00 42.67  ? 412  HIS   C ND1 1 
ATOM   7683  C  CD2 . HIS   C  1 111 ? 11.921  42.094  -84.763  1.00 42.00  ? 412  HIS   C CD2 1 
ATOM   7684  C  CE1 . HIS   C  1 111 ? 10.647  42.973  -83.209  1.00 46.46  ? 412  HIS   C CE1 1 
ATOM   7685  N  NE2 . HIS   C  1 111 ? 11.297  43.238  -84.328  1.00 46.03  ? 412  HIS   C NE2 1 
ATOM   7686  N  N   . ALA   C  1 112 ? 14.282  37.189  -83.580  1.00 46.68  ? 413  ALA   C N   1 
ATOM   7687  C  CA  . ALA   C  1 112 ? 14.824  36.013  -82.908  1.00 47.12  ? 413  ALA   C CA  1 
ATOM   7688  C  C   . ALA   C  1 112 ? 16.143  36.339  -82.221  1.00 42.61  ? 413  ALA   C C   1 
ATOM   7689  O  O   . ALA   C  1 112 ? 16.435  35.811  -81.144  1.00 40.16  ? 413  ALA   C O   1 
ATOM   7690  C  CB  . ALA   C  1 112 ? 15.016  34.882  -83.902  1.00 40.49  ? 413  ALA   C CB  1 
ATOM   7691  N  N   . TRP   C  1 113 ? 16.959  37.188  -82.847  1.00 32.20  ? 414  TRP   C N   1 
ATOM   7692  C  CA  . TRP   C  1 113 ? 18.141  37.708  -82.180  1.00 32.67  ? 414  TRP   C CA  1 
ATOM   7693  C  C   . TRP   C  1 113 ? 17.747  38.629  -81.024  1.00 41.54  ? 414  TRP   C C   1 
ATOM   7694  O  O   . TRP   C  1 113 ? 18.345  38.572  -79.946  1.00 42.89  ? 414  TRP   C O   1 
ATOM   7695  C  CB  . TRP   C  1 113 ? 19.042  38.434  -83.190  1.00 26.24  ? 414  TRP   C CB  1 
ATOM   7696  C  CG  . TRP   C  1 113 ? 20.364  38.895  -82.598  1.00 31.43  ? 414  TRP   C CG  1 
ATOM   7697  C  CD1 . TRP   C  1 113 ? 20.884  38.566  -81.352  1.00 28.79  ? 414  TRP   C CD1 1 
ATOM   7698  C  CD2 . TRP   C  1 113 ? 21.326  39.771  -83.208  1.00 32.66  ? 414  TRP   C CD2 1 
ATOM   7699  N  NE1 . TRP   C  1 113 ? 22.095  39.182  -81.176  1.00 26.11  ? 414  TRP   C NE1 1 
ATOM   7700  C  CE2 . TRP   C  1 113 ? 22.387  39.929  -82.296  1.00 30.38  ? 414  TRP   C CE2 1 
ATOM   7701  C  CE3 . TRP   C  1 113 ? 21.395  40.433  -84.441  1.00 32.25  ? 414  TRP   C CE3 1 
ATOM   7702  C  CZ2 . TRP   C  1 113 ? 23.498  40.727  -82.582  1.00 30.27  ? 414  TRP   C CZ2 1 
ATOM   7703  C  CZ3 . TRP   C  1 113 ? 22.508  41.224  -84.723  1.00 28.31  ? 414  TRP   C CZ3 1 
ATOM   7704  C  CH2 . TRP   C  1 113 ? 23.542  41.354  -83.806  1.00 35.81  ? 414  TRP   C CH2 1 
ATOM   7705  N  N   . ARG   C  1 114 ? 16.739  39.474  -81.221  1.00 35.67  ? 415  ARG   C N   1 
ATOM   7706  C  CA  . ARG   C  1 114 ? 16.326  40.373  -80.150  1.00 37.19  ? 415  ARG   C CA  1 
ATOM   7707  C  C   . ARG   C  1 114 ? 15.809  39.604  -78.937  1.00 47.05  ? 415  ARG   C C   1 
ATOM   7708  O  O   . ARG   C  1 114 ? 15.949  40.066  -77.794  1.00 47.29  ? 415  ARG   C O   1 
ATOM   7709  C  CB  . ARG   C  1 114 ? 15.247  41.313  -80.665  1.00 34.98  ? 415  ARG   C CB  1 
ATOM   7710  C  CG  . ARG   C  1 114 ? 15.071  42.577  -79.887  1.00 28.78  ? 415  ARG   C CG  1 
ATOM   7711  C  CD  . ARG   C  1 114 ? 13.787  43.255  -80.302  1.00 28.62  ? 415  ARG   C CD  1 
ATOM   7712  N  NE  . ARG   C  1 114 ? 13.594  44.531  -79.626  1.00 35.76  ? 415  ARG   C NE  1 
ATOM   7713  C  CZ  . ARG   C  1 114 ? 12.638  45.395  -79.937  1.00 36.95  ? 415  ARG   C CZ  1 
ATOM   7714  N  NH1 . ARG   C  1 114 ? 12.519  46.546  -79.274  1.00 31.06  ? 415  ARG   C NH1 1 
ATOM   7715  N  NH2 . ARG   C  1 114 ? 11.801  45.101  -80.922  1.00 32.63  ? 415  ARG   C NH2 1 
ATOM   7716  N  N   . ASN   C  1 115 ? 15.206  38.441  -79.164  1.00 41.05  ? 416  ASN   C N   1 
ATOM   7717  C  CA  . ASN   C  1 115 ? 14.563  37.684  -78.104  1.00 39.19  ? 416  ASN   C CA  1 
ATOM   7718  C  C   . ASN   C  1 115 ? 15.490  36.654  -77.475  1.00 39.65  ? 416  ASN   C C   1 
ATOM   7719  O  O   . ASN   C  1 115 ? 15.070  35.966  -76.535  1.00 37.11  ? 416  ASN   C O   1 
ATOM   7720  C  CB  . ASN   C  1 115 ? 13.303  36.983  -78.635  1.00 31.37  ? 416  ASN   C CB  1 
ATOM   7721  C  CG  . ASN   C  1 115 ? 12.249  37.959  -79.143  1.00 38.72  ? 416  ASN   C CG  1 
ATOM   7722  O  OD1 . ASN   C  1 115 ? 12.142  39.089  -78.653  1.00 35.81  ? 416  ASN   C OD1 1 
ATOM   7723  N  ND2 . ASN   C  1 115 ? 11.468  37.525  -80.149  1.00 36.98  ? 416  ASN   C ND2 1 
ATOM   7724  N  N   . ALA   C  1 116 ? 16.729  36.534  -77.969  1.00 33.87  ? 417  ALA   C N   1 
ATOM   7725  C  CA  . ALA   C  1 116 ? 17.679  35.522  -77.511  1.00 36.92  ? 417  ALA   C CA  1 
ATOM   7726  C  C   . ALA   C  1 116 ? 18.200  35.873  -76.115  1.00 41.86  ? 417  ALA   C C   1 
ATOM   7727  O  O   . ALA   C  1 116 ? 19.202  36.584  -75.962  1.00 39.08  ? 417  ALA   C O   1 
ATOM   7728  C  CB  . ALA   C  1 116 ? 18.830  35.365  -78.512  1.00 34.10  ? 417  ALA   C CB  1 
ATOM   7729  N  N   . SER   C  1 117 ? 17.528  35.338  -75.090  1.00 36.97  ? 418  SER   C N   1 
ATOM   7730  C  CA  A SER   C  1 117 ? 17.775  35.803  -73.731  0.70 38.92  ? 418  SER   C CA  1 
ATOM   7731  C  CA  B SER   C  1 117 ? 17.763  35.751  -73.710  0.30 37.84  ? 418  SER   C CA  1 
ATOM   7732  C  C   . SER   C  1 117 ? 19.199  35.534  -73.268  1.00 39.70  ? 418  SER   C C   1 
ATOM   7733  O  O   . SER   C  1 117 ? 19.657  36.193  -72.330  1.00 42.30  ? 418  SER   C O   1 
ATOM   7734  C  CB  A SER   C  1 117 ? 16.766  35.170  -72.773  0.70 34.92  ? 418  SER   C CB  1 
ATOM   7735  C  CB  B SER   C  1 117 ? 16.829  34.984  -72.778  0.30 34.92  ? 418  SER   C CB  1 
ATOM   7736  O  OG  A SER   C  1 117 ? 16.956  33.775  -72.639  0.70 33.07  ? 418  SER   C OG  1 
ATOM   7737  O  OG  B SER   C  1 117 ? 15.486  35.033  -73.225  0.30 33.03  ? 418  SER   C OG  1 
ATOM   7738  N  N   . ARG   C  1 118 ? 19.908  34.615  -73.913  1.00 39.61  ? 419  ARG   C N   1 
ATOM   7739  C  CA  . ARG   C  1 118 ? 21.261  34.262  -73.529  1.00 27.33  ? 419  ARG   C CA  1 
ATOM   7740  C  C   . ARG   C  1 118 ? 22.333  35.128  -74.173  1.00 37.40  ? 419  ARG   C C   1 
ATOM   7741  O  O   . ARG   C  1 118 ? 23.510  34.976  -73.830  1.00 30.79  ? 419  ARG   C O   1 
ATOM   7742  C  CB  . ARG   C  1 118 ? 21.498  32.783  -73.851  1.00 25.58  ? 419  ARG   C CB  1 
ATOM   7743  C  CG  . ARG   C  1 118 ? 20.646  31.880  -72.939  1.00 26.85  ? 419  ARG   C CG  1 
ATOM   7744  C  CD  . ARG   C  1 118 ? 20.916  30.407  -73.146  1.00 33.13  ? 419  ARG   C CD  1 
ATOM   7745  N  NE  . ARG   C  1 118 ? 20.297  29.630  -72.069  1.00 37.84  ? 419  ARG   C NE  1 
ATOM   7746  C  CZ  . ARG   C  1 118 ? 20.131  28.311  -72.082  1.00 45.95  ? 419  ARG   C CZ  1 
ATOM   7747  N  NH1 . ARG   C  1 118 ? 20.522  27.609  -73.130  1.00 56.47  ? 419  ARG   C NH1 1 
ATOM   7748  N  NH2 . ARG   C  1 118 ? 19.560  27.692  -71.052  1.00 45.94  ? 419  ARG   C NH2 1 
ATOM   7749  N  N   . CYS   C  1 119 ? 21.970  36.033  -75.081  1.00 39.72  ? 420  CYS   C N   1 
ATOM   7750  C  CA  . CYS   C  1 119 ? 22.949  36.729  -75.903  1.00 38.70  ? 420  CYS   C CA  1 
ATOM   7751  C  C   . CYS   C  1 119 ? 23.242  38.106  -75.321  1.00 32.34  ? 420  CYS   C C   1 
ATOM   7752  O  O   . CYS   C  1 119 ? 22.348  38.956  -75.234  1.00 34.14  ? 420  CYS   C O   1 
ATOM   7753  C  CB  . CYS   C  1 119 ? 22.457  36.853  -77.345  1.00 40.87  ? 420  CYS   C CB  1 
ATOM   7754  S  SG  . CYS   C  1 119 ? 23.533  37.862  -78.342  1.00 35.66  ? 420  CYS   C SG  1 
ATOM   7755  N  N   . VAL   C  1 120 ? 24.510  38.339  -74.974  1.00 31.15  ? 421  VAL   C N   1 
ATOM   7756  C  CA  . VAL   C  1 120 ? 24.918  39.629  -74.424  1.00 32.27  ? 421  VAL   C CA  1 
ATOM   7757  C  C   . VAL   C  1 120 ? 25.116  40.694  -75.489  1.00 35.78  ? 421  VAL   C C   1 
ATOM   7758  O  O   . VAL   C  1 120 ? 25.165  41.884  -75.149  1.00 35.61  ? 421  VAL   C O   1 
ATOM   7759  C  CB  . VAL   C  1 120 ? 26.194  39.442  -73.575  1.00 34.40  ? 421  VAL   C CB  1 
ATOM   7760  C  CG1 . VAL   C  1 120 ? 27.397  39.079  -74.448  1.00 30.03  ? 421  VAL   C CG1 1 
ATOM   7761  C  CG2 . VAL   C  1 120 ? 26.463  40.674  -72.706  1.00 29.17  ? 421  VAL   C CG2 1 
ATOM   7762  N  N   . GLY   C  1 121 ? 25.181  40.310  -76.771  1.00 40.38  ? 422  GLY   C N   1 
ATOM   7763  C  CA  . GLY   C  1 121 ? 25.435  41.212  -77.872  1.00 36.84  ? 422  GLY   C CA  1 
ATOM   7764  C  C   . GLY   C  1 121 ? 24.225  41.891  -78.477  1.00 42.29  ? 422  GLY   C C   1 
ATOM   7765  O  O   . GLY   C  1 121 ? 24.388  42.648  -79.436  1.00 45.24  ? 422  GLY   C O   1 
ATOM   7766  N  N   . ARG   C  1 122 ? 23.028  41.683  -77.939  1.00 41.36  ? 423  ARG   C N   1 
ATOM   7767  C  CA  . ARG   C  1 122 ? 21.795  42.074  -78.608  1.00 37.53  ? 423  ARG   C CA  1 
ATOM   7768  C  C   . ARG   C  1 122 ? 21.600  43.588  -78.789  1.00 37.70  ? 423  ARG   C C   1 
ATOM   7769  O  O   . ARG   C  1 122 ? 20.559  43.971  -79.343  1.00 42.68  ? 423  ARG   C O   1 
ATOM   7770  C  CB  . ARG   C  1 122 ? 20.590  41.531  -77.850  1.00 29.84  ? 423  ARG   C CB  1 
ATOM   7771  C  CG  . ARG   C  1 122 ? 20.391  40.046  -77.987  1.00 28.85  ? 423  ARG   C CG  1 
ATOM   7772  C  CD  . ARG   C  1 122 ? 19.206  39.628  -77.150  1.00 35.93  ? 423  ARG   C CD  1 
ATOM   7773  N  NE  . ARG   C  1 122 ? 19.492  39.638  -75.707  1.00 34.89  ? 423  ARG   C NE  1 
ATOM   7774  C  CZ  . ARG   C  1 122 ? 18.560  39.484  -74.767  1.00 37.67  ? 423  ARG   C CZ  1 
ATOM   7775  N  NH1 . ARG   C  1 122 ? 17.277  39.341  -75.105  1.00 25.96  ? 423  ARG   C NH1 1 
ATOM   7776  N  NH2 . ARG   C  1 122 ? 18.907  39.474  -73.480  1.00 40.07  ? 423  ARG   C NH2 1 
ATOM   7777  N  N   . ILE   C  1 123 ? 22.518  44.466  -78.371  1.00 39.52  ? 424  ILE   C N   1 
ATOM   7778  C  CA  . ILE   C  1 123 ? 22.285  45.879  -78.637  1.00 37.71  ? 424  ILE   C CA  1 
ATOM   7779  C  C   . ILE   C  1 123 ? 22.366  46.176  -80.137  1.00 40.97  ? 424  ILE   C C   1 
ATOM   7780  O  O   . ILE   C  1 123 ? 21.856  47.206  -80.592  1.00 34.47  ? 424  ILE   C O   1 
ATOM   7781  C  CB  . ILE   C  1 123 ? 23.251  46.771  -77.836  1.00 39.29  ? 424  ILE   C CB  1 
ATOM   7782  C  CG1 . ILE   C  1 123 ? 22.720  48.213  -77.786  1.00 31.89  ? 424  ILE   C CG1 1 
ATOM   7783  C  CG2 . ILE   C  1 123 ? 24.657  46.728  -78.383  1.00 25.90  ? 424  ILE   C CG2 1 
ATOM   7784  C  CD1 . ILE   C  1 123 ? 23.423  49.073  -76.771  1.00 39.19  ? 424  ILE   C CD1 1 
ATOM   7785  N  N   . GLN   C  1 124 ? 22.957  45.267  -80.914  1.00 41.19  ? 425  GLN   C N   1 
ATOM   7786  C  CA  . GLN   C  1 124 ? 23.113  45.372  -82.361  1.00 43.82  ? 425  GLN   C CA  1 
ATOM   7787  C  C   . GLN   C  1 124 ? 21.965  44.730  -83.143  1.00 43.50  ? 425  GLN   C C   1 
ATOM   7788  O  O   . GLN   C  1 124 ? 22.011  44.717  -84.376  1.00 47.03  ? 425  GLN   C O   1 
ATOM   7789  C  CB  . GLN   C  1 124 ? 24.437  44.721  -82.767  1.00 45.76  ? 425  GLN   C CB  1 
ATOM   7790  C  CG  . GLN   C  1 124 ? 25.681  45.378  -82.172  1.00 48.20  ? 425  GLN   C CG  1 
ATOM   7791  C  CD  . GLN   C  1 124 ? 26.159  46.537  -83.017  1.00 55.79  ? 425  GLN   C CD  1 
ATOM   7792  O  OE1 . GLN   C  1 124 ? 25.983  46.544  -84.232  1.00 64.95  ? 425  GLN   C OE1 1 
ATOM   7793  N  NE2 . GLN   C  1 124 ? 26.755  47.525  -82.382  1.00 64.93  ? 425  GLN   C NE2 1 
ATOM   7794  N  N   . TRP   C  1 125 ? 20.930  44.233  -82.450  1.00 37.02  ? 426  TRP   C N   1 
ATOM   7795  C  CA  . TRP   C  1 125 ? 19.964  43.303  -83.035  1.00 34.84  ? 426  TRP   C CA  1 
ATOM   7796  C  C   . TRP   C  1 125 ? 19.342  43.825  -84.332  1.00 45.38  ? 426  TRP   C C   1 
ATOM   7797  O  O   . TRP   C  1 125 ? 19.085  43.045  -85.256  1.00 49.49  ? 426  TRP   C O   1 
ATOM   7798  C  CB  . TRP   C  1 125 ? 18.863  42.997  -82.025  1.00 32.60  ? 426  TRP   C CB  1 
ATOM   7799  C  CG  . TRP   C  1 125 ? 17.898  44.129  -81.803  1.00 30.61  ? 426  TRP   C CG  1 
ATOM   7800  C  CD1 . TRP   C  1 125 ? 18.002  45.118  -80.863  1.00 33.07  ? 426  TRP   C CD1 1 
ATOM   7801  C  CD2 . TRP   C  1 125 ? 16.667  44.378  -82.517  1.00 33.92  ? 426  TRP   C CD2 1 
ATOM   7802  N  NE1 . TRP   C  1 125 ? 16.919  45.962  -80.953  1.00 37.87  ? 426  TRP   C NE1 1 
ATOM   7803  C  CE2 . TRP   C  1 125 ? 16.088  45.535  -81.959  1.00 38.07  ? 426  TRP   C CE2 1 
ATOM   7804  C  CE3 . TRP   C  1 125 ? 16.008  43.740  -83.572  1.00 41.70  ? 426  TRP   C CE3 1 
ATOM   7805  C  CZ2 . TRP   C  1 125 ? 14.869  46.063  -82.415  1.00 34.44  ? 426  TRP   C CZ2 1 
ATOM   7806  C  CZ3 . TRP   C  1 125 ? 14.797  44.275  -84.036  1.00 40.35  ? 426  TRP   C CZ3 1 
ATOM   7807  C  CH2 . TRP   C  1 125 ? 14.249  45.424  -83.456  1.00 39.79  ? 426  TRP   C CH2 1 
ATOM   7808  N  N   . SER   C  1 126 ? 19.060  45.126  -84.409  1.00 43.21  ? 427  SER   C N   1 
ATOM   7809  C  CA  . SER   C  1 126 ? 18.412  45.686  -85.588  1.00 44.48  ? 427  SER   C CA  1 
ATOM   7810  C  C   . SER   C  1 126 ? 19.365  45.875  -86.765  1.00 51.77  ? 427  SER   C C   1 
ATOM   7811  O  O   . SER   C  1 126 ? 18.911  46.196  -87.872  1.00 62.53  ? 427  SER   C O   1 
ATOM   7812  C  CB  . SER   C  1 126 ? 17.773  47.022  -85.244  1.00 42.14  ? 427  SER   C CB  1 
ATOM   7813  O  OG  . SER   C  1 126 ? 18.780  47.971  -84.984  1.00 52.71  ? 427  SER   C OG  1 
ATOM   7814  N  N   . LYS   C  1 127 ? 20.660  45.677  -86.556  1.00 50.91  ? 428  LYS   C N   1 
ATOM   7815  C  CA  . LYS   C  1 127 ? 21.676  45.851  -87.583  1.00 50.07  ? 428  LYS   C CA  1 
ATOM   7816  C  C   . LYS   C  1 127 ? 22.222  44.479  -87.971  1.00 59.69  ? 428  LYS   C C   1 
ATOM   7817  O  O   . LYS   C  1 127 ? 23.366  44.129  -87.678  1.00 76.40  ? 428  LYS   C O   1 
ATOM   7818  C  CB  . LYS   C  1 127 ? 22.774  46.782  -87.060  1.00 47.83  ? 428  LYS   C CB  1 
ATOM   7819  C  CG  . LYS   C  1 127 ? 23.727  47.245  -88.116  1.00 64.81  ? 428  LYS   C CG  1 
ATOM   7820  C  CD  . LYS   C  1 127 ? 25.177  47.095  -87.679  1.00 73.54  ? 428  LYS   C CD  1 
ATOM   7821  C  CE  . LYS   C  1 127 ? 26.124  47.407  -88.843  1.00 77.32  ? 428  LYS   C CE  1 
ATOM   7822  N  NZ  . LYS   C  1 127 ? 25.952  48.791  -89.383  1.00 75.80  ? 428  LYS   C NZ  1 
ATOM   7823  N  N   . LEU   C  1 128 ? 21.373  43.679  -88.610  1.00 50.25  ? 429  LEU   C N   1 
ATOM   7824  C  CA  . LEU   C  1 128 ? 21.703  42.315  -89.006  1.00 41.25  ? 429  LEU   C CA  1 
ATOM   7825  C  C   . LEU   C  1 128 ? 21.498  42.184  -90.505  1.00 37.32  ? 429  LEU   C C   1 
ATOM   7826  O  O   . LEU   C  1 128 ? 20.427  42.520  -91.007  1.00 43.20  ? 429  LEU   C O   1 
ATOM   7827  C  CB  . LEU   C  1 128 ? 20.824  41.294  -88.279  1.00 27.44  ? 429  LEU   C CB  1 
ATOM   7828  C  CG  . LEU   C  1 128 ? 20.944  39.829  -88.683  1.00 25.14  ? 429  LEU   C CG  1 
ATOM   7829  C  CD1 . LEU   C  1 128 ? 22.228  39.166  -88.157  1.00 22.83  ? 429  LEU   C CD1 1 
ATOM   7830  C  CD2 . LEU   C  1 128 ? 19.728  39.059  -88.229  1.00 32.37  ? 429  LEU   C CD2 1 
ATOM   7831  N  N   . GLN   C  1 129 ? 22.506  41.696  -91.217  1.00 34.61  ? 430  GLN   C N   1 
ATOM   7832  C  CA  . GLN   C  1 129 ? 22.380  41.464  -92.656  1.00 37.42  ? 430  GLN   C CA  1 
ATOM   7833  C  C   . GLN   C  1 129 ? 21.763  40.081  -92.878  1.00 35.20  ? 430  GLN   C C   1 
ATOM   7834  O  O   . GLN   C  1 129 ? 22.303  39.080  -92.402  1.00 46.17  ? 430  GLN   C O   1 
ATOM   7835  C  CB  . GLN   C  1 129 ? 23.749  41.588  -93.321  1.00 42.49  ? 430  GLN   C CB  1 
ATOM   7836  C  CG  . GLN   C  1 129 ? 23.773  41.418  -94.842  1.00 50.05  ? 430  GLN   C CG  1 
ATOM   7837  C  CD  . GLN   C  1 129 ? 22.820  42.343  -95.554  1.00 50.28  ? 430  GLN   C CD  1 
ATOM   7838  O  OE1 . GLN   C  1 129 ? 22.688  43.513  -95.198  1.00 50.99  ? 430  GLN   C OE1 1 
ATOM   7839  N  NE2 . GLN   C  1 129 ? 22.134  41.818  -96.561  1.00 58.64  ? 430  GLN   C NE2 1 
ATOM   7840  N  N   . VAL   C  1 130 ? 20.613  40.025  -93.557  1.00 39.28  ? 431  VAL   C N   1 
ATOM   7841  C  CA  . VAL   C  1 130 ? 19.889  38.769  -93.796  1.00 39.42  ? 431  VAL   C CA  1 
ATOM   7842  C  C   . VAL   C  1 130 ? 20.116  38.312  -95.235  1.00 42.35  ? 431  VAL   C C   1 
ATOM   7843  O  O   . VAL   C  1 130 ? 19.756  39.017  -96.184  1.00 49.60  ? 431  VAL   C O   1 
ATOM   7844  C  CB  . VAL   C  1 130 ? 18.383  38.913  -93.522  1.00 41.41  ? 431  VAL   C CB  1 
ATOM   7845  C  CG1 . VAL   C  1 130 ? 17.661  37.573  -93.804  1.00 35.42  ? 431  VAL   C CG1 1 
ATOM   7846  C  CG2 . VAL   C  1 130 ? 18.132  39.383  -92.096  1.00 49.82  ? 431  VAL   C CG2 1 
ATOM   7847  N  N   . PHE   C  1 131 ? 20.688  37.125  -95.400  1.00 42.38  ? 432  PHE   C N   1 
ATOM   7848  C  CA  . PHE   C  1 131 ? 20.887  36.515  -96.710  1.00 34.69  ? 432  PHE   C CA  1 
ATOM   7849  C  C   . PHE   C  1 131 ? 19.814  35.461  -96.902  1.00 41.16  ? 432  PHE   C C   1 
ATOM   7850  O  O   . PHE   C  1 131 ? 19.832  34.415  -96.242  1.00 39.07  ? 432  PHE   C O   1 
ATOM   7851  C  CB  . PHE   C  1 131 ? 22.283  35.917  -96.825  1.00 32.73  ? 432  PHE   C CB  1 
ATOM   7852  C  CG  . PHE   C  1 131 ? 23.350  36.947  -96.801  1.00 34.77  ? 432  PHE   C CG  1 
ATOM   7853  C  CD1 . PHE   C  1 131 ? 23.298  38.029  -97.675  1.00 25.69  ? 432  PHE   C CD1 1 
ATOM   7854  C  CD2 . PHE   C  1 131 ? 24.379  36.878  -95.881  1.00 34.19  ? 432  PHE   C CD2 1 
ATOM   7855  C  CE1 . PHE   C  1 131 ? 24.263  39.019  -97.623  1.00 46.31  ? 432  PHE   C CE1 1 
ATOM   7856  C  CE2 . PHE   C  1 131 ? 25.360  37.866  -95.835  1.00 38.46  ? 432  PHE   C CE2 1 
ATOM   7857  C  CZ  . PHE   C  1 131 ? 25.304  38.937  -96.702  1.00 37.33  ? 432  PHE   C CZ  1 
ATOM   7858  N  N   . ASP   C  1 132 ? 18.866  35.756  -97.782  1.00 38.08  ? 433  ASP   C N   1 
ATOM   7859  C  CA  . ASP   C  1 132 ? 17.800  34.823  -98.111  1.00 41.47  ? 433  ASP   C CA  1 
ATOM   7860  C  C   . ASP   C  1 132 ? 18.354  33.757  -99.054  1.00 43.77  ? 433  ASP   C C   1 
ATOM   7861  O  O   . ASP   C  1 132 ? 18.825  34.078  -100.143 1.00 48.21  ? 433  ASP   C O   1 
ATOM   7862  C  CB  . ASP   C  1 132 ? 16.635  35.592  -98.732  1.00 32.06  ? 433  ASP   C CB  1 
ATOM   7863  C  CG  . ASP   C  1 132 ? 15.440  34.731  -99.013  1.00 36.64  ? 433  ASP   C CG  1 
ATOM   7864  O  OD1 . ASP   C  1 132 ? 15.504  33.499  -98.825  1.00 35.67  ? 433  ASP   C OD1 1 
ATOM   7865  O  OD2 . ASP   C  1 132 ? 14.415  35.303  -99.438  1.00 48.35  ? 433  ASP   C OD2 1 
ATOM   7866  N  N   . ALA   C  1 133 ? 18.339  32.502  -98.619  1.00 45.42  ? 434  ALA   C N   1 
ATOM   7867  C  CA  . ALA   C  1 133 ? 18.876  31.390  -99.392  1.00 39.66  ? 434  ALA   C CA  1 
ATOM   7868  C  C   . ALA   C  1 133 ? 17.830  30.303  -99.531  1.00 34.86  ? 434  ALA   C C   1 
ATOM   7869  O  O   . ALA   C  1 133 ? 18.153  29.115  -99.656  1.00 28.87  ? 434  ALA   C O   1 
ATOM   7870  C  CB  . ALA   C  1 133 ? 20.147  30.824  -98.756  1.00 33.89  ? 434  ALA   C CB  1 
ATOM   7871  N  N   . ARG   C  1 134 ? 16.565  30.705  -99.494  1.00 32.01  ? 435  ARG   C N   1 
ATOM   7872  C  CA  . ARG   C  1 134 ? 15.490  29.734  -99.551  1.00 37.68  ? 435  ARG   C CA  1 
ATOM   7873  C  C   . ARG   C  1 134 ? 15.293  29.162  -100.939 1.00 39.07  ? 435  ARG   C C   1 
ATOM   7874  O  O   . ARG   C  1 134 ? 14.427  28.307  -101.117 1.00 46.60  ? 435  ARG   C O   1 
ATOM   7875  C  CB  . ARG   C  1 134 ? 14.196  30.374  -99.058  1.00 42.17  ? 435  ARG   C CB  1 
ATOM   7876  C  CG  . ARG   C  1 134 ? 14.209  30.700  -97.588  1.00 41.38  ? 435  ARG   C CG  1 
ATOM   7877  C  CD  . ARG   C  1 134 ? 12.937  31.407  -97.226  1.00 38.16  ? 435  ARG   C CD  1 
ATOM   7878  N  NE  . ARG   C  1 134 ? 12.897  32.751  -97.774  1.00 36.90  ? 435  ARG   C NE  1 
ATOM   7879  C  CZ  . ARG   C  1 134 ? 11.787  33.467  -97.862  1.00 35.92  ? 435  ARG   C CZ  1 
ATOM   7880  N  NH1 . ARG   C  1 134 ? 10.640  32.951  -97.437  1.00 36.03  ? 435  ARG   C NH1 1 
ATOM   7881  N  NH2 . ARG   C  1 134 ? 11.819  34.690  -98.368  1.00 35.22  ? 435  ARG   C NH2 1 
ATOM   7882  N  N   . ASP   C  1 135 ? 16.058  29.608  -101.926 1.00 39.62  ? 436  ASP   C N   1 
ATOM   7883  C  CA  . ASP   C  1 135 ? 15.999  28.983  -103.232 1.00 39.16  ? 436  ASP   C CA  1 
ATOM   7884  C  C   . ASP   C  1 135 ? 17.024  27.872  -103.360 1.00 43.46  ? 436  ASP   C C   1 
ATOM   7885  O  O   . ASP   C  1 135 ? 17.075  27.206  -104.398 1.00 39.91  ? 436  ASP   C O   1 
ATOM   7886  C  CB  . ASP   C  1 135 ? 16.191  30.030  -104.332 1.00 35.79  ? 436  ASP   C CB  1 
ATOM   7887  C  CG  . ASP   C  1 135 ? 17.563  30.661  -104.293 1.00 45.63  ? 436  ASP   C CG  1 
ATOM   7888  O  OD1 . ASP   C  1 135 ? 18.288  30.412  -103.306 1.00 45.61  ? 436  ASP   C OD1 1 
ATOM   7889  O  OD2 . ASP   C  1 135 ? 17.920  31.403  -105.237 1.00 47.56  ? 436  ASP   C OD2 1 
ATOM   7890  N  N   . CYS   C  1 136 ? 17.839  27.665  -102.331 1.00 40.67  ? 437  CYS   C N   1 
ATOM   7891  C  CA  . CYS   C  1 136 ? 18.890  26.660  -102.404 1.00 43.28  ? 437  CYS   C CA  1 
ATOM   7892  C  C   . CYS   C  1 136 ? 18.289  25.266  -102.552 1.00 48.67  ? 437  CYS   C C   1 
ATOM   7893  O  O   . CYS   C  1 136 ? 17.204  24.980  -102.035 1.00 50.91  ? 437  CYS   C O   1 
ATOM   7894  C  CB  . CYS   C  1 136 ? 19.768  26.737  -101.160 1.00 33.20  ? 437  CYS   C CB  1 
ATOM   7895  S  SG  . CYS   C  1 136 ? 21.321  25.843  -101.262 1.00 39.80  ? 437  CYS   C SG  1 
ATOM   7896  N  N   . THR   C  1 137 ? 18.981  24.398  -103.302 1.00 41.68  ? 438  THR   C N   1 
ATOM   7897  C  CA  . THR   C  1 137 ? 18.509  23.033  -103.502 1.00 33.44  ? 438  THR   C CA  1 
ATOM   7898  C  C   . THR   C  1 137 ? 19.544  21.946  -103.254 1.00 36.28  ? 438  THR   C C   1 
ATOM   7899  O  O   . THR   C  1 137 ? 19.142  20.789  -103.108 1.00 39.52  ? 438  THR   C O   1 
ATOM   7900  C  CB  . THR   C  1 137 ? 17.958  22.836  -104.925 1.00 43.55  ? 438  THR   C CB  1 
ATOM   7901  O  OG1 . THR   C  1 137 ? 19.037  22.588  -105.839 1.00 38.79  ? 438  THR   C OG1 1 
ATOM   7902  C  CG2 . THR   C  1 137 ? 17.177  24.044  -105.375 1.00 42.69  ? 438  THR   C CG2 1 
ATOM   7903  N  N   . THR   C  1 138 ? 20.846  22.248  -103.225 1.00 39.86  ? 439  THR   C N   1 
ATOM   7904  C  CA  . THR   C  1 138 ? 21.854  21.205  -103.059 1.00 36.22  ? 439  THR   C CA  1 
ATOM   7905  C  C   . THR   C  1 138 ? 22.925  21.639  -102.071 1.00 38.12  ? 439  THR   C C   1 
ATOM   7906  O  O   . THR   C  1 138 ? 23.089  22.825  -101.767 1.00 41.64  ? 439  THR   C O   1 
ATOM   7907  C  CB  . THR   C  1 138 ? 22.583  20.828  -104.366 1.00 42.60  ? 439  THR   C CB  1 
ATOM   7908  O  OG1 . THR   C  1 138 ? 23.450  21.909  -104.754 1.00 42.71  ? 439  THR   C OG1 1 
ATOM   7909  C  CG2 . THR   C  1 138 ? 21.598  20.482  -105.487 1.00 35.32  ? 439  THR   C CG2 1 
ATOM   7910  N  N   . ALA   C  1 139 ? 23.692  20.639  -101.612 1.00 45.76  ? 440  ALA   C N   1 
ATOM   7911  C  CA  . ALA   C  1 139 ? 24.820  20.902  -100.723 1.00 43.51  ? 440  ALA   C CA  1 
ATOM   7912  C  C   . ALA   C  1 139 ? 25.830  21.847  -101.370 1.00 43.43  ? 440  ALA   C C   1 
ATOM   7913  O  O   . ALA   C  1 139 ? 26.413  22.701  -100.687 1.00 51.47  ? 440  ALA   C O   1 
ATOM   7914  C  CB  . ALA   C  1 139 ? 25.484  19.585  -100.317 1.00 41.94  ? 440  ALA   C CB  1 
ATOM   7915  N  N   . HIS   C  1 140 ? 26.046  21.712  -102.687 1.00 48.40  ? 441  HIS   C N   1 
ATOM   7916  C  CA  . HIS   C  1 140 ? 26.902  22.651  -103.417 1.00 43.58  ? 441  HIS   C CA  1 
ATOM   7917  C  C   . HIS   C  1 140 ? 26.379  24.072  -103.301 1.00 34.47  ? 441  HIS   C C   1 
ATOM   7918  O  O   . HIS   C  1 140 ? 27.132  24.998  -102.985 1.00 35.24  ? 441  HIS   C O   1 
ATOM   7919  C  CB  . HIS   C  1 140 ? 27.022  22.240  -104.894 1.00 38.83  ? 441  HIS   C CB  1 
ATOM   7920  C  CG  . HIS   C  1 140 ? 28.089  21.220  -105.149 1.00 45.17  ? 441  HIS   C CG  1 
ATOM   7921  N  ND1 . HIS   C  1 140 ? 27.846  19.864  -105.120 1.00 48.77  ? 441  HIS   C ND1 1 
ATOM   7922  C  CD2 . HIS   C  1 140 ? 29.414  21.358  -105.397 1.00 49.96  ? 441  HIS   C CD2 1 
ATOM   7923  C  CE1 . HIS   C  1 140 ? 28.971  19.213  -105.360 1.00 52.96  ? 441  HIS   C CE1 1 
ATOM   7924  N  NE2 . HIS   C  1 140 ? 29.939  20.096  -105.526 1.00 49.20  ? 441  HIS   C NE2 1 
ATOM   7925  N  N   . GLY   C  1 141 ? 25.090  24.268  -103.564 1.00 32.80  ? 442  GLY   C N   1 
ATOM   7926  C  CA  . GLY   C  1 141 ? 24.505  25.579  -103.356 1.00 32.89  ? 442  GLY   C CA  1 
ATOM   7927  C  C   . GLY   C  1 141 ? 24.626  26.061  -101.918 1.00 41.85  ? 442  GLY   C C   1 
ATOM   7928  O  O   . GLY   C  1 141 ? 24.863  27.248  -101.670 1.00 45.65  ? 442  GLY   C O   1 
ATOM   7929  N  N   . MET   C  1 142 ? 24.466  25.153  -100.949 1.00 34.31  ? 443  MET   C N   1 
ATOM   7930  C  CA  . MET   C  1 142 ? 24.664  25.546  -99.553  1.00 36.26  ? 443  MET   C CA  1 
ATOM   7931  C  C   . MET   C  1 142 ? 26.090  26.006  -99.328  1.00 39.49  ? 443  MET   C C   1 
ATOM   7932  O  O   . MET   C  1 142 ? 26.340  26.930  -98.548  1.00 42.49  ? 443  MET   C O   1 
ATOM   7933  C  CB  . MET   C  1 142 ? 24.336  24.387  -98.612  1.00 33.15  ? 443  MET   C CB  1 
ATOM   7934  C  CG  . MET   C  1 142 ? 22.884  24.076  -98.475  1.00 31.84  ? 443  MET   C CG  1 
ATOM   7935  S  SD  . MET   C  1 142 ? 22.651  22.596  -97.448  1.00 43.04  ? 443  MET   C SD  1 
ATOM   7936  C  CE  . MET   C  1 142 ? 23.026  23.243  -95.797  1.00 35.79  ? 443  MET   C CE  1 
ATOM   7937  N  N   . PHE   C  1 143 ? 27.043  25.369  -100.006 1.00 40.95  ? 444  PHE   C N   1 
ATOM   7938  C  CA  . PHE   C  1 143 ? 28.433  25.756  -99.829  1.00 37.89  ? 444  PHE   C CA  1 
ATOM   7939  C  C   . PHE   C  1 143 ? 28.688  27.129  -100.429 1.00 39.00  ? 444  PHE   C C   1 
ATOM   7940  O  O   . PHE   C  1 143 ? 29.397  27.952  -99.836  1.00 39.20  ? 444  PHE   C O   1 
ATOM   7941  C  CB  . PHE   C  1 143 ? 29.345  24.683  -100.430 1.00 40.66  ? 444  PHE   C CB  1 
ATOM   7942  C  CG  . PHE   C  1 143 ? 30.792  25.083  -100.508 1.00 39.82  ? 444  PHE   C CG  1 
ATOM   7943  C  CD1 . PHE   C  1 143 ? 31.575  25.137  -99.371  1.00 40.95  ? 444  PHE   C CD1 1 
ATOM   7944  C  CD2 . PHE   C  1 143 ? 31.367  25.399  -101.719 1.00 33.75  ? 444  PHE   C CD2 1 
ATOM   7945  C  CE1 . PHE   C  1 143 ? 32.906  25.490  -99.440  1.00 42.66  ? 444  PHE   C CE1 1 
ATOM   7946  C  CE2 . PHE   C  1 143 ? 32.701  25.764  -101.792 1.00 44.30  ? 444  PHE   C CE2 1 
ATOM   7947  C  CZ  . PHE   C  1 143 ? 33.467  25.812  -100.648 1.00 45.49  ? 444  PHE   C CZ  1 
ATOM   7948  N  N   . ASN   C  1 144 ? 28.098  27.402  -101.595 1.00 45.00  ? 445  ASN   C N   1 
ATOM   7949  C  CA  . ASN   C  1 144 ? 28.262  28.706  -102.233 1.00 42.80  ? 445  ASN   C CA  1 
ATOM   7950  C  C   . ASN   C  1 144 ? 27.709  29.823  -101.350 1.00 43.11  ? 445  ASN   C C   1 
ATOM   7951  O  O   . ASN   C  1 144 ? 28.323  30.894  -101.215 1.00 36.66  ? 445  ASN   C O   1 
ATOM   7952  C  CB  . ASN   C  1 144 ? 27.572  28.691  -103.604 1.00 43.08  ? 445  ASN   C CB  1 
ATOM   7953  C  CG  . ASN   C  1 144 ? 27.656  30.026  -104.327 1.00 50.00  ? 445  ASN   C CG  1 
ATOM   7954  O  OD1 . ASN   C  1 144 ? 26.638  30.640  -104.660 1.00 55.56  ? 445  ASN   C OD1 1 
ATOM   7955  N  ND2 . ASN   C  1 144 ? 28.866  30.472  -104.582 1.00 45.90  ? 445  ASN   C ND2 1 
ATOM   7956  N  N   . TYR   C  1 145 ? 26.549  29.584  -100.737 1.00 38.29  ? 446  TYR   C N   1 
ATOM   7957  C  CA  . TYR   C  1 145 ? 25.929  30.591  -99.879  1.00 47.05  ? 446  TYR   C CA  1 
ATOM   7958  C  C   . TYR   C  1 145 ? 26.746  30.833  -98.611  1.00 42.70  ? 446  TYR   C C   1 
ATOM   7959  O  O   . TYR   C  1 145 ? 26.945  31.983  -98.201  1.00 36.39  ? 446  TYR   C O   1 
ATOM   7960  C  CB  . TYR   C  1 145 ? 24.523  30.150  -99.510  1.00 42.71  ? 446  TYR   C CB  1 
ATOM   7961  C  CG  . TYR   C  1 145 ? 23.415  30.612  -100.428 1.00 42.47  ? 446  TYR   C CG  1 
ATOM   7962  C  CD1 . TYR   C  1 145 ? 23.079  31.951  -100.515 1.00 27.87  ? 446  TYR   C CD1 1 
ATOM   7963  C  CD2 . TYR   C  1 145 ? 22.656  29.693  -101.155 1.00 34.63  ? 446  TYR   C CD2 1 
ATOM   7964  C  CE1 . TYR   C  1 145 ? 22.041  32.367  -101.306 1.00 29.58  ? 446  TYR   C CE1 1 
ATOM   7965  C  CE2 . TYR   C  1 145 ? 21.617  30.106  -101.941 1.00 29.04  ? 446  TYR   C CE2 1 
ATOM   7966  C  CZ  . TYR   C  1 145 ? 21.315  31.450  -102.011 1.00 36.18  ? 446  TYR   C CZ  1 
ATOM   7967  O  OH  . TYR   C  1 145 ? 20.287  31.890  -102.804 1.00 45.32  ? 446  TYR   C OH  1 
ATOM   7968  N  N   . ILE   C  1 146 ? 27.228  29.756  -97.984  1.00 41.30  ? 447  ILE   C N   1 
ATOM   7969  C  CA  . ILE   C  1 146 ? 28.013  29.878  -96.759  1.00 40.71  ? 447  ILE   C CA  1 
ATOM   7970  C  C   . ILE   C  1 146 ? 29.325  30.602  -97.035  1.00 43.34  ? 447  ILE   C C   1 
ATOM   7971  O  O   . ILE   C  1 146 ? 29.770  31.444  -96.242  1.00 41.59  ? 447  ILE   C O   1 
ATOM   7972  C  CB  . ILE   C  1 146 ? 28.226  28.478  -96.155  1.00 38.69  ? 447  ILE   C CB  1 
ATOM   7973  C  CG1 . ILE   C  1 146 ? 26.915  27.974  -95.548  1.00 34.74  ? 447  ILE   C CG1 1 
ATOM   7974  C  CG2 . ILE   C  1 146 ? 29.311  28.490  -95.104  1.00 32.98  ? 447  ILE   C CG2 1 
ATOM   7975  C  CD1 . ILE   C  1 146 ? 26.882  26.484  -95.292  1.00 28.42  ? 447  ILE   C CD1 1 
ATOM   7976  N  N   . CYS   C  1 147 ? 29.950  30.312  -98.178  1.00 34.66  ? 448  CYS   C N   1 
ATOM   7977  C  CA  . CYS   C  1 147 ? 31.171  31.016  -98.545  1.00 35.11  ? 448  CYS   C CA  1 
ATOM   7978  C  C   . CYS   C  1 147 ? 30.931  32.510  -98.680  1.00 39.92  ? 448  CYS   C C   1 
ATOM   7979  O  O   . CYS   C  1 147 ? 31.761  33.320  -98.251  1.00 34.80  ? 448  CYS   C O   1 
ATOM   7980  C  CB  . CYS   C  1 147 ? 31.733  30.461  -99.851  1.00 35.60  ? 448  CYS   C CB  1 
ATOM   7981  S  SG  . CYS   C  1 147 ? 32.666  28.941  -99.663  1.00 39.86  ? 448  CYS   C SG  1 
ATOM   7982  N  N   . ASN   C  1 148 ? 29.818  32.900  -99.302  1.00 42.03  ? 449  ASN   C N   1 
ATOM   7983  C  CA  . ASN   C  1 148 ? 29.540  34.324  -99.440  1.00 32.40  ? 449  ASN   C CA  1 
ATOM   7984  C  C   . ASN   C  1 148 ? 29.229  34.948  -98.082  1.00 35.92  ? 449  ASN   C C   1 
ATOM   7985  O  O   . ASN   C  1 148 ? 29.606  36.096  -97.816  1.00 35.87  ? 449  ASN   C O   1 
ATOM   7986  C  CB  . ASN   C  1 148 ? 28.391  34.548  -100.421 1.00 31.82  ? 449  ASN   C CB  1 
ATOM   7987  C  CG  . ASN   C  1 148 ? 28.701  34.029  -101.836 1.00 38.64  ? 449  ASN   C CG  1 
ATOM   7988  O  OD1 . ASN   C  1 148 ? 29.861  33.911  -102.243 1.00 30.62  ? 449  ASN   C OD1 1 
ATOM   7989  N  ND2 . ASN   C  1 148 ? 27.649  33.699  -102.574 1.00 30.84  ? 449  ASN   C ND2 1 
ATOM   7990  N  N   . HIS   C  1 149 ? 28.539  34.204  -97.214  1.00 32.57  ? 450  HIS   C N   1 
ATOM   7991  C  CA  . HIS   C  1 149 ? 28.294  34.667  -95.852  1.00 34.43  ? 450  HIS   C CA  1 
ATOM   7992  C  C   . HIS   C  1 149 ? 29.607  34.977  -95.144  1.00 33.48  ? 450  HIS   C C   1 
ATOM   7993  O  O   . HIS   C  1 149 ? 29.804  36.081  -94.618  1.00 31.80  ? 450  HIS   C O   1 
ATOM   7994  C  CB  . HIS   C  1 149 ? 27.498  33.600  -95.084  1.00 35.82  ? 450  HIS   C CB  1 
ATOM   7995  C  CG  . HIS   C  1 149 ? 27.163  33.979  -93.665  1.00 39.45  ? 450  HIS   C CG  1 
ATOM   7996  N  ND1 . HIS   C  1 149 ? 25.941  33.698  -93.093  1.00 39.71  ? 450  HIS   C ND1 1 
ATOM   7997  C  CD2 . HIS   C  1 149 ? 27.892  34.597  -92.704  1.00 40.47  ? 450  HIS   C CD2 1 
ATOM   7998  C  CE1 . HIS   C  1 149 ? 25.924  34.143  -91.848  1.00 41.98  ? 450  HIS   C CE1 1 
ATOM   7999  N  NE2 . HIS   C  1 149 ? 27.095  34.692  -91.586  1.00 43.77  ? 450  HIS   C NE2 1 
ATOM   8000  N  N   . VAL   C  1 150 ? 30.515  34.003  -95.131  1.00 32.53  ? 451  VAL   C N   1 
ATOM   8001  C  CA  . VAL   C  1 150 ? 31.771  34.140  -94.412  1.00 25.94  ? 451  VAL   C CA  1 
ATOM   8002  C  C   . VAL   C  1 150 ? 32.571  35.316  -94.945  1.00 41.29  ? 451  VAL   C C   1 
ATOM   8003  O  O   . VAL   C  1 150 ? 33.223  36.037  -94.179  1.00 33.38  ? 451  VAL   C O   1 
ATOM   8004  C  CB  . VAL   C  1 150 ? 32.552  32.815  -94.492  1.00 27.44  ? 451  VAL   C CB  1 
ATOM   8005  C  CG1 . VAL   C  1 150 ? 33.976  32.986  -94.037  1.00 27.08  ? 451  VAL   C CG1 1 
ATOM   8006  C  CG2 . VAL   C  1 150 ? 31.840  31.744  -93.642  1.00 25.92  ? 451  VAL   C CG2 1 
ATOM   8007  N  N   . LYS   C  1 151 ? 32.532  35.538  -96.267  1.00 44.76  ? 452  LYS   C N   1 
ATOM   8008  C  CA  . LYS   C  1 151 ? 33.321  36.616  -96.853  1.00 33.53  ? 452  LYS   C CA  1 
ATOM   8009  C  C   . LYS   C  1 151 ? 32.713  37.966  -96.511  1.00 33.63  ? 452  LYS   C C   1 
ATOM   8010  O  O   . LYS   C  1 151 ? 33.420  38.884  -96.081  1.00 36.29  ? 452  LYS   C O   1 
ATOM   8011  C  CB  . LYS   C  1 151 ? 33.447  36.431  -98.375  1.00 33.10  ? 452  LYS   C CB  1 
ATOM   8012  C  CG  . LYS   C  1 151 ? 34.428  37.404  -99.047  1.00 34.04  ? 452  LYS   C CG  1 
ATOM   8013  C  CD  . LYS   C  1 151 ? 34.609  37.078  -100.570 1.00 33.94  ? 452  LYS   C CD  1 
ATOM   8014  C  CE  . LYS   C  1 151 ? 35.643  37.985  -101.243 1.00 33.02  ? 452  LYS   C CE  1 
ATOM   8015  N  NZ  . LYS   C  1 151 ? 35.958  37.597  -102.674 1.00 47.17  ? 452  LYS   C NZ  1 
ATOM   8016  N  N   . TYR   C  1 152 ? 31.395  38.097  -96.667  1.00 35.51  ? 453  TYR   C N   1 
ATOM   8017  C  CA  . TYR   C  1 152 ? 30.731  39.344  -96.302  1.00 35.55  ? 453  TYR   C CA  1 
ATOM   8018  C  C   . TYR   C  1 152 ? 30.932  39.668  -94.825  1.00 35.46  ? 453  TYR   C C   1 
ATOM   8019  O  O   . TYR   C  1 152 ? 31.284  40.798  -94.470  1.00 40.69  ? 453  TYR   C O   1 
ATOM   8020  C  CB  . TYR   C  1 152 ? 29.239  39.263  -96.635  1.00 33.73  ? 453  TYR   C CB  1 
ATOM   8021  C  CG  . TYR   C  1 152 ? 28.467  40.431  -96.081  1.00 36.50  ? 453  TYR   C CG  1 
ATOM   8022  C  CD1 . TYR   C  1 152 ? 27.950  40.394  -94.788  1.00 36.24  ? 453  TYR   C CD1 1 
ATOM   8023  C  CD2 . TYR   C  1 152 ? 28.297  41.591  -96.824  1.00 31.52  ? 453  TYR   C CD2 1 
ATOM   8024  C  CE1 . TYR   C  1 152 ? 27.269  41.463  -94.266  1.00 38.12  ? 453  TYR   C CE1 1 
ATOM   8025  C  CE2 . TYR   C  1 152 ? 27.599  42.672  -96.313  1.00 34.55  ? 453  TYR   C CE2 1 
ATOM   8026  C  CZ  . TYR   C  1 152 ? 27.089  42.599  -95.031  1.00 42.90  ? 453  TYR   C CZ  1 
ATOM   8027  O  OH  . TYR   C  1 152 ? 26.400  43.667  -94.503  1.00 50.70  ? 453  TYR   C OH  1 
ATOM   8028  N  N   . ALA   C  1 153 ? 30.714  38.680  -93.951  1.00 35.61  ? 454  ALA   C N   1 
ATOM   8029  C  CA  . ALA   C  1 153 ? 30.761  38.904  -92.501  1.00 34.95  ? 454  ALA   C CA  1 
ATOM   8030  C  C   . ALA   C  1 153 ? 32.170  39.173  -91.996  1.00 38.20  ? 454  ALA   C C   1 
ATOM   8031  O  O   . ALA   C  1 153 ? 32.346  39.945  -91.038  1.00 34.74  ? 454  ALA   C O   1 
ATOM   8032  C  CB  . ALA   C  1 153 ? 30.186  37.695  -91.760  1.00 26.21  ? 454  ALA   C CB  1 
ATOM   8033  N  N   . THR   C  1 154 ? 33.175  38.511  -92.586  1.00 36.52  ? 455  THR   C N   1 
ATOM   8034  C  CA  . THR   C  1 154 ? 34.559  38.734  -92.175  1.00 37.71  ? 455  THR   C CA  1 
ATOM   8035  C  C   . THR   C  1 154 ? 34.999  40.148  -92.529  1.00 42.95  ? 455  THR   C C   1 
ATOM   8036  O  O   . THR   C  1 154 ? 35.593  40.849  -91.701  1.00 38.70  ? 455  THR   C O   1 
ATOM   8037  C  CB  . THR   C  1 154 ? 35.490  37.705  -92.833  1.00 41.11  ? 455  THR   C CB  1 
ATOM   8038  O  OG1 . THR   C  1 154 ? 35.106  36.378  -92.466  1.00 34.34  ? 455  THR   C OG1 1 
ATOM   8039  C  CG2 . THR   C  1 154 ? 36.944  37.946  -92.446  1.00 33.56  ? 455  THR   C CG2 1 
ATOM   8040  N  N   . ASN   C  1 155 ? 34.724  40.575  -93.771  1.00 49.28  ? 456  ASN   C N   1 
ATOM   8041  C  CA  . ASN   C  1 155 ? 34.949  41.955  -94.227  1.00 40.01  ? 456  ASN   C CA  1 
ATOM   8042  C  C   . ASN   C  1 155 ? 36.345  42.445  -93.834  1.00 42.92  ? 456  ASN   C C   1 
ATOM   8043  O  O   . ASN   C  1 155 ? 36.529  43.542  -93.299  1.00 41.29  ? 456  ASN   C O   1 
ATOM   8044  C  CB  . ASN   C  1 155 ? 33.854  42.886  -93.689  1.00 37.99  ? 456  ASN   C CB  1 
ATOM   8045  C  CG  . ASN   C  1 155 ? 33.927  44.293  -94.268  1.00 45.52  ? 456  ASN   C CG  1 
ATOM   8046  O  OD1 . ASN   C  1 155 ? 34.291  44.489  -95.428  1.00 47.80  ? 456  ASN   C OD1 1 
ATOM   8047  N  ND2 . ASN   C  1 155 ? 33.569  45.281  -93.461  1.00 45.27  ? 456  ASN   C ND2 1 
ATOM   8048  N  N   . LYS   C  1 156 ? 37.340  41.590  -94.081  1.00 40.54  ? 457  LYS   C N   1 
ATOM   8049  C  CA  . LYS   C  1 156 ? 38.750  41.915  -93.876  1.00 47.28  ? 457  LYS   C CA  1 
ATOM   8050  C  C   . LYS   C  1 156 ? 39.054  42.291  -92.425  1.00 48.67  ? 457  LYS   C C   1 
ATOM   8051  O  O   . LYS   C  1 156 ? 39.990  43.042  -92.152  1.00 53.61  ? 457  LYS   C O   1 
ATOM   8052  C  CB  . LYS   C  1 156 ? 39.201  43.024  -94.836  1.00 45.07  ? 457  LYS   C CB  1 
ATOM   8053  C  CG  . LYS   C  1 156 ? 39.243  42.588  -96.300  1.00 45.03  ? 457  LYS   C CG  1 
ATOM   8054  C  CD  . LYS   C  1 156 ? 39.602  43.751  -97.220  1.00 53.14  ? 457  LYS   C CD  1 
ATOM   8055  C  CE  . LYS   C  1 156 ? 39.670  43.323  -98.676  1.00 65.94  ? 457  LYS   C CE  1 
ATOM   8056  N  NZ  . LYS   C  1 156 ? 40.602  42.173  -98.887  1.00 68.61  ? 457  LYS   C NZ  1 
ATOM   8057  N  N   . GLY   C  1 157 ? 38.278  41.760  -91.482  1.00 52.05  ? 458  GLY   C N   1 
ATOM   8058  C  CA  . GLY   C  1 157 ? 38.474  42.025  -90.076  1.00 43.78  ? 458  GLY   C CA  1 
ATOM   8059  C  C   . GLY   C  1 157 ? 37.498  43.013  -89.474  1.00 43.49  ? 458  GLY   C C   1 
ATOM   8060  O  O   . GLY   C  1 157 ? 37.298  42.991  -88.259  1.00 51.69  ? 458  GLY   C O   1 
ATOM   8061  N  N   . ASN   C  1 158 ? 36.885  43.881  -90.279  1.00 42.94  ? 459  ASN   C N   1 
ATOM   8062  C  CA  . ASN   C  1 158 ? 35.816  44.739  -89.775  1.00 47.64  ? 459  ASN   C CA  1 
ATOM   8063  C  C   . ASN   C  1 158 ? 34.503  43.951  -89.821  1.00 48.38  ? 459  ASN   C C   1 
ATOM   8064  O  O   . ASN   C  1 158 ? 33.670  44.107  -90.724  1.00 48.08  ? 459  ASN   C O   1 
ATOM   8065  C  CB  . ASN   C  1 158 ? 35.736  46.032  -90.573  1.00 47.03  ? 459  ASN   C CB  1 
ATOM   8066  C  CG  . ASN   C  1 158 ? 34.666  46.970  -90.037  1.00 55.19  ? 459  ASN   C CG  1 
ATOM   8067  O  OD1 . ASN   C  1 158 ? 34.331  46.928  -88.851  1.00 61.95  ? 459  ASN   C OD1 1 
ATOM   8068  N  ND2 . ASN   C  1 158 ? 34.112  47.811  -90.908  1.00 48.05  ? 459  ASN   C ND2 1 
ATOM   8069  N  N   . LEU   C  1 159 ? 34.314  43.107  -88.798  1.00 39.61  ? 460  LEU   C N   1 
ATOM   8070  C  CA  . LEU   C  1 159 ? 33.276  42.082  -88.828  1.00 34.51  ? 460  LEU   C CA  1 
ATOM   8071  C  C   . LEU   C  1 159 ? 31.882  42.694  -88.874  1.00 35.26  ? 460  LEU   C C   1 
ATOM   8072  O  O   . LEU   C  1 159 ? 31.618  43.758  -88.306  1.00 35.60  ? 460  LEU   C O   1 
ATOM   8073  C  CB  . LEU   C  1 159 ? 33.377  41.161  -87.609  1.00 36.73  ? 460  LEU   C CB  1 
ATOM   8074  C  CG  . LEU   C  1 159 ? 34.644  40.329  -87.394  1.00 41.73  ? 460  LEU   C CG  1 
ATOM   8075  C  CD1 . LEU   C  1 159 ? 34.341  39.149  -86.503  1.00 46.52  ? 460  LEU   C CD1 1 
ATOM   8076  C  CD2 . LEU   C  1 159 ? 35.229  39.858  -88.699  1.00 38.95  ? 460  LEU   C CD2 1 
ATOM   8077  N  N   . ARG   C  1 160 ? 30.983  41.994  -89.561  1.00 29.06  ? 461  ARG   C N   1 
ATOM   8078  C  CA  . ARG   C  1 160 ? 29.614  42.432  -89.776  1.00 28.65  ? 461  ARG   C CA  1 
ATOM   8079  C  C   . ARG   C  1 160 ? 28.705  41.271  -89.426  1.00 32.93  ? 461  ARG   C C   1 
ATOM   8080  O  O   . ARG   C  1 160 ? 29.011  40.120  -89.747  1.00 37.59  ? 461  ARG   C O   1 
ATOM   8081  C  CB  . ARG   C  1 160 ? 29.360  42.854  -91.250  1.00 35.50  ? 461  ARG   C CB  1 
ATOM   8082  C  CG  . ARG   C  1 160 ? 30.232  43.984  -91.756  1.00 46.48  ? 461  ARG   C CG  1 
ATOM   8083  C  CD  . ARG   C  1 160 ? 29.840  44.428  -93.184  1.00 50.69  ? 461  ARG   C CD  1 
ATOM   8084  N  NE  . ARG   C  1 160 ? 30.432  43.577  -94.216  1.00 51.04  ? 461  ARG   C NE  1 
ATOM   8085  C  CZ  . ARG   C  1 160 ? 30.615  43.939  -95.484  1.00 41.41  ? 461  ARG   C CZ  1 
ATOM   8086  N  NH1 . ARG   C  1 160 ? 30.260  45.137  -95.899  1.00 36.99  ? 461  ARG   C NH1 1 
ATOM   8087  N  NH2 . ARG   C  1 160 ? 31.162  43.096  -96.334  1.00 40.63  ? 461  ARG   C NH2 1 
ATOM   8088  N  N   . SER   C  1 161 ? 27.590  41.547  -88.772  1.00 33.33  ? 462  SER   C N   1 
ATOM   8089  C  CA  . SER   C  1 161 ? 26.737  40.437  -88.375  1.00 40.97  ? 462  SER   C CA  1 
ATOM   8090  C  C   . SER   C  1 161 ? 25.857  40.006  -89.546  1.00 39.75  ? 462  SER   C C   1 
ATOM   8091  O  O   . SER   C  1 161 ? 25.367  40.836  -90.321  1.00 36.46  ? 462  SER   C O   1 
ATOM   8092  C  CB  . SER   C  1 161 ? 25.905  40.801  -87.140  1.00 46.51  ? 462  SER   C CB  1 
ATOM   8093  O  OG  . SER   C  1 161 ? 25.345  42.089  -87.258  1.00 60.91  ? 462  SER   C OG  1 
ATOM   8094  N  N   . ALA   C  1 162 ? 25.675  38.694  -89.689  1.00 41.20  ? 463  ALA   C N   1 
ATOM   8095  C  CA  . ALA   C  1 162 ? 24.836  38.187  -90.765  1.00 35.94  ? 463  ALA   C CA  1 
ATOM   8096  C  C   . ALA   C  1 162 ? 24.176  36.887  -90.351  1.00 38.46  ? 463  ALA   C C   1 
ATOM   8097  O  O   . ALA   C  1 162 ? 24.629  36.186  -89.436  1.00 26.94  ? 463  ALA   C O   1 
ATOM   8098  C  CB  . ALA   C  1 162 ? 25.625  37.944  -92.053  1.00 39.76  ? 463  ALA   C CB  1 
ATOM   8099  N  N   . ILE   C  1 163 ? 23.117  36.555  -91.082  1.00 35.86  ? 464  ILE   C N   1 
ATOM   8100  C  CA  . ILE   C  1 163 ? 22.495  35.242  -91.026  1.00 37.89  ? 464  ILE   C CA  1 
ATOM   8101  C  C   . ILE   C  1 163 ? 22.143  34.835  -92.455  1.00 38.51  ? 464  ILE   C C   1 
ATOM   8102  O  O   . ILE   C  1 163 ? 21.734  35.671  -93.264  1.00 36.07  ? 464  ILE   C O   1 
ATOM   8103  C  CB  . ILE   C  1 163 ? 21.251  35.248  -90.122  1.00 29.95  ? 464  ILE   C CB  1 
ATOM   8104  C  CG1 . ILE   C  1 163 ? 20.660  33.841  -89.988  1.00 28.40  ? 464  ILE   C CG1 1 
ATOM   8105  C  CG2 . ILE   C  1 163 ? 20.228  36.268  -90.635  1.00 27.14  ? 464  ILE   C CG2 1 
ATOM   8106  C  CD1 . ILE   C  1 163 ? 19.651  33.708  -88.791  1.00 26.24  ? 464  ILE   C CD1 1 
ATOM   8107  N  N   . THR   C  1 164 ? 22.319  33.556  -92.770  1.00 39.98  ? 465  THR   C N   1 
ATOM   8108  C  CA  . THR   C  1 164 ? 21.935  32.998  -94.058  1.00 38.58  ? 465  THR   C CA  1 
ATOM   8109  C  C   . THR   C  1 164 ? 20.866  31.950  -93.804  1.00 36.63  ? 465  THR   C C   1 
ATOM   8110  O  O   . THR   C  1 164 ? 21.108  31.005  -93.053  1.00 34.54  ? 465  THR   C O   1 
ATOM   8111  C  CB  . THR   C  1 164 ? 23.147  32.399  -94.775  1.00 33.91  ? 465  THR   C CB  1 
ATOM   8112  O  OG1 . THR   C  1 164 ? 23.983  33.460  -95.254  1.00 33.58  ? 465  THR   C OG1 1 
ATOM   8113  C  CG2 . THR   C  1 164 ? 22.712  31.515  -95.928  1.00 40.39  ? 465  THR   C CG2 1 
ATOM   8114  N  N   . ILE   C  1 165 ? 19.699  32.113  -94.436  1.00 34.77  ? 466  ILE   C N   1 
ATOM   8115  C  CA  . ILE   C  1 165 ? 18.504  31.343  -94.111  1.00 37.55  ? 466  ILE   C CA  1 
ATOM   8116  C  C   . ILE   C  1 165 ? 18.149  30.408  -95.270  1.00 44.69  ? 466  ILE   C C   1 
ATOM   8117  O  O   . ILE   C  1 165 ? 17.679  30.844  -96.329  1.00 43.80  ? 466  ILE   C O   1 
ATOM   8118  C  CB  . ILE   C  1 165 ? 17.333  32.262  -93.744  1.00 42.91  ? 466  ILE   C CB  1 
ATOM   8119  C  CG1 . ILE   C  1 165 ? 17.742  33.156  -92.562  1.00 38.38  ? 466  ILE   C CG1 1 
ATOM   8120  C  CG2 . ILE   C  1 165 ? 16.123  31.433  -93.350  1.00 40.77  ? 466  ILE   C CG2 1 
ATOM   8121  C  CD1 . ILE   C  1 165 ? 16.670  34.081  -92.065  1.00 30.40  ? 466  ILE   C CD1 1 
ATOM   8122  N  N   . PHE   C  1 166 ? 18.327  29.114  -95.034  1.00 43.66  ? 467  PHE   C N   1 
ATOM   8123  C  CA  . PHE   C  1 166 ? 18.083  28.043  -95.988  1.00 33.51  ? 467  PHE   C CA  1 
ATOM   8124  C  C   . PHE   C  1 166 ? 16.642  27.559  -95.893  1.00 43.36  ? 467  PHE   C C   1 
ATOM   8125  O  O   . PHE   C  1 166 ? 15.946  27.851  -94.915  1.00 42.92  ? 467  PHE   C O   1 
ATOM   8126  C  CB  . PHE   C  1 166 ? 19.058  26.908  -95.712  1.00 37.97  ? 467  PHE   C CB  1 
ATOM   8127  C  CG  . PHE   C  1 166 ? 20.466  27.238  -96.053  1.00 42.75  ? 467  PHE   C CG  1 
ATOM   8128  C  CD1 . PHE   C  1 166 ? 20.870  27.321  -97.392  1.00 42.16  ? 467  PHE   C CD1 1 
ATOM   8129  C  CD2 . PHE   C  1 166 ? 21.393  27.472  -95.050  1.00 29.94  ? 467  PHE   C CD2 1 
ATOM   8130  C  CE1 . PHE   C  1 166 ? 22.177  27.632  -97.720  1.00 39.32  ? 467  PHE   C CE1 1 
ATOM   8131  C  CE2 . PHE   C  1 166 ? 22.708  27.782  -95.360  1.00 34.60  ? 467  PHE   C CE2 1 
ATOM   8132  C  CZ  . PHE   C  1 166 ? 23.107  27.861  -96.703  1.00 41.45  ? 467  PHE   C CZ  1 
ATOM   8133  N  N   . PRO   C  1 167 ? 16.163  26.788  -96.886  1.00 41.41  ? 468  PRO   C N   1 
ATOM   8134  C  CA  . PRO   C  1 167 ? 14.722  26.490  -96.960  1.00 38.11  ? 468  PRO   C CA  1 
ATOM   8135  C  C   . PRO   C  1 167 ? 14.177  25.814  -95.702  1.00 42.70  ? 468  PRO   C C   1 
ATOM   8136  O  O   . PRO   C  1 167 ? 14.827  24.968  -95.085  1.00 36.59  ? 468  PRO   C O   1 
ATOM   8137  C  CB  . PRO   C  1 167 ? 14.617  25.560  -98.176  1.00 42.05  ? 468  PRO   C CB  1 
ATOM   8138  C  CG  . PRO   C  1 167 ? 15.834  25.807  -98.963  1.00 38.29  ? 468  PRO   C CG  1 
ATOM   8139  C  CD  . PRO   C  1 167 ? 16.899  26.096  -97.960  1.00 40.93  ? 468  PRO   C CD  1 
ATOM   8140  N  N   . GLN   C  1 168 ? 12.947  26.164  -95.359  1.00 45.98  ? 469  GLN   C N   1 
ATOM   8141  C  CA  . GLN   C  1 168 ? 12.341  25.710  -94.117  1.00 42.41  ? 469  GLN   C CA  1 
ATOM   8142  C  C   . GLN   C  1 168 ? 12.068  24.213  -94.143  1.00 48.17  ? 469  GLN   C C   1 
ATOM   8143  O  O   . GLN   C  1 168 ? 12.020  23.569  -95.200  1.00 44.18  ? 469  GLN   C O   1 
ATOM   8144  C  CB  . GLN   C  1 168 ? 11.037  26.446  -93.871  1.00 36.20  ? 469  GLN   C CB  1 
ATOM   8145  C  CG  . GLN   C  1 168 ? 10.027  26.233  -94.967  1.00 35.33  ? 469  GLN   C CG  1 
ATOM   8146  C  CD  . GLN   C  1 168 ? 9.090   27.399  -95.060  1.00 41.51  ? 469  GLN   C CD  1 
ATOM   8147  O  OE1 . GLN   C  1 168 ? 9.505   28.549  -94.898  1.00 37.26  ? 469  GLN   C OE1 1 
ATOM   8148  N  NE2 . GLN   C  1 168 ? 7.807   27.119  -95.294  1.00 44.49  ? 469  GLN   C NE2 1 
ATOM   8149  N  N   . ARG   C  1 169 ? 11.886  23.660  -92.946  1.00 44.23  ? 470  ARG   C N   1 
ATOM   8150  C  CA  . ARG   C  1 169 ? 11.497  22.266  -92.811  1.00 44.84  ? 470  ARG   C CA  1 
ATOM   8151  C  C   . ARG   C  1 169 ? 10.109  22.069  -93.405  1.00 42.84  ? 470  ARG   C C   1 
ATOM   8152  O  O   . ARG   C  1 169 ? 9.263   22.962  -93.347  1.00 45.35  ? 470  ARG   C O   1 
ATOM   8153  C  CB  . ARG   C  1 169 ? 11.532  21.847  -91.339  1.00 53.12  ? 470  ARG   C CB  1 
ATOM   8154  C  CG  . ARG   C  1 169 ? 11.118  20.410  -91.075  1.00 59.69  ? 470  ARG   C CG  1 
ATOM   8155  C  CD  . ARG   C  1 169 ? 11.231  20.079  -89.603  1.00 56.51  ? 470  ARG   C CD  1 
ATOM   8156  N  NE  . ARG   C  1 169 ? 12.616  19.890  -89.194  1.00 52.21  ? 470  ARG   C NE  1 
ATOM   8157  C  CZ  . ARG   C  1 169 ? 13.079  20.237  -88.001  1.00 66.11  ? 470  ARG   C CZ  1 
ATOM   8158  N  NH1 . ARG   C  1 169 ? 12.265  20.810  -87.123  1.00 65.10  ? 470  ARG   C NH1 1 
ATOM   8159  N  NH2 . ARG   C  1 169 ? 14.353  20.032  -87.688  1.00 75.39  ? 470  ARG   C NH2 1 
ATOM   8160  N  N   . THR   C  1 170 ? 9.889   20.907  -94.022  1.00 44.77  ? 471  THR   C N   1 
ATOM   8161  C  CA  . THR   C  1 170 ? 8.608   20.616  -94.662  1.00 52.87  ? 471  THR   C CA  1 
ATOM   8162  C  C   . THR   C  1 170 ? 7.946   19.414  -94.005  1.00 57.97  ? 471  THR   C C   1 
ATOM   8163  O  O   . THR   C  1 170 ? 6.967   19.582  -93.279  1.00 63.45  ? 471  THR   C O   1 
ATOM   8164  C  CB  . THR   C  1 170 ? 8.795   20.378  -96.159  1.00 53.96  ? 471  THR   C CB  1 
ATOM   8165  O  OG1 . THR   C  1 170 ? 9.668   19.256  -96.345  1.00 60.72  ? 471  THR   C OG1 1 
ATOM   8166  C  CG2 . THR   C  1 170 ? 9.386   21.610  -96.827  1.00 50.87  ? 471  THR   C CG2 1 
ATOM   8167  N  N   . ASP   C  1 171 ? 8.443   18.205  -94.244  1.00 60.47  ? 472  ASP   C N   1 
ATOM   8168  C  CA  . ASP   C  1 171 ? 7.899   17.009  -93.629  1.00 66.13  ? 472  ASP   C CA  1 
ATOM   8169  C  C   . ASP   C  1 171 ? 8.836   16.390  -92.602  1.00 67.00  ? 472  ASP   C C   1 
ATOM   8170  O  O   . ASP   C  1 171 ? 8.449   15.421  -91.943  1.00 77.19  ? 472  ASP   C O   1 
ATOM   8171  C  CB  . ASP   C  1 171 ? 7.555   15.967  -94.704  1.00 72.41  ? 472  ASP   C CB  1 
ATOM   8172  C  CG  . ASP   C  1 171 ? 8.790   15.386  -95.374  1.00 71.92  ? 472  ASP   C CG  1 
ATOM   8173  O  OD1 . ASP   C  1 171 ? 9.895   15.934  -95.186  1.00 75.42  ? 472  ASP   C OD1 1 
ATOM   8174  O  OD2 . ASP   C  1 171 ? 8.657   14.372  -96.080  1.00 71.42  ? 472  ASP   C OD2 1 
ATOM   8175  N  N   . GLY   C  1 172 ? 10.047  16.920  -92.444  1.00 59.34  ? 473  GLY   C N   1 
ATOM   8176  C  CA  . GLY   C  1 172 ? 11.012  16.381  -91.514  1.00 55.05  ? 473  GLY   C CA  1 
ATOM   8177  C  C   . GLY   C  1 172 ? 11.992  15.406  -92.131  1.00 58.99  ? 473  GLY   C C   1 
ATOM   8178  O  O   . GLY   C  1 172 ? 13.074  15.195  -91.574  1.00 58.50  ? 473  GLY   C O   1 
ATOM   8179  N  N   . LYS   C  1 173 ? 11.647  14.812  -93.265  1.00 59.47  ? 474  LYS   C N   1 
ATOM   8180  C  CA  . LYS   C  1 173 ? 12.560  13.927  -93.965  1.00 69.96  ? 474  LYS   C CA  1 
ATOM   8181  C  C   . LYS   C  1 173 ? 13.366  14.654  -95.040  1.00 76.92  ? 474  LYS   C C   1 
ATOM   8182  O  O   . LYS   C  1 173 ? 14.095  14.005  -95.797  1.00 83.88  ? 474  LYS   C O   1 
ATOM   8183  C  CB  . LYS   C  1 173 ? 11.778  12.755  -94.567  1.00 71.49  ? 474  LYS   C CB  1 
ATOM   8184  C  CG  . LYS   C  1 173 ? 11.152  11.839  -93.515  1.00 77.93  ? 474  LYS   C CG  1 
ATOM   8185  C  CD  . LYS   C  1 173 ? 10.196  10.821  -94.134  1.00 84.91  ? 474  LYS   C CD  1 
ATOM   8186  C  CE  . LYS   C  1 173 ? 9.775   9.756   -93.116  1.00 84.43  ? 474  LYS   C CE  1 
ATOM   8187  N  NZ  . LYS   C  1 173 ? 8.955   8.669   -93.734  1.00 81.12  ? 474  LYS   C NZ  1 
ATOM   8188  N  N   . HIS   C  1 174 ? 13.258  15.979  -95.120  1.00 67.24  ? 475  HIS   C N   1 
ATOM   8189  C  CA  . HIS   C  1 174 ? 13.943  16.759  -96.143  1.00 68.30  ? 475  HIS   C CA  1 
ATOM   8190  C  C   . HIS   C  1 174 ? 14.613  17.968  -95.522  1.00 64.61  ? 475  HIS   C C   1 
ATOM   8191  O  O   . HIS   C  1 174 ? 14.636  19.056  -96.102  1.00 58.92  ? 475  HIS   C O   1 
ATOM   8192  C  CB  . HIS   C  1 174 ? 12.985  17.195  -97.249  1.00 68.82  ? 475  HIS   C CB  1 
ATOM   8193  C  CG  . HIS   C  1 174 ? 12.413  16.063  -98.043  1.00 73.13  ? 475  HIS   C CG  1 
ATOM   8194  N  ND1 . HIS   C  1 174 ? 11.169  15.526  -97.786  1.00 75.79  ? 475  HIS   C ND1 1 
ATOM   8195  C  CD2 . HIS   C  1 174 ? 12.913  15.367  -99.090  1.00 72.87  ? 475  HIS   C CD2 1 
ATOM   8196  C  CE1 . HIS   C  1 174 ? 10.929  14.546  -98.636  1.00 76.35  ? 475  HIS   C CE1 1 
ATOM   8197  N  NE2 . HIS   C  1 174 ? 11.971  14.431  -99.440  1.00 77.25  ? 475  HIS   C NE2 1 
ATOM   8198  N  N   . ASP   C  1 175 ? 15.156  17.802  -94.322  1.00 60.99  ? 476  ASP   C N   1 
ATOM   8199  C  CA  . ASP   C  1 175 ? 15.781  18.925  -93.639  1.00 50.40  ? 476  ASP   C CA  1 
ATOM   8200  C  C   . ASP   C  1 175 ? 17.030  19.381  -94.377  1.00 45.73  ? 476  ASP   C C   1 
ATOM   8201  O  O   . ASP   C  1 175 ? 17.805  18.566  -94.881  1.00 47.31  ? 476  ASP   C O   1 
ATOM   8202  C  CB  . ASP   C  1 175 ? 16.166  18.547  -92.208  1.00 50.04  ? 476  ASP   C CB  1 
ATOM   8203  C  CG  . ASP   C  1 175 ? 14.987  18.513  -91.267  1.00 49.86  ? 476  ASP   C CG  1 
ATOM   8204  O  OD1 . ASP   C  1 175 ? 13.841  18.681  -91.726  1.00 52.66  ? 476  ASP   C OD1 1 
ATOM   8205  O  OD2 . ASP   C  1 175 ? 15.221  18.317  -90.058  1.00 54.28  ? 476  ASP   C OD2 1 
ATOM   8206  N  N   . PHE   C  1 176 ? 17.227  20.692  -94.427  1.00 38.01  ? 477  PHE   C N   1 
ATOM   8207  C  CA  . PHE   C  1 176 ? 18.542  21.265  -94.663  1.00 42.12  ? 477  PHE   C CA  1 
ATOM   8208  C  C   . PHE   C  1 176 ? 19.261  21.388  -93.325  1.00 44.90  ? 477  PHE   C C   1 
ATOM   8209  O  O   . PHE   C  1 176 ? 18.662  21.827  -92.336  1.00 45.92  ? 477  PHE   C O   1 
ATOM   8210  C  CB  . PHE   C  1 176 ? 18.426  22.633  -95.339  1.00 44.02  ? 477  PHE   C CB  1 
ATOM   8211  C  CG  . PHE   C  1 176 ? 17.970  22.565  -96.771  1.00 49.78  ? 477  PHE   C CG  1 
ATOM   8212  C  CD1 . PHE   C  1 176 ? 16.681  22.162  -97.089  1.00 52.53  ? 477  PHE   C CD1 1 
ATOM   8213  C  CD2 . PHE   C  1 176 ? 18.827  22.901  -97.796  1.00 48.41  ? 477  PHE   C CD2 1 
ATOM   8214  C  CE1 . PHE   C  1 176 ? 16.265  22.092  -98.399  1.00 46.21  ? 477  PHE   C CE1 1 
ATOM   8215  C  CE2 . PHE   C  1 176 ? 18.412  22.831  -99.094  1.00 48.07  ? 477  PHE   C CE2 1 
ATOM   8216  C  CZ  . PHE   C  1 176 ? 17.125  22.422  -99.394  1.00 44.57  ? 477  PHE   C CZ  1 
ATOM   8217  N  N   . ARG   C  1 177 ? 20.537  20.995  -93.292  1.00 42.93  ? 478  ARG   C N   1 
ATOM   8218  C  CA  . ARG   C  1 177 ? 21.330  21.055  -92.067  1.00 40.68  ? 478  ARG   C CA  1 
ATOM   8219  C  C   . ARG   C  1 177 ? 22.791  21.352  -92.374  1.00 38.90  ? 478  ARG   C C   1 
ATOM   8220  O  O   . ARG   C  1 177 ? 23.409  20.682  -93.204  1.00 52.86  ? 478  ARG   C O   1 
ATOM   8221  C  CB  . ARG   C  1 177 ? 21.247  19.733  -91.276  1.00 39.75  ? 478  ARG   C CB  1 
ATOM   8222  C  CG  . ARG   C  1 177 ? 19.916  19.441  -90.595  1.00 43.33  ? 478  ARG   C CG  1 
ATOM   8223  C  CD  . ARG   C  1 177 ? 19.554  20.476  -89.520  1.00 43.66  ? 478  ARG   C CD  1 
ATOM   8224  N  NE  . ARG   C  1 177 ? 20.479  20.504  -88.393  1.00 45.86  ? 478  ARG   C NE  1 
ATOM   8225  C  CZ  . ARG   C  1 177 ? 20.313  19.829  -87.256  1.00 47.33  ? 478  ARG   C CZ  1 
ATOM   8226  N  NH1 . ARG   C  1 177 ? 19.255  19.047  -87.075  1.00 42.62  ? 478  ARG   C NH1 1 
ATOM   8227  N  NH2 . ARG   C  1 177 ? 21.215  19.938  -86.291  1.00 43.45  ? 478  ARG   C NH2 1 
ATOM   8228  N  N   . VAL   C  1 178 ? 23.341  22.348  -91.696  1.00 41.95  ? 479  VAL   C N   1 
ATOM   8229  C  CA  . VAL   C  1 178 ? 24.783  22.428  -91.488  1.00 39.43  ? 479  VAL   C CA  1 
ATOM   8230  C  C   . VAL   C  1 178 ? 25.106  21.460  -90.359  1.00 44.51  ? 479  VAL   C C   1 
ATOM   8231  O  O   . VAL   C  1 178 ? 24.562  21.585  -89.254  1.00 45.74  ? 479  VAL   C O   1 
ATOM   8232  C  CB  . VAL   C  1 178 ? 25.215  23.860  -91.142  1.00 38.25  ? 479  VAL   C CB  1 
ATOM   8233  C  CG1 . VAL   C  1 178 ? 26.714  23.959  -90.959  1.00 26.43  ? 479  VAL   C CG1 1 
ATOM   8234  C  CG2 . VAL   C  1 178 ? 24.728  24.832  -92.217  1.00 40.68  ? 479  VAL   C CG2 1 
ATOM   8235  N  N   . TRP   C  1 179 ? 25.925  20.445  -90.651  1.00 48.19  ? 480  TRP   C N   1 
ATOM   8236  C  CA  . TRP   C  1 179 ? 26.260  19.469  -89.615  1.00 45.29  ? 480  TRP   C CA  1 
ATOM   8237  C  C   . TRP   C  1 179 ? 27.296  20.005  -88.642  1.00 41.50  ? 480  TRP   C C   1 
ATOM   8238  O  O   . TRP   C  1 179 ? 27.373  19.519  -87.513  1.00 41.57  ? 480  TRP   C O   1 
ATOM   8239  C  CB  . TRP   C  1 179 ? 26.749  18.149  -90.233  1.00 44.17  ? 480  TRP   C CB  1 
ATOM   8240  C  CG  . TRP   C  1 179 ? 25.619  17.274  -90.693  1.00 45.51  ? 480  TRP   C CG  1 
ATOM   8241  C  CD1 . TRP   C  1 179 ? 24.444  17.692  -91.272  1.00 40.36  ? 480  TRP   C CD1 1 
ATOM   8242  C  CD2 . TRP   C  1 179 ? 25.530  15.844  -90.591  1.00 43.68  ? 480  TRP   C CD2 1 
ATOM   8243  N  NE1 . TRP   C  1 179 ? 23.640  16.610  -91.541  1.00 41.86  ? 480  TRP   C NE1 1 
ATOM   8244  C  CE2 . TRP   C  1 179 ? 24.277  15.466  -91.129  1.00 43.21  ? 480  TRP   C CE2 1 
ATOM   8245  C  CE3 . TRP   C  1 179 ? 26.386  14.847  -90.107  1.00 40.50  ? 480  TRP   C CE3 1 
ATOM   8246  C  CZ2 . TRP   C  1 179 ? 23.864  14.134  -91.197  1.00 43.32  ? 480  TRP   C CZ2 1 
ATOM   8247  C  CZ3 . TRP   C  1 179 ? 25.974  13.522  -90.176  1.00 37.43  ? 480  TRP   C CZ3 1 
ATOM   8248  C  CH2 . TRP   C  1 179 ? 24.724  13.178  -90.715  1.00 44.73  ? 480  TRP   C CH2 1 
ATOM   8249  N  N   . ASN   C  1 180 ? 28.089  20.984  -89.054  1.00 38.32  ? 481  ASN   C N   1 
ATOM   8250  C  CA  . ASN   C  1 180 ? 28.999  21.658  -88.147  1.00 42.83  ? 481  ASN   C CA  1 
ATOM   8251  C  C   . ASN   C  1 180 ? 28.219  22.432  -87.101  1.00 52.29  ? 481  ASN   C C   1 
ATOM   8252  O  O   . ASN   C  1 180 ? 27.132  22.953  -87.372  1.00 56.83  ? 481  ASN   C O   1 
ATOM   8253  C  CB  . ASN   C  1 180 ? 29.881  22.639  -88.909  1.00 36.80  ? 481  ASN   C CB  1 
ATOM   8254  C  CG  . ASN   C  1 180 ? 30.634  21.984  -90.031  1.00 38.97  ? 481  ASN   C CG  1 
ATOM   8255  O  OD1 . ASN   C  1 180 ? 30.049  21.578  -91.041  1.00 38.59  ? 481  ASN   C OD1 1 
ATOM   8256  N  ND2 . ASN   C  1 180 ? 31.949  21.890  -89.873  1.00 44.15  ? 481  ASN   C ND2 1 
ATOM   8257  N  N   . SER   C  1 181 ? 28.803  22.545  -85.906  1.00 42.62  ? 482  SER   C N   1 
ATOM   8258  C  CA  . SER   C  1 181 ? 28.174  23.370  -84.882  1.00 38.54  ? 482  SER   C CA  1 
ATOM   8259  C  C   . SER   C  1 181 ? 28.474  24.845  -85.117  1.00 31.18  ? 482  SER   C C   1 
ATOM   8260  O  O   . SER   C  1 181 ? 27.588  25.691  -84.969  1.00 36.56  ? 482  SER   C O   1 
ATOM   8261  C  CB  . SER   C  1 181 ? 28.613  22.903  -83.487  1.00 38.34  ? 482  SER   C CB  1 
ATOM   8262  O  OG  . SER   C  1 181 ? 30.010  22.683  -83.418  1.00 39.97  ? 482  SER   C OG  1 
ATOM   8263  N  N   . GLN   C  1 182 ? 29.695  25.170  -85.533  1.00 29.93  ? 483  GLN   C N   1 
ATOM   8264  C  CA  . GLN   C  1 182 ? 30.007  26.481  -86.087  1.00 31.84  ? 483  GLN   C CA  1 
ATOM   8265  C  C   . GLN   C  1 182 ? 30.664  26.306  -87.455  1.00 42.51  ? 483  GLN   C C   1 
ATOM   8266  O  O   . GLN   C  1 182 ? 31.286  25.272  -87.735  1.00 42.25  ? 483  GLN   C O   1 
ATOM   8267  C  CB  . GLN   C  1 182 ? 30.924  27.293  -85.196  1.00 35.78  ? 483  GLN   C CB  1 
ATOM   8268  C  CG  . GLN   C  1 182 ? 30.354  27.632  -83.815  1.00 44.30  ? 483  GLN   C CG  1 
ATOM   8269  C  CD  . GLN   C  1 182 ? 31.463  27.985  -82.847  1.00 48.92  ? 483  GLN   C CD  1 
ATOM   8270  O  OE1 . GLN   C  1 182 ? 32.238  28.921  -83.084  1.00 49.37  ? 483  GLN   C OE1 1 
ATOM   8271  N  NE2 . GLN   C  1 182 ? 31.590  27.198  -81.782  1.00 44.02  ? 483  GLN   C NE2 1 
ATOM   8272  N  N   . LEU   C  1 183 ? 30.518  27.326  -88.310  1.00 36.89  ? 484  LEU   C N   1 
ATOM   8273  C  CA  . LEU   C  1 183 ? 31.083  27.236  -89.657  1.00 37.02  ? 484  LEU   C CA  1 
ATOM   8274  C  C   . LEU   C  1 183 ? 32.571  26.973  -89.605  1.00 39.73  ? 484  LEU   C C   1 
ATOM   8275  O  O   . LEU   C  1 183 ? 33.089  26.186  -90.398  1.00 40.73  ? 484  LEU   C O   1 
ATOM   8276  C  CB  . LEU   C  1 183 ? 30.800  28.509  -90.447  1.00 25.99  ? 484  LEU   C CB  1 
ATOM   8277  C  CG  . LEU   C  1 183 ? 29.301  28.750  -90.594  1.00 31.55  ? 484  LEU   C CG  1 
ATOM   8278  C  CD1 . LEU   C  1 183 ? 29.001  29.984  -91.428  1.00 25.55  ? 484  LEU   C CD1 1 
ATOM   8279  C  CD2 . LEU   C  1 183 ? 28.636  27.526  -91.157  1.00 25.09  ? 484  LEU   C CD2 1 
ATOM   8280  N  N   . ILE   C  1 184 ? 33.263  27.587  -88.646  1.00 44.33  ? 485  ILE   C N   1 
ATOM   8281  C  CA  . ILE   C  1 184 ? 34.710  27.479  -88.503  1.00 39.49  ? 485  ILE   C CA  1 
ATOM   8282  C  C   . ILE   C  1 184 ? 35.011  26.973  -87.091  1.00 45.53  ? 485  ILE   C C   1 
ATOM   8283  O  O   . ILE   C  1 184 ? 34.735  27.669  -86.106  1.00 42.73  ? 485  ILE   C O   1 
ATOM   8284  C  CB  . ILE   C  1 184 ? 35.408  28.820  -88.775  1.00 35.77  ? 485  ILE   C CB  1 
ATOM   8285  C  CG1 . ILE   C  1 184 ? 35.236  29.205  -90.253  1.00 38.52  ? 485  ILE   C CG1 1 
ATOM   8286  C  CG2 . ILE   C  1 184 ? 36.895  28.757  -88.428  1.00 31.92  ? 485  ILE   C CG2 1 
ATOM   8287  C  CD1 . ILE   C  1 184 ? 35.257  30.684  -90.485  1.00 39.36  ? 485  ILE   C CD1 1 
ATOM   8288  N  N   . ARG   C  1 185 ? 35.537  25.750  -86.995  1.00 50.04  ? 486  ARG   C N   1 
ATOM   8289  C  CA  . ARG   C  1 185 ? 36.059  25.182  -85.755  1.00 46.21  ? 486  ARG   C CA  1 
ATOM   8290  C  C   . ARG   C  1 185 ? 37.263  24.321  -86.099  1.00 43.87  ? 486  ARG   C C   1 
ATOM   8291  O  O   . ARG   C  1 185 ? 37.445  23.923  -87.252  1.00 43.91  ? 486  ARG   C O   1 
ATOM   8292  C  CB  . ARG   C  1 185 ? 35.012  24.337  -85.008  1.00 39.80  ? 486  ARG   C CB  1 
ATOM   8293  C  CG  . ARG   C  1 185 ? 33.789  25.111  -84.557  1.00 40.79  ? 486  ARG   C CG  1 
ATOM   8294  C  CD  . ARG   C  1 185 ? 33.025  24.362  -83.482  1.00 50.61  ? 486  ARG   C CD  1 
ATOM   8295  N  NE  . ARG   C  1 185 ? 33.721  24.436  -82.206  1.00 59.91  ? 486  ARG   C NE  1 
ATOM   8296  C  CZ  . ARG   C  1 185 ? 33.256  23.926  -81.073  1.00 57.02  ? 486  ARG   C CZ  1 
ATOM   8297  N  NH1 . ARG   C  1 185 ? 32.087  23.303  -81.054  1.00 54.11  ? 486  ARG   C NH1 1 
ATOM   8298  N  NH2 . ARG   C  1 185 ? 33.966  24.040  -79.962  1.00 55.04  ? 486  ARG   C NH2 1 
ATOM   8299  N  N   . TYR   C  1 186 ? 38.092  24.030  -85.101  1.00 37.80  ? 487  TYR   C N   1 
ATOM   8300  C  CA  . TYR   C  1 186 ? 39.251  23.178  -85.320  1.00 37.98  ? 487  TYR   C CA  1 
ATOM   8301  C  C   . TYR   C  1 186 ? 38.953  21.724  -84.959  1.00 46.35  ? 487  TYR   C C   1 
ATOM   8302  O  O   . TYR   C  1 186 ? 38.103  21.429  -84.116  1.00 53.46  ? 487  TYR   C O   1 
ATOM   8303  C  CB  . TYR   C  1 186 ? 40.462  23.678  -84.528  1.00 37.95  ? 487  TYR   C CB  1 
ATOM   8304  C  CG  . TYR   C  1 186 ? 40.874  25.108  -84.828  1.00 44.25  ? 487  TYR   C CG  1 
ATOM   8305  C  CD1 . TYR   C  1 186 ? 41.405  25.453  -86.068  1.00 46.70  ? 487  TYR   C CD1 1 
ATOM   8306  C  CD2 . TYR   C  1 186 ? 40.755  26.105  -83.869  1.00 40.73  ? 487  TYR   C CD2 1 
ATOM   8307  C  CE1 . TYR   C  1 186 ? 41.801  26.752  -86.344  1.00 46.84  ? 487  TYR   C CE1 1 
ATOM   8308  C  CE2 . TYR   C  1 186 ? 41.143  27.417  -84.136  1.00 37.59  ? 487  TYR   C CE2 1 
ATOM   8309  C  CZ  . TYR   C  1 186 ? 41.668  27.734  -85.379  1.00 45.80  ? 487  TYR   C CZ  1 
ATOM   8310  O  OH  . TYR   C  1 186 ? 42.058  29.032  -85.665  1.00 38.30  ? 487  TYR   C OH  1 
ATOM   8311  N  N   . ALA   C  1 187 ? 39.687  20.820  -85.601  1.00 56.02  ? 488  ALA   C N   1 
ATOM   8312  C  CA  . ALA   C  1 187 ? 39.513  19.385  -85.443  1.00 52.47  ? 488  ALA   C CA  1 
ATOM   8313  C  C   . ALA   C  1 187 ? 39.998  18.903  -84.079  1.00 54.38  ? 488  ALA   C C   1 
ATOM   8314  O  O   . ALA   C  1 187 ? 40.843  19.520  -83.426  1.00 59.59  ? 488  ALA   C O   1 
ATOM   8315  C  CB  . ALA   C  1 187 ? 40.277  18.636  -86.535  1.00 43.62  ? 488  ALA   C CB  1 
ATOM   8316  N  N   . GLY   C  1 188 ? 39.454  17.763  -83.664  1.00 54.96  ? 489  GLY   C N   1 
ATOM   8317  C  CA  . GLY   C  1 188 ? 39.894  17.090  -82.455  1.00 53.71  ? 489  GLY   C CA  1 
ATOM   8318  C  C   . GLY   C  1 188 ? 40.255  15.645  -82.724  1.00 51.62  ? 489  GLY   C C   1 
ATOM   8319  O  O   . GLY   C  1 188 ? 39.462  14.901  -83.304  1.00 57.66  ? 489  GLY   C O   1 
ATOM   8320  N  N   . TYR   C  1 189 ? 41.449  15.231  -82.320  1.00 53.41  ? 490  TYR   C N   1 
ATOM   8321  C  CA  . TYR   C  1 189 ? 41.962  13.912  -82.652  1.00 56.62  ? 490  TYR   C CA  1 
ATOM   8322  C  C   . TYR   C  1 189 ? 42.169  13.096  -81.385  1.00 67.80  ? 490  TYR   C C   1 
ATOM   8323  O  O   . TYR   C  1 189 ? 42.700  13.603  -80.389  1.00 66.36  ? 490  TYR   C O   1 
ATOM   8324  C  CB  . TYR   C  1 189 ? 43.266  14.024  -83.447  1.00 57.19  ? 490  TYR   C CB  1 
ATOM   8325  C  CG  . TYR   C  1 189 ? 43.125  14.844  -84.713  1.00 59.59  ? 490  TYR   C CG  1 
ATOM   8326  C  CD1 . TYR   C  1 189 ? 42.311  14.419  -85.753  1.00 62.91  ? 490  TYR   C CD1 1 
ATOM   8327  C  CD2 . TYR   C  1 189 ? 43.797  16.047  -84.857  1.00 64.07  ? 490  TYR   C CD2 1 
ATOM   8328  C  CE1 . TYR   C  1 189 ? 42.182  15.169  -86.918  1.00 69.74  ? 490  TYR   C CE1 1 
ATOM   8329  C  CE2 . TYR   C  1 189 ? 43.671  16.807  -86.003  1.00 68.77  ? 490  TYR   C CE2 1 
ATOM   8330  C  CZ  . TYR   C  1 189 ? 42.872  16.364  -87.040  1.00 69.73  ? 490  TYR   C CZ  1 
ATOM   8331  O  OH  . TYR   C  1 189 ? 42.756  17.130  -88.188  1.00 56.01  ? 490  TYR   C OH  1 
ATOM   8332  N  N   . LYS   C  1 190 ? 41.741  11.836  -81.432  1.00 75.12  ? 491  LYS   C N   1 
ATOM   8333  C  CA  . LYS   C  1 190 ? 41.869  10.910  -80.314  1.00 78.16  ? 491  LYS   C CA  1 
ATOM   8334  C  C   . LYS   C  1 190 ? 43.226  10.216  -80.421  1.00 83.98  ? 491  LYS   C C   1 
ATOM   8335  O  O   . LYS   C  1 190 ? 43.419  9.339   -81.266  1.00 92.19  ? 491  LYS   C O   1 
ATOM   8336  C  CB  . LYS   C  1 190 ? 40.717  9.910   -80.328  1.00 82.19  ? 491  LYS   C CB  1 
ATOM   8337  C  CG  . LYS   C  1 190 ? 40.392  9.290   -78.979  1.00 90.67  ? 491  LYS   C CG  1 
ATOM   8338  C  CD  . LYS   C  1 190 ? 39.237  10.004  -78.280  1.00 92.87  ? 491  LYS   C CD  1 
ATOM   8339  C  CE  . LYS   C  1 190 ? 39.719  11.147  -77.391  1.00 90.70  ? 491  LYS   C CE  1 
ATOM   8340  N  NZ  . LYS   C  1 190 ? 40.753  10.685  -76.423  1.00 88.97  ? 491  LYS   C NZ  1 
ATOM   8341  N  N   . GLN   C  1 191 ? 44.165  10.607  -79.562  1.00 88.25  ? 492  GLN   C N   1 
ATOM   8342  C  CA  . GLN   C  1 191 ? 45.549  10.159  -79.672  1.00 92.43  ? 492  GLN   C CA  1 
ATOM   8343  C  C   . GLN   C  1 191 ? 45.709  8.706   -79.214  1.00 90.65  ? 492  GLN   C C   1 
ATOM   8344  O  O   . GLN   C  1 191 ? 44.829  8.151   -78.551  1.00 83.83  ? 492  GLN   C O   1 
ATOM   8345  C  CB  . GLN   C  1 191 ? 46.460  11.080  -78.860  1.00 95.93  ? 492  GLN   C CB  1 
ATOM   8346  C  CG  . GLN   C  1 191 ? 46.590  12.492  -79.415  1.00 97.63  ? 492  GLN   C CG  1 
ATOM   8347  C  CD  . GLN   C  1 191 ? 47.458  12.581  -80.659  1.00 97.71  ? 492  GLN   C CD  1 
ATOM   8348  O  OE1 . GLN   C  1 191 ? 47.279  11.836  -81.626  1.00 94.86  ? 492  GLN   C OE1 1 
ATOM   8349  N  NE2 . GLN   C  1 191 ? 48.403  13.510  -80.641  1.00 100.34 ? 492  GLN   C NE2 1 
ATOM   8350  N  N   . PRO   C  1 192 ? 46.841  8.058   -79.571  1.00 95.59  ? 493  PRO   C N   1 
ATOM   8351  C  CA  . PRO   C  1 192 ? 47.025  6.643   -79.216  1.00 97.52  ? 493  PRO   C CA  1 
ATOM   8352  C  C   . PRO   C  1 192 ? 47.153  6.401   -77.718  1.00 100.73 ? 493  PRO   C C   1 
ATOM   8353  O  O   . PRO   C  1 192 ? 46.522  5.486   -77.174  1.00 95.30  ? 493  PRO   C O   1 
ATOM   8354  C  CB  . PRO   C  1 192 ? 48.318  6.268   -79.952  1.00 95.76  ? 493  PRO   C CB  1 
ATOM   8355  C  CG  . PRO   C  1 192 ? 49.040  7.556   -80.120  1.00 96.46  ? 493  PRO   C CG  1 
ATOM   8356  C  CD  . PRO   C  1 192 ? 47.960  8.552   -80.395  1.00 97.08  ? 493  PRO   C CD  1 
ATOM   8357  N  N   . ASP   C  1 193 ? 47.977  7.207   -77.041  1.00 101.96 ? 494  ASP   C N   1 
ATOM   8358  C  CA  . ASP   C  1 193 ? 48.156  7.021   -75.606  1.00 99.84  ? 494  ASP   C CA  1 
ATOM   8359  C  C   . ASP   C  1 193 ? 46.844  7.210   -74.858  1.00 98.59  ? 494  ASP   C C   1 
ATOM   8360  O  O   . ASP   C  1 193 ? 46.620  6.578   -73.818  1.00 104.45 ? 494  ASP   C O   1 
ATOM   8361  C  CB  . ASP   C  1 193 ? 49.234  7.973   -75.073  1.00 100.07 ? 494  ASP   C CB  1 
ATOM   8362  C  CG  . ASP   C  1 193 ? 48.913  9.443   -75.312  1.00 97.98  ? 494  ASP   C CG  1 
ATOM   8363  O  OD1 . ASP   C  1 193 ? 47.760  9.775   -75.654  1.00 95.79  ? 494  ASP   C OD1 1 
ATOM   8364  O  OD2 . ASP   C  1 193 ? 49.830  10.277  -75.155  1.00 97.12  ? 494  ASP   C OD2 1 
ATOM   8365  N  N   . GLY   C  1 194 ? 45.963  8.056   -75.377  1.00 88.81  ? 495  GLY   C N   1 
ATOM   8366  C  CA  . GLY   C  1 194 ? 44.679  8.266   -74.750  1.00 78.99  ? 495  GLY   C CA  1 
ATOM   8367  C  C   . GLY   C  1 194 ? 44.332  9.726   -74.589  1.00 74.85  ? 495  GLY   C C   1 
ATOM   8368  O  O   . GLY   C  1 194 ? 43.181  10.058  -74.292  1.00 74.92  ? 495  GLY   C O   1 
ATOM   8369  N  N   . SER   C  1 195 ? 45.308  10.609  -74.781  1.00 81.64  ? 496  SER   C N   1 
ATOM   8370  C  CA  . SER   C  1 195 ? 45.066  12.044  -74.693  1.00 87.21  ? 496  SER   C CA  1 
ATOM   8371  C  C   . SER   C  1 195 ? 44.333  12.511  -75.954  1.00 85.31  ? 496  SER   C C   1 
ATOM   8372  O  O   . SER   C  1 195 ? 43.843  11.705  -76.751  1.00 87.73  ? 496  SER   C O   1 
ATOM   8373  C  CB  . SER   C  1 195 ? 46.376  12.799  -74.480  1.00 88.99  ? 496  SER   C CB  1 
ATOM   8374  O  OG  . SER   C  1 195 ? 47.153  12.818  -75.664  1.00 89.96  ? 496  SER   C OG  1 
ATOM   8375  N  N   . THR   C  1 196 ? 44.256  13.825  -76.157  1.00 77.39  ? 497  THR   C N   1 
ATOM   8376  C  CA  . THR   C  1 196 ? 43.492  14.385  -77.263  1.00 73.28  ? 497  THR   C CA  1 
ATOM   8377  C  C   . THR   C  1 196 ? 44.271  15.516  -77.909  1.00 65.60  ? 497  THR   C C   1 
ATOM   8378  O  O   . THR   C  1 196 ? 44.771  16.398  -77.209  1.00 66.32  ? 497  THR   C O   1 
ATOM   8379  C  CB  . THR   C  1 196 ? 42.127  14.907  -76.790  1.00 77.55  ? 497  THR   C CB  1 
ATOM   8380  O  OG1 . THR   C  1 196 ? 41.363  13.838  -76.205  1.00 81.93  ? 497  THR   C OG1 1 
ATOM   8381  C  CG2 . THR   C  1 196 ? 41.360  15.498  -77.960  1.00 71.62  ? 497  THR   C CG2 1 
ATOM   8382  N  N   . LEU   C  1 197 ? 44.353  15.506  -79.239  1.00 65.95  ? 498  LEU   C N   1 
ATOM   8383  C  CA  . LEU   C  1 197 ? 45.037  16.550  -79.992  1.00 60.90  ? 498  LEU   C CA  1 
ATOM   8384  C  C   . LEU   C  1 197 ? 44.019  17.464  -80.659  1.00 61.24  ? 498  LEU   C C   1 
ATOM   8385  O  O   . LEU   C  1 197 ? 43.019  16.995  -81.208  1.00 61.98  ? 498  LEU   C O   1 
ATOM   8386  C  CB  . LEU   C  1 197 ? 45.970  15.948  -81.048  1.00 59.40  ? 498  LEU   C CB  1 
ATOM   8387  C  CG  . LEU   C  1 197 ? 46.591  16.979  -81.993  1.00 60.46  ? 498  LEU   C CG  1 
ATOM   8388  C  CD1 . LEU   C  1 197 ? 47.539  17.899  -81.249  1.00 63.92  ? 498  LEU   C CD1 1 
ATOM   8389  C  CD2 . LEU   C  1 197 ? 47.289  16.310  -83.159  1.00 64.66  ? 498  LEU   C CD2 1 
ATOM   8390  N  N   . GLY   C  1 198 ? 44.274  18.770  -80.612  1.00 62.44  ? 499  GLY   C N   1 
ATOM   8391  C  CA  . GLY   C  1 198 ? 43.323  19.741  -81.130  1.00 62.85  ? 499  GLY   C CA  1 
ATOM   8392  C  C   . GLY   C  1 198 ? 42.230  20.119  -80.144  1.00 63.54  ? 499  GLY   C C   1 
ATOM   8393  O  O   . GLY   C  1 198 ? 42.511  20.357  -78.969  1.00 70.71  ? 499  GLY   C O   1 
ATOM   8394  N  N   . ASP   C  1 199 ? 40.974  20.159  -80.608  1.00 55.13  ? 500  ASP   C N   1 
ATOM   8395  C  CA  . ASP   C  1 199 ? 39.840  20.626  -79.816  1.00 47.97  ? 500  ASP   C CA  1 
ATOM   8396  C  C   . ASP   C  1 199 ? 38.989  19.434  -79.413  1.00 55.07  ? 500  ASP   C C   1 
ATOM   8397  O  O   . ASP   C  1 199 ? 38.290  18.863  -80.266  1.00 50.07  ? 500  ASP   C O   1 
ATOM   8398  C  CB  . ASP   C  1 199 ? 39.003  21.627  -80.610  1.00 50.08  ? 500  ASP   C CB  1 
ATOM   8399  C  CG  . ASP   C  1 199 ? 37.878  22.261  -79.796  1.00 53.26  ? 500  ASP   C CG  1 
ATOM   8400  O  OD1 . ASP   C  1 199 ? 37.299  21.606  -78.894  1.00 60.76  ? 500  ASP   C OD1 1 
ATOM   8401  O  OD2 . ASP   C  1 199 ? 37.563  23.440  -80.079  1.00 49.80  ? 500  ASP   C OD2 1 
ATOM   8402  N  N   . PRO   C  1 200 ? 38.968  19.057  -78.130  1.00 50.01  ? 501  PRO   C N   1 
ATOM   8403  C  CA  . PRO   C  1 200 ? 38.288  17.811  -77.743  1.00 48.49  ? 501  PRO   C CA  1 
ATOM   8404  C  C   . PRO   C  1 200 ? 36.780  17.832  -77.946  1.00 49.23  ? 501  PRO   C C   1 
ATOM   8405  O  O   . PRO   C  1 200 ? 36.186  16.757  -78.104  1.00 55.15  ? 501  PRO   C O   1 
ATOM   8406  C  CB  . PRO   C  1 200 ? 38.661  17.659  -76.261  1.00 45.33  ? 501  PRO   C CB  1 
ATOM   8407  C  CG  . PRO   C  1 200 ? 39.949  18.418  -76.138  1.00 44.35  ? 501  PRO   C CG  1 
ATOM   8408  C  CD  . PRO   C  1 200 ? 39.773  19.611  -77.032  1.00 43.30  ? 501  PRO   C CD  1 
ATOM   8409  N  N   . ALA   C  1 201 ? 36.141  19.007  -77.963  1.00 43.77  ? 502  ALA   C N   1 
ATOM   8410  C  CA  . ALA   C  1 201 ? 34.695  19.055  -78.180  1.00 45.61  ? 502  ALA   C CA  1 
ATOM   8411  C  C   . ALA   C  1 201 ? 34.316  18.550  -79.569  1.00 54.78  ? 502  ALA   C C   1 
ATOM   8412  O  O   . ALA   C  1 201 ? 33.197  18.066  -79.782  1.00 48.82  ? 502  ALA   C O   1 
ATOM   8413  C  CB  . ALA   C  1 201 ? 34.185  20.483  -77.981  1.00 47.49  ? 502  ALA   C CB  1 
ATOM   8414  N  N   . ASN   C  1 202 ? 35.234  18.646  -80.519  1.00 54.92  ? 503  ASN   C N   1 
ATOM   8415  C  CA  . ASN   C  1 202 ? 34.953  18.304  -81.899  1.00 48.08  ? 503  ASN   C CA  1 
ATOM   8416  C  C   . ASN   C  1 202 ? 35.471  16.926  -82.277  1.00 55.17  ? 503  ASN   C C   1 
ATOM   8417  O  O   . ASN   C  1 202 ? 35.401  16.553  -83.448  1.00 61.50  ? 503  ASN   C O   1 
ATOM   8418  C  CB  . ASN   C  1 202 ? 35.537  19.383  -82.795  1.00 36.23  ? 503  ASN   C CB  1 
ATOM   8419  C  CG  . ASN   C  1 202 ? 34.893  20.724  -82.548  1.00 40.40  ? 503  ASN   C CG  1 
ATOM   8420  O  OD1 . ASN   C  1 202 ? 33.669  20.804  -82.343  1.00 46.68  ? 503  ASN   C OD1 1 
ATOM   8421  N  ND2 . ASN   C  1 202 ? 35.706  21.791  -82.534  1.00 36.86  ? 503  ASN   C ND2 1 
ATOM   8422  N  N   . VAL   C  1 203 ? 35.964  16.155  -81.302  1.00 59.61  ? 504  VAL   C N   1 
ATOM   8423  C  CA  . VAL   C  1 203 ? 36.512  14.831  -81.585  1.00 60.59  ? 504  VAL   C CA  1 
ATOM   8424  C  C   . VAL   C  1 203 ? 35.509  13.995  -82.364  1.00 61.66  ? 504  VAL   C C   1 
ATOM   8425  O  O   . VAL   C  1 203 ? 35.852  13.357  -83.370  1.00 67.74  ? 504  VAL   C O   1 
ATOM   8426  C  CB  . VAL   C  1 203 ? 36.927  14.132  -80.278  1.00 58.84  ? 504  VAL   C CB  1 
ATOM   8427  C  CG1 . VAL   C  1 203 ? 37.141  12.646  -80.525  1.00 51.06  ? 504  VAL   C CG1 1 
ATOM   8428  C  CG2 . VAL   C  1 203 ? 38.184  14.776  -79.713  1.00 58.99  ? 504  VAL   C CG2 1 
ATOM   8429  N  N   . GLN   C  1 204 ? 34.250  13.995  -81.921  1.00 52.92  ? 505  GLN   C N   1 
ATOM   8430  C  CA  . GLN   C  1 204 ? 33.263  13.144  -82.574  1.00 55.90  ? 505  GLN   C CA  1 
ATOM   8431  C  C   . GLN   C  1 204 ? 32.981  13.629  -83.990  1.00 61.64  ? 505  GLN   C C   1 
ATOM   8432  O  O   . GLN   C  1 204 ? 32.920  12.828  -84.930  1.00 62.26  ? 505  GLN   C O   1 
ATOM   8433  C  CB  . GLN   C  1 204 ? 31.967  13.086  -81.766  1.00 53.12  ? 505  GLN   C CB  1 
ATOM   8434  C  CG  . GLN   C  1 204 ? 31.046  11.978  -82.250  1.00 65.06  ? 505  GLN   C CG  1 
ATOM   8435  C  CD  . GLN   C  1 204 ? 29.610  12.132  -81.789  1.00 72.83  ? 505  GLN   C CD  1 
ATOM   8436  O  OE1 . GLN   C  1 204 ? 29.201  13.203  -81.336  1.00 70.17  ? 505  GLN   C OE1 1 
ATOM   8437  N  NE2 . GLN   C  1 204 ? 28.832  11.054  -81.903  1.00 76.27  ? 505  GLN   C NE2 1 
ATOM   8438  N  N   . PHE   C  1 205 ? 32.804  14.939  -84.160  1.00 55.53  ? 506  PHE   C N   1 
ATOM   8439  C  CA  . PHE   C  1 205 ? 32.537  15.477  -85.485  1.00 50.63  ? 506  PHE   C CA  1 
ATOM   8440  C  C   . PHE   C  1 205 ? 33.741  15.299  -86.409  1.00 53.85  ? 506  PHE   C C   1 
ATOM   8441  O  O   . PHE   C  1 205 ? 33.576  14.999  -87.598  1.00 59.08  ? 506  PHE   C O   1 
ATOM   8442  C  CB  . PHE   C  1 205 ? 32.143  16.948  -85.376  1.00 45.39  ? 506  PHE   C CB  1 
ATOM   8443  C  CG  . PHE   C  1 205 ? 31.777  17.572  -86.696  1.00 52.69  ? 506  PHE   C CG  1 
ATOM   8444  C  CD1 . PHE   C  1 205 ? 30.530  17.342  -87.262  1.00 51.45  ? 506  PHE   C CD1 1 
ATOM   8445  C  CD2 . PHE   C  1 205 ? 32.684  18.382  -87.375  1.00 52.77  ? 506  PHE   C CD2 1 
ATOM   8446  C  CE1 . PHE   C  1 205 ? 30.179  17.924  -88.472  1.00 52.22  ? 506  PHE   C CE1 1 
ATOM   8447  C  CE2 . PHE   C  1 205 ? 32.348  18.964  -88.588  1.00 52.13  ? 506  PHE   C CE2 1 
ATOM   8448  C  CZ  . PHE   C  1 205 ? 31.091  18.737  -89.140  1.00 49.03  ? 506  PHE   C CZ  1 
ATOM   8449  N  N   . THR   C  1 206 ? 34.955  15.477  -85.877  1.00 42.11  ? 507  THR   C N   1 
ATOM   8450  C  CA  . THR   C  1 206 ? 36.159  15.210  -86.650  1.00 46.03  ? 507  THR   C CA  1 
ATOM   8451  C  C   . THR   C  1 206 ? 36.184  13.776  -87.167  1.00 50.38  ? 507  THR   C C   1 
ATOM   8452  O  O   . THR   C  1 206 ? 36.582  13.529  -88.311  1.00 51.93  ? 507  THR   C O   1 
ATOM   8453  C  CB  . THR   C  1 206 ? 37.399  15.485  -85.805  1.00 50.26  ? 507  THR   C CB  1 
ATOM   8454  O  OG1 . THR   C  1 206 ? 37.393  16.848  -85.370  1.00 54.28  ? 507  THR   C OG1 1 
ATOM   8455  C  CG2 . THR   C  1 206 ? 38.658  15.221  -86.621  1.00 44.16  ? 507  THR   C CG2 1 
ATOM   8456  N  N   . GLU   C  1 207 ? 35.758  12.816  -86.343  1.00 52.89  ? 508  GLU   C N   1 
ATOM   8457  C  CA  . GLU   C  1 207 ? 35.749  11.425  -86.785  1.00 57.07  ? 508  GLU   C CA  1 
ATOM   8458  C  C   . GLU   C  1 207 ? 34.676  11.185  -87.842  1.00 57.73  ? 508  GLU   C C   1 
ATOM   8459  O  O   . GLU   C  1 207 ? 34.888  10.394  -88.767  1.00 61.24  ? 508  GLU   C O   1 
ATOM   8460  C  CB  . GLU   C  1 207 ? 35.564  10.489  -85.588  1.00 68.01  ? 508  GLU   C CB  1 
ATOM   8461  C  CG  . GLU   C  1 207 ? 36.869  10.115  -84.876  1.00 84.01  ? 508  GLU   C CG  1 
ATOM   8462  C  CD  . GLU   C  1 207 ? 36.657  9.645   -83.431  1.00 96.06  ? 508  GLU   C CD  1 
ATOM   8463  O  OE1 . GLU   C  1 207 ? 35.494  9.371   -83.048  1.00 95.31  ? 508  GLU   C OE1 1 
ATOM   8464  O  OE2 . GLU   C  1 207 ? 37.657  9.556   -82.677  1.00 98.19  ? 508  GLU   C OE2 1 
ATOM   8465  N  N   . ILE   C  1 208 ? 33.523  11.861  -87.730  1.00 55.90  ? 509  ILE   C N   1 
ATOM   8466  C  CA  . ILE   C  1 208 ? 32.497  11.763  -88.769  1.00 59.77  ? 509  ILE   C CA  1 
ATOM   8467  C  C   . ILE   C  1 208 ? 33.055  12.231  -90.104  1.00 63.57  ? 509  ILE   C C   1 
ATOM   8468  O  O   . ILE   C  1 208 ? 32.816  11.614  -91.149  1.00 71.36  ? 509  ILE   C O   1 
ATOM   8469  C  CB  . ILE   C  1 208 ? 31.247  12.578  -88.388  1.00 57.93  ? 509  ILE   C CB  1 
ATOM   8470  C  CG1 . ILE   C  1 208 ? 30.664  12.127  -87.054  1.00 58.22  ? 509  ILE   C CG1 1 
ATOM   8471  C  CG2 . ILE   C  1 208 ? 30.197  12.474  -89.488  1.00 57.71  ? 509  ILE   C CG2 1 
ATOM   8472  C  CD1 . ILE   C  1 208 ? 29.376  12.856  -86.686  1.00 52.13  ? 509  ILE   C CD1 1 
ATOM   8473  N  N   . CYS   C  1 209 ? 33.807  13.332  -90.087  1.00 60.41  ? 510  CYS   C N   1 
ATOM   8474  C  CA  . CYS   C  1 209 ? 34.400  13.853  -91.314  1.00 52.30  ? 510  CYS   C CA  1 
ATOM   8475  C  C   . CYS   C  1 209 ? 35.443  12.902  -91.868  1.00 54.47  ? 510  CYS   C C   1 
ATOM   8476  O  O   . CYS   C  1 209 ? 35.460  12.625  -93.072  1.00 59.87  ? 510  CYS   C O   1 
ATOM   8477  C  CB  . CYS   C  1 209 ? 35.024  15.219  -91.058  1.00 50.43  ? 510  CYS   C CB  1 
ATOM   8478  S  SG  . CYS   C  1 209 ? 33.839  16.481  -90.583  1.00 55.87  ? 510  CYS   C SG  1 
ATOM   8479  N  N   . ILE   C  1 210 ? 36.339  12.412  -91.002  1.00 60.56  ? 511  ILE   C N   1 
ATOM   8480  C  CA  . ILE   C  1 210 ? 37.354  11.453  -91.437  1.00 64.44  ? 511  ILE   C CA  1 
ATOM   8481  C  C   . ILE   C  1 210 ? 36.686  10.206  -91.999  1.00 66.13  ? 511  ILE   C C   1 
ATOM   8482  O  O   . ILE   C  1 210 ? 37.083  9.684   -93.049  1.00 65.87  ? 511  ILE   C O   1 
ATOM   8483  C  CB  . ILE   C  1 210 ? 38.316  11.114  -90.282  1.00 59.42  ? 511  ILE   C CB  1 
ATOM   8484  C  CG1 . ILE   C  1 210 ? 39.044  12.362  -89.791  1.00 65.48  ? 511  ILE   C CG1 1 
ATOM   8485  C  CG2 . ILE   C  1 210 ? 39.347  10.132  -90.745  1.00 56.37  ? 511  ILE   C CG2 1 
ATOM   8486  C  CD1 . ILE   C  1 210 ? 39.743  12.171  -88.457  1.00 72.88  ? 511  ILE   C CD1 1 
ATOM   8487  N  N   . GLN   C  1 211 ? 35.640  9.734   -91.323  1.00 64.56  ? 512  GLN   C N   1 
ATOM   8488  C  CA  . GLN   C  1 211 ? 34.832  8.621   -91.795  1.00 72.74  ? 512  GLN   C CA  1 
ATOM   8489  C  C   . GLN   C  1 211 ? 34.072  8.952   -93.076  1.00 72.91  ? 512  GLN   C C   1 
ATOM   8490  O  O   . GLN   C  1 211 ? 33.596  8.038   -93.755  1.00 79.29  ? 512  GLN   C O   1 
ATOM   8491  C  CB  . GLN   C  1 211 ? 33.881  8.199   -90.671  1.00 84.45  ? 512  GLN   C CB  1 
ATOM   8492  C  CG  . GLN   C  1 211 ? 32.932  7.077   -90.993  1.00 95.83  ? 512  GLN   C CG  1 
ATOM   8493  C  CD  . GLN   C  1 211 ? 31.500  7.557   -91.080  1.00 104.02 ? 512  GLN   C CD  1 
ATOM   8494  O  OE1 . GLN   C  1 211 ? 31.031  8.307   -90.219  1.00 105.77 ? 512  GLN   C OE1 1 
ATOM   8495  N  NE2 . GLN   C  1 211 ? 30.795  7.138   -92.127  1.00 107.67 ? 512  GLN   C NE2 1 
ATOM   8496  N  N   . GLN   C  1 212 ? 33.974  10.221  -93.446  1.00 66.74  ? 513  GLN   C N   1 
ATOM   8497  C  CA  . GLN   C  1 212 ? 33.387  10.598  -94.722  1.00 65.55  ? 513  GLN   C CA  1 
ATOM   8498  C  C   . GLN   C  1 212 ? 34.429  10.784  -95.809  1.00 65.57  ? 513  GLN   C C   1 
ATOM   8499  O  O   . GLN   C  1 212 ? 34.081  11.178  -96.923  1.00 61.05  ? 513  GLN   C O   1 
ATOM   8500  C  CB  . GLN   C  1 212 ? 32.570  11.882  -94.565  1.00 76.07  ? 513  GLN   C CB  1 
ATOM   8501  C  CG  . GLN   C  1 212 ? 31.224  11.660  -93.928  1.00 74.50  ? 513  GLN   C CG  1 
ATOM   8502  C  CD  . GLN   C  1 212 ? 30.449  10.590  -94.655  1.00 80.08  ? 513  GLN   C CD  1 
ATOM   8503  O  OE1 . GLN   C  1 212 ? 30.053  9.592   -94.064  1.00 85.41  ? 513  GLN   C OE1 1 
ATOM   8504  N  NE2 . GLN   C  1 212 ? 30.240  10.786  -95.950  1.00 81.61  ? 513  GLN   C NE2 1 
ATOM   8505  N  N   . GLY   C  1 213 ? 35.692  10.510  -95.515  1.00 69.99  ? 514  GLY   C N   1 
ATOM   8506  C  CA  . GLY   C  1 213 ? 36.755  10.692  -96.473  1.00 60.84  ? 514  GLY   C CA  1 
ATOM   8507  C  C   . GLY   C  1 213 ? 37.566  11.958  -96.320  1.00 60.06  ? 514  GLY   C C   1 
ATOM   8508  O  O   . GLY   C  1 213 ? 38.364  12.271  -97.212  1.00 54.76  ? 514  GLY   C O   1 
ATOM   8509  N  N   . TRP   C  1 214 ? 37.384  12.707  -95.235  1.00 59.20  ? 515  TRP   C N   1 
ATOM   8510  C  CA  . TRP   C  1 214 ? 38.262  13.840  -94.986  1.00 63.55  ? 515  TRP   C CA  1 
ATOM   8511  C  C   . TRP   C  1 214 ? 39.647  13.331  -94.599  1.00 70.47  ? 515  TRP   C C   1 
ATOM   8512  O  O   . TRP   C  1 214 ? 39.782  12.420  -93.772  1.00 66.07  ? 515  TRP   C O   1 
ATOM   8513  C  CB  . TRP   C  1 214 ? 37.688  14.741  -93.893  1.00 61.03  ? 515  TRP   C CB  1 
ATOM   8514  C  CG  . TRP   C  1 214 ? 38.428  16.036  -93.739  1.00 66.67  ? 515  TRP   C CG  1 
ATOM   8515  C  CD1 . TRP   C  1 214 ? 38.615  16.993  -94.700  1.00 62.51  ? 515  TRP   C CD1 1 
ATOM   8516  C  CD2 . TRP   C  1 214 ? 39.065  16.532  -92.551  1.00 67.77  ? 515  TRP   C CD2 1 
ATOM   8517  N  NE1 . TRP   C  1 214 ? 39.335  18.047  -94.185  1.00 64.07  ? 515  TRP   C NE1 1 
ATOM   8518  C  CE2 . TRP   C  1 214 ? 39.626  17.789  -92.870  1.00 67.82  ? 515  TRP   C CE2 1 
ATOM   8519  C  CE3 . TRP   C  1 214 ? 39.216  16.038  -91.252  1.00 71.60  ? 515  TRP   C CE3 1 
ATOM   8520  C  CZ2 . TRP   C  1 214 ? 40.327  18.557  -91.933  1.00 65.29  ? 515  TRP   C CZ2 1 
ATOM   8521  C  CZ3 . TRP   C  1 214 ? 39.916  16.805  -90.320  1.00 71.02  ? 515  TRP   C CZ3 1 
ATOM   8522  C  CH2 . TRP   C  1 214 ? 40.465  18.045  -90.670  1.00 67.00  ? 515  TRP   C CH2 1 
ATOM   8523  N  N   . LYS   C  1 215 ? 40.673  13.898  -95.231  1.00 74.23  ? 516  LYS   C N   1 
ATOM   8524  C  CA  . LYS   C  1 215 ? 42.060  13.601  -94.908  1.00 76.97  ? 516  LYS   C CA  1 
ATOM   8525  C  C   . LYS   C  1 215 ? 42.520  14.566  -93.830  1.00 75.91  ? 516  LYS   C C   1 
ATOM   8526  O  O   . LYS   C  1 215 ? 42.770  15.745  -94.110  1.00 77.85  ? 516  LYS   C O   1 
ATOM   8527  C  CB  . LYS   C  1 215 ? 42.950  13.717  -96.141  1.00 83.64  ? 516  LYS   C CB  1 
ATOM   8528  C  CG  . LYS   C  1 215 ? 42.645  12.689  -97.205  1.00 93.15  ? 516  LYS   C CG  1 
ATOM   8529  C  CD  . LYS   C  1 215 ? 43.214  11.330  -96.829  1.00 98.91  ? 516  LYS   C CD  1 
ATOM   8530  C  CE  . LYS   C  1 215 ? 42.946  10.291  -97.913  1.00 96.83  ? 516  LYS   C CE  1 
ATOM   8531  N  NZ  . LYS   C  1 215 ? 41.501  9.940   -97.961  1.00 90.91  ? 516  LYS   C NZ  1 
ATOM   8532  N  N   . PRO   C  1 216 ? 42.625  14.118  -92.590  1.00 71.85  ? 517  PRO   C N   1 
ATOM   8533  C  CA  . PRO   C  1 216 ? 43.064  15.009  -91.525  1.00 75.05  ? 517  PRO   C CA  1 
ATOM   8534  C  C   . PRO   C  1 216 ? 44.545  15.312  -91.655  1.00 76.22  ? 517  PRO   C C   1 
ATOM   8535  O  O   . PRO   C  1 216 ? 45.370  14.391  -91.751  1.00 75.37  ? 517  PRO   C O   1 
ATOM   8536  C  CB  . PRO   C  1 216 ? 42.766  14.206  -90.253  1.00 78.83  ? 517  PRO   C CB  1 
ATOM   8537  C  CG  . PRO   C  1 216 ? 42.865  12.777  -90.696  1.00 80.82  ? 517  PRO   C CG  1 
ATOM   8538  C  CD  . PRO   C  1 216 ? 42.350  12.754  -92.109  1.00 71.87  ? 517  PRO   C CD  1 
ATOM   8539  N  N   . PRO   C  1 217 ? 44.927  16.590  -91.686  1.00 72.11  ? 518  PRO   C N   1 
ATOM   8540  C  CA  . PRO   C  1 217 ? 46.348  16.933  -91.501  1.00 66.92  ? 518  PRO   C CA  1 
ATOM   8541  C  C   . PRO   C  1 217 ? 46.861  16.598  -90.103  1.00 61.92  ? 518  PRO   C C   1 
ATOM   8542  O  O   . PRO   C  1 217 ? 48.080  16.604  -89.885  1.00 63.77  ? 518  PRO   C O   1 
ATOM   8543  C  CB  . PRO   C  1 217 ? 46.392  18.444  -91.775  1.00 63.62  ? 518  PRO   C CB  1 
ATOM   8544  C  CG  . PRO   C  1 217 ? 44.968  18.919  -91.678  1.00 56.06  ? 518  PRO   C CG  1 
ATOM   8545  C  CD  . PRO   C  1 217 ? 44.093  17.758  -92.021  1.00 61.96  ? 518  PRO   C CD  1 
ATOM   8546  N  N   . ARG   C  1 218 ? 45.963  16.307  -89.164  1.00 60.93  ? 519  ARG   C N   1 
ATOM   8547  C  CA  . ARG   C  1 218 ? 46.306  15.856  -87.810  1.00 71.90  ? 519  ARG   C CA  1 
ATOM   8548  C  C   . ARG   C  1 218 ? 47.198  16.853  -87.067  1.00 75.43  ? 519  ARG   C C   1 
ATOM   8549  O  O   . ARG   C  1 218 ? 48.265  16.513  -86.546  1.00 73.72  ? 519  ARG   C O   1 
ATOM   8550  C  CB  . ARG   C  1 218 ? 46.919  14.457  -87.839  1.00 72.56  ? 519  ARG   C CB  1 
ATOM   8551  C  CG  . ARG   C  1 218 ? 45.883  13.411  -88.226  1.00 76.04  ? 519  ARG   C CG  1 
ATOM   8552  C  CD  . ARG   C  1 218 ? 46.207  12.012  -87.734  1.00 79.92  ? 519  ARG   C CD  1 
ATOM   8553  N  NE  . ARG   C  1 218 ? 45.092  11.097  -87.988  1.00 85.66  ? 519  ARG   C NE  1 
ATOM   8554  C  CZ  . ARG   C  1 218 ? 44.185  10.729  -87.081  1.00 89.83  ? 519  ARG   C CZ  1 
ATOM   8555  N  NH1 . ARG   C  1 218 ? 43.206  9.896   -87.424  1.00 94.85  ? 519  ARG   C NH1 1 
ATOM   8556  N  NH2 . ARG   C  1 218 ? 44.257  11.177  -85.832  1.00 81.90  ? 519  ARG   C NH2 1 
ATOM   8557  N  N   . GLY   C  1 219 ? 46.716  18.093  -86.982  1.00 75.03  ? 520  GLY   C N   1 
ATOM   8558  C  CA  . GLY   C  1 219 ? 47.361  19.146  -86.220  1.00 71.61  ? 520  GLY   C CA  1 
ATOM   8559  C  C   . GLY   C  1 219 ? 46.474  19.690  -85.121  1.00 69.96  ? 520  GLY   C C   1 
ATOM   8560  O  O   . GLY   C  1 219 ? 45.368  19.197  -84.892  1.00 69.74  ? 520  GLY   C O   1 
ATOM   8561  N  N   . ARG   C  1 220 ? 46.955  20.716  -84.424  1.00 70.54  ? 521  ARG   C N   1 
ATOM   8562  C  CA  . ARG   C  1 220 ? 46.236  21.281  -83.299  1.00 61.41  ? 521  ARG   C CA  1 
ATOM   8563  C  C   . ARG   C  1 220 ? 45.185  22.295  -83.719  1.00 62.51  ? 521  ARG   C C   1 
ATOM   8564  O  O   . ARG   C  1 220 ? 44.216  22.505  -82.977  1.00 63.12  ? 521  ARG   C O   1 
ATOM   8565  C  CB  . ARG   C  1 220 ? 47.231  21.932  -82.334  1.00 64.49  ? 521  ARG   C CB  1 
ATOM   8566  C  CG  . ARG   C  1 220 ? 46.661  22.343  -80.997  1.00 67.32  ? 521  ARG   C CG  1 
ATOM   8567  C  CD  . ARG   C  1 220 ? 47.717  22.196  -79.919  1.00 73.99  ? 521  ARG   C CD  1 
ATOM   8568  N  NE  . ARG   C  1 220 ? 47.124  22.216  -78.590  1.00 78.36  ? 521  ARG   C NE  1 
ATOM   8569  C  CZ  . ARG   C  1 220 ? 47.435  23.098  -77.647  1.00 81.39  ? 521  ARG   C CZ  1 
ATOM   8570  N  NH1 . ARG   C  1 220 ? 48.355  24.029  -77.881  1.00 80.35  ? 521  ARG   C NH1 1 
ATOM   8571  N  NH2 . ARG   C  1 220 ? 46.832  23.037  -76.467  1.00 80.51  ? 521  ARG   C NH2 1 
ATOM   8572  N  N   . PHE   C  1 221 ? 45.349  22.934  -84.895  1.00 54.70  ? 522  PHE   C N   1 
ATOM   8573  C  CA  . PHE   C  1 221 ? 44.428  23.955  -85.382  1.00 56.89  ? 522  PHE   C CA  1 
ATOM   8574  C  C   . PHE   C  1 221 ? 44.111  23.665  -86.856  1.00 66.13  ? 522  PHE   C C   1 
ATOM   8575  O  O   . PHE   C  1 221 ? 44.466  24.414  -87.770  1.00 71.38  ? 522  PHE   C O   1 
ATOM   8576  C  CB  . PHE   C  1 221 ? 45.006  25.358  -85.181  1.00 59.06  ? 522  PHE   C CB  1 
ATOM   8577  C  CG  . PHE   C  1 221 ? 45.314  25.689  -83.738  1.00 60.77  ? 522  PHE   C CG  1 
ATOM   8578  C  CD1 . PHE   C  1 221 ? 44.326  26.171  -82.898  1.00 64.21  ? 522  PHE   C CD1 1 
ATOM   8579  C  CD2 . PHE   C  1 221 ? 46.586  25.513  -83.220  1.00 58.26  ? 522  PHE   C CD2 1 
ATOM   8580  C  CE1 . PHE   C  1 221 ? 44.600  26.469  -81.562  1.00 55.90  ? 522  PHE   C CE1 1 
ATOM   8581  C  CE2 . PHE   C  1 221 ? 46.861  25.809  -81.891  1.00 60.33  ? 522  PHE   C CE2 1 
ATOM   8582  C  CZ  . PHE   C  1 221 ? 45.869  26.284  -81.064  1.00 50.85  ? 522  PHE   C CZ  1 
ATOM   8583  N  N   . ASP   C  1 222 ? 43.441  22.534  -87.091  1.00 63.23  ? 523  ASP   C N   1 
ATOM   8584  C  CA  . ASP   C  1 222 ? 42.999  22.123  -88.422  1.00 53.50  ? 523  ASP   C CA  1 
ATOM   8585  C  C   . ASP   C  1 222 ? 41.561  22.589  -88.616  1.00 51.52  ? 523  ASP   C C   1 
ATOM   8586  O  O   . ASP   C  1 222 ? 40.645  22.062  -87.979  1.00 53.97  ? 523  ASP   C O   1 
ATOM   8587  C  CB  . ASP   C  1 222 ? 43.074  20.603  -88.582  1.00 62.12  ? 523  ASP   C CB  1 
ATOM   8588  C  CG  . ASP   C  1 222 ? 44.496  20.061  -88.532  1.00 68.53  ? 523  ASP   C CG  1 
ATOM   8589  O  OD1 . ASP   C  1 222 ? 45.454  20.862  -88.563  1.00 71.68  ? 523  ASP   C OD1 1 
ATOM   8590  O  OD2 . ASP   C  1 222 ? 44.650  18.819  -88.474  1.00 64.92  ? 523  ASP   C OD2 1 
ATOM   8591  N  N   . VAL   C  1 223 ? 41.348  23.566  -89.497  1.00 53.21  ? 524  VAL   C N   1 
ATOM   8592  C  CA  . VAL   C  1 223 ? 39.984  24.015  -89.757  1.00 45.94  ? 524  VAL   C CA  1 
ATOM   8593  C  C   . VAL   C  1 223 ? 39.180  22.851  -90.310  1.00 44.66  ? 524  VAL   C C   1 
ATOM   8594  O  O   . VAL   C  1 223 ? 39.587  22.204  -91.279  1.00 47.23  ? 524  VAL   C O   1 
ATOM   8595  C  CB  . VAL   C  1 223 ? 39.984  25.214  -90.716  1.00 46.84  ? 524  VAL   C CB  1 
ATOM   8596  C  CG1 . VAL   C  1 223 ? 38.558  25.578  -91.117  1.00 45.87  ? 524  VAL   C CG1 1 
ATOM   8597  C  CG2 . VAL   C  1 223 ? 40.685  26.402  -90.070  1.00 35.25  ? 524  VAL   C CG2 1 
ATOM   8598  N  N   . LEU   C  1 224 ? 38.041  22.567  -89.690  1.00 42.82  ? 525  LEU   C N   1 
ATOM   8599  C  CA  . LEU   C  1 224 ? 37.239  21.439  -90.134  1.00 46.09  ? 525  LEU   C CA  1 
ATOM   8600  C  C   . LEU   C  1 224 ? 36.589  21.746  -91.482  1.00 45.83  ? 525  LEU   C C   1 
ATOM   8601  O  O   . LEU   C  1 224 ? 36.355  22.909  -91.815  1.00 44.03  ? 525  LEU   C O   1 
ATOM   8602  C  CB  . LEU   C  1 224 ? 36.161  21.106  -89.109  1.00 51.06  ? 525  LEU   C CB  1 
ATOM   8603  C  CG  . LEU   C  1 224 ? 36.642  20.472  -87.806  1.00 57.85  ? 525  LEU   C CG  1 
ATOM   8604  C  CD1 . LEU   C  1 224 ? 35.619  20.698  -86.728  1.00 46.38  ? 525  LEU   C CD1 1 
ATOM   8605  C  CD2 . LEU   C  1 224 ? 36.894  18.982  -88.015  1.00 67.46  ? 525  LEU   C CD2 1 
ATOM   8606  N  N   . PRO   C  1 225 ? 36.307  20.724  -92.287  1.00 47.23  ? 526  PRO   C N   1 
ATOM   8607  C  CA  . PRO   C  1 225 ? 35.531  20.954  -93.507  1.00 41.45  ? 526  PRO   C CA  1 
ATOM   8608  C  C   . PRO   C  1 225 ? 34.075  21.172  -93.148  1.00 41.40  ? 526  PRO   C C   1 
ATOM   8609  O  O   . PRO   C  1 225 ? 33.615  20.799  -92.068  1.00 50.58  ? 526  PRO   C O   1 
ATOM   8610  C  CB  . PRO   C  1 225 ? 35.718  19.657  -94.299  1.00 39.11  ? 526  PRO   C CB  1 
ATOM   8611  C  CG  . PRO   C  1 225 ? 35.892  18.622  -93.244  1.00 47.37  ? 526  PRO   C CG  1 
ATOM   8612  C  CD  . PRO   C  1 225 ? 36.656  19.300  -92.122  1.00 41.28  ? 526  PRO   C CD  1 
ATOM   8613  N  N   . LEU   C  1 226 ? 33.343  21.797  -94.063  1.00 44.70  ? 527  LEU   C N   1 
ATOM   8614  C  CA  . LEU   C  1 226 ? 31.896  21.867  -93.919  1.00 49.77  ? 527  LEU   C CA  1 
ATOM   8615  C  C   . LEU   C  1 226 ? 31.281  20.517  -94.278  1.00 53.51  ? 527  LEU   C C   1 
ATOM   8616  O  O   . LEU   C  1 226 ? 31.733  19.845  -95.207  1.00 52.12  ? 527  LEU   C O   1 
ATOM   8617  C  CB  . LEU   C  1 226 ? 31.316  22.972  -94.804  1.00 45.08  ? 527  LEU   C CB  1 
ATOM   8618  C  CG  . LEU   C  1 226 ? 31.761  24.406  -94.476  1.00 44.09  ? 527  LEU   C CG  1 
ATOM   8619  C  CD1 . LEU   C  1 226 ? 31.397  25.353  -95.595  1.00 43.98  ? 527  LEU   C CD1 1 
ATOM   8620  C  CD2 . LEU   C  1 226 ? 31.183  24.915  -93.143  1.00 37.91  ? 527  LEU   C CD2 1 
ATOM   8621  N  N   . LEU   C  1 227 ? 30.286  20.095  -93.498  1.00 55.97  ? 528  LEU   C N   1 
ATOM   8622  C  CA  . LEU   C  1 227 ? 29.492  18.900  -93.785  1.00 48.95  ? 528  LEU   C CA  1 
ATOM   8623  C  C   . LEU   C  1 227 ? 28.060  19.383  -93.980  1.00 54.04  ? 528  LEU   C C   1 
ATOM   8624  O  O   . LEU   C  1 227 ? 27.367  19.681  -93.000  1.00 47.19  ? 528  LEU   C O   1 
ATOM   8625  C  CB  . LEU   C  1 227 ? 29.580  17.871  -92.661  1.00 39.57  ? 528  LEU   C CB  1 
ATOM   8626  C  CG  . LEU   C  1 227 ? 29.900  16.392  -92.930  1.00 48.57  ? 528  LEU   C CG  1 
ATOM   8627  C  CD1 . LEU   C  1 227 ? 29.215  15.491  -91.893  1.00 43.23  ? 528  LEU   C CD1 1 
ATOM   8628  C  CD2 . LEU   C  1 227 ? 29.619  15.919  -94.381  1.00 41.12  ? 528  LEU   C CD2 1 
ATOM   8629  N  N   . LEU   C  1 228 ? 27.625  19.478  -95.239  1.00 53.59  ? 529  LEU   C N   1 
ATOM   8630  C  CA  . LEU   C  1 228 ? 26.383  20.156  -95.590  1.00 47.44  ? 529  LEU   C CA  1 
ATOM   8631  C  C   . LEU   C  1 228 ? 25.342  19.164  -96.089  1.00 48.48  ? 529  LEU   C C   1 
ATOM   8632  O  O   . LEU   C  1 228 ? 25.635  18.321  -96.945  1.00 47.06  ? 529  LEU   C O   1 
ATOM   8633  C  CB  . LEU   C  1 228 ? 26.639  21.229  -96.645  1.00 40.72  ? 529  LEU   C CB  1 
ATOM   8634  C  CG  . LEU   C  1 228 ? 27.754  22.210  -96.271  1.00 42.72  ? 529  LEU   C CG  1 
ATOM   8635  C  CD1 . LEU   C  1 228 ? 27.863  23.334  -97.292  1.00 29.42  ? 529  LEU   C CD1 1 
ATOM   8636  C  CD2 . LEU   C  1 228 ? 27.557  22.813  -94.896  1.00 28.72  ? 529  LEU   C CD2 1 
ATOM   8637  N  N   . GLN   C  1 229 ? 24.126  19.273  -95.552  1.00 49.07  ? 530  GLN   C N   1 
ATOM   8638  C  CA  . GLN   C  1 229 ? 23.003  18.426  -95.937  1.00 47.35  ? 530  GLN   C CA  1 
ATOM   8639  C  C   . GLN   C  1 229 ? 21.862  19.280  -96.476  1.00 41.01  ? 530  GLN   C C   1 
ATOM   8640  O  O   . GLN   C  1 229 ? 21.393  20.205  -95.797  1.00 37.75  ? 530  GLN   C O   1 
ATOM   8641  C  CB  . GLN   C  1 229 ? 22.509  17.599  -94.757  1.00 48.14  ? 530  GLN   C CB  1 
ATOM   8642  C  CG  . GLN   C  1 229 ? 21.173  16.965  -95.034  1.00 51.62  ? 530  GLN   C CG  1 
ATOM   8643  C  CD  . GLN   C  1 229 ? 20.565  16.312  -93.822  1.00 53.96  ? 530  GLN   C CD  1 
ATOM   8644  O  OE1 . GLN   C  1 229 ? 20.874  16.665  -92.683  1.00 48.21  ? 530  GLN   C OE1 1 
ATOM   8645  N  NE2 . GLN   C  1 229 ? 19.695  15.340  -94.060  1.00 63.50  ? 530  GLN   C NE2 1 
ATOM   8646  N  N   . ALA   C  1 230 ? 21.414  18.959  -97.687  1.00 47.65  ? 531  ALA   C N   1 
ATOM   8647  C  CA  . ALA   C  1 230 ? 20.341  19.668  -98.373  1.00 47.97  ? 531  ALA   C CA  1 
ATOM   8648  C  C   . ALA   C  1 230 ? 19.223  18.699  -98.714  1.00 46.81  ? 531  ALA   C C   1 
ATOM   8649  O  O   . ALA   C  1 230 ? 19.482  17.577  -99.162  1.00 39.66  ? 531  ALA   C O   1 
ATOM   8650  C  CB  . ALA   C  1 230 ? 20.837  20.325  -99.653  1.00 58.35  ? 531  ALA   C CB  1 
ATOM   8651  N  N   . ASN   C  1 231 ? 17.986  19.136  -98.477  1.00 48.90  ? 532  ASN   C N   1 
ATOM   8652  C  CA  . ASN   C  1 231 ? 16.784  18.368  -98.805  1.00 52.71  ? 532  ASN   C CA  1 
ATOM   8653  C  C   . ASN   C  1 231 ? 16.846  16.919  -98.306  1.00 53.54  ? 532  ASN   C C   1 
ATOM   8654  O  O   . ASN   C  1 231 ? 16.474  15.982  -99.011  1.00 58.66  ? 532  ASN   C O   1 
ATOM   8655  C  CB  . ASN   C  1 231 ? 16.518  18.410  -100.306 1.00 58.63  ? 532  ASN   C CB  1 
ATOM   8656  C  CG  . ASN   C  1 231 ? 15.065  18.180  -100.631 1.00 69.09  ? 532  ASN   C CG  1 
ATOM   8657  O  OD1 . ASN   C  1 231 ? 14.177  18.591  -99.879  1.00 70.50  ? 532  ASN   C OD1 1 
ATOM   8658  N  ND2 . ASN   C  1 231 ? 14.808  17.505  -101.749 1.00 73.32  ? 532  ASN   C ND2 1 
ATOM   8659  N  N   . GLY   C  1 232 ? 17.305  16.732  -97.072  1.00 54.92  ? 533  GLY   C N   1 
ATOM   8660  C  CA  . GLY   C  1 232 ? 17.285  15.427  -96.437  1.00 52.78  ? 533  GLY   C CA  1 
ATOM   8661  C  C   . GLY   C  1 232 ? 18.284  14.411  -96.953  1.00 62.16  ? 533  GLY   C C   1 
ATOM   8662  O  O   . GLY   C  1 232 ? 18.299  13.276  -96.454  1.00 61.17  ? 533  GLY   C O   1 
ATOM   8663  N  N   . ASN   C  1 233 ? 19.123  14.769  -97.923  1.00 60.63  ? 534  ASN   C N   1 
ATOM   8664  C  CA  . ASN   C  1 233 ? 20.049  13.815  -98.510  1.00 59.18  ? 534  ASN   C CA  1 
ATOM   8665  C  C   . ASN   C  1 233 ? 21.273  13.609  -97.610  1.00 51.46  ? 534  ASN   C C   1 
ATOM   8666  O  O   . ASN   C  1 233 ? 21.463  14.287  -96.599  1.00 50.84  ? 534  ASN   C O   1 
ATOM   8667  C  CB  . ASN   C  1 233 ? 20.462  14.280  -99.907  1.00 62.24  ? 534  ASN   C CB  1 
ATOM   8668  C  CG  . ASN   C  1 233 ? 19.281  14.331  -100.876 1.00 61.82  ? 534  ASN   C CG  1 
ATOM   8669  O  OD1 . ASN   C  1 233 ? 18.725  13.297  -101.245 1.00 70.42  ? 534  ASN   C OD1 1 
ATOM   8670  N  ND2 . ASN   C  1 233 ? 18.891  15.530  -101.279 1.00 53.07  ? 534  ASN   C ND2 1 
ATOM   8671  N  N   . ASP   C  1 234 ? 22.099  12.636  -97.981  1.00 50.23  ? 535  ASP   C N   1 
ATOM   8672  C  CA  . ASP   C  1 234 ? 23.358  12.425  -97.283  1.00 50.61  ? 535  ASP   C CA  1 
ATOM   8673  C  C   . ASP   C  1 234 ? 24.215  13.694  -97.332  1.00 53.31  ? 535  ASP   C C   1 
ATOM   8674  O  O   . ASP   C  1 234 ? 24.246  14.389  -98.353  1.00 54.73  ? 535  ASP   C O   1 
ATOM   8675  C  CB  . ASP   C  1 234 ? 24.124  11.250  -97.896  1.00 61.06  ? 535  ASP   C CB  1 
ATOM   8676  C  CG  . ASP   C  1 234 ? 23.485  9.900   -97.599  1.00 64.44  ? 535  ASP   C CG  1 
ATOM   8677  O  OD1 . ASP   C  1 234 ? 22.558  9.837   -96.760  1.00 62.55  ? 535  ASP   C OD1 1 
ATOM   8678  O  OD2 . ASP   C  1 234 ? 23.920  8.899   -98.214  1.00 65.70  ? 535  ASP   C OD2 1 
ATOM   8679  N  N   . PRO   C  1 235 ? 24.898  14.040  -96.243  1.00 57.53  ? 536  PRO   C N   1 
ATOM   8680  C  CA  . PRO   C  1 235 ? 25.734  15.246  -96.244  1.00 52.87  ? 536  PRO   C CA  1 
ATOM   8681  C  C   . PRO   C  1 235 ? 26.967  15.105  -97.127  1.00 49.46  ? 536  PRO   C C   1 
ATOM   8682  O  O   . PRO   C  1 235 ? 27.423  14.005  -97.442  1.00 51.00  ? 536  PRO   C O   1 
ATOM   8683  C  CB  . PRO   C  1 235 ? 26.127  15.405  -94.771  1.00 42.65  ? 536  PRO   C CB  1 
ATOM   8684  C  CG  . PRO   C  1 235 ? 25.918  14.056  -94.169  1.00 49.11  ? 536  PRO   C CG  1 
ATOM   8685  C  CD  . PRO   C  1 235 ? 24.747  13.476  -94.892  1.00 48.13  ? 536  PRO   C CD  1 
ATOM   8686  N  N   . GLU   C  1 236 ? 27.524  16.260  -97.506  1.00 45.74  ? 537  GLU   C N   1 
ATOM   8687  C  CA  . GLU   C  1 236 ? 28.655  16.344  -98.422  1.00 44.70  ? 537  GLU   C CA  1 
ATOM   8688  C  C   . GLU   C  1 236 ? 29.754  17.230  -97.841  1.00 43.59  ? 537  GLU   C C   1 
ATOM   8689  O  O   . GLU   C  1 236 ? 29.473  18.299  -97.294  1.00 40.14  ? 537  GLU   C O   1 
ATOM   8690  C  CB  . GLU   C  1 236 ? 28.184  16.881  -99.787  1.00 39.48  ? 537  GLU   C CB  1 
ATOM   8691  C  CG  . GLU   C  1 236 ? 26.968  16.121  -100.316 1.00 43.96  ? 537  GLU   C CG  1 
ATOM   8692  C  CD  . GLU   C  1 236 ? 26.538  16.520  -101.732 1.00 55.67  ? 537  GLU   C CD  1 
ATOM   8693  O  OE1 . GLU   C  1 236 ? 27.347  17.099  -102.497 1.00 57.64  ? 537  GLU   C OE1 1 
ATOM   8694  O  OE2 . GLU   C  1 236 ? 25.372  16.233  -102.081 1.00 56.52  ? 537  GLU   C OE2 1 
ATOM   8695  N  N   . LEU   C  1 237 ? 31.006  16.788  -97.967  1.00 40.06  ? 538  LEU   C N   1 
ATOM   8696  C  CA  . LEU   C  1 237 ? 32.143  17.557  -97.474  1.00 41.17  ? 538  LEU   C CA  1 
ATOM   8697  C  C   . LEU   C  1 237 ? 32.561  18.653  -98.457  1.00 45.37  ? 538  LEU   C C   1 
ATOM   8698  O  O   . LEU   C  1 237 ? 32.493  18.482  -99.675  1.00 50.62  ? 538  LEU   C O   1 
ATOM   8699  C  CB  . LEU   C  1 237 ? 33.335  16.637  -97.192  1.00 37.84  ? 538  LEU   C CB  1 
ATOM   8700  C  CG  . LEU   C  1 237 ? 33.236  15.721  -95.962  1.00 55.40  ? 538  LEU   C CG  1 
ATOM   8701  C  CD1 . LEU   C  1 237 ? 34.329  14.663  -95.958  1.00 59.75  ? 538  LEU   C CD1 1 
ATOM   8702  C  CD2 . LEU   C  1 237 ? 33.262  16.523  -94.654  1.00 52.51  ? 538  LEU   C CD2 1 
ATOM   8703  N  N   . PHE   C  1 238 ? 33.006  19.785  -97.900  1.00 47.15  ? 539  PHE   C N   1 
ATOM   8704  C  CA  . PHE   C  1 238 ? 33.534  20.928  -98.638  1.00 44.90  ? 539  PHE   C CA  1 
ATOM   8705  C  C   . PHE   C  1 238 ? 34.623  21.603  -97.816  1.00 53.64  ? 539  PHE   C C   1 
ATOM   8706  O  O   . PHE   C  1 238 ? 34.410  21.881  -96.633  1.00 60.84  ? 539  PHE   C O   1 
ATOM   8707  C  CB  . PHE   C  1 238 ? 32.435  21.950  -98.926  1.00 44.84  ? 539  PHE   C CB  1 
ATOM   8708  C  CG  . PHE   C  1 238 ? 31.313  21.418  -99.750  1.00 47.56  ? 539  PHE   C CG  1 
ATOM   8709  C  CD1 . PHE   C  1 238 ? 30.227  20.798  -99.148  1.00 46.01  ? 539  PHE   C CD1 1 
ATOM   8710  C  CD2 . PHE   C  1 238 ? 31.340  21.540  -101.135 1.00 43.65  ? 539  PHE   C CD2 1 
ATOM   8711  C  CE1 . PHE   C  1 238 ? 29.191  20.298  -99.908  1.00 48.91  ? 539  PHE   C CE1 1 
ATOM   8712  C  CE2 . PHE   C  1 238 ? 30.302  21.048  -101.910 1.00 42.68  ? 539  PHE   C CE2 1 
ATOM   8713  C  CZ  . PHE   C  1 238 ? 29.223  20.431  -101.305 1.00 45.01  ? 539  PHE   C CZ  1 
ATOM   8714  N  N   . GLN   C  1 239 ? 35.764  21.905  -98.436  1.00 57.30  ? 540  GLN   C N   1 
ATOM   8715  C  CA  . GLN   C  1 239 ? 36.825  22.652  -97.760  1.00 54.38  ? 540  GLN   C CA  1 
ATOM   8716  C  C   . GLN   C  1 239 ? 36.622  24.147  -97.986  1.00 41.47  ? 540  GLN   C C   1 
ATOM   8717  O  O   . GLN   C  1 239 ? 36.612  24.609  -99.132  1.00 46.01  ? 540  GLN   C O   1 
ATOM   8718  C  CB  . GLN   C  1 239 ? 38.207  22.227  -98.257  1.00 64.03  ? 540  GLN   C CB  1 
ATOM   8719  C  CG  . GLN   C  1 239 ? 39.340  22.871  -97.465  1.00 75.94  ? 540  GLN   C CG  1 
ATOM   8720  C  CD  . GLN   C  1 239 ? 40.538  23.262  -98.323  1.00 85.70  ? 540  GLN   C CD  1 
ATOM   8721  O  OE1 . GLN   C  1 239 ? 40.600  22.951  -99.512  1.00 88.08  ? 540  GLN   C OE1 1 
ATOM   8722  N  NE2 . GLN   C  1 239 ? 41.492  23.962  -97.718  1.00 91.71  ? 540  GLN   C NE2 1 
ATOM   8723  N  N   . ILE   C  1 240 ? 36.436  24.895  -96.905  1.00 36.80  ? 541  ILE   C N   1 
ATOM   8724  C  CA  . ILE   C  1 240 ? 36.359  26.360  -97.016  1.00 39.36  ? 541  ILE   C CA  1 
ATOM   8725  C  C   . ILE   C  1 240 ? 37.681  26.881  -97.567  1.00 42.79  ? 541  ILE   C C   1 
ATOM   8726  O  O   . ILE   C  1 240 ? 38.757  26.440  -97.115  1.00 42.50  ? 541  ILE   C O   1 
ATOM   8727  C  CB  . ILE   C  1 240 ? 36.059  26.993  -95.647  1.00 43.81  ? 541  ILE   C CB  1 
ATOM   8728  C  CG1 . ILE   C  1 240 ? 34.833  26.353  -95.004  1.00 39.86  ? 541  ILE   C CG1 1 
ATOM   8729  C  CG2 . ILE   C  1 240 ? 35.856  28.492  -95.768  1.00 38.39  ? 541  ILE   C CG2 1 
ATOM   8730  C  CD1 . ILE   C  1 240 ? 34.624  26.805  -93.598  1.00 44.73  ? 541  ILE   C CD1 1 
ATOM   8731  N  N   . PRO   C  1 241 ? 37.681  27.781  -98.544  1.00 37.51  ? 542  PRO   C N   1 
ATOM   8732  C  CA  . PRO   C  1 241 ? 38.943  28.335  -99.024  1.00 40.54  ? 542  PRO   C CA  1 
ATOM   8733  C  C   . PRO   C  1 241 ? 39.652  29.071  -97.905  1.00 39.45  ? 542  PRO   C C   1 
ATOM   8734  O  O   . PRO   C  1 241 ? 39.068  29.972  -97.280  1.00 44.53  ? 542  PRO   C O   1 
ATOM   8735  C  CB  . PRO   C  1 241 ? 38.518  29.288  -100.155 1.00 43.59  ? 542  PRO   C CB  1 
ATOM   8736  C  CG  . PRO   C  1 241 ? 37.188  28.792  -100.603 1.00 34.37  ? 542  PRO   C CG  1 
ATOM   8737  C  CD  . PRO   C  1 241 ? 36.534  28.217  -99.360  1.00 38.57  ? 542  PRO   C CD  1 
ATOM   8738  N  N   . PRO   C  1 242 ? 40.899  28.689  -97.611  1.00 42.99  ? 543  PRO   C N   1 
ATOM   8739  C  CA  . PRO   C  1 242 ? 41.630  29.290  -96.483  1.00 47.05  ? 543  PRO   C CA  1 
ATOM   8740  C  C   . PRO   C  1 242 ? 41.643  30.805  -96.493  1.00 52.21  ? 543  PRO   C C   1 
ATOM   8741  O  O   . PRO   C  1 242 ? 41.625  31.436  -95.419  1.00 49.69  ? 543  PRO   C O   1 
ATOM   8742  C  CB  . PRO   C  1 242 ? 43.044  28.726  -96.659  1.00 49.36  ? 543  PRO   C CB  1 
ATOM   8743  C  CG  . PRO   C  1 242 ? 42.861  27.453  -97.399  1.00 43.07  ? 543  PRO   C CG  1 
ATOM   8744  C  CD  . PRO   C  1 242 ? 41.679  27.638  -98.286  1.00 46.19  ? 543  PRO   C CD  1 
ATOM   8745  N  N   . GLU   C  1 243 ? 41.648  31.411  -97.684  1.00 40.91  ? 544  GLU   C N   1 
ATOM   8746  C  CA  . GLU   C  1 243 ? 41.708  32.860  -97.784  1.00 41.58  ? 544  GLU   C CA  1 
ATOM   8747  C  C   . GLU   C  1 243 ? 40.452  33.513  -97.248  1.00 39.96  ? 544  GLU   C C   1 
ATOM   8748  O  O   . GLU   C  1 243 ? 40.463  34.718  -96.983  1.00 40.97  ? 544  GLU   C O   1 
ATOM   8749  C  CB  . GLU   C  1 243 ? 41.941  33.298  -99.243  1.00 47.39  ? 544  GLU   C CB  1 
ATOM   8750  C  CG  . GLU   C  1 243 ? 40.849  32.882  -100.218 1.00 47.84  ? 544  GLU   C CG  1 
ATOM   8751  C  CD  . GLU   C  1 243 ? 41.166  31.583  -100.928 1.00 52.20  ? 544  GLU   C CD  1 
ATOM   8752  O  OE1 . GLU   C  1 243 ? 42.025  30.844  -100.408 1.00 48.65  ? 544  GLU   C OE1 1 
ATOM   8753  O  OE2 . GLU   C  1 243 ? 40.577  31.304  -102.007 1.00 59.72  ? 544  GLU   C OE2 1 
ATOM   8754  N  N   . LEU   C  1 244 ? 39.375  32.750  -97.085  1.00 40.19  ? 545  LEU   C N   1 
ATOM   8755  C  CA  . LEU   C  1 244 ? 38.190  33.234  -96.396  1.00 36.93  ? 545  LEU   C CA  1 
ATOM   8756  C  C   . LEU   C  1 244 ? 38.245  33.033  -94.877  1.00 43.10  ? 545  LEU   C C   1 
ATOM   8757  O  O   . LEU   C  1 244 ? 37.412  33.618  -94.172  1.00 41.35  ? 545  LEU   C O   1 
ATOM   8758  C  CB  . LEU   C  1 244 ? 36.936  32.548  -96.956  1.00 38.68  ? 545  LEU   C CB  1 
ATOM   8759  C  CG  . LEU   C  1 244 ? 36.660  32.610  -98.477  1.00 38.89  ? 545  LEU   C CG  1 
ATOM   8760  C  CD1 . LEU   C  1 244 ? 35.319  31.996  -98.795  1.00 34.26  ? 545  LEU   C CD1 1 
ATOM   8761  C  CD2 . LEU   C  1 244 ? 36.700  34.033  -98.995  1.00 34.69  ? 545  LEU   C CD2 1 
ATOM   8762  N  N   . VAL   C  1 245 ? 39.174  32.231  -94.349  1.00 45.60  ? 546  VAL   C N   1 
ATOM   8763  C  CA  . VAL   C  1 245 ? 39.184  31.893  -92.912  1.00 42.66  ? 546  VAL   C CA  1 
ATOM   8764  C  C   . VAL   C  1 245 ? 40.222  32.781  -92.236  1.00 36.38  ? 546  VAL   C C   1 
ATOM   8765  O  O   . VAL   C  1 245 ? 41.417  32.458  -92.190  1.00 37.07  ? 546  VAL   C O   1 
ATOM   8766  C  CB  . VAL   C  1 245 ? 39.473  30.415  -92.664  1.00 41.86  ? 546  VAL   C CB  1 
ATOM   8767  C  CG1 . VAL   C  1 245 ? 39.421  30.131  -91.182  1.00 32.21  ? 546  VAL   C CG1 1 
ATOM   8768  C  CG2 . VAL   C  1 245 ? 38.471  29.532  -93.413  1.00 39.94  ? 546  VAL   C CG2 1 
ATOM   8769  N  N   . LEU   C  1 246 ? 39.761  33.911  -91.708  1.00 39.52  ? 547  LEU   C N   1 
ATOM   8770  C  CA  . LEU   C  1 246 ? 40.648  34.847  -91.026  1.00 38.72  ? 547  LEU   C CA  1 
ATOM   8771  C  C   . LEU   C  1 246 ? 41.042  34.290  -89.663  1.00 42.18  ? 547  LEU   C C   1 
ATOM   8772  O  O   . LEU   C  1 246 ? 40.181  33.863  -88.896  1.00 36.97  ? 547  LEU   C O   1 
ATOM   8773  C  CB  . LEU   C  1 246 ? 39.953  36.198  -90.862  1.00 35.96  ? 547  LEU   C CB  1 
ATOM   8774  C  CG  . LEU   C  1 246 ? 40.740  37.282  -90.136  1.00 39.29  ? 547  LEU   C CG  1 
ATOM   8775  C  CD1 . LEU   C  1 246 ? 42.093  37.491  -90.804  1.00 34.18  ? 547  LEU   C CD1 1 
ATOM   8776  C  CD2 . LEU   C  1 246 ? 39.944  38.568  -90.136  1.00 39.73  ? 547  LEU   C CD2 1 
ATOM   8777  N  N   . GLU   C  1 247 ? 42.344  34.274  -89.378  1.00 46.87  ? 548  GLU   C N   1 
ATOM   8778  C  CA  . GLU   C  1 247 ? 42.885  33.724  -88.144  1.00 42.95  ? 548  GLU   C CA  1 
ATOM   8779  C  C   . GLU   C  1 247 ? 43.856  34.711  -87.514  1.00 47.49  ? 548  GLU   C C   1 
ATOM   8780  O  O   . GLU   C  1 247 ? 44.553  35.453  -88.214  1.00 42.03  ? 548  GLU   C O   1 
ATOM   8781  C  CB  . GLU   C  1 247 ? 43.599  32.392  -88.377  1.00 40.73  ? 548  GLU   C CB  1 
ATOM   8782  C  CG  . GLU   C  1 247 ? 42.678  31.237  -88.714  1.00 41.65  ? 548  GLU   C CG  1 
ATOM   8783  C  CD  . GLU   C  1 247 ? 43.438  29.930  -88.872  1.00 47.94  ? 548  GLU   C CD  1 
ATOM   8784  O  OE1 . GLU   C  1 247 ? 44.335  29.861  -89.730  1.00 50.22  ? 548  GLU   C OE1 1 
ATOM   8785  O  OE2 . GLU   C  1 247 ? 43.161  28.973  -88.128  1.00 53.78  ? 548  GLU   C OE2 1 
ATOM   8786  N  N   . VAL   C  1 248 ? 43.915  34.685  -86.181  1.00 42.52  ? 549  VAL   C N   1 
ATOM   8787  C  CA  . VAL   C  1 248 ? 44.715  35.628  -85.409  1.00 43.84  ? 549  VAL   C CA  1 
ATOM   8788  C  C   . VAL   C  1 248 ? 45.741  34.857  -84.587  1.00 51.28  ? 549  VAL   C C   1 
ATOM   8789  O  O   . VAL   C  1 248 ? 45.355  34.085  -83.696  1.00 57.55  ? 549  VAL   C O   1 
ATOM   8790  C  CB  . VAL   C  1 248 ? 43.827  36.494  -84.495  1.00 49.75  ? 549  VAL   C CB  1 
ATOM   8791  C  CG1 . VAL   C  1 248 ? 44.655  37.569  -83.794  1.00 48.65  ? 549  VAL   C CG1 1 
ATOM   8792  C  CG2 . VAL   C  1 248 ? 42.680  37.122  -85.277  1.00 55.85  ? 549  VAL   C CG2 1 
ATOM   8793  N  N   . PRO   C  1 249 ? 47.041  35.023  -84.838  1.00 52.56  ? 550  PRO   C N   1 
ATOM   8794  C  CA  . PRO   C  1 249 ? 48.046  34.401  -83.959  1.00 49.27  ? 550  PRO   C CA  1 
ATOM   8795  C  C   . PRO   C  1 249 ? 48.104  35.145  -82.637  1.00 59.77  ? 550  PRO   C C   1 
ATOM   8796  O  O   . PRO   C  1 249 ? 48.149  36.376  -82.609  1.00 62.92  ? 550  PRO   C O   1 
ATOM   8797  C  CB  . PRO   C  1 249 ? 49.350  34.546  -84.745  1.00 54.60  ? 550  PRO   C CB  1 
ATOM   8798  C  CG  . PRO   C  1 249 ? 49.123  35.764  -85.607  1.00 57.94  ? 550  PRO   C CG  1 
ATOM   8799  C  CD  . PRO   C  1 249 ? 47.656  35.776  -85.950  1.00 55.82  ? 550  PRO   C CD  1 
ATOM   8800  N  N   . ILE   C  1 250 ? 48.084  34.392  -81.541  1.00 58.99  ? 551  ILE   C N   1 
ATOM   8801  C  CA  . ILE   C  1 250 ? 47.954  34.972  -80.208  1.00 50.16  ? 551  ILE   C CA  1 
ATOM   8802  C  C   . ILE   C  1 250 ? 49.339  35.267  -79.656  1.00 53.41  ? 551  ILE   C C   1 
ATOM   8803  O  O   . ILE   C  1 250 ? 50.132  34.349  -79.412  1.00 50.93  ? 551  ILE   C O   1 
ATOM   8804  C  CB  . ILE   C  1 250 ? 47.179  34.043  -79.259  1.00 50.74  ? 551  ILE   C CB  1 
ATOM   8805  C  CG1 . ILE   C  1 250 ? 45.903  33.523  -79.936  1.00 39.84  ? 551  ILE   C CG1 1 
ATOM   8806  C  CG2 . ILE   C  1 250 ? 46.853  34.792  -77.963  1.00 40.14  ? 551  ILE   C CG2 1 
ATOM   8807  C  CD1 . ILE   C  1 250 ? 44.838  34.563  -80.095  1.00 35.31  ? 551  ILE   C CD1 1 
ATOM   8808  N  N   . ARG   C  1 251 ? 49.627  36.548  -79.449  1.00 61.37  ? 552  ARG   C N   1 
ATOM   8809  C  CA  . ARG   C  1 251 ? 50.833  36.981  -78.759  1.00 60.19  ? 552  ARG   C CA  1 
ATOM   8810  C  C   . ARG   C  1 251 ? 50.457  37.839  -77.548  1.00 56.19  ? 552  ARG   C C   1 
ATOM   8811  O  O   . ARG   C  1 251 ? 49.316  38.293  -77.403  1.00 46.71  ? 552  ARG   C O   1 
ATOM   8812  C  CB  . ARG   C  1 251 ? 51.758  37.752  -79.703  1.00 64.01  ? 552  ARG   C CB  1 
ATOM   8813  C  CG  . ARG   C  1 251 ? 51.082  38.887  -80.416  1.00 66.41  ? 552  ARG   C CG  1 
ATOM   8814  C  CD  . ARG   C  1 251 ? 50.542  38.469  -81.778  1.00 63.92  ? 552  ARG   C CD  1 
ATOM   8815  N  NE  . ARG   C  1 251 ? 50.141  39.650  -82.531  1.00 63.97  ? 552  ARG   C NE  1 
ATOM   8816  C  CZ  . ARG   C  1 251 ? 49.231  39.660  -83.497  1.00 61.31  ? 552  ARG   C CZ  1 
ATOM   8817  N  NH1 . ARG   C  1 251 ? 48.939  40.801  -84.100  1.00 67.39  ? 552  ARG   C NH1 1 
ATOM   8818  N  NH2 . ARG   C  1 251 ? 48.607  38.545  -83.852  1.00 54.04  ? 552  ARG   C NH2 1 
ATOM   8819  N  N   . HIS   C  1 252 ? 51.444  38.068  -76.669  1.00 55.62  ? 553  HIS   C N   1 
ATOM   8820  C  CA  . HIS   C  1 252 ? 51.236  38.828  -75.448  1.00 55.57  ? 553  HIS   C CA  1 
ATOM   8821  C  C   . HIS   C  1 252 ? 52.024  40.126  -75.493  1.00 57.78  ? 553  HIS   C C   1 
ATOM   8822  O  O   . HIS   C  1 252 ? 53.172  40.138  -75.946  1.00 62.17  ? 553  HIS   C O   1 
ATOM   8823  C  CB  . HIS   C  1 252 ? 51.668  38.028  -74.215  1.00 52.46  ? 553  HIS   C CB  1 
ATOM   8824  C  CG  . HIS   C  1 252 ? 51.163  38.579  -72.919  1.00 61.88  ? 553  HIS   C CG  1 
ATOM   8825  N  ND1 . HIS   C  1 252 ? 51.811  39.584  -72.233  1.00 65.74  ? 553  HIS   C ND1 1 
ATOM   8826  C  CD2 . HIS   C  1 252 ? 50.086  38.245  -72.168  1.00 60.15  ? 553  HIS   C CD2 1 
ATOM   8827  C  CE1 . HIS   C  1 252 ? 51.150  39.853  -71.123  1.00 62.03  ? 553  HIS   C CE1 1 
ATOM   8828  N  NE2 . HIS   C  1 252 ? 50.099  39.056  -71.060  1.00 62.00  ? 553  HIS   C NE2 1 
ATOM   8829  N  N   . PRO   C  1 253 ? 51.438  41.230  -75.028  1.00 50.01  ? 554  PRO   C N   1 
ATOM   8830  C  CA  . PRO   C  1 253 ? 52.144  42.517  -75.097  1.00 49.91  ? 554  PRO   C CA  1 
ATOM   8831  C  C   . PRO   C  1 253 ? 53.395  42.581  -74.241  1.00 60.31  ? 554  PRO   C C   1 
ATOM   8832  O  O   . PRO   C  1 253 ? 54.270  43.405  -74.528  1.00 65.38  ? 554  PRO   C O   1 
ATOM   8833  C  CB  . PRO   C  1 253 ? 51.088  43.523  -74.620  1.00 46.39  ? 554  PRO   C CB  1 
ATOM   8834  C  CG  . PRO   C  1 253 ? 50.117  42.700  -73.825  1.00 49.76  ? 554  PRO   C CG  1 
ATOM   8835  C  CD  . PRO   C  1 253 ? 50.056  41.383  -74.548  1.00 43.67  ? 554  PRO   C CD  1 
ATOM   8836  N  N   . LYS   C  1 254 ? 53.514  41.748  -73.213  1.00 58.76  ? 555  LYS   C N   1 
ATOM   8837  C  CA  . LYS   C  1 254 ? 54.646  41.764  -72.290  1.00 62.70  ? 555  LYS   C CA  1 
ATOM   8838  C  C   . LYS   C  1 254 ? 55.490  40.501  -72.350  1.00 63.32  ? 555  LYS   C C   1 
ATOM   8839  O  O   . LYS   C  1 254 ? 56.721  40.581  -72.347  1.00 61.85  ? 555  LYS   C O   1 
ATOM   8840  C  CB  . LYS   C  1 254 ? 54.141  41.973  -70.849  1.00 68.28  ? 555  LYS   C CB  1 
ATOM   8841  C  CG  . LYS   C  1 254 ? 54.019  43.431  -70.437  1.00 77.52  ? 555  LYS   C CG  1 
ATOM   8842  C  CD  . LYS   C  1 254 ? 55.371  43.978  -69.970  1.00 89.63  ? 555  LYS   C CD  1 
ATOM   8843  C  CE  . LYS   C  1 254 ? 55.510  45.489  -70.195  1.00 92.58  ? 555  LYS   C CE  1 
ATOM   8844  N  NZ  . LYS   C  1 254 ? 54.600  46.312  -69.344  1.00 87.85  ? 555  LYS   C NZ  1 
ATOM   8845  N  N   . PHE   C  1 255 ? 54.859  39.335  -72.421  1.00 69.59  ? 556  PHE   C N   1 
ATOM   8846  C  CA  . PHE   C  1 255 ? 55.554  38.051  -72.405  1.00 74.46  ? 556  PHE   C CA  1 
ATOM   8847  C  C   . PHE   C  1 255 ? 55.988  37.718  -73.825  1.00 73.09  ? 556  PHE   C C   1 
ATOM   8848  O  O   . PHE   C  1 255 ? 55.187  37.247  -74.630  1.00 64.90  ? 556  PHE   C O   1 
ATOM   8849  C  CB  . PHE   C  1 255 ? 54.641  36.958  -71.856  1.00 74.40  ? 556  PHE   C CB  1 
ATOM   8850  C  CG  . PHE   C  1 255 ? 54.135  37.219  -70.459  1.00 70.16  ? 556  PHE   C CG  1 
ATOM   8851  C  CD1 . PHE   C  1 255 ? 54.999  37.608  -69.458  1.00 65.01  ? 556  PHE   C CD1 1 
ATOM   8852  C  CD2 . PHE   C  1 255 ? 52.791  37.059  -70.150  1.00 69.70  ? 556  PHE   C CD2 1 
ATOM   8853  C  CE1 . PHE   C  1 255 ? 54.537  37.837  -68.180  1.00 64.60  ? 556  PHE   C CE1 1 
ATOM   8854  C  CE2 . PHE   C  1 255 ? 52.325  37.282  -68.864  1.00 63.48  ? 556  PHE   C CE2 1 
ATOM   8855  C  CZ  . PHE   C  1 255 ? 53.199  37.674  -67.884  1.00 59.92  ? 556  PHE   C CZ  1 
ATOM   8856  N  N   . GLU   C  1 256 ? 57.265  37.949  -74.137  1.00 82.24  ? 557  GLU   C N   1 
ATOM   8857  C  CA  . GLU   C  1 256 ? 57.765  37.588  -75.461  1.00 85.92  ? 557  GLU   C CA  1 
ATOM   8858  C  C   . GLU   C  1 256 ? 57.559  36.108  -75.743  1.00 81.07  ? 557  GLU   C C   1 
ATOM   8859  O  O   . GLU   C  1 256 ? 57.331  35.717  -76.893  1.00 86.81  ? 557  GLU   C O   1 
ATOM   8860  C  CB  . GLU   C  1 256 ? 59.248  37.941  -75.591  1.00 93.81  ? 557  GLU   C CB  1 
ATOM   8861  C  CG  . GLU   C  1 256 ? 59.553  39.420  -75.492  1.00 103.07 ? 557  GLU   C CG  1 
ATOM   8862  C  CD  . GLU   C  1 256 ? 59.459  40.134  -76.825  1.00 113.96 ? 557  GLU   C CD  1 
ATOM   8863  O  OE1 . GLU   C  1 256 ? 59.990  41.259  -76.923  1.00 119.57 ? 557  GLU   C OE1 1 
ATOM   8864  O  OE2 . GLU   C  1 256 ? 58.866  39.577  -77.776  1.00 116.16 ? 557  GLU   C OE2 1 
ATOM   8865  N  N   . TRP   C  1 257 ? 57.616  35.273  -74.709  1.00 72.56  ? 558  TRP   C N   1 
ATOM   8866  C  CA  . TRP   C  1 257 ? 57.539  33.834  -74.893  1.00 67.53  ? 558  TRP   C CA  1 
ATOM   8867  C  C   . TRP   C  1 257 ? 56.134  33.356  -75.201  1.00 67.86  ? 558  TRP   C C   1 
ATOM   8868  O  O   . TRP   C  1 257 ? 55.957  32.170  -75.496  1.00 75.45  ? 558  TRP   C O   1 
ATOM   8869  C  CB  . TRP   C  1 257 ? 58.049  33.126  -73.640  1.00 74.88  ? 558  TRP   C CB  1 
ATOM   8870  C  CG  . TRP   C  1 257 ? 57.430  33.637  -72.377  1.00 70.58  ? 558  TRP   C CG  1 
ATOM   8871  C  CD1 . TRP   C  1 257 ? 57.985  34.513  -71.487  1.00 78.44  ? 558  TRP   C CD1 1 
ATOM   8872  C  CD2 . TRP   C  1 257 ? 56.136  33.309  -71.862  1.00 64.70  ? 558  TRP   C CD2 1 
ATOM   8873  N  NE1 . TRP   C  1 257 ? 57.119  34.746  -70.445  1.00 71.64  ? 558  TRP   C NE1 1 
ATOM   8874  C  CE2 . TRP   C  1 257 ? 55.977  34.020  -70.651  1.00 66.04  ? 558  TRP   C CE2 1 
ATOM   8875  C  CE3 . TRP   C  1 257 ? 55.102  32.479  -72.298  1.00 59.28  ? 558  TRP   C CE3 1 
ATOM   8876  C  CZ2 . TRP   C  1 257 ? 54.823  33.930  -69.878  1.00 64.06  ? 558  TRP   C CZ2 1 
ATOM   8877  C  CZ3 . TRP   C  1 257 ? 53.946  32.400  -71.533  1.00 61.68  ? 558  TRP   C CZ3 1 
ATOM   8878  C  CH2 . TRP   C  1 257 ? 53.821  33.115  -70.333  1.00 68.07  ? 558  TRP   C CH2 1 
ATOM   8879  N  N   . PHE   C  1 258 ? 55.135  34.233  -75.117  1.00 65.22  ? 559  PHE   C N   1 
ATOM   8880  C  CA  . PHE   C  1 258 ? 53.759  33.796  -75.316  1.00 63.41  ? 559  PHE   C CA  1 
ATOM   8881  C  C   . PHE   C  1 258 ? 53.522  33.355  -76.755  1.00 60.04  ? 559  PHE   C C   1 
ATOM   8882  O  O   . PHE   C  1 258 ? 52.895  32.318  -77.000  1.00 57.82  ? 559  PHE   C O   1 
ATOM   8883  C  CB  . PHE   C  1 258 ? 52.791  34.910  -74.938  1.00 63.39  ? 559  PHE   C CB  1 
ATOM   8884  C  CG  . PHE   C  1 258 ? 51.422  34.414  -74.583  1.00 65.48  ? 559  PHE   C CG  1 
ATOM   8885  C  CD1 . PHE   C  1 258 ? 50.539  33.992  -75.573  1.00 57.21  ? 559  PHE   C CD1 1 
ATOM   8886  C  CD2 . PHE   C  1 258 ? 51.019  34.354  -73.254  1.00 62.67  ? 559  PHE   C CD2 1 
ATOM   8887  C  CE1 . PHE   C  1 258 ? 49.287  33.514  -75.243  1.00 54.57  ? 559  PHE   C CE1 1 
ATOM   8888  C  CE2 . PHE   C  1 258 ? 49.764  33.888  -72.914  1.00 57.55  ? 559  PHE   C CE2 1 
ATOM   8889  C  CZ  . PHE   C  1 258 ? 48.892  33.468  -73.911  1.00 52.62  ? 559  PHE   C CZ  1 
ATOM   8890  N  N   . LYS   C  1 259 ? 53.996  34.141  -77.723  1.00 55.11  ? 560  LYS   C N   1 
ATOM   8891  C  CA  . LYS   C  1 259 ? 53.823  33.755  -79.119  1.00 57.08  ? 560  LYS   C CA  1 
ATOM   8892  C  C   . LYS   C  1 259 ? 54.361  32.350  -79.361  1.00 60.62  ? 560  LYS   C C   1 
ATOM   8893  O  O   . LYS   C  1 259 ? 53.797  31.593  -80.160  1.00 52.84  ? 560  LYS   C O   1 
ATOM   8894  C  CB  . LYS   C  1 259 ? 54.515  34.772  -80.036  1.00 59.01  ? 560  LYS   C CB  1 
ATOM   8895  C  CG  . LYS   C  1 259 ? 56.010  34.953  -79.765  1.00 63.12  ? 560  LYS   C CG  1 
ATOM   8896  C  CD  . LYS   C  1 259 ? 56.611  36.055  -80.621  1.00 68.14  ? 560  LYS   C CD  1 
ATOM   8897  C  CE  . LYS   C  1 259 ? 58.131  36.105  -80.499  1.00 73.03  ? 560  LYS   C CE  1 
ATOM   8898  N  NZ  . LYS   C  1 259 ? 58.618  36.766  -79.245  1.00 73.31  ? 560  LYS   C NZ  1 
ATOM   8899  N  N   . ASP   C  1 260 ? 55.406  31.963  -78.626  1.00 67.26  ? 561  ASP   C N   1 
ATOM   8900  C  CA  . ASP   C  1 260 ? 56.027  30.657  -78.784  1.00 69.43  ? 561  ASP   C CA  1 
ATOM   8901  C  C   . ASP   C  1 260 ? 55.123  29.510  -78.353  1.00 63.32  ? 561  ASP   C C   1 
ATOM   8902  O  O   . ASP   C  1 260 ? 55.449  28.355  -78.643  1.00 68.82  ? 561  ASP   C O   1 
ATOM   8903  C  CB  . ASP   C  1 260 ? 57.345  30.623  -78.005  1.00 82.72  ? 561  ASP   C CB  1 
ATOM   8904  C  CG  . ASP   C  1 260 ? 58.257  31.794  -78.352  1.00 88.33  ? 561  ASP   C CG  1 
ATOM   8905  O  OD1 . ASP   C  1 260 ? 58.030  32.418  -79.417  1.00 88.69  ? 561  ASP   C OD1 1 
ATOM   8906  O  OD2 . ASP   C  1 260 ? 59.190  32.085  -77.564  1.00 87.86  ? 561  ASP   C OD2 1 
ATOM   8907  N  N   . LEU   C  1 261 ? 54.004  29.786  -77.676  1.00 58.31  ? 562  LEU   C N   1 
ATOM   8908  C  CA  . LEU   C  1 261 ? 53.031  28.734  -77.389  1.00 62.37  ? 562  LEU   C CA  1 
ATOM   8909  C  C   . LEU   C  1 261 ? 52.363  28.197  -78.652  1.00 70.37  ? 562  LEU   C C   1 
ATOM   8910  O  O   . LEU   C  1 261 ? 51.689  27.162  -78.582  1.00 69.24  ? 562  LEU   C O   1 
ATOM   8911  C  CB  . LEU   C  1 261 ? 51.962  29.246  -76.426  1.00 57.77  ? 562  LEU   C CB  1 
ATOM   8912  C  CG  . LEU   C  1 261 ? 52.443  29.576  -75.014  1.00 63.88  ? 562  LEU   C CG  1 
ATOM   8913  C  CD1 . LEU   C  1 261 ? 51.493  30.545  -74.301  1.00 61.09  ? 562  LEU   C CD1 1 
ATOM   8914  C  CD2 . LEU   C  1 261 ? 52.587  28.294  -74.213  1.00 70.32  ? 562  LEU   C CD2 1 
ATOM   8915  N  N   . GLY   C  1 262 ? 52.533  28.874  -79.786  1.00 64.83  ? 563  GLY   C N   1 
ATOM   8916  C  CA  . GLY   C  1 262 ? 51.981  28.415  -81.047  1.00 66.56  ? 563  GLY   C CA  1 
ATOM   8917  C  C   . GLY   C  1 262 ? 50.473  28.382  -81.077  1.00 65.84  ? 563  GLY   C C   1 
ATOM   8918  O  O   . GLY   C  1 262 ? 49.885  27.441  -81.621  1.00 66.55  ? 563  GLY   C O   1 
ATOM   8919  N  N   . LEU   C  1 263 ? 49.833  29.387  -80.495  1.00 61.50  ? 564  LEU   C N   1 
ATOM   8920  C  CA  . LEU   C  1 263 ? 48.388  29.429  -80.374  1.00 53.19  ? 564  LEU   C CA  1 
ATOM   8921  C  C   . LEU   C  1 263 ? 47.804  30.427  -81.368  1.00 47.88  ? 564  LEU   C C   1 
ATOM   8922  O  O   . LEU   C  1 263 ? 48.406  31.465  -81.659  1.00 48.91  ? 564  LEU   C O   1 
ATOM   8923  C  CB  . LEU   C  1 263 ? 47.972  29.828  -78.950  1.00 48.64  ? 564  LEU   C CB  1 
ATOM   8924  C  CG  . LEU   C  1 263 ? 48.327  28.896  -77.793  1.00 50.39  ? 564  LEU   C CG  1 
ATOM   8925  C  CD1 . LEU   C  1 263 ? 48.116  29.616  -76.458  1.00 49.47  ? 564  LEU   C CD1 1 
ATOM   8926  C  CD2 . LEU   C  1 263 ? 47.510  27.619  -77.836  1.00 47.35  ? 564  LEU   C CD2 1 
ATOM   8927  N  N   . LYS   C  1 264 ? 46.611  30.109  -81.868  1.00 46.00  ? 565  LYS   C N   1 
ATOM   8928  C  CA  . LYS   C  1 264 ? 45.852  31.014  -82.721  1.00 48.64  ? 565  LYS   C CA  1 
ATOM   8929  C  C   . LYS   C  1 264 ? 44.380  30.697  -82.535  1.00 44.88  ? 565  LYS   C C   1 
ATOM   8930  O  O   . LYS   C  1 264 ? 44.014  29.654  -81.987  1.00 55.69  ? 565  LYS   C O   1 
ATOM   8931  C  CB  . LYS   C  1 264 ? 46.256  30.900  -84.200  1.00 42.82  ? 565  LYS   C CB  1 
ATOM   8932  C  CG  . LYS   C  1 264 ? 46.065  29.509  -84.782  1.00 57.83  ? 565  LYS   C CG  1 
ATOM   8933  C  CD  . LYS   C  1 264 ? 46.558  29.418  -86.242  1.00 61.56  ? 565  LYS   C CD  1 
ATOM   8934  C  CE  . LYS   C  1 264 ? 46.880  27.978  -86.648  1.00 71.54  ? 565  LYS   C CE  1 
ATOM   8935  N  NZ  . LYS   C  1 264 ? 48.055  27.850  -87.590  1.00 74.24  ? 565  LYS   C NZ  1 
ATOM   8936  N  N   . TRP   C  1 265 ? 43.528  31.620  -82.970  1.00 36.84  ? 566  TRP   C N   1 
ATOM   8937  C  CA  . TRP   C  1 265 ? 42.096  31.369  -83.016  1.00 31.63  ? 566  TRP   C CA  1 
ATOM   8938  C  C   . TRP   C  1 265 ? 41.562  32.052  -84.261  1.00 46.51  ? 566  TRP   C C   1 
ATOM   8939  O  O   . TRP   C  1 265 ? 42.238  32.887  -84.870  1.00 49.05  ? 566  TRP   C O   1 
ATOM   8940  C  CB  . TRP   C  1 265 ? 41.357  31.851  -81.752  1.00 37.30  ? 566  TRP   C CB  1 
ATOM   8941  C  CG  . TRP   C  1 265 ? 40.074  31.090  -81.518  1.00 34.92  ? 566  TRP   C CG  1 
ATOM   8942  C  CD1 . TRP   C  1 265 ? 38.806  31.553  -81.691  1.00 36.21  ? 566  TRP   C CD1 1 
ATOM   8943  C  CD2 . TRP   C  1 265 ? 39.947  29.716  -81.101  1.00 39.57  ? 566  TRP   C CD2 1 
ATOM   8944  N  NE1 . TRP   C  1 265 ? 37.895  30.559  -81.410  1.00 39.92  ? 566  TRP   C NE1 1 
ATOM   8945  C  CE2 . TRP   C  1 265 ? 38.572  29.425  -81.041  1.00 36.00  ? 566  TRP   C CE2 1 
ATOM   8946  C  CE3 . TRP   C  1 265 ? 40.867  28.706  -80.779  1.00 31.04  ? 566  TRP   C CE3 1 
ATOM   8947  C  CZ2 . TRP   C  1 265 ? 38.093  28.177  -80.666  1.00 30.74  ? 566  TRP   C CZ2 1 
ATOM   8948  C  CZ3 . TRP   C  1 265 ? 40.391  27.471  -80.419  1.00 35.39  ? 566  TRP   C CZ3 1 
ATOM   8949  C  CH2 . TRP   C  1 265 ? 39.018  27.214  -80.360  1.00 39.77  ? 566  TRP   C CH2 1 
ATOM   8950  N  N   . TYR   C  1 266 ? 40.354  31.669  -84.654  1.00 41.38  ? 567  TYR   C N   1 
ATOM   8951  C  CA  . TYR   C  1 266 ? 39.730  32.258  -85.829  1.00 43.11  ? 567  TYR   C CA  1 
ATOM   8952  C  C   . TYR   C  1 266 ? 38.932  33.504  -85.456  1.00 47.74  ? 567  TYR   C C   1 
ATOM   8953  O  O   . TYR   C  1 266 ? 38.541  33.711  -84.302  1.00 46.33  ? 567  TYR   C O   1 
ATOM   8954  C  CB  . TYR   C  1 266 ? 38.824  31.248  -86.527  1.00 39.59  ? 567  TYR   C CB  1 
ATOM   8955  C  CG  . TYR   C  1 266 ? 37.919  30.462  -85.602  1.00 38.05  ? 567  TYR   C CG  1 
ATOM   8956  C  CD1 . TYR   C  1 266 ? 38.345  29.282  -85.017  1.00 42.28  ? 567  TYR   C CD1 1 
ATOM   8957  C  CD2 . TYR   C  1 266 ? 36.627  30.889  -85.342  1.00 40.98  ? 567  TYR   C CD2 1 
ATOM   8958  C  CE1 . TYR   C  1 266 ? 37.500  28.546  -84.186  1.00 39.64  ? 567  TYR   C CE1 1 
ATOM   8959  C  CE2 . TYR   C  1 266 ? 35.781  30.172  -84.530  1.00 37.91  ? 567  TYR   C CE2 1 
ATOM   8960  C  CZ  . TYR   C  1 266 ? 36.215  29.006  -83.942  1.00 42.58  ? 567  TYR   C CZ  1 
ATOM   8961  O  OH  . TYR   C  1 266 ? 35.352  28.306  -83.113  1.00 46.42  ? 567  TYR   C OH  1 
ATOM   8962  N  N   . GLY   C  1 267 ? 38.686  34.334  -86.460  1.00 42.35  ? 568  GLY   C N   1 
ATOM   8963  C  CA  . GLY   C  1 267 ? 38.091  35.628  -86.220  1.00 29.46  ? 568  GLY   C CA  1 
ATOM   8964  C  C   . GLY   C  1 267 ? 36.591  35.666  -86.218  1.00 31.92  ? 568  GLY   C C   1 
ATOM   8965  O  O   . GLY   C  1 267 ? 36.019  36.630  -85.703  1.00 38.12  ? 568  GLY   C O   1 
ATOM   8966  N  N   . LEU   C  1 268 ? 35.934  34.643  -86.744  1.00 35.10  ? 569  LEU   C N   1 
ATOM   8967  C  CA  . LEU   C  1 268 ? 34.507  34.720  -87.039  1.00 33.56  ? 569  LEU   C CA  1 
ATOM   8968  C  C   . LEU   C  1 268 ? 33.743  33.651  -86.267  1.00 37.57  ? 569  LEU   C C   1 
ATOM   8969  O  O   . LEU   C  1 268 ? 33.854  32.455  -86.604  1.00 34.69  ? 569  LEU   C O   1 
ATOM   8970  C  CB  . LEU   C  1 268 ? 34.277  34.571  -88.551  1.00 33.28  ? 569  LEU   C CB  1 
ATOM   8971  C  CG  . LEU   C  1 268 ? 32.812  34.697  -88.955  1.00 33.73  ? 569  LEU   C CG  1 
ATOM   8972  C  CD1 . LEU   C  1 268 ? 32.326  36.129  -88.701  1.00 35.82  ? 569  LEU   C CD1 1 
ATOM   8973  C  CD2 . LEU   C  1 268 ? 32.532  34.261  -90.390  1.00 36.85  ? 569  LEU   C CD2 1 
ATOM   8974  N  N   . PRO   C  1 269 ? 32.952  34.010  -85.216  1.00 36.42  ? 570  PRO   C N   1 
ATOM   8975  C  CA  . PRO   C  1 269 ? 32.114  32.997  -84.577  1.00 32.50  ? 570  PRO   C CA  1 
ATOM   8976  C  C   . PRO   C  1 269 ? 30.806  32.909  -85.327  1.00 30.26  ? 570  PRO   C C   1 
ATOM   8977  O  O   . PRO   C  1 269 ? 30.087  33.903  -85.452  1.00 38.01  ? 570  PRO   C O   1 
ATOM   8978  C  CB  . PRO   C  1 269 ? 31.932  33.524  -83.143  1.00 26.12  ? 570  PRO   C CB  1 
ATOM   8979  C  CG  . PRO   C  1 269 ? 31.983  35.032  -83.294  1.00 30.08  ? 570  PRO   C CG  1 
ATOM   8980  C  CD  . PRO   C  1 269 ? 32.798  35.331  -84.565  1.00 34.44  ? 570  PRO   C CD  1 
ATOM   8981  N  N   . ALA   C  1 270 ? 30.464  31.729  -85.813  1.00 33.32  ? 571  ALA   C N   1 
ATOM   8982  C  CA  . ALA   C  1 270 ? 29.332  31.597  -86.725  1.00 31.22  ? 571  ALA   C CA  1 
ATOM   8983  C  C   . ALA   C  1 270 ? 28.531  30.366  -86.313  1.00 27.80  ? 571  ALA   C C   1 
ATOM   8984  O  O   . ALA   C  1 270 ? 28.866  29.253  -86.713  1.00 31.06  ? 571  ALA   C O   1 
ATOM   8985  C  CB  . ALA   C  1 270 ? 29.836  31.503  -88.174  1.00 24.72  ? 571  ALA   C CB  1 
ATOM   8986  N  N   . VAL   C  1 271 ? 27.489  30.555  -85.501  1.00 39.69  ? 572  VAL   C N   1 
ATOM   8987  C  CA  . VAL   C  1 271 ? 26.770  29.406  -84.947  1.00 33.41  ? 572  VAL   C CA  1 
ATOM   8988  C  C   . VAL   C  1 271 ? 25.892  28.810  -86.035  1.00 39.69  ? 572  VAL   C C   1 
ATOM   8989  O  O   . VAL   C  1 271 ? 25.084  29.518  -86.644  1.00 38.90  ? 572  VAL   C O   1 
ATOM   8990  C  CB  . VAL   C  1 271 ? 25.918  29.807  -83.735  1.00 29.17  ? 572  VAL   C CB  1 
ATOM   8991  C  CG1 . VAL   C  1 271 ? 24.948  28.684  -83.437  1.00 35.80  ? 572  VAL   C CG1 1 
ATOM   8992  C  CG2 . VAL   C  1 271 ? 26.782  30.065  -82.515  1.00 29.34  ? 572  VAL   C CG2 1 
ATOM   8993  N  N   . SER   C  1 272 ? 26.012  27.494  -86.257  1.00 41.18  ? 573  SER   C N   1 
ATOM   8994  C  CA  . SER   C  1 272 ? 25.336  26.883  -87.394  1.00 40.05  ? 573  SER   C CA  1 
ATOM   8995  C  C   . SER   C  1 272 ? 24.477  25.668  -87.071  1.00 44.36  ? 573  SER   C C   1 
ATOM   8996  O  O   . SER   C  1 272 ? 23.942  25.055  -88.004  1.00 44.93  ? 573  SER   C O   1 
ATOM   8997  C  CB  . SER   C  1 272 ? 26.362  26.500  -88.475  1.00 25.08  ? 573  SER   C CB  1 
ATOM   8998  O  OG  . SER   C  1 272 ? 27.313  25.571  -87.974  1.00 27.71  ? 573  SER   C OG  1 
ATOM   8999  N  N   . ASN   C  1 273 ? 24.310  25.303  -85.799  1.00 43.32  ? 574  ASN   C N   1 
ATOM   9000  C  CA  . ASN   C  1 273 ? 23.518  24.123  -85.466  1.00 38.68  ? 574  ASN   C CA  1 
ATOM   9001  C  C   . ASN   C  1 273 ? 22.168  24.444  -84.836  1.00 39.80  ? 574  ASN   C C   1 
ATOM   9002  O  O   . ASN   C  1 273 ? 21.489  23.524  -84.367  1.00 41.47  ? 574  ASN   C O   1 
ATOM   9003  C  CB  . ASN   C  1 273 ? 24.299  23.177  -84.549  1.00 38.97  ? 574  ASN   C CB  1 
ATOM   9004  C  CG  . ASN   C  1 273 ? 24.736  23.829  -83.233  1.00 40.07  ? 574  ASN   C CG  1 
ATOM   9005  O  OD1 . ASN   C  1 273 ? 24.445  24.987  -82.958  1.00 37.02  ? 574  ASN   C OD1 1 
ATOM   9006  N  ND2 . ASN   C  1 273 ? 25.451  23.069  -82.423  1.00 44.00  ? 574  ASN   C ND2 1 
ATOM   9007  N  N   . MET   C  1 274 ? 21.743  25.701  -84.823  1.00 37.31  ? 575  MET   C N   1 
ATOM   9008  C  CA  . MET   C  1 274 ? 20.490  26.048  -84.165  1.00 39.19  ? 575  MET   C CA  1 
ATOM   9009  C  C   . MET   C  1 274 ? 19.373  26.167  -85.190  1.00 44.14  ? 575  MET   C C   1 
ATOM   9010  O  O   . MET   C  1 274 ? 19.599  26.131  -86.400  1.00 33.34  ? 575  MET   C O   1 
ATOM   9011  C  CB  . MET   C  1 274 ? 20.633  27.341  -83.359  1.00 38.63  ? 575  MET   C CB  1 
ATOM   9012  C  CG  . MET   C  1 274 ? 21.436  27.136  -82.077  1.00 32.94  ? 575  MET   C CG  1 
ATOM   9013  S  SD  . MET   C  1 274 ? 21.505  28.585  -81.017  1.00 41.97  ? 575  MET   C SD  1 
ATOM   9014  C  CE  . MET   C  1 274 ? 19.993  28.388  -80.043  1.00 34.79  ? 575  MET   C CE  1 
ATOM   9015  N  N   . LEU   C  1 275 ? 18.149  26.271  -84.683  1.00 38.19  ? 576  LEU   C N   1 
ATOM   9016  C  CA  . LEU   C  1 275 ? 16.952  26.309  -85.508  1.00 36.56  ? 576  LEU   C CA  1 
ATOM   9017  C  C   . LEU   C  1 275 ? 16.272  27.652  -85.311  1.00 38.91  ? 576  LEU   C C   1 
ATOM   9018  O  O   . LEU   C  1 275 ? 16.132  28.121  -84.181  1.00 41.90  ? 576  LEU   C O   1 
ATOM   9019  C  CB  . LEU   C  1 275 ? 16.010  25.157  -85.146  1.00 46.00  ? 576  LEU   C CB  1 
ATOM   9020  C  CG  . LEU   C  1 275 ? 14.702  24.918  -85.903  1.00 43.92  ? 576  LEU   C CG  1 
ATOM   9021  C  CD1 . LEU   C  1 275 ? 14.307  23.459  -85.787  1.00 46.59  ? 576  LEU   C CD1 1 
ATOM   9022  C  CD2 . LEU   C  1 275 ? 13.577  25.793  -85.369  1.00 36.24  ? 576  LEU   C CD2 1 
ATOM   9023  N  N   . LEU   C  1 276 ? 15.862  28.272  -86.407  1.00 35.89  ? 577  LEU   C N   1 
ATOM   9024  C  CA  . LEU   C  1 276 ? 15.174  29.554  -86.380  1.00 30.43  ? 577  LEU   C CA  1 
ATOM   9025  C  C   . LEU   C  1 276 ? 13.683  29.312  -86.556  1.00 35.30  ? 577  LEU   C C   1 
ATOM   9026  O  O   . LEU   C  1 276 ? 13.271  28.676  -87.530  1.00 42.96  ? 577  LEU   C O   1 
ATOM   9027  C  CB  . LEU   C  1 276 ? 15.709  30.473  -87.485  1.00 30.14  ? 577  LEU   C CB  1 
ATOM   9028  C  CG  . LEU   C  1 276 ? 14.998  31.788  -87.757  1.00 34.35  ? 577  LEU   C CG  1 
ATOM   9029  C  CD1 . LEU   C  1 276 ? 15.112  32.722  -86.569  1.00 42.46  ? 577  LEU   C CD1 1 
ATOM   9030  C  CD2 . LEU   C  1 276 ? 15.581  32.456  -88.990  1.00 35.19  ? 577  LEU   C CD2 1 
ATOM   9031  N  N   . GLU   C  1 277 ? 12.879  29.825  -85.628  1.00 34.41  ? 578  GLU   C N   1 
ATOM   9032  C  CA  . GLU   C  1 277 ? 11.443  29.583  -85.617  1.00 36.26  ? 578  GLU   C CA  1 
ATOM   9033  C  C   . GLU   C  1 277 ? 10.704  30.904  -85.804  1.00 40.55  ? 578  GLU   C C   1 
ATOM   9034  O  O   . GLU   C  1 277 ? 10.889  31.843  -85.019  1.00 40.34  ? 578  GLU   C O   1 
ATOM   9035  C  CB  . GLU   C  1 277 ? 11.023  28.890  -84.316  1.00 46.86  ? 578  GLU   C CB  1 
ATOM   9036  C  CG  . GLU   C  1 277 ? 9.626   28.298  -84.319  1.00 51.88  ? 578  GLU   C CG  1 
ATOM   9037  C  CD  . GLU   C  1 277 ? 8.599   29.252  -83.754  1.00 67.05  ? 578  GLU   C CD  1 
ATOM   9038  O  OE1 . GLU   C  1 277 ? 7.620   29.563  -84.464  1.00 70.06  ? 578  GLU   C OE1 1 
ATOM   9039  O  OE2 . GLU   C  1 277 ? 8.772   29.694  -82.595  1.00 77.23  ? 578  GLU   C OE2 1 
ATOM   9040  N  N   . ILE   C  1 278 ? 9.866   30.968  -86.844  1.00 35.40  ? 579  ILE   C N   1 
ATOM   9041  C  CA  . ILE   C  1 278 ? 9.088   32.159  -87.187  1.00 41.76  ? 579  ILE   C CA  1 
ATOM   9042  C  C   . ILE   C  1 278 ? 7.696   31.715  -87.622  1.00 46.66  ? 579  ILE   C C   1 
ATOM   9043  O  O   . ILE   C  1 278 ? 7.560   30.847  -88.491  1.00 33.66  ? 579  ILE   C O   1 
ATOM   9044  C  CB  . ILE   C  1 278 ? 9.748   32.984  -88.312  1.00 36.95  ? 579  ILE   C CB  1 
ATOM   9045  C  CG1 . ILE   C  1 278 ? 11.129  33.485  -87.900  1.00 33.01  ? 579  ILE   C CG1 1 
ATOM   9046  C  CG2 . ILE   C  1 278 ? 8.861   34.145  -88.692  1.00 28.07  ? 579  ILE   C CG2 1 
ATOM   9047  C  CD1 . ILE   C  1 278 ? 11.993  33.923  -89.084  1.00 35.23  ? 579  ILE   C CD1 1 
ATOM   9048  N  N   . GLY   C  1 279 ? 6.669   32.300  -87.011  1.00 48.49  ? 580  GLY   C N   1 
ATOM   9049  C  CA  . GLY   C  1 279 ? 5.284   31.951  -87.270  1.00 47.33  ? 580  GLY   C CA  1 
ATOM   9050  C  C   . GLY   C  1 279 ? 4.974   30.483  -87.473  1.00 48.32  ? 580  GLY   C C   1 
ATOM   9051  O  O   . GLY   C  1 279 ? 4.200   30.123  -88.369  1.00 51.76  ? 580  GLY   C O   1 
ATOM   9052  N  N   . GLY   C  1 280 ? 5.566   29.619  -86.658  1.00 40.96  ? 581  GLY   C N   1 
ATOM   9053  C  CA  . GLY   C  1 280 ? 5.359   28.188  -86.800  1.00 47.55  ? 581  GLY   C CA  1 
ATOM   9054  C  C   . GLY   C  1 280 ? 6.232   27.505  -87.834  1.00 45.31  ? 581  GLY   C C   1 
ATOM   9055  O  O   . GLY   C  1 280 ? 6.231   26.265  -87.899  1.00 43.90  ? 581  GLY   C O   1 
ATOM   9056  N  N   . LEU   C  1 281 ? 6.981   28.268  -88.633  1.00 37.73  ? 582  LEU   C N   1 
ATOM   9057  C  CA  . LEU   C  1 281 ? 7.921   27.725  -89.600  1.00 40.60  ? 582  LEU   C CA  1 
ATOM   9058  C  C   . LEU   C  1 281 ? 9.279   27.500  -88.954  1.00 40.94  ? 582  LEU   C C   1 
ATOM   9059  O  O   . LEU   C  1 281 ? 9.697   28.243  -88.063  1.00 48.24  ? 582  LEU   C O   1 
ATOM   9060  C  CB  . LEU   C  1 281 ? 8.074   28.664  -90.802  1.00 36.55  ? 582  LEU   C CB  1 
ATOM   9061  C  CG  . LEU   C  1 281 ? 6.773   29.066  -91.488  1.00 43.47  ? 582  LEU   C CG  1 
ATOM   9062  C  CD1 . LEU   C  1 281 ? 7.071   30.029  -92.616  1.00 45.33  ? 582  LEU   C CD1 1 
ATOM   9063  C  CD2 . LEU   C  1 281 ? 6.042   27.842  -92.002  1.00 37.26  ? 582  LEU   C CD2 1 
ATOM   9064  N  N   . GLU   C  1 282 ? 9.983   26.480  -89.438  1.00 40.81  ? 583  GLU   C N   1 
ATOM   9065  C  CA  . GLU   C  1 282 ? 11.205  25.992  -88.809  1.00 36.97  ? 583  GLU   C CA  1 
ATOM   9066  C  C   . GLU   C  1 282 ? 12.332  25.957  -89.834  1.00 43.33  ? 583  GLU   C C   1 
ATOM   9067  O  O   . GLU   C  1 282 ? 12.368  25.074  -90.698  1.00 40.50  ? 583  GLU   C O   1 
ATOM   9068  C  CB  . GLU   C  1 282 ? 10.993  24.602  -88.216  1.00 42.19  ? 583  GLU   C CB  1 
ATOM   9069  C  CG  . GLU   C  1 282 ? 9.912   24.521  -87.173  1.00 52.98  ? 583  GLU   C CG  1 
ATOM   9070  C  CD  . GLU   C  1 282 ? 9.882   23.165  -86.527  1.00 60.57  ? 583  GLU   C CD  1 
ATOM   9071  O  OE1 . GLU   C  1 282 ? 9.882   22.162  -87.273  1.00 57.76  ? 583  GLU   C OE1 1 
ATOM   9072  O  OE2 . GLU   C  1 282 ? 9.880   23.102  -85.277  1.00 69.87  ? 583  GLU   C OE2 1 
ATOM   9073  N  N   . PHE   C  1 283 ? 13.271  26.879  -89.709  1.00 41.40  ? 584  PHE   C N   1 
ATOM   9074  C  CA  . PHE   C  1 283 ? 14.466  26.890  -90.535  1.00 33.52  ? 584  PHE   C CA  1 
ATOM   9075  C  C   . PHE   C  1 283 ? 15.577  26.163  -89.780  1.00 38.11  ? 584  PHE   C C   1 
ATOM   9076  O  O   . PHE   C  1 283 ? 16.211  26.719  -88.879  1.00 38.60  ? 584  PHE   C O   1 
ATOM   9077  C  CB  . PHE   C  1 283 ? 14.829  28.320  -90.901  1.00 38.08  ? 584  PHE   C CB  1 
ATOM   9078  C  CG  . PHE   C  1 283 ? 13.698  29.055  -91.559  1.00 40.71  ? 584  PHE   C CG  1 
ATOM   9079  C  CD1 . PHE   C  1 283 ? 12.742  29.717  -90.796  1.00 34.39  ? 584  PHE   C CD1 1 
ATOM   9080  C  CD2 . PHE   C  1 283 ? 13.560  29.045  -92.940  1.00 36.92  ? 584  PHE   C CD2 1 
ATOM   9081  C  CE1 . PHE   C  1 283 ? 11.685  30.385  -91.397  1.00 37.94  ? 584  PHE   C CE1 1 
ATOM   9082  C  CE2 . PHE   C  1 283 ? 12.516  29.725  -93.558  1.00 42.23  ? 584  PHE   C CE2 1 
ATOM   9083  C  CZ  . PHE   C  1 283 ? 11.570  30.393  -92.787  1.00 41.21  ? 584  PHE   C CZ  1 
ATOM   9084  N  N   . SER   C  1 284 ? 15.798  24.906  -90.158  1.00 36.16  ? 585  SER   C N   1 
ATOM   9085  C  CA  . SER   C  1 284 ? 16.790  24.056  -89.527  1.00 34.55  ? 585  SER   C CA  1 
ATOM   9086  C  C   . SER   C  1 284 ? 18.217  24.389  -89.932  1.00 36.76  ? 585  SER   C C   1 
ATOM   9087  O  O   . SER   C  1 284 ? 19.149  23.834  -89.336  1.00 38.02  ? 585  SER   C O   1 
ATOM   9088  C  CB  . SER   C  1 284 ? 16.490  22.595  -89.854  1.00 42.97  ? 585  SER   C CB  1 
ATOM   9089  O  OG  . SER   C  1 284 ? 16.143  22.430  -91.217  1.00 60.14  ? 585  SER   C OG  1 
ATOM   9090  N  N   . ALA   C  1 285 ? 18.411  25.250  -90.935  1.00 38.56  ? 586  ALA   C N   1 
ATOM   9091  C  CA  . ALA   C  1 285 ? 19.742  25.650  -91.389  1.00 37.72  ? 586  ALA   C CA  1 
ATOM   9092  C  C   . ALA   C  1 285 ? 19.728  27.162  -91.506  1.00 33.65  ? 586  ALA   C C   1 
ATOM   9093  O  O   . ALA   C  1 285 ? 19.128  27.711  -92.435  1.00 38.23  ? 586  ALA   C O   1 
ATOM   9094  C  CB  . ALA   C  1 285 ? 20.120  24.990  -92.711  1.00 42.56  ? 586  ALA   C CB  1 
ATOM   9095  N  N   . CYS   C  1 286 ? 20.383  27.825  -90.555  1.00 32.02  ? 587  CYS   C N   1 
ATOM   9096  C  CA  . CYS   C  1 286 ? 20.350  29.275  -90.447  1.00 31.42  ? 587  CYS   C CA  1 
ATOM   9097  C  C   . CYS   C  1 286 ? 21.629  29.810  -89.811  1.00 36.37  ? 587  CYS   C C   1 
ATOM   9098  O  O   . CYS   C  1 286 ? 21.558  30.507  -88.789  1.00 41.92  ? 587  CYS   C O   1 
ATOM   9099  C  CB  . CYS   C  1 286 ? 19.147  29.693  -89.614  1.00 36.41  ? 587  CYS   C CB  1 
ATOM   9100  S  SG  . CYS   C  1 286 ? 19.157  28.944  -87.951  1.00 37.47  ? 587  CYS   C SG  1 
ATOM   9101  N  N   . PRO   C  1 287 ? 22.807  29.527  -90.372  1.00 34.16  ? 588  PRO   C N   1 
ATOM   9102  C  CA  . PRO   C  1 287 ? 24.042  29.961  -89.712  1.00 28.56  ? 588  PRO   C CA  1 
ATOM   9103  C  C   . PRO   C  1 287 ? 24.079  31.476  -89.562  1.00 37.60  ? 588  PRO   C C   1 
ATOM   9104  O  O   . PRO   C  1 287 ? 23.811  32.221  -90.515  1.00 38.90  ? 588  PRO   C O   1 
ATOM   9105  C  CB  . PRO   C  1 287 ? 25.140  29.446  -90.646  1.00 34.71  ? 588  PRO   C CB  1 
ATOM   9106  C  CG  . PRO   C  1 287 ? 24.462  29.276  -92.010  1.00 29.68  ? 588  PRO   C CG  1 
ATOM   9107  C  CD  . PRO   C  1 287 ? 23.061  28.885  -91.687  1.00 30.49  ? 588  PRO   C CD  1 
ATOM   9108  N  N   . PHE   C  1 288 ? 24.385  31.932  -88.338  1.00 27.98  ? 589  PHE   C N   1 
ATOM   9109  C  CA  . PHE   C  1 288 ? 24.507  33.352  -88.008  1.00 27.01  ? 589  PHE   C CA  1 
ATOM   9110  C  C   . PHE   C  1 288 ? 25.859  33.635  -87.372  1.00 31.32  ? 589  PHE   C C   1 
ATOM   9111  O  O   . PHE   C  1 288 ? 26.454  32.782  -86.708  1.00 33.40  ? 589  PHE   C O   1 
ATOM   9112  C  CB  . PHE   C  1 288 ? 23.407  33.848  -87.053  1.00 24.93  ? 589  PHE   C CB  1 
ATOM   9113  C  CG  . PHE   C  1 288 ? 23.246  33.008  -85.783  1.00 30.16  ? 589  PHE   C CG  1 
ATOM   9114  C  CD1 . PHE   C  1 288 ? 23.923  33.338  -84.610  1.00 36.12  ? 589  PHE   C CD1 1 
ATOM   9115  C  CD2 . PHE   C  1 288 ? 22.380  31.925  -85.760  1.00 31.32  ? 589  PHE   C CD2 1 
ATOM   9116  C  CE1 . PHE   C  1 288 ? 23.757  32.587  -83.448  1.00 30.81  ? 589  PHE   C CE1 1 
ATOM   9117  C  CE2 . PHE   C  1 288 ? 22.202  31.170  -84.601  1.00 41.06  ? 589  PHE   C CE2 1 
ATOM   9118  C  CZ  . PHE   C  1 288 ? 22.894  31.502  -83.444  1.00 32.03  ? 589  PHE   C CZ  1 
ATOM   9119  N  N   . SER   C  1 289 ? 26.339  34.855  -87.564  1.00 34.98  ? 590  SER   C N   1 
ATOM   9120  C  CA  . SER   C  1 289 ? 27.656  35.179  -87.062  1.00 27.40  ? 590  SER   C CA  1 
ATOM   9121  C  C   . SER   C  1 289 ? 27.649  36.611  -86.571  1.00 28.12  ? 590  SER   C C   1 
ATOM   9122  O  O   . SER   C  1 289 ? 26.824  37.426  -86.987  1.00 25.36  ? 590  SER   C O   1 
ATOM   9123  C  CB  . SER   C  1 289 ? 28.748  34.962  -88.120  1.00 29.54  ? 590  SER   C CB  1 
ATOM   9124  O  OG  . SER   C  1 289 ? 28.671  35.930  -89.160  1.00 36.60  ? 590  SER   C OG  1 
ATOM   9125  N  N   . GLY   C  1 290 ? 28.533  36.892  -85.620  1.00 32.08  ? 591  GLY   C N   1 
ATOM   9126  C  CA  . GLY   C  1 290 ? 28.720  38.259  -85.180  1.00 24.17  ? 591  GLY   C CA  1 
ATOM   9127  C  C   . GLY   C  1 290 ? 30.198  38.498  -85.002  1.00 38.38  ? 591  GLY   C C   1 
ATOM   9128  O  O   . GLY   C  1 290 ? 30.964  38.345  -85.955  1.00 40.93  ? 591  GLY   C O   1 
ATOM   9129  N  N   . TRP   C  1 291 ? 30.620  38.852  -83.789  1.00 38.97  ? 592  TRP   C N   1 
ATOM   9130  C  CA  . TRP   C  1 291 ? 32.034  38.896  -83.458  1.00 40.05  ? 592  TRP   C CA  1 
ATOM   9131  C  C   . TRP   C  1 291 ? 32.199  38.433  -82.012  1.00 34.85  ? 592  TRP   C C   1 
ATOM   9132  O  O   . TRP   C  1 291 ? 31.233  38.315  -81.265  1.00 40.76  ? 592  TRP   C O   1 
ATOM   9133  C  CB  . TRP   C  1 291 ? 32.618  40.295  -83.698  1.00 36.84  ? 592  TRP   C CB  1 
ATOM   9134  C  CG  . TRP   C  1 291 ? 31.830  41.338  -83.017  1.00 41.98  ? 592  TRP   C CG  1 
ATOM   9135  C  CD1 . TRP   C  1 291 ? 31.851  41.630  -81.693  1.00 39.42  ? 592  TRP   C CD1 1 
ATOM   9136  C  CD2 . TRP   C  1 291 ? 30.884  42.231  -83.613  1.00 41.19  ? 592  TRP   C CD2 1 
ATOM   9137  N  NE1 . TRP   C  1 291 ? 30.971  42.643  -81.413  1.00 46.70  ? 592  TRP   C NE1 1 
ATOM   9138  C  CE2 . TRP   C  1 291 ? 30.364  43.037  -82.574  1.00 42.29  ? 592  TRP   C CE2 1 
ATOM   9139  C  CE3 . TRP   C  1 291 ? 30.414  42.421  -84.920  1.00 37.16  ? 592  TRP   C CE3 1 
ATOM   9140  C  CZ2 . TRP   C  1 291 ? 29.405  44.026  -82.798  1.00 42.27  ? 592  TRP   C CZ2 1 
ATOM   9141  C  CZ3 . TRP   C  1 291 ? 29.459  43.404  -85.150  1.00 40.77  ? 592  TRP   C CZ3 1 
ATOM   9142  C  CH2 . TRP   C  1 291 ? 28.969  44.201  -84.093  1.00 52.25  ? 592  TRP   C CH2 1 
ATOM   9143  N  N   . TYR   C  1 292 ? 33.430  38.115  -81.648  1.00 32.76  ? 593  TYR   C N   1 
ATOM   9144  C  CA  . TYR   C  1 292 ? 33.728  37.459  -80.390  1.00 34.31  ? 593  TYR   C CA  1 
ATOM   9145  C  C   . TYR   C  1 292 ? 33.769  38.446  -79.231  1.00 35.63  ? 593  TYR   C C   1 
ATOM   9146  O  O   . TYR   C  1 292 ? 34.180  39.602  -79.370  1.00 42.45  ? 593  TYR   C O   1 
ATOM   9147  C  CB  . TYR   C  1 292 ? 35.085  36.764  -80.446  1.00 31.22  ? 593  TYR   C CB  1 
ATOM   9148  C  CG  . TYR   C  1 292 ? 35.047  35.333  -80.858  1.00 36.99  ? 593  TYR   C CG  1 
ATOM   9149  C  CD1 . TYR   C  1 292 ? 34.311  34.417  -80.136  1.00 35.97  ? 593  TYR   C CD1 1 
ATOM   9150  C  CD2 . TYR   C  1 292 ? 35.778  34.883  -81.954  1.00 36.35  ? 593  TYR   C CD2 1 
ATOM   9151  C  CE1 . TYR   C  1 292 ? 34.283  33.096  -80.499  1.00 31.42  ? 593  TYR   C CE1 1 
ATOM   9152  C  CE2 . TYR   C  1 292 ? 35.762  33.567  -82.320  1.00 36.74  ? 593  TYR   C CE2 1 
ATOM   9153  C  CZ  . TYR   C  1 292 ? 35.007  32.673  -81.590  1.00 39.78  ? 593  TYR   C CZ  1 
ATOM   9154  O  OH  . TYR   C  1 292 ? 34.978  31.343  -81.935  1.00 49.98  ? 593  TYR   C OH  1 
ATOM   9155  N  N   . MET   C  1 293 ? 33.348  37.962  -78.071  1.00 40.85  ? 594  MET   C N   1 
ATOM   9156  C  CA  . MET   C  1 293 ? 33.787  38.522  -76.808  1.00 38.42  ? 594  MET   C CA  1 
ATOM   9157  C  C   . MET   C  1 293 ? 35.042  37.753  -76.421  1.00 35.69  ? 594  MET   C C   1 
ATOM   9158  O  O   . MET   C  1 293 ? 35.063  36.520  -76.505  1.00 37.71  ? 594  MET   C O   1 
ATOM   9159  C  CB  . MET   C  1 293 ? 32.692  38.397  -75.746  1.00 37.85  ? 594  MET   C CB  1 
ATOM   9160  C  CG  . MET   C  1 293 ? 32.978  39.187  -74.490  1.00 40.13  ? 594  MET   C CG  1 
ATOM   9161  S  SD  . MET   C  1 293 ? 31.501  39.461  -73.480  1.00 42.17  ? 594  MET   C SD  1 
ATOM   9162  C  CE  . MET   C  1 293 ? 31.219  37.835  -72.810  1.00 23.77  ? 594  MET   C CE  1 
ATOM   9163  N  N   . GLY   C  1 294 ? 36.094  38.480  -76.034  1.00 40.09  ? 595  GLY   C N   1 
ATOM   9164  C  CA  . GLY   C  1 294 ? 37.374  37.843  -75.748  1.00 42.84  ? 595  GLY   C CA  1 
ATOM   9165  C  C   . GLY   C  1 294 ? 37.301  36.631  -74.839  1.00 38.52  ? 595  GLY   C C   1 
ATOM   9166  O  O   . GLY   C  1 294 ? 38.091  35.690  -74.989  1.00 37.27  ? 595  GLY   C O   1 
ATOM   9167  N  N   . THR   C  1 295 ? 36.352  36.620  -73.895  1.00 32.20  ? 596  THR   C N   1 
ATOM   9168  C  CA  . THR   C  1 295 ? 36.314  35.529  -72.920  1.00 33.14  ? 596  THR   C CA  1 
ATOM   9169  C  C   . THR   C  1 295 ? 35.919  34.203  -73.548  1.00 37.14  ? 596  THR   C C   1 
ATOM   9170  O  O   . THR   C  1 295 ? 36.330  33.146  -73.049  1.00 40.41  ? 596  THR   C O   1 
ATOM   9171  C  CB  . THR   C  1 295 ? 35.354  35.849  -71.778  1.00 35.51  ? 596  THR   C CB  1 
ATOM   9172  O  OG1 . THR   C  1 295 ? 34.094  36.243  -72.326  1.00 34.81  ? 596  THR   C OG1 1 
ATOM   9173  C  CG2 . THR   C  1 295 ? 35.913  36.975  -70.894  1.00 32.77  ? 596  THR   C CG2 1 
ATOM   9174  N  N   . GLU   C  1 296 ? 35.116  34.229  -74.619  1.00 34.07  ? 597  GLU   C N   1 
ATOM   9175  C  CA  . GLU   C  1 296 ? 34.711  32.982  -75.255  1.00 41.05  ? 597  GLU   C CA  1 
ATOM   9176  C  C   . GLU   C  1 296 ? 35.925  32.182  -75.712  1.00 40.51  ? 597  GLU   C C   1 
ATOM   9177  O  O   . GLU   C  1 296 ? 35.965  30.957  -75.549  1.00 42.34  ? 597  GLU   C O   1 
ATOM   9178  C  CB  . GLU   C  1 296 ? 33.785  33.268  -76.432  1.00 44.41  ? 597  GLU   C CB  1 
ATOM   9179  C  CG  . GLU   C  1 296 ? 32.556  34.081  -76.091  1.00 38.07  ? 597  GLU   C CG  1 
ATOM   9180  C  CD  . GLU   C  1 296 ? 31.710  34.397  -77.334  1.00 38.80  ? 597  GLU   C CD  1 
ATOM   9181  O  OE1 . GLU   C  1 296 ? 31.062  33.462  -77.854  1.00 35.86  ? 597  GLU   C OE1 1 
ATOM   9182  O  OE2 . GLU   C  1 296 ? 31.700  35.563  -77.780  1.00 30.03  ? 597  GLU   C OE2 1 
ATOM   9183  N  N   . ILE   C  1 297 ? 36.936  32.870  -76.251  1.00 36.91  ? 598  ILE   C N   1 
ATOM   9184  C  CA  . ILE   C  1 297 ? 38.181  32.225  -76.651  1.00 36.38  ? 598  ILE   C CA  1 
ATOM   9185  C  C   . ILE   C  1 297 ? 39.098  32.025  -75.455  1.00 42.58  ? 598  ILE   C C   1 
ATOM   9186  O  O   . ILE   C  1 297 ? 39.616  30.928  -75.229  1.00 47.02  ? 598  ILE   C O   1 
ATOM   9187  C  CB  . ILE   C  1 297 ? 38.907  33.071  -77.706  1.00 38.62  ? 598  ILE   C CB  1 
ATOM   9188  C  CG1 . ILE   C  1 297 ? 37.971  33.451  -78.855  1.00 43.29  ? 598  ILE   C CG1 1 
ATOM   9189  C  CG2 . ILE   C  1 297 ? 40.137  32.333  -78.164  1.00 29.32  ? 598  ILE   C CG2 1 
ATOM   9190  C  CD1 . ILE   C  1 297 ? 38.480  34.608  -79.669  1.00 41.62  ? 598  ILE   C CD1 1 
ATOM   9191  N  N   . GLY   C  1 298 ? 39.375  33.114  -74.727  1.00 42.67  ? 599  GLY   C N   1 
ATOM   9192  C  CA  . GLY   C  1 298 ? 40.433  33.092  -73.727  1.00 48.89  ? 599  GLY   C CA  1 
ATOM   9193  C  C   . GLY   C  1 298 ? 40.064  32.343  -72.457  1.00 44.63  ? 599  GLY   C C   1 
ATOM   9194  O  O   . GLY   C  1 298 ? 40.917  31.698  -71.844  1.00 42.07  ? 599  GLY   C O   1 
ATOM   9195  N  N   . VAL   C  1 299 ? 38.798  32.406  -72.051  1.00 36.89  ? 600  VAL   C N   1 
ATOM   9196  C  CA  . VAL   C  1 299 ? 38.360  31.648  -70.889  1.00 36.08  ? 600  VAL   C CA  1 
ATOM   9197  C  C   . VAL   C  1 299 ? 37.891  30.256  -71.282  1.00 44.46  ? 600  VAL   C C   1 
ATOM   9198  O  O   . VAL   C  1 299 ? 38.500  29.257  -70.878  1.00 43.55  ? 600  VAL   C O   1 
ATOM   9199  C  CB  . VAL   C  1 299 ? 37.250  32.390  -70.133  1.00 31.71  ? 600  VAL   C CB  1 
ATOM   9200  C  CG1 . VAL   C  1 299 ? 36.864  31.579  -68.942  1.00 39.54  ? 600  VAL   C CG1 1 
ATOM   9201  C  CG2 . VAL   C  1 299 ? 37.717  33.777  -69.709  1.00 31.90  ? 600  VAL   C CG2 1 
ATOM   9202  N  N   . ARG   C  1 300 ? 36.807  30.182  -72.072  1.00 46.92  ? 601  ARG   C N   1 
ATOM   9203  C  CA  . ARG   C  1 300 ? 36.125  28.911  -72.322  1.00 42.68  ? 601  ARG   C CA  1 
ATOM   9204  C  C   . ARG   C  1 300 ? 36.871  28.044  -73.333  1.00 51.25  ? 601  ARG   C C   1 
ATOM   9205  O  O   . ARG   C  1 300 ? 37.132  26.863  -73.066  1.00 49.60  ? 601  ARG   C O   1 
ATOM   9206  C  CB  . ARG   C  1 300 ? 34.688  29.153  -72.803  1.00 32.43  ? 601  ARG   C CB  1 
ATOM   9207  C  CG  . ARG   C  1 300 ? 33.840  29.994  -71.881  1.00 31.58  ? 601  ARG   C CG  1 
ATOM   9208  C  CD  . ARG   C  1 300 ? 33.725  29.380  -70.476  1.00 39.92  ? 601  ARG   C CD  1 
ATOM   9209  N  NE  . ARG   C  1 300 ? 33.325  27.975  -70.548  1.00 48.19  ? 601  ARG   C NE  1 
ATOM   9210  C  CZ  . ARG   C  1 300 ? 32.089  27.553  -70.811  1.00 42.89  ? 601  ARG   C CZ  1 
ATOM   9211  N  NH1 . ARG   C  1 300 ? 31.105  28.421  -71.021  1.00 41.06  ? 601  ARG   C NH1 1 
ATOM   9212  N  NH2 . ARG   C  1 300 ? 31.840  26.256  -70.870  1.00 39.83  ? 601  ARG   C NH2 1 
ATOM   9213  N  N   . ASP   C  1 301 ? 37.202  28.604  -74.509  1.00 46.22  ? 602  ASP   C N   1 
ATOM   9214  C  CA  . ASP   C  1 301 ? 37.855  27.811  -75.551  1.00 48.59  ? 602  ASP   C CA  1 
ATOM   9215  C  C   . ASP   C  1 301 ? 39.234  27.334  -75.107  1.00 50.10  ? 602  ASP   C C   1 
ATOM   9216  O  O   . ASP   C  1 301 ? 39.602  26.174  -75.327  1.00 45.65  ? 602  ASP   C O   1 
ATOM   9217  C  CB  . ASP   C  1 301 ? 37.968  28.621  -76.846  1.00 52.40  ? 602  ASP   C CB  1 
ATOM   9218  C  CG  . ASP   C  1 301 ? 36.626  28.809  -77.541  1.00 55.66  ? 602  ASP   C CG  1 
ATOM   9219  O  OD1 . ASP   C  1 301 ? 35.761  27.909  -77.436  1.00 55.15  ? 602  ASP   C OD1 1 
ATOM   9220  O  OD2 . ASP   C  1 301 ? 36.437  29.861  -78.191  1.00 53.37  ? 602  ASP   C OD2 1 
ATOM   9221  N  N   . TYR   C  1 302 ? 39.999  28.203  -74.456  1.00 51.03  ? 603  TYR   C N   1 
ATOM   9222  C  CA  . TYR   C  1 302 ? 41.369  27.873  -74.097  1.00 43.01  ? 603  TYR   C CA  1 
ATOM   9223  C  C   . TYR   C  1 302 ? 41.515  27.187  -72.744  1.00 48.49  ? 603  TYR   C C   1 
ATOM   9224  O  O   . TYR   C  1 302 ? 42.407  26.343  -72.598  1.00 48.57  ? 603  TYR   C O   1 
ATOM   9225  C  CB  . TYR   C  1 302 ? 42.216  29.139  -74.102  1.00 51.95  ? 603  TYR   C CB  1 
ATOM   9226  C  CG  . TYR   C  1 302 ? 42.704  29.532  -75.466  1.00 57.94  ? 603  TYR   C CG  1 
ATOM   9227  C  CD1 . TYR   C  1 302 ? 42.684  28.630  -76.520  1.00 55.27  ? 603  TYR   C CD1 1 
ATOM   9228  C  CD2 . TYR   C  1 302 ? 43.207  30.804  -75.698  1.00 62.56  ? 603  TYR   C CD2 1 
ATOM   9229  C  CE1 . TYR   C  1 302 ? 43.139  28.994  -77.752  1.00 55.91  ? 603  TYR   C CE1 1 
ATOM   9230  C  CE2 . TYR   C  1 302 ? 43.674  31.169  -76.930  1.00 53.28  ? 603  TYR   C CE2 1 
ATOM   9231  C  CZ  . TYR   C  1 302 ? 43.635  30.265  -77.951  1.00 57.68  ? 603  TYR   C CZ  1 
ATOM   9232  O  OH  . TYR   C  1 302 ? 44.093  30.643  -79.193  1.00 63.97  ? 603  TYR   C OH  1 
ATOM   9233  N  N   . CYS   C  1 303 ? 40.669  27.513  -71.749  1.00 44.13  ? 604  CYS   C N   1 
ATOM   9234  C  CA  . CYS   C  1 303 ? 40.929  27.095  -70.372  1.00 51.55  ? 604  CYS   C CA  1 
ATOM   9235  C  C   . CYS   C  1 303 ? 39.930  26.109  -69.768  1.00 45.12  ? 604  CYS   C C   1 
ATOM   9236  O  O   . CYS   C  1 303 ? 40.245  25.535  -68.718  1.00 48.46  ? 604  CYS   C O   1 
ATOM   9237  C  CB  . CYS   C  1 303 ? 41.023  28.316  -69.440  1.00 53.28  ? 604  CYS   C CB  1 
ATOM   9238  S  SG  . CYS   C  1 303 ? 42.418  29.424  -69.818  1.00 53.94  ? 604  CYS   C SG  1 
ATOM   9239  N  N   . ASP   C  1 304 ? 38.747  25.898  -70.368  1.00 38.55  ? 605  ASP   C N   1 
ATOM   9240  C  CA  . ASP   C  1 304 ? 37.894  24.786  -69.947  1.00 41.70  ? 605  ASP   C CA  1 
ATOM   9241  C  C   . ASP   C  1 304 ? 38.714  23.501  -69.910  1.00 51.98  ? 605  ASP   C C   1 
ATOM   9242  O  O   . ASP   C  1 304 ? 39.640  23.309  -70.706  1.00 66.71  ? 605  ASP   C O   1 
ATOM   9243  C  CB  . ASP   C  1 304 ? 36.696  24.592  -70.890  1.00 36.97  ? 605  ASP   C CB  1 
ATOM   9244  C  CG  . ASP   C  1 304 ? 35.492  25.461  -70.535  1.00 51.61  ? 605  ASP   C CG  1 
ATOM   9245  O  OD1 . ASP   C  1 304 ? 35.627  26.403  -69.715  1.00 52.72  ? 605  ASP   C OD1 1 
ATOM   9246  O  OD2 . ASP   C  1 304 ? 34.400  25.193  -71.100  1.00 56.15  ? 605  ASP   C OD2 1 
ATOM   9247  N  N   . ASN   C  1 305 ? 38.373  22.607  -68.981  1.00 54.73  ? 606  ASN   C N   1 
ATOM   9248  C  CA  . ASN   C  1 305 ? 39.169  21.392  -68.826  1.00 56.73  ? 606  ASN   C CA  1 
ATOM   9249  C  C   . ASN   C  1 305 ? 39.016  20.467  -70.028  1.00 57.85  ? 606  ASN   C C   1 
ATOM   9250  O  O   . ASN   C  1 305 ? 39.989  19.835  -70.456  1.00 61.75  ? 606  ASN   C O   1 
ATOM   9251  C  CB  . ASN   C  1 305 ? 38.791  20.659  -67.538  1.00 58.75  ? 606  ASN   C CB  1 
ATOM   9252  C  CG  . ASN   C  1 305 ? 39.562  21.164  -66.345  1.00 64.75  ? 606  ASN   C CG  1 
ATOM   9253  O  OD1 . ASN   C  1 305 ? 38.988  21.706  -65.402  1.00 69.75  ? 606  ASN   C OD1 1 
ATOM   9254  N  ND2 . ASN   C  1 305 ? 40.880  21.003  -66.384  1.00 65.16  ? 606  ASN   C ND2 1 
ATOM   9255  N  N   . SER   C  1 306 ? 37.802  20.359  -70.576  1.00 55.25  ? 607  SER   C N   1 
ATOM   9256  C  CA  . SER   C  1 306 ? 37.555  19.485  -71.711  1.00 62.88  ? 607  SER   C CA  1 
ATOM   9257  C  C   . SER   C  1 306 ? 37.662  20.231  -73.041  1.00 61.94  ? 607  SER   C C   1 
ATOM   9258  O  O   . SER   C  1 306 ? 37.161  19.745  -74.070  1.00 65.70  ? 607  SER   C O   1 
ATOM   9259  C  CB  . SER   C  1 306 ? 36.201  18.790  -71.558  1.00 58.39  ? 607  SER   C CB  1 
ATOM   9260  O  OG  . SER   C  1 306 ? 35.249  19.646  -70.976  1.00 62.73  ? 607  SER   C OG  1 
ATOM   9261  N  N   . ARG   C  1 307 ? 38.315  21.384  -73.034  1.00 54.45  ? 608  ARG   C N   1 
ATOM   9262  C  CA  . ARG   C  1 307 ? 38.650  22.129  -74.245  1.00 53.59  ? 608  ARG   C CA  1 
ATOM   9263  C  C   . ARG   C  1 307 ? 40.170  22.155  -74.378  1.00 53.20  ? 608  ARG   C C   1 
ATOM   9264  O  O   . ARG   C  1 307 ? 40.792  21.097  -74.221  1.00 60.26  ? 608  ARG   C O   1 
ATOM   9265  C  CB  . ARG   C  1 307 ? 37.965  23.494  -74.193  1.00 46.92  ? 608  ARG   C CB  1 
ATOM   9266  C  CG  . ARG   C  1 307 ? 36.469  23.389  -74.255  1.00 44.61  ? 608  ARG   C CG  1 
ATOM   9267  C  CD  . ARG   C  1 307 ? 35.972  22.719  -75.548  1.00 52.71  ? 608  ARG   C CD  1 
ATOM   9268  N  NE  . ARG   C  1 307 ? 36.397  23.428  -76.757  1.00 47.41  ? 608  ARG   C NE  1 
ATOM   9269  C  CZ  . ARG   C  1 307 ? 35.945  24.628  -77.127  1.00 51.54  ? 608  ARG   C CZ  1 
ATOM   9270  N  NH1 . ARG   C  1 307 ? 35.038  25.263  -76.386  1.00 42.80  ? 608  ARG   C NH1 1 
ATOM   9271  N  NH2 . ARG   C  1 307 ? 36.400  25.200  -78.247  1.00 43.87  ? 608  ARG   C NH2 1 
ATOM   9272  N  N   . TYR   C  1 308 ? 40.806  23.296  -74.665  1.00 48.21  ? 609  TYR   C N   1 
ATOM   9273  C  CA  . TYR   C  1 308 ? 42.238  23.239  -74.955  1.00 43.67  ? 609  TYR   C CA  1 
ATOM   9274  C  C   . TYR   C  1 308 ? 43.078  23.086  -73.695  1.00 48.83  ? 609  TYR   C C   1 
ATOM   9275  O  O   . TYR   C  1 308 ? 44.174  22.529  -73.775  1.00 53.21  ? 609  TYR   C O   1 
ATOM   9276  C  CB  . TYR   C  1 308 ? 42.689  24.455  -75.768  1.00 45.70  ? 609  TYR   C CB  1 
ATOM   9277  C  CG  . TYR   C  1 308 ? 42.509  24.216  -77.261  1.00 62.48  ? 609  TYR   C CG  1 
ATOM   9278  C  CD1 . TYR   C  1 308 ? 41.292  24.478  -77.887  1.00 58.26  ? 609  TYR   C CD1 1 
ATOM   9279  C  CD2 . TYR   C  1 308 ? 43.536  23.684  -78.031  1.00 67.02  ? 609  TYR   C CD2 1 
ATOM   9280  C  CE1 . TYR   C  1 308 ? 41.115  24.240  -79.239  1.00 56.57  ? 609  TYR   C CE1 1 
ATOM   9281  C  CE2 . TYR   C  1 308 ? 43.368  23.448  -79.383  1.00 67.41  ? 609  TYR   C CE2 1 
ATOM   9282  C  CZ  . TYR   C  1 308 ? 42.156  23.725  -79.977  1.00 63.43  ? 609  TYR   C CZ  1 
ATOM   9283  O  OH  . TYR   C  1 308 ? 41.995  23.482  -81.323  1.00 60.99  ? 609  TYR   C OH  1 
ATOM   9284  N  N   . ASN   C  1 309 ? 42.596  23.569  -72.542  1.00 40.99  ? 610  ASN   C N   1 
ATOM   9285  C  CA  . ASN   C  1 309 ? 43.207  23.266  -71.235  1.00 47.54  ? 610  ASN   C CA  1 
ATOM   9286  C  C   . ASN   C  1 309 ? 44.659  23.746  -71.146  1.00 50.32  ? 610  ASN   C C   1 
ATOM   9287  O  O   . ASN   C  1 309 ? 45.561  23.005  -70.745  1.00 53.62  ? 610  ASN   C O   1 
ATOM   9288  C  CB  . ASN   C  1 309 ? 43.113  21.766  -70.935  1.00 45.06  ? 610  ASN   C CB  1 
ATOM   9289  C  CG  . ASN   C  1 309 ? 43.305  21.441  -69.457  1.00 51.60  ? 610  ASN   C CG  1 
ATOM   9290  O  OD1 . ASN   C  1 309 ? 42.784  22.125  -68.580  1.00 53.83  ? 610  ASN   C OD1 1 
ATOM   9291  N  ND2 . ASN   C  1 309 ? 44.049  20.387  -69.185  1.00 49.04  ? 610  ASN   C ND2 1 
ATOM   9292  N  N   . ILE   C  1 310 ? 44.886  25.004  -71.520  1.00 52.49  ? 611  ILE   C N   1 
ATOM   9293  C  CA  . ILE   C  1 310 ? 46.253  25.502  -71.657  1.00 59.42  ? 611  ILE   C CA  1 
ATOM   9294  C  C   . ILE   C  1 310 ? 46.751  26.151  -70.366  1.00 60.75  ? 611  ILE   C C   1 
ATOM   9295  O  O   . ILE   C  1 310 ? 47.880  26.656  -70.319  1.00 58.75  ? 611  ILE   C O   1 
ATOM   9296  C  CB  . ILE   C  1 310 ? 46.361  26.488  -72.832  1.00 61.68  ? 611  ILE   C CB  1 
ATOM   9297  C  CG1 . ILE   C  1 310 ? 45.766  27.841  -72.447  1.00 58.84  ? 611  ILE   C CG1 1 
ATOM   9298  C  CG2 . ILE   C  1 310 ? 45.650  25.933  -74.057  1.00 62.64  ? 611  ILE   C CG2 1 
ATOM   9299  C  CD1 . ILE   C  1 310 ? 45.953  28.900  -73.509  1.00 53.00  ? 611  ILE   C CD1 1 
ATOM   9300  N  N   . LEU   C  1 311 ? 45.930  26.130  -69.307  1.00 57.97  ? 612  LEU   C N   1 
ATOM   9301  C  CA  . LEU   C  1 311 ? 46.289  26.834  -68.075  1.00 59.43  ? 612  LEU   C CA  1 
ATOM   9302  C  C   . LEU   C  1 311 ? 47.613  26.333  -67.508  1.00 57.11  ? 612  LEU   C C   1 
ATOM   9303  O  O   . LEU   C  1 311 ? 48.500  27.132  -67.188  1.00 60.61  ? 612  LEU   C O   1 
ATOM   9304  C  CB  . LEU   C  1 311 ? 45.174  26.700  -67.031  1.00 53.42  ? 612  LEU   C CB  1 
ATOM   9305  C  CG  . LEU   C  1 311 ? 44.017  27.690  -67.163  1.00 44.30  ? 612  LEU   C CG  1 
ATOM   9306  C  CD1 . LEU   C  1 311 ? 42.905  27.400  -66.176  1.00 36.03  ? 612  LEU   C CD1 1 
ATOM   9307  C  CD2 . LEU   C  1 311 ? 44.509  29.108  -66.999  1.00 39.39  ? 612  LEU   C CD2 1 
ATOM   9308  N  N   . GLU   C  1 312 ? 47.775  25.014  -67.393  1.00 59.69  ? 613  GLU   C N   1 
ATOM   9309  C  CA  . GLU   C  1 312 ? 49.007  24.469  -66.828  1.00 67.33  ? 613  GLU   C CA  1 
ATOM   9310  C  C   . GLU   C  1 312 ? 50.234  24.965  -67.581  1.00 71.07  ? 613  GLU   C C   1 
ATOM   9311  O  O   . GLU   C  1 312 ? 51.213  25.412  -66.970  1.00 68.80  ? 613  GLU   C O   1 
ATOM   9312  C  CB  . GLU   C  1 312 ? 48.964  22.945  -66.841  1.00 74.97  ? 613  GLU   C CB  1 
ATOM   9313  C  CG  . GLU   C  1 312 ? 48.297  22.350  -65.639  1.00 88.20  ? 613  GLU   C CG  1 
ATOM   9314  C  CD  . GLU   C  1 312 ? 48.461  20.853  -65.593  1.00 102.75 ? 613  GLU   C CD  1 
ATOM   9315  O  OE1 . GLU   C  1 312 ? 47.452  20.145  -65.776  1.00 110.15 ? 613  GLU   C OE1 1 
ATOM   9316  O  OE2 . GLU   C  1 312 ? 49.602  20.383  -65.397  1.00 107.13 ? 613  GLU   C OE2 1 
ATOM   9317  N  N   . GLU   C  1 313 ? 50.190  24.905  -68.917  1.00 76.07  ? 614  GLU   C N   1 
ATOM   9318  C  CA  . GLU   C  1 313 ? 51.362  25.232  -69.724  1.00 76.56  ? 614  GLU   C CA  1 
ATOM   9319  C  C   . GLU   C  1 313 ? 51.680  26.719  -69.672  1.00 75.00  ? 614  GLU   C C   1 
ATOM   9320  O  O   . GLU   C  1 313 ? 52.853  27.108  -69.647  1.00 78.76  ? 614  GLU   C O   1 
ATOM   9321  C  CB  . GLU   C  1 313 ? 51.133  24.779  -71.160  1.00 77.78  ? 614  GLU   C CB  1 
ATOM   9322  C  CG  . GLU   C  1 313 ? 52.124  25.325  -72.159  1.00 86.70  ? 614  GLU   C CG  1 
ATOM   9323  C  CD  . GLU   C  1 313 ? 52.200  24.463  -73.405  1.00 97.40  ? 614  GLU   C CD  1 
ATOM   9324  O  OE1 . GLU   C  1 313 ? 53.266  24.449  -74.061  1.00 101.85 ? 614  GLU   C OE1 1 
ATOM   9325  O  OE2 . GLU   C  1 313 ? 51.192  23.788  -73.718  1.00 99.65  ? 614  GLU   C OE2 1 
ATOM   9326  N  N   . VAL   C  1 314 ? 50.650  27.565  -69.666  1.00 70.95  ? 615  VAL   C N   1 
ATOM   9327  C  CA  . VAL   C  1 314 ? 50.871  28.994  -69.471  1.00 68.50  ? 615  VAL   C CA  1 
ATOM   9328  C  C   . VAL   C  1 314 ? 51.407  29.264  -68.068  1.00 66.25  ? 615  VAL   C C   1 
ATOM   9329  O  O   . VAL   C  1 314 ? 52.282  30.116  -67.873  1.00 63.23  ? 615  VAL   C O   1 
ATOM   9330  C  CB  . VAL   C  1 314 ? 49.570  29.763  -69.751  1.00 61.60  ? 615  VAL   C CB  1 
ATOM   9331  C  CG1 . VAL   C  1 314 ? 49.725  31.233  -69.419  1.00 56.89  ? 615  VAL   C CG1 1 
ATOM   9332  C  CG2 . VAL   C  1 314 ? 49.170  29.585  -71.214  1.00 57.87  ? 615  VAL   C CG2 1 
ATOM   9333  N  N   . ALA   C  1 315 ? 50.915  28.525  -67.073  1.00 68.24  ? 616  ALA   C N   1 
ATOM   9334  C  CA  . ALA   C  1 315 ? 51.378  28.740  -65.707  1.00 67.49  ? 616  ALA   C CA  1 
ATOM   9335  C  C   . ALA   C  1 315 ? 52.860  28.396  -65.565  1.00 63.85  ? 616  ALA   C C   1 
ATOM   9336  O  O   . ALA   C  1 315 ? 53.631  29.180  -65.001  1.00 62.12  ? 616  ALA   C O   1 
ATOM   9337  C  CB  . ALA   C  1 315 ? 50.517  27.934  -64.732  1.00 67.29  ? 616  ALA   C CB  1 
ATOM   9338  N  N   . LYS   C  1 316 ? 53.280  27.235  -66.082  1.00 69.30  ? 617  LYS   C N   1 
ATOM   9339  C  CA  . LYS   C  1 316 ? 54.699  26.877  -66.098  1.00 74.20  ? 617  LYS   C CA  1 
ATOM   9340  C  C   . LYS   C  1 316 ? 55.546  28.030  -66.622  1.00 72.25  ? 617  LYS   C C   1 
ATOM   9341  O  O   . LYS   C  1 316 ? 56.455  28.519  -65.939  1.00 69.60  ? 617  LYS   C O   1 
ATOM   9342  C  CB  . LYS   C  1 316 ? 54.926  25.628  -66.961  1.00 76.20  ? 617  LYS   C CB  1 
ATOM   9343  C  CG  . LYS   C  1 316 ? 54.394  24.324  -66.390  1.00 81.09  ? 617  LYS   C CG  1 
ATOM   9344  C  CD  . LYS   C  1 316 ? 54.243  23.266  -67.479  1.00 87.04  ? 617  LYS   C CD  1 
ATOM   9345  C  CE  . LYS   C  1 316 ? 55.586  22.849  -68.074  1.00 96.80  ? 617  LYS   C CE  1 
ATOM   9346  N  NZ  . LYS   C  1 316 ? 56.123  21.599  -67.467  1.00 98.60  ? 617  LYS   C NZ  1 
ATOM   9347  N  N   . LYS   C  1 317 ? 55.232  28.494  -67.835  1.00 66.10  ? 618  LYS   C N   1 
ATOM   9348  C  CA  . LYS   C  1 317 ? 55.997  29.575  -68.448  1.00 71.14  ? 618  LYS   C CA  1 
ATOM   9349  C  C   . LYS   C  1 317 ? 56.025  30.827  -67.575  1.00 74.30  ? 618  LYS   C C   1 
ATOM   9350  O  O   . LYS   C  1 317 ? 57.012  31.571  -67.595  1.00 75.15  ? 618  LYS   C O   1 
ATOM   9351  C  CB  . LYS   C  1 317 ? 55.417  29.899  -69.827  1.00 70.42  ? 618  LYS   C CB  1 
ATOM   9352  C  CG  . LYS   C  1 317 ? 55.822  28.939  -70.948  1.00 76.86  ? 618  LYS   C CG  1 
ATOM   9353  C  CD  . LYS   C  1 317 ? 57.224  29.246  -71.451  1.00 84.42  ? 618  LYS   C CD  1 
ATOM   9354  C  CE  . LYS   C  1 317 ? 57.638  28.287  -72.550  1.00 91.37  ? 618  LYS   C CE  1 
ATOM   9355  N  NZ  . LYS   C  1 317 ? 57.608  26.878  -72.079  1.00 93.64  ? 618  LYS   C NZ  1 
ATOM   9356  N  N   . MET   C  1 318 ? 54.972  31.074  -66.792  1.00 71.90  ? 619  MET   C N   1 
ATOM   9357  C  CA  . MET   C  1 318 ? 54.926  32.267  -65.958  1.00 68.09  ? 619  MET   C CA  1 
ATOM   9358  C  C   . MET   C  1 318 ? 55.655  32.102  -64.631  1.00 69.01  ? 619  MET   C C   1 
ATOM   9359  O  O   . MET   C  1 318 ? 55.797  33.094  -63.911  1.00 63.15  ? 619  MET   C O   1 
ATOM   9360  C  CB  . MET   C  1 318 ? 53.480  32.678  -65.677  1.00 65.35  ? 619  MET   C CB  1 
ATOM   9361  C  CG  . MET   C  1 318 ? 52.756  33.264  -66.872  1.00 59.99  ? 619  MET   C CG  1 
ATOM   9362  S  SD  . MET   C  1 318 ? 51.051  33.736  -66.504  1.00 62.12  ? 619  MET   C SD  1 
ATOM   9363  C  CE  . MET   C  1 318 ? 51.290  34.935  -65.198  1.00 67.84  ? 619  MET   C CE  1 
ATOM   9364  N  N   . ASN   C  1 319 ? 56.097  30.888  -64.291  1.00 73.82  ? 620  ASN   C N   1 
ATOM   9365  C  CA  . ASN   C  1 319 ? 56.808  30.602  -63.042  1.00 77.50  ? 620  ASN   C CA  1 
ATOM   9366  C  C   . ASN   C  1 319 ? 55.930  30.870  -61.816  1.00 75.46  ? 620  ASN   C C   1 
ATOM   9367  O  O   . ASN   C  1 319 ? 56.247  31.697  -60.955  1.00 74.75  ? 620  ASN   C O   1 
ATOM   9368  C  CB  . ASN   C  1 319 ? 58.119  31.397  -62.962  1.00 80.79  ? 620  ASN   C CB  1 
ATOM   9369  C  CG  . ASN   C  1 319 ? 59.115  30.964  -64.010  1.00 91.45  ? 620  ASN   C CG  1 
ATOM   9370  O  OD1 . ASN   C  1 319 ? 59.725  29.906  -63.879  1.00 103.25 ? 620  ASN   C OD1 1 
ATOM   9371  N  ND2 . ASN   C  1 319 ? 59.291  31.777  -65.055  1.00 85.99  ? 620  ASN   C ND2 1 
ATOM   9372  N  N   . LEU   C  1 320 ? 54.822  30.138  -61.744  1.00 72.03  ? 621  LEU   C N   1 
ATOM   9373  C  CA  . LEU   C  1 320 ? 53.848  30.285  -60.675  1.00 66.15  ? 621  LEU   C CA  1 
ATOM   9374  C  C   . LEU   C  1 320 ? 53.887  29.060  -59.775  1.00 75.19  ? 621  LEU   C C   1 
ATOM   9375  O  O   . LEU   C  1 320 ? 54.178  27.952  -60.230  1.00 75.27  ? 621  LEU   C O   1 
ATOM   9376  C  CB  . LEU   C  1 320 ? 52.434  30.466  -61.232  1.00 57.75  ? 621  LEU   C CB  1 
ATOM   9377  C  CG  . LEU   C  1 320 ? 52.195  31.587  -62.244  1.00 57.41  ? 621  LEU   C CG  1 
ATOM   9378  C  CD1 . LEU   C  1 320 ? 50.776  31.511  -62.789  1.00 50.33  ? 621  LEU   C CD1 1 
ATOM   9379  C  CD2 . LEU   C  1 320 ? 52.465  32.950  -61.621  1.00 49.19  ? 621  LEU   C CD2 1 
ATOM   9380  N  N   . ASP   C  1 321 ? 53.595  29.271  -58.491  1.00 81.15  ? 622  ASP   C N   1 
ATOM   9381  C  CA  . ASP   C  1 321 ? 53.515  28.165  -57.540  1.00 85.48  ? 622  ASP   C CA  1 
ATOM   9382  C  C   . ASP   C  1 321 ? 52.271  27.357  -57.862  1.00 74.53  ? 622  ASP   C C   1 
ATOM   9383  O  O   . ASP   C  1 321 ? 51.164  27.716  -57.460  1.00 79.73  ? 622  ASP   C O   1 
ATOM   9384  C  CB  . ASP   C  1 321 ? 53.470  28.671  -56.103  1.00 93.83  ? 622  ASP   C CB  1 
ATOM   9385  C  CG  . ASP   C  1 321 ? 53.324  27.540  -55.096  1.00 103.69 ? 622  ASP   C CG  1 
ATOM   9386  O  OD1 . ASP   C  1 321 ? 53.822  26.424  -55.378  1.00 103.33 ? 622  ASP   C OD1 1 
ATOM   9387  O  OD2 . ASP   C  1 321 ? 52.694  27.759  -54.037  1.00 108.33 ? 622  ASP   C OD2 1 
ATOM   9388  N  N   . MET   C  1 322 ? 52.442  26.263  -58.591  1.00 69.95  ? 623  MET   C N   1 
ATOM   9389  C  CA  . MET   C  1 322 ? 51.318  25.415  -58.947  1.00 67.60  ? 623  MET   C CA  1 
ATOM   9390  C  C   . MET   C  1 322 ? 51.102  24.281  -57.955  1.00 73.72  ? 623  MET   C C   1 
ATOM   9391  O  O   . MET   C  1 322 ? 50.373  23.336  -58.270  1.00 78.26  ? 623  MET   C O   1 
ATOM   9392  C  CB  . MET   C  1 322 ? 51.511  24.860  -60.353  1.00 56.64  ? 623  MET   C CB  1 
ATOM   9393  C  CG  . MET   C  1 322 ? 51.675  25.951  -61.389  1.00 67.38  ? 623  MET   C CG  1 
ATOM   9394  S  SD  . MET   C  1 322 ? 52.149  25.318  -63.010  1.00 77.28  ? 623  MET   C SD  1 
ATOM   9395  C  CE  . MET   C  1 322 ? 50.737  24.288  -63.405  1.00 73.72  ? 623  MET   C CE  1 
ATOM   9396  N  N   . ARG   C  1 323 ? 51.704  24.361  -56.765  1.00 76.90  ? 624  ARG   C N   1 
ATOM   9397  C  CA  . ARG   C  1 323 ? 51.555  23.297  -55.775  1.00 77.79  ? 624  ARG   C CA  1 
ATOM   9398  C  C   . ARG   C  1 323 ? 50.106  23.162  -55.337  1.00 71.80  ? 624  ARG   C C   1 
ATOM   9399  O  O   . ARG   C  1 323 ? 49.518  22.082  -55.423  1.00 73.61  ? 624  ARG   C O   1 
ATOM   9400  C  CB  . ARG   C  1 323 ? 52.445  23.566  -54.562  1.00 84.35  ? 624  ARG   C CB  1 
ATOM   9401  C  CG  . ARG   C  1 323 ? 53.531  22.525  -54.334  1.00 99.33  ? 624  ARG   C CG  1 
ATOM   9402  C  CD  . ARG   C  1 323 ? 53.823  22.261  -52.838  1.00 108.20 ? 624  ARG   C CD  1 
ATOM   9403  N  NE  . ARG   C  1 323 ? 53.373  23.321  -51.932  1.00 113.91 ? 624  ARG   C NE  1 
ATOM   9404  C  CZ  . ARG   C  1 323 ? 54.015  24.469  -51.731  1.00 119.74 ? 624  ARG   C CZ  1 
ATOM   9405  N  NH1 . ARG   C  1 323 ? 55.135  24.734  -52.387  1.00 124.17 ? 624  ARG   C NH1 1 
ATOM   9406  N  NH2 . ARG   C  1 323 ? 53.526  25.364  -50.885  1.00 119.79 ? 624  ARG   C NH2 1 
ATOM   9407  N  N   . LYS   C  1 324 ? 49.517  24.255  -54.862  1.00 71.59  ? 625  LYS   C N   1 
ATOM   9408  C  CA  . LYS   C  1 324 ? 48.171  24.264  -54.304  1.00 78.46  ? 625  LYS   C CA  1 
ATOM   9409  C  C   . LYS   C  1 324 ? 47.291  25.252  -55.065  1.00 75.60  ? 625  LYS   C C   1 
ATOM   9410  O  O   . LYS   C  1 324 ? 47.771  26.097  -55.823  1.00 81.12  ? 625  LYS   C O   1 
ATOM   9411  C  CB  . LYS   C  1 324 ? 48.211  24.617  -52.813  1.00 79.82  ? 625  LYS   C CB  1 
ATOM   9412  C  CG  . LYS   C  1 324 ? 48.962  25.904  -52.549  1.00 86.19  ? 625  LYS   C CG  1 
ATOM   9413  C  CD  . LYS   C  1 324 ? 49.767  25.846  -51.264  1.00 95.34  ? 625  LYS   C CD  1 
ATOM   9414  C  CE  . LYS   C  1 324 ? 50.755  27.001  -51.209  1.00 97.52  ? 625  LYS   C CE  1 
ATOM   9415  N  NZ  . LYS   C  1 324 ? 50.087  28.307  -51.487  1.00 93.42  ? 625  LYS   C NZ  1 
ATOM   9416  N  N   . THR   C  1 325 ? 45.979  25.153  -54.850  1.00 64.56  ? 626  THR   C N   1 
ATOM   9417  C  CA  . THR   C  1 325 ? 45.077  26.072  -55.535  1.00 63.09  ? 626  THR   C CA  1 
ATOM   9418  C  C   . THR   C  1 325 ? 45.149  27.487  -54.963  1.00 57.16  ? 626  THR   C C   1 
ATOM   9419  O  O   . THR   C  1 325 ? 45.031  28.459  -55.716  1.00 51.11  ? 626  THR   C O   1 
ATOM   9420  C  CB  . THR   C  1 325 ? 43.642  25.549  -55.471  1.00 62.88  ? 626  THR   C CB  1 
ATOM   9421  O  OG1 . THR   C  1 325 ? 43.174  25.616  -54.124  1.00 64.99  ? 626  THR   C OG1 1 
ATOM   9422  C  CG2 . THR   C  1 325 ? 43.581  24.111  -55.930  1.00 62.98  ? 626  THR   C CG2 1 
ATOM   9423  N  N   . SER   C  1 326 ? 45.348  27.625  -53.646  1.00 56.07  ? 627  SER   C N   1 
ATOM   9424  C  CA  . SER   C  1 326 ? 45.227  28.923  -52.984  1.00 51.41  ? 627  SER   C CA  1 
ATOM   9425  C  C   . SER   C  1 326 ? 46.235  29.958  -53.482  1.00 53.93  ? 627  SER   C C   1 
ATOM   9426  O  O   . SER   C  1 326 ? 46.030  31.148  -53.230  1.00 51.67  ? 627  SER   C O   1 
ATOM   9427  C  CB  . SER   C  1 326 ? 45.348  28.763  -51.455  1.00 47.94  ? 627  SER   C CB  1 
ATOM   9428  O  OG  . SER   C  1 326 ? 46.557  28.133  -51.088  1.00 60.17  ? 627  SER   C OG  1 
ATOM   9429  N  N   . SER   C  1 327 ? 47.304  29.554  -54.182  1.00 48.07  ? 628  SER   C N   1 
ATOM   9430  C  CA  . SER   C  1 327 ? 48.149  30.529  -54.864  1.00 46.83  ? 628  SER   C CA  1 
ATOM   9431  C  C   . SER   C  1 327 ? 47.418  31.249  -55.983  1.00 44.94  ? 628  SER   C C   1 
ATOM   9432  O  O   . SER   C  1 327 ? 47.955  32.216  -56.525  1.00 52.65  ? 628  SER   C O   1 
ATOM   9433  C  CB  . SER   C  1 327 ? 49.383  29.862  -55.457  1.00 49.02  ? 628  SER   C CB  1 
ATOM   9434  O  OG  . SER   C  1 327 ? 49.007  29.068  -56.561  1.00 53.60  ? 628  SER   C OG  1 
ATOM   9435  N  N   . LEU   C  1 328 ? 46.221  30.796  -56.342  1.00 45.10  ? 629  LEU   C N   1 
ATOM   9436  C  CA  . LEU   C  1 328 ? 45.436  31.390  -57.415  1.00 51.83  ? 629  LEU   C CA  1 
ATOM   9437  C  C   . LEU   C  1 328 ? 46.192  31.384  -58.751  1.00 56.45  ? 629  LEU   C C   1 
ATOM   9438  O  O   . LEU   C  1 328 ? 46.021  32.280  -59.591  1.00 55.39  ? 629  LEU   C O   1 
ATOM   9439  C  CB  . LEU   C  1 328 ? 44.984  32.800  -57.027  1.00 44.69  ? 629  LEU   C CB  1 
ATOM   9440  C  CG  . LEU   C  1 328 ? 44.056  32.862  -55.807  1.00 41.21  ? 629  LEU   C CG  1 
ATOM   9441  C  CD1 . LEU   C  1 328 ? 43.225  34.110  -55.870  1.00 39.80  ? 629  LEU   C CD1 1 
ATOM   9442  C  CD2 . LEU   C  1 328 ? 43.143  31.655  -55.709  1.00 39.73  ? 629  LEU   C CD2 1 
ATOM   9443  N  N   . TRP   C  1 329 ? 47.022  30.357  -58.965  1.00 52.63  ? 630  TRP   C N   1 
ATOM   9444  C  CA  . TRP   C  1 329 ? 47.847  30.310  -60.169  1.00 47.86  ? 630  TRP   C CA  1 
ATOM   9445  C  C   . TRP   C  1 329 ? 46.992  30.196  -61.435  1.00 50.47  ? 630  TRP   C C   1 
ATOM   9446  O  O   . TRP   C  1 329 ? 47.284  30.847  -62.449  1.00 50.12  ? 630  TRP   C O   1 
ATOM   9447  C  CB  . TRP   C  1 329 ? 48.866  29.167  -60.068  1.00 47.34  ? 630  TRP   C CB  1 
ATOM   9448  C  CG  . TRP   C  1 329 ? 48.283  27.783  -60.012  1.00 51.16  ? 630  TRP   C CG  1 
ATOM   9449  C  CD1 . TRP   C  1 329 ? 47.984  27.060  -58.893  1.00 58.68  ? 630  TRP   C CD1 1 
ATOM   9450  C  CD2 . TRP   C  1 329 ? 47.947  26.949  -61.127  1.00 56.62  ? 630  TRP   C CD2 1 
ATOM   9451  N  NE1 . TRP   C  1 329 ? 47.474  25.831  -59.242  1.00 56.62  ? 630  TRP   C NE1 1 
ATOM   9452  C  CE2 . TRP   C  1 329 ? 47.442  25.739  -60.608  1.00 58.15  ? 630  TRP   C CE2 1 
ATOM   9453  C  CE3 . TRP   C  1 329 ? 48.030  27.105  -62.515  1.00 56.24  ? 630  TRP   C CE3 1 
ATOM   9454  C  CZ2 . TRP   C  1 329 ? 47.018  24.697  -61.429  1.00 55.09  ? 630  TRP   C CZ2 1 
ATOM   9455  C  CZ3 . TRP   C  1 329 ? 47.602  26.073  -63.327  1.00 52.69  ? 630  TRP   C CZ3 1 
ATOM   9456  C  CH2 . TRP   C  1 329 ? 47.103  24.884  -62.781  1.00 48.77  ? 630  TRP   C CH2 1 
ATOM   9457  N  N   . LYS   C  1 330 ? 45.916  29.399  -61.392  1.00 47.16  ? 631  LYS   C N   1 
ATOM   9458  C  CA  . LYS   C  1 330 ? 44.996  29.355  -62.524  1.00 39.88  ? 631  LYS   C CA  1 
ATOM   9459  C  C   . LYS   C  1 330 ? 44.404  30.727  -62.817  1.00 48.61  ? 631  LYS   C C   1 
ATOM   9460  O  O   . LYS   C  1 330 ? 44.325  31.139  -63.983  1.00 40.42  ? 631  LYS   C O   1 
ATOM   9461  C  CB  . LYS   C  1 330 ? 43.876  28.349  -62.277  1.00 42.66  ? 631  LYS   C CB  1 
ATOM   9462  C  CG  . LYS   C  1 330 ? 44.333  26.900  -62.282  1.00 52.44  ? 631  LYS   C CG  1 
ATOM   9463  C  CD  . LYS   C  1 330 ? 43.165  25.950  -62.127  1.00 48.89  ? 631  LYS   C CD  1 
ATOM   9464  C  CE  . LYS   C  1 330 ? 43.587  24.534  -62.412  1.00 45.82  ? 631  LYS   C CE  1 
ATOM   9465  N  NZ  . LYS   C  1 330 ? 42.468  23.611  -62.127  1.00 58.12  ? 631  LYS   C NZ  1 
ATOM   9466  N  N   . ASP   C  1 331 ? 43.975  31.449  -61.774  1.00 44.73  ? 632  ASP   C N   1 
ATOM   9467  C  CA  . ASP   C  1 331 ? 43.346  32.750  -61.986  1.00 43.81  ? 632  ASP   C CA  1 
ATOM   9468  C  C   . ASP   C  1 331 ? 44.309  33.721  -62.656  1.00 40.47  ? 632  ASP   C C   1 
ATOM   9469  O  O   . ASP   C  1 331 ? 43.917  34.496  -63.543  1.00 42.04  ? 632  ASP   C O   1 
ATOM   9470  C  CB  . ASP   C  1 331 ? 42.853  33.323  -60.653  1.00 36.44  ? 632  ASP   C CB  1 
ATOM   9471  C  CG  . ASP   C  1 331 ? 42.026  32.326  -59.861  1.00 37.41  ? 632  ASP   C CG  1 
ATOM   9472  O  OD1 . ASP   C  1 331 ? 42.635  31.419  -59.269  1.00 43.40  ? 632  ASP   C OD1 1 
ATOM   9473  O  OD2 . ASP   C  1 331 ? 40.781  32.429  -59.833  1.00 35.26  ? 632  ASP   C OD2 1 
ATOM   9474  N  N   . GLN   C  1 332 ? 45.571  33.675  -62.244  1.00 43.11  ? 633  GLN   C N   1 
ATOM   9475  C  CA  . GLN   C  1 332 ? 46.576  34.611  -62.720  1.00 50.55  ? 633  GLN   C CA  1 
ATOM   9476  C  C   . GLN   C  1 332 ? 46.874  34.388  -64.195  1.00 51.68  ? 633  GLN   C C   1 
ATOM   9477  O  O   . GLN   C  1 332 ? 46.864  35.335  -64.990  1.00 39.33  ? 633  GLN   C O   1 
ATOM   9478  C  CB  . GLN   C  1 332 ? 47.841  34.451  -61.884  1.00 60.93  ? 633  GLN   C CB  1 
ATOM   9479  C  CG  . GLN   C  1 332 ? 48.647  35.705  -61.742  1.00 70.34  ? 633  GLN   C CG  1 
ATOM   9480  C  CD  . GLN   C  1 332 ? 49.453  35.702  -60.468  1.00 75.35  ? 633  GLN   C CD  1 
ATOM   9481  O  OE1 . GLN   C  1 332 ? 49.842  34.645  -59.964  1.00 71.19  ? 633  GLN   C OE1 1 
ATOM   9482  N  NE2 . GLN   C  1 332 ? 49.695  36.885  -59.924  1.00 82.88  ? 633  GLN   C NE2 1 
ATOM   9483  N  N   . ALA   C  1 333 ? 47.159  33.136  -64.566  1.00 42.76  ? 634  ALA   C N   1 
ATOM   9484  C  CA  . ALA   C  1 333 ? 47.397  32.815  -65.964  1.00 49.54  ? 634  ALA   C CA  1 
ATOM   9485  C  C   . ALA   C  1 333 ? 46.159  33.105  -66.788  1.00 48.96  ? 634  ALA   C C   1 
ATOM   9486  O  O   . ALA   C  1 333 ? 46.257  33.642  -67.897  1.00 51.04  ? 634  ALA   C O   1 
ATOM   9487  C  CB  . ALA   C  1 333 ? 47.817  31.352  -66.113  1.00 40.89  ? 634  ALA   C CB  1 
ATOM   9488  N  N   . LEU   C  1 334 ? 44.978  32.792  -66.238  1.00 47.37  ? 635  LEU   C N   1 
ATOM   9489  C  CA  . LEU   C  1 334 ? 43.737  33.031  -66.966  1.00 53.55  ? 635  LEU   C CA  1 
ATOM   9490  C  C   . LEU   C  1 334 ? 43.613  34.495  -67.380  1.00 56.25  ? 635  LEU   C C   1 
ATOM   9491  O  O   . LEU   C  1 334 ? 43.128  34.803  -68.477  1.00 55.45  ? 635  LEU   C O   1 
ATOM   9492  C  CB  . LEU   C  1 334 ? 42.535  32.608  -66.122  1.00 42.11  ? 635  LEU   C CB  1 
ATOM   9493  C  CG  . LEU   C  1 334 ? 41.196  32.977  -66.775  1.00 43.37  ? 635  LEU   C CG  1 
ATOM   9494  C  CD1 . LEU   C  1 334 ? 40.957  32.150  -68.022  1.00 43.53  ? 635  LEU   C CD1 1 
ATOM   9495  C  CD2 . LEU   C  1 334 ? 40.034  32.862  -65.826  1.00 39.85  ? 635  LEU   C CD2 1 
ATOM   9496  N  N   . VAL   C  1 335 ? 44.074  35.408  -66.525  1.00 52.57  ? 636  VAL   C N   1 
ATOM   9497  C  CA  . VAL   C  1 335 ? 43.999  36.827  -66.844  1.00 44.86  ? 636  VAL   C CA  1 
ATOM   9498  C  C   . VAL   C  1 335 ? 44.952  37.176  -67.987  1.00 43.44  ? 636  VAL   C C   1 
ATOM   9499  O  O   . VAL   C  1 335 ? 44.597  37.936  -68.898  1.00 44.80  ? 636  VAL   C O   1 
ATOM   9500  C  CB  . VAL   C  1 335 ? 44.277  37.665  -65.587  1.00 48.96  ? 636  VAL   C CB  1 
ATOM   9501  C  CG1 . VAL   C  1 335 ? 44.433  39.123  -65.950  1.00 44.56  ? 636  VAL   C CG1 1 
ATOM   9502  C  CG2 . VAL   C  1 335 ? 43.148  37.485  -64.583  1.00 54.96  ? 636  VAL   C CG2 1 
ATOM   9503  N  N   . GLU   C  1 336 ? 46.164  36.616  -67.970  1.00 41.57  ? 637  GLU   C N   1 
ATOM   9504  C  CA  . GLU   C  1 336 ? 47.133  36.928  -69.013  1.00 45.52  ? 637  GLU   C CA  1 
ATOM   9505  C  C   . GLU   C  1 336 ? 46.696  36.373  -70.366  1.00 50.14  ? 637  GLU   C C   1 
ATOM   9506  O  O   . GLU   C  1 336 ? 46.894  37.020  -71.402  1.00 51.70  ? 637  GLU   C O   1 
ATOM   9507  C  CB  . GLU   C  1 336 ? 48.504  36.389  -68.631  1.00 44.39  ? 637  GLU   C CB  1 
ATOM   9508  C  CG  . GLU   C  1 336 ? 49.025  36.913  -67.304  1.00 57.25  ? 637  GLU   C CG  1 
ATOM   9509  C  CD  . GLU   C  1 336 ? 49.451  38.385  -67.326  1.00 63.39  ? 637  GLU   C CD  1 
ATOM   9510  O  OE1 . GLU   C  1 336 ? 49.325  39.073  -68.362  1.00 60.88  ? 637  GLU   C OE1 1 
ATOM   9511  O  OE2 . GLU   C  1 336 ? 49.929  38.856  -66.279  1.00 66.19  ? 637  GLU   C OE2 1 
ATOM   9512  N  N   . ILE   C  1 337 ? 46.099  35.179  -70.379  1.00 48.22  ? 638  ILE   C N   1 
ATOM   9513  C  CA  . ILE   C  1 337 ? 45.617  34.611  -71.633  1.00 48.19  ? 638  ILE   C CA  1 
ATOM   9514  C  C   . ILE   C  1 337 ? 44.584  35.535  -72.270  1.00 51.41  ? 638  ILE   C C   1 
ATOM   9515  O  O   . ILE   C  1 337 ? 44.613  35.786  -73.482  1.00 50.39  ? 638  ILE   C O   1 
ATOM   9516  C  CB  . ILE   C  1 337 ? 45.060  33.195  -71.396  1.00 45.80  ? 638  ILE   C CB  1 
ATOM   9517  C  CG1 . ILE   C  1 337 ? 46.201  32.258  -70.994  1.00 47.15  ? 638  ILE   C CG1 1 
ATOM   9518  C  CG2 . ILE   C  1 337 ? 44.359  32.667  -72.648  1.00 42.30  ? 638  ILE   C CG2 1 
ATOM   9519  C  CD1 . ILE   C  1 337 ? 45.756  31.073  -70.172  1.00 48.05  ? 638  ILE   C CD1 1 
ATOM   9520  N  N   . ASN   C  1 338 ? 43.675  36.082  -71.462  1.00 46.87  ? 639  ASN   C N   1 
ATOM   9521  C  CA  . ASN   C  1 338 ? 42.647  36.956  -72.012  1.00 49.54  ? 639  ASN   C CA  1 
ATOM   9522  C  C   . ASN   C  1 338 ? 43.202  38.326  -72.383  1.00 54.35  ? 639  ASN   C C   1 
ATOM   9523  O  O   . ASN   C  1 338 ? 42.646  38.988  -73.268  1.00 50.92  ? 639  ASN   C O   1 
ATOM   9524  C  CB  . ASN   C  1 338 ? 41.475  37.087  -71.034  1.00 46.37  ? 639  ASN   C CB  1 
ATOM   9525  C  CG  . ASN   C  1 338 ? 40.542  35.892  -71.097  1.00 44.20  ? 639  ASN   C CG  1 
ATOM   9526  O  OD1 . ASN   C  1 338 ? 39.484  35.934  -71.740  1.00 41.22  ? 639  ASN   C OD1 1 
ATOM   9527  N  ND2 . ASN   C  1 338 ? 40.951  34.797  -70.455  1.00 42.56  ? 639  ASN   C ND2 1 
ATOM   9528  N  N   . ILE   C  1 339 ? 44.278  38.775  -71.723  1.00 51.27  ? 640  ILE   C N   1 
ATOM   9529  C  CA  . ILE   C  1 339 ? 44.972  39.977  -72.184  1.00 48.13  ? 640  ILE   C CA  1 
ATOM   9530  C  C   . ILE   C  1 339 ? 45.585  39.730  -73.558  1.00 52.04  ? 640  ILE   C C   1 
ATOM   9531  O  O   . ILE   C  1 339 ? 45.480  40.561  -74.468  1.00 55.92  ? 640  ILE   C O   1 
ATOM   9532  C  CB  . ILE   C  1 339 ? 46.039  40.412  -71.166  1.00 40.28  ? 640  ILE   C CB  1 
ATOM   9533  C  CG1 . ILE   C  1 339 ? 45.385  41.011  -69.924  1.00 43.15  ? 640  ILE   C CG1 1 
ATOM   9534  C  CG2 . ILE   C  1 339 ? 46.979  41.446  -71.752  1.00 38.78  ? 640  ILE   C CG2 1 
ATOM   9535  C  CD1 . ILE   C  1 339 ? 46.376  41.293  -68.832  1.00 38.59  ? 640  ILE   C CD1 1 
ATOM   9536  N  N   . ALA   C  1 340 ? 46.232  38.575  -73.723  1.00 51.92  ? 641  ALA   C N   1 
ATOM   9537  C  CA  . ALA   C  1 340 ? 46.882  38.248  -74.987  1.00 50.62  ? 641  ALA   C CA  1 
ATOM   9538  C  C   . ALA   C  1 340 ? 45.870  38.193  -76.119  1.00 48.55  ? 641  ALA   C C   1 
ATOM   9539  O  O   . ALA   C  1 340 ? 46.078  38.783  -77.183  1.00 51.18  ? 641  ALA   C O   1 
ATOM   9540  C  CB  . ALA   C  1 340 ? 47.616  36.914  -74.863  1.00 45.98  ? 641  ALA   C CB  1 
ATOM   9541  N  N   . VAL   C  1 341 ? 44.762  37.491  -75.895  1.00 46.51  ? 642  VAL   C N   1 
ATOM   9542  C  CA  . VAL   C  1 341 ? 43.749  37.318  -76.930  1.00 43.79  ? 642  VAL   C CA  1 
ATOM   9543  C  C   . VAL   C  1 341 ? 43.228  38.672  -77.397  1.00 51.82  ? 642  VAL   C C   1 
ATOM   9544  O  O   . VAL   C  1 341 ? 43.213  38.967  -78.602  1.00 45.38  ? 642  VAL   C O   1 
ATOM   9545  C  CB  . VAL   C  1 341 ? 42.622  36.410  -76.411  1.00 35.29  ? 642  VAL   C CB  1 
ATOM   9546  C  CG1 . VAL   C  1 341 ? 41.362  36.636  -77.166  1.00 30.43  ? 642  VAL   C CG1 1 
ATOM   9547  C  CG2 . VAL   C  1 341 ? 43.057  34.937  -76.476  1.00 36.89  ? 642  VAL   C CG2 1 
ATOM   9548  N  N   . LEU   C  1 342 ? 42.826  39.529  -76.449  1.00 48.38  ? 643  LEU   C N   1 
ATOM   9549  C  CA  . LEU   C  1 342 ? 42.343  40.861  -76.813  1.00 47.38  ? 643  LEU   C CA  1 
ATOM   9550  C  C   . LEU   C  1 342 ? 43.407  41.648  -77.570  1.00 49.03  ? 643  LEU   C C   1 
ATOM   9551  O  O   . LEU   C  1 342 ? 43.128  42.242  -78.620  1.00 51.39  ? 643  LEU   C O   1 
ATOM   9552  C  CB  . LEU   C  1 342 ? 41.907  41.636  -75.569  1.00 38.60  ? 643  LEU   C CB  1 
ATOM   9553  C  CG  . LEU   C  1 342 ? 40.673  41.159  -74.814  1.00 45.50  ? 643  LEU   C CG  1 
ATOM   9554  C  CD1 . LEU   C  1 342 ? 40.630  41.801  -73.408  1.00 32.27  ? 643  LEU   C CD1 1 
ATOM   9555  C  CD2 . LEU   C  1 342 ? 39.420  41.465  -75.622  1.00 43.07  ? 643  LEU   C CD2 1 
ATOM   9556  N  N   . TYR   C  1 343 ? 44.629  41.685  -77.031  1.00 49.42  ? 644  TYR   C N   1 
ATOM   9557  C  CA  . TYR   C  1 343 ? 45.701  42.454  -77.656  1.00 51.45  ? 644  TYR   C CA  1 
ATOM   9558  C  C   . TYR   C  1 343 ? 46.023  41.941  -79.061  1.00 55.35  ? 644  TYR   C C   1 
ATOM   9559  O  O   . TYR   C  1 343 ? 46.362  42.731  -79.952  1.00 51.89  ? 644  TYR   C O   1 
ATOM   9560  C  CB  . TYR   C  1 343 ? 46.931  42.416  -76.753  1.00 40.47  ? 644  TYR   C CB  1 
ATOM   9561  C  CG  . TYR   C  1 343 ? 48.238  42.761  -77.413  1.00 44.75  ? 644  TYR   C CG  1 
ATOM   9562  C  CD1 . TYR   C  1 343 ? 48.668  44.076  -77.502  1.00 45.86  ? 644  TYR   C CD1 1 
ATOM   9563  C  CD2 . TYR   C  1 343 ? 49.063  41.764  -77.925  1.00 50.95  ? 644  TYR   C CD2 1 
ATOM   9564  C  CE1 . TYR   C  1 343 ? 49.864  44.389  -78.112  1.00 53.70  ? 644  TYR   C CE1 1 
ATOM   9565  C  CE2 . TYR   C  1 343 ? 50.256  42.068  -78.530  1.00 48.25  ? 644  TYR   C CE2 1 
ATOM   9566  C  CZ  . TYR   C  1 343 ? 50.656  43.383  -78.619  1.00 57.71  ? 644  TYR   C CZ  1 
ATOM   9567  O  OH  . TYR   C  1 343 ? 51.853  43.698  -79.224  1.00 67.91  ? 644  TYR   C OH  1 
ATOM   9568  N  N   . SER   C  1 344 ? 45.900  40.634  -79.286  1.00 55.61  ? 645  SER   C N   1 
ATOM   9569  C  CA  . SER   C  1 344 ? 46.229  40.074  -80.589  1.00 49.63  ? 645  SER   C CA  1 
ATOM   9570  C  C   . SER   C  1 344 ? 45.178  40.440  -81.630  1.00 49.01  ? 645  SER   C C   1 
ATOM   9571  O  O   . SER   C  1 344 ? 45.513  40.914  -82.723  1.00 54.61  ? 645  SER   C O   1 
ATOM   9572  C  CB  . SER   C  1 344 ? 46.383  38.561  -80.468  1.00 42.33  ? 645  SER   C CB  1 
ATOM   9573  O  OG  . SER   C  1 344 ? 47.589  38.256  -79.794  1.00 50.48  ? 645  SER   C OG  1 
ATOM   9574  N  N   . PHE   C  1 345 ? 43.901  40.226  -81.308  1.00 46.03  ? 646  PHE   C N   1 
ATOM   9575  C  CA  . PHE   C  1 345 ? 42.824  40.627  -82.208  1.00 48.22  ? 646  PHE   C CA  1 
ATOM   9576  C  C   . PHE   C  1 345 ? 42.888  42.118  -82.523  1.00 55.88  ? 646  PHE   C C   1 
ATOM   9577  O  O   . PHE   C  1 345 ? 42.737  42.519  -83.679  1.00 55.84  ? 646  PHE   C O   1 
ATOM   9578  C  CB  . PHE   C  1 345 ? 41.463  40.264  -81.601  1.00 38.62  ? 646  PHE   C CB  1 
ATOM   9579  C  CG  . PHE   C  1 345 ? 41.011  38.859  -81.900  1.00 35.02  ? 646  PHE   C CG  1 
ATOM   9580  C  CD1 . PHE   C  1 345 ? 41.752  37.767  -81.477  1.00 36.68  ? 646  PHE   C CD1 1 
ATOM   9581  C  CD2 . PHE   C  1 345 ? 39.843  38.631  -82.615  1.00 31.08  ? 646  PHE   C CD2 1 
ATOM   9582  C  CE1 . PHE   C  1 345 ? 41.335  36.465  -81.757  1.00 33.14  ? 646  PHE   C CE1 1 
ATOM   9583  C  CE2 . PHE   C  1 345 ? 39.420  37.345  -82.894  1.00 34.52  ? 646  PHE   C CE2 1 
ATOM   9584  C  CZ  . PHE   C  1 345 ? 40.162  36.260  -82.457  1.00 38.26  ? 646  PHE   C CZ  1 
ATOM   9585  N  N   . GLN   C  1 346 ? 43.115  42.957  -81.511  1.00 57.39  ? 647  GLN   C N   1 
ATOM   9586  C  CA  . GLN   C  1 346 ? 43.143  44.395  -81.763  1.00 52.94  ? 647  GLN   C CA  1 
ATOM   9587  C  C   . GLN   C  1 346 ? 44.341  44.802  -82.608  1.00 53.34  ? 647  GLN   C C   1 
ATOM   9588  O  O   . GLN   C  1 346 ? 44.247  45.753  -83.394  1.00 50.56  ? 647  GLN   C O   1 
ATOM   9589  C  CB  . GLN   C  1 346 ? 43.137  45.160  -80.445  1.00 51.48  ? 647  GLN   C CB  1 
ATOM   9590  C  CG  . GLN   C  1 346 ? 41.775  45.156  -79.779  1.00 52.51  ? 647  GLN   C CG  1 
ATOM   9591  C  CD  . GLN   C  1 346 ? 41.823  45.539  -78.315  1.00 49.95  ? 647  GLN   C CD  1 
ATOM   9592  O  OE1 . GLN   C  1 346 ? 42.879  45.895  -77.778  1.00 50.46  ? 647  GLN   C OE1 1 
ATOM   9593  N  NE2 . GLN   C  1 346 ? 40.673  45.460  -77.657  1.00 43.89  ? 647  GLN   C NE2 1 
ATOM   9594  N  N   . SER   C  1 347 ? 45.465  44.097  -82.471  1.00 52.86  ? 648  SER   C N   1 
ATOM   9595  C  CA  . SER   C  1 347 ? 46.645  44.430  -83.257  1.00 50.39  ? 648  SER   C CA  1 
ATOM   9596  C  C   . SER   C  1 347 ? 46.433  44.134  -84.734  1.00 56.17  ? 648  SER   C C   1 
ATOM   9597  O  O   . SER   C  1 347 ? 46.999  44.822  -85.592  1.00 61.50  ? 648  SER   C O   1 
ATOM   9598  C  CB  . SER   C  1 347 ? 47.856  43.660  -82.733  1.00 53.73  ? 648  SER   C CB  1 
ATOM   9599  O  OG  . SER   C  1 347 ? 48.196  44.072  -81.412  1.00 61.38  ? 648  SER   C OG  1 
ATOM   9600  N  N   . ASP   C  1 348 ? 45.645  43.107  -85.043  1.00 48.66  ? 649  ASP   C N   1 
ATOM   9601  C  CA  . ASP   C  1 348 ? 45.358  42.701  -86.407  1.00 38.57  ? 649  ASP   C CA  1 
ATOM   9602  C  C   . ASP   C  1 348 ? 44.068  43.322  -86.930  1.00 44.45  ? 649  ASP   C C   1 
ATOM   9603  O  O   . ASP   C  1 348 ? 43.529  42.855  -87.938  1.00 45.17  ? 649  ASP   C O   1 
ATOM   9604  C  CB  . ASP   C  1 348 ? 45.283  41.180  -86.490  1.00 38.16  ? 649  ASP   C CB  1 
ATOM   9605  C  CG  . ASP   C  1 348 ? 46.622  40.524  -86.283  1.00 49.18  ? 649  ASP   C CG  1 
ATOM   9606  O  OD1 . ASP   C  1 348 ? 47.639  41.247  -86.263  1.00 48.82  ? 649  ASP   C OD1 1 
ATOM   9607  O  OD2 . ASP   C  1 348 ? 46.662  39.285  -86.141  1.00 53.51  ? 649  ASP   C OD2 1 
ATOM   9608  N  N   . LYS   C  1 349 ? 43.563  44.354  -86.247  1.00 46.50  ? 650  LYS   C N   1 
ATOM   9609  C  CA  . LYS   C  1 349 ? 42.334  45.055  -86.613  1.00 51.34  ? 650  LYS   C CA  1 
ATOM   9610  C  C   . LYS   C  1 349 ? 41.206  44.080  -86.945  1.00 55.91  ? 650  LYS   C C   1 
ATOM   9611  O  O   . LYS   C  1 349 ? 40.497  44.225  -87.941  1.00 55.06  ? 650  LYS   C O   1 
ATOM   9612  C  CB  . LYS   C  1 349 ? 42.575  46.022  -87.773  1.00 53.20  ? 650  LYS   C CB  1 
ATOM   9613  C  CG  . LYS   C  1 349 ? 43.564  47.134  -87.488  1.00 66.83  ? 650  LYS   C CG  1 
ATOM   9614  C  CD  . LYS   C  1 349 ? 44.972  46.775  -87.959  1.00 80.62  ? 650  LYS   C CD  1 
ATOM   9615  C  CE  . LYS   C  1 349 ? 45.228  47.228  -89.387  1.00 90.48  ? 650  LYS   C CE  1 
ATOM   9616  N  NZ  . LYS   C  1 349 ? 45.126  48.711  -89.515  1.00 94.07  ? 650  LYS   C NZ  1 
ATOM   9617  N  N   . VAL   C  1 350 ? 41.043  43.066  -86.099  1.00 49.48  ? 651  VAL   C N   1 
ATOM   9618  C  CA  . VAL   C  1 350 ? 39.903  42.159  -86.176  1.00 43.98  ? 651  VAL   C CA  1 
ATOM   9619  C  C   . VAL   C  1 350 ? 38.964  42.489  -85.022  1.00 48.70  ? 651  VAL   C C   1 
ATOM   9620  O  O   . VAL   C  1 350 ? 39.394  42.563  -83.861  1.00 46.10  ? 651  VAL   C O   1 
ATOM   9621  C  CB  . VAL   C  1 350 ? 40.341  40.685  -86.141  1.00 41.28  ? 651  VAL   C CB  1 
ATOM   9622  C  CG1 . VAL   C  1 350 ? 39.142  39.771  -86.269  1.00 35.97  ? 651  VAL   C CG1 1 
ATOM   9623  C  CG2 . VAL   C  1 350 ? 41.357  40.399  -87.234  1.00 34.78  ? 651  VAL   C CG2 1 
ATOM   9624  N  N   . THR   C  1 351 ? 37.688  42.708  -85.346  1.00 43.99  ? 652  THR   C N   1 
ATOM   9625  C  CA  . THR   C  1 351 ? 36.709  43.103  -84.344  1.00 42.43  ? 652  THR   C CA  1 
ATOM   9626  C  C   . THR   C  1 351 ? 36.701  42.124  -83.182  1.00 42.00  ? 652  THR   C C   1 
ATOM   9627  O  O   . THR   C  1 351 ? 36.688  40.905  -83.376  1.00 46.06  ? 652  THR   C O   1 
ATOM   9628  C  CB  . THR   C  1 351 ? 35.314  43.183  -84.960  1.00 40.50  ? 652  THR   C CB  1 
ATOM   9629  O  OG1 . THR   C  1 351 ? 35.371  43.925  -86.178  1.00 47.42  ? 652  THR   C OG1 1 
ATOM   9630  C  CG2 . THR   C  1 351 ? 34.350  43.885  -84.006  1.00 36.06  ? 652  THR   C CG2 1 
ATOM   9631  N  N   . ILE   C  1 352 ? 36.739  42.679  -81.972  1.00 39.63  ? 653  ILE   C N   1 
ATOM   9632  C  CA  . ILE   C  1 352 ? 36.588  41.913  -80.736  1.00 30.05  ? 653  ILE   C CA  1 
ATOM   9633  C  C   . ILE   C  1 352 ? 36.143  42.913  -79.681  1.00 41.93  ? 653  ILE   C C   1 
ATOM   9634  O  O   . ILE   C  1 352 ? 36.322  44.126  -79.839  1.00 37.35  ? 653  ILE   C O   1 
ATOM   9635  C  CB  . ILE   C  1 352 ? 37.900  41.180  -80.343  1.00 28.34  ? 653  ILE   C CB  1 
ATOM   9636  C  CG1 . ILE   C  1 352 ? 37.645  40.100  -79.291  1.00 39.94  ? 653  ILE   C CG1 1 
ATOM   9637  C  CG2 . ILE   C  1 352 ? 38.951  42.152  -79.834  1.00 29.62  ? 653  ILE   C CG2 1 
ATOM   9638  C  CD1 . ILE   C  1 352 ? 38.862  39.245  -78.990  1.00 34.80  ? 653  ILE   C CD1 1 
ATOM   9639  N  N   . VAL   C  1 353 ? 35.514  42.411  -78.616  1.00 44.91  ? 654  VAL   C N   1 
ATOM   9640  C  CA  . VAL   C  1 353 ? 35.006  43.256  -77.540  1.00 44.79  ? 654  VAL   C CA  1 
ATOM   9641  C  C   . VAL   C  1 353 ? 35.329  42.577  -76.215  1.00 38.26  ? 654  VAL   C C   1 
ATOM   9642  O  O   . VAL   C  1 353 ? 35.122  41.369  -76.073  1.00 43.39  ? 654  VAL   C O   1 
ATOM   9643  C  CB  . VAL   C  1 353 ? 33.492  43.532  -77.697  1.00 45.69  ? 654  VAL   C CB  1 
ATOM   9644  C  CG1 . VAL   C  1 353 ? 32.686  42.251  -77.697  1.00 39.65  ? 654  VAL   C CG1 1 
ATOM   9645  C  CG2 . VAL   C  1 353 ? 32.992  44.487  -76.630  1.00 50.10  ? 654  VAL   C CG2 1 
ATOM   9646  N  N   . ASP   C  1 354 ? 35.905  43.333  -75.272  1.00 34.54  ? 655  ASP   C N   1 
ATOM   9647  C  CA  . ASP   C  1 354 ? 36.199  42.757  -73.960  1.00 35.63  ? 655  ASP   C CA  1 
ATOM   9648  C  C   . ASP   C  1 354 ? 34.900  42.549  -73.174  1.00 43.21  ? 655  ASP   C C   1 
ATOM   9649  O  O   . ASP   C  1 354 ? 33.822  43.001  -73.572  1.00 44.79  ? 655  ASP   C O   1 
ATOM   9650  C  CB  . ASP   C  1 354 ? 37.188  43.637  -73.175  1.00 34.60  ? 655  ASP   C CB  1 
ATOM   9651  C  CG  . ASP   C  1 354 ? 36.616  45.003  -72.816  1.00 43.07  ? 655  ASP   C CG  1 
ATOM   9652  O  OD1 . ASP   C  1 354 ? 35.638  45.073  -72.042  1.00 44.33  ? 655  ASP   C OD1 1 
ATOM   9653  O  OD2 . ASP   C  1 354 ? 37.156  46.023  -73.296  1.00 51.48  ? 655  ASP   C OD2 1 
ATOM   9654  N  N   . HIS   C  1 355 ? 35.005  41.855  -72.033  1.00 38.65  ? 656  HIS   C N   1 
ATOM   9655  C  CA  . HIS   C  1 355 ? 33.798  41.558  -71.276  1.00 37.70  ? 656  HIS   C CA  1 
ATOM   9656  C  C   . HIS   C  1 355 ? 33.281  42.775  -70.504  1.00 44.33  ? 656  HIS   C C   1 
ATOM   9657  O  O   . HIS   C  1 355 ? 32.072  42.863  -70.256  1.00 42.74  ? 656  HIS   C O   1 
ATOM   9658  C  CB  . HIS   C  1 355 ? 34.045  40.374  -70.341  1.00 39.53  ? 656  HIS   C CB  1 
ATOM   9659  C  CG  . HIS   C  1 355 ? 35.331  40.460  -69.585  1.00 38.98  ? 656  HIS   C CG  1 
ATOM   9660  N  ND1 . HIS   C  1 355 ? 36.552  40.213  -70.173  1.00 39.19  ? 656  HIS   C ND1 1 
ATOM   9661  C  CD2 . HIS   C  1 355 ? 35.589  40.755  -68.287  1.00 37.83  ? 656  HIS   C CD2 1 
ATOM   9662  C  CE1 . HIS   C  1 355 ? 37.508  40.349  -69.269  1.00 43.67  ? 656  HIS   C CE1 1 
ATOM   9663  N  NE2 . HIS   C  1 355 ? 36.951  40.684  -68.119  1.00 37.81  ? 656  HIS   C NE2 1 
ATOM   9664  N  N   . HIS   C  1 356 ? 34.161  43.724  -70.138  1.00 38.52  ? 657  HIS   C N   1 
ATOM   9665  C  CA  . HIS   C  1 356 ? 33.719  44.967  -69.495  1.00 39.78  ? 657  HIS   C CA  1 
ATOM   9666  C  C   . HIS   C  1 356 ? 32.852  45.810  -70.429  1.00 40.59  ? 657  HIS   C C   1 
ATOM   9667  O  O   . HIS   C  1 356 ? 31.763  46.267  -70.055  1.00 35.69  ? 657  HIS   C O   1 
ATOM   9668  C  CB  . HIS   C  1 356 ? 34.934  45.780  -69.037  1.00 37.99  ? 657  HIS   C CB  1 
ATOM   9669  C  CG  . HIS   C  1 356 ? 35.889  45.001  -68.189  1.00 40.38  ? 657  HIS   C CG  1 
ATOM   9670  N  ND1 . HIS   C  1 356 ? 35.552  44.532  -66.933  1.00 34.03  ? 657  HIS   C ND1 1 
ATOM   9671  C  CD2 . HIS   C  1 356 ? 37.153  44.578  -68.426  1.00 35.97  ? 657  HIS   C CD2 1 
ATOM   9672  C  CE1 . HIS   C  1 356 ? 36.576  43.863  -66.434  1.00 39.07  ? 657  HIS   C CE1 1 
ATOM   9673  N  NE2 . HIS   C  1 356 ? 37.559  43.878  -67.317  1.00 38.82  ? 657  HIS   C NE2 1 
ATOM   9674  N  N   . SER   C  1 357 ? 33.336  46.043  -71.648  1.00 45.00  ? 658  SER   C N   1 
ATOM   9675  C  CA  A SER   C  1 357 ? 32.594  46.837  -72.624  0.49 40.89  ? 658  SER   C CA  1 
ATOM   9676  C  CA  B SER   C  1 357 ? 32.571  46.854  -72.583  0.51 40.84  ? 658  SER   C CA  1 
ATOM   9677  C  C   . SER   C  1 357 ? 31.297  46.142  -73.020  1.00 33.33  ? 658  SER   C C   1 
ATOM   9678  O  O   . SER   C  1 357 ? 30.243  46.778  -73.151  1.00 30.91  ? 658  SER   C O   1 
ATOM   9679  C  CB  A SER   C  1 357 ? 33.480  47.077  -73.852  0.49 44.16  ? 658  SER   C CB  1 
ATOM   9680  C  CB  B SER   C  1 357 ? 33.438  47.213  -73.786  0.51 44.33  ? 658  SER   C CB  1 
ATOM   9681  O  OG  A SER   C  1 357 ? 32.775  47.683  -74.923  0.49 44.19  ? 658  SER   C OG  1 
ATOM   9682  O  OG  B SER   C  1 357 ? 34.541  48.002  -73.374  0.51 47.78  ? 658  SER   C OG  1 
ATOM   9683  N  N   . ALA   C  1 358 ? 31.360  44.832  -73.220  1.00 31.90  ? 659  ALA   C N   1 
ATOM   9684  C  CA  . ALA   C  1 358 ? 30.192  44.115  -73.715  1.00 37.60  ? 659  ALA   C CA  1 
ATOM   9685  C  C   . ALA   C  1 358 ? 29.090  44.056  -72.667  1.00 42.00  ? 659  ALA   C C   1 
ATOM   9686  O  O   . ALA   C  1 358 ? 27.907  44.214  -72.999  1.00 35.34  ? 659  ALA   C O   1 
ATOM   9687  C  CB  . ALA   C  1 358 ? 30.593  42.708  -74.156  1.00 36.73  ? 659  ALA   C CB  1 
ATOM   9688  N  N   . THR   C  1 359 ? 29.456  43.827  -71.395  1.00 40.89  ? 660  THR   C N   1 
ATOM   9689  C  CA  . THR   C  1 359 ? 28.437  43.790  -70.351  1.00 34.67  ? 660  THR   C CA  1 
ATOM   9690  C  C   . THR   C  1 359 ? 27.850  45.171  -70.122  1.00 32.55  ? 660  THR   C C   1 
ATOM   9691  O  O   . THR   C  1 359 ? 26.637  45.307  -69.937  1.00 37.35  ? 660  THR   C O   1 
ATOM   9692  C  CB  . THR   C  1 359 ? 29.008  43.223  -69.050  1.00 31.66  ? 660  THR   C CB  1 
ATOM   9693  O  OG1 . THR   C  1 359 ? 30.201  43.938  -68.676  1.00 32.68  ? 660  THR   C OG1 1 
ATOM   9694  C  CG2 . THR   C  1 359 ? 29.295  41.763  -69.213  1.00 31.76  ? 660  THR   C CG2 1 
ATOM   9695  N  N   . GLU   C  1 360 ? 28.694  46.206  -70.144  1.00 32.54  ? 661  GLU   C N   1 
ATOM   9696  C  CA  . GLU   C  1 360 ? 28.196  47.572  -70.022  1.00 34.28  ? 661  GLU   C CA  1 
ATOM   9697  C  C   . GLU   C  1 360 ? 27.225  47.909  -71.149  1.00 41.69  ? 661  GLU   C C   1 
ATOM   9698  O  O   . GLU   C  1 360 ? 26.206  48.574  -70.922  1.00 43.29  ? 661  GLU   C O   1 
ATOM   9699  C  CB  . GLU   C  1 360 ? 29.369  48.549  -70.012  1.00 47.03  ? 661  GLU   C CB  1 
ATOM   9700  C  CG  . GLU   C  1 360 ? 28.962  50.005  -70.109  1.00 64.87  ? 661  GLU   C CG  1 
ATOM   9701  C  CD  . GLU   C  1 360 ? 30.135  50.930  -70.439  1.00 78.78  ? 661  GLU   C CD  1 
ATOM   9702  O  OE1 . GLU   C  1 360 ? 31.187  50.434  -70.904  1.00 78.46  ? 661  GLU   C OE1 1 
ATOM   9703  O  OE2 . GLU   C  1 360 ? 30.002  52.157  -70.230  1.00 82.27  ? 661  GLU   C OE2 1 
ATOM   9704  N  N   . SER   C  1 361 ? 27.531  47.467  -72.376  1.00 32.34  ? 662  SER   C N   1 
ATOM   9705  C  CA  . SER   C  1 361 ? 26.617  47.691  -73.495  1.00 39.33  ? 662  SER   C CA  1 
ATOM   9706  C  C   . SER   C  1 361 ? 25.279  47.019  -73.242  1.00 45.88  ? 662  SER   C C   1 
ATOM   9707  O  O   . SER   C  1 361 ? 24.225  47.567  -73.585  1.00 47.96  ? 662  SER   C O   1 
ATOM   9708  C  CB  . SER   C  1 361 ? 27.230  47.175  -74.800  1.00 48.63  ? 662  SER   C CB  1 
ATOM   9709  O  OG  . SER   C  1 361 ? 28.384  47.934  -75.146  1.00 59.82  ? 662  SER   C OG  1 
ATOM   9710  N  N   . PHE   C  1 362 ? 25.299  45.835  -72.622  1.00 39.67  ? 663  PHE   C N   1 
ATOM   9711  C  CA  . PHE   C  1 362 ? 24.053  45.111  -72.418  1.00 38.08  ? 663  PHE   C CA  1 
ATOM   9712  C  C   . PHE   C  1 362 ? 23.145  45.830  -71.418  1.00 45.28  ? 663  PHE   C C   1 
ATOM   9713  O  O   . PHE   C  1 362 ? 21.932  45.926  -71.641  1.00 45.43  ? 663  PHE   C O   1 
ATOM   9714  C  CB  . PHE   C  1 362 ? 24.333  43.664  -71.996  1.00 30.82  ? 663  PHE   C CB  1 
ATOM   9715  C  CG  . PHE   C  1 362 ? 23.089  42.839  -71.883  1.00 34.91  ? 663  PHE   C CG  1 
ATOM   9716  C  CD1 . PHE   C  1 362 ? 22.433  42.382  -73.024  1.00 37.77  ? 663  PHE   C CD1 1 
ATOM   9717  C  CD2 . PHE   C  1 362 ? 22.517  42.593  -70.644  1.00 39.28  ? 663  PHE   C CD2 1 
ATOM   9718  C  CE1 . PHE   C  1 362 ? 21.255  41.644  -72.930  1.00 32.32  ? 663  PHE   C CE1 1 
ATOM   9719  C  CE2 . PHE   C  1 362 ? 21.351  41.862  -70.539  1.00 38.15  ? 663  PHE   C CE2 1 
ATOM   9720  C  CZ  . PHE   C  1 362 ? 20.714  41.391  -71.681  1.00 40.72  ? 663  PHE   C CZ  1 
ATOM   9721  N  N   . ILE   C  1 363 ? 23.710  46.358  -70.322  1.00 48.16  ? 664  ILE   C N   1 
ATOM   9722  C  CA  . ILE   C  1 363 ? 22.926  47.172  -69.388  1.00 45.71  ? 664  ILE   C CA  1 
ATOM   9723  C  C   . ILE   C  1 363 ? 22.231  48.314  -70.132  1.00 47.20  ? 664  ILE   C C   1 
ATOM   9724  O  O   . ILE   C  1 363 ? 21.024  48.552  -69.973  1.00 43.73  ? 664  ILE   C O   1 
ATOM   9725  C  CB  . ILE   C  1 363 ? 23.821  47.713  -68.254  1.00 43.36  ? 664  ILE   C CB  1 
ATOM   9726  C  CG1 . ILE   C  1 363 ? 24.446  46.587  -67.408  1.00 40.45  ? 664  ILE   C CG1 1 
ATOM   9727  C  CG2 . ILE   C  1 363 ? 23.044  48.707  -67.410  1.00 29.37  ? 664  ILE   C CG2 1 
ATOM   9728  C  CD1 . ILE   C  1 363 ? 23.457  45.767  -66.553  1.00 40.94  ? 664  ILE   C CD1 1 
ATOM   9729  N  N   . LYS   C  1 364 ? 22.994  49.036  -70.961  1.00 44.20  ? 665  LYS   C N   1 
ATOM   9730  C  CA  . LYS   C  1 364 ? 22.416  50.088  -71.794  1.00 46.35  ? 665  LYS   C CA  1 
ATOM   9731  C  C   . LYS   C  1 364 ? 21.321  49.537  -72.713  1.00 46.05  ? 665  LYS   C C   1 
ATOM   9732  O  O   . LYS   C  1 364 ? 20.272  50.172  -72.888  1.00 46.43  ? 665  LYS   C O   1 
ATOM   9733  C  CB  . LYS   C  1 364 ? 23.530  50.764  -72.596  1.00 48.22  ? 665  LYS   C CB  1 
ATOM   9734  C  CG  . LYS   C  1 364 ? 23.102  51.901  -73.507  1.00 62.16  ? 665  LYS   C CG  1 
ATOM   9735  C  CD  . LYS   C  1 364 ? 24.019  51.947  -74.736  1.00 83.14  ? 665  LYS   C CD  1 
ATOM   9736  C  CE  . LYS   C  1 364 ? 23.806  53.186  -75.619  1.00 90.76  ? 665  LYS   C CE  1 
ATOM   9737  N  NZ  . LYS   C  1 364 ? 24.694  54.327  -75.229  1.00 90.62  ? 665  LYS   C NZ  1 
ATOM   9738  N  N   . HIS   C  1 365 ? 21.533  48.344  -73.286  1.00 39.47  ? 666  HIS   C N   1 
ATOM   9739  C  CA  . HIS   C  1 365 ? 20.503  47.744  -74.134  1.00 44.05  ? 666  HIS   C CA  1 
ATOM   9740  C  C   . HIS   C  1 365 ? 19.264  47.386  -73.313  1.00 52.31  ? 666  HIS   C C   1 
ATOM   9741  O  O   . HIS   C  1 365 ? 18.133  47.693  -73.722  1.00 45.43  ? 666  HIS   C O   1 
ATOM   9742  C  CB  . HIS   C  1 365 ? 21.071  46.519  -74.871  1.00 38.92  ? 666  HIS   C CB  1 
ATOM   9743  C  CG  . HIS   C  1 365 ? 20.046  45.706  -75.613  1.00 42.64  ? 666  HIS   C CG  1 
ATOM   9744  N  ND1 . HIS   C  1 365 ? 19.291  46.212  -76.652  1.00 43.49  ? 666  HIS   C ND1 1 
ATOM   9745  C  CD2 . HIS   C  1 365 ? 19.674  44.408  -75.482  1.00 40.88  ? 666  HIS   C CD2 1 
ATOM   9746  C  CE1 . HIS   C  1 365 ? 18.486  45.268  -77.113  1.00 32.01  ? 666  HIS   C CE1 1 
ATOM   9747  N  NE2 . HIS   C  1 365 ? 18.703  44.161  -76.425  1.00 35.70  ? 666  HIS   C NE2 1 
ATOM   9748  N  N   . MET   C  1 366 ? 19.463  46.755  -72.145  1.00 48.14  ? 667  MET   C N   1 
ATOM   9749  C  CA  . MET   C  1 366 ? 18.362  46.516  -71.213  1.00 39.92  ? 667  MET   C CA  1 
ATOM   9750  C  C   . MET   C  1 366 ? 17.546  47.784  -70.996  1.00 37.64  ? 667  MET   C C   1 
ATOM   9751  O  O   . MET   C  1 366 ? 16.316  47.780  -71.132  1.00 36.65  ? 667  MET   C O   1 
ATOM   9752  C  CB  . MET   C  1 366 ? 18.893  45.995  -69.864  1.00 41.13  ? 667  MET   C CB  1 
ATOM   9753  C  CG  . MET   C  1 366 ? 19.104  44.495  -69.769  1.00 43.92  ? 667  MET   C CG  1 
ATOM   9754  S  SD  . MET   C  1 366 ? 19.113  43.819  -68.064  1.00 50.15  ? 667  MET   C SD  1 
ATOM   9755  C  CE  . MET   C  1 366 ? 17.431  44.102  -67.532  1.00 45.04  ? 667  MET   C CE  1 
ATOM   9756  N  N   . GLU   C  1 367 ? 18.215  48.886  -70.647  1.00 39.48  ? 668  GLU   C N   1 
ATOM   9757  C  CA  . GLU   C  1 367 ? 17.477  50.114  -70.375  1.00 44.93  ? 668  GLU   C CA  1 
ATOM   9758  C  C   . GLU   C  1 367 ? 16.649  50.527  -71.585  1.00 51.11  ? 668  GLU   C C   1 
ATOM   9759  O  O   . GLU   C  1 367 ? 15.467  50.868  -71.453  1.00 48.53  ? 668  GLU   C O   1 
ATOM   9760  C  CB  . GLU   C  1 367 ? 18.432  51.226  -69.959  1.00 51.35  ? 668  GLU   C CB  1 
ATOM   9761  C  CG  . GLU   C  1 367 ? 18.672  51.264  -68.457  1.00 72.08  ? 668  GLU   C CG  1 
ATOM   9762  C  CD  . GLU   C  1 367 ? 20.033  51.809  -68.103  1.00 76.16  ? 668  GLU   C CD  1 
ATOM   9763  O  OE1 . GLU   C  1 367 ? 20.456  52.800  -68.736  1.00 81.69  ? 668  GLU   C OE1 1 
ATOM   9764  O  OE2 . GLU   C  1 367 ? 20.682  51.228  -67.207  1.00 69.70  ? 668  GLU   C OE2 1 
ATOM   9765  N  N   . ASN   C  1 368 ? 17.248  50.476  -72.779  1.00 50.25  ? 669  ASN   C N   1 
ATOM   9766  C  CA  . ASN   C  1 368 ? 16.521  50.843  -73.993  1.00 43.96  ? 669  ASN   C CA  1 
ATOM   9767  C  C   . ASN   C  1 368 ? 15.270  49.995  -74.158  1.00 44.10  ? 669  ASN   C C   1 
ATOM   9768  O  O   . ASN   C  1 368 ? 14.178  50.519  -74.401  1.00 46.78  ? 669  ASN   C O   1 
ATOM   9769  C  CB  . ASN   C  1 368 ? 17.417  50.679  -75.217  1.00 47.64  ? 669  ASN   C CB  1 
ATOM   9770  C  CG  . ASN   C  1 368 ? 18.541  51.670  -75.256  1.00 50.02  ? 669  ASN   C CG  1 
ATOM   9771  O  OD1 . ASN   C  1 368 ? 18.442  52.752  -74.676  1.00 49.40  ? 669  ASN   C OD1 1 
ATOM   9772  N  ND2 . ASN   C  1 368 ? 19.632  51.312  -75.957  1.00 47.06  ? 669  ASN   C ND2 1 
ATOM   9773  N  N   . GLU   C  1 369 ? 15.412  48.674  -74.018  1.00 39.30  ? 670  GLU   C N   1 
ATOM   9774  C  CA  . GLU   C  1 369 ? 14.287  47.774  -74.249  1.00 41.01  ? 670  GLU   C CA  1 
ATOM   9775  C  C   . GLU   C  1 369 ? 13.153  48.037  -73.260  1.00 48.66  ? 670  GLU   C C   1 
ATOM   9776  O  O   . GLU   C  1 369 ? 11.983  48.123  -73.654  1.00 43.58  ? 670  GLU   C O   1 
ATOM   9777  C  CB  . GLU   C  1 369 ? 14.762  46.316  -74.179  1.00 34.62  ? 670  GLU   C CB  1 
ATOM   9778  C  CG  . GLU   C  1 369 ? 15.708  45.916  -75.291  1.00 43.13  ? 670  GLU   C CG  1 
ATOM   9779  C  CD  . GLU   C  1 369 ? 14.989  45.701  -76.640  1.00 46.14  ? 670  GLU   C CD  1 
ATOM   9780  O  OE1 . GLU   C  1 369 ? 14.830  44.524  -77.057  1.00 40.77  ? 670  GLU   C OE1 1 
ATOM   9781  O  OE2 . GLU   C  1 369 ? 14.579  46.703  -77.265  1.00 40.86  ? 670  GLU   C OE2 1 
ATOM   9782  N  N   . TYR   C  1 370 ? 13.475  48.182  -71.966  1.00 48.71  ? 671  TYR   C N   1 
ATOM   9783  C  CA  . TYR   C  1 370 ? 12.422  48.449  -70.988  1.00 41.08  ? 671  TYR   C CA  1 
ATOM   9784  C  C   . TYR   C  1 370 ? 11.718  49.764  -71.300  1.00 42.46  ? 671  TYR   C C   1 
ATOM   9785  O  O   . TYR   C  1 370 ? 10.488  49.850  -71.223  1.00 56.07  ? 671  TYR   C O   1 
ATOM   9786  C  CB  . TYR   C  1 370 ? 12.992  48.430  -69.556  1.00 37.51  ? 671  TYR   C CB  1 
ATOM   9787  C  CG  . TYR   C  1 370 ? 12.998  47.021  -68.964  1.00 42.51  ? 671  TYR   C CG  1 
ATOM   9788  C  CD1 . TYR   C  1 370 ? 14.073  46.162  -69.163  1.00 42.51  ? 671  TYR   C CD1 1 
ATOM   9789  C  CD2 . TYR   C  1 370 ? 11.906  46.537  -68.254  1.00 48.89  ? 671  TYR   C CD2 1 
ATOM   9790  C  CE1 . TYR   C  1 370 ? 14.071  44.874  -68.653  1.00 39.26  ? 671  TYR   C CE1 1 
ATOM   9791  C  CE2 . TYR   C  1 370 ? 11.890  45.246  -67.743  1.00 39.47  ? 671  TYR   C CE2 1 
ATOM   9792  C  CZ  . TYR   C  1 370 ? 12.972  44.419  -67.946  1.00 38.80  ? 671  TYR   C CZ  1 
ATOM   9793  O  OH  . TYR   C  1 370 ? 12.958  43.137  -67.441  1.00 40.68  ? 671  TYR   C OH  1 
ATOM   9794  N  N   . ARG   C  1 371 ? 12.479  50.787  -71.703  1.00 43.96  ? 672  ARG   C N   1 
ATOM   9795  C  CA  . ARG   C  1 371 ? 11.897  52.091  -72.031  1.00 50.88  ? 672  ARG   C CA  1 
ATOM   9796  C  C   . ARG   C  1 371 ? 10.935  52.005  -73.223  1.00 56.35  ? 672  ARG   C C   1 
ATOM   9797  O  O   . ARG   C  1 371 ? 9.845   52.590  -73.201  1.00 59.60  ? 672  ARG   C O   1 
ATOM   9798  C  CB  . ARG   C  1 371 ? 13.023  53.087  -72.315  1.00 62.35  ? 672  ARG   C CB  1 
ATOM   9799  C  CG  . ARG   C  1 371 ? 12.583  54.460  -72.810  1.00 74.02  ? 672  ARG   C CG  1 
ATOM   9800  C  CD  . ARG   C  1 371 ? 13.709  55.167  -73.576  1.00 86.55  ? 672  ARG   C CD  1 
ATOM   9801  N  NE  . ARG   C  1 371 ? 15.042  54.687  -73.206  1.00 95.80  ? 672  ARG   C NE  1 
ATOM   9802  C  CZ  . ARG   C  1 371 ? 15.724  55.107  -72.142  1.00 107.39 ? 672  ARG   C CZ  1 
ATOM   9803  N  NH1 . ARG   C  1 371 ? 15.199  56.017  -71.328  1.00 111.91 ? 672  ARG   C NH1 1 
ATOM   9804  N  NH2 . ARG   C  1 371 ? 16.930  54.612  -71.882  1.00 109.52 ? 672  ARG   C NH2 1 
ATOM   9805  N  N   . CYS   C  1 372 ? 11.317  51.293  -74.281  1.00 51.07  ? 673  CYS   C N   1 
ATOM   9806  C  CA  . CYS   C  1 372 ? 10.493  51.306  -75.484  1.00 57.84  ? 673  CYS   C CA  1 
ATOM   9807  C  C   . CYS   C  1 372 ? 9.631   50.061  -75.660  1.00 54.01  ? 673  CYS   C C   1 
ATOM   9808  O  O   . CYS   C  1 372 ? 8.615   50.131  -76.356  1.00 61.53  ? 673  CYS   C O   1 
ATOM   9809  C  CB  . CYS   C  1 372 ? 11.372  51.489  -76.728  1.00 65.15  ? 673  CYS   C CB  1 
ATOM   9810  S  SG  . CYS   C  1 372 ? 12.209  49.986  -77.193  1.00 75.36  ? 673  CYS   C SG  1 
ATOM   9811  N  N   . ARG   C  1 373 ? 9.990   48.937  -75.050  1.00 52.45  ? 674  ARG   C N   1 
ATOM   9812  C  CA  . ARG   C  1 373 ? 9.296   47.677  -75.284  1.00 50.65  ? 674  ARG   C CA  1 
ATOM   9813  C  C   . ARG   C  1 373 ? 8.627   47.123  -74.033  1.00 55.51  ? 674  ARG   C C   1 
ATOM   9814  O  O   . ARG   C  1 373 ? 7.810   46.201  -74.141  1.00 47.97  ? 674  ARG   C O   1 
ATOM   9815  C  CB  . ARG   C  1 373 ? 10.287  46.639  -75.844  1.00 43.68  ? 674  ARG   C CB  1 
ATOM   9816  C  CG  . ARG   C  1 373 ? 9.673   45.472  -76.590  1.00 44.16  ? 674  ARG   C CG  1 
ATOM   9817  C  CD  . ARG   C  1 373 ? 10.761  44.541  -77.101  1.00 42.97  ? 674  ARG   C CD  1 
ATOM   9818  N  NE  . ARG   C  1 373 ? 10.193  43.413  -77.828  1.00 44.10  ? 674  ARG   C NE  1 
ATOM   9819  C  CZ  . ARG   C  1 373 ? 10.816  42.263  -78.060  1.00 47.52  ? 674  ARG   C CZ  1 
ATOM   9820  N  NH1 . ARG   C  1 373 ? 12.051  42.064  -77.617  1.00 46.76  ? 674  ARG   C NH1 1 
ATOM   9821  N  NH2 . ARG   C  1 373 ? 10.194  41.302  -78.737  1.00 47.26  ? 674  ARG   C NH2 1 
ATOM   9822  N  N   . GLY   C  1 374 ? 8.946   47.655  -72.855  1.00 59.05  ? 675  GLY   C N   1 
ATOM   9823  C  CA  . GLY   C  1 374 ? 8.387   47.152  -71.621  1.00 48.73  ? 675  GLY   C CA  1 
ATOM   9824  C  C   . GLY   C  1 374 ? 9.081   45.934  -71.061  1.00 49.53  ? 675  GLY   C C   1 
ATOM   9825  O  O   . GLY   C  1 374 ? 8.481   45.223  -70.246  1.00 45.77  ? 675  GLY   C O   1 
ATOM   9826  N  N   . GLY   C  1 375 ? 10.312  45.663  -71.469  1.00 44.05  ? 676  GLY   C N   1 
ATOM   9827  C  CA  . GLY   C  1 375 ? 11.041  44.528  -70.936  1.00 42.16  ? 676  GLY   C CA  1 
ATOM   9828  C  C   . GLY   C  1 375 ? 12.092  44.019  -71.902  1.00 51.94  ? 676  GLY   C C   1 
ATOM   9829  O  O   . GLY   C  1 375 ? 12.211  44.469  -73.045  1.00 45.69  ? 676  GLY   C O   1 
ATOM   9830  N  N   . CYS   C  1 376 ? 12.873  43.047  -71.406  1.00 46.66  ? 677  CYS   C N   1 
ATOM   9831  C  CA  . CYS   C  1 376 ? 13.944  42.409  -72.165  1.00 43.24  ? 677  CYS   C CA  1 
ATOM   9832  C  C   . CYS   C  1 376 ? 14.306  41.071  -71.523  1.00 45.33  ? 677  CYS   C C   1 
ATOM   9833  O  O   . CYS   C  1 376 ? 14.850  41.049  -70.415  1.00 41.44  ? 677  CYS   C O   1 
ATOM   9834  C  CB  . CYS   C  1 376 ? 15.163  43.332  -72.242  1.00 31.47  ? 677  CYS   C CB  1 
ATOM   9835  S  SG  . CYS   C  1 376 ? 16.580  42.591  -73.007  1.00 37.57  ? 677  CYS   C SG  1 
ATOM   9836  N  N   . PRO   C  1 377 ? 14.010  39.941  -72.173  1.00 40.24  ? 678  PRO   C N   1 
ATOM   9837  C  CA  . PRO   C  1 377 ? 14.349  38.636  -71.582  1.00 38.35  ? 678  PRO   C CA  1 
ATOM   9838  C  C   . PRO   C  1 377 ? 15.854  38.418  -71.523  1.00 42.53  ? 678  PRO   C C   1 
ATOM   9839  O  O   . PRO   C  1 377 ? 16.564  38.609  -72.512  1.00 29.75  ? 678  PRO   C O   1 
ATOM   9840  C  CB  . PRO   C  1 377 ? 13.674  37.629  -72.521  1.00 39.50  ? 678  PRO   C CB  1 
ATOM   9841  C  CG  . PRO   C  1 377 ? 13.548  38.377  -73.846  1.00 44.24  ? 678  PRO   C CG  1 
ATOM   9842  C  CD  . PRO   C  1 377 ? 13.241  39.797  -73.420  1.00 43.10  ? 678  PRO   C CD  1 
ATOM   9843  N  N   . ALA   C  1 378 ? 16.343  38.001  -70.349  1.00 40.11  ? 679  ALA   C N   1 
ATOM   9844  C  CA  . ALA   C  1 378 ? 17.780  37.871  -70.156  1.00 42.51  ? 679  ALA   C CA  1 
ATOM   9845  C  C   . ALA   C  1 378 ? 18.073  36.745  -69.174  1.00 45.04  ? 679  ALA   C C   1 
ATOM   9846  O  O   . ALA   C  1 378 ? 17.466  36.677  -68.098  1.00 43.24  ? 679  ALA   C O   1 
ATOM   9847  C  CB  . ALA   C  1 378 ? 18.390  39.192  -69.670  1.00 42.22  ? 679  ALA   C CB  1 
ATOM   9848  N  N   . ASP   C  1 379 ? 19.010  35.877  -69.556  1.00 39.11  ? 680  ASP   C N   1 
ATOM   9849  C  CA  . ASP   C  1 379 ? 19.407  34.711  -68.771  1.00 41.24  ? 680  ASP   C CA  1 
ATOM   9850  C  C   . ASP   C  1 379 ? 20.690  35.064  -68.003  1.00 41.19  ? 680  ASP   C C   1 
ATOM   9851  O  O   . ASP   C  1 379 ? 21.783  35.090  -68.573  1.00 36.95  ? 680  ASP   C O   1 
ATOM   9852  C  CB  . ASP   C  1 379 ? 19.582  33.512  -69.699  1.00 33.99  ? 680  ASP   C CB  1 
ATOM   9853  C  CG  . ASP   C  1 379 ? 19.856  32.212  -68.964  1.00 43.38  ? 680  ASP   C CG  1 
ATOM   9854  O  OD1 . ASP   C  1 379 ? 20.352  32.228  -67.816  1.00 52.05  ? 680  ASP   C OD1 1 
ATOM   9855  O  OD2 . ASP   C  1 379 ? 19.582  31.148  -69.554  1.00 46.21  ? 680  ASP   C OD2 1 
ATOM   9856  N  N   . TRP   C  1 380 ? 20.557  35.313  -66.691  1.00 38.40  ? 681  TRP   C N   1 
ATOM   9857  C  CA  . TRP   C  1 380 ? 21.693  35.798  -65.903  1.00 34.67  ? 681  TRP   C CA  1 
ATOM   9858  C  C   . TRP   C  1 380 ? 22.869  34.829  -65.966  1.00 31.65  ? 681  TRP   C C   1 
ATOM   9859  O  O   . TRP   C  1 380 ? 24.027  35.248  -66.080  1.00 28.35  ? 681  TRP   C O   1 
ATOM   9860  C  CB  . TRP   C  1 380 ? 21.251  36.019  -64.448  1.00 26.79  ? 681  TRP   C CB  1 
ATOM   9861  C  CG  . TRP   C  1 380 ? 22.201  36.784  -63.592  1.00 31.36  ? 681  TRP   C CG  1 
ATOM   9862  C  CD1 . TRP   C  1 380 ? 22.118  38.108  -63.273  1.00 35.27  ? 681  TRP   C CD1 1 
ATOM   9863  C  CD2 . TRP   C  1 380 ? 23.344  36.268  -62.881  1.00 35.88  ? 681  TRP   C CD2 1 
ATOM   9864  N  NE1 . TRP   C  1 380 ? 23.144  38.452  -62.427  1.00 34.69  ? 681  TRP   C NE1 1 
ATOM   9865  C  CE2 . TRP   C  1 380 ? 23.915  37.347  -62.176  1.00 37.23  ? 681  TRP   C CE2 1 
ATOM   9866  C  CE3 . TRP   C  1 380 ? 23.945  35.006  -62.785  1.00 36.48  ? 681  TRP   C CE3 1 
ATOM   9867  C  CZ2 . TRP   C  1 380 ? 25.065  37.206  -61.379  1.00 38.95  ? 681  TRP   C CZ2 1 
ATOM   9868  C  CZ3 . TRP   C  1 380 ? 25.100  34.867  -61.994  1.00 32.48  ? 681  TRP   C CZ3 1 
ATOM   9869  C  CH2 . TRP   C  1 380 ? 25.637  35.963  -61.298  1.00 34.70  ? 681  TRP   C CH2 1 
ATOM   9870  N  N   . VAL   C  1 381 ? 22.582  33.530  -65.874  1.00 31.06  ? 682  VAL   C N   1 
ATOM   9871  C  CA  . VAL   C  1 381 ? 23.601  32.488  -65.913  1.00 31.87  ? 682  VAL   C CA  1 
ATOM   9872  C  C   . VAL   C  1 381 ? 24.484  32.594  -67.151  1.00 36.60  ? 682  VAL   C C   1 
ATOM   9873  O  O   . VAL   C  1 381 ? 25.673  32.263  -67.095  1.00 38.21  ? 682  VAL   C O   1 
ATOM   9874  C  CB  . VAL   C  1 381 ? 22.916  31.114  -65.830  1.00 32.41  ? 682  VAL   C CB  1 
ATOM   9875  C  CG1 . VAL   C  1 381 ? 23.921  30.019  -65.981  1.00 24.22  ? 682  VAL   C CG1 1 
ATOM   9876  C  CG2 . VAL   C  1 381 ? 22.147  30.976  -64.513  1.00 33.00  ? 682  VAL   C CG2 1 
ATOM   9877  N  N   . TRP   C  1 382 ? 23.928  33.048  -68.281  1.00 37.00  ? 683  TRP   C N   1 
ATOM   9878  C  CA  . TRP   C  1 382 ? 24.659  33.136  -69.548  1.00 33.05  ? 683  TRP   C CA  1 
ATOM   9879  C  C   . TRP   C  1 382 ? 25.196  34.532  -69.848  1.00 35.98  ? 683  TRP   C C   1 
ATOM   9880  O  O   . TRP   C  1 382 ? 26.196  34.657  -70.562  1.00 40.32  ? 683  TRP   C O   1 
ATOM   9881  C  CB  . TRP   C  1 382 ? 23.762  32.688  -70.714  1.00 34.24  ? 683  TRP   C CB  1 
ATOM   9882  C  CG  . TRP   C  1 382 ? 23.667  31.185  -70.853  1.00 40.23  ? 683  TRP   C CG  1 
ATOM   9883  C  CD1 . TRP   C  1 382 ? 23.110  30.308  -69.956  1.00 37.46  ? 683  TRP   C CD1 1 
ATOM   9884  C  CD2 . TRP   C  1 382 ? 24.141  30.387  -71.949  1.00 39.98  ? 683  TRP   C CD2 1 
ATOM   9885  N  NE1 . TRP   C  1 382 ? 23.220  29.019  -70.424  1.00 39.57  ? 683  TRP   C NE1 1 
ATOM   9886  C  CE2 . TRP   C  1 382 ? 23.851  29.037  -71.641  1.00 43.31  ? 683  TRP   C CE2 1 
ATOM   9887  C  CE3 . TRP   C  1 382 ? 24.787  30.679  -73.150  1.00 43.51  ? 683  TRP   C CE3 1 
ATOM   9888  C  CZ2 . TRP   C  1 382 ? 24.179  27.980  -72.501  1.00 45.96  ? 683  TRP   C CZ2 1 
ATOM   9889  C  CZ3 . TRP   C  1 382 ? 25.118  29.621  -74.009  1.00 47.65  ? 683  TRP   C CZ3 1 
ATOM   9890  C  CH2 . TRP   C  1 382 ? 24.811  28.291  -73.674  1.00 40.31  ? 683  TRP   C CH2 1 
ATOM   9891  N  N   . ILE   C  1 383 ? 24.554  35.582  -69.330  1.00 35.44  ? 684  ILE   C N   1 
ATOM   9892  C  CA  . ILE   C  1 383 ? 24.984  36.945  -69.623  1.00 34.49  ? 684  ILE   C CA  1 
ATOM   9893  C  C   . ILE   C  1 383 ? 26.233  37.307  -68.820  1.00 41.89  ? 684  ILE   C C   1 
ATOM   9894  O  O   . ILE   C  1 383 ? 27.106  38.041  -69.310  1.00 36.62  ? 684  ILE   C O   1 
ATOM   9895  C  CB  . ILE   C  1 383 ? 23.830  37.925  -69.350  1.00 31.90  ? 684  ILE   C CB  1 
ATOM   9896  C  CG1 . ILE   C  1 383 ? 22.679  37.686  -70.319  1.00 32.26  ? 684  ILE   C CG1 1 
ATOM   9897  C  CG2 . ILE   C  1 383 ? 24.324  39.376  -69.386  1.00 28.79  ? 684  ILE   C CG2 1 
ATOM   9898  C  CD1 . ILE   C  1 383 ? 23.107  37.725  -71.772  1.00 42.58  ? 684  ILE   C CD1 1 
ATOM   9899  N  N   . VAL   C  1 384 ? 26.338  36.808  -67.584  1.00 39.02  ? 685  VAL   C N   1 
ATOM   9900  C  CA  . VAL   C  1 384 ? 27.483  37.127  -66.713  1.00 35.65  ? 685  VAL   C CA  1 
ATOM   9901  C  C   . VAL   C  1 384 ? 28.725  36.423  -67.241  1.00 36.23  ? 685  VAL   C C   1 
ATOM   9902  O  O   . VAL   C  1 384 ? 28.708  35.190  -67.402  1.00 38.99  ? 685  VAL   C O   1 
ATOM   9903  C  CB  . VAL   C  1 384 ? 27.201  36.706  -65.269  1.00 31.89  ? 685  VAL   C CB  1 
ATOM   9904  C  CG1 . VAL   C  1 384 ? 28.507  36.738  -64.462  1.00 24.97  ? 685  VAL   C CG1 1 
ATOM   9905  C  CG2 . VAL   C  1 384 ? 26.156  37.609  -64.656  1.00 37.28  ? 685  VAL   C CG2 1 
ATOM   9906  N  N   . PRO   C  1 385 ? 29.824  37.137  -67.482  1.00 34.65  ? 686  PRO   C N   1 
ATOM   9907  C  CA  . PRO   C  1 385 ? 30.959  36.514  -68.165  1.00 32.82  ? 686  PRO   C CA  1 
ATOM   9908  C  C   . PRO   C  1 385 ? 31.631  35.481  -67.274  1.00 40.55  ? 686  PRO   C C   1 
ATOM   9909  O  O   . PRO   C  1 385 ? 31.559  35.567  -66.037  1.00 43.12  ? 686  PRO   C O   1 
ATOM   9910  C  CB  . PRO   C  1 385 ? 31.897  37.700  -68.461  1.00 34.08  ? 686  PRO   C CB  1 
ATOM   9911  C  CG  . PRO   C  1 385 ? 31.045  38.912  -68.331  1.00 36.23  ? 686  PRO   C CG  1 
ATOM   9912  C  CD  . PRO   C  1 385 ? 30.015  38.581  -67.295  1.00 26.64  ? 686  PRO   C CD  1 
ATOM   9913  N  N   . PRO   C  1 386 ? 32.299  34.487  -67.864  1.00 40.97  ? 687  PRO   C N   1 
ATOM   9914  C  CA  . PRO   C  1 386 ? 32.866  33.388  -67.074  1.00 35.83  ? 687  PRO   C CA  1 
ATOM   9915  C  C   . PRO   C  1 386 ? 34.195  33.706  -66.404  1.00 36.06  ? 687  PRO   C C   1 
ATOM   9916  O  O   . PRO   C  1 386 ? 34.796  32.802  -65.811  1.00 43.56  ? 687  PRO   C O   1 
ATOM   9917  C  CB  . PRO   C  1 386 ? 33.022  32.278  -68.123  1.00 34.85  ? 687  PRO   C CB  1 
ATOM   9918  C  CG  . PRO   C  1 386 ? 33.349  33.043  -69.381  1.00 38.87  ? 687  PRO   C CG  1 
ATOM   9919  C  CD  . PRO   C  1 386 ? 32.545  34.316  -69.310  1.00 34.52  ? 687  PRO   C CD  1 
ATOM   9920  N  N   . MET   C  1 387 ? 34.687  34.944  -66.469  1.00 37.99  ? 688  MET   C N   1 
ATOM   9921  C  CA  . MET   C  1 387 ? 35.697  35.415  -65.528  1.00 36.19  ? 688  MET   C CA  1 
ATOM   9922  C  C   . MET   C  1 387 ? 35.271  36.778  -64.990  1.00 42.22  ? 688  MET   C C   1 
ATOM   9923  O  O   . MET   C  1 387 ? 34.480  37.500  -65.616  1.00 40.09  ? 688  MET   C O   1 
ATOM   9924  C  CB  . MET   C  1 387 ? 37.095  35.507  -66.154  1.00 37.88  ? 688  MET   C CB  1 
ATOM   9925  C  CG  . MET   C  1 387 ? 37.303  36.716  -67.076  1.00 48.67  ? 688  MET   C CG  1 
ATOM   9926  S  SD  . MET   C  1 387 ? 38.929  36.730  -67.886  1.00 54.67  ? 688  MET   C SD  1 
ATOM   9927  C  CE  . MET   C  1 387 ? 39.952  37.493  -66.629  1.00 54.46  ? 688  MET   C CE  1 
ATOM   9928  N  N   . SER   C  1 388 ? 35.782  37.110  -63.797  1.00 36.09  ? 689  SER   C N   1 
ATOM   9929  C  CA  . SER   C  1 388 ? 35.631  38.448  -63.219  1.00 34.45  ? 689  SER   C CA  1 
ATOM   9930  C  C   . SER   C  1 388 ? 34.167  38.873  -63.112  1.00 34.41  ? 689  SER   C C   1 
ATOM   9931  O  O   . SER   C  1 388 ? 33.821  40.039  -63.309  1.00 41.06  ? 689  SER   C O   1 
ATOM   9932  C  CB  . SER   C  1 388 ? 36.424  39.466  -64.036  1.00 39.71  ? 689  SER   C CB  1 
ATOM   9933  O  OG  . SER   C  1 388 ? 37.790  39.130  -64.046  1.00 44.29  ? 689  SER   C OG  1 
ATOM   9934  N  N   . GLY   C  1 389 ? 33.300  37.915  -62.808  1.00 32.68  ? 690  GLY   C N   1 
ATOM   9935  C  CA  . GLY   C  1 389 ? 31.870  38.154  -62.773  1.00 32.91  ? 690  GLY   C CA  1 
ATOM   9936  C  C   . GLY   C  1 389 ? 31.418  39.442  -62.111  1.00 41.68  ? 690  GLY   C C   1 
ATOM   9937  O  O   . GLY   C  1 389 ? 30.821  40.310  -62.763  1.00 35.76  ? 690  GLY   C O   1 
ATOM   9938  N  N   . SER   C  1 390 ? 31.720  39.594  -60.813  1.00 39.08  ? 691  SER   C N   1 
ATOM   9939  C  CA  . SER   C  1 390 ? 31.119  40.685  -60.065  1.00 34.75  ? 691  SER   C CA  1 
ATOM   9940  C  C   . SER   C  1 390 ? 31.764  42.039  -60.356  1.00 35.51  ? 691  SER   C C   1 
ATOM   9941  O  O   . SER   C  1 390 ? 31.219  43.069  -59.941  1.00 38.33  ? 691  SER   C O   1 
ATOM   9942  C  CB  . SER   C  1 390 ? 31.142  40.372  -58.545  1.00 36.08  ? 691  SER   C CB  1 
ATOM   9943  O  OG  . SER   C  1 390 ? 32.453  40.388  -58.023  1.00 35.42  ? 691  SER   C OG  1 
ATOM   9944  N  N   . ILE   C  1 391 ? 32.882  42.097  -61.074  1.00 40.85  ? 692  ILE   C N   1 
ATOM   9945  C  CA  . ILE   C  1 391 ? 33.373  43.428  -61.418  1.00 48.50  ? 692  ILE   C CA  1 
ATOM   9946  C  C   . ILE   C  1 391 ? 32.817  43.871  -62.768  1.00 43.48  ? 692  ILE   C C   1 
ATOM   9947  O  O   . ILE   C  1 391 ? 33.252  44.889  -63.307  1.00 46.03  ? 692  ILE   C O   1 
ATOM   9948  C  CB  . ILE   C  1 391 ? 34.915  43.542  -61.396  1.00 50.64  ? 692  ILE   C CB  1 
ATOM   9949  C  CG1 . ILE   C  1 391 ? 35.579  42.564  -62.353  1.00 44.62  ? 692  ILE   C CG1 1 
ATOM   9950  C  CG2 . ILE   C  1 391 ? 35.478  43.425  -59.944  1.00 50.46  ? 692  ILE   C CG2 1 
ATOM   9951  C  CD1 . ILE   C  1 391 ? 37.032  42.847  -62.510  1.00 34.87  ? 692  ILE   C CD1 1 
ATOM   9952  N  N   . THR   C  1 392 ? 31.825  43.129  -63.316  1.00 44.94  ? 693  THR   C N   1 
ATOM   9953  C  CA  . THR   C  1 392 ? 31.083  43.638  -64.466  1.00 47.76  ? 693  THR   C CA  1 
ATOM   9954  C  C   . THR   C  1 392 ? 29.669  44.012  -64.022  1.00 45.04  ? 693  THR   C C   1 
ATOM   9955  O  O   . THR   C  1 392 ? 29.127  43.399  -63.102  1.00 44.72  ? 693  THR   C O   1 
ATOM   9956  C  CB  . THR   C  1 392 ? 31.005  42.638  -65.639  1.00 42.81  ? 693  THR   C CB  1 
ATOM   9957  O  OG1 . THR   C  1 392 ? 30.100  41.567  -65.340  1.00 42.13  ? 693  THR   C OG1 1 
ATOM   9958  C  CG2 . THR   C  1 392 ? 32.387  42.049  -65.987  1.00 44.38  ? 693  THR   C CG2 1 
ATOM   9959  N  N   . PRO   C  1 393 ? 29.040  45.010  -64.652  1.00 44.65  ? 694  PRO   C N   1 
ATOM   9960  C  CA  . PRO   C  1 393 ? 27.788  45.543  -64.092  1.00 41.83  ? 694  PRO   C CA  1 
ATOM   9961  C  C   . PRO   C  1 393 ? 26.632  44.564  -64.126  1.00 42.27  ? 694  PRO   C C   1 
ATOM   9962  O  O   . PRO   C  1 393 ? 25.688  44.723  -63.338  1.00 52.57  ? 694  PRO   C O   1 
ATOM   9963  C  CB  . PRO   C  1 393 ? 27.502  46.767  -64.973  1.00 37.56  ? 694  PRO   C CB  1 
ATOM   9964  C  CG  . PRO   C  1 393 ? 28.150  46.432  -66.285  1.00 31.81  ? 694  PRO   C CG  1 
ATOM   9965  C  CD  . PRO   C  1 393 ? 29.417  45.701  -65.897  1.00 38.71  ? 694  PRO   C CD  1 
ATOM   9966  N  N   . VAL   C  1 394 ? 26.669  43.551  -64.991  1.00 40.75  ? 695  VAL   C N   1 
ATOM   9967  C  CA  . VAL   C  1 394 ? 25.505  42.689  -65.128  1.00 38.03  ? 695  VAL   C CA  1 
ATOM   9968  C  C   . VAL   C  1 394 ? 25.404  41.693  -63.988  1.00 34.07  ? 695  VAL   C C   1 
ATOM   9969  O  O   . VAL   C  1 394 ? 24.319  41.155  -63.755  1.00 34.33  ? 695  VAL   C O   1 
ATOM   9970  C  CB  . VAL   C  1 394 ? 25.490  41.938  -66.474  1.00 33.45  ? 695  VAL   C CB  1 
ATOM   9971  C  CG1 . VAL   C  1 394 ? 25.311  42.921  -67.622  1.00 34.19  ? 695  VAL   C CG1 1 
ATOM   9972  C  CG2 . VAL   C  1 394 ? 26.756  41.130  -66.647  1.00 30.52  ? 695  VAL   C CG2 1 
ATOM   9973  N  N   . PHE   C  1 395 ? 26.509  41.418  -63.292  1.00 42.31  ? 696  PHE   C N   1 
ATOM   9974  C  CA  . PHE   C  1 395 ? 26.445  40.571  -62.103  1.00 42.47  ? 696  PHE   C CA  1 
ATOM   9975  C  C   . PHE   C  1 395 ? 25.443  41.126  -61.100  1.00 41.47  ? 696  PHE   C C   1 
ATOM   9976  O  O   . PHE   C  1 395 ? 24.661  40.372  -60.514  1.00 31.87  ? 696  PHE   C O   1 
ATOM   9977  C  CB  . PHE   C  1 395 ? 27.837  40.443  -61.474  1.00 39.63  ? 696  PHE   C CB  1 
ATOM   9978  C  CG  . PHE   C  1 395 ? 27.866  39.666  -60.155  1.00 39.41  ? 696  PHE   C CG  1 
ATOM   9979  C  CD1 . PHE   C  1 395 ? 27.442  40.251  -58.977  1.00 41.48  ? 696  PHE   C CD1 1 
ATOM   9980  C  CD2 . PHE   C  1 395 ? 28.364  38.370  -60.109  1.00 39.35  ? 696  PHE   C CD2 1 
ATOM   9981  C  CE1 . PHE   C  1 395 ? 27.478  39.550  -57.772  1.00 51.36  ? 696  PHE   C CE1 1 
ATOM   9982  C  CE2 . PHE   C  1 395 ? 28.416  37.668  -58.923  1.00 46.41  ? 696  PHE   C CE2 1 
ATOM   9983  C  CZ  . PHE   C  1 395 ? 27.969  38.256  -57.750  1.00 49.95  ? 696  PHE   C CZ  1 
ATOM   9984  N  N   . HIS   C  1 396 ? 25.425  42.452  -60.940  1.00 40.20  ? 697  HIS   C N   1 
ATOM   9985  C  CA  . HIS   C  1 396 ? 24.598  43.181  -59.991  1.00 38.71  ? 697  HIS   C CA  1 
ATOM   9986  C  C   . HIS   C  1 396 ? 23.236  43.566  -60.547  1.00 39.33  ? 697  HIS   C C   1 
ATOM   9987  O  O   . HIS   C  1 396 ? 22.550  44.395  -59.939  1.00 44.88  ? 697  HIS   C O   1 
ATOM   9988  C  CB  . HIS   C  1 396 ? 25.343  44.437  -59.541  1.00 37.93  ? 697  HIS   C CB  1 
ATOM   9989  C  CG  . HIS   C  1 396 ? 26.752  44.159  -59.136  1.00 42.47  ? 697  HIS   C CG  1 
ATOM   9990  N  ND1 . HIS   C  1 396 ? 27.102  43.841  -57.844  1.00 37.82  ? 697  HIS   C ND1 1 
ATOM   9991  C  CD2 . HIS   C  1 396 ? 27.891  44.083  -59.863  1.00 44.00  ? 697  HIS   C CD2 1 
ATOM   9992  C  CE1 . HIS   C  1 396 ? 28.401  43.614  -57.783  1.00 41.41  ? 697  HIS   C CE1 1 
ATOM   9993  N  NE2 . HIS   C  1 396 ? 28.904  43.751  -58.995  1.00 43.76  ? 697  HIS   C NE2 1 
ATOM   9994  N  N   . GLN   C  1 397 ? 22.826  42.982  -61.671  1.00 36.95  ? 698  GLN   C N   1 
ATOM   9995  C  CA  . GLN   C  1 397 ? 21.587  43.348  -62.347  1.00 38.25  ? 698  GLN   C CA  1 
ATOM   9996  C  C   . GLN   C  1 397 ? 20.624  42.164  -62.335  1.00 37.12  ? 698  GLN   C C   1 
ATOM   9997  O  O   . GLN   C  1 397 ? 20.913  41.114  -62.921  1.00 46.22  ? 698  GLN   C O   1 
ATOM   9998  C  CB  . GLN   C  1 397 ? 21.873  43.797  -63.784  1.00 34.41  ? 698  GLN   C CB  1 
ATOM   9999  C  CG  . GLN   C  1 397 ? 20.619  44.037  -64.612  1.00 33.85  ? 698  GLN   C CG  1 
ATOM   10000 C  CD  . GLN   C  1 397 ? 19.968  45.358  -64.274  1.00 36.34  ? 698  GLN   C CD  1 
ATOM   10001 O  OE1 . GLN   C  1 397 ? 20.616  46.410  -64.319  1.00 36.24  ? 698  GLN   C OE1 1 
ATOM   10002 N  NE2 . GLN   C  1 397 ? 18.687  45.312  -63.906  1.00 38.85  ? 698  GLN   C NE2 1 
ATOM   10003 N  N   . GLU   C  1 398 ? 19.474  42.344  -61.693  1.00 32.96  ? 699  GLU   C N   1 
ATOM   10004 C  CA  . GLU   C  1 398 ? 18.431  41.332  -61.749  1.00 34.24  ? 699  GLU   C CA  1 
ATOM   10005 C  C   . GLU   C  1 398 ? 17.876  41.249  -63.168  1.00 43.04  ? 699  GLU   C C   1 
ATOM   10006 O  O   . GLU   C  1 398 ? 17.744  42.261  -63.855  1.00 42.70  ? 699  GLU   C O   1 
ATOM   10007 C  CB  . GLU   C  1 398 ? 17.316  41.660  -60.764  1.00 34.68  ? 699  GLU   C CB  1 
ATOM   10008 C  CG  . GLU   C  1 398 ? 17.782  41.696  -59.304  1.00 44.43  ? 699  GLU   C CG  1 
ATOM   10009 C  CD  . GLU   C  1 398 ? 16.647  41.921  -58.319  1.00 53.33  ? 699  GLU   C CD  1 
ATOM   10010 O  OE1 . GLU   C  1 398 ? 16.821  41.556  -57.131  1.00 46.09  ? 699  GLU   C OE1 1 
ATOM   10011 O  OE2 . GLU   C  1 398 ? 15.588  42.451  -58.728  1.00 59.89  ? 699  GLU   C OE2 1 
ATOM   10012 N  N   . MET   C  1 399 ? 17.548  40.040  -63.601  1.00 41.81  ? 700  MET   C N   1 
ATOM   10013 C  CA  . MET   C  1 399 ? 16.998  39.820  -64.931  1.00 40.05  ? 700  MET   C CA  1 
ATOM   10014 C  C   . MET   C  1 399 ? 15.800  38.885  -64.845  1.00 46.87  ? 700  MET   C C   1 
ATOM   10015 O  O   . MET   C  1 399 ? 15.760  37.984  -64.001  1.00 59.52  ? 700  MET   C O   1 
ATOM   10016 C  CB  . MET   C  1 399 ? 18.062  39.238  -65.866  1.00 33.87  ? 700  MET   C CB  1 
ATOM   10017 C  CG  . MET   C  1 399 ? 19.189  40.204  -66.214  1.00 29.22  ? 700  MET   C CG  1 
ATOM   10018 S  SD  . MET   C  1 399 ? 20.713  39.339  -66.635  1.00 36.28  ? 700  MET   C SD  1 
ATOM   10019 C  CE  . MET   C  1 399 ? 21.882  40.693  -66.666  1.00 34.82  ? 700  MET   C CE  1 
ATOM   10020 N  N   . LEU   C  1 400 ? 14.809  39.133  -65.688  1.00 41.18  ? 701  LEU   C N   1 
ATOM   10021 C  CA  . LEU   C  1 400 ? 13.690  38.223  -65.890  1.00 34.87  ? 701  LEU   C CA  1 
ATOM   10022 C  C   . LEU   C  1 400 ? 13.891  37.438  -67.178  1.00 41.72  ? 701  LEU   C C   1 
ATOM   10023 O  O   . LEU   C  1 400 ? 14.247  38.008  -68.216  1.00 42.30  ? 701  LEU   C O   1 
ATOM   10024 C  CB  . LEU   C  1 400 ? 12.375  38.985  -65.968  1.00 30.22  ? 701  LEU   C CB  1 
ATOM   10025 C  CG  . LEU   C  1 400 ? 11.843  39.604  -64.694  1.00 43.62  ? 701  LEU   C CG  1 
ATOM   10026 C  CD1 . LEU   C  1 400 ? 10.608  40.442  -65.026  1.00 48.35  ? 701  LEU   C CD1 1 
ATOM   10027 C  CD2 . LEU   C  1 400 ? 11.520  38.494  -63.709  1.00 41.25  ? 701  LEU   C CD2 1 
ATOM   10028 N  N   . ASN   C  1 401 ? 13.665  36.130  -67.118  1.00 42.37  ? 702  ASN   C N   1 
ATOM   10029 C  CA  . ASN   C  1 401 ? 13.814  35.281  -68.292  1.00 40.16  ? 702  ASN   C CA  1 
ATOM   10030 C  C   . ASN   C  1 401 ? 12.455  34.719  -68.685  1.00 43.87  ? 702  ASN   C C   1 
ATOM   10031 O  O   . ASN   C  1 401 ? 11.724  34.190  -67.838  1.00 42.21  ? 702  ASN   C O   1 
ATOM   10032 C  CB  . ASN   C  1 401 ? 14.819  34.147  -68.058  1.00 37.71  ? 702  ASN   C CB  1 
ATOM   10033 C  CG  . ASN   C  1 401 ? 15.398  33.614  -69.366  1.00 36.95  ? 702  ASN   C CG  1 
ATOM   10034 O  OD1 . ASN   C  1 401 ? 15.244  34.230  -70.401  1.00 34.07  ? 702  ASN   C OD1 1 
ATOM   10035 N  ND2 . ASN   C  1 401 ? 16.037  32.473  -69.318  1.00 33.77  ? 702  ASN   C ND2 1 
ATOM   10036 N  N   . TYR   C  1 402 ? 12.114  34.871  -69.966  1.00 41.23  ? 703  TYR   C N   1 
ATOM   10037 C  CA  . TYR   C  1 402 ? 10.883  34.347  -70.540  1.00 29.26  ? 703  TYR   C CA  1 
ATOM   10038 C  C   . TYR   C  1 402 ? 11.128  34.133  -72.032  1.00 35.99  ? 703  TYR   C C   1 
ATOM   10039 O  O   . TYR   C  1 402 ? 12.131  34.588  -72.586  1.00 35.47  ? 703  TYR   C O   1 
ATOM   10040 C  CB  . TYR   C  1 402 ? 9.695   35.280  -70.265  1.00 34.53  ? 703  TYR   C CB  1 
ATOM   10041 C  CG  . TYR   C  1 402 ? 9.971   36.773  -70.432  1.00 40.02  ? 703  TYR   C CG  1 
ATOM   10042 C  CD1 . TYR   C  1 402 ? 10.538  37.512  -69.401  1.00 37.27  ? 703  TYR   C CD1 1 
ATOM   10043 C  CD2 . TYR   C  1 402 ? 9.629   37.451  -71.613  1.00 35.33  ? 703  TYR   C CD2 1 
ATOM   10044 C  CE1 . TYR   C  1 402 ? 10.778  38.877  -69.533  1.00 36.25  ? 703  TYR   C CE1 1 
ATOM   10045 C  CE2 . TYR   C  1 402 ? 9.869   38.823  -71.759  1.00 32.22  ? 703  TYR   C CE2 1 
ATOM   10046 C  CZ  . TYR   C  1 402 ? 10.440  39.533  -70.704  1.00 40.66  ? 703  TYR   C CZ  1 
ATOM   10047 O  OH  . TYR   C  1 402 ? 10.694  40.889  -70.808  1.00 36.98  ? 703  TYR   C OH  1 
ATOM   10048 N  N   . ARG   C  1 403 ? 10.221  33.400  -72.667  1.00 42.07  ? 704  ARG   C N   1 
ATOM   10049 C  CA  . ARG   C  1 403 ? 10.420  32.888  -74.024  1.00 41.07  ? 704  ARG   C CA  1 
ATOM   10050 C  C   . ARG   C  1 403 ? 9.450   33.585  -74.984  1.00 45.22  ? 704  ARG   C C   1 
ATOM   10051 O  O   . ARG   C  1 403 ? 8.240   33.327  -74.957  1.00 47.38  ? 704  ARG   C O   1 
ATOM   10052 C  CB  . ARG   C  1 403 ? 10.236  31.370  -74.060  1.00 40.27  ? 704  ARG   C CB  1 
ATOM   10053 C  CG  . ARG   C  1 403 ? 11.140  30.561  -73.138  1.00 44.74  ? 704  ARG   C CG  1 
ATOM   10054 C  CD  . ARG   C  1 403 ? 12.347  29.971  -73.852  1.00 61.85  ? 704  ARG   C CD  1 
ATOM   10055 N  NE  . ARG   C  1 403 ? 12.013  29.170  -75.036  1.00 69.70  ? 704  ARG   C NE  1 
ATOM   10056 C  CZ  . ARG   C  1 403 ? 11.445  27.965  -75.008  1.00 62.63  ? 704  ARG   C CZ  1 
ATOM   10057 N  NH1 . ARG   C  1 403 ? 11.106  27.403  -73.859  1.00 61.71  ? 704  ARG   C NH1 1 
ATOM   10058 N  NH2 . ARG   C  1 403 ? 11.200  27.325  -76.138  1.00 59.97  ? 704  ARG   C NH2 1 
ATOM   10059 N  N   . LEU   C  1 404 ? 9.991   34.459  -75.831  1.00 50.71  ? 705  LEU   C N   1 
ATOM   10060 C  CA  . LEU   C  1 404 ? 9.256   35.169  -76.872  1.00 45.63  ? 705  LEU   C CA  1 
ATOM   10061 C  C   . LEU   C  1 404 ? 9.511   34.530  -78.234  1.00 46.66  ? 705  LEU   C C   1 
ATOM   10062 O  O   . LEU   C  1 404 ? 10.564  33.938  -78.475  1.00 43.58  ? 705  LEU   C O   1 
ATOM   10063 C  CB  . LEU   C  1 404 ? 9.666   36.644  -76.925  1.00 38.45  ? 705  LEU   C CB  1 
ATOM   10064 C  CG  . LEU   C  1 404 ? 9.489   37.488  -75.656  1.00 48.37  ? 705  LEU   C CG  1 
ATOM   10065 C  CD1 . LEU   C  1 404 ? 9.830   38.960  -75.938  1.00 38.73  ? 705  LEU   C CD1 1 
ATOM   10066 C  CD2 . LEU   C  1 404 ? 8.068   37.341  -75.095  1.00 28.49  ? 705  LEU   C CD2 1 
ATOM   10067 N  N   . THR   C  1 405 ? 8.535   34.653  -79.127  1.00 47.62  ? 706  THR   C N   1 
ATOM   10068 C  CA  . THR   C  1 405 ? 8.720   34.197  -80.490  1.00 44.84  ? 706  THR   C CA  1 
ATOM   10069 C  C   . THR   C  1 405 ? 8.638   35.388  -81.442  1.00 44.80  ? 706  THR   C C   1 
ATOM   10070 O  O   . THR   C  1 405 ? 7.963   36.375  -81.129  1.00 41.35  ? 706  THR   C O   1 
ATOM   10071 C  CB  . THR   C  1 405 ? 7.668   33.143  -80.866  1.00 50.27  ? 706  THR   C CB  1 
ATOM   10072 O  OG1 . THR   C  1 405 ? 8.075   32.455  -82.051  1.00 54.51  ? 706  THR   C OG1 1 
ATOM   10073 C  CG2 . THR   C  1 405 ? 6.298   33.777  -81.092  1.00 46.70  ? 706  THR   C CG2 1 
ATOM   10074 N  N   . PRO   C  1 406 ? 9.368   35.367  -82.586  1.00 42.02  ? 707  PRO   C N   1 
ATOM   10075 C  CA  . PRO   C  1 406 ? 10.342  34.393  -83.120  1.00 38.28  ? 707  PRO   C CA  1 
ATOM   10076 C  C   . PRO   C  1 406 ? 11.547  34.109  -82.216  1.00 39.89  ? 707  PRO   C C   1 
ATOM   10077 O  O   . PRO   C  1 406 ? 11.899  34.966  -81.395  1.00 39.23  ? 707  PRO   C O   1 
ATOM   10078 C  CB  . PRO   C  1 406 ? 10.826  35.052  -84.416  1.00 44.31  ? 707  PRO   C CB  1 
ATOM   10079 C  CG  . PRO   C  1 406 ? 9.719   35.967  -84.811  1.00 47.12  ? 707  PRO   C CG  1 
ATOM   10080 C  CD  . PRO   C  1 406 ? 9.148   36.483  -83.526  1.00 40.21  ? 707  PRO   C CD  1 
ATOM   10081 N  N   . SER   C  1 407 ? 12.184  32.946  -82.394  1.00 27.88  ? 708  SER   C N   1 
ATOM   10082 C  CA  . SER   C  1 407 ? 13.307  32.571  -81.553  1.00 39.09  ? 708  SER   C CA  1 
ATOM   10083 C  C   . SER   C  1 407 ? 14.267  31.655  -82.294  1.00 35.91  ? 708  SER   C C   1 
ATOM   10084 O  O   . SER   C  1 407 ? 13.920  31.014  -83.288  1.00 39.12  ? 708  SER   C O   1 
ATOM   10085 C  CB  . SER   C  1 407 ? 12.841  31.864  -80.268  1.00 51.71  ? 708  SER   C CB  1 
ATOM   10086 O  OG  . SER   C  1 407 ? 12.162  30.662  -80.592  1.00 60.39  ? 708  SER   C OG  1 
ATOM   10087 N  N   . PHE   C  1 408 ? 15.484  31.600  -81.769  1.00 39.41  ? 709  PHE   C N   1 
ATOM   10088 C  CA  . PHE   C  1 408 ? 16.429  30.537  -82.051  1.00 29.75  ? 709  PHE   C CA  1 
ATOM   10089 C  C   . PHE   C  1 408 ? 16.269  29.436  -81.012  1.00 41.01  ? 709  PHE   C C   1 
ATOM   10090 O  O   . PHE   C  1 408 ? 16.111  29.714  -79.817  1.00 45.70  ? 709  PHE   C O   1 
ATOM   10091 C  CB  . PHE   C  1 408 ? 17.854  31.085  -82.034  1.00 22.86  ? 709  PHE   C CB  1 
ATOM   10092 C  CG  . PHE   C  1 408 ? 18.139  32.043  -83.150  1.00 36.76  ? 709  PHE   C CG  1 
ATOM   10093 C  CD1 . PHE   C  1 408 ? 18.285  31.585  -84.458  1.00 32.68  ? 709  PHE   C CD1 1 
ATOM   10094 C  CD2 . PHE   C  1 408 ? 18.262  33.400  -82.898  1.00 37.86  ? 709  PHE   C CD2 1 
ATOM   10095 C  CE1 . PHE   C  1 408 ? 18.553  32.474  -85.490  1.00 31.21  ? 709  PHE   C CE1 1 
ATOM   10096 C  CE2 . PHE   C  1 408 ? 18.523  34.291  -83.912  1.00 28.94  ? 709  PHE   C CE2 1 
ATOM   10097 C  CZ  . PHE   C  1 408 ? 18.668  33.833  -85.221  1.00 33.17  ? 709  PHE   C CZ  1 
ATOM   10098 N  N   . GLU   C  1 409 ? 16.302  28.185  -81.469  1.00 41.15  ? 710  GLU   C N   1 
ATOM   10099 C  CA  . GLU   C  1 409 ? 16.097  27.039  -80.600  1.00 36.07  ? 710  GLU   C CA  1 
ATOM   10100 C  C   . GLU   C  1 409 ? 17.231  26.050  -80.778  1.00 39.70  ? 710  GLU   C C   1 
ATOM   10101 O  O   . GLU   C  1 409 ? 17.897  26.018  -81.808  1.00 41.15  ? 710  GLU   C O   1 
ATOM   10102 C  CB  . GLU   C  1 409 ? 14.763  26.323  -80.888  1.00 40.50  ? 710  GLU   C CB  1 
ATOM   10103 C  CG  . GLU   C  1 409 ? 13.518  27.206  -80.805  1.00 48.50  ? 710  GLU   C CG  1 
ATOM   10104 C  CD  . GLU   C  1 409 ? 13.198  27.688  -79.382  1.00 58.17  ? 710  GLU   C CD  1 
ATOM   10105 O  OE1 . GLU   C  1 409 ? 13.808  27.186  -78.404  1.00 66.34  ? 710  GLU   C OE1 1 
ATOM   10106 O  OE2 . GLU   C  1 409 ? 12.316  28.567  -79.247  1.00 47.68  ? 710  GLU   C OE2 1 
ATOM   10107 N  N   . TYR   C  1 410 ? 17.432  25.218  -79.765  1.00 39.53  ? 711  TYR   C N   1 
ATOM   10108 C  CA  . TYR   C  1 410 ? 18.305  24.083  -79.966  1.00 37.64  ? 711  TYR   C CA  1 
ATOM   10109 C  C   . TYR   C  1 410 ? 17.576  23.022  -80.778  1.00 35.17  ? 711  TYR   C C   1 
ATOM   10110 O  O   . TYR   C  1 410 ? 16.345  23.013  -80.882  1.00 34.41  ? 711  TYR   C O   1 
ATOM   10111 C  CB  . TYR   C  1 410 ? 18.767  23.479  -78.639  1.00 46.73  ? 711  TYR   C CB  1 
ATOM   10112 C  CG  . TYR   C  1 410 ? 19.474  24.447  -77.739  1.00 55.48  ? 711  TYR   C CG  1 
ATOM   10113 C  CD1 . TYR   C  1 410 ? 20.644  25.062  -78.143  1.00 60.97  ? 711  TYR   C CD1 1 
ATOM   10114 C  CD2 . TYR   C  1 410 ? 18.974  24.743  -76.480  1.00 68.14  ? 711  TYR   C CD2 1 
ATOM   10115 C  CE1 . TYR   C  1 410 ? 21.296  25.952  -77.326  1.00 69.56  ? 711  TYR   C CE1 1 
ATOM   10116 C  CE2 . TYR   C  1 410 ? 19.620  25.631  -75.651  1.00 75.86  ? 711  TYR   C CE2 1 
ATOM   10117 C  CZ  . TYR   C  1 410 ? 20.783  26.237  -76.081  1.00 75.11  ? 711  TYR   C CZ  1 
ATOM   10118 O  OH  . TYR   C  1 410 ? 21.446  27.126  -75.265  1.00 73.69  ? 711  TYR   C OH  1 
ATOM   10119 N  N   . GLN   C  1 411 ? 18.361  22.126  -81.366  1.00 37.38  ? 712  GLN   C N   1 
ATOM   10120 C  CA  . GLN   C  1 411 ? 17.844  21.017  -82.146  1.00 36.17  ? 712  GLN   C CA  1 
ATOM   10121 C  C   . GLN   C  1 411 ? 18.861  19.897  -82.025  1.00 42.45  ? 712  GLN   C C   1 
ATOM   10122 O  O   . GLN   C  1 411 ? 20.042  20.161  -81.763  1.00 37.39  ? 712  GLN   C O   1 
ATOM   10123 C  CB  . GLN   C  1 411 ? 17.588  21.407  -83.619  1.00 41.06  ? 712  GLN   C CB  1 
ATOM   10124 C  CG  . GLN   C  1 411 ? 18.816  21.669  -84.491  1.00 37.25  ? 712  GLN   C CG  1 
ATOM   10125 C  CD  . GLN   C  1 411 ? 18.461  22.159  -85.910  1.00 40.11  ? 712  GLN   C CD  1 
ATOM   10126 O  OE1 . GLN   C  1 411 ? 17.520  21.676  -86.549  1.00 49.47  ? 712  GLN   C OE1 1 
ATOM   10127 N  NE2 . GLN   C  1 411 ? 19.217  23.128  -86.394  1.00 37.71  ? 712  GLN   C NE2 1 
ATOM   10128 N  N   . PRO   C  1 412 ? 18.432  18.646  -82.126  1.00 48.78  ? 713  PRO   C N   1 
ATOM   10129 C  CA  . PRO   C  1 412 ? 19.378  17.545  -81.945  1.00 51.81  ? 713  PRO   C CA  1 
ATOM   10130 C  C   . PRO   C  1 412 ? 20.375  17.497  -83.094  1.00 49.59  ? 713  PRO   C C   1 
ATOM   10131 O  O   . PRO   C  1 412 ? 20.085  17.930  -84.208  1.00 47.07  ? 713  PRO   C O   1 
ATOM   10132 C  CB  . PRO   C  1 412 ? 18.482  16.303  -81.920  1.00 53.61  ? 713  PRO   C CB  1 
ATOM   10133 C  CG  . PRO   C  1 412 ? 17.198  16.722  -82.585  1.00 48.72  ? 713  PRO   C CG  1 
ATOM   10134 C  CD  . PRO   C  1 412 ? 17.048  18.182  -82.343  1.00 47.33  ? 713  PRO   C CD  1 
ATOM   10135 N  N   . ASP   C  1 413 ? 21.573  17.000  -82.790  1.00 53.76  ? 714  ASP   C N   1 
ATOM   10136 C  CA  . ASP   C  1 413 ? 22.596  16.807  -83.805  1.00 61.57  ? 714  ASP   C CA  1 
ATOM   10137 C  C   . ASP   C  1 413 ? 22.066  15.890  -84.902  1.00 60.53  ? 714  ASP   C C   1 
ATOM   10138 O  O   . ASP   C  1 413 ? 21.473  14.846  -84.594  1.00 63.37  ? 714  ASP   C O   1 
ATOM   10139 C  CB  . ASP   C  1 413 ? 23.856  16.191  -83.199  1.00 69.81  ? 714  ASP   C CB  1 
ATOM   10140 C  CG  . ASP   C  1 413 ? 24.486  17.062  -82.143  1.00 71.52  ? 714  ASP   C CG  1 
ATOM   10141 O  OD1 . ASP   C  1 413 ? 24.480  18.301  -82.311  1.00 71.72  ? 714  ASP   C OD1 1 
ATOM   10142 O  OD2 . ASP   C  1 413 ? 24.996  16.500  -81.148  1.00 72.98  ? 714  ASP   C OD2 1 
ATOM   10143 N  N   . PRO   C  1 414 ? 22.275  16.222  -86.177  1.00 57.80  ? 715  PRO   C N   1 
ATOM   10144 C  CA  . PRO   C  1 414 ? 21.642  15.433  -87.244  1.00 49.72  ? 715  PRO   C CA  1 
ATOM   10145 C  C   . PRO   C  1 414 ? 22.112  13.990  -87.304  1.00 54.23  ? 715  PRO   C C   1 
ATOM   10146 O  O   . PRO   C  1 414 ? 21.357  13.136  -87.783  1.00 58.12  ? 715  PRO   C O   1 
ATOM   10147 C  CB  . PRO   C  1 414 ? 22.002  16.206  -88.523  1.00 45.31  ? 715  PRO   C CB  1 
ATOM   10148 C  CG  . PRO   C  1 414 ? 23.202  16.990  -88.184  1.00 49.75  ? 715  PRO   C CG  1 
ATOM   10149 C  CD  . PRO   C  1 414 ? 23.121  17.308  -86.700  1.00 54.21  ? 715  PRO   C CD  1 
ATOM   10150 N  N   . TRP   C  1 415 ? 23.304  13.666  -86.813  1.00 58.28  ? 716  TRP   C N   1 
ATOM   10151 C  CA  . TRP   C  1 415 ? 23.733  12.278  -86.928  1.00 62.35  ? 716  TRP   C CA  1 
ATOM   10152 C  C   . TRP   C  1 415 ? 23.062  11.362  -85.912  1.00 69.15  ? 716  TRP   C C   1 
ATOM   10153 O  O   . TRP   C  1 415 ? 23.208  10.140  -86.018  1.00 69.74  ? 716  TRP   C O   1 
ATOM   10154 C  CB  . TRP   C  1 415 ? 25.250  12.173  -86.795  1.00 59.62  ? 716  TRP   C CB  1 
ATOM   10155 C  CG  . TRP   C  1 415 ? 25.753  12.758  -85.543  1.00 63.24  ? 716  TRP   C CG  1 
ATOM   10156 C  CD1 . TRP   C  1 415 ? 25.795  12.158  -84.317  1.00 67.38  ? 716  TRP   C CD1 1 
ATOM   10157 C  CD2 . TRP   C  1 415 ? 26.284  14.072  -85.366  1.00 63.59  ? 716  TRP   C CD2 1 
ATOM   10158 N  NE1 . TRP   C  1 415 ? 26.327  13.018  -83.389  1.00 63.12  ? 716  TRP   C NE1 1 
ATOM   10159 C  CE2 . TRP   C  1 415 ? 26.638  14.200  -84.007  1.00 64.62  ? 716  TRP   C CE2 1 
ATOM   10160 C  CE3 . TRP   C  1 415 ? 26.498  15.153  -86.223  1.00 62.14  ? 716  TRP   C CE3 1 
ATOM   10161 C  CZ2 . TRP   C  1 415 ? 27.195  15.364  -83.488  1.00 66.22  ? 716  TRP   C CZ2 1 
ATOM   10162 C  CZ3 . TRP   C  1 415 ? 27.050  16.306  -85.707  1.00 62.86  ? 716  TRP   C CZ3 1 
ATOM   10163 C  CH2 . TRP   C  1 415 ? 27.392  16.404  -84.353  1.00 65.94  ? 716  TRP   C CH2 1 
ATOM   10164 N  N   . ASN   C  1 416 ? 22.340  11.912  -84.933  1.00 73.93  ? 717  ASN   C N   1 
ATOM   10165 C  CA  . ASN   C  1 416 ? 21.517  11.097  -84.047  1.00 72.43  ? 717  ASN   C CA  1 
ATOM   10166 C  C   . ASN   C  1 416 ? 20.195  10.709  -84.683  1.00 80.52  ? 717  ASN   C C   1 
ATOM   10167 O  O   . ASN   C  1 416 ? 19.506  9.829   -84.154  1.00 85.94  ? 717  ASN   C O   1 
ATOM   10168 C  CB  . ASN   C  1 416 ? 21.235  11.836  -82.739  1.00 62.17  ? 717  ASN   C CB  1 
ATOM   10169 C  CG  . ASN   C  1 416 ? 22.494  12.283  -82.049  1.00 64.24  ? 717  ASN   C CG  1 
ATOM   10170 O  OD1 . ASN   C  1 416 ? 23.535  11.634  -82.155  1.00 66.73  ? 717  ASN   C OD1 1 
ATOM   10171 N  ND2 . ASN   C  1 416 ? 22.412  13.397  -81.331  1.00 65.59  ? 717  ASN   C ND2 1 
ATOM   10172 N  N   . THR   C  1 417 ? 19.839  11.338  -85.805  1.00 79.76  ? 718  THR   C N   1 
ATOM   10173 C  CA  . THR   C  1 417 ? 18.513  11.212  -86.392  1.00 79.97  ? 718  THR   C CA  1 
ATOM   10174 C  C   . THR   C  1 417 ? 18.504  10.887  -87.883  1.00 84.21  ? 718  THR   C C   1 
ATOM   10175 O  O   . THR   C  1 417 ? 17.457  10.463  -88.388  1.00 90.38  ? 718  THR   C O   1 
ATOM   10176 C  CB  . THR   C  1 417 ? 17.714  12.505  -86.159  1.00 74.67  ? 718  THR   C CB  1 
ATOM   10177 O  OG1 . THR   C  1 417 ? 18.572  13.638  -86.342  1.00 71.35  ? 718  THR   C OG1 1 
ATOM   10178 C  CG2 . THR   C  1 417 ? 17.160  12.540  -84.744  1.00 70.56  ? 718  THR   C CG2 1 
ATOM   10179 N  N   . HIS   C  1 418 ? 19.616  11.041  -88.598  1.00 81.10  ? 719  HIS   C N   1 
ATOM   10180 C  CA  . HIS   C  1 418 ? 19.627  10.889  -90.051  1.00 81.38  ? 719  HIS   C CA  1 
ATOM   10181 C  C   . HIS   C  1 418 ? 19.895  9.438   -90.443  1.00 80.89  ? 719  HIS   C C   1 
ATOM   10182 O  O   . HIS   C  1 418 ? 20.881  8.840   -90.000  1.00 75.10  ? 719  HIS   C O   1 
ATOM   10183 C  CB  . HIS   C  1 418 ? 20.677  11.812  -90.677  1.00 75.21  ? 719  HIS   C CB  1 
ATOM   10184 C  CG  . HIS   C  1 418 ? 20.960  11.519  -92.115  1.00 70.73  ? 719  HIS   C CG  1 
ATOM   10185 N  ND1 . HIS   C  1 418 ? 20.167  11.987  -93.140  1.00 69.45  ? 719  HIS   C ND1 1 
ATOM   10186 C  CD2 . HIS   C  1 418 ? 21.944  10.794  -92.699  1.00 71.87  ? 719  HIS   C CD2 1 
ATOM   10187 C  CE1 . HIS   C  1 418 ? 20.650  11.562  -94.294  1.00 72.79  ? 719  HIS   C CE1 1 
ATOM   10188 N  NE2 . HIS   C  1 418 ? 21.729  10.838  -94.055  1.00 71.44  ? 719  HIS   C NE2 1 
ATOM   10189 N  N   . VAL   C  1 419 ? 19.016  8.878   -91.274  1.00 86.30  ? 720  VAL   C N   1 
ATOM   10190 C  CA  . VAL   C  1 419 ? 19.180  7.531   -91.816  1.00 91.08  ? 720  VAL   C CA  1 
ATOM   10191 C  C   . VAL   C  1 419 ? 19.851  7.664   -93.179  1.00 96.52  ? 720  VAL   C C   1 
ATOM   10192 O  O   . VAL   C  1 419 ? 19.272  8.223   -94.116  1.00 100.48 ? 720  VAL   C O   1 
ATOM   10193 C  CB  . VAL   C  1 419 ? 17.841  6.787   -91.917  1.00 88.78  ? 720  VAL   C CB  1 
ATOM   10194 C  CG1 . VAL   C  1 419 ? 17.610  5.935   -90.674  1.00 88.32  ? 720  VAL   C CG1 1 
ATOM   10195 C  CG2 . VAL   C  1 419 ? 16.691  7.776   -92.119  1.00 85.33  ? 720  VAL   C CG2 1 
ATOM   10196 N  N   . TRP   C  1 420 ? 21.072  7.146   -93.293  1.00 96.73  ? 721  TRP   C N   1 
ATOM   10197 C  CA  . TRP   C  1 420 ? 21.880  7.351   -94.490  1.00 96.37  ? 721  TRP   C CA  1 
ATOM   10198 C  C   . TRP   C  1 420 ? 21.296  6.627   -95.696  1.00 100.17 ? 721  TRP   C C   1 
ATOM   10199 O  O   . TRP   C  1 420 ? 20.597  5.619   -95.569  1.00 103.83 ? 721  TRP   C O   1 
ATOM   10200 C  CB  . TRP   C  1 420 ? 23.310  6.872   -94.253  1.00 96.75  ? 721  TRP   C CB  1 
ATOM   10201 C  CG  . TRP   C  1 420 ? 24.093  7.748   -93.326  1.00 94.70  ? 721  TRP   C CG  1 
ATOM   10202 C  CD1 . TRP   C  1 420 ? 23.946  7.848   -91.972  1.00 92.98  ? 721  TRP   C CD1 1 
ATOM   10203 C  CD2 . TRP   C  1 420 ? 25.152  8.645   -93.683  1.00 89.90  ? 721  TRP   C CD2 1 
ATOM   10204 N  NE1 . TRP   C  1 420 ? 24.844  8.757   -91.464  1.00 87.72  ? 721  TRP   C NE1 1 
ATOM   10205 C  CE2 . TRP   C  1 420 ? 25.599  9.257   -92.492  1.00 88.34  ? 721  TRP   C CE2 1 
ATOM   10206 C  CE3 . TRP   C  1 420 ? 25.764  8.991   -94.892  1.00 83.75  ? 721  TRP   C CE3 1 
ATOM   10207 C  CZ2 . TRP   C  1 420 ? 26.630  10.192  -92.476  1.00 86.17  ? 721  TRP   C CZ2 1 
ATOM   10208 C  CZ3 . TRP   C  1 420 ? 26.785  9.918   -94.875  1.00 85.88  ? 721  TRP   C CZ3 1 
ATOM   10209 C  CH2 . TRP   C  1 420 ? 27.207  10.511  -93.674  1.00 88.27  ? 721  TRP   C CH2 1 
ATOM   10210 N  N   . LYS   C  1 421 ? 21.594  7.154   -96.880  1.00 100.08 ? 722  LYS   C N   1 
ATOM   10211 C  CA  . LYS   C  1 421 ? 21.175  6.516   -98.121  1.00 98.90  ? 722  LYS   C CA  1 
ATOM   10212 C  C   . LYS   C  1 421 ? 22.285  5.593   -98.618  1.00 95.74  ? 722  LYS   C C   1 
ATOM   10213 O  O   . LYS   C  1 421 ? 22.087  4.390   -98.798  1.00 92.94  ? 722  LYS   C O   1 
ATOM   10214 C  CB  . LYS   C  1 421 ? 20.832  7.558   -99.189  1.00 99.28  ? 722  LYS   C CB  1 
ATOM   10215 C  CG  . LYS   C  1 421 ? 20.099  8.799   -98.675  1.00 98.36  ? 722  LYS   C CG  1 
ATOM   10216 C  CD  . LYS   C  1 421 ? 18.587  8.677   -98.768  1.00 95.58  ? 722  LYS   C CD  1 
ATOM   10217 C  CE  . LYS   C  1 421 ? 17.953  10.057  -98.883  1.00 90.29  ? 722  LYS   C CE  1 
ATOM   10218 N  NZ  . LYS   C  1 421 ? 16.625  10.141  -98.220  1.00 87.30  ? 722  LYS   C NZ  1 
ATOM   10219 N  N   . ARG   D  1 3   ? 7.659   11.785  -60.099  1.00 88.93  ? 304  ARG   D N   1 
ATOM   10220 C  CA  . ARG   D  1 3   ? 8.641   11.458  -61.125  1.00 95.10  ? 304  ARG   D CA  1 
ATOM   10221 C  C   . ARG   D  1 3   ? 10.063  11.820  -60.688  1.00 91.62  ? 304  ARG   D C   1 
ATOM   10222 O  O   . ARG   D  1 3   ? 10.390  11.812  -59.499  1.00 92.81  ? 304  ARG   D O   1 
ATOM   10223 C  CB  . ARG   D  1 3   ? 8.303   12.158  -62.456  1.00 103.45 ? 304  ARG   D CB  1 
ATOM   10224 C  CG  . ARG   D  1 3   ? 8.280   13.689  -62.431  1.00 103.77 ? 304  ARG   D CG  1 
ATOM   10225 C  CD  . ARG   D  1 3   ? 6.960   14.214  -61.881  1.00 106.69 ? 304  ARG   D CD  1 
ATOM   10226 N  NE  . ARG   D  1 3   ? 6.952   15.664  -61.721  1.00 109.48 ? 304  ARG   D NE  1 
ATOM   10227 C  CZ  . ARG   D  1 3   ? 7.656   16.313  -60.801  1.00 111.15 ? 304  ARG   D CZ  1 
ATOM   10228 N  NH1 . ARG   D  1 3   ? 8.438   15.637  -59.977  1.00 114.95 ? 304  ARG   D NH1 1 
ATOM   10229 N  NH2 . ARG   D  1 3   ? 7.592   17.635  -60.712  1.00 107.21 ? 304  ARG   D NH2 1 
ATOM   10230 N  N   . PHE   D  1 4   ? 10.905  12.129  -61.670  1.00 85.06  ? 305  PHE   D N   1 
ATOM   10231 C  CA  . PHE   D  1 4   ? 12.320  12.360  -61.450  1.00 75.59  ? 305  PHE   D CA  1 
ATOM   10232 C  C   . PHE   D  1 4   ? 12.739  13.585  -62.251  1.00 64.34  ? 305  PHE   D C   1 
ATOM   10233 O  O   . PHE   D  1 4   ? 12.059  13.994  -63.193  1.00 65.13  ? 305  PHE   D O   1 
ATOM   10234 C  CB  . PHE   D  1 4   ? 13.156  11.132  -61.862  1.00 83.98  ? 305  PHE   D CB  1 
ATOM   10235 C  CG  . PHE   D  1 4   ? 12.792  9.857   -61.123  1.00 97.59  ? 305  PHE   D CG  1 
ATOM   10236 C  CD1 . PHE   D  1 4   ? 11.744  9.053   -61.557  1.00 104.54 ? 305  PHE   D CD1 1 
ATOM   10237 C  CD2 . PHE   D  1 4   ? 13.511  9.452   -60.002  1.00 98.12  ? 305  PHE   D CD2 1 
ATOM   10238 C  CE1 . PHE   D  1 4   ? 11.414  7.877   -60.873  1.00 104.04 ? 305  PHE   D CE1 1 
ATOM   10239 C  CE2 . PHE   D  1 4   ? 13.188  8.275   -59.319  1.00 95.75  ? 305  PHE   D CE2 1 
ATOM   10240 C  CZ  . PHE   D  1 4   ? 12.140  7.492   -59.754  1.00 97.95  ? 305  PHE   D CZ  1 
ATOM   10241 N  N   . LEU   D  1 5   ? 13.860  14.182  -61.853  1.00 51.21  ? 306  LEU   D N   1 
ATOM   10242 C  CA  . LEU   D  1 5   ? 14.485  15.253  -62.616  1.00 38.63  ? 306  LEU   D CA  1 
ATOM   10243 C  C   . LEU   D  1 5   ? 15.981  15.034  -62.610  1.00 43.72  ? 306  LEU   D C   1 
ATOM   10244 O  O   . LEU   D  1 5   ? 16.554  14.681  -61.579  1.00 53.33  ? 306  LEU   D O   1 
ATOM   10245 C  CB  . LEU   D  1 5   ? 14.174  16.637  -62.059  1.00 33.27  ? 306  LEU   D CB  1 
ATOM   10246 C  CG  . LEU   D  1 5   ? 12.722  17.071  -62.231  1.00 40.85  ? 306  LEU   D CG  1 
ATOM   10247 C  CD1 . LEU   D  1 5   ? 12.446  18.297  -61.401  1.00 41.11  ? 306  LEU   D CD1 1 
ATOM   10248 C  CD2 . LEU   D  1 5   ? 12.442  17.350  -63.710  1.00 52.56  ? 306  LEU   D CD2 1 
ATOM   10249 N  N   . LYS   D  1 6   ? 16.616  15.240  -63.758  1.00 45.82  ? 307  LYS   D N   1 
ATOM   10250 C  CA  . LYS   D  1 6   ? 18.042  15.000  -63.882  1.00 45.25  ? 307  LYS   D CA  1 
ATOM   10251 C  C   . LYS   D  1 6   ? 18.783  16.319  -64.010  1.00 43.20  ? 307  LYS   D C   1 
ATOM   10252 O  O   . LYS   D  1 6   ? 18.258  17.296  -64.554  1.00 45.11  ? 307  LYS   D O   1 
ATOM   10253 C  CB  . LYS   D  1 6   ? 18.341  14.084  -65.070  1.00 49.20  ? 307  LYS   D CB  1 
ATOM   10254 C  CG  . LYS   D  1 6   ? 17.727  12.719  -64.891  1.00 51.97  ? 307  LYS   D CG  1 
ATOM   10255 C  CD  . LYS   D  1 6   ? 18.368  11.691  -65.778  1.00 66.83  ? 307  LYS   D CD  1 
ATOM   10256 C  CE  . LYS   D  1 6   ? 17.982  10.291  -65.326  1.00 76.86  ? 307  LYS   D CE  1 
ATOM   10257 N  NZ  . LYS   D  1 6   ? 17.508  9.465   -66.470  1.00 82.78  ? 307  LYS   D NZ  1 
ATOM   10258 N  N   . VAL   D  1 7   ? 19.985  16.348  -63.443  1.00 42.67  ? 308  VAL   D N   1 
ATOM   10259 C  CA  . VAL   D  1 7   ? 20.942  17.427  -63.637  1.00 41.44  ? 308  VAL   D CA  1 
ATOM   10260 C  C   . VAL   D  1 7   ? 22.209  16.812  -64.217  1.00 38.55  ? 308  VAL   D C   1 
ATOM   10261 O  O   . VAL   D  1 7   ? 22.591  15.697  -63.854  1.00 43.77  ? 308  VAL   D O   1 
ATOM   10262 C  CB  . VAL   D  1 7   ? 21.244  18.200  -62.328  1.00 40.52  ? 308  VAL   D CB  1 
ATOM   10263 C  CG1 . VAL   D  1 7   ? 20.029  18.977  -61.877  1.00 37.08  ? 308  VAL   D CG1 1 
ATOM   10264 C  CG2 . VAL   D  1 7   ? 21.730  17.263  -61.217  1.00 41.58  ? 308  VAL   D CG2 1 
ATOM   10265 N  N   . LYS   D  1 8   ? 22.847  17.527  -65.135  1.00 42.70  ? 309  LYS   D N   1 
ATOM   10266 C  CA  . LYS   D  1 8   ? 24.045  17.045  -65.806  1.00 33.04  ? 309  LYS   D CA  1 
ATOM   10267 C  C   . LYS   D  1 8   ? 25.214  17.972  -65.503  1.00 37.87  ? 309  LYS   D C   1 
ATOM   10268 O  O   . LYS   D  1 8   ? 25.048  19.192  -65.412  1.00 48.02  ? 309  LYS   D O   1 
ATOM   10269 C  CB  . LYS   D  1 8   ? 23.796  16.941  -67.323  1.00 43.14  ? 309  LYS   D CB  1 
ATOM   10270 C  CG  . LYS   D  1 8   ? 25.019  16.685  -68.201  1.00 40.99  ? 309  LYS   D CG  1 
ATOM   10271 C  CD  . LYS   D  1 8   ? 24.555  16.374  -69.617  1.00 42.32  ? 309  LYS   D CD  1 
ATOM   10272 C  CE  . LYS   D  1 8   ? 25.702  16.327  -70.625  1.00 48.17  ? 309  LYS   D CE  1 
ATOM   10273 N  NZ  . LYS   D  1 8   ? 25.221  15.886  -71.982  1.00 51.30  ? 309  LYS   D NZ  1 
ATOM   10274 N  N   . ASN   D  1 9   ? 26.398  17.388  -65.341  1.00 42.73  ? 310  ASN   D N   1 
ATOM   10275 C  CA  . ASN   D  1 9   ? 27.646  18.138  -65.337  1.00 44.91  ? 310  ASN   D CA  1 
ATOM   10276 C  C   . ASN   D  1 9   ? 28.222  18.088  -66.746  1.00 47.19  ? 310  ASN   D C   1 
ATOM   10277 O  O   . ASN   D  1 9   ? 28.458  17.002  -67.279  1.00 48.58  ? 310  ASN   D O   1 
ATOM   10278 C  CB  . ASN   D  1 9   ? 28.634  17.569  -64.317  1.00 46.85  ? 310  ASN   D CB  1 
ATOM   10279 C  CG  . ASN   D  1 9   ? 29.857  18.458  -64.126  1.00 48.07  ? 310  ASN   D CG  1 
ATOM   10280 O  OD1 . ASN   D  1 9   ? 30.652  18.650  -65.048  1.00 44.81  ? 310  ASN   D OD1 1 
ATOM   10281 N  ND2 . ASN   D  1 9   ? 30.023  18.991  -62.915  1.00 48.40  ? 310  ASN   D ND2 1 
ATOM   10282 N  N   . TRP   D  1 10  ? 28.420  19.257  -67.355  1.00 48.94  ? 311  TRP   D N   1 
ATOM   10283 C  CA  . TRP   D  1 10  ? 28.865  19.334  -68.742  1.00 51.83  ? 311  TRP   D CA  1 
ATOM   10284 C  C   . TRP   D  1 10  ? 30.377  19.267  -68.897  1.00 53.98  ? 311  TRP   D C   1 
ATOM   10285 O  O   . TRP   D  1 10  ? 30.871  19.257  -70.028  1.00 62.20  ? 311  TRP   D O   1 
ATOM   10286 C  CB  . TRP   D  1 10  ? 28.326  20.607  -69.391  1.00 48.85  ? 311  TRP   D CB  1 
ATOM   10287 C  CG  . TRP   D  1 10  ? 26.848  20.560  -69.534  1.00 46.66  ? 311  TRP   D CG  1 
ATOM   10288 C  CD1 . TRP   D  1 10  ? 25.923  20.970  -68.624  1.00 41.75  ? 311  TRP   D CD1 1 
ATOM   10289 C  CD2 . TRP   D  1 10  ? 26.118  20.042  -70.649  1.00 40.92  ? 311  TRP   D CD2 1 
ATOM   10290 N  NE1 . TRP   D  1 10  ? 24.649  20.747  -69.109  1.00 42.62  ? 311  TRP   D NE1 1 
ATOM   10291 C  CE2 . TRP   D  1 10  ? 24.746  20.184  -70.354  1.00 40.15  ? 311  TRP   D CE2 1 
ATOM   10292 C  CE3 . TRP   D  1 10  ? 26.489  19.483  -71.873  1.00 53.98  ? 311  TRP   D CE3 1 
ATOM   10293 C  CZ2 . TRP   D  1 10  ? 23.748  19.780  -71.234  1.00 48.55  ? 311  TRP   D CZ2 1 
ATOM   10294 C  CZ3 . TRP   D  1 10  ? 25.492  19.083  -72.757  1.00 51.56  ? 311  TRP   D CZ3 1 
ATOM   10295 C  CH2 . TRP   D  1 10  ? 24.140  19.235  -72.432  1.00 52.06  ? 311  TRP   D CH2 1 
ATOM   10296 N  N   . GLU   D  1 11  ? 31.115  19.232  -67.795  1.00 52.70  ? 312  GLU   D N   1 
ATOM   10297 C  CA  . GLU   D  1 11  ? 32.542  18.941  -67.780  1.00 52.49  ? 312  GLU   D CA  1 
ATOM   10298 C  C   . GLU   D  1 11  ? 32.803  17.441  -67.636  1.00 49.48  ? 312  GLU   D C   1 
ATOM   10299 O  O   . GLU   D  1 11  ? 33.652  16.887  -68.341  1.00 50.29  ? 312  GLU   D O   1 
ATOM   10300 C  CB  . GLU   D  1 11  ? 33.206  19.705  -66.625  1.00 55.46  ? 312  GLU   D CB  1 
ATOM   10301 C  CG  . GLU   D  1 11  ? 34.672  20.022  -66.819  1.00 56.01  ? 312  GLU   D CG  1 
ATOM   10302 C  CD  . GLU   D  1 11  ? 35.404  20.252  -65.512  1.00 61.96  ? 312  GLU   D CD  1 
ATOM   10303 O  OE1 . GLU   D  1 11  ? 34.824  20.875  -64.599  1.00 58.16  ? 312  GLU   D OE1 1 
ATOM   10304 O  OE2 . GLU   D  1 11  ? 36.563  19.794  -65.394  1.00 64.81  ? 312  GLU   D OE2 1 
ATOM   10305 N  N   . THR   D  1 12  ? 32.068  16.768  -66.745  1.00 43.27  ? 313  THR   D N   1 
ATOM   10306 C  CA  . THR   D  1 12  ? 32.307  15.372  -66.413  1.00 40.06  ? 313  THR   D CA  1 
ATOM   10307 C  C   . THR   D  1 12  ? 31.288  14.425  -67.023  1.00 49.13  ? 313  THR   D C   1 
ATOM   10308 O  O   . THR   D  1 12  ? 31.532  13.215  -67.037  1.00 53.37  ? 313  THR   D O   1 
ATOM   10309 C  CB  . THR   D  1 12  ? 32.316  15.166  -64.884  1.00 43.98  ? 313  THR   D CB  1 
ATOM   10310 O  OG1 . THR   D  1 12  ? 31.018  15.440  -64.348  1.00 43.97  ? 313  THR   D OG1 1 
ATOM   10311 C  CG2 . THR   D  1 12  ? 33.321  16.087  -64.209  1.00 42.88  ? 313  THR   D CG2 1 
ATOM   10312 N  N   . GLU   D  1 13  ? 30.162  14.935  -67.523  1.00 49.48  ? 314  GLU   D N   1 
ATOM   10313 C  CA  . GLU   D  1 13  ? 29.049  14.153  -68.067  1.00 45.39  ? 314  GLU   D CA  1 
ATOM   10314 C  C   . GLU   D  1 13  ? 28.303  13.349  -67.005  1.00 53.39  ? 314  GLU   D C   1 
ATOM   10315 O  O   . GLU   D  1 13  ? 27.426  12.546  -67.356  1.00 51.56  ? 314  GLU   D O   1 
ATOM   10316 C  CB  . GLU   D  1 13  ? 29.494  13.216  -69.197  1.00 60.19  ? 314  GLU   D CB  1 
ATOM   10317 C  CG  . GLU   D  1 13  ? 30.494  13.821  -70.165  1.00 63.82  ? 314  GLU   D CG  1 
ATOM   10318 C  CD  . GLU   D  1 13  ? 30.017  13.768  -71.591  1.00 79.99  ? 314  GLU   D CD  1 
ATOM   10319 O  OE1 . GLU   D  1 13  ? 28.977  14.399  -71.904  1.00 83.81  ? 314  GLU   D OE1 1 
ATOM   10320 O  OE2 . GLU   D  1 13  ? 30.682  13.085  -72.399  1.00 86.67  ? 314  GLU   D OE2 1 
ATOM   10321 N  N   . VAL   D  1 14  ? 28.596  13.560  -65.714  1.00 52.86  ? 315  VAL   D N   1 
ATOM   10322 C  CA  . VAL   D  1 14  ? 27.864  12.883  -64.651  1.00 54.27  ? 315  VAL   D CA  1 
ATOM   10323 C  C   . VAL   D  1 14  ? 26.421  13.366  -64.624  1.00 54.26  ? 315  VAL   D C   1 
ATOM   10324 O  O   . VAL   D  1 14  ? 26.145  14.569  -64.740  1.00 52.13  ? 315  VAL   D O   1 
ATOM   10325 C  CB  . VAL   D  1 14  ? 28.545  13.135  -63.296  1.00 57.37  ? 315  VAL   D CB  1 
ATOM   10326 C  CG1 . VAL   D  1 14  ? 27.707  12.561  -62.152  1.00 57.70  ? 315  VAL   D CG1 1 
ATOM   10327 C  CG2 . VAL   D  1 14  ? 29.946  12.555  -63.299  1.00 54.57  ? 315  VAL   D CG2 1 
ATOM   10328 N  N   . VAL   D  1 15  ? 25.487  12.436  -64.440  1.00 54.97  ? 316  VAL   D N   1 
ATOM   10329 C  CA  . VAL   D  1 15  ? 24.077  12.780  -64.315  1.00 54.53  ? 316  VAL   D CA  1 
ATOM   10330 C  C   . VAL   D  1 15  ? 23.551  12.279  -62.977  1.00 50.98  ? 316  VAL   D C   1 
ATOM   10331 O  O   . VAL   D  1 15  ? 23.808  11.136  -62.589  1.00 52.73  ? 316  VAL   D O   1 
ATOM   10332 C  CB  . VAL   D  1 15  ? 23.252  12.219  -65.483  1.00 55.46  ? 316  VAL   D CB  1 
ATOM   10333 C  CG1 . VAL   D  1 15  ? 21.803  12.693  -65.378  1.00 49.57  ? 316  VAL   D CG1 1 
ATOM   10334 C  CG2 . VAL   D  1 15  ? 23.885  12.641  -66.818  1.00 50.12  ? 316  VAL   D CG2 1 
ATOM   10335 N  N   . LEU   D  1 16  ? 22.819  13.146  -62.275  1.00 50.93  ? 317  LEU   D N   1 
ATOM   10336 C  CA  . LEU   D  1 16  ? 22.207  12.847  -60.989  1.00 43.80  ? 317  LEU   D CA  1 
ATOM   10337 C  C   . LEU   D  1 16  ? 20.700  13.038  -61.090  1.00 46.59  ? 317  LEU   D C   1 
ATOM   10338 O  O   . LEU   D  1 16  ? 20.215  13.915  -61.812  1.00 53.14  ? 317  LEU   D O   1 
ATOM   10339 C  CB  . LEU   D  1 16  ? 22.756  13.751  -59.880  1.00 43.48  ? 317  LEU   D CB  1 
ATOM   10340 C  CG  . LEU   D  1 16  ? 24.265  13.965  -59.880  1.00 45.34  ? 317  LEU   D CG  1 
ATOM   10341 C  CD1 . LEU   D  1 16  ? 24.684  15.086  -58.900  1.00 36.64  ? 317  LEU   D CD1 1 
ATOM   10342 C  CD2 . LEU   D  1 16  ? 24.952  12.645  -59.567  1.00 48.61  ? 317  LEU   D CD2 1 
ATOM   10343 N  N   . THR   D  1 17  ? 19.969  12.208  -60.356  1.00 46.40  ? 318  THR   D N   1 
ATOM   10344 C  CA  . THR   D  1 17  ? 18.516  12.151  -60.413  1.00 50.17  ? 318  THR   D CA  1 
ATOM   10345 C  C   . THR   D  1 17  ? 17.945  12.728  -59.124  1.00 51.90  ? 318  THR   D C   1 
ATOM   10346 O  O   . THR   D  1 17  ? 18.196  12.202  -58.037  1.00 50.56  ? 318  THR   D O   1 
ATOM   10347 C  CB  . THR   D  1 17  ? 18.046  10.711  -60.617  1.00 50.15  ? 318  THR   D CB  1 
ATOM   10348 O  OG1 . THR   D  1 17  ? 18.758  10.140  -61.719  1.00 48.60  ? 318  THR   D OG1 1 
ATOM   10349 C  CG2 . THR   D  1 17  ? 16.557  10.662  -60.894  1.00 45.38  ? 318  THR   D CG2 1 
ATOM   10350 N  N   . ASP   D  1 18  ? 17.182  13.803  -59.249  1.00 50.61  ? 319  ASP   D N   1 
ATOM   10351 C  CA  . ASP   D  1 18  ? 16.649  14.516  -58.102  1.00 44.73  ? 319  ASP   D CA  1 
ATOM   10352 C  C   . ASP   D  1 18  ? 15.220  14.052  -57.855  1.00 51.62  ? 319  ASP   D C   1 
ATOM   10353 O  O   . ASP   D  1 18  ? 14.329  14.297  -58.674  1.00 51.88  ? 319  ASP   D O   1 
ATOM   10354 C  CB  . ASP   D  1 18  ? 16.712  16.019  -58.335  1.00 41.96  ? 319  ASP   D CB  1 
ATOM   10355 C  CG  . ASP   D  1 18  ? 16.343  16.813  -57.101  1.00 46.62  ? 319  ASP   D CG  1 
ATOM   10356 O  OD1 . ASP   D  1 18  ? 15.166  16.743  -56.681  1.00 49.38  ? 319  ASP   D OD1 1 
ATOM   10357 O  OD2 . ASP   D  1 18  ? 17.234  17.501  -56.551  1.00 49.14  ? 319  ASP   D OD2 1 
ATOM   10358 N  N   . THR   D  1 19  ? 15.016  13.362  -56.735  1.00 48.80  ? 320  THR   D N   1 
ATOM   10359 C  CA  . THR   D  1 19  ? 13.685  13.095  -56.207  1.00 50.98  ? 320  THR   D CA  1 
ATOM   10360 C  C   . THR   D  1 19  ? 13.296  14.031  -55.069  1.00 53.30  ? 320  THR   D C   1 
ATOM   10361 O  O   . THR   D  1 19  ? 12.098  14.233  -54.840  1.00 49.94  ? 320  THR   D O   1 
ATOM   10362 C  CB  . THR   D  1 19  ? 13.602  11.664  -55.682  1.00 46.63  ? 320  THR   D CB  1 
ATOM   10363 O  OG1 . THR   D  1 19  ? 14.584  11.518  -54.648  1.00 51.34  ? 320  THR   D OG1 1 
ATOM   10364 C  CG2 . THR   D  1 19  ? 13.869  10.657  -56.789  1.00 40.33  ? 320  THR   D CG2 1 
ATOM   10365 N  N   . LEU   D  1 20  ? 14.278  14.613  -54.369  1.00 44.68  ? 321  LEU   D N   1 
ATOM   10366 C  CA  . LEU   D  1 20  ? 13.999  15.353  -53.142  1.00 41.91  ? 321  LEU   D CA  1 
ATOM   10367 C  C   . LEU   D  1 20  ? 13.104  16.567  -53.386  1.00 49.39  ? 321  LEU   D C   1 
ATOM   10368 O  O   . LEU   D  1 20  ? 12.373  16.986  -52.477  1.00 40.09  ? 321  LEU   D O   1 
ATOM   10369 C  CB  . LEU   D  1 20  ? 15.316  15.770  -52.484  1.00 35.15  ? 321  LEU   D CB  1 
ATOM   10370 C  CG  . LEU   D  1 20  ? 15.251  16.584  -51.172  1.00 43.07  ? 321  LEU   D CG  1 
ATOM   10371 C  CD1 . LEU   D  1 20  ? 14.486  15.838  -50.056  1.00 35.11  ? 321  LEU   D CD1 1 
ATOM   10372 C  CD2 . LEU   D  1 20  ? 16.647  16.977  -50.697  1.00 37.85  ? 321  LEU   D CD2 1 
ATOM   10373 N  N   . HIS   D  1 21  ? 13.124  17.129  -54.602  1.00 45.10  ? 322  HIS   D N   1 
ATOM   10374 C  CA  . HIS   D  1 21  ? 12.327  18.316  -54.902  1.00 39.11  ? 322  HIS   D CA  1 
ATOM   10375 C  C   . HIS   D  1 21  ? 10.840  18.072  -54.723  1.00 41.35  ? 322  HIS   D C   1 
ATOM   10376 O  O   . HIS   D  1 21  ? 10.078  19.033  -54.589  1.00 41.10  ? 322  HIS   D O   1 
ATOM   10377 C  CB  . HIS   D  1 21  ? 12.568  18.778  -56.339  1.00 44.28  ? 322  HIS   D CB  1 
ATOM   10378 C  CG  . HIS   D  1 21  ? 12.006  17.839  -57.358  1.00 43.80  ? 322  HIS   D CG  1 
ATOM   10379 N  ND1 . HIS   D  1 21  ? 12.671  16.702  -57.767  1.00 45.13  ? 322  HIS   D ND1 1 
ATOM   10380 C  CD2 . HIS   D  1 21  ? 10.826  17.840  -58.015  1.00 45.59  ? 322  HIS   D CD2 1 
ATOM   10381 C  CE1 . HIS   D  1 21  ? 11.930  16.052  -58.648  1.00 46.12  ? 322  HIS   D CE1 1 
ATOM   10382 N  NE2 . HIS   D  1 21  ? 10.805  16.720  -58.813  1.00 48.06  ? 322  HIS   D NE2 1 
ATOM   10383 N  N   . LEU   D  1 22  ? 10.410  16.811  -54.747  1.00 47.55  ? 323  LEU   D N   1 
ATOM   10384 C  CA  . LEU   D  1 22  ? 9.010   16.478  -54.502  1.00 52.40  ? 323  LEU   D CA  1 
ATOM   10385 C  C   . LEU   D  1 22  ? 8.552   16.859  -53.098  1.00 57.93  ? 323  LEU   D C   1 
ATOM   10386 O  O   . LEU   D  1 22  ? 7.349   17.037  -52.871  1.00 57.68  ? 323  LEU   D O   1 
ATOM   10387 C  CB  . LEU   D  1 22  ? 8.798   14.982  -54.734  1.00 50.64  ? 323  LEU   D CB  1 
ATOM   10388 C  CG  . LEU   D  1 22  ? 9.031   14.566  -56.181  1.00 56.58  ? 323  LEU   D CG  1 
ATOM   10389 C  CD1 . LEU   D  1 22  ? 9.248   13.071  -56.282  1.00 54.47  ? 323  LEU   D CD1 1 
ATOM   10390 C  CD2 . LEU   D  1 22  ? 7.839   15.003  -57.016  1.00 56.08  ? 323  LEU   D CD2 1 
ATOM   10391 N  N   . LYS   D  1 23  ? 9.476   17.001  -52.153  1.00 58.48  ? 324  LYS   D N   1 
ATOM   10392 C  CA  . LYS   D  1 23  ? 9.120   17.287  -50.775  1.00 58.61  ? 324  LYS   D CA  1 
ATOM   10393 C  C   . LYS   D  1 23  ? 9.254   18.759  -50.426  1.00 62.03  ? 324  LYS   D C   1 
ATOM   10394 O  O   . LYS   D  1 23  ? 9.298   19.100  -49.241  1.00 69.73  ? 324  LYS   D O   1 
ATOM   10395 C  CB  . LYS   D  1 23  ? 9.957   16.424  -49.831  1.00 61.67  ? 324  LYS   D CB  1 
ATOM   10396 C  CG  . LYS   D  1 23  ? 9.455   14.984  -49.782  1.00 72.50  ? 324  LYS   D CG  1 
ATOM   10397 C  CD  . LYS   D  1 23  ? 8.957   14.589  -48.402  1.00 83.42  ? 324  LYS   D CD  1 
ATOM   10398 C  CE  . LYS   D  1 23  ? 10.110  14.031  -47.606  1.00 93.74  ? 324  LYS   D CE  1 
ATOM   10399 N  NZ  . LYS   D  1 23  ? 11.028  13.303  -48.536  1.00 97.10  ? 324  LYS   D NZ  1 
ATOM   10400 N  N   . SER   D  1 24  ? 9.304   19.640  -51.421  1.00 60.31  ? 325  SER   D N   1 
ATOM   10401 C  CA  . SER   D  1 24  ? 9.314   21.073  -51.165  1.00 64.05  ? 325  SER   D CA  1 
ATOM   10402 C  C   . SER   D  1 24  ? 7.895   21.608  -51.275  1.00 67.02  ? 325  SER   D C   1 
ATOM   10403 O  O   . SER   D  1 24  ? 7.099   21.106  -52.070  1.00 68.22  ? 325  SER   D O   1 
ATOM   10404 C  CB  . SER   D  1 24  ? 10.241  21.813  -52.135  1.00 61.52  ? 325  SER   D CB  1 
ATOM   10405 O  OG  . SER   D  1 24  ? 9.693   21.878  -53.434  1.00 63.79  ? 325  SER   D OG  1 
ATOM   10406 N  N   . THR   D  1 25  ? 7.571   22.610  -50.450  1.00 77.38  ? 326  THR   D N   1 
ATOM   10407 C  CA  . THR   D  1 25  ? 6.246   23.217  -50.511  1.00 88.89  ? 326  THR   D CA  1 
ATOM   10408 C  C   . THR   D  1 25  ? 6.288   24.731  -50.354  1.00 85.57  ? 326  THR   D C   1 
ATOM   10409 O  O   . THR   D  1 25  ? 5.235   25.344  -50.150  1.00 90.49  ? 326  THR   D O   1 
ATOM   10410 C  CB  . THR   D  1 25  ? 5.304   22.629  -49.449  1.00 97.79  ? 326  THR   D CB  1 
ATOM   10411 O  OG1 . THR   D  1 25  ? 6.038   21.750  -48.586  1.00 104.00 ? 326  THR   D OG1 1 
ATOM   10412 C  CG2 . THR   D  1 25  ? 4.132   21.877  -50.110  1.00 93.75  ? 326  THR   D CG2 1 
ATOM   10413 N  N   . LEU   D  1 26  ? 7.457   25.346  -50.436  1.00 76.57  ? 327  LEU   D N   1 
ATOM   10414 C  CA  . LEU   D  1 26  ? 7.581   26.792  -50.406  1.00 77.69  ? 327  LEU   D CA  1 
ATOM   10415 C  C   . LEU   D  1 26  ? 7.960   27.291  -51.799  1.00 79.60  ? 327  LEU   D C   1 
ATOM   10416 O  O   . LEU   D  1 26  ? 8.555   26.560  -52.599  1.00 84.35  ? 327  LEU   D O   1 
ATOM   10417 C  CB  . LEU   D  1 26  ? 8.617   27.225  -49.356  1.00 73.46  ? 327  LEU   D CB  1 
ATOM   10418 C  CG  . LEU   D  1 26  ? 8.387   26.795  -47.893  1.00 68.71  ? 327  LEU   D CG  1 
ATOM   10419 C  CD1 . LEU   D  1 26  ? 9.494   27.296  -46.951  1.00 67.36  ? 327  LEU   D CD1 1 
ATOM   10420 C  CD2 . LEU   D  1 26  ? 7.029   27.264  -47.400  1.00 64.00  ? 327  LEU   D CD2 1 
ATOM   10421 N  N   . GLU   D  1 27  ? 7.606   28.541  -52.089  1.00 73.70  ? 328  GLU   D N   1 
ATOM   10422 C  CA  . GLU   D  1 27  ? 7.745   29.070  -53.440  1.00 67.71  ? 328  GLU   D CA  1 
ATOM   10423 C  C   . GLU   D  1 27  ? 9.185   29.454  -53.771  1.00 68.89  ? 328  GLU   D C   1 
ATOM   10424 O  O   . GLU   D  1 27  ? 9.969   29.840  -52.899  1.00 73.12  ? 328  GLU   D O   1 
ATOM   10425 C  CB  . GLU   D  1 27  ? 6.855   30.292  -53.629  1.00 67.55  ? 328  GLU   D CB  1 
ATOM   10426 C  CG  . GLU   D  1 27  ? 5.389   29.974  -53.775  1.00 77.34  ? 328  GLU   D CG  1 
ATOM   10427 C  CD  . GLU   D  1 27  ? 4.613   31.140  -54.337  1.00 91.86  ? 328  GLU   D CD  1 
ATOM   10428 O  OE1 . GLU   D  1 27  ? 3.498   30.911  -54.853  1.00 100.28 ? 328  GLU   D OE1 1 
ATOM   10429 O  OE2 . GLU   D  1 27  ? 5.124   32.282  -54.273  1.00 94.76  ? 328  GLU   D OE2 1 
ATOM   10430 N  N   . THR   D  1 28  ? 9.523   29.337  -55.060  1.00 60.82  ? 329  THR   D N   1 
ATOM   10431 C  CA  . THR   D  1 28  ? 10.754  29.889  -55.613  1.00 50.27  ? 329  THR   D CA  1 
ATOM   10432 C  C   . THR   D  1 28  ? 10.573  31.301  -56.143  1.00 43.81  ? 329  THR   D C   1 
ATOM   10433 O  O   . THR   D  1 28  ? 11.559  32.023  -56.293  1.00 52.03  ? 329  THR   D O   1 
ATOM   10434 C  CB  . THR   D  1 28  ? 11.280  29.021  -56.768  1.00 51.82  ? 329  THR   D CB  1 
ATOM   10435 O  OG1 . THR   D  1 28  ? 10.324  28.992  -57.854  1.00 43.18  ? 329  THR   D OG1 1 
ATOM   10436 C  CG2 . THR   D  1 28  ? 11.576  27.607  -56.293  1.00 51.66  ? 329  THR   D CG2 1 
ATOM   10437 N  N   . GLY   D  1 29  ? 9.347   31.700  -56.454  1.00 39.21  ? 330  GLY   D N   1 
ATOM   10438 C  CA  . GLY   D  1 29  ? 9.093   32.956  -57.106  1.00 45.79  ? 330  GLY   D CA  1 
ATOM   10439 C  C   . GLY   D  1 29  ? 9.003   32.861  -58.613  1.00 53.86  ? 330  GLY   D C   1 
ATOM   10440 O  O   . GLY   D  1 29  ? 8.424   33.752  -59.241  1.00 64.15  ? 330  GLY   D O   1 
ATOM   10441 N  N   . CYS   D  1 30  ? 9.552   31.807  -59.208  1.00 45.22  ? 331  CYS   D N   1 
ATOM   10442 C  CA  . CYS   D  1 30  ? 9.357   31.587  -60.635  1.00 42.77  ? 331  CYS   D CA  1 
ATOM   10443 C  C   . CYS   D  1 30  ? 7.931   31.126  -60.905  1.00 46.33  ? 331  CYS   D C   1 
ATOM   10444 O  O   . CYS   D  1 30  ? 7.293   30.494  -60.064  1.00 50.45  ? 331  CYS   D O   1 
ATOM   10445 C  CB  . CYS   D  1 30  ? 10.338  30.537  -61.161  1.00 35.33  ? 331  CYS   D CB  1 
ATOM   10446 S  SG  . CYS   D  1 30  ? 12.085  30.953  -61.042  1.00 43.02  ? 331  CYS   D SG  1 
ATOM   10447 N  N   . THR   D  1 31  ? 7.429   31.452  -62.090  1.00 47.92  ? 332  THR   D N   1 
ATOM   10448 C  CA  . THR   D  1 31  ? 6.178   30.902  -62.589  1.00 49.94  ? 332  THR   D CA  1 
ATOM   10449 C  C   . THR   D  1 31  ? 6.494   29.910  -63.702  1.00 44.77  ? 332  THR   D C   1 
ATOM   10450 O  O   . THR   D  1 31  ? 7.654   29.702  -64.072  1.00 49.94  ? 332  THR   D O   1 
ATOM   10451 C  CB  . THR   D  1 31  ? 5.232   32.005  -63.086  1.00 58.14  ? 332  THR   D CB  1 
ATOM   10452 O  OG1 . THR   D  1 31  ? 5.648   32.454  -64.383  1.00 66.72  ? 332  THR   D OG1 1 
ATOM   10453 C  CG2 . THR   D  1 31  ? 5.206   33.192  -62.116  1.00 53.09  ? 332  THR   D CG2 1 
ATOM   10454 N  N   . GLU   D  1 32  ? 5.451   29.288  -64.246  1.00 46.37  ? 333  GLU   D N   1 
ATOM   10455 C  CA  . GLU   D  1 32  ? 5.683   28.362  -65.349  1.00 55.94  ? 333  GLU   D CA  1 
ATOM   10456 C  C   . GLU   D  1 32  ? 6.174   29.073  -66.610  1.00 56.16  ? 333  GLU   D C   1 
ATOM   10457 O  O   . GLU   D  1 32  ? 6.800   28.430  -67.462  1.00 55.21  ? 333  GLU   D O   1 
ATOM   10458 C  CB  . GLU   D  1 32  ? 4.417   27.547  -65.628  1.00 69.07  ? 333  GLU   D CB  1 
ATOM   10459 C  CG  . GLU   D  1 32  ? 4.608   26.039  -65.415  1.00 81.82  ? 333  GLU   D CG  1 
ATOM   10460 C  CD  . GLU   D  1 32  ? 3.343   25.317  -64.963  1.00 86.97  ? 333  GLU   D CD  1 
ATOM   10461 O  OE1 . GLU   D  1 32  ? 2.276   25.969  -64.891  1.00 88.64  ? 333  GLU   D OE1 1 
ATOM   10462 O  OE2 . GLU   D  1 32  ? 3.425   24.097  -64.677  1.00 83.65  ? 333  GLU   D OE2 1 
ATOM   10463 N  N   . TYR   D  1 33  ? 5.946   30.387  -66.736  1.00 48.28  ? 334  TYR   D N   1 
ATOM   10464 C  CA  . TYR   D  1 33  ? 6.356   31.117  -67.926  1.00 45.06  ? 334  TYR   D CA  1 
ATOM   10465 C  C   . TYR   D  1 33  ? 7.359   32.230  -67.671  1.00 43.17  ? 334  TYR   D C   1 
ATOM   10466 O  O   . TYR   D  1 33  ? 7.740   32.907  -68.626  1.00 42.83  ? 334  TYR   D O   1 
ATOM   10467 C  CB  . TYR   D  1 33  ? 5.132   31.704  -68.655  1.00 48.22  ? 334  TYR   D CB  1 
ATOM   10468 C  CG  . TYR   D  1 33  ? 4.224   30.644  -69.255  1.00 60.01  ? 334  TYR   D CG  1 
ATOM   10469 C  CD1 . TYR   D  1 33  ? 4.541   30.026  -70.461  1.00 61.34  ? 334  TYR   D CD1 1 
ATOM   10470 C  CD2 . TYR   D  1 33  ? 3.061   30.247  -68.607  1.00 62.38  ? 334  TYR   D CD2 1 
ATOM   10471 C  CE1 . TYR   D  1 33  ? 3.721   29.047  -71.003  1.00 67.37  ? 334  TYR   D CE1 1 
ATOM   10472 C  CE2 . TYR   D  1 33  ? 2.237   29.275  -69.143  1.00 63.84  ? 334  TYR   D CE2 1 
ATOM   10473 C  CZ  . TYR   D  1 33  ? 2.569   28.676  -70.339  1.00 68.75  ? 334  TYR   D CZ  1 
ATOM   10474 O  OH  . TYR   D  1 33  ? 1.751   27.701  -70.879  1.00 70.91  ? 334  TYR   D OH  1 
ATOM   10475 N  N   . ILE   D  1 34  ? 7.794   32.455  -66.433  1.00 49.30  ? 335  ILE   D N   1 
ATOM   10476 C  CA  . ILE   D  1 34  ? 8.841   33.432  -66.149  1.00 43.40  ? 335  ILE   D CA  1 
ATOM   10477 C  C   . ILE   D  1 34  ? 9.812   32.803  -65.164  1.00 47.72  ? 335  ILE   D C   1 
ATOM   10478 O  O   . ILE   D  1 34  ? 9.389   32.136  -64.214  1.00 48.96  ? 335  ILE   D O   1 
ATOM   10479 C  CB  . ILE   D  1 34  ? 8.269   34.758  -65.591  1.00 48.53  ? 335  ILE   D CB  1 
ATOM   10480 C  CG1 . ILE   D  1 34  ? 7.314   35.423  -66.589  1.00 61.10  ? 335  ILE   D CG1 1 
ATOM   10481 C  CG2 . ILE   D  1 34  ? 9.389   35.746  -65.304  1.00 47.45  ? 335  ILE   D CG2 1 
ATOM   10482 C  CD1 . ILE   D  1 34  ? 5.845   35.118  -66.387  1.00 68.27  ? 335  ILE   D CD1 1 
ATOM   10483 N  N   . CYS   D  1 35  ? 11.115  32.980  -65.399  1.00 43.21  ? 336  CYS   D N   1 
ATOM   10484 C  CA  . CYS   D  1 35  ? 12.128  32.579  -64.426  1.00 42.21  ? 336  CYS   D CA  1 
ATOM   10485 C  C   . CYS   D  1 35  ? 12.631  33.816  -63.702  1.00 43.52  ? 336  CYS   D C   1 
ATOM   10486 O  O   . CYS   D  1 35  ? 12.992  34.809  -64.343  1.00 44.25  ? 336  CYS   D O   1 
ATOM   10487 C  CB  . CYS   D  1 35  ? 13.305  31.840  -65.069  1.00 41.10  ? 336  CYS   D CB  1 
ATOM   10488 S  SG  . CYS   D  1 35  ? 14.631  31.371  -63.874  1.00 41.10  ? 336  CYS   D SG  1 
ATOM   10489 N  N   . MET   D  1 36  ? 12.637  33.754  -62.366  1.00 45.36  ? 337  MET   D N   1 
ATOM   10490 C  CA  . MET   D  1 36  ? 13.120  34.834  -61.509  1.00 45.90  ? 337  MET   D CA  1 
ATOM   10491 C  C   . MET   D  1 36  ? 14.375  34.446  -60.740  1.00 43.15  ? 337  MET   D C   1 
ATOM   10492 O  O   . MET   D  1 36  ? 14.725  35.104  -59.755  1.00 36.72  ? 337  MET   D O   1 
ATOM   10493 C  CB  . MET   D  1 36  ? 12.009  35.286  -60.560  1.00 48.83  ? 337  MET   D CB  1 
ATOM   10494 C  CG  . MET   D  1 36  ? 10.774  35.710  -61.331  1.00 58.14  ? 337  MET   D CG  1 
ATOM   10495 S  SD  . MET   D  1 36  ? 9.603   36.684  -60.401  1.00 67.61  ? 337  MET   D SD  1 
ATOM   10496 C  CE  . MET   D  1 36  ? 10.541  38.172  -60.097  1.00 77.62  ? 337  MET   D CE  1 
ATOM   10497 N  N   . GLY   D  1 37  ? 15.079  33.417  -61.209  1.00 36.31  ? 338  GLY   D N   1 
ATOM   10498 C  CA  . GLY   D  1 37  ? 16.304  32.896  -60.622  1.00 35.74  ? 338  GLY   D CA  1 
ATOM   10499 C  C   . GLY   D  1 37  ? 17.439  33.844  -60.270  1.00 37.51  ? 338  GLY   D C   1 
ATOM   10500 O  O   . GLY   D  1 37  ? 18.337  33.425  -59.526  1.00 47.89  ? 338  GLY   D O   1 
ATOM   10501 N  N   . SER   D  1 38  ? 17.442  35.088  -60.776  1.00 34.09  ? 339  SER   D N   1 
ATOM   10502 C  CA  . SER   D  1 38  ? 18.433  36.099  -60.394  1.00 35.45  ? 339  SER   D CA  1 
ATOM   10503 C  C   . SER   D  1 38  ? 17.853  37.261  -59.594  1.00 40.45  ? 339  SER   D C   1 
ATOM   10504 O  O   . SER   D  1 38  ? 18.572  38.227  -59.322  1.00 46.53  ? 339  SER   D O   1 
ATOM   10505 C  CB  . SER   D  1 38  ? 19.151  36.659  -61.630  1.00 40.06  ? 339  SER   D CB  1 
ATOM   10506 O  OG  . SER   D  1 38  ? 18.269  37.365  -62.506  1.00 37.66  ? 339  SER   D OG  1 
ATOM   10507 N  N   . ILE   D  1 39  ? 16.575  37.203  -59.226  1.00 39.72  ? 340  ILE   D N   1 
ATOM   10508 C  CA  . ILE   D  1 39  ? 16.015  38.168  -58.285  1.00 40.11  ? 340  ILE   D CA  1 
ATOM   10509 C  C   . ILE   D  1 39  ? 16.542  37.854  -56.887  1.00 41.17  ? 340  ILE   D C   1 
ATOM   10510 O  O   . ILE   D  1 39  ? 16.485  36.701  -56.432  1.00 37.47  ? 340  ILE   D O   1 
ATOM   10511 C  CB  . ILE   D  1 39  ? 14.480  38.122  -58.325  1.00 43.19  ? 340  ILE   D CB  1 
ATOM   10512 C  CG1 . ILE   D  1 39  ? 13.965  38.200  -59.771  1.00 47.26  ? 340  ILE   D CG1 1 
ATOM   10513 C  CG2 . ILE   D  1 39  ? 13.879  39.198  -57.437  1.00 44.32  ? 340  ILE   D CG2 1 
ATOM   10514 C  CD1 . ILE   D  1 39  ? 14.312  39.451  -60.511  1.00 43.56  ? 340  ILE   D CD1 1 
ATOM   10515 N  N   . MET   D  1 40  ? 17.054  38.877  -56.193  1.00 40.58  ? 341  MET   D N   1 
ATOM   10516 C  CA  . MET   D  1 40  ? 17.652  38.626  -54.880  1.00 47.92  ? 341  MET   D CA  1 
ATOM   10517 C  C   . MET   D  1 40  ? 16.605  38.236  -53.836  1.00 46.41  ? 341  MET   D C   1 
ATOM   10518 O  O   . MET   D  1 40  ? 16.794  37.260  -53.104  1.00 46.33  ? 341  MET   D O   1 
ATOM   10519 C  CB  . MET   D  1 40  ? 18.460  39.825  -54.397  1.00 56.59  ? 341  MET   D CB  1 
ATOM   10520 C  CG  . MET   D  1 40  ? 19.334  39.452  -53.196  1.00 69.91  ? 341  MET   D CG  1 
ATOM   10521 S  SD  . MET   D  1 40  ? 20.641  40.631  -52.836  1.00 82.69  ? 341  MET   D SD  1 
ATOM   10522 C  CE  . MET   D  1 40  ? 21.582  40.608  -54.353  1.00 72.99  ? 341  MET   D CE  1 
ATOM   10523 N  N   . HIS   D  1 41  ? 15.496  38.977  -53.745  1.00 48.63  ? 342  HIS   D N   1 
ATOM   10524 C  CA  . HIS   D  1 41  ? 14.412  38.662  -52.810  1.00 51.10  ? 342  HIS   D CA  1 
ATOM   10525 C  C   . HIS   D  1 41  ? 13.101  38.523  -53.575  1.00 56.41  ? 342  HIS   D C   1 
ATOM   10526 O  O   . HIS   D  1 41  ? 12.389  39.518  -53.777  1.00 56.34  ? 342  HIS   D O   1 
ATOM   10527 C  CB  . HIS   D  1 41  ? 14.272  39.743  -51.733  1.00 62.19  ? 342  HIS   D CB  1 
ATOM   10528 C  CG  . HIS   D  1 41  ? 15.540  40.064  -50.996  1.00 73.51  ? 342  HIS   D CG  1 
ATOM   10529 N  ND1 . HIS   D  1 41  ? 15.896  41.355  -50.662  1.00 75.83  ? 342  HIS   D ND1 1 
ATOM   10530 C  CD2 . HIS   D  1 41  ? 16.521  39.267  -50.505  1.00 76.36  ? 342  HIS   D CD2 1 
ATOM   10531 C  CE1 . HIS   D  1 41  ? 17.049  41.339  -50.016  1.00 75.66  ? 342  HIS   D CE1 1 
ATOM   10532 N  NE2 . HIS   D  1 41  ? 17.451  40.085  -49.909  1.00 73.96  ? 342  HIS   D NE2 1 
ATOM   10533 N  N   . PRO   D  1 42  ? 12.736  37.324  -54.032  1.00 64.96  ? 343  PRO   D N   1 
ATOM   10534 C  CA  . PRO   D  1 42  ? 11.426  37.167  -54.681  1.00 70.86  ? 343  PRO   D CA  1 
ATOM   10535 C  C   . PRO   D  1 42  ? 10.321  37.048  -53.642  1.00 81.16  ? 343  PRO   D C   1 
ATOM   10536 O  O   . PRO   D  1 42  ? 10.499  36.446  -52.579  1.00 83.20  ? 343  PRO   D O   1 
ATOM   10537 C  CB  . PRO   D  1 42  ? 11.572  35.871  -55.495  1.00 65.35  ? 343  PRO   D CB  1 
ATOM   10538 C  CG  . PRO   D  1 42  ? 13.041  35.511  -55.437  1.00 65.81  ? 343  PRO   D CG  1 
ATOM   10539 C  CD  . PRO   D  1 42  ? 13.543  36.102  -54.148  1.00 61.60  ? 343  PRO   D CD  1 
ATOM   10540 N  N   . SER   D  1 43  ? 9.176   37.646  -53.950  1.00 87.10  ? 344  SER   D N   1 
ATOM   10541 C  CA  . SER   D  1 43  ? 8.039   37.595  -53.038  1.00 93.52  ? 344  SER   D CA  1 
ATOM   10542 C  C   . SER   D  1 43  ? 7.089   36.472  -53.429  1.00 97.82  ? 344  SER   D C   1 
ATOM   10543 O  O   . SER   D  1 43  ? 6.224   36.087  -52.646  1.00 102.65 ? 344  SER   D O   1 
ATOM   10544 C  CB  . SER   D  1 43  ? 7.289   38.928  -53.018  1.00 91.08  ? 344  SER   D CB  1 
ATOM   10545 O  OG  . SER   D  1 43  ? 6.433   39.049  -54.141  1.00 85.83  ? 344  SER   D OG  1 
ATOM   10546 N  N   . PRO   D  1 49  ? 4.653   42.612  -37.776  1.00 128.58 ? 350  PRO   D N   1 
ATOM   10547 C  CA  . PRO   D  1 49  ? 4.103   42.401  -36.431  1.00 131.72 ? 350  PRO   D CA  1 
ATOM   10548 C  C   . PRO   D  1 49  ? 3.065   41.278  -36.382  1.00 135.54 ? 350  PRO   D C   1 
ATOM   10549 O  O   . PRO   D  1 49  ? 3.313   40.243  -35.763  1.00 132.37 ? 350  PRO   D O   1 
ATOM   10550 C  CB  . PRO   D  1 49  ? 3.473   43.757  -36.102  1.00 129.98 ? 350  PRO   D CB  1 
ATOM   10551 C  CG  . PRO   D  1 49  ? 4.339   44.735  -36.832  1.00 127.83 ? 350  PRO   D CG  1 
ATOM   10552 C  CD  . PRO   D  1 49  ? 4.753   44.045  -38.114  1.00 126.81 ? 350  PRO   D CD  1 
ATOM   10553 N  N   . GLU   D  1 50  ? 1.915   41.476  -37.031  1.00 143.23 ? 351  GLU   D N   1 
ATOM   10554 C  CA  . GLU   D  1 50  ? 0.906   40.430  -37.150  1.00 145.93 ? 351  GLU   D CA  1 
ATOM   10555 C  C   . GLU   D  1 50  ? 1.281   39.367  -38.186  1.00 142.19 ? 351  GLU   D C   1 
ATOM   10556 O  O   . GLU   D  1 50  ? 0.399   38.636  -38.655  1.00 139.22 ? 351  GLU   D O   1 
ATOM   10557 C  CB  . GLU   D  1 50  ? -0.461  41.036  -37.493  1.00 148.33 ? 351  GLU   D CB  1 
ATOM   10558 C  CG  . GLU   D  1 50  ? -1.303  41.467  -36.285  1.00 147.08 ? 351  GLU   D CG  1 
ATOM   10559 C  CD  . GLU   D  1 50  ? -0.921  42.832  -35.747  1.00 144.49 ? 351  GLU   D CD  1 
ATOM   10560 O  OE1 . GLU   D  1 50  ? 0.130   42.948  -35.077  1.00 142.14 ? 351  GLU   D OE1 1 
ATOM   10561 O  OE2 . GLU   D  1 50  ? -1.680  43.791  -36.002  1.00 144.22 ? 351  GLU   D OE2 1 
ATOM   10562 N  N   . ASP   D  1 51  ? 2.562   39.277  -38.557  1.00 141.42 ? 352  ASP   D N   1 
ATOM   10563 C  CA  . ASP   D  1 51  ? 3.071   38.180  -39.381  1.00 138.10 ? 352  ASP   D CA  1 
ATOM   10564 C  C   . ASP   D  1 51  ? 3.321   36.952  -38.500  1.00 128.99 ? 352  ASP   D C   1 
ATOM   10565 O  O   . ASP   D  1 51  ? 4.435   36.440  -38.391  1.00 131.78 ? 352  ASP   D O   1 
ATOM   10566 C  CB  . ASP   D  1 51  ? 4.344   38.597  -40.112  1.00 140.30 ? 352  ASP   D CB  1 
ATOM   10567 C  CG  . ASP   D  1 51  ? 4.326   40.053  -40.553  1.00 142.22 ? 352  ASP   D CG  1 
ATOM   10568 O  OD1 . ASP   D  1 51  ? 3.468   40.425  -41.385  1.00 142.86 ? 352  ASP   D OD1 1 
ATOM   10569 O  OD2 . ASP   D  1 51  ? 5.176   40.828  -40.061  1.00 141.47 ? 352  ASP   D OD2 1 
ATOM   10570 N  N   . VAL   D  1 52  ? 2.252   36.488  -37.853  1.00 111.22 ? 353  VAL   D N   1 
ATOM   10571 C  CA  . VAL   D  1 52  ? 2.331   35.423  -36.859  1.00 92.32  ? 353  VAL   D CA  1 
ATOM   10572 C  C   . VAL   D  1 52  ? 1.282   34.371  -37.178  1.00 75.06  ? 353  VAL   D C   1 
ATOM   10573 O  O   . VAL   D  1 52  ? 0.094   34.691  -37.312  1.00 72.33  ? 353  VAL   D O   1 
ATOM   10574 C  CB  . VAL   D  1 52  ? 2.144   35.957  -35.427  1.00 91.79  ? 353  VAL   D CB  1 
ATOM   10575 C  CG1 . VAL   D  1 52  ? 3.422   36.630  -34.958  1.00 84.87  ? 353  VAL   D CG1 1 
ATOM   10576 C  CG2 . VAL   D  1 52  ? 0.959   36.923  -35.360  1.00 95.23  ? 353  VAL   D CG2 1 
ATOM   10577 N  N   . ALA   D  1 53  ? 1.722   33.118  -37.278  1.00 60.74  ? 354  ALA   D N   1 
ATOM   10578 C  CA  . ALA   D  1 53  ? 0.862   32.053  -37.770  1.00 60.58  ? 354  ALA   D CA  1 
ATOM   10579 C  C   . ALA   D  1 53  ? -0.308  31.813  -36.824  1.00 68.82  ? 354  ALA   D C   1 
ATOM   10580 O  O   . ALA   D  1 53  ? -0.181  31.942  -35.605  1.00 76.08  ? 354  ALA   D O   1 
ATOM   10581 C  CB  . ALA   D  1 53  ? 1.674   30.772  -37.958  1.00 55.78  ? 354  ALA   D CB  1 
ATOM   10582 N  N   . THR   D  1 54  ? -1.461  31.476  -37.393  1.00 73.04  ? 355  THR   D N   1 
ATOM   10583 C  CA  . THR   D  1 54  ? -2.612  31.157  -36.565  1.00 76.21  ? 355  THR   D CA  1 
ATOM   10584 C  C   . THR   D  1 54  ? -2.494  29.736  -36.024  1.00 81.34  ? 355  THR   D C   1 
ATOM   10585 O  O   . THR   D  1 54  ? -1.587  28.978  -36.381  1.00 82.75  ? 355  THR   D O   1 
ATOM   10586 C  CB  . THR   D  1 54  ? -3.912  31.303  -37.350  1.00 75.08  ? 355  THR   D CB  1 
ATOM   10587 O  OG1 . THR   D  1 54  ? -3.960  30.310  -38.385  1.00 83.65  ? 355  THR   D OG1 1 
ATOM   10588 C  CG2 . THR   D  1 54  ? -4.006  32.689  -37.965  1.00 74.44  ? 355  THR   D CG2 1 
ATOM   10589 N  N   . LYS   D  1 55  ? -3.435  29.376  -35.149  1.00 86.21  ? 356  LYS   D N   1 
ATOM   10590 C  CA  . LYS   D  1 55  ? -3.463  28.019  -34.614  1.00 84.07  ? 356  LYS   D CA  1 
ATOM   10591 C  C   . LYS   D  1 55  ? -3.579  26.998  -35.736  1.00 81.82  ? 356  LYS   D C   1 
ATOM   10592 O  O   . LYS   D  1 55  ? -2.858  25.995  -35.755  1.00 75.03  ? 356  LYS   D O   1 
ATOM   10593 C  CB  . LYS   D  1 55  ? -4.623  27.859  -33.633  1.00 82.04  ? 356  LYS   D CB  1 
ATOM   10594 C  CG  . LYS   D  1 55  ? -4.235  27.914  -32.179  1.00 79.23  ? 356  LYS   D CG  1 
ATOM   10595 C  CD  . LYS   D  1 55  ? -5.458  27.745  -31.297  1.00 80.41  ? 356  LYS   D CD  1 
ATOM   10596 C  CE  . LYS   D  1 55  ? -5.124  28.049  -29.850  1.00 83.85  ? 356  LYS   D CE  1 
ATOM   10597 N  NZ  . LYS   D  1 55  ? -6.326  28.045  -28.967  1.00 89.64  ? 356  LYS   D NZ  1 
ATOM   10598 N  N   . ASP   D  1 56  ? -4.481  27.245  -36.689  1.00 88.07  ? 357  ASP   D N   1 
ATOM   10599 C  CA  . ASP   D  1 56  ? -4.752  26.274  -37.744  1.00 91.71  ? 357  ASP   D CA  1 
ATOM   10600 C  C   . ASP   D  1 56  ? -3.655  26.250  -38.804  1.00 81.52  ? 357  ASP   D C   1 
ATOM   10601 O  O   . ASP   D  1 56  ? -3.472  25.228  -39.473  1.00 82.44  ? 357  ASP   D O   1 
ATOM   10602 C  CB  . ASP   D  1 56  ? -6.111  26.562  -38.394  1.00 99.60  ? 357  ASP   D CB  1 
ATOM   10603 C  CG  . ASP   D  1 56  ? -7.267  26.453  -37.409  1.00 103.11 ? 357  ASP   D CG  1 
ATOM   10604 O  OD1 . ASP   D  1 56  ? -7.192  25.627  -36.471  1.00 101.84 ? 357  ASP   D OD1 1 
ATOM   10605 O  OD2 . ASP   D  1 56  ? -8.249  27.205  -37.577  1.00 106.71 ? 357  ASP   D OD2 1 
ATOM   10606 N  N   . GLN   D  1 57  ? -2.924  27.353  -38.983  1.00 69.00  ? 358  GLN   D N   1 
ATOM   10607 C  CA  . GLN   D  1 57  ? -1.753  27.302  -39.847  1.00 63.25  ? 358  GLN   D CA  1 
ATOM   10608 C  C   . GLN   D  1 57  ? -0.626  26.501  -39.209  1.00 60.91  ? 358  GLN   D C   1 
ATOM   10609 O  O   . GLN   D  1 57  ? 0.154   25.861  -39.924  1.00 57.96  ? 358  GLN   D O   1 
ATOM   10610 C  CB  . GLN   D  1 57  ? -1.272  28.715  -40.180  1.00 66.35  ? 358  GLN   D CB  1 
ATOM   10611 C  CG  . GLN   D  1 57  ? -2.257  29.562  -40.993  1.00 73.67  ? 358  GLN   D CG  1 
ATOM   10612 C  CD  . GLN   D  1 57  ? -1.702  30.942  -41.345  1.00 76.83  ? 358  GLN   D CD  1 
ATOM   10613 O  OE1 . GLN   D  1 57  ? -1.182  31.658  -40.488  1.00 74.37  ? 358  GLN   D OE1 1 
ATOM   10614 N  NE2 . GLN   D  1 57  ? -1.800  31.309  -42.616  1.00 81.10  ? 358  GLN   D NE2 1 
ATOM   10615 N  N   . LEU   D  1 58  ? -0.540  26.502  -37.869  1.00 53.32  ? 359  LEU   D N   1 
ATOM   10616 C  CA  . LEU   D  1 58  ? 0.638   25.959  -37.190  1.00 55.60  ? 359  LEU   D CA  1 
ATOM   10617 C  C   . LEU   D  1 58  ? 0.610   24.435  -37.107  1.00 59.30  ? 359  LEU   D C   1 
ATOM   10618 O  O   . LEU   D  1 58  ? 1.648   23.793  -37.302  1.00 57.58  ? 359  LEU   D O   1 
ATOM   10619 C  CB  . LEU   D  1 58  ? 0.778   26.568  -35.784  1.00 49.01  ? 359  LEU   D CB  1 
ATOM   10620 C  CG  . LEU   D  1 58  ? 2.149   26.379  -35.118  1.00 46.92  ? 359  LEU   D CG  1 
ATOM   10621 C  CD1 . LEU   D  1 58  ? 3.285   26.841  -36.041  1.00 48.84  ? 359  LEU   D CD1 1 
ATOM   10622 C  CD2 . LEU   D  1 58  ? 2.262   27.090  -33.767  1.00 46.11  ? 359  LEU   D CD2 1 
ATOM   10623 N  N   . PHE   D  1 59  ? -0.560  23.839  -36.812  1.00 60.96  ? 360  PHE   D N   1 
ATOM   10624 C  CA  . PHE   D  1 59  ? -0.706  22.389  -36.697  1.00 63.34  ? 360  PHE   D CA  1 
ATOM   10625 C  C   . PHE   D  1 59  ? -0.015  21.646  -37.844  1.00 61.29  ? 360  PHE   D C   1 
ATOM   10626 O  O   . PHE   D  1 59  ? 0.879   20.828  -37.584  1.00 61.85  ? 360  PHE   D O   1 
ATOM   10627 C  CB  . PHE   D  1 59  ? -2.181  21.975  -36.649  1.00 71.84  ? 360  PHE   D CB  1 
ATOM   10628 C  CG  . PHE   D  1 59  ? -2.874  22.253  -35.338  1.00 81.34  ? 360  PHE   D CG  1 
ATOM   10629 C  CD1 . PHE   D  1 59  ? -2.404  21.714  -34.150  1.00 81.35  ? 360  PHE   D CD1 1 
ATOM   10630 C  CD2 . PHE   D  1 59  ? -4.043  23.005  -35.309  1.00 83.76  ? 360  PHE   D CD2 1 
ATOM   10631 C  CE1 . PHE   D  1 59  ? -3.072  21.954  -32.952  1.00 78.20  ? 360  PHE   D CE1 1 
ATOM   10632 C  CE2 . PHE   D  1 59  ? -4.710  23.245  -34.120  1.00 80.30  ? 360  PHE   D CE2 1 
ATOM   10633 C  CZ  . PHE   D  1 59  ? -4.224  22.723  -32.941  1.00 76.06  ? 360  PHE   D CZ  1 
ATOM   10634 N  N   . PRO   D  1 60  ? -0.371  21.886  -39.114  1.00 55.22  ? 361  PRO   D N   1 
ATOM   10635 C  CA  . PRO   D  1 60  ? 0.234   21.066  -40.179  1.00 54.22  ? 361  PRO   D CA  1 
ATOM   10636 C  C   . PRO   D  1 60  ? 1.723   21.302  -40.346  1.00 55.51  ? 361  PRO   D C   1 
ATOM   10637 O  O   . PRO   D  1 60  ? 2.457   20.361  -40.676  1.00 66.01  ? 361  PRO   D O   1 
ATOM   10638 C  CB  . PRO   D  1 60  ? -0.552  21.473  -41.431  1.00 53.89  ? 361  PRO   D CB  1 
ATOM   10639 C  CG  . PRO   D  1 60  ? -0.968  22.866  -41.158  1.00 58.04  ? 361  PRO   D CG  1 
ATOM   10640 C  CD  . PRO   D  1 60  ? -1.237  22.943  -39.675  1.00 53.74  ? 361  PRO   D CD  1 
ATOM   10641 N  N   . LEU   D  1 61  ? 2.196   22.528  -40.130  1.00 50.05  ? 362  LEU   D N   1 
ATOM   10642 C  CA  . LEU   D  1 61  ? 3.630   22.781  -40.213  1.00 50.63  ? 362  LEU   D CA  1 
ATOM   10643 C  C   . LEU   D  1 61  ? 4.371   21.987  -39.155  1.00 51.09  ? 362  LEU   D C   1 
ATOM   10644 O  O   . LEU   D  1 61  ? 5.388   21.343  -39.437  1.00 46.21  ? 362  LEU   D O   1 
ATOM   10645 C  CB  . LEU   D  1 61  ? 3.916   24.273  -40.052  1.00 45.19  ? 362  LEU   D CB  1 
ATOM   10646 C  CG  . LEU   D  1 61  ? 3.357   25.163  -41.145  1.00 48.31  ? 362  LEU   D CG  1 
ATOM   10647 C  CD1 . LEU   D  1 61  ? 3.644   26.609  -40.787  1.00 50.01  ? 362  LEU   D CD1 1 
ATOM   10648 C  CD2 . LEU   D  1 61  ? 3.976   24.766  -42.490  1.00 46.27  ? 362  LEU   D CD2 1 
ATOM   10649 N  N   . ALA   D  1 62  ? 3.872   22.034  -37.916  1.00 47.61  ? 363  ALA   D N   1 
ATOM   10650 C  CA  . ALA   D  1 62  ? 4.522   21.307  -36.841  1.00 44.11  ? 363  ALA   D CA  1 
ATOM   10651 C  C   . ALA   D  1 62  ? 4.502   19.813  -37.120  1.00 42.85  ? 363  ALA   D C   1 
ATOM   10652 O  O   . ALA   D  1 62  ? 5.518   19.130  -36.944  1.00 44.64  ? 363  ALA   D O   1 
ATOM   10653 C  CB  . ALA   D  1 62  ? 3.853   21.637  -35.506  1.00 46.87  ? 363  ALA   D CB  1 
ATOM   10654 N  N   . LYS   D  1 63  ? 3.365   19.294  -37.592  1.00 44.30  ? 364  LYS   D N   1 
ATOM   10655 C  CA  . LYS   D  1 63  ? 3.288   17.872  -37.909  1.00 48.96  ? 364  LYS   D CA  1 
ATOM   10656 C  C   . LYS   D  1 63  ? 4.368   17.481  -38.908  1.00 51.56  ? 364  LYS   D C   1 
ATOM   10657 O  O   . LYS   D  1 63  ? 5.100   16.509  -38.693  1.00 55.44  ? 364  LYS   D O   1 
ATOM   10658 C  CB  . LYS   D  1 63  ? 1.904   17.511  -38.448  1.00 49.57  ? 364  LYS   D CB  1 
ATOM   10659 C  CG  . LYS   D  1 63  ? 1.570   16.007  -38.347  1.00 54.53  ? 364  LYS   D CG  1 
ATOM   10660 C  CD  . LYS   D  1 63  ? 0.985   15.461  -39.655  1.00 70.52  ? 364  LYS   D CD  1 
ATOM   10661 C  CE  . LYS   D  1 63  ? 0.466   14.020  -39.528  1.00 77.44  ? 364  LYS   D CE  1 
ATOM   10662 N  NZ  . LYS   D  1 63  ? 1.528   12.970  -39.625  1.00 80.40  ? 364  LYS   D NZ  1 
ATOM   10663 N  N   . GLU   D  1 64  ? 4.505   18.249  -39.992  1.00 56.10  ? 365  GLU   D N   1 
ATOM   10664 C  CA  . GLU   D  1 64  ? 5.487   17.907  -41.020  1.00 55.57  ? 365  GLU   D CA  1 
ATOM   10665 C  C   . GLU   D  1 64  ? 6.892   17.831  -40.437  1.00 47.10  ? 365  GLU   D C   1 
ATOM   10666 O  O   . GLU   D  1 64  ? 7.625   16.869  -40.694  1.00 39.75  ? 365  GLU   D O   1 
ATOM   10667 C  CB  . GLU   D  1 64  ? 5.425   18.920  -42.164  1.00 64.61  ? 365  GLU   D CB  1 
ATOM   10668 C  CG  . GLU   D  1 64  ? 5.500   18.305  -43.561  1.00 79.77  ? 365  GLU   D CG  1 
ATOM   10669 C  CD  . GLU   D  1 64  ? 6.931   18.147  -44.080  1.00 91.47  ? 365  GLU   D CD  1 
ATOM   10670 O  OE1 . GLU   D  1 64  ? 7.745   17.462  -43.418  1.00 93.53  ? 365  GLU   D OE1 1 
ATOM   10671 O  OE2 . GLU   D  1 64  ? 7.245   18.716  -45.155  1.00 92.62  ? 365  GLU   D OE2 1 
ATOM   10672 N  N   . PHE   D  1 65  ? 7.268   18.817  -39.613  1.00 43.66  ? 366  PHE   D N   1 
ATOM   10673 C  CA  . PHE   D  1 65  ? 8.611   18.832  -39.038  1.00 46.84  ? 366  PHE   D CA  1 
ATOM   10674 C  C   . PHE   D  1 65  ? 8.830   17.666  -38.073  1.00 46.56  ? 366  PHE   D C   1 
ATOM   10675 O  O   . PHE   D  1 65  ? 9.859   16.982  -38.142  1.00 46.01  ? 366  PHE   D O   1 
ATOM   10676 C  CB  . PHE   D  1 65  ? 8.886   20.161  -38.329  1.00 36.74  ? 366  PHE   D CB  1 
ATOM   10677 C  CG  . PHE   D  1 65  ? 10.114  20.124  -37.473  1.00 38.26  ? 366  PHE   D CG  1 
ATOM   10678 C  CD1 . PHE   D  1 65  ? 11.370  20.252  -38.040  1.00 37.18  ? 366  PHE   D CD1 1 
ATOM   10679 C  CD2 . PHE   D  1 65  ? 10.017  19.918  -36.105  1.00 42.57  ? 366  PHE   D CD2 1 
ATOM   10680 C  CE1 . PHE   D  1 65  ? 12.504  20.200  -37.266  1.00 39.86  ? 366  PHE   D CE1 1 
ATOM   10681 C  CE2 . PHE   D  1 65  ? 11.148  19.856  -35.322  1.00 42.99  ? 366  PHE   D CE2 1 
ATOM   10682 C  CZ  . PHE   D  1 65  ? 12.394  20.007  -35.897  1.00 46.68  ? 366  PHE   D CZ  1 
ATOM   10683 N  N   . ILE   D  1 66  ? 7.893   17.444  -37.145  1.00 42.30  ? 367  ILE   D N   1 
ATOM   10684 C  CA  . ILE   D  1 66  ? 8.050   16.340  -36.198  1.00 45.97  ? 367  ILE   D CA  1 
ATOM   10685 C  C   . ILE   D  1 66  ? 8.096   15.011  -36.941  1.00 49.70  ? 367  ILE   D C   1 
ATOM   10686 O  O   . ILE   D  1 66  ? 8.852   14.098  -36.575  1.00 43.63  ? 367  ILE   D O   1 
ATOM   10687 C  CB  . ILE   D  1 66  ? 6.925   16.364  -35.146  1.00 42.77  ? 367  ILE   D CB  1 
ATOM   10688 C  CG1 . ILE   D  1 66  ? 6.949   17.672  -34.362  1.00 36.86  ? 367  ILE   D CG1 1 
ATOM   10689 C  CG2 . ILE   D  1 66  ? 7.066   15.184  -34.173  1.00 38.39  ? 367  ILE   D CG2 1 
ATOM   10690 C  CD1 . ILE   D  1 66  ? 8.168   17.836  -33.471  1.00 43.63  ? 367  ILE   D CD1 1 
ATOM   10691 N  N   . ASP   D  1 67  ? 7.298   14.886  -38.005  1.00 53.50  ? 368  ASP   D N   1 
ATOM   10692 C  CA  . ASP   D  1 67  ? 7.323   13.672  -38.814  1.00 49.15  ? 368  ASP   D CA  1 
ATOM   10693 C  C   . ASP   D  1 67  ? 8.694   13.463  -39.419  1.00 43.39  ? 368  ASP   D C   1 
ATOM   10694 O  O   . ASP   D  1 67  ? 9.240   12.355  -39.385  1.00 44.48  ? 368  ASP   D O   1 
ATOM   10695 C  CB  . ASP   D  1 67  ? 6.266   13.742  -39.914  1.00 48.06  ? 368  ASP   D CB  1 
ATOM   10696 C  CG  . ASP   D  1 67  ? 4.873   13.457  -39.401  1.00 56.52  ? 368  ASP   D CG  1 
ATOM   10697 O  OD1 . ASP   D  1 67  ? 4.715   13.126  -38.193  1.00 60.70  ? 368  ASP   D OD1 1 
ATOM   10698 O  OD2 . ASP   D  1 67  ? 3.935   13.564  -40.213  1.00 54.39  ? 368  ASP   D OD2 1 
ATOM   10699 N  N   . GLN   D  1 68  ? 9.272   14.528  -39.974  1.00 42.25  ? 369  GLN   D N   1 
ATOM   10700 C  CA  . GLN   D  1 68  ? 10.553  14.391  -40.642  1.00 43.33  ? 369  GLN   D CA  1 
ATOM   10701 C  C   . GLN   D  1 68  ? 11.674  14.205  -39.631  1.00 50.24  ? 369  GLN   D C   1 
ATOM   10702 O  O   . GLN   D  1 68  ? 12.653  13.500  -39.909  1.00 46.34  ? 369  GLN   D O   1 
ATOM   10703 C  CB  . GLN   D  1 68  ? 10.795  15.596  -41.556  1.00 47.97  ? 369  GLN   D CB  1 
ATOM   10704 C  CG  . GLN   D  1 68  ? 11.696  16.668  -40.987  1.00 56.46  ? 369  GLN   D CG  1 
ATOM   10705 C  CD  . GLN   D  1 68  ? 12.108  17.726  -42.011  1.00 56.66  ? 369  GLN   D CD  1 
ATOM   10706 O  OE1 . GLN   D  1 68  ? 13.302  18.009  -42.187  1.00 57.66  ? 369  GLN   D OE1 1 
ATOM   10707 N  NE2 . GLN   D  1 68  ? 11.123  18.328  -42.668  1.00 53.69  ? 369  GLN   D NE2 1 
ATOM   10708 N  N   . TYR   D  1 69  ? 11.540  14.791  -38.440  1.00 51.93  ? 370  TYR   D N   1 
ATOM   10709 C  CA  . TYR   D  1 69  ? 12.540  14.531  -37.416  1.00 48.31  ? 370  TYR   D CA  1 
ATOM   10710 C  C   . TYR   D  1 69  ? 12.519  13.066  -37.012  1.00 45.89  ? 370  TYR   D C   1 
ATOM   10711 O  O   . TYR   D  1 69  ? 13.573  12.432  -36.867  1.00 49.47  ? 370  TYR   D O   1 
ATOM   10712 C  CB  . TYR   D  1 69  ? 12.326  15.422  -36.195  1.00 39.83  ? 370  TYR   D CB  1 
ATOM   10713 C  CG  . TYR   D  1 69  ? 13.181  14.951  -35.053  1.00 45.60  ? 370  TYR   D CG  1 
ATOM   10714 C  CD1 . TYR   D  1 69  ? 14.533  15.235  -35.027  1.00 53.71  ? 370  TYR   D CD1 1 
ATOM   10715 C  CD2 . TYR   D  1 69  ? 12.650  14.192  -34.023  1.00 47.86  ? 370  TYR   D CD2 1 
ATOM   10716 C  CE1 . TYR   D  1 69  ? 15.330  14.805  -34.004  1.00 50.91  ? 370  TYR   D CE1 1 
ATOM   10717 C  CE2 . TYR   D  1 69  ? 13.455  13.747  -32.982  1.00 54.10  ? 370  TYR   D CE2 1 
ATOM   10718 C  CZ  . TYR   D  1 69  ? 14.795  14.064  -32.987  1.00 52.44  ? 370  TYR   D CZ  1 
ATOM   10719 O  OH  . TYR   D  1 69  ? 15.630  13.643  -31.986  1.00 54.26  ? 370  TYR   D OH  1 
ATOM   10720 N  N   . TYR   D  1 70  ? 11.335  12.501  -36.846  1.00 39.67  ? 371  TYR   D N   1 
ATOM   10721 C  CA  . TYR   D  1 70  ? 11.296  11.111  -36.423  1.00 48.17  ? 371  TYR   D CA  1 
ATOM   10722 C  C   . TYR   D  1 70  ? 11.691  10.173  -37.551  1.00 52.41  ? 371  TYR   D C   1 
ATOM   10723 O  O   . TYR   D  1 70  ? 12.227  9.093   -37.290  1.00 49.58  ? 371  TYR   D O   1 
ATOM   10724 C  CB  . TYR   D  1 70  ? 9.924   10.777  -35.846  1.00 48.51  ? 371  TYR   D CB  1 
ATOM   10725 C  CG  . TYR   D  1 70  ? 9.878   11.157  -34.382  1.00 45.71  ? 371  TYR   D CG  1 
ATOM   10726 C  CD1 . TYR   D  1 70  ? 10.271  10.262  -33.408  1.00 42.98  ? 371  TYR   D CD1 1 
ATOM   10727 C  CD2 . TYR   D  1 70  ? 9.515   12.433  -33.993  1.00 45.62  ? 371  TYR   D CD2 1 
ATOM   10728 C  CE1 . TYR   D  1 70  ? 10.258  10.609  -32.075  1.00 52.21  ? 371  TYR   D CE1 1 
ATOM   10729 C  CE2 . TYR   D  1 70  ? 9.502   12.794  -32.671  1.00 45.93  ? 371  TYR   D CE2 1 
ATOM   10730 C  CZ  . TYR   D  1 70  ? 9.876   11.875  -31.705  1.00 52.03  ? 371  TYR   D CZ  1 
ATOM   10731 O  OH  . TYR   D  1 70  ? 9.858   12.230  -30.367  1.00 46.06  ? 371  TYR   D OH  1 
ATOM   10732 N  N   . SER   D  1 71  ? 11.480  10.578  -38.802  1.00 53.00  ? 372  SER   D N   1 
ATOM   10733 C  CA  . SER   D  1 71  ? 12.001  9.786   -39.907  1.00 56.83  ? 372  SER   D CA  1 
ATOM   10734 C  C   . SER   D  1 71  ? 13.527  9.776   -39.902  1.00 51.62  ? 372  SER   D C   1 
ATOM   10735 O  O   . SER   D  1 71  ? 14.151  8.721   -40.061  1.00 51.27  ? 372  SER   D O   1 
ATOM   10736 C  CB  . SER   D  1 71  ? 11.472  10.320  -41.231  1.00 61.99  ? 372  SER   D CB  1 
ATOM   10737 O  OG  . SER   D  1 71  ? 12.231  9.785   -42.299  1.00 73.02  ? 372  SER   D OG  1 
ATOM   10738 N  N   . SER   D  1 72  ? 14.147  10.944  -39.697  1.00 42.55  ? 373  SER   D N   1 
ATOM   10739 C  CA  . SER   D  1 72  ? 15.605  11.020  -39.749  1.00 43.14  ? 373  SER   D CA  1 
ATOM   10740 C  C   . SER   D  1 72  ? 16.267  10.060  -38.768  1.00 60.40  ? 373  SER   D C   1 
ATOM   10741 O  O   . SER   D  1 72  ? 17.357  9.550   -39.048  1.00 67.78  ? 373  SER   D O   1 
ATOM   10742 C  CB  . SER   D  1 72  ? 16.065  12.444  -39.473  1.00 41.21  ? 373  SER   D CB  1 
ATOM   10743 O  OG  . SER   D  1 72  ? 15.847  12.783  -38.113  1.00 60.24  ? 373  SER   D OG  1 
ATOM   10744 N  N   . ILE   D  1 73  ? 15.625  9.790   -37.632  1.00 62.09  ? 374  ILE   D N   1 
ATOM   10745 C  CA  . ILE   D  1 73  ? 16.197  8.939   -36.596  1.00 61.14  ? 374  ILE   D CA  1 
ATOM   10746 C  C   . ILE   D  1 73  ? 15.564  7.544   -36.591  1.00 62.29  ? 374  ILE   D C   1 
ATOM   10747 O  O   . ILE   D  1 73  ? 15.607  6.851   -35.572  1.00 63.15  ? 374  ILE   D O   1 
ATOM   10748 C  CB  . ILE   D  1 73  ? 16.093  9.592   -35.208  1.00 56.68  ? 374  ILE   D CB  1 
ATOM   10749 C  CG1 . ILE   D  1 73  ? 14.628  9.696   -34.773  1.00 51.81  ? 374  ILE   D CG1 1 
ATOM   10750 C  CG2 . ILE   D  1 73  ? 16.793  10.952  -35.200  1.00 47.86  ? 374  ILE   D CG2 1 
ATOM   10751 C  CD1 . ILE   D  1 73  ? 14.434  10.240  -33.368  1.00 47.90  ? 374  ILE   D CD1 1 
ATOM   10752 N  N   . LYS   D  1 74  ? 14.974  7.123   -37.711  1.00 62.98  ? 375  LYS   D N   1 
ATOM   10753 C  CA  . LYS   D  1 74  ? 14.417  5.772   -37.869  1.00 72.71  ? 375  LYS   D CA  1 
ATOM   10754 C  C   . LYS   D  1 74  ? 13.469  5.407   -36.727  1.00 71.35  ? 375  LYS   D C   1 
ATOM   10755 O  O   . LYS   D  1 74  ? 13.462  4.274   -36.243  1.00 73.72  ? 375  LYS   D O   1 
ATOM   10756 C  CB  . LYS   D  1 74  ? 15.522  4.713   -37.990  1.00 81.37  ? 375  LYS   D CB  1 
ATOM   10757 C  CG  . LYS   D  1 74  ? 16.847  5.180   -38.595  1.00 85.59  ? 375  LYS   D CG  1 
ATOM   10758 C  CD  . LYS   D  1 74  ? 16.777  5.389   -40.098  1.00 90.87  ? 375  LYS   D CD  1 
ATOM   10759 C  CE  . LYS   D  1 74  ? 18.148  5.779   -40.640  1.00 92.68  ? 375  LYS   D CE  1 
ATOM   10760 N  NZ  . LYS   D  1 74  ? 18.057  6.575   -41.897  1.00 89.01  ? 375  LYS   D NZ  1 
ATOM   10761 N  N   . ARG   D  1 75  ? 12.673  6.384   -36.276  1.00 68.69  ? 376  ARG   D N   1 
ATOM   10762 C  CA  . ARG   D  1 75  ? 11.637  6.159   -35.271  1.00 63.43  ? 376  ARG   D CA  1 
ATOM   10763 C  C   . ARG   D  1 75  ? 10.275  6.651   -35.754  1.00 58.94  ? 376  ARG   D C   1 
ATOM   10764 O  O   . ARG   D  1 75  ? 9.438   7.061   -34.942  1.00 56.41  ? 376  ARG   D O   1 
ATOM   10765 C  CB  . ARG   D  1 75  ? 11.981  6.838   -33.946  1.00 66.48  ? 376  ARG   D CB  1 
ATOM   10766 C  CG  . ARG   D  1 75  ? 13.201  6.301   -33.232  1.00 68.31  ? 376  ARG   D CG  1 
ATOM   10767 C  CD  . ARG   D  1 75  ? 12.965  4.906   -32.706  1.00 74.24  ? 376  ARG   D CD  1 
ATOM   10768 N  NE  . ARG   D  1 75  ? 13.928  4.555   -31.666  1.00 75.15  ? 376  ARG   D NE  1 
ATOM   10769 C  CZ  . ARG   D  1 75  ? 15.174  4.151   -31.903  1.00 73.05  ? 376  ARG   D CZ  1 
ATOM   10770 N  NH1 . ARG   D  1 75  ? 15.971  3.846   -30.888  1.00 64.40  ? 376  ARG   D NH1 1 
ATOM   10771 N  NH2 . ARG   D  1 75  ? 15.622  4.049   -33.153  1.00 67.76  ? 376  ARG   D NH2 1 
ATOM   10772 N  N   . PHE   D  1 76  ? 10.037  6.631   -37.067  1.00 57.71  ? 377  PHE   D N   1 
ATOM   10773 C  CA  . PHE   D  1 76  ? 8.740   7.045   -37.591  1.00 55.69  ? 377  PHE   D CA  1 
ATOM   10774 C  C   . PHE   D  1 76  ? 7.683   6.019   -37.204  1.00 60.33  ? 377  PHE   D C   1 
ATOM   10775 O  O   . PHE   D  1 76  ? 7.909   4.810   -37.286  1.00 65.14  ? 377  PHE   D O   1 
ATOM   10776 C  CB  . PHE   D  1 76  ? 8.799   7.208   -39.113  1.00 59.47  ? 377  PHE   D CB  1 
ATOM   10777 C  CG  . PHE   D  1 76  ? 7.556   7.828   -39.712  1.00 61.05  ? 377  PHE   D CG  1 
ATOM   10778 C  CD1 . PHE   D  1 76  ? 6.487   7.037   -40.114  1.00 64.24  ? 377  PHE   D CD1 1 
ATOM   10779 C  CD2 . PHE   D  1 76  ? 7.465   9.198   -39.887  1.00 53.10  ? 377  PHE   D CD2 1 
ATOM   10780 C  CE1 . PHE   D  1 76  ? 5.349   7.605   -40.665  1.00 58.96  ? 377  PHE   D CE1 1 
ATOM   10781 C  CE2 . PHE   D  1 76  ? 6.329   9.767   -40.429  1.00 50.39  ? 377  PHE   D CE2 1 
ATOM   10782 C  CZ  . PHE   D  1 76  ? 5.273   8.972   -40.818  1.00 52.93  ? 377  PHE   D CZ  1 
ATOM   10783 N  N   . GLY   D  1 77  ? 6.526   6.504   -36.760  1.00 60.47  ? 378  GLY   D N   1 
ATOM   10784 C  CA  . GLY   D  1 77  ? 5.498   5.638   -36.224  1.00 57.31  ? 378  GLY   D CA  1 
ATOM   10785 C  C   . GLY   D  1 77  ? 5.748   5.123   -34.823  1.00 61.24  ? 378  GLY   D C   1 
ATOM   10786 O  O   . GLY   D  1 77  ? 4.856   4.485   -34.253  1.00 70.65  ? 378  GLY   D O   1 
ATOM   10787 N  N   . SER   D  1 78  ? 6.918   5.384   -34.241  1.00 57.13  ? 379  SER   D N   1 
ATOM   10788 C  CA  . SER   D  1 78  ? 7.222   4.886   -32.905  1.00 66.17  ? 379  SER   D CA  1 
ATOM   10789 C  C   . SER   D  1 78  ? 6.296   5.506   -31.864  1.00 63.60  ? 379  SER   D C   1 
ATOM   10790 O  O   . SER   D  1 78  ? 5.601   6.497   -32.111  1.00 53.65  ? 379  SER   D O   1 
ATOM   10791 C  CB  . SER   D  1 78  ? 8.679   5.169   -32.536  1.00 68.18  ? 379  SER   D CB  1 
ATOM   10792 O  OG  . SER   D  1 78  ? 8.945   6.558   -32.505  1.00 61.04  ? 379  SER   D OG  1 
ATOM   10793 N  N   . LYS   D  1 79  ? 6.283   4.882   -30.683  1.00 70.80  ? 380  LYS   D N   1 
ATOM   10794 C  CA  . LYS   D  1 79  ? 5.456   5.374   -29.588  1.00 71.57  ? 380  LYS   D CA  1 
ATOM   10795 C  C   . LYS   D  1 79  ? 5.806   6.820   -29.254  1.00 60.90  ? 380  LYS   D C   1 
ATOM   10796 O  O   . LYS   D  1 79  ? 4.923   7.680   -29.167  1.00 67.36  ? 380  LYS   D O   1 
ATOM   10797 C  CB  . LYS   D  1 79  ? 5.626   4.472   -28.363  1.00 80.70  ? 380  LYS   D CB  1 
ATOM   10798 C  CG  . LYS   D  1 79  ? 4.329   4.031   -27.706  1.00 85.48  ? 380  LYS   D CG  1 
ATOM   10799 C  CD  . LYS   D  1 79  ? 4.582   2.869   -26.747  1.00 95.10  ? 380  LYS   D CD  1 
ATOM   10800 C  CE  . LYS   D  1 79  ? 3.311   2.063   -26.458  1.00 103.05 ? 380  LYS   D CE  1 
ATOM   10801 N  NZ  . LYS   D  1 79  ? 2.324   2.779   -25.594  1.00 105.04 ? 380  LYS   D NZ  1 
ATOM   10802 N  N   . ALA   D  1 80  ? 7.098   7.113   -29.092  1.00 54.15  ? 381  ALA   D N   1 
ATOM   10803 C  CA  . ALA   D  1 80  ? 7.511   8.487   -28.816  1.00 55.42  ? 381  ALA   D CA  1 
ATOM   10804 C  C   . ALA   D  1 80  ? 7.179   9.432   -29.970  1.00 55.23  ? 381  ALA   D C   1 
ATOM   10805 O  O   . ALA   D  1 80  ? 6.983   10.634  -29.746  1.00 54.25  ? 381  ALA   D O   1 
ATOM   10806 C  CB  . ALA   D  1 80  ? 9.006   8.536   -28.504  1.00 49.12  ? 381  ALA   D CB  1 
ATOM   10807 N  N   . HIS   D  1 81  ? 7.105   8.921   -31.202  1.00 52.49  ? 382  HIS   D N   1 
ATOM   10808 C  CA  . HIS   D  1 81  ? 6.661   9.759   -32.317  1.00 54.84  ? 382  HIS   D CA  1 
ATOM   10809 C  C   . HIS   D  1 81  ? 5.211   10.193  -32.120  1.00 49.85  ? 382  HIS   D C   1 
ATOM   10810 O  O   . HIS   D  1 81  ? 4.885   11.380  -32.226  1.00 54.05  ? 382  HIS   D O   1 
ATOM   10811 C  CB  . HIS   D  1 81  ? 6.832   9.012   -33.649  1.00 52.71  ? 382  HIS   D CB  1 
ATOM   10812 C  CG  . HIS   D  1 81  ? 6.449   9.809   -34.861  1.00 52.87  ? 382  HIS   D CG  1 
ATOM   10813 N  ND1 . HIS   D  1 81  ? 6.403   9.257   -36.126  1.00 55.98  ? 382  HIS   D ND1 1 
ATOM   10814 C  CD2 . HIS   D  1 81  ? 6.122   11.115  -35.010  1.00 54.12  ? 382  HIS   D CD2 1 
ATOM   10815 C  CE1 . HIS   D  1 81  ? 6.055   10.187  -36.998  1.00 56.28  ? 382  HIS   D CE1 1 
ATOM   10816 N  NE2 . HIS   D  1 81  ? 5.883   11.325  -36.348  1.00 57.36  ? 382  HIS   D NE2 1 
ATOM   10817 N  N   . MET   D  1 82  ? 4.331   9.242   -31.814  1.00 48.20  ? 383  MET   D N   1 
ATOM   10818 C  CA  . MET   D  1 82  ? 2.916   9.555   -31.634  1.00 54.51  ? 383  MET   D CA  1 
ATOM   10819 C  C   . MET   D  1 82  ? 2.691   10.449  -30.422  1.00 60.18  ? 383  MET   D C   1 
ATOM   10820 O  O   . MET   D  1 82  ? 1.902   11.401  -30.479  1.00 56.26  ? 383  MET   D O   1 
ATOM   10821 C  CB  . MET   D  1 82  ? 2.115   8.260   -31.507  1.00 49.34  ? 383  MET   D CB  1 
ATOM   10822 C  CG  . MET   D  1 82  ? 1.230   7.969   -32.713  1.00 68.91  ? 383  MET   D CG  1 
ATOM   10823 S  SD  . MET   D  1 82  ? 1.994   8.447   -34.278  1.00 81.28  ? 383  MET   D SD  1 
ATOM   10824 C  CE  . MET   D  1 82  ? 0.571   9.012   -35.210  1.00 80.57  ? 383  MET   D CE  1 
ATOM   10825 N  N   . GLU   D  1 83  ? 3.379   10.160  -29.318  1.00 65.34  ? 384  GLU   D N   1 
ATOM   10826 C  CA  . GLU   D  1 83  ? 3.200   10.964  -28.117  1.00 59.45  ? 384  GLU   D CA  1 
ATOM   10827 C  C   . GLU   D  1 83  ? 3.713   12.377  -28.329  1.00 55.91  ? 384  GLU   D C   1 
ATOM   10828 O  O   . GLU   D  1 83  ? 3.138   13.335  -27.800  1.00 58.29  ? 384  GLU   D O   1 
ATOM   10829 C  CB  . GLU   D  1 83  ? 3.894   10.294  -26.932  1.00 59.17  ? 384  GLU   D CB  1 
ATOM   10830 C  CG  . GLU   D  1 83  ? 3.037   9.222   -26.281  1.00 71.80  ? 384  GLU   D CG  1 
ATOM   10831 C  CD  . GLU   D  1 83  ? 3.819   8.269   -25.400  1.00 75.59  ? 384  GLU   D CD  1 
ATOM   10832 O  OE1 . GLU   D  1 83  ? 4.976   8.585   -25.036  1.00 78.39  ? 384  GLU   D OE1 1 
ATOM   10833 O  OE2 . GLU   D  1 83  ? 3.261   7.196   -25.083  1.00 75.13  ? 384  GLU   D OE2 1 
ATOM   10834 N  N   . ARG   D  1 84  ? 4.782   12.529  -29.111  1.00 50.13  ? 385  ARG   D N   1 
ATOM   10835 C  CA  . ARG   D  1 84  ? 5.305   13.864  -29.382  1.00 49.52  ? 385  ARG   D CA  1 
ATOM   10836 C  C   . ARG   D  1 84  ? 4.310   14.674  -30.205  1.00 53.08  ? 385  ARG   D C   1 
ATOM   10837 O  O   . ARG   D  1 84  ? 4.024   15.833  -29.886  1.00 54.06  ? 385  ARG   D O   1 
ATOM   10838 C  CB  . ARG   D  1 84  ? 6.658   13.752  -30.082  1.00 50.47  ? 385  ARG   D CB  1 
ATOM   10839 C  CG  . ARG   D  1 84  ? 7.329   15.072  -30.382  1.00 49.94  ? 385  ARG   D CG  1 
ATOM   10840 C  CD  . ARG   D  1 84  ? 7.523   15.914  -29.137  1.00 46.54  ? 385  ARG   D CD  1 
ATOM   10841 N  NE  . ARG   D  1 84  ? 8.089   17.206  -29.504  1.00 46.63  ? 385  ARG   D NE  1 
ATOM   10842 C  CZ  . ARG   D  1 84  ? 7.962   18.323  -28.795  1.00 48.23  ? 385  ARG   D CZ  1 
ATOM   10843 N  NH1 . ARG   D  1 84  ? 7.281   18.315  -27.654  1.00 48.26  ? 385  ARG   D NH1 1 
ATOM   10844 N  NH2 . ARG   D  1 84  ? 8.506   19.454  -29.239  1.00 40.47  ? 385  ARG   D NH2 1 
ATOM   10845 N  N   . LEU   D  1 85  ? 3.755   14.065  -31.258  1.00 56.16  ? 386  LEU   D N   1 
ATOM   10846 C  CA  . LEU   D  1 85  ? 2.707   14.715  -32.045  1.00 55.05  ? 386  LEU   D CA  1 
ATOM   10847 C  C   . LEU   D  1 85  ? 1.555   15.168  -31.163  1.00 64.02  ? 386  LEU   D C   1 
ATOM   10848 O  O   . LEU   D  1 85  ? 1.150   16.335  -31.203  1.00 62.34  ? 386  LEU   D O   1 
ATOM   10849 C  CB  . LEU   D  1 85  ? 2.193   13.763  -33.115  1.00 46.87  ? 386  LEU   D CB  1 
ATOM   10850 C  CG  . LEU   D  1 85  ? 2.939   13.672  -34.440  1.00 51.07  ? 386  LEU   D CG  1 
ATOM   10851 C  CD1 . LEU   D  1 85  ? 2.140   12.768  -35.352  1.00 49.50  ? 386  LEU   D CD1 1 
ATOM   10852 C  CD2 . LEU   D  1 85  ? 3.099   15.055  -35.044  1.00 56.28  ? 386  LEU   D CD2 1 
ATOM   10853 N  N   . GLU   D  1 86  ? 1.002   14.243  -30.372  1.00 68.87  ? 387  GLU   D N   1 
ATOM   10854 C  CA  . GLU   D  1 86  ? -0.074  14.598  -29.452  1.00 68.02  ? 387  GLU   D CA  1 
ATOM   10855 C  C   . GLU   D  1 86  ? 0.352   15.732  -28.528  1.00 55.67  ? 387  GLU   D C   1 
ATOM   10856 O  O   . GLU   D  1 86  ? -0.385  16.709  -28.348  1.00 51.18  ? 387  GLU   D O   1 
ATOM   10857 C  CB  . GLU   D  1 86  ? -0.504  13.364  -28.655  1.00 84.22  ? 387  GLU   D CB  1 
ATOM   10858 C  CG  . GLU   D  1 86  ? -1.539  13.623  -27.559  1.00 101.63 ? 387  GLU   D CG  1 
ATOM   10859 C  CD  . GLU   D  1 86  ? -2.835  14.222  -28.087  1.00 116.57 ? 387  GLU   D CD  1 
ATOM   10860 O  OE1 . GLU   D  1 86  ? -3.193  13.967  -29.263  1.00 117.73 ? 387  GLU   D OE1 1 
ATOM   10861 O  OE2 . GLU   D  1 86  ? -3.493  14.958  -27.317  1.00 122.89 ? 387  GLU   D OE2 1 
ATOM   10862 N  N   . GLU   D  1 87  ? 1.566   15.643  -27.980  1.00 51.05  ? 388  GLU   D N   1 
ATOM   10863 C  CA  . GLU   D  1 87  ? 2.060   16.679  -27.079  1.00 49.02  ? 388  GLU   D CA  1 
ATOM   10864 C  C   . GLU   D  1 87  ? 2.124   18.039  -27.772  1.00 56.82  ? 388  GLU   D C   1 
ATOM   10865 O  O   . GLU   D  1 87  ? 1.727   19.054  -27.189  1.00 62.37  ? 388  GLU   D O   1 
ATOM   10866 C  CB  . GLU   D  1 87  ? 3.430   16.273  -26.531  1.00 43.47  ? 388  GLU   D CB  1 
ATOM   10867 C  CG  . GLU   D  1 87  ? 4.041   17.261  -25.538  1.00 47.46  ? 388  GLU   D CG  1 
ATOM   10868 C  CD  . GLU   D  1 87  ? 5.442   16.857  -25.087  1.00 59.64  ? 388  GLU   D CD  1 
ATOM   10869 O  OE1 . GLU   D  1 87  ? 6.211   16.320  -25.918  1.00 60.87  ? 388  GLU   D OE1 1 
ATOM   10870 O  OE2 . GLU   D  1 87  ? 5.772   17.071  -23.897  1.00 64.24  ? 388  GLU   D OE2 1 
ATOM   10871 N  N   . VAL   D  1 88  ? 2.606   18.081  -29.020  1.00 56.16  ? 389  VAL   D N   1 
ATOM   10872 C  CA  . VAL   D  1 88  ? 2.688   19.352  -29.742  1.00 49.75  ? 389  VAL   D CA  1 
ATOM   10873 C  C   . VAL   D  1 88  ? 1.300   19.942  -29.934  1.00 57.26  ? 389  VAL   D C   1 
ATOM   10874 O  O   . VAL   D  1 88  ? 1.067   21.125  -29.664  1.00 59.28  ? 389  VAL   D O   1 
ATOM   10875 C  CB  . VAL   D  1 88  ? 3.399   19.172  -31.093  1.00 45.88  ? 389  VAL   D CB  1 
ATOM   10876 C  CG1 . VAL   D  1 88  ? 3.166   20.392  -31.965  1.00 49.79  ? 389  VAL   D CG1 1 
ATOM   10877 C  CG2 . VAL   D  1 88  ? 4.891   18.944  -30.894  1.00 40.23  ? 389  VAL   D CG2 1 
ATOM   10878 N  N   . ASN   D  1 89  ? 0.359   19.116  -30.400  1.00 61.59  ? 390  ASN   D N   1 
ATOM   10879 C  CA  . ASN   D  1 89  ? -1.024  19.540  -30.602  1.00 64.27  ? 390  ASN   D CA  1 
ATOM   10880 C  C   . ASN   D  1 89  ? -1.631  20.155  -29.343  1.00 65.61  ? 390  ASN   D C   1 
ATOM   10881 O  O   . ASN   D  1 89  ? -2.288  21.200  -29.411  1.00 64.10  ? 390  ASN   D O   1 
ATOM   10882 C  CB  . ASN   D  1 89  ? -1.858  18.345  -31.055  1.00 76.69  ? 390  ASN   D CB  1 
ATOM   10883 C  CG  . ASN   D  1 89  ? -1.935  18.223  -32.559  1.00 85.92  ? 390  ASN   D CG  1 
ATOM   10884 O  OD1 . ASN   D  1 89  ? -3.024  18.063  -33.114  1.00 91.41  ? 390  ASN   D OD1 1 
ATOM   10885 N  ND2 . ASN   D  1 89  ? -0.784  18.307  -33.232  1.00 83.31  ? 390  ASN   D ND2 1 
ATOM   10886 N  N   . LYS   D  1 90  ? -1.466  19.482  -28.195  1.00 62.63  ? 391  LYS   D N   1 
ATOM   10887 C  CA  . LYS   D  1 90  ? -1.918  20.030  -26.917  1.00 65.99  ? 391  LYS   D CA  1 
ATOM   10888 C  C   . LYS   D  1 90  ? -1.414  21.447  -26.735  1.00 57.08  ? 391  LYS   D C   1 
ATOM   10889 O  O   . LYS   D  1 90  ? -2.186  22.373  -26.459  1.00 60.50  ? 391  LYS   D O   1 
ATOM   10890 C  CB  . LYS   D  1 90  ? -1.408  19.173  -25.751  1.00 70.00  ? 391  LYS   D CB  1 
ATOM   10891 C  CG  . LYS   D  1 90  ? -2.151  17.887  -25.464  1.00 78.16  ? 391  LYS   D CG  1 
ATOM   10892 C  CD  . LYS   D  1 90  ? -1.521  17.188  -24.252  1.00 84.64  ? 391  LYS   D CD  1 
ATOM   10893 C  CE  . LYS   D  1 90  ? -2.489  16.227  -23.576  1.00 87.59  ? 391  LYS   D CE  1 
ATOM   10894 N  NZ  . LYS   D  1 90  ? -2.986  15.200  -24.525  1.00 89.80  ? 391  LYS   D NZ  1 
ATOM   10895 N  N   . GLU   D  1 91  ? -0.099  21.616  -26.876  1.00 44.34  ? 392  GLU   D N   1 
ATOM   10896 C  CA  . GLU   D  1 91  ? 0.539   22.906  -26.663  1.00 45.34  ? 392  GLU   D CA  1 
ATOM   10897 C  C   . GLU   D  1 91  ? -0.003  23.962  -27.622  1.00 51.31  ? 392  GLU   D C   1 
ATOM   10898 O  O   . GLU   D  1 91  ? -0.288  25.092  -27.209  1.00 54.17  ? 392  GLU   D O   1 
ATOM   10899 C  CB  . GLU   D  1 91  ? 2.044   22.740  -26.821  1.00 45.15  ? 392  GLU   D CB  1 
ATOM   10900 C  CG  . GLU   D  1 91  ? 2.890   23.447  -25.797  1.00 45.31  ? 392  GLU   D CG  1 
ATOM   10901 C  CD  . GLU   D  1 91  ? 4.324   22.961  -25.821  1.00 55.23  ? 392  GLU   D CD  1 
ATOM   10902 O  OE1 . GLU   D  1 91  ? 5.244   23.801  -25.749  1.00 59.97  ? 392  GLU   D OE1 1 
ATOM   10903 O  OE2 . GLU   D  1 91  ? 4.531   21.734  -25.926  1.00 57.80  ? 392  GLU   D OE2 1 
ATOM   10904 N  N   . ILE   D  1 92  ? -0.156  23.623  -28.906  1.00 49.64  ? 393  ILE   D N   1 
ATOM   10905 C  CA  . ILE   D  1 92  ? -0.703  24.602  -29.846  1.00 57.04  ? 393  ILE   D CA  1 
ATOM   10906 C  C   . ILE   D  1 92  ? -2.125  24.985  -29.447  1.00 73.20  ? 393  ILE   D C   1 
ATOM   10907 O  O   . ILE   D  1 92  ? -2.530  26.147  -29.569  1.00 74.22  ? 393  ILE   D O   1 
ATOM   10908 C  CB  . ILE   D  1 92  ? -0.647  24.067  -31.288  1.00 52.64  ? 393  ILE   D CB  1 
ATOM   10909 C  CG1 . ILE   D  1 92  ? 0.767   23.582  -31.629  1.00 48.16  ? 393  ILE   D CG1 1 
ATOM   10910 C  CG2 . ILE   D  1 92  ? -1.097  25.149  -32.271  1.00 48.48  ? 393  ILE   D CG2 1 
ATOM   10911 C  CD1 . ILE   D  1 92  ? 0.965   23.230  -33.084  1.00 46.40  ? 393  ILE   D CD1 1 
ATOM   10912 N  N   . ASP   D  1 93  ? -2.902  24.020  -28.952  1.00 79.66  ? 394  ASP   D N   1 
ATOM   10913 C  CA  . ASP   D  1 93  ? -4.280  24.299  -28.560  1.00 80.13  ? 394  ASP   D CA  1 
ATOM   10914 C  C   . ASP   D  1 93  ? -4.341  25.208  -27.342  1.00 77.39  ? 394  ASP   D C   1 
ATOM   10915 O  O   . ASP   D  1 93  ? -5.129  26.161  -27.305  1.00 78.83  ? 394  ASP   D O   1 
ATOM   10916 C  CB  . ASP   D  1 93  ? -5.017  22.998  -28.274  1.00 86.90  ? 394  ASP   D CB  1 
ATOM   10917 C  CG  . ASP   D  1 93  ? -6.269  22.855  -29.092  1.00 93.17  ? 394  ASP   D CG  1 
ATOM   10918 O  OD1 . ASP   D  1 93  ? -6.315  23.421  -30.208  1.00 98.13  ? 394  ASP   D OD1 1 
ATOM   10919 O  OD2 . ASP   D  1 93  ? -7.200  22.169  -28.621  1.00 90.29  ? 394  ASP   D OD2 1 
ATOM   10920 N  N   . THR   D  1 94  ? -3.525  24.921  -26.327  1.00 77.28  ? 395  THR   D N   1 
ATOM   10921 C  CA  . THR   D  1 94  ? -3.588  25.674  -25.082  1.00 78.84  ? 395  THR   D CA  1 
ATOM   10922 C  C   . THR   D  1 94  ? -2.849  27.003  -25.147  1.00 79.58  ? 395  THR   D C   1 
ATOM   10923 O  O   . THR   D  1 94  ? -3.208  27.926  -24.409  1.00 86.35  ? 395  THR   D O   1 
ATOM   10924 C  CB  . THR   D  1 94  ? -3.023  24.845  -23.927  1.00 79.41  ? 395  THR   D CB  1 
ATOM   10925 O  OG1 . THR   D  1 94  ? -1.667  24.488  -24.217  1.00 80.89  ? 395  THR   D OG1 1 
ATOM   10926 C  CG2 . THR   D  1 94  ? -3.839  23.581  -23.736  1.00 81.76  ? 395  THR   D CG2 1 
ATOM   10927 N  N   . THR   D  1 95  ? -1.828  27.127  -25.997  1.00 75.79  ? 396  THR   D N   1 
ATOM   10928 C  CA  . THR   D  1 95  ? -0.975  28.310  -25.990  1.00 71.29  ? 396  THR   D CA  1 
ATOM   10929 C  C   . THR   D  1 95  ? -0.829  28.983  -27.341  1.00 72.19  ? 396  THR   D C   1 
ATOM   10930 O  O   . THR   D  1 95  ? -0.171  30.027  -27.413  1.00 78.31  ? 396  THR   D O   1 
ATOM   10931 C  CB  . THR   D  1 95  ? 0.440   27.973  -25.481  1.00 61.59  ? 396  THR   D CB  1 
ATOM   10932 O  OG1 . THR   D  1 95  ? 1.159   27.260  -26.495  1.00 59.47  ? 396  THR   D OG1 1 
ATOM   10933 C  CG2 . THR   D  1 95  ? 0.393   27.133  -24.203  1.00 53.10  ? 396  THR   D CG2 1 
ATOM   10934 N  N   . SER   D  1 96  ? -1.388  28.416  -28.404  1.00 64.41  ? 397  SER   D N   1 
ATOM   10935 C  CA  . SER   D  1 96  ? -1.226  28.885  -29.772  1.00 65.28  ? 397  SER   D CA  1 
ATOM   10936 C  C   . SER   D  1 96  ? 0.205   28.766  -30.272  1.00 59.61  ? 397  SER   D C   1 
ATOM   10937 O  O   . SER   D  1 96  ? 0.530   29.359  -31.302  1.00 54.67  ? 397  SER   D O   1 
ATOM   10938 C  CB  . SER   D  1 96  ? -1.703  30.330  -29.937  1.00 75.26  ? 397  SER   D CB  1 
ATOM   10939 O  OG  . SER   D  1 96  ? -2.961  30.504  -29.308  1.00 84.31  ? 397  SER   D OG  1 
ATOM   10940 N  N   . THR   D  1 97  ? 1.067   28.022  -29.580  1.00 56.77  ? 398  THR   D N   1 
ATOM   10941 C  CA  . THR   D  1 97  ? 2.436   27.775  -30.035  1.00 50.05  ? 398  THR   D CA  1 
ATOM   10942 C  C   . THR   D  1 97  ? 2.951   26.525  -29.327  1.00 54.89  ? 398  THR   D C   1 
ATOM   10943 O  O   . THR   D  1 97  ? 2.202   25.849  -28.615  1.00 57.74  ? 398  THR   D O   1 
ATOM   10944 C  CB  . THR   D  1 97  ? 3.333   28.989  -29.784  1.00 47.04  ? 398  THR   D CB  1 
ATOM   10945 O  OG1 . THR   D  1 97  ? 4.617   28.755  -30.372  1.00 49.87  ? 398  THR   D OG1 1 
ATOM   10946 C  CG2 . THR   D  1 97  ? 3.492   29.245  -28.292  1.00 44.98  ? 398  THR   D CG2 1 
ATOM   10947 N  N   . TYR   D  1 98  ? 4.231   26.203  -29.528  1.00 49.28  ? 399  TYR   D N   1 
ATOM   10948 C  CA  . TYR   D  1 98  ? 4.830   25.064  -28.846  1.00 37.03  ? 399  TYR   D CA  1 
ATOM   10949 C  C   . TYR   D  1 98  ? 6.325   25.301  -28.694  1.00 42.04  ? 399  TYR   D C   1 
ATOM   10950 O  O   . TYR   D  1 98  ? 6.863   26.322  -29.128  1.00 42.04  ? 399  TYR   D O   1 
ATOM   10951 C  CB  . TYR   D  1 98  ? 4.520   23.747  -29.576  1.00 35.96  ? 399  TYR   D CB  1 
ATOM   10952 C  CG  . TYR   D  1 98  ? 5.234   23.522  -30.901  1.00 43.69  ? 399  TYR   D CG  1 
ATOM   10953 C  CD1 . TYR   D  1 98  ? 4.899   24.257  -32.038  1.00 37.30  ? 399  TYR   D CD1 1 
ATOM   10954 C  CD2 . TYR   D  1 98  ? 6.209   22.537  -31.023  1.00 41.91  ? 399  TYR   D CD2 1 
ATOM   10955 C  CE1 . TYR   D  1 98  ? 5.541   24.042  -33.248  1.00 34.56  ? 399  TYR   D CE1 1 
ATOM   10956 C  CE2 . TYR   D  1 98  ? 6.848   22.307  -32.229  1.00 46.08  ? 399  TYR   D CE2 1 
ATOM   10957 C  CZ  . TYR   D  1 98  ? 6.515   23.062  -33.338  1.00 41.62  ? 399  TYR   D CZ  1 
ATOM   10958 O  OH  . TYR   D  1 98  ? 7.156   22.825  -34.523  1.00 44.96  ? 399  TYR   D OH  1 
ATOM   10959 N  N   . GLN   D  1 99  ? 6.994   24.351  -28.047  1.00 49.20  ? 400  GLN   D N   1 
ATOM   10960 C  CA  . GLN   D  1 99  ? 8.408   24.458  -27.713  1.00 48.22  ? 400  GLN   D CA  1 
ATOM   10961 C  C   . GLN   D  1 99  ? 9.144   23.266  -28.294  1.00 47.53  ? 400  GLN   D C   1 
ATOM   10962 O  O   . GLN   D  1 99  ? 8.753   22.118  -28.057  1.00 46.61  ? 400  GLN   D O   1 
ATOM   10963 C  CB  . GLN   D  1 99  ? 8.635   24.497  -26.191  1.00 48.87  ? 400  GLN   D CB  1 
ATOM   10964 C  CG  . GLN   D  1 99  ? 8.091   25.717  -25.500  1.00 42.93  ? 400  GLN   D CG  1 
ATOM   10965 C  CD  . GLN   D  1 99  ? 8.666   26.986  -26.084  1.00 49.47  ? 400  GLN   D CD  1 
ATOM   10966 O  OE1 . GLN   D  1 99  ? 9.882   27.192  -26.071  1.00 60.39  ? 400  GLN   D OE1 1 
ATOM   10967 N  NE2 . GLN   D  1 99  ? 7.796   27.837  -26.625  1.00 41.76  ? 400  GLN   D NE2 1 
ATOM   10968 N  N   . LEU   D  1 100 ? 10.212  23.534  -29.034  1.00 41.58  ? 401  LEU   D N   1 
ATOM   10969 C  CA  . LEU   D  1 100 ? 11.045  22.447  -29.523  1.00 41.27  ? 401  LEU   D CA  1 
ATOM   10970 C  C   . LEU   D  1 100 ? 11.833  21.834  -28.375  1.00 45.38  ? 401  LEU   D C   1 
ATOM   10971 O  O   . LEU   D  1 100 ? 12.312  22.541  -27.485  1.00 45.49  ? 401  LEU   D O   1 
ATOM   10972 C  CB  . LEU   D  1 100 ? 11.999  22.950  -30.608  1.00 28.98  ? 401  LEU   D CB  1 
ATOM   10973 C  CG  . LEU   D  1 100 ? 11.292  23.423  -31.882  1.00 31.46  ? 401  LEU   D CG  1 
ATOM   10974 C  CD1 . LEU   D  1 100 ? 12.248  24.225  -32.772  1.00 35.49  ? 401  LEU   D CD1 1 
ATOM   10975 C  CD2 . LEU   D  1 100 ? 10.727  22.220  -32.644  1.00 35.14  ? 401  LEU   D CD2 1 
ATOM   10976 N  N   . LYS   D  1 101 ? 11.950  20.507  -28.393  1.00 44.56  ? 402  LYS   D N   1 
ATOM   10977 C  CA  . LYS   D  1 101 ? 12.975  19.839  -27.606  1.00 36.28  ? 402  LYS   D CA  1 
ATOM   10978 C  C   . LYS   D  1 101 ? 14.352  20.238  -28.120  1.00 42.23  ? 402  LYS   D C   1 
ATOM   10979 O  O   . LYS   D  1 101 ? 14.509  20.684  -29.262  1.00 44.25  ? 402  LYS   D O   1 
ATOM   10980 C  CB  . LYS   D  1 101 ? 12.824  18.325  -27.702  1.00 36.15  ? 402  LYS   D CB  1 
ATOM   10981 C  CG  . LYS   D  1 101 ? 11.407  17.836  -27.540  1.00 52.12  ? 402  LYS   D CG  1 
ATOM   10982 C  CD  . LYS   D  1 101 ? 10.885  18.121  -26.123  1.00 60.75  ? 402  LYS   D CD  1 
ATOM   10983 C  CE  . LYS   D  1 101 ? 10.362  16.860  -25.461  1.00 63.93  ? 402  LYS   D CE  1 
ATOM   10984 N  NZ  . LYS   D  1 101 ? 9.207   17.171  -24.585  1.00 71.90  ? 402  LYS   D NZ  1 
ATOM   10985 N  N   . ASP   D  1 102 ? 15.360  20.044  -27.269  1.00 41.57  ? 403  ASP   D N   1 
ATOM   10986 C  CA  . ASP   D  1 102 ? 16.729  20.380  -27.642  1.00 41.61  ? 403  ASP   D CA  1 
ATOM   10987 C  C   . ASP   D  1 102 ? 17.181  19.580  -28.854  1.00 42.05  ? 403  ASP   D C   1 
ATOM   10988 O  O   . ASP   D  1 102 ? 17.885  20.102  -29.727  1.00 48.60  ? 403  ASP   D O   1 
ATOM   10989 C  CB  . ASP   D  1 102 ? 17.672  20.132  -26.460  1.00 50.99  ? 403  ASP   D CB  1 
ATOM   10990 C  CG  . ASP   D  1 102 ? 17.265  20.908  -25.198  1.00 59.64  ? 403  ASP   D CG  1 
ATOM   10991 O  OD1 . ASP   D  1 102 ? 16.270  21.673  -25.248  1.00 54.73  ? 403  ASP   D OD1 1 
ATOM   10992 O  OD2 . ASP   D  1 102 ? 17.945  20.743  -24.153  1.00 64.17  ? 403  ASP   D OD2 1 
ATOM   10993 N  N   . THR   D  1 103 ? 16.794  18.305  -28.923  1.00 45.33  ? 404  THR   D N   1 
ATOM   10994 C  CA  . THR   D  1 103 ? 17.169  17.478  -30.065  1.00 43.63  ? 404  THR   D CA  1 
ATOM   10995 C  C   . THR   D  1 103 ? 16.610  18.041  -31.368  1.00 40.81  ? 404  THR   D C   1 
ATOM   10996 O  O   . THR   D  1 103 ? 17.297  18.053  -32.391  1.00 43.07  ? 404  THR   D O   1 
ATOM   10997 C  CB  . THR   D  1 103 ? 16.666  16.058  -29.851  1.00 40.78  ? 404  THR   D CB  1 
ATOM   10998 O  OG1 . THR   D  1 103 ? 15.338  16.120  -29.321  1.00 48.32  ? 404  THR   D OG1 1 
ATOM   10999 C  CG2 . THR   D  1 103 ? 17.557  15.324  -28.876  1.00 37.27  ? 404  THR   D CG2 1 
ATOM   11000 N  N   . GLU   D  1 104 ? 15.358  18.502  -31.342  1.00 40.92  ? 405  GLU   D N   1 
ATOM   11001 C  CA  . GLU   D  1 104 ? 14.716  19.050  -32.527  1.00 45.05  ? 405  GLU   D CA  1 
ATOM   11002 C  C   . GLU   D  1 104 ? 15.377  20.354  -32.940  1.00 47.66  ? 405  GLU   D C   1 
ATOM   11003 O  O   . GLU   D  1 104 ? 15.599  20.598  -34.134  1.00 47.93  ? 405  GLU   D O   1 
ATOM   11004 C  CB  . GLU   D  1 104 ? 13.215  19.250  -32.258  1.00 42.36  ? 405  GLU   D CB  1 
ATOM   11005 C  CG  . GLU   D  1 104 ? 12.514  17.987  -31.754  1.00 38.53  ? 405  GLU   D CG  1 
ATOM   11006 C  CD  . GLU   D  1 104 ? 11.209  18.255  -31.016  1.00 40.42  ? 405  GLU   D CD  1 
ATOM   11007 O  OE1 . GLU   D  1 104 ? 10.371  17.333  -30.925  1.00 44.90  ? 405  GLU   D OE1 1 
ATOM   11008 O  OE2 . GLU   D  1 104 ? 11.018  19.379  -30.524  1.00 50.05  ? 405  GLU   D OE2 1 
ATOM   11009 N  N   . LEU   D  1 105 ? 15.722  21.187  -31.958  1.00 45.57  ? 406  LEU   D N   1 
ATOM   11010 C  CA  . LEU   D  1 105 ? 16.367  22.461  -32.244  1.00 45.29  ? 406  LEU   D CA  1 
ATOM   11011 C  C   . LEU   D  1 105 ? 17.704  22.255  -32.950  1.00 44.59  ? 406  LEU   D C   1 
ATOM   11012 O  O   . LEU   D  1 105 ? 18.005  22.930  -33.932  1.00 44.11  ? 406  LEU   D O   1 
ATOM   11013 C  CB  . LEU   D  1 105 ? 16.554  23.234  -30.945  1.00 37.13  ? 406  LEU   D CB  1 
ATOM   11014 C  CG  . LEU   D  1 105 ? 17.063  24.660  -31.084  1.00 34.67  ? 406  LEU   D CG  1 
ATOM   11015 C  CD1 . LEU   D  1 105 ? 15.941  25.604  -31.491  1.00 31.60  ? 406  LEU   D CD1 1 
ATOM   11016 C  CD2 . LEU   D  1 105 ? 17.704  25.090  -29.779  1.00 32.97  ? 406  LEU   D CD2 1 
ATOM   11017 N  N   . ILE   D  1 106 ? 18.521  21.329  -32.450  1.00 45.16  ? 407  ILE   D N   1 
ATOM   11018 C  CA  . ILE   D  1 106 ? 19.798  21.015  -33.086  1.00 36.78  ? 407  ILE   D CA  1 
ATOM   11019 C  C   . ILE   D  1 106 ? 19.567  20.480  -34.497  1.00 40.51  ? 407  ILE   D C   1 
ATOM   11020 O  O   . ILE   D  1 106 ? 20.217  20.907  -35.464  1.00 37.86  ? 407  ILE   D O   1 
ATOM   11021 C  CB  . ILE   D  1 106 ? 20.577  20.008  -32.220  1.00 34.61  ? 407  ILE   D CB  1 
ATOM   11022 C  CG1 . ILE   D  1 106 ? 21.109  20.662  -30.942  1.00 38.32  ? 407  ILE   D CG1 1 
ATOM   11023 C  CG2 . ILE   D  1 106 ? 21.686  19.339  -32.990  1.00 29.00  ? 407  ILE   D CG2 1 
ATOM   11024 C  CD1 . ILE   D  1 106 ? 21.377  19.632  -29.830  1.00 26.75  ? 407  ILE   D CD1 1 
ATOM   11025 N  N   . TYR   D  1 107 ? 18.625  19.540  -34.628  1.00 38.33  ? 408  TYR   D N   1 
ATOM   11026 C  CA  . TYR   D  1 107 ? 18.306  18.946  -35.915  1.00 41.26  ? 408  TYR   D CA  1 
ATOM   11027 C  C   . TYR   D  1 107 ? 17.762  19.986  -36.883  1.00 43.00  ? 408  TYR   D C   1 
ATOM   11028 O  O   . TYR   D  1 107 ? 18.103  19.973  -38.071  1.00 42.92  ? 408  TYR   D O   1 
ATOM   11029 C  CB  . TYR   D  1 107 ? 17.296  17.815  -35.724  1.00 38.75  ? 408  TYR   D CB  1 
ATOM   11030 C  CG  . TYR   D  1 107 ? 16.647  17.386  -37.018  1.00 36.31  ? 408  TYR   D CG  1 
ATOM   11031 C  CD1 . TYR   D  1 107 ? 15.504  18.026  -37.499  1.00 35.87  ? 408  TYR   D CD1 1 
ATOM   11032 C  CD2 . TYR   D  1 107 ? 17.172  16.339  -37.754  1.00 26.76  ? 408  TYR   D CD2 1 
ATOM   11033 C  CE1 . TYR   D  1 107 ? 14.915  17.639  -38.707  1.00 41.13  ? 408  TYR   D CE1 1 
ATOM   11034 C  CE2 . TYR   D  1 107 ? 16.576  15.928  -38.953  1.00 27.03  ? 408  TYR   D CE2 1 
ATOM   11035 C  CZ  . TYR   D  1 107 ? 15.462  16.584  -39.426  1.00 39.22  ? 408  TYR   D CZ  1 
ATOM   11036 O  OH  . TYR   D  1 107 ? 14.893  16.167  -40.606  1.00 44.97  ? 408  TYR   D OH  1 
ATOM   11037 N  N   . GLY   D  1 108 ? 16.887  20.869  -36.395  1.00 43.10  ? 409  GLY   D N   1 
ATOM   11038 C  CA  . GLY   D  1 108 ? 16.301  21.884  -37.255  1.00 36.56  ? 409  GLY   D CA  1 
ATOM   11039 C  C   . GLY   D  1 108 ? 17.328  22.885  -37.741  1.00 37.90  ? 409  GLY   D C   1 
ATOM   11040 O  O   . GLY   D  1 108 ? 17.334  23.267  -38.914  1.00 38.48  ? 409  GLY   D O   1 
ATOM   11041 N  N   . ALA   D  1 109 ? 18.228  23.298  -36.857  1.00 29.14  ? 410  ALA   D N   1 
ATOM   11042 C  CA  . ALA   D  1 109 ? 19.232  24.280  -37.230  1.00 33.66  ? 410  ALA   D CA  1 
ATOM   11043 C  C   . ALA   D  1 109 ? 20.256  23.688  -38.189  1.00 30.80  ? 410  ALA   D C   1 
ATOM   11044 O  O   . ALA   D  1 109 ? 20.711  24.370  -39.110  1.00 35.11  ? 410  ALA   D O   1 
ATOM   11045 C  CB  . ALA   D  1 109 ? 19.917  24.831  -35.978  1.00 33.40  ? 410  ALA   D CB  1 
ATOM   11046 N  N   . LYS   D  1 110 ? 20.633  22.429  -37.984  1.00 33.18  ? 411  LYS   D N   1 
ATOM   11047 C  CA  . LYS   D  1 110 ? 21.547  21.771  -38.905  1.00 29.94  ? 411  LYS   D CA  1 
ATOM   11048 C  C   . LYS   D  1 110 ? 20.908  21.613  -40.278  1.00 42.84  ? 411  LYS   D C   1 
ATOM   11049 O  O   . LYS   D  1 110 ? 21.564  21.820  -41.305  1.00 37.35  ? 411  LYS   D O   1 
ATOM   11050 C  CB  . LYS   D  1 110 ? 21.983  20.407  -38.356  1.00 29.25  ? 411  LYS   D CB  1 
ATOM   11051 C  CG  . LYS   D  1 110 ? 22.884  20.468  -37.093  1.00 34.59  ? 411  LYS   D CG  1 
ATOM   11052 C  CD  . LYS   D  1 110 ? 23.450  19.097  -36.736  1.00 30.57  ? 411  LYS   D CD  1 
ATOM   11053 C  CE  . LYS   D  1 110 ? 24.299  19.188  -35.495  1.00 42.60  ? 411  LYS   D CE  1 
ATOM   11054 N  NZ  . LYS   D  1 110 ? 25.210  18.036  -35.297  1.00 44.68  ? 411  LYS   D NZ  1 
ATOM   11055 N  N   . HIS   D  1 111 ? 19.620  21.275  -40.317  1.00 41.69  ? 412  HIS   D N   1 
ATOM   11056 C  CA  . HIS   D  1 111 ? 18.980  21.065  -41.611  1.00 42.82  ? 412  HIS   D CA  1 
ATOM   11057 C  C   . HIS   D  1 111 ? 18.637  22.373  -42.318  1.00 42.73  ? 412  HIS   D C   1 
ATOM   11058 O  O   . HIS   D  1 111 ? 18.665  22.427  -43.550  1.00 40.77  ? 412  HIS   D O   1 
ATOM   11059 C  CB  . HIS   D  1 111 ? 17.757  20.167  -41.440  1.00 37.70  ? 412  HIS   D CB  1 
ATOM   11060 C  CG  . HIS   D  1 111 ? 18.117  18.719  -41.435  1.00 39.91  ? 412  HIS   D CG  1 
ATOM   11061 N  ND1 . HIS   D  1 111 ? 18.727  18.110  -40.357  1.00 40.50  ? 412  HIS   D ND1 1 
ATOM   11062 C  CD2 . HIS   D  1 111 ? 18.043  17.781  -42.407  1.00 36.45  ? 412  HIS   D CD2 1 
ATOM   11063 C  CE1 . HIS   D  1 111 ? 18.988  16.852  -40.661  1.00 41.77  ? 412  HIS   D CE1 1 
ATOM   11064 N  NE2 . HIS   D  1 111 ? 18.580  16.626  -41.897  1.00 39.60  ? 412  HIS   D NE2 1 
ATOM   11065 N  N   . ALA   D  1 112 ? 18.363  23.439  -41.568  1.00 43.66  ? 413  ALA   D N   1 
ATOM   11066 C  CA  . ALA   D  1 112 ? 18.249  24.754  -42.178  1.00 41.14  ? 413  ALA   D CA  1 
ATOM   11067 C  C   . ALA   D  1 112 ? 19.522  25.131  -42.926  1.00 39.49  ? 413  ALA   D C   1 
ATOM   11068 O  O   . ALA   D  1 112 ? 19.470  25.753  -43.989  1.00 34.60  ? 413  ALA   D O   1 
ATOM   11069 C  CB  . ALA   D  1 112 ? 17.935  25.792  -41.104  1.00 34.82  ? 413  ALA   D CB  1 
ATOM   11070 N  N   . TRP   D  1 113 ? 20.682  24.797  -42.367  1.00 40.70  ? 414  TRP   D N   1 
ATOM   11071 C  CA  . TRP   D  1 113 ? 21.924  25.026  -43.091  1.00 37.73  ? 414  TRP   D CA  1 
ATOM   11072 C  C   . TRP   D  1 113 ? 22.019  24.095  -44.291  1.00 38.58  ? 414  TRP   D C   1 
ATOM   11073 O  O   . TRP   D  1 113 ? 22.368  24.524  -45.394  1.00 40.22  ? 414  TRP   D O   1 
ATOM   11074 C  CB  . TRP   D  1 113 ? 23.116  24.835  -42.156  1.00 35.73  ? 414  TRP   D CB  1 
ATOM   11075 C  CG  . TRP   D  1 113 ? 24.463  25.120  -42.761  1.00 37.72  ? 414  TRP   D CG  1 
ATOM   11076 C  CD1 . TRP   D  1 113 ? 24.723  25.734  -43.958  1.00 34.38  ? 414  TRP   D CD1 1 
ATOM   11077 C  CD2 . TRP   D  1 113 ? 25.743  24.798  -42.192  1.00 43.13  ? 414  TRP   D CD2 1 
ATOM   11078 N  NE1 . TRP   D  1 113 ? 26.080  25.819  -44.160  1.00 32.22  ? 414  TRP   D NE1 1 
ATOM   11079 C  CE2 . TRP   D  1 113 ? 26.729  25.241  -43.100  1.00 42.34  ? 414  TRP   D CE2 1 
ATOM   11080 C  CE3 . TRP   D  1 113 ? 26.151  24.186  -41.002  1.00 38.74  ? 414  TRP   D CE3 1 
ATOM   11081 C  CZ2 . TRP   D  1 113 ? 28.097  25.085  -42.855  1.00 38.74  ? 414  TRP   D CZ2 1 
ATOM   11082 C  CZ3 . TRP   D  1 113 ? 27.507  24.030  -40.766  1.00 33.47  ? 414  TRP   D CZ3 1 
ATOM   11083 C  CH2 . TRP   D  1 113 ? 28.463  24.488  -41.682  1.00 36.88  ? 414  TRP   D CH2 1 
ATOM   11084 N  N   . ARG   D  1 114 ? 21.701  22.820  -44.084  1.00 39.03  ? 415  ARG   D N   1 
ATOM   11085 C  CA  . ARG   D  1 114 ? 21.718  21.840  -45.159  1.00 33.86  ? 415  ARG   D CA  1 
ATOM   11086 C  C   . ARG   D  1 114 ? 20.859  22.276  -46.333  1.00 42.12  ? 415  ARG   D C   1 
ATOM   11087 O  O   . ARG   D  1 114 ? 21.195  21.989  -47.487  1.00 41.14  ? 415  ARG   D O   1 
ATOM   11088 C  CB  . ARG   D  1 114 ? 21.225  20.501  -44.626  1.00 30.27  ? 415  ARG   D CB  1 
ATOM   11089 C  CG  . ARG   D  1 114 ? 21.539  19.286  -45.488  1.00 31.65  ? 415  ARG   D CG  1 
ATOM   11090 C  CD  . ARG   D  1 114 ? 20.933  18.048  -44.867  1.00 35.20  ? 415  ARG   D CD  1 
ATOM   11091 N  NE  . ARG   D  1 114 ? 21.331  16.838  -45.568  1.00 38.11  ? 415  ARG   D NE  1 
ATOM   11092 C  CZ  . ARG   D  1 114 ? 20.935  15.619  -45.228  1.00 39.15  ? 415  ARG   D CZ  1 
ATOM   11093 N  NH1 . ARG   D  1 114 ? 21.344  14.558  -45.918  1.00 30.03  ? 415  ARG   D NH1 1 
ATOM   11094 N  NH2 . ARG   D  1 114 ? 20.148  15.465  -44.175  1.00 39.75  ? 415  ARG   D NH2 1 
ATOM   11095 N  N   . ASN   D  1 115 ? 19.757  22.965  -46.059  1.00 39.25  ? 416  ASN   D N   1 
ATOM   11096 C  CA  . ASN   D  1 115 ? 18.773  23.320  -47.071  1.00 35.29  ? 416  ASN   D CA  1 
ATOM   11097 C  C   . ASN   D  1 115 ? 19.018  24.693  -47.677  1.00 32.44  ? 416  ASN   D C   1 
ATOM   11098 O  O   . ASN   D  1 115 ? 18.192  25.148  -48.473  1.00 38.79  ? 416  ASN   D O   1 
ATOM   11099 C  CB  . ASN   D  1 115 ? 17.357  23.292  -46.478  1.00 34.16  ? 416  ASN   D CB  1 
ATOM   11100 C  CG  . ASN   D  1 115 ? 16.938  21.913  -46.013  1.00 29.46  ? 416  ASN   D CG  1 
ATOM   11101 O  OD1 . ASN   D  1 115 ? 17.455  20.906  -46.475  1.00 35.81  ? 416  ASN   D OD1 1 
ATOM   11102 N  ND2 . ASN   D  1 115 ? 15.980  21.865  -45.086  1.00 34.74  ? 416  ASN   D ND2 1 
ATOM   11103 N  N   . ALA   D  1 116 ? 20.108  25.366  -47.306  1.00 29.72  ? 417  ALA   D N   1 
ATOM   11104 C  CA  . ALA   D  1 116 ? 20.383  26.722  -47.764  1.00 34.08  ? 417  ALA   D CA  1 
ATOM   11105 C  C   . ALA   D  1 116 ? 20.958  26.648  -49.181  1.00 35.81  ? 417  ALA   D C   1 
ATOM   11106 O  O   . ALA   D  1 116 ? 22.160  26.516  -49.381  1.00 31.60  ? 417  ALA   D O   1 
ATOM   11107 C  CB  . ALA   D  1 116 ? 21.332  27.420  -46.796  1.00 33.09  ? 417  ALA   D CB  1 
ATOM   11108 N  N   . SER   D  1 117 ? 20.078  26.764  -50.180  1.00 39.41  ? 418  SER   D N   1 
ATOM   11109 C  CA  A SER   D  1 117 ? 20.501  26.518  -51.552  0.88 35.63  ? 418  SER   D CA  1 
ATOM   11110 C  CA  B SER   D  1 117 ? 20.472  26.546  -51.568  0.12 36.76  ? 418  SER   D CA  1 
ATOM   11111 C  C   . SER   D  1 117 ? 21.589  27.484  -52.007  1.00 39.32  ? 418  SER   D C   1 
ATOM   11112 O  O   . SER   D  1 117 ? 22.366  27.141  -52.901  1.00 40.50  ? 418  SER   D O   1 
ATOM   11113 C  CB  A SER   D  1 117 ? 19.291  26.585  -52.490  0.88 36.23  ? 418  SER   D CB  1 
ATOM   11114 C  CB  B SER   D  1 117 ? 19.258  26.717  -52.486  0.12 35.06  ? 418  SER   D CB  1 
ATOM   11115 O  OG  A SER   D  1 117 ? 18.716  27.878  -52.517  0.88 31.20  ? 418  SER   D OG  1 
ATOM   11116 O  OG  B SER   D  1 117 ? 18.194  25.868  -52.092  0.12 34.22  ? 418  SER   D OG  1 
ATOM   11117 N  N   . ARG   D  1 118 ? 21.698  28.662  -51.390  1.00 30.26  ? 419  ARG   D N   1 
ATOM   11118 C  CA  . ARG   D  1 118 ? 22.712  29.622  -51.803  1.00 32.09  ? 419  ARG   D CA  1 
ATOM   11119 C  C   . ARG   D  1 118 ? 24.066  29.428  -51.132  1.00 32.84  ? 419  ARG   D C   1 
ATOM   11120 O  O   . ARG   D  1 118 ? 24.977  30.205  -51.420  1.00 35.11  ? 419  ARG   D O   1 
ATOM   11121 C  CB  . ARG   D  1 118 ? 22.230  31.059  -51.550  1.00 36.33  ? 419  ARG   D CB  1 
ATOM   11122 C  CG  . ARG   D  1 118 ? 21.065  31.472  -52.424  1.00 34.63  ? 419  ARG   D CG  1 
ATOM   11123 C  CD  . ARG   D  1 118 ? 20.657  32.914  -52.244  1.00 36.21  ? 419  ARG   D CD  1 
ATOM   11124 N  NE  . ARG   D  1 118 ? 19.712  33.296  -53.301  1.00 37.99  ? 419  ARG   D NE  1 
ATOM   11125 C  CZ  . ARG   D  1 118 ? 19.016  34.429  -53.323  1.00 44.93  ? 419  ARG   D CZ  1 
ATOM   11126 N  NH1 . ARG   D  1 118 ? 19.157  35.315  -52.350  1.00 49.83  ? 419  ARG   D NH1 1 
ATOM   11127 N  NH2 . ARG   D  1 118 ? 18.169  34.675  -54.319  1.00 50.09  ? 419  ARG   D NH2 1 
ATOM   11128 N  N   . CYS   D  1 119 ? 24.246  28.428  -50.260  1.00 32.23  ? 420  CYS   D N   1 
ATOM   11129 C  CA  . CYS   D  1 119 ? 25.478  28.304  -49.480  1.00 30.71  ? 420  CYS   D CA  1 
ATOM   11130 C  C   . CYS   D  1 119 ? 26.385  27.228  -50.068  1.00 29.12  ? 420  CYS   D C   1 
ATOM   11131 O  O   . CYS   D  1 119 ? 25.997  26.056  -50.154  1.00 27.23  ? 420  CYS   D O   1 
ATOM   11132 C  CB  . CYS   D  1 119 ? 25.194  27.981  -48.011  1.00 36.77  ? 420  CYS   D CB  1 
ATOM   11133 S  SG  . CYS   D  1 119 ? 26.700  27.661  -47.021  1.00 36.45  ? 420  CYS   D SG  1 
ATOM   11134 N  N   . VAL   D  1 120 ? 27.616  27.619  -50.407  1.00 28.14  ? 421  VAL   D N   1 
ATOM   11135 C  CA  . VAL   D  1 120 ? 28.588  26.683  -50.963  1.00 30.22  ? 421  VAL   D CA  1 
ATOM   11136 C  C   . VAL   D  1 120 ? 29.334  25.887  -49.900  1.00 37.34  ? 421  VAL   D C   1 
ATOM   11137 O  O   . VAL   D  1 120 ? 30.044  24.933  -50.243  1.00 33.91  ? 421  VAL   D O   1 
ATOM   11138 C  CB  . VAL   D  1 120 ? 29.554  27.473  -51.866  1.00 36.54  ? 421  VAL   D CB  1 
ATOM   11139 C  CG1 . VAL   D  1 120 ? 30.434  28.424  -51.038  1.00 25.74  ? 421  VAL   D CG1 1 
ATOM   11140 C  CG2 . VAL   D  1 120 ? 30.378  26.536  -52.780  1.00 31.16  ? 421  VAL   D CG2 1 
ATOM   11141 N  N   . GLY   D  1 121 ? 29.160  26.206  -48.613  1.00 32.97  ? 422  GLY   D N   1 
ATOM   11142 C  CA  . GLY   D  1 121 ? 29.956  25.548  -47.590  1.00 26.69  ? 422  GLY   D CA  1 
ATOM   11143 C  C   . GLY   D  1 121 ? 29.265  24.382  -46.914  1.00 37.38  ? 422  GLY   D C   1 
ATOM   11144 O  O   . GLY   D  1 121 ? 29.687  23.953  -45.836  1.00 43.07  ? 422  GLY   D O   1 
ATOM   11145 N  N   . ARG   D  1 122 ? 28.213  23.844  -47.538  1.00 31.93  ? 423  ARG   D N   1 
ATOM   11146 C  CA  . ARG   D  1 122 ? 27.325  22.920  -46.854  1.00 29.92  ? 423  ARG   D CA  1 
ATOM   11147 C  C   . ARG   D  1 122 ? 27.902  21.529  -46.654  1.00 37.00  ? 423  ARG   D C   1 
ATOM   11148 O  O   . ARG   D  1 122 ? 27.293  20.735  -45.925  1.00 37.02  ? 423  ARG   D O   1 
ATOM   11149 C  CB  . ARG   D  1 122 ? 25.995  22.817  -47.582  1.00 29.04  ? 423  ARG   D CB  1 
ATOM   11150 C  CG  . ARG   D  1 122 ? 25.074  23.988  -47.339  1.00 31.09  ? 423  ARG   D CG  1 
ATOM   11151 C  CD  . ARG   D  1 122 ? 23.791  23.787  -48.121  1.00 40.76  ? 423  ARG   D CD  1 
ATOM   11152 N  NE  . ARG   D  1 122 ? 23.912  24.196  -49.523  1.00 37.16  ? 423  ARG   D NE  1 
ATOM   11153 C  CZ  . ARG   D  1 122 ? 23.055  23.836  -50.479  1.00 39.90  ? 423  ARG   D CZ  1 
ATOM   11154 N  NH1 . ARG   D  1 122 ? 22.033  23.029  -50.197  1.00 31.20  ? 423  ARG   D NH1 1 
ATOM   11155 N  NH2 . ARG   D  1 122 ? 23.220  24.277  -51.718  1.00 38.78  ? 423  ARG   D NH2 1 
ATOM   11156 N  N   . ILE   D  1 123 ? 29.058  21.212  -47.240  1.00 33.56  ? 424  ILE   D N   1 
ATOM   11157 C  CA  . ILE   D  1 123 ? 29.646  19.910  -46.947  1.00 35.45  ? 424  ILE   D CA  1 
ATOM   11158 C  C   . ILE   D  1 123 ? 29.854  19.752  -45.449  1.00 37.53  ? 424  ILE   D C   1 
ATOM   11159 O  O   . ILE   D  1 123 ? 29.874  18.631  -44.940  1.00 39.64  ? 424  ILE   D O   1 
ATOM   11160 C  CB  . ILE   D  1 123 ? 30.972  19.687  -47.701  1.00 35.10  ? 424  ILE   D CB  1 
ATOM   11161 C  CG1 . ILE   D  1 123 ? 31.421  18.225  -47.561  1.00 41.68  ? 424  ILE   D CG1 1 
ATOM   11162 C  CG2 . ILE   D  1 123 ? 32.050  20.579  -47.137  1.00 30.36  ? 424  ILE   D CG2 1 
ATOM   11163 C  CD1 . ILE   D  1 123 ? 32.515  17.800  -48.529  1.00 49.23  ? 424  ILE   D CD1 1 
ATOM   11164 N  N   . GLN   D  1 124 ? 29.995  20.862  -44.726  1.00 41.60  ? 425  GLN   D N   1 
ATOM   11165 C  CA  . GLN   D  1 124 ? 30.247  20.898  -43.289  1.00 50.39  ? 425  GLN   D CA  1 
ATOM   11166 C  C   . GLN   D  1 124 ? 28.972  20.865  -42.446  1.00 47.95  ? 425  GLN   D C   1 
ATOM   11167 O  O   . GLN   D  1 124 ? 29.066  20.953  -41.217  1.00 46.10  ? 425  GLN   D O   1 
ATOM   11168 C  CB  . GLN   D  1 124 ? 31.038  22.170  -42.929  1.00 50.71  ? 425  GLN   D CB  1 
ATOM   11169 C  CG  . GLN   D  1 124 ? 32.458  22.257  -43.466  1.00 50.11  ? 425  GLN   D CG  1 
ATOM   11170 C  CD  . GLN   D  1 124 ? 33.430  21.418  -42.663  1.00 55.77  ? 425  GLN   D CD  1 
ATOM   11171 O  OE1 . GLN   D  1 124 ? 33.092  20.914  -41.598  1.00 61.78  ? 425  GLN   D OE1 1 
ATOM   11172 N  NE2 . GLN   D  1 124 ? 34.644  21.267  -43.171  1.00 65.41  ? 425  GLN   D NE2 1 
ATOM   11173 N  N   . TRP   D  1 125 ? 27.795  20.732  -43.075  1.00 45.28  ? 426  TRP   D N   1 
ATOM   11174 C  CA  . TRP   D  1 125 ? 26.536  21.073  -42.414  1.00 38.74  ? 426  TRP   D CA  1 
ATOM   11175 C  C   . TRP   D  1 125 ? 26.301  20.274  -41.140  1.00 48.18  ? 426  TRP   D C   1 
ATOM   11176 O  O   . TRP   D  1 125 ? 25.645  20.767  -40.222  1.00 47.72  ? 426  TRP   D O   1 
ATOM   11177 C  CB  . TRP   D  1 125 ? 25.351  20.856  -43.346  1.00 32.61  ? 426  TRP   D CB  1 
ATOM   11178 C  CG  . TRP   D  1 125 ? 24.978  19.396  -43.551  1.00 32.57  ? 426  TRP   D CG  1 
ATOM   11179 C  CD1 . TRP   D  1 125 ? 25.448  18.561  -44.523  1.00 39.64  ? 426  TRP   D CD1 1 
ATOM   11180 C  CD2 . TRP   D  1 125 ? 24.043  18.625  -42.785  1.00 35.04  ? 426  TRP   D CD2 1 
ATOM   11181 N  NE1 . TRP   D  1 125 ? 24.880  17.315  -44.403  1.00 35.05  ? 426  TRP   D NE1 1 
ATOM   11182 C  CE2 . TRP   D  1 125 ? 24.011  17.328  -43.345  1.00 38.38  ? 426  TRP   D CE2 1 
ATOM   11183 C  CE3 . TRP   D  1 125 ? 23.237  18.900  -41.668  1.00 32.11  ? 426  TRP   D CE3 1 
ATOM   11184 C  CZ2 . TRP   D  1 125 ? 23.207  16.307  -42.827  1.00 44.35  ? 426  TRP   D CZ2 1 
ATOM   11185 C  CZ3 . TRP   D  1 125 ? 22.442  17.891  -41.163  1.00 29.15  ? 426  TRP   D CZ3 1 
ATOM   11186 C  CH2 . TRP   D  1 125 ? 22.432  16.607  -41.741  1.00 41.35  ? 426  TRP   D CH2 1 
ATOM   11187 N  N   . SER   D  1 126 ? 26.779  19.036  -41.070  1.00 44.36  ? 427  SER   D N   1 
ATOM   11188 C  CA  . SER   D  1 126 ? 26.460  18.265  -39.884  1.00 42.89  ? 427  SER   D CA  1 
ATOM   11189 C  C   . SER   D  1 126 ? 27.399  18.571  -38.722  1.00 46.61  ? 427  SER   D C   1 
ATOM   11190 O  O   . SER   D  1 126 ? 27.166  18.065  -37.625  1.00 38.56  ? 427  SER   D O   1 
ATOM   11191 C  CB  . SER   D  1 126 ? 26.478  16.771  -40.198  1.00 39.76  ? 427  SER   D CB  1 
ATOM   11192 O  OG  . SER   D  1 126 ? 27.807  16.284  -40.233  1.00 50.00  ? 427  SER   D OG  1 
ATOM   11193 N  N   . LYS   D  1 127 ? 28.439  19.383  -38.934  1.00 46.57  ? 428  LYS   D N   1 
ATOM   11194 C  CA  . LYS   D  1 127 ? 29.368  19.785  -37.877  1.00 47.47  ? 428  LYS   D CA  1 
ATOM   11195 C  C   . LYS   D  1 127 ? 29.054  21.228  -37.479  1.00 56.89  ? 428  LYS   D C   1 
ATOM   11196 O  O   . LYS   D  1 127 ? 29.713  22.180  -37.897  1.00 74.16  ? 428  LYS   D O   1 
ATOM   11197 C  CB  . LYS   D  1 127 ? 30.812  19.630  -38.349  1.00 50.77  ? 428  LYS   D CB  1 
ATOM   11198 C  CG  . LYS   D  1 127 ? 31.375  18.214  -38.253  1.00 66.22  ? 428  LYS   D CG  1 
ATOM   11199 C  CD  . LYS   D  1 127 ? 32.896  18.209  -38.426  1.00 81.28  ? 428  LYS   D CD  1 
ATOM   11200 C  CE  . LYS   D  1 127 ? 33.587  17.139  -37.561  1.00 89.88  ? 428  LYS   D CE  1 
ATOM   11201 N  NZ  . LYS   D  1 127 ? 33.505  17.398  -36.083  1.00 89.21  ? 428  LYS   D NZ  1 
ATOM   11202 N  N   . LEU   D  1 128 ? 28.022  21.389  -36.657  1.00 37.69  ? 429  LEU   D N   1 
ATOM   11203 C  CA  . LEU   D  1 128 ? 27.509  22.701  -36.287  1.00 35.37  ? 429  LEU   D CA  1 
ATOM   11204 C  C   . LEU   D  1 128 ? 27.223  22.696  -34.794  1.00 39.38  ? 429  LEU   D C   1 
ATOM   11205 O  O   . LEU   D  1 128 ? 26.511  21.819  -34.298  1.00 36.58  ? 429  LEU   D O   1 
ATOM   11206 C  CB  . LEU   D  1 128 ? 26.233  23.060  -37.075  1.00 26.23  ? 429  LEU   D CB  1 
ATOM   11207 C  CG  . LEU   D  1 128 ? 25.527  24.374  -36.669  1.00 28.08  ? 429  LEU   D CG  1 
ATOM   11208 C  CD1 . LEU   D  1 128 ? 26.326  25.662  -36.995  1.00 27.68  ? 429  LEU   D CD1 1 
ATOM   11209 C  CD2 . LEU   D  1 128 ? 24.086  24.477  -37.160  1.00 28.51  ? 429  LEU   D CD2 1 
ATOM   11210 N  N   . GLN   D  1 129 ? 27.792  23.654  -34.077  1.00 38.73  ? 430  GLN   D N   1 
ATOM   11211 C  CA  . GLN   D  1 129 ? 27.594  23.745  -32.640  1.00 33.37  ? 430  GLN   D CA  1 
ATOM   11212 C  C   . GLN   D  1 129 ? 26.384  24.637  -32.394  1.00 38.11  ? 430  GLN   D C   1 
ATOM   11213 O  O   . GLN   D  1 129 ? 26.396  25.821  -32.745  1.00 44.72  ? 430  GLN   D O   1 
ATOM   11214 C  CB  . GLN   D  1 129 ? 28.852  24.284  -31.968  1.00 43.56  ? 430  GLN   D CB  1 
ATOM   11215 C  CG  . GLN   D  1 129 ? 28.849  24.142  -30.456  1.00 47.70  ? 430  GLN   D CG  1 
ATOM   11216 C  CD  . GLN   D  1 129 ? 28.564  22.717  -29.993  1.00 51.82  ? 430  GLN   D CD  1 
ATOM   11217 O  OE1 . GLN   D  1 129 ? 29.283  21.770  -30.342  1.00 45.57  ? 430  GLN   D OE1 1 
ATOM   11218 N  NE2 . GLN   D  1 129 ? 27.505  22.560  -29.212  1.00 59.13  ? 430  GLN   D NE2 1 
ATOM   11219 N  N   . VAL   D  1 130 ? 25.317  24.065  -31.849  1.00 32.44  ? 431  VAL   D N   1 
ATOM   11220 C  CA  . VAL   D  1 130 ? 24.084  24.805  -31.610  1.00 35.54  ? 431  VAL   D CA  1 
ATOM   11221 C  C   . VAL   D  1 130 ? 24.096  25.289  -30.163  1.00 43.21  ? 431  VAL   D C   1 
ATOM   11222 O  O   . VAL   D  1 130 ? 24.251  24.490  -29.234  1.00 33.77  ? 431  VAL   D O   1 
ATOM   11223 C  CB  . VAL   D  1 130 ? 22.841  23.952  -31.902  1.00 38.01  ? 431  VAL   D CB  1 
ATOM   11224 C  CG1 . VAL   D  1 130 ? 21.589  24.763  -31.656  1.00 40.87  ? 431  VAL   D CG1 1 
ATOM   11225 C  CG2 . VAL   D  1 130 ? 22.860  23.456  -33.348  1.00 42.94  ? 431  VAL   D CG2 1 
ATOM   11226 N  N   . PHE   D  1 131 ? 23.974  26.598  -29.970  1.00 40.04  ? 432  PHE   D N   1 
ATOM   11227 C  CA  . PHE   D  1 131 ? 23.915  27.191  -28.638  1.00 33.62  ? 432  PHE   D CA  1 
ATOM   11228 C  C   . PHE   D  1 131 ? 22.471  27.601  -28.387  1.00 37.01  ? 432  PHE   D C   1 
ATOM   11229 O  O   . PHE   D  1 131 ? 21.959  28.513  -29.045  1.00 44.03  ? 432  PHE   D O   1 
ATOM   11230 C  CB  . PHE   D  1 131 ? 24.879  28.373  -28.515  1.00 28.97  ? 432  PHE   D CB  1 
ATOM   11231 C  CG  . PHE   D  1 131 ? 26.337  27.965  -28.476  1.00 32.95  ? 432  PHE   D CG  1 
ATOM   11232 C  CD1 . PHE   D  1 131 ? 26.841  27.219  -27.403  1.00 30.90  ? 432  PHE   D CD1 1 
ATOM   11233 C  CD2 . PHE   D  1 131 ? 27.208  28.331  -29.500  1.00 37.49  ? 432  PHE   D CD2 1 
ATOM   11234 C  CE1 . PHE   D  1 131 ? 28.169  26.841  -27.368  1.00 31.05  ? 432  PHE   D CE1 1 
ATOM   11235 C  CE2 . PHE   D  1 131 ? 28.544  27.962  -29.467  1.00 31.84  ? 432  PHE   D CE2 1 
ATOM   11236 C  CZ  . PHE   D  1 131 ? 29.027  27.214  -28.403  1.00 34.93  ? 432  PHE   D CZ  1 
ATOM   11237 N  N   . ASP   D  1 132 ? 21.809  26.902  -27.458  1.00 32.94  ? 433  ASP   D N   1 
ATOM   11238 C  CA  . ASP   D  1 132 ? 20.407  27.151  -27.130  1.00 32.28  ? 433  ASP   D CA  1 
ATOM   11239 C  C   . ASP   D  1 132 ? 20.326  28.359  -26.216  1.00 39.35  ? 433  ASP   D C   1 
ATOM   11240 O  O   . ASP   D  1 132 ? 20.690  28.278  -25.040  1.00 49.30  ? 433  ASP   D O   1 
ATOM   11241 C  CB  . ASP   D  1 132 ? 19.803  25.915  -26.463  1.00 31.02  ? 433  ASP   D CB  1 
ATOM   11242 C  CG  . ASP   D  1 132 ? 18.296  26.016  -26.261  1.00 39.62  ? 433  ASP   D CG  1 
ATOM   11243 O  OD1 . ASP   D  1 132 ? 17.726  27.118  -26.408  1.00 40.76  ? 433  ASP   D OD1 1 
ATOM   11244 O  OD2 . ASP   D  1 132 ? 17.672  24.969  -25.968  1.00 43.01  ? 433  ASP   D OD2 1 
ATOM   11245 N  N   . ALA   D  1 133 ? 19.845  29.481  -26.736  1.00 38.30  ? 434  ALA   D N   1 
ATOM   11246 C  CA  . ALA   D  1 133 ? 19.698  30.680  -25.920  1.00 32.98  ? 434  ALA   D CA  1 
ATOM   11247 C  C   . ALA   D  1 133 ? 18.236  31.071  -25.760  1.00 32.44  ? 434  ALA   D C   1 
ATOM   11248 O  O   . ALA   D  1 133 ? 17.910  32.248  -25.580  1.00 37.37  ? 434  ALA   D O   1 
ATOM   11249 C  CB  . ALA   D  1 133 ? 20.506  31.841  -26.492  1.00 32.21  ? 434  ALA   D CB  1 
ATOM   11250 N  N   . ARG   D  1 134 ? 17.346  30.083  -25.814  1.00 31.72  ? 435  ARG   D N   1 
ATOM   11251 C  CA  . ARG   D  1 134 ? 15.921  30.328  -25.642  1.00 36.44  ? 435  ARG   D CA  1 
ATOM   11252 C  C   . ARG   D  1 134 ? 15.535  30.734  -24.218  1.00 44.86  ? 435  ARG   D C   1 
ATOM   11253 O  O   . ARG   D  1 134 ? 14.384  31.127  -24.004  1.00 43.98  ? 435  ARG   D O   1 
ATOM   11254 C  CB  . ARG   D  1 134 ? 15.143  29.091  -26.085  1.00 34.88  ? 435  ARG   D CB  1 
ATOM   11255 C  CG  . ARG   D  1 134 ? 15.130  28.930  -27.622  1.00 35.59  ? 435  ARG   D CG  1 
ATOM   11256 C  CD  . ARG   D  1 134 ? 14.391  27.693  -28.007  1.00 36.38  ? 435  ARG   D CD  1 
ATOM   11257 N  NE  . ARG   D  1 134 ? 15.035  26.537  -27.400  1.00 39.22  ? 435  ARG   D NE  1 
ATOM   11258 C  CZ  . ARG   D  1 134 ? 14.497  25.329  -27.350  1.00 38.14  ? 435  ARG   D CZ  1 
ATOM   11259 N  NH1 . ARG   D  1 134 ? 13.298  25.127  -27.877  1.00 43.70  ? 435  ARG   D NH1 1 
ATOM   11260 N  NH2 . ARG   D  1 134 ? 15.147  24.333  -26.757  1.00 36.76  ? 435  ARG   D NH2 1 
ATOM   11261 N  N   . ASP   D  1 135 ? 16.452  30.685  -23.248  1.00 43.09  ? 436  ASP   D N   1 
ATOM   11262 C  CA  . ASP   D  1 135 ? 16.138  31.180  -21.910  1.00 45.90  ? 436  ASP   D CA  1 
ATOM   11263 C  C   . ASP   D  1 135 ? 16.479  32.654  -21.738  1.00 46.78  ? 436  ASP   D C   1 
ATOM   11264 O  O   . ASP   D  1 135 ? 16.234  33.210  -20.661  1.00 48.29  ? 436  ASP   D O   1 
ATOM   11265 C  CB  . ASP   D  1 135 ? 16.847  30.342  -20.827  1.00 43.64  ? 436  ASP   D CB  1 
ATOM   11266 C  CG  . ASP   D  1 135 ? 18.353  30.521  -20.822  1.00 46.22  ? 436  ASP   D CG  1 
ATOM   11267 O  OD1 . ASP   D  1 135 ? 18.916  31.032  -21.819  1.00 50.79  ? 436  ASP   D OD1 1 
ATOM   11268 O  OD2 . ASP   D  1 135 ? 18.983  30.112  -19.822  1.00 50.08  ? 436  ASP   D OD2 1 
ATOM   11269 N  N   . CYS   D  1 136 ? 16.992  33.302  -22.785  1.00 45.70  ? 437  CYS   D N   1 
ATOM   11270 C  CA  . CYS   D  1 136 ? 17.432  34.688  -22.688  1.00 38.10  ? 437  CYS   D CA  1 
ATOM   11271 C  C   . CYS   D  1 136 ? 16.236  35.627  -22.555  1.00 40.19  ? 437  CYS   D C   1 
ATOM   11272 O  O   . CYS   D  1 136 ? 15.170  35.377  -23.125  1.00 35.27  ? 437  CYS   D O   1 
ATOM   11273 C  CB  . CYS   D  1 136 ? 18.260  35.042  -23.924  1.00 34.45  ? 437  CYS   D CB  1 
ATOM   11274 S  SG  . CYS   D  1 136 ? 19.091  36.600  -23.837  1.00 36.13  ? 437  CYS   D SG  1 
ATOM   11275 N  N   . THR   D  1 137 ? 16.388  36.701  -21.757  1.00 35.83  ? 438  THR   D N   1 
ATOM   11276 C  CA  . THR   D  1 137 ? 15.282  37.638  -21.580  1.00 33.12  ? 438  THR   D CA  1 
ATOM   11277 C  C   . THR   D  1 137 ? 15.639  39.108  -21.778  1.00 39.67  ? 438  THR   D C   1 
ATOM   11278 O  O   . THR   D  1 137 ? 14.718  39.926  -21.898  1.00 43.15  ? 438  THR   D O   1 
ATOM   11279 C  CB  . THR   D  1 137 ? 14.629  37.483  -20.184  1.00 43.41  ? 438  THR   D CB  1 
ATOM   11280 O  OG1 . THR   D  1 137 ? 15.450  38.078  -19.166  1.00 35.93  ? 438  THR   D OG1 1 
ATOM   11281 C  CG2 . THR   D  1 137 ? 14.382  36.018  -19.848  1.00 42.92  ? 438  THR   D CG2 1 
ATOM   11282 N  N   . THR   D  1 138 ? 16.916  39.479  -21.810  1.00 37.91  ? 439  THR   D N   1 
ATOM   11283 C  CA  . THR   D  1 138 ? 17.287  40.886  -21.901  1.00 39.03  ? 439  THR   D CA  1 
ATOM   11284 C  C   . THR   D  1 138 ? 18.478  41.044  -22.841  1.00 39.42  ? 439  THR   D C   1 
ATOM   11285 O  O   . THR   D  1 138 ? 19.215  40.087  -23.113  1.00 46.41  ? 439  THR   D O   1 
ATOM   11286 C  CB  . THR   D  1 138 ? 17.676  41.502  -20.546  1.00 32.46  ? 439  THR   D CB  1 
ATOM   11287 O  OG1 . THR   D  1 138 ? 18.935  40.956  -20.133  1.00 33.21  ? 439  THR   D OG1 1 
ATOM   11288 C  CG2 . THR   D  1 138 ? 16.621  41.240  -19.471  1.00 34.65  ? 439  THR   D CG2 1 
ATOM   11289 N  N   . ALA   D  1 139 ? 18.684  42.290  -23.299  1.00 42.52  ? 440  ALA   D N   1 
ATOM   11290 C  CA  . ALA   D  1 139 ? 19.764  42.570  -24.250  1.00 42.72  ? 440  ALA   D CA  1 
ATOM   11291 C  C   . ALA   D  1 139 ? 21.124  42.234  -23.654  1.00 45.34  ? 440  ALA   D C   1 
ATOM   11292 O  O   . ALA   D  1 139 ? 21.983  41.667  -24.343  1.00 34.83  ? 440  ALA   D O   1 
ATOM   11293 C  CB  . ALA   D  1 139 ? 19.713  44.030  -24.699  1.00 39.12  ? 440  ALA   D CB  1 
ATOM   11294 N  N   . HIS   D  1 140 ? 21.325  42.538  -22.359  1.00 45.08  ? 441  HIS   D N   1 
ATOM   11295 C  CA  . HIS   D  1 140 ? 22.536  42.094  -21.670  1.00 36.86  ? 441  HIS   D CA  1 
ATOM   11296 C  C   . HIS   D  1 140 ? 22.720  40.586  -21.788  1.00 40.42  ? 441  HIS   D C   1 
ATOM   11297 O  O   . HIS   D  1 140 ? 23.831  40.106  -22.043  1.00 36.29  ? 441  HIS   D O   1 
ATOM   11298 C  CB  . HIS   D  1 140 ? 22.498  42.517  -20.195  1.00 37.52  ? 441  HIS   D CB  1 
ATOM   11299 C  CG  . HIS   D  1 140 ? 22.938  43.925  -19.969  1.00 34.51  ? 441  HIS   D CG  1 
ATOM   11300 N  ND1 . HIS   D  1 140 ? 22.088  45.000  -20.106  1.00 38.22  ? 441  HIS   D ND1 1 
ATOM   11301 C  CD2 . HIS   D  1 140 ? 24.154  44.439  -19.670  1.00 30.13  ? 441  HIS   D CD2 1 
ATOM   11302 C  CE1 . HIS   D  1 140 ? 22.756  46.114  -19.866  1.00 38.03  ? 441  HIS   D CE1 1 
ATOM   11303 N  NE2 . HIS   D  1 140 ? 24.014  45.803  -19.618  1.00 32.15  ? 441  HIS   D NE2 1 
ATOM   11304 N  N   . GLY   D  1 141 ? 21.638  39.823  -21.600  1.00 39.53  ? 442  GLY   D N   1 
ATOM   11305 C  CA  . GLY   D  1 141 ? 21.723  38.388  -21.797  1.00 37.08  ? 442  GLY   D CA  1 
ATOM   11306 C  C   . GLY   D  1 141 ? 22.172  38.017  -23.199  1.00 41.98  ? 442  GLY   D C   1 
ATOM   11307 O  O   . GLY   D  1 141 ? 23.039  37.155  -23.376  1.00 37.15  ? 442  GLY   D O   1 
ATOM   11308 N  N   . MET   D  1 142 ? 21.604  38.684  -24.213  1.00 40.11  ? 443  MET   D N   1 
ATOM   11309 C  CA  . MET   D  1 142 ? 22.012  38.445  -25.597  1.00 38.49  ? 443  MET   D CA  1 
ATOM   11310 C  C   . MET   D  1 142 ? 23.495  38.726  -25.808  1.00 37.94  ? 443  MET   D C   1 
ATOM   11311 O  O   . MET   D  1 142 ? 24.193  37.956  -26.489  1.00 32.08  ? 443  MET   D O   1 
ATOM   11312 C  CB  . MET   D  1 142 ? 21.176  39.307  -26.537  1.00 31.02  ? 443  MET   D CB  1 
ATOM   11313 C  CG  . MET   D  1 142 ? 19.704  38.982  -26.493  1.00 31.10  ? 443  MET   D CG  1 
ATOM   11314 S  SD  . MET   D  1 142 ? 18.708  40.122  -27.472  1.00 42.79  ? 443  MET   D SD  1 
ATOM   11315 C  CE  . MET   D  1 142 ? 18.975  39.506  -29.145  1.00 33.40  ? 443  MET   D CE  1 
ATOM   11316 N  N   . PHE   D  1 143 ? 23.990  39.828  -25.236  1.00 31.05  ? 444  PHE   D N   1 
ATOM   11317 C  CA  . PHE   D  1 143 ? 25.407  40.165  -25.345  1.00 34.18  ? 444  PHE   D CA  1 
ATOM   11318 C  C   . PHE   D  1 143 ? 26.287  39.060  -24.759  1.00 41.54  ? 444  PHE   D C   1 
ATOM   11319 O  O   . PHE   D  1 143 ? 27.284  38.656  -25.372  1.00 46.13  ? 444  PHE   D O   1 
ATOM   11320 C  CB  . PHE   D  1 143 ? 25.659  41.514  -24.655  1.00 39.89  ? 444  PHE   D CB  1 
ATOM   11321 C  CG  . PHE   D  1 143 ? 27.106  41.909  -24.593  1.00 39.64  ? 444  PHE   D CG  1 
ATOM   11322 C  CD1 . PHE   D  1 143 ? 27.766  42.366  -25.716  1.00 35.83  ? 444  PHE   D CD1 1 
ATOM   11323 C  CD2 . PHE   D  1 143 ? 27.806  41.813  -23.411  1.00 33.99  ? 444  PHE   D CD2 1 
ATOM   11324 C  CE1 . PHE   D  1 143 ? 29.091  42.727  -25.660  1.00 37.05  ? 444  PHE   D CE1 1 
ATOM   11325 C  CE2 . PHE   D  1 143 ? 29.142  42.161  -23.347  1.00 38.26  ? 444  PHE   D CE2 1 
ATOM   11326 C  CZ  . PHE   D  1 143 ? 29.783  42.624  -24.461  1.00 42.36  ? 444  PHE   D CZ  1 
ATOM   11327 N  N   . ASN   D  1 144 ? 25.928  38.558  -23.568  1.00 37.58  ? 445  ASN   D N   1 
ATOM   11328 C  CA  . ASN   D  1 144 ? 26.663  37.448  -22.958  1.00 39.21  ? 445  ASN   D CA  1 
ATOM   11329 C  C   . ASN   D  1 144 ? 26.679  36.222  -23.872  1.00 38.02  ? 445  ASN   D C   1 
ATOM   11330 O  O   . ASN   D  1 144 ? 27.724  35.600  -24.081  1.00 38.96  ? 445  ASN   D O   1 
ATOM   11331 C  CB  . ASN   D  1 144 ? 26.045  37.102  -21.590  1.00 37.35  ? 445  ASN   D CB  1 
ATOM   11332 C  CG  . ASN   D  1 144 ? 26.873  36.092  -20.802  1.00 40.29  ? 445  ASN   D CG  1 
ATOM   11333 O  OD1 . ASN   D  1 144 ? 28.084  36.238  -20.672  1.00 45.73  ? 445  ASN   D OD1 1 
ATOM   11334 N  ND2 . ASN   D  1 144 ? 26.221  35.054  -20.287  1.00 46.19  ? 445  ASN   D ND2 1 
ATOM   11335 N  N   . TYR   D  1 145 ? 25.526  35.861  -24.432  1.00 38.67  ? 446  TYR   D N   1 
ATOM   11336 C  CA  . TYR   D  1 145 ? 25.481  34.734  -25.362  1.00 38.58  ? 446  TYR   D CA  1 
ATOM   11337 C  C   . TYR   D  1 145 ? 26.310  34.991  -26.626  1.00 38.02  ? 446  TYR   D C   1 
ATOM   11338 O  O   . TYR   D  1 145 ? 26.970  34.079  -27.139  1.00 36.65  ? 446  TYR   D O   1 
ATOM   11339 C  CB  . TYR   D  1 145 ? 24.034  34.428  -25.740  1.00 40.41  ? 446  TYR   D CB  1 
ATOM   11340 C  CG  . TYR   D  1 145 ? 23.323  33.455  -24.826  1.00 34.96  ? 446  TYR   D CG  1 
ATOM   11341 C  CD1 . TYR   D  1 145 ? 23.689  32.113  -24.796  1.00 31.09  ? 446  TYR   D CD1 1 
ATOM   11342 C  CD2 . TYR   D  1 145 ? 22.259  33.872  -24.018  1.00 29.80  ? 446  TYR   D CD2 1 
ATOM   11343 C  CE1 . TYR   D  1 145 ? 23.023  31.202  -23.979  1.00 32.86  ? 446  TYR   D CE1 1 
ATOM   11344 C  CE2 . TYR   D  1 145 ? 21.571  32.961  -23.203  1.00 27.41  ? 446  TYR   D CE2 1 
ATOM   11345 C  CZ  . TYR   D  1 145 ? 21.975  31.637  -23.176  1.00 31.45  ? 446  TYR   D CZ  1 
ATOM   11346 O  OH  . TYR   D  1 145 ? 21.328  30.727  -22.369  1.00 39.12  ? 446  TYR   D OH  1 
ATOM   11347 N  N   . ILE   D  1 146 ? 26.291  36.215  -27.149  1.00 35.79  ? 447  ILE   D N   1 
ATOM   11348 C  CA  . ILE   D  1 146 ? 26.995  36.458  -28.413  1.00 37.10  ? 447  ILE   D CA  1 
ATOM   11349 C  C   . ILE   D  1 146 ? 28.500  36.486  -28.196  1.00 35.80  ? 447  ILE   D C   1 
ATOM   11350 O  O   . ILE   D  1 146 ? 29.264  36.020  -29.053  1.00 29.05  ? 447  ILE   D O   1 
ATOM   11351 C  CB  . ILE   D  1 146 ? 26.463  37.745  -29.084  1.00 32.09  ? 447  ILE   D CB  1 
ATOM   11352 C  CG1 . ILE   D  1 146 ? 25.019  37.517  -29.537  1.00 31.63  ? 447  ILE   D CG1 1 
ATOM   11353 C  CG2 . ILE   D  1 146 ? 27.334  38.171  -30.254  1.00 36.60  ? 447  ILE   D CG2 1 
ATOM   11354 C  CD1 . ILE   D  1 146 ? 24.264  38.763  -29.981  1.00 34.49  ? 447  ILE   D CD1 1 
ATOM   11355 N  N   . CYS   D  1 147 ? 28.955  36.984  -27.034  1.00 44.37  ? 448  CYS   D N   1 
ATOM   11356 C  CA  . CYS   D  1 147 ? 30.381  36.929  -26.712  1.00 33.99  ? 448  CYS   D CA  1 
ATOM   11357 C  C   . CYS   D  1 147 ? 30.875  35.492  -26.626  1.00 37.08  ? 448  CYS   D C   1 
ATOM   11358 O  O   . CYS   D  1 147 ? 31.945  35.156  -27.152  1.00 42.68  ? 448  CYS   D O   1 
ATOM   11359 C  CB  . CYS   D  1 147 ? 30.661  37.647  -25.394  1.00 39.18  ? 448  CYS   D CB  1 
ATOM   11360 S  SG  . CYS   D  1 147 ? 30.529  39.404  -25.477  1.00 37.28  ? 448  CYS   D SG  1 
ATOM   11361 N  N   . ASN   D  1 148 ? 30.126  34.632  -25.939  1.00 37.15  ? 449  ASN   D N   1 
ATOM   11362 C  CA  . ASN   D  1 148 ? 30.555  33.244  -25.840  1.00 32.65  ? 449  ASN   D CA  1 
ATOM   11363 C  C   . ASN   D  1 148 ? 30.538  32.585  -27.220  1.00 30.43  ? 449  ASN   D C   1 
ATOM   11364 O  O   . ASN   D  1 148 ? 31.416  31.777  -27.541  1.00 34.08  ? 449  ASN   D O   1 
ATOM   11365 C  CB  . ASN   D  1 148 ? 29.671  32.475  -24.844  1.00 25.24  ? 449  ASN   D CB  1 
ATOM   11366 C  CG  . ASN   D  1 148 ? 29.780  33.000  -23.379  1.00 39.41  ? 449  ASN   D CG  1 
ATOM   11367 O  OD1 . ASN   D  1 148 ? 30.747  33.671  -22.991  1.00 33.11  ? 449  ASN   D OD1 1 
ATOM   11368 N  ND2 . ASN   D  1 148 ? 28.770  32.667  -22.567  1.00 34.89  ? 449  ASN   D ND2 1 
ATOM   11369 N  N   . HIS   D  1 149 ? 29.550  32.929  -28.052  1.00 36.05  ? 450  HIS   D N   1 
ATOM   11370 C  CA  . HIS   D  1 149 ? 29.546  32.458  -29.439  1.00 32.49  ? 450  HIS   D CA  1 
ATOM   11371 C  C   . HIS   D  1 149 ? 30.838  32.845  -30.144  1.00 31.00  ? 450  HIS   D C   1 
ATOM   11372 O  O   . HIS   D  1 149 ? 31.541  31.988  -30.695  1.00 35.53  ? 450  HIS   D O   1 
ATOM   11373 C  CB  . HIS   D  1 149 ? 28.328  33.015  -30.184  1.00 30.40  ? 450  HIS   D CB  1 
ATOM   11374 C  CG  . HIS   D  1 149 ? 28.200  32.545  -31.615  1.00 39.47  ? 450  HIS   D CG  1 
ATOM   11375 N  ND1 . HIS   D  1 149 ? 27.025  32.034  -32.123  1.00 35.38  ? 450  HIS   D ND1 1 
ATOM   11376 C  CD2 . HIS   D  1 149 ? 29.079  32.558  -32.650  1.00 35.76  ? 450  HIS   D CD2 1 
ATOM   11377 C  CE1 . HIS   D  1 149 ? 27.194  31.727  -33.399  1.00 42.86  ? 450  HIS   D CE1 1 
ATOM   11378 N  NE2 . HIS   D  1 149 ? 28.434  32.028  -33.739  1.00 36.36  ? 450  HIS   D NE2 1 
ATOM   11379 N  N   . VAL   D  1 150 ? 31.184  34.135  -30.115  1.00 33.12  ? 451  VAL   D N   1 
ATOM   11380 C  CA  . VAL   D  1 150 ? 32.347  34.603  -30.869  1.00 29.54  ? 451  VAL   D CA  1 
ATOM   11381 C  C   . VAL   D  1 150 ? 33.613  33.908  -30.392  1.00 37.79  ? 451  VAL   D C   1 
ATOM   11382 O  O   . VAL   D  1 150 ? 34.430  33.433  -31.195  1.00 36.99  ? 451  VAL   D O   1 
ATOM   11383 C  CB  . VAL   D  1 150 ? 32.470  36.128  -30.757  1.00 31.17  ? 451  VAL   D CB  1 
ATOM   11384 C  CG1 . VAL   D  1 150 ? 33.873  36.563  -31.122  1.00 28.30  ? 451  VAL   D CG1 1 
ATOM   11385 C  CG2 . VAL   D  1 150 ? 31.441  36.792  -31.653  1.00 31.92  ? 451  VAL   D CG2 1 
ATOM   11386 N  N   . LYS   D  1 151 ? 33.787  33.834  -29.069  1.00 38.06  ? 452  LYS   D N   1 
ATOM   11387 C  CA  . LYS   D  1 151 ? 34.991  33.247  -28.505  1.00 36.18  ? 452  LYS   D CA  1 
ATOM   11388 C  C   . LYS   D  1 151 ? 35.108  31.783  -28.897  1.00 31.09  ? 452  LYS   D C   1 
ATOM   11389 O  O   . LYS   D  1 151 ? 36.186  31.317  -29.284  1.00 33.34  ? 452  LYS   D O   1 
ATOM   11390 C  CB  . LYS   D  1 151 ? 34.974  33.411  -26.975  1.00 35.38  ? 452  LYS   D CB  1 
ATOM   11391 C  CG  . LYS   D  1 151 ? 36.184  32.867  -26.267  1.00 33.31  ? 452  LYS   D CG  1 
ATOM   11392 C  CD  . LYS   D  1 151 ? 36.213  33.411  -24.831  1.00 33.29  ? 452  LYS   D CD  1 
ATOM   11393 C  CE  . LYS   D  1 151 ? 37.516  33.104  -24.123  1.00 37.94  ? 452  LYS   D CE  1 
ATOM   11394 N  NZ  . LYS   D  1 151 ? 37.705  33.935  -22.902  1.00 40.22  ? 452  LYS   D NZ  1 
ATOM   11395 N  N   . TYR   D  1 152 ? 34.004  31.044  -28.793  1.00 29.46  ? 453  TYR   D N   1 
ATOM   11396 C  CA  . TYR   D  1 152 ? 33.995  29.635  -29.166  1.00 37.27  ? 453  TYR   D CA  1 
ATOM   11397 C  C   . TYR   D  1 152 ? 34.273  29.450  -30.659  1.00 35.08  ? 453  TYR   D C   1 
ATOM   11398 O  O   . TYR   D  1 152 ? 35.053  28.576  -31.052  1.00 35.37  ? 453  TYR   D O   1 
ATOM   11399 C  CB  . TYR   D  1 152 ? 32.648  29.002  -28.810  1.00 34.28  ? 453  TYR   D CB  1 
ATOM   11400 C  CG  . TYR   D  1 152 ? 32.528  27.616  -29.399  1.00 40.53  ? 453  TYR   D CG  1 
ATOM   11401 C  CD1 . TYR   D  1 152 ? 33.042  26.518  -28.722  1.00 42.47  ? 453  TYR   D CD1 1 
ATOM   11402 C  CD2 . TYR   D  1 152 ? 31.947  27.405  -30.648  1.00 43.37  ? 453  TYR   D CD2 1 
ATOM   11403 C  CE1 . TYR   D  1 152 ? 32.966  25.262  -29.249  1.00 42.78  ? 453  TYR   D CE1 1 
ATOM   11404 C  CE2 . TYR   D  1 152 ? 31.874  26.144  -31.190  1.00 42.18  ? 453  TYR   D CE2 1 
ATOM   11405 C  CZ  . TYR   D  1 152 ? 32.387  25.077  -30.487  1.00 42.98  ? 453  TYR   D CZ  1 
ATOM   11406 O  OH  . TYR   D  1 152 ? 32.319  23.804  -31.002  1.00 46.83  ? 453  TYR   D OH  1 
ATOM   11407 N  N   . ALA   D  1 153 ? 33.585  30.225  -31.500  1.00 37.13  ? 454  ALA   D N   1 
ATOM   11408 C  CA  . ALA   D  1 153 ? 33.730  30.092  -32.952  1.00 37.90  ? 454  ALA   D CA  1 
ATOM   11409 C  C   . ALA   D  1 153 ? 35.137  30.435  -33.411  1.00 37.17  ? 454  ALA   D C   1 
ATOM   11410 O  O   . ALA   D  1 153 ? 35.711  29.720  -34.235  1.00 40.82  ? 454  ALA   D O   1 
ATOM   11411 C  CB  . ALA   D  1 153 ? 32.725  30.986  -33.663  1.00 22.12  ? 454  ALA   D CB  1 
ATOM   11412 N  N   . THR   D  1 154 ? 35.717  31.512  -32.862  1.00 39.72  ? 455  THR   D N   1 
ATOM   11413 C  CA  . THR   D  1 154 ? 37.007  32.010  -33.326  1.00 32.78  ? 455  THR   D CA  1 
ATOM   11414 C  C   . THR   D  1 154 ? 38.138  31.033  -33.015  1.00 43.54  ? 455  THR   D C   1 
ATOM   11415 O  O   . THR   D  1 154 ? 39.032  30.834  -33.852  1.00 49.36  ? 455  THR   D O   1 
ATOM   11416 C  CB  . THR   D  1 154 ? 37.283  33.392  -32.720  1.00 37.41  ? 455  THR   D CB  1 
ATOM   11417 O  OG1 . THR   D  1 154 ? 36.282  34.324  -33.150  1.00 40.55  ? 455  THR   D OG1 1 
ATOM   11418 C  CG2 . THR   D  1 154 ? 38.639  33.910  -33.148  1.00 32.81  ? 455  THR   D CG2 1 
ATOM   11419 N  N   . ASN   D  1 155 ? 38.128  30.433  -31.814  1.00 45.54  ? 456  ASN   D N   1 
ATOM   11420 C  CA  . ASN   D  1 155 ? 39.041  29.345  -31.428  1.00 29.01  ? 456  ASN   D CA  1 
ATOM   11421 C  C   . ASN   D  1 155 ? 40.498  29.644  -31.770  1.00 37.80  ? 456  ASN   D C   1 
ATOM   11422 O  O   . ASN   D  1 155 ? 41.247  28.764  -32.204  1.00 42.51  ? 456  ASN   D O   1 
ATOM   11423 C  CB  . ASN   D  1 155 ? 38.615  28.017  -32.057  1.00 28.49  ? 456  ASN   D CB  1 
ATOM   11424 C  CG  . ASN   D  1 155 ? 39.273  26.821  -31.394  1.00 37.73  ? 456  ASN   D CG  1 
ATOM   11425 O  OD1 . ASN   D  1 155 ? 39.445  26.789  -30.177  1.00 48.43  ? 456  ASN   D OD1 1 
ATOM   11426 N  ND2 . ASN   D  1 155 ? 39.646  25.835  -32.189  1.00 35.83  ? 456  ASN   D ND2 1 
ATOM   11427 N  N   . LYS   D  1 156 ? 40.911  30.894  -31.559  1.00 38.28  ? 457  LYS   D N   1 
ATOM   11428 C  CA  . LYS   D  1 156 ? 42.285  31.332  -31.813  1.00 33.32  ? 457  LYS   D CA  1 
ATOM   11429 C  C   . LYS   D  1 156 ? 42.704  31.153  -33.276  1.00 36.98  ? 457  LYS   D C   1 
ATOM   11430 O  O   . LYS   D  1 156 ? 43.884  30.963  -33.570  1.00 35.21  ? 457  LYS   D O   1 
ATOM   11431 C  CB  . LYS   D  1 156 ? 43.272  30.623  -30.886  1.00 37.47  ? 457  LYS   D CB  1 
ATOM   11432 C  CG  . LYS   D  1 156 ? 43.225  31.157  -29.462  1.00 50.70  ? 457  LYS   D CG  1 
ATOM   11433 C  CD  . LYS   D  1 156 ? 44.590  31.128  -28.821  1.00 65.33  ? 457  LYS   D CD  1 
ATOM   11434 C  CE  . LYS   D  1 156 ? 44.889  29.765  -28.227  1.00 77.22  ? 457  LYS   D CE  1 
ATOM   11435 N  NZ  . LYS   D  1 156 ? 44.171  29.531  -26.933  1.00 77.13  ? 457  LYS   D NZ  1 
ATOM   11436 N  N   . GLY   D  1 157 ? 41.742  31.224  -34.202  1.00 37.38  ? 458  GLY   D N   1 
ATOM   11437 C  CA  . GLY   D  1 157 ? 42.009  31.112  -35.611  1.00 40.53  ? 458  GLY   D CA  1 
ATOM   11438 C  C   . GLY   D  1 157 ? 41.626  29.782  -36.210  1.00 42.59  ? 458  GLY   D C   1 
ATOM   11439 O  O   . GLY   D  1 157 ? 41.515  29.669  -37.442  1.00 40.39  ? 458  GLY   D O   1 
ATOM   11440 N  N   . ASN   D  1 158 ? 41.409  28.773  -35.377  1.00 39.01  ? 459  ASN   D N   1 
ATOM   11441 C  CA  . ASN   D  1 158 ? 40.975  27.478  -35.880  1.00 45.67  ? 459  ASN   D CA  1 
ATOM   11442 C  C   . ASN   D  1 158 ? 39.448  27.451  -35.840  1.00 48.38  ? 459  ASN   D C   1 
ATOM   11443 O  O   . ASN   D  1 158 ? 38.831  26.873  -34.946  1.00 52.66  ? 459  ASN   D O   1 
ATOM   11444 C  CB  . ASN   D  1 158 ? 41.607  26.367  -35.062  1.00 46.09  ? 459  ASN   D CB  1 
ATOM   11445 C  CG  . ASN   D  1 158 ? 41.232  25.017  -35.567  1.00 49.02  ? 459  ASN   D CG  1 
ATOM   11446 O  OD1 . ASN   D  1 158 ? 40.763  24.878  -36.696  1.00 53.79  ? 459  ASN   D OD1 1 
ATOM   11447 N  ND2 . ASN   D  1 158 ? 41.418  24.005  -34.741  1.00 42.75  ? 459  ASN   D ND2 1 
ATOM   11448 N  N   . LEU   D  1 159 ? 38.830  28.090  -36.842  1.00 44.68  ? 460  LEU   D N   1 
ATOM   11449 C  CA  . LEU   D  1 159 ? 37.427  28.483  -36.736  1.00 43.03  ? 460  LEU   D CA  1 
ATOM   11450 C  C   . LEU   D  1 159 ? 36.487  27.281  -36.729  1.00 42.13  ? 460  LEU   D C   1 
ATOM   11451 O  O   . LEU   D  1 159 ? 36.726  26.263  -37.388  1.00 38.65  ? 460  LEU   D O   1 
ATOM   11452 C  CB  . LEU   D  1 159 ? 37.040  29.416  -37.877  1.00 39.67  ? 460  LEU   D CB  1 
ATOM   11453 C  CG  . LEU   D  1 159 ? 37.944  30.646  -38.020  1.00 51.42  ? 460  LEU   D CG  1 
ATOM   11454 C  CD1 . LEU   D  1 159 ? 37.691  31.412  -39.343  1.00 47.66  ? 460  LEU   D CD1 1 
ATOM   11455 C  CD2 . LEU   D  1 159 ? 37.789  31.562  -36.834  1.00 41.48  ? 460  LEU   D CD2 1 
ATOM   11456 N  N   . ARG   D  1 160 ? 35.393  27.426  -35.976  1.00 34.07  ? 461  ARG   D N   1 
ATOM   11457 C  CA  . ARG   D  1 160 ? 34.399  26.383  -35.775  1.00 36.11  ? 461  ARG   D CA  1 
ATOM   11458 C  C   . ARG   D  1 160 ? 33.009  26.957  -36.002  1.00 38.12  ? 461  ARG   D C   1 
ATOM   11459 O  O   . ARG   D  1 160 ? 32.690  28.042  -35.507  1.00 36.11  ? 461  ARG   D O   1 
ATOM   11460 C  CB  . ARG   D  1 160 ? 34.461  25.787  -34.344  1.00 38.49  ? 461  ARG   D CB  1 
ATOM   11461 C  CG  . ARG   D  1 160 ? 35.777  25.202  -33.970  1.00 35.91  ? 461  ARG   D CG  1 
ATOM   11462 C  CD  . ARG   D  1 160 ? 35.733  24.623  -32.571  1.00 39.86  ? 461  ARG   D CD  1 
ATOM   11463 N  NE  . ARG   D  1 160 ? 35.735  25.615  -31.507  1.00 36.64  ? 461  ARG   D NE  1 
ATOM   11464 C  CZ  . ARG   D  1 160 ? 36.116  25.321  -30.270  1.00 43.16  ? 461  ARG   D CZ  1 
ATOM   11465 N  NH1 . ARG   D  1 160 ? 36.503  24.090  -29.998  1.00 45.10  ? 461  ARG   D NH1 1 
ATOM   11466 N  NH2 . ARG   D  1 160 ? 36.117  26.234  -29.313  1.00 37.23  ? 461  ARG   D NH2 1 
ATOM   11467 N  N   . SER   D  1 161 ? 32.174  26.206  -36.719  1.00 34.74  ? 462  SER   D N   1 
ATOM   11468 C  CA  . SER   D  1 161 ? 30.838  26.676  -37.053  1.00 41.33  ? 462  SER   D CA  1 
ATOM   11469 C  C   . SER   D  1 161 ? 29.910  26.619  -35.848  1.00 35.45  ? 462  SER   D C   1 
ATOM   11470 O  O   . SER   D  1 161 ? 29.902  25.644  -35.088  1.00 36.14  ? 462  SER   D O   1 
ATOM   11471 C  CB  . SER   D  1 161 ? 30.256  25.835  -38.185  1.00 46.93  ? 462  SER   D CB  1 
ATOM   11472 O  OG  . SER   D  1 161 ? 31.241  25.627  -39.170  1.00 58.56  ? 462  SER   D OG  1 
ATOM   11473 N  N   . ALA   D  1 162 ? 29.080  27.646  -35.714  1.00 35.84  ? 463  ALA   D N   1 
ATOM   11474 C  CA  . ALA   D  1 162 ? 28.225  27.739  -34.540  1.00 35.99  ? 463  ALA   D CA  1 
ATOM   11475 C  C   . ALA   D  1 162 ? 27.037  28.631  -34.848  1.00 34.75  ? 463  ALA   D C   1 
ATOM   11476 O  O   . ALA   D  1 162 ? 27.107  29.507  -35.714  1.00 37.70  ? 463  ALA   D O   1 
ATOM   11477 C  CB  . ALA   D  1 162 ? 28.998  28.287  -33.328  1.00 29.47  ? 463  ALA   D CB  1 
ATOM   11478 N  N   . ILE   D  1 163 ? 25.955  28.400  -34.108  1.00 41.66  ? 464  ILE   D N   1 
ATOM   11479 C  CA  . ILE   D  1 163 ? 24.741  29.202  -34.173  1.00 37.68  ? 464  ILE   D CA  1 
ATOM   11480 C  C   . ILE   D  1 163 ? 24.216  29.388  -32.749  1.00 41.47  ? 464  ILE   D C   1 
ATOM   11481 O  O   . ILE   D  1 163 ? 24.291  28.478  -31.915  1.00 45.19  ? 464  ILE   D O   1 
ATOM   11482 C  CB  . ILE   D  1 163 ? 23.689  28.554  -35.104  1.00 26.47  ? 464  ILE   D CB  1 
ATOM   11483 C  CG1 . ILE   D  1 163 ? 22.474  29.470  -35.276  1.00 26.85  ? 464  ILE   D CG1 1 
ATOM   11484 C  CG2 . ILE   D  1 163 ? 23.275  27.199  -34.584  1.00 30.91  ? 464  ILE   D CG2 1 
ATOM   11485 C  CD1 . ILE   D  1 163 ? 21.451  28.990  -36.313  1.00 32.94  ? 464  ILE   D CD1 1 
ATOM   11486 N  N   . THR   D  1 164 ? 23.725  30.584  -32.454  1.00 41.68  ? 465  THR   D N   1 
ATOM   11487 C  CA  . THR   D  1 164 ? 23.076  30.871  -31.183  1.00 34.58  ? 465  THR   D CA  1 
ATOM   11488 C  C   . THR   D  1 164 ? 21.639  31.257  -31.472  1.00 34.81  ? 465  THR   D C   1 
ATOM   11489 O  O   . THR   D  1 164 ? 21.395  32.237  -32.179  1.00 36.75  ? 465  THR   D O   1 
ATOM   11490 C  CB  . THR   D  1 164 ? 23.781  31.997  -30.424  1.00 34.73  ? 465  THR   D CB  1 
ATOM   11491 O  OG1 . THR   D  1 164 ? 25.132  31.609  -30.150  1.00 27.44  ? 465  THR   D OG1 1 
ATOM   11492 C  CG2 . THR   D  1 164 ? 23.033  32.288  -29.095  1.00 26.83  ? 465  THR   D CG2 1 
ATOM   11493 N  N   . ILE   D  1 165 ? 20.696  30.512  -30.903  1.00 37.91  ? 466  ILE   D N   1 
ATOM   11494 C  CA  . ILE   D  1 165 ? 19.278  30.645  -31.211  1.00 35.22  ? 466  ILE   D CA  1 
ATOM   11495 C  C   . ILE   D  1 165 ? 18.564  31.293  -30.027  1.00 48.72  ? 466  ILE   D C   1 
ATOM   11496 O  O   . ILE   D  1 165 ? 18.574  30.765  -28.909  1.00 44.52  ? 466  ILE   D O   1 
ATOM   11497 C  CB  . ILE   D  1 165 ? 18.664  29.283  -31.555  1.00 34.61  ? 466  ILE   D CB  1 
ATOM   11498 C  CG1 . ILE   D  1 165 ? 19.436  28.648  -32.726  1.00 35.93  ? 466  ILE   D CG1 1 
ATOM   11499 C  CG2 . ILE   D  1 165 ? 17.177  29.444  -31.823  1.00 32.27  ? 466  ILE   D CG2 1 
ATOM   11500 C  CD1 . ILE   D  1 165 ? 19.029  27.212  -33.036  1.00 37.16  ? 466  ILE   D CD1 1 
ATOM   11501 N  N   . PHE   D  1 166 ? 17.929  32.418  -30.276  1.00 51.96  ? 467  PHE   D N   1 
ATOM   11502 C  CA  . PHE   D  1 166 ? 17.248  33.195  -29.258  1.00 36.52  ? 467  PHE   D CA  1 
ATOM   11503 C  C   . PHE   D  1 166 ? 15.762  32.875  -29.258  1.00 37.88  ? 467  PHE   D C   1 
ATOM   11504 O  O   . PHE   D  1 166 ? 15.275  32.157  -30.135  1.00 43.59  ? 467  PHE   D O   1 
ATOM   11505 C  CB  . PHE   D  1 166 ? 17.517  34.679  -29.498  1.00 34.72  ? 467  PHE   D CB  1 
ATOM   11506 C  CG  . PHE   D  1 166 ? 18.890  35.087  -29.077  1.00 37.50  ? 467  PHE   D CG  1 
ATOM   11507 C  CD1 . PHE   D  1 166 ? 19.210  35.155  -27.730  1.00 33.89  ? 467  PHE   D CD1 1 
ATOM   11508 C  CD2 . PHE   D  1 166 ? 19.877  35.345  -30.009  1.00 35.59  ? 467  PHE   D CD2 1 
ATOM   11509 C  CE1 . PHE   D  1 166 ? 20.482  35.507  -27.317  1.00 37.57  ? 467  PHE   D CE1 1 
ATOM   11510 C  CE2 . PHE   D  1 166 ? 21.157  35.699  -29.603  1.00 43.51  ? 467  PHE   D CE2 1 
ATOM   11511 C  CZ  . PHE   D  1 166 ? 21.460  35.781  -28.251  1.00 40.16  ? 467  PHE   D CZ  1 
ATOM   11512 N  N   . PRO   D  1 167 ? 15.006  33.360  -28.261  1.00 40.51  ? 468  PRO   D N   1 
ATOM   11513 C  CA  . PRO   D  1 167 ? 13.601  32.934  -28.137  1.00 40.26  ? 468  PRO   D CA  1 
ATOM   11514 C  C   . PRO   D  1 167 ? 12.801  33.221  -29.402  1.00 38.99  ? 468  PRO   D C   1 
ATOM   11515 O  O   . PRO   D  1 167 ? 12.949  34.274  -30.023  1.00 37.21  ? 468  PRO   D O   1 
ATOM   11516 C  CB  . PRO   D  1 167 ? 13.082  33.754  -26.944  1.00 41.38  ? 468  PRO   D CB  1 
ATOM   11517 C  CG  . PRO   D  1 167 ? 14.291  34.003  -26.113  1.00 38.22  ? 468  PRO   D CG  1 
ATOM   11518 C  CD  . PRO   D  1 167 ? 15.431  34.165  -27.096  1.00 40.44  ? 468  PRO   D CD  1 
ATOM   11519 N  N   . GLN   D  1 168 ? 11.953  32.256  -29.780  1.00 35.53  ? 469  GLN   D N   1 
ATOM   11520 C  CA  . GLN   D  1 168 ? 11.177  32.346  -31.011  1.00 35.84  ? 469  GLN   D CA  1 
ATOM   11521 C  C   . GLN   D  1 168 ? 10.164  33.476  -30.931  1.00 45.20  ? 469  GLN   D C   1 
ATOM   11522 O  O   . GLN   D  1 168 ? 9.822   33.979  -29.852  1.00 37.95  ? 469  GLN   D O   1 
ATOM   11523 C  CB  . GLN   D  1 168 ? 10.425  31.049  -31.280  1.00 35.10  ? 469  GLN   D CB  1 
ATOM   11524 C  CG  . GLN   D  1 168 ? 9.273   30.785  -30.290  1.00 32.81  ? 469  GLN   D CG  1 
ATOM   11525 C  CD  . GLN   D  1 168 ? 9.147   29.329  -29.950  1.00 35.90  ? 469  GLN   D CD  1 
ATOM   11526 O  OE1 . GLN   D  1 168 ? 10.147  28.650  -29.767  1.00 41.23  ? 469  GLN   D OE1 1 
ATOM   11527 N  NE2 . GLN   D  1 168 ? 7.913   28.825  -29.892  1.00 40.36  ? 469  GLN   D NE2 1 
ATOM   11528 N  N   . ARG   D  1 169 ? 9.656   33.846  -32.099  1.00 47.00  ? 470  ARG   D N   1 
ATOM   11529 C  CA  . ARG   D  1 169 ? 8.599   34.838  -32.174  1.00 47.18  ? 470  ARG   D CA  1 
ATOM   11530 C  C   . ARG   D  1 169 ? 7.374   34.350  -31.402  1.00 41.63  ? 470  ARG   D C   1 
ATOM   11531 O  O   . ARG   D  1 169 ? 7.148   33.147  -31.264  1.00 44.48  ? 470  ARG   D O   1 
ATOM   11532 C  CB  . ARG   D  1 169 ? 8.260   35.108  -33.639  1.00 49.18  ? 470  ARG   D CB  1 
ATOM   11533 C  CG  . ARG   D  1 169 ? 7.150   36.102  -33.851  1.00 55.78  ? 470  ARG   D CG  1 
ATOM   11534 C  CD  . ARG   D  1 169 ? 7.131   36.606  -35.279  1.00 58.01  ? 470  ARG   D CD  1 
ATOM   11535 N  NE  . ARG   D  1 169 ? 8.274   37.458  -35.567  1.00 52.53  ? 470  ARG   D NE  1 
ATOM   11536 C  CZ  . ARG   D  1 169 ? 8.725   37.677  -36.791  1.00 59.33  ? 470  ARG   D CZ  1 
ATOM   11537 N  NH1 . ARG   D  1 169 ? 8.119   37.091  -37.812  1.00 71.96  ? 470  ARG   D NH1 1 
ATOM   11538 N  NH2 . ARG   D  1 169 ? 9.776   38.463  -36.995  1.00 54.11  ? 470  ARG   D NH2 1 
ATOM   11539 N  N   . THR   D  1 170 ? 6.605   35.298  -30.856  1.00 36.81  ? 471  THR   D N   1 
ATOM   11540 C  CA  . THR   D  1 170 ? 5.339   34.976  -30.212  1.00 41.49  ? 471  THR   D CA  1 
ATOM   11541 C  C   . THR   D  1 170 ? 4.204   35.700  -30.923  1.00 45.53  ? 471  THR   D C   1 
ATOM   11542 O  O   . THR   D  1 170 ? 3.544   35.124  -31.779  1.00 42.98  ? 471  THR   D O   1 
ATOM   11543 C  CB  . THR   D  1 170 ? 5.329   35.333  -28.715  1.00 45.60  ? 471  THR   D CB  1 
ATOM   11544 O  OG1 . THR   D  1 170 ? 5.452   36.749  -28.541  1.00 58.18  ? 471  THR   D OG1 1 
ATOM   11545 C  CG2 . THR   D  1 170 ? 6.474   34.654  -27.979  1.00 35.77  ? 471  THR   D CG2 1 
ATOM   11546 N  N   . ASP   D  1 171 ? 3.975   36.957  -30.574  1.00 53.95  ? 472  ASP   D N   1 
ATOM   11547 C  CA  . ASP   D  1 171 ? 2.951   37.749  -31.255  1.00 54.80  ? 472  ASP   D CA  1 
ATOM   11548 C  C   . ASP   D  1 171 ? 3.537   38.730  -32.259  1.00 60.93  ? 472  ASP   D C   1 
ATOM   11549 O  O   . ASP   D  1 171 ? 2.808   39.556  -32.800  1.00 68.96  ? 472  ASP   D O   1 
ATOM   11550 C  CB  . ASP   D  1 171 ? 2.078   38.487  -30.229  1.00 61.27  ? 472  ASP   D CB  1 
ATOM   11551 C  CG  . ASP   D  1 171 ? 2.858   39.444  -29.341  1.00 63.77  ? 472  ASP   D CG  1 
ATOM   11552 O  OD1 . ASP   D  1 171 ? 4.087   39.566  -29.483  1.00 64.12  ? 472  ASP   D OD1 1 
ATOM   11553 O  OD2 . ASP   D  1 171 ? 2.217   40.091  -28.487  1.00 67.34  ? 472  ASP   D OD2 1 
ATOM   11554 N  N   . GLY   D  1 172 ? 4.841   38.630  -32.542  1.00 60.64  ? 473  GLY   D N   1 
ATOM   11555 C  CA  . GLY   D  1 172 ? 5.490   39.584  -33.418  1.00 54.75  ? 473  GLY   D CA  1 
ATOM   11556 C  C   . GLY   D  1 172 ? 5.717   40.948  -32.809  1.00 57.81  ? 473  GLY   D C   1 
ATOM   11557 O  O   . GLY   D  1 172 ? 6.338   41.800  -33.455  1.00 51.84  ? 473  GLY   D O   1 
ATOM   11558 N  N   . LYS   D  1 173 ? 5.244   41.179  -31.583  1.00 55.90  ? 474  LYS   D N   1 
ATOM   11559 C  CA  . LYS   D  1 173 ? 5.468   42.424  -30.867  1.00 56.12  ? 474  LYS   D CA  1 
ATOM   11560 C  C   . LYS   D  1 173 ? 6.527   42.275  -29.786  1.00 55.13  ? 474  LYS   D C   1 
ATOM   11561 O  O   . LYS   D  1 173 ? 6.795   43.232  -29.055  1.00 55.74  ? 474  LYS   D O   1 
ATOM   11562 C  CB  . LYS   D  1 173 ? 4.147   42.927  -30.270  1.00 61.30  ? 474  LYS   D CB  1 
ATOM   11563 C  CG  . LYS   D  1 173 ? 2.953   42.713  -31.200  1.00 74.54  ? 474  LYS   D CG  1 
ATOM   11564 C  CD  . LYS   D  1 173 ? 2.222   43.999  -31.562  1.00 86.43  ? 474  LYS   D CD  1 
ATOM   11565 C  CE  . LYS   D  1 173 ? 1.359   44.478  -30.403  1.00 96.39  ? 474  LYS   D CE  1 
ATOM   11566 N  NZ  . LYS   D  1 173 ? 0.340   43.462  -29.998  1.00 100.46 ? 474  LYS   D NZ  1 
ATOM   11567 N  N   . HIS   D  1 174 ? 7.150   41.105  -29.686  1.00 56.79  ? 475  HIS   D N   1 
ATOM   11568 C  CA  . HIS   D  1 174 ? 8.179   40.838  -28.690  1.00 53.28  ? 475  HIS   D CA  1 
ATOM   11569 C  C   . HIS   D  1 174 ? 9.367   40.133  -29.318  1.00 49.95  ? 475  HIS   D C   1 
ATOM   11570 O  O   . HIS   D  1 174 ? 9.962   39.233  -28.720  1.00 42.50  ? 475  HIS   D O   1 
ATOM   11571 C  CB  . HIS   D  1 174 ? 7.609   40.021  -27.536  1.00 54.06  ? 475  HIS   D CB  1 
ATOM   11572 C  CG  . HIS   D  1 174 ? 6.484   40.703  -26.829  1.00 59.88  ? 475  HIS   D CG  1 
ATOM   11573 N  ND1 . HIS   D  1 174 ? 5.189   40.685  -27.302  1.00 61.81  ? 475  HIS   D ND1 1 
ATOM   11574 C  CD2 . HIS   D  1 174 ? 6.464   41.448  -25.699  1.00 62.66  ? 475  HIS   D CD2 1 
ATOM   11575 C  CE1 . HIS   D  1 174 ? 4.418   41.380  -26.487  1.00 65.32  ? 475  HIS   D CE1 1 
ATOM   11576 N  NE2 . HIS   D  1 174 ? 5.166   41.851  -25.503  1.00 65.42  ? 475  HIS   D NE2 1 
ATOM   11577 N  N   . ASP   D  1 175 ? 9.731   40.538  -30.536  1.00 51.27  ? 476  ASP   D N   1 
ATOM   11578 C  CA  . ASP   D  1 175 ? 10.820  39.884  -31.251  1.00 47.44  ? 476  ASP   D CA  1 
ATOM   11579 C  C   . ASP   D  1 175 ? 12.161  40.150  -30.565  1.00 39.35  ? 476  ASP   D C   1 
ATOM   11580 O  O   . ASP   D  1 175 ? 12.431  41.252  -30.084  1.00 47.54  ? 476  ASP   D O   1 
ATOM   11581 C  CB  . ASP   D  1 175 ? 10.882  40.369  -32.708  1.00 58.33  ? 476  ASP   D CB  1 
ATOM   11582 C  CG  . ASP   D  1 175 ? 9.692   39.908  -33.557  1.00 59.87  ? 476  ASP   D CG  1 
ATOM   11583 O  OD1 . ASP   D  1 175 ? 8.784   39.229  -33.033  1.00 58.09  ? 476  ASP   D OD1 1 
ATOM   11584 O  OD2 . ASP   D  1 175 ? 9.678   40.232  -34.767  1.00 57.81  ? 476  ASP   D OD2 1 
ATOM   11585 N  N   . PHE   D  1 176 ? 12.985  39.116  -30.486  1.00 35.85  ? 477  PHE   D N   1 
ATOM   11586 C  CA  . PHE   D  1 176 ? 14.415  39.288  -30.321  1.00 36.58  ? 477  PHE   D CA  1 
ATOM   11587 C  C   . PHE   D  1 176 ? 15.033  39.506  -31.706  1.00 49.33  ? 477  PHE   D C   1 
ATOM   11588 O  O   . PHE   D  1 176 ? 14.673  38.831  -32.681  1.00 43.01  ? 477  PHE   D O   1 
ATOM   11589 C  CB  . PHE   D  1 176 ? 15.041  38.064  -29.655  1.00 29.35  ? 477  PHE   D CB  1 
ATOM   11590 C  CG  . PHE   D  1 176 ? 14.664  37.874  -28.199  1.00 41.42  ? 477  PHE   D CG  1 
ATOM   11591 C  CD1 . PHE   D  1 176 ? 13.379  37.496  -27.833  1.00 39.90  ? 477  PHE   D CD1 1 
ATOM   11592 C  CD2 . PHE   D  1 176 ? 15.621  38.011  -27.201  1.00 36.55  ? 477  PHE   D CD2 1 
ATOM   11593 C  CE1 . PHE   D  1 176 ? 13.053  37.292  -26.507  1.00 46.56  ? 477  PHE   D CE1 1 
ATOM   11594 C  CE2 . PHE   D  1 176 ? 15.294  37.808  -25.866  1.00 42.05  ? 477  PHE   D CE2 1 
ATOM   11595 C  CZ  . PHE   D  1 176 ? 14.009  37.450  -25.522  1.00 45.38  ? 477  PHE   D CZ  1 
ATOM   11596 N  N   . ARG   D  1 177 ? 15.961  40.454  -31.787  1.00 49.08  ? 478  ARG   D N   1 
ATOM   11597 C  CA  . ARG   D  1 177 ? 16.628  40.791  -33.033  1.00 41.57  ? 478  ARG   D CA  1 
ATOM   11598 C  C   . ARG   D  1 177 ? 18.061  41.201  -32.732  1.00 37.12  ? 478  ARG   D C   1 
ATOM   11599 O  O   . ARG   D  1 177 ? 18.306  41.968  -31.798  1.00 41.04  ? 478  ARG   D O   1 
ATOM   11600 C  CB  . ARG   D  1 177 ? 15.912  41.944  -33.756  1.00 31.98  ? 478  ARG   D CB  1 
ATOM   11601 C  CG  . ARG   D  1 177 ? 14.531  41.617  -34.277  1.00 36.91  ? 478  ARG   D CG  1 
ATOM   11602 C  CD  . ARG   D  1 177 ? 14.550  40.508  -35.354  1.00 41.99  ? 478  ARG   D CD  1 
ATOM   11603 N  NE  . ARG   D  1 177 ? 15.335  40.826  -36.549  1.00 43.05  ? 478  ARG   D NE  1 
ATOM   11604 C  CZ  . ARG   D  1 177 ? 14.882  41.521  -37.594  1.00 40.26  ? 478  ARG   D CZ  1 
ATOM   11605 N  NH1 . ARG   D  1 177 ? 13.651  42.019  -37.593  1.00 35.09  ? 478  ARG   D NH1 1 
ATOM   11606 N  NH2 . ARG   D  1 177 ? 15.673  41.724  -38.642  1.00 34.20  ? 478  ARG   D NH2 1 
ATOM   11607 N  N   . VAL   D  1 178 ? 19.003  40.717  -33.536  1.00 40.39  ? 479  VAL   D N   1 
ATOM   11608 C  CA  . VAL   D  1 178 ? 20.302  41.364  -33.653  1.00 38.42  ? 479  VAL   D CA  1 
ATOM   11609 C  C   . VAL   D  1 178 ? 20.184  42.377  -34.784  1.00 43.20  ? 479  VAL   D C   1 
ATOM   11610 O  O   . VAL   D  1 178 ? 19.976  42.003  -35.941  1.00 47.23  ? 479  VAL   D O   1 
ATOM   11611 C  CB  . VAL   D  1 178 ? 21.426  40.363  -33.925  1.00 37.90  ? 479  VAL   D CB  1 
ATOM   11612 C  CG1 . VAL   D  1 178 ? 22.763  41.080  -33.898  1.00 40.27  ? 479  VAL   D CG1 1 
ATOM   11613 C  CG2 . VAL   D  1 178 ? 21.410  39.222  -32.919  1.00 36.67  ? 479  VAL   D CG2 1 
ATOM   11614 N  N   . TRP   D  1 179 ? 20.317  43.666  -34.457  1.00 40.02  ? 480  TRP   D N   1 
ATOM   11615 C  CA  . TRP   D  1 179 ? 20.169  44.683  -35.496  1.00 39.14  ? 480  TRP   D CA  1 
ATOM   11616 C  C   . TRP   D  1 179 ? 21.353  44.698  -36.464  1.00 37.35  ? 480  TRP   D C   1 
ATOM   11617 O  O   . TRP   D  1 179 ? 21.181  45.051  -37.633  1.00 39.08  ? 480  TRP   D O   1 
ATOM   11618 C  CB  . TRP   D  1 179 ? 19.963  46.062  -34.868  1.00 41.02  ? 480  TRP   D CB  1 
ATOM   11619 C  CG  . TRP   D  1 179 ? 18.567  46.246  -34.314  1.00 38.93  ? 480  TRP   D CG  1 
ATOM   11620 C  CD1 . TRP   D  1 179 ? 17.785  45.291  -33.729  1.00 32.57  ? 480  TRP   D CD1 1 
ATOM   11621 C  CD2 . TRP   D  1 179 ? 17.782  47.450  -34.333  1.00 35.19  ? 480  TRP   D CD2 1 
ATOM   11622 N  NE1 . TRP   D  1 179 ? 16.573  45.831  -33.367  1.00 33.13  ? 480  TRP   D NE1 1 
ATOM   11623 C  CE2 . TRP   D  1 179 ? 16.546  47.152  -33.729  1.00 36.67  ? 480  TRP   D CE2 1 
ATOM   11624 C  CE3 . TRP   D  1 179 ? 18.003  48.744  -34.803  1.00 34.21  ? 480  TRP   D CE3 1 
ATOM   11625 C  CZ2 . TRP   D  1 179 ? 15.537  48.100  -33.591  1.00 37.43  ? 480  TRP   D CZ2 1 
ATOM   11626 C  CZ3 . TRP   D  1 179 ? 17.006  49.680  -34.665  1.00 43.11  ? 480  TRP   D CZ3 1 
ATOM   11627 C  CH2 . TRP   D  1 179 ? 15.791  49.358  -34.058  1.00 43.71  ? 480  TRP   D CH2 1 
ATOM   11628 N  N   . ASN   D  1 180 ? 22.541  44.321  -36.000  1.00 33.05  ? 481  ASN   D N   1 
ATOM   11629 C  CA  . ASN   D  1 180 ? 23.694  44.108  -36.869  1.00 34.27  ? 481  ASN   D CA  1 
ATOM   11630 C  C   . ASN   D  1 180 ? 23.401  43.061  -37.932  1.00 34.91  ? 481  ASN   D C   1 
ATOM   11631 O  O   . ASN   D  1 180 ? 22.773  42.037  -37.647  1.00 34.08  ? 481  ASN   D O   1 
ATOM   11632 C  CB  . ASN   D  1 180 ? 24.886  43.635  -36.038  1.00 32.53  ? 481  ASN   D CB  1 
ATOM   11633 C  CG  . ASN   D  1 180 ? 25.130  44.500  -34.847  1.00 36.98  ? 481  ASN   D CG  1 
ATOM   11634 O  OD1 . ASN   D  1 180 ? 24.324  44.554  -33.917  1.00 40.08  ? 481  ASN   D OD1 1 
ATOM   11635 N  ND2 . ASN   D  1 180 ? 26.254  45.189  -34.857  1.00 41.87  ? 481  ASN   D ND2 1 
ATOM   11636 N  N   . SER   D  1 181 ? 23.896  43.295  -39.159  1.00 32.35  ? 482  SER   D N   1 
ATOM   11637 C  CA  . SER   D  1 181 ? 23.709  42.290  -40.201  1.00 27.30  ? 482  SER   D CA  1 
ATOM   11638 C  C   . SER   D  1 181 ? 24.703  41.156  -40.024  1.00 32.20  ? 482  SER   D C   1 
ATOM   11639 O  O   . SER   D  1 181 ? 24.347  39.979  -40.201  1.00 32.91  ? 482  SER   D O   1 
ATOM   11640 C  CB  . SER   D  1 181 ? 23.805  42.916  -41.610  1.00 38.14  ? 482  SER   D CB  1 
ATOM   11641 O  OG  . SER   D  1 181 ? 25.017  43.620  -41.847  1.00 33.98  ? 482  SER   D OG  1 
ATOM   11642 N  N   . GLN   D  1 182 ? 25.940  41.486  -39.637  1.00 34.90  ? 483  GLN   D N   1 
ATOM   11643 C  CA  . GLN   D  1 182 ? 26.905  40.515  -39.140  1.00 37.66  ? 483  GLN   D CA  1 
ATOM   11644 C  C   . GLN   D  1 182 ? 27.380  40.947  -37.755  1.00 40.74  ? 483  GLN   D C   1 
ATOM   11645 O  O   . GLN   D  1 182 ? 27.298  42.128  -37.401  1.00 38.70  ? 483  GLN   D O   1 
ATOM   11646 C  CB  . GLN   D  1 182 ? 28.107  40.362  -40.085  1.00 38.84  ? 483  GLN   D CB  1 
ATOM   11647 C  CG  . GLN   D  1 182 ? 27.810  39.681  -41.422  1.00 44.13  ? 483  GLN   D CG  1 
ATOM   11648 C  CD  . GLN   D  1 182 ? 28.891  39.969  -42.469  1.00 50.39  ? 483  GLN   D CD  1 
ATOM   11649 O  OE1 . GLN   D  1 182 ? 30.055  39.575  -42.320  1.00 47.66  ? 483  GLN   D OE1 1 
ATOM   11650 N  NE2 . GLN   D  1 182 ? 28.512  40.687  -43.514  1.00 51.38  ? 483  GLN   D NE2 1 
ATOM   11651 N  N   . LEU   D  1 183 ? 27.884  39.984  -36.962  1.00 37.85  ? 484  LEU   D N   1 
ATOM   11652 C  CA  . LEU   D  1 183 ? 28.324  40.317  -35.600  1.00 36.49  ? 484  LEU   D CA  1 
ATOM   11653 C  C   . LEU   D  1 183 ? 29.568  41.197  -35.630  1.00 37.68  ? 484  LEU   D C   1 
ATOM   11654 O  O   . LEU   D  1 183 ? 29.690  42.147  -34.847  1.00 36.46  ? 484  LEU   D O   1 
ATOM   11655 C  CB  . LEU   D  1 183 ? 28.583  39.050  -34.763  1.00 29.49  ? 484  LEU   D CB  1 
ATOM   11656 C  CG  . LEU   D  1 183 ? 27.468  38.011  -34.575  1.00 27.53  ? 484  LEU   D CG  1 
ATOM   11657 C  CD1 . LEU   D  1 183 ? 27.947  36.769  -33.829  1.00 21.79  ? 484  LEU   D CD1 1 
ATOM   11658 C  CD2 . LEU   D  1 183 ? 26.239  38.601  -33.920  1.00 24.21  ? 484  LEU   D CD2 1 
ATOM   11659 N  N   . ILE   D  1 184 ? 30.498  40.913  -36.531  1.00 32.59  ? 485  ILE   D N   1 
ATOM   11660 C  CA  . ILE   D  1 184 ? 31.697  41.728  -36.679  1.00 36.27  ? 485  ILE   D CA  1 
ATOM   11661 C  C   . ILE   D  1 184 ? 31.661  42.379  -38.064  1.00 39.37  ? 485  ILE   D C   1 
ATOM   11662 O  O   . ILE   D  1 184 ? 31.778  41.686  -39.077  1.00 37.76  ? 485  ILE   D O   1 
ATOM   11663 C  CB  . ILE   D  1 184 ? 32.968  40.895  -36.480  1.00 31.52  ? 485  ILE   D CB  1 
ATOM   11664 C  CG1 . ILE   D  1 184 ? 32.973  40.289  -35.076  1.00 43.71  ? 485  ILE   D CG1 1 
ATOM   11665 C  CG2 . ILE   D  1 184 ? 34.192  41.744  -36.697  1.00 26.64  ? 485  ILE   D CG2 1 
ATOM   11666 C  CD1 . ILE   D  1 184 ? 34.135  39.381  -34.832  1.00 54.83  ? 485  ILE   D CD1 1 
ATOM   11667 N  N   . ARG   D  1 185 ? 31.470  43.702  -38.105  1.00 41.00  ? 486  ARG   D N   1 
ATOM   11668 C  CA  . ARG   D  1 185 ? 31.566  44.515  -39.318  1.00 42.62  ? 486  ARG   D CA  1 
ATOM   11669 C  C   . ARG   D  1 185 ? 32.216  45.852  -38.994  1.00 47.70  ? 486  ARG   D C   1 
ATOM   11670 O  O   . ARG   D  1 185 ? 32.261  46.285  -37.836  1.00 45.81  ? 486  ARG   D O   1 
ATOM   11671 C  CB  . ARG   D  1 185 ? 30.205  44.813  -39.966  1.00 41.48  ? 486  ARG   D CB  1 
ATOM   11672 C  CG  . ARG   D  1 185 ? 29.506  43.634  -40.540  1.00 50.20  ? 486  ARG   D CG  1 
ATOM   11673 C  CD  . ARG   D  1 185 ? 28.491  44.079  -41.550  1.00 58.00  ? 486  ARG   D CD  1 
ATOM   11674 N  NE  . ARG   D  1 185 ? 29.085  44.223  -42.868  1.00 63.82  ? 486  ARG   D NE  1 
ATOM   11675 C  CZ  . ARG   D  1 185 ? 28.379  44.317  -43.988  1.00 63.54  ? 486  ARG   D CZ  1 
ATOM   11676 N  NH1 . ARG   D  1 185 ? 27.055  44.280  -43.941  1.00 60.70  ? 486  ARG   D NH1 1 
ATOM   11677 N  NH2 . ARG   D  1 185 ? 28.996  44.452  -45.150  1.00 59.79  ? 486  ARG   D NH2 1 
ATOM   11678 N  N   . TYR   D  1 186 ? 32.676  46.533  -40.042  1.00 40.06  ? 487  TYR   D N   1 
ATOM   11679 C  CA  . TYR   D  1 186 ? 33.322  47.824  -39.882  1.00 34.58  ? 487  TYR   D CA  1 
ATOM   11680 C  C   . TYR   D  1 186 ? 32.366  48.978  -40.177  1.00 40.88  ? 487  TYR   D C   1 
ATOM   11681 O  O   . TYR   D  1 186 ? 31.425  48.859  -40.966  1.00 46.73  ? 487  TYR   D O   1 
ATOM   11682 C  CB  . TYR   D  1 186 ? 34.553  47.922  -40.767  1.00 39.20  ? 487  TYR   D CB  1 
ATOM   11683 C  CG  . TYR   D  1 186 ? 35.639  46.931  -40.434  1.00 40.80  ? 487  TYR   D CG  1 
ATOM   11684 C  CD1 . TYR   D  1 186 ? 36.216  46.906  -39.170  1.00 43.90  ? 487  TYR   D CD1 1 
ATOM   11685 C  CD2 . TYR   D  1 186 ? 36.108  46.033  -41.392  1.00 43.99  ? 487  TYR   D CD2 1 
ATOM   11686 C  CE1 . TYR   D  1 186 ? 37.224  46.013  -38.865  1.00 44.34  ? 487  TYR   D CE1 1 
ATOM   11687 C  CE2 . TYR   D  1 186 ? 37.117  45.138  -41.093  1.00 45.66  ? 487  TYR   D CE2 1 
ATOM   11688 C  CZ  . TYR   D  1 186 ? 37.674  45.132  -39.830  1.00 43.35  ? 487  TYR   D CZ  1 
ATOM   11689 O  OH  . TYR   D  1 186 ? 38.681  44.237  -39.532  1.00 44.74  ? 487  TYR   D OH  1 
ATOM   11690 N  N   . ALA   D  1 187 ? 32.626  50.104  -39.527  1.00 39.78  ? 488  ALA   D N   1 
ATOM   11691 C  CA  . ALA   D  1 187 ? 31.754  51.257  -39.634  1.00 45.09  ? 488  ALA   D CA  1 
ATOM   11692 C  C   . ALA   D  1 187 ? 31.944  51.941  -40.976  1.00 43.64  ? 488  ALA   D C   1 
ATOM   11693 O  O   . ALA   D  1 187 ? 32.976  51.806  -41.632  1.00 41.25  ? 488  ALA   D O   1 
ATOM   11694 C  CB  . ALA   D  1 187 ? 32.024  52.257  -38.508  1.00 40.17  ? 488  ALA   D CB  1 
ATOM   11695 N  N   . GLY   D  1 188 ? 30.916  52.682  -41.375  1.00 50.50  ? 489  GLY   D N   1 
ATOM   11696 C  CA  . GLY   D  1 188 ? 30.975  53.527  -42.543  1.00 52.51  ? 489  GLY   D CA  1 
ATOM   11697 C  C   . GLY   D  1 188 ? 30.579  54.943  -42.181  1.00 57.73  ? 489  GLY   D C   1 
ATOM   11698 O  O   . GLY   D  1 188 ? 29.563  55.166  -41.516  1.00 56.25  ? 489  GLY   D O   1 
ATOM   11699 N  N   . TYR   D  1 189 ? 31.383  55.913  -42.601  1.00 58.36  ? 490  TYR   D N   1 
ATOM   11700 C  CA  . TYR   D  1 189 ? 31.118  57.317  -42.325  1.00 49.33  ? 490  TYR   D CA  1 
ATOM   11701 C  C   . TYR   D  1 189 ? 31.146  58.070  -43.644  1.00 57.35  ? 490  TYR   D C   1 
ATOM   11702 O  O   . TYR   D  1 189 ? 32.213  58.221  -44.246  1.00 59.68  ? 490  TYR   D O   1 
ATOM   11703 C  CB  . TYR   D  1 189 ? 32.150  57.897  -41.370  1.00 43.32  ? 490  TYR   D CB  1 
ATOM   11704 C  CG  . TYR   D  1 189 ? 32.437  57.065  -40.143  1.00 51.50  ? 490  TYR   D CG  1 
ATOM   11705 C  CD1 . TYR   D  1 189 ? 31.668  57.208  -38.987  1.00 55.38  ? 490  TYR   D CD1 1 
ATOM   11706 C  CD2 . TYR   D  1 189 ? 33.502  56.165  -40.118  1.00 50.38  ? 490  TYR   D CD2 1 
ATOM   11707 C  CE1 . TYR   D  1 189 ? 31.937  56.463  -37.841  1.00 50.70  ? 490  TYR   D CE1 1 
ATOM   11708 C  CE2 . TYR   D  1 189 ? 33.778  55.416  -38.974  1.00 56.65  ? 490  TYR   D CE2 1 
ATOM   11709 C  CZ  . TYR   D  1 189 ? 32.991  55.575  -37.842  1.00 54.43  ? 490  TYR   D CZ  1 
ATOM   11710 O  OH  . TYR   D  1 189 ? 33.254  54.840  -36.718  1.00 57.17  ? 490  TYR   D OH  1 
ATOM   11711 N  N   . LYS   D  1 190 ? 29.997  58.566  -44.084  1.00 51.38  ? 491  LYS   D N   1 
ATOM   11712 C  CA  . LYS   D  1 190 ? 30.002  59.456  -45.236  1.00 59.39  ? 491  LYS   D CA  1 
ATOM   11713 C  C   . LYS   D  1 190 ? 30.496  60.838  -44.810  1.00 59.11  ? 491  LYS   D C   1 
ATOM   11714 O  O   . LYS   D  1 190 ? 30.107  61.349  -43.756  1.00 61.81  ? 491  LYS   D O   1 
ATOM   11715 C  CB  . LYS   D  1 190 ? 28.618  59.523  -45.884  1.00 68.24  ? 491  LYS   D CB  1 
ATOM   11716 C  CG  . LYS   D  1 190 ? 28.683  59.321  -47.407  1.00 83.03  ? 491  LYS   D CG  1 
ATOM   11717 C  CD  . LYS   D  1 190 ? 27.337  59.527  -48.098  1.00 90.93  ? 491  LYS   D CD  1 
ATOM   11718 C  CE  . LYS   D  1 190 ? 27.502  59.669  -49.607  1.00 90.00  ? 491  LYS   D CE  1 
ATOM   11719 N  NZ  . LYS   D  1 190 ? 26.351  60.378  -50.240  1.00 88.60  ? 491  LYS   D NZ  1 
ATOM   11720 N  N   . GLN   D  1 191 ? 31.395  61.433  -45.622  1.00 53.42  ? 492  GLN   D N   1 
ATOM   11721 C  CA  . GLN   D  1 191 ? 32.032  62.713  -45.349  1.00 51.38  ? 492  GLN   D CA  1 
ATOM   11722 C  C   . GLN   D  1 191 ? 31.248  63.859  -45.979  1.00 51.91  ? 492  GLN   D C   1 
ATOM   11723 O  O   . GLN   D  1 191 ? 30.421  63.650  -46.873  1.00 56.68  ? 492  GLN   D O   1 
ATOM   11724 C  CB  . GLN   D  1 191 ? 33.462  62.712  -45.886  1.00 64.36  ? 492  GLN   D CB  1 
ATOM   11725 C  CG  . GLN   D  1 191 ? 34.244  61.442  -45.601  1.00 69.71  ? 492  GLN   D CG  1 
ATOM   11726 C  CD  . GLN   D  1 191 ? 34.971  61.486  -44.285  1.00 70.86  ? 492  GLN   D CD  1 
ATOM   11727 O  OE1 . GLN   D  1 191 ? 34.380  61.775  -43.248  1.00 71.60  ? 492  GLN   D OE1 1 
ATOM   11728 N  NE2 . GLN   D  1 191 ? 36.269  61.205  -44.318  1.00 72.19  ? 492  GLN   D NE2 1 
ATOM   11729 N  N   . PRO   D  1 192 ? 31.477  65.096  -45.531  1.00 53.85  ? 493  PRO   D N   1 
ATOM   11730 C  CA  . PRO   D  1 192 ? 30.753  66.224  -46.140  1.00 55.31  ? 493  PRO   D CA  1 
ATOM   11731 C  C   . PRO   D  1 192 ? 31.052  66.389  -47.614  1.00 58.68  ? 493  PRO   D C   1 
ATOM   11732 O  O   . PRO   D  1 192 ? 30.226  66.945  -48.350  1.00 66.08  ? 493  PRO   D O   1 
ATOM   11733 C  CB  . PRO   D  1 192 ? 31.236  67.438  -45.330  1.00 54.10  ? 493  PRO   D CB  1 
ATOM   11734 C  CG  . PRO   D  1 192 ? 31.716  66.864  -44.035  1.00 52.27  ? 493  PRO   D CG  1 
ATOM   11735 C  CD  . PRO   D  1 192 ? 32.272  65.512  -44.359  1.00 54.79  ? 493  PRO   D CD  1 
ATOM   11736 N  N   . ASP   D  1 193 ? 32.213  65.926  -48.066  1.00 53.66  ? 494  ASP   D N   1 
ATOM   11737 C  CA  . ASP   D  1 193 ? 32.642  66.115  -49.446  1.00 58.86  ? 494  ASP   D CA  1 
ATOM   11738 C  C   . ASP   D  1 193 ? 32.134  65.021  -50.377  1.00 58.41  ? 494  ASP   D C   1 
ATOM   11739 O  O   . ASP   D  1 193 ? 32.502  65.005  -51.557  1.00 64.38  ? 494  ASP   D O   1 
ATOM   11740 C  CB  . ASP   D  1 193 ? 34.173  66.203  -49.516  1.00 60.16  ? 494  ASP   D CB  1 
ATOM   11741 C  CG  . ASP   D  1 193 ? 34.856  64.860  -49.310  1.00 64.23  ? 494  ASP   D CG  1 
ATOM   11742 O  OD1 . ASP   D  1 193 ? 34.280  63.970  -48.654  1.00 66.31  ? 494  ASP   D OD1 1 
ATOM   11743 O  OD2 . ASP   D  1 193 ? 35.989  64.700  -49.809  1.00 68.80  ? 494  ASP   D OD2 1 
ATOM   11744 N  N   . GLY   D  1 194 ? 31.295  64.115  -49.876  1.00 57.89  ? 495  GLY   D N   1 
ATOM   11745 C  CA  . GLY   D  1 194 ? 30.759  63.026  -50.640  1.00 55.57  ? 495  GLY   D CA  1 
ATOM   11746 C  C   . GLY   D  1 194 ? 31.519  61.726  -50.480  1.00 55.00  ? 495  GLY   D C   1 
ATOM   11747 O  O   . GLY   D  1 194 ? 30.942  60.653  -50.693  1.00 52.93  ? 495  GLY   D O   1 
ATOM   11748 N  N   . SER   D  1 195 ? 32.794  61.792  -50.106  1.00 53.59  ? 496  SER   D N   1 
ATOM   11749 C  CA  . SER   D  1 195 ? 33.566  60.572  -49.962  1.00 52.46  ? 496  SER   D CA  1 
ATOM   11750 C  C   . SER   D  1 195 ? 33.059  59.763  -48.768  1.00 56.99  ? 496  SER   D C   1 
ATOM   11751 O  O   . SER   D  1 195 ? 32.281  60.237  -47.930  1.00 53.85  ? 496  SER   D O   1 
ATOM   11752 C  CB  . SER   D  1 195 ? 35.053  60.889  -49.810  1.00 50.93  ? 496  SER   D CB  1 
ATOM   11753 O  OG  . SER   D  1 195 ? 35.345  61.379  -48.524  1.00 59.70  ? 496  SER   D OG  1 
ATOM   11754 N  N   . THR   D  1 196 ? 33.490  58.511  -48.708  1.00 57.94  ? 497  THR   D N   1 
ATOM   11755 C  CA  . THR   D  1 196 ? 33.065  57.609  -47.654  1.00 57.75  ? 497  THR   D CA  1 
ATOM   11756 C  C   . THR   D  1 196 ? 34.287  57.030  -46.953  1.00 60.08  ? 497  THR   D C   1 
ATOM   11757 O  O   . THR   D  1 196 ? 35.272  56.669  -47.598  1.00 59.83  ? 497  THR   D O   1 
ATOM   11758 C  CB  . THR   D  1 196 ? 32.181  56.495  -48.213  1.00 60.09  ? 497  THR   D CB  1 
ATOM   11759 O  OG1 . THR   D  1 196 ? 31.052  57.077  -48.879  1.00 63.55  ? 497  THR   D OG1 1 
ATOM   11760 C  CG2 . THR   D  1 196 ? 31.697  55.585  -47.087  1.00 59.83  ? 497  THR   D CG2 1 
ATOM   11761 N  N   . LEU   D  1 197 ? 34.229  56.980  -45.625  1.00 61.67  ? 498  LEU   D N   1 
ATOM   11762 C  CA  . LEU   D  1 197 ? 35.285  56.411  -44.803  1.00 54.40  ? 498  LEU   D CA  1 
ATOM   11763 C  C   . LEU   D  1 197 ? 34.782  55.102  -44.220  1.00 48.72  ? 498  LEU   D C   1 
ATOM   11764 O  O   . LEU   D  1 197 ? 33.628  55.011  -43.789  1.00 50.57  ? 498  LEU   D O   1 
ATOM   11765 C  CB  . LEU   D  1 197 ? 35.695  57.371  -43.693  1.00 57.76  ? 498  LEU   D CB  1 
ATOM   11766 C  CG  . LEU   D  1 197 ? 36.771  56.893  -42.722  1.00 60.18  ? 498  LEU   D CG  1 
ATOM   11767 C  CD1 . LEU   D  1 197 ? 38.002  56.417  -43.479  1.00 55.77  ? 498  LEU   D CD1 1 
ATOM   11768 C  CD2 . LEU   D  1 197 ? 37.126  58.009  -41.729  1.00 58.23  ? 498  LEU   D CD2 1 
ATOM   11769 N  N   . GLY   D  1 198 ? 35.633  54.078  -44.246  1.00 46.29  ? 499  GLY   D N   1 
ATOM   11770 C  CA  . GLY   D  1 198 ? 35.183  52.744  -43.864  1.00 44.93  ? 499  GLY   D CA  1 
ATOM   11771 C  C   . GLY   D  1 198 ? 34.342  52.047  -44.921  1.00 50.52  ? 499  GLY   D C   1 
ATOM   11772 O  O   . GLY   D  1 198 ? 34.526  52.225  -46.127  1.00 57.16  ? 499  GLY   D O   1 
ATOM   11773 N  N   . ASP   D  1 199 ? 33.388  51.254  -44.453  1.00 51.07  ? 500  ASP   D N   1 
ATOM   11774 C  CA  . ASP   D  1 199 ? 32.631  50.358  -45.309  1.00 47.29  ? 500  ASP   D CA  1 
ATOM   11775 C  C   . ASP   D  1 199 ? 31.342  51.045  -45.750  1.00 47.62  ? 500  ASP   D C   1 
ATOM   11776 O  O   . ASP   D  1 199 ? 30.440  51.242  -44.918  1.00 49.57  ? 500  ASP   D O   1 
ATOM   11777 C  CB  . ASP   D  1 199 ? 32.330  49.063  -44.552  1.00 44.85  ? 500  ASP   D CB  1 
ATOM   11778 C  CG  . ASP   D  1 199 ? 31.718  47.989  -45.423  1.00 49.30  ? 500  ASP   D CG  1 
ATOM   11779 O  OD1 . ASP   D  1 199 ? 30.904  48.309  -46.318  1.00 52.28  ? 500  ASP   D OD1 1 
ATOM   11780 O  OD2 . ASP   D  1 199 ? 32.055  46.810  -45.191  1.00 44.48  ? 500  ASP   D OD2 1 
ATOM   11781 N  N   . PRO   D  1 200 ? 31.198  51.418  -47.021  1.00 53.05  ? 501  PRO   D N   1 
ATOM   11782 C  CA  . PRO   D  1 200 ? 29.978  52.134  -47.439  1.00 48.59  ? 501  PRO   D CA  1 
ATOM   11783 C  C   . PRO   D  1 200 ? 28.696  51.339  -47.240  1.00 48.97  ? 501  PRO   D C   1 
ATOM   11784 O  O   . PRO   D  1 200 ? 27.627  51.948  -47.097  1.00 49.14  ? 501  PRO   D O   1 
ATOM   11785 C  CB  . PRO   D  1 200 ? 30.247  52.431  -48.921  1.00 42.92  ? 501  PRO   D CB  1 
ATOM   11786 C  CG  . PRO   D  1 200 ? 31.765  52.451  -49.003  1.00 35.95  ? 501  PRO   D CG  1 
ATOM   11787 C  CD  . PRO   D  1 200 ? 32.201  51.354  -48.100  1.00 41.36  ? 501  PRO   D CD  1 
ATOM   11788 N  N   . ALA   D  1 201 ? 28.775  50.006  -47.190  1.00 50.71  ? 502  ALA   D N   1 
ATOM   11789 C  CA  . ALA   D  1 201 ? 27.602  49.175  -46.929  1.00 51.80  ? 502  ALA   D CA  1 
ATOM   11790 C  C   . ALA   D  1 201 ? 26.996  49.422  -45.555  1.00 52.44  ? 502  ALA   D C   1 
ATOM   11791 O  O   . ALA   D  1 201 ? 25.795  49.204  -45.360  1.00 55.19  ? 502  ALA   D O   1 
ATOM   11792 C  CB  . ALA   D  1 201 ? 27.968  47.697  -47.039  1.00 45.74  ? 502  ALA   D CB  1 
ATOM   11793 N  N   . ASN   D  1 202 ? 27.789  49.868  -44.595  1.00 49.41  ? 503  ASN   D N   1 
ATOM   11794 C  CA  . ASN   D  1 202 ? 27.323  49.922  -43.220  1.00 47.07  ? 503  ASN   D CA  1 
ATOM   11795 C  C   . ASN   D  1 202 ? 27.035  51.347  -42.775  1.00 50.45  ? 503  ASN   D C   1 
ATOM   11796 O  O   . ASN   D  1 202 ? 26.905  51.602  -41.578  1.00 55.23  ? 503  ASN   D O   1 
ATOM   11797 C  CB  . ASN   D  1 202 ? 28.348  49.245  -42.313  1.00 38.32  ? 503  ASN   D CB  1 
ATOM   11798 C  CG  . ASN   D  1 202 ? 28.520  47.777  -42.641  1.00 39.76  ? 503  ASN   D CG  1 
ATOM   11799 O  OD1 . ASN   D  1 202 ? 27.555  47.118  -43.034  1.00 44.48  ? 503  ASN   D OD1 1 
ATOM   11800 N  ND2 . ASN   D  1 202 ? 29.742  47.244  -42.461  1.00 38.92  ? 503  ASN   D ND2 1 
ATOM   11801 N  N   . VAL   D  1 203 ? 26.912  52.280  -43.727  1.00 51.09  ? 504  VAL   D N   1 
ATOM   11802 C  CA  . VAL   D  1 203 ? 26.762  53.688  -43.376  1.00 43.61  ? 504  VAL   D CA  1 
ATOM   11803 C  C   . VAL   D  1 203 ? 25.457  53.921  -42.625  1.00 53.94  ? 504  VAL   D C   1 
ATOM   11804 O  O   . VAL   D  1 203 ? 25.425  54.650  -41.622  1.00 57.23  ? 504  VAL   D O   1 
ATOM   11805 C  CB  . VAL   D  1 203 ? 26.874  54.564  -44.636  1.00 43.57  ? 504  VAL   D CB  1 
ATOM   11806 C  CG1 . VAL   D  1 203 ? 26.210  55.915  -44.428  1.00 39.97  ? 504  VAL   D CG1 1 
ATOM   11807 C  CG2 . VAL   D  1 203 ? 28.329  54.747  -44.997  1.00 43.19  ? 504  VAL   D CG2 1 
ATOM   11808 N  N   . GLN   D  1 204 ? 24.368  53.285  -43.068  1.00 49.68  ? 505  GLN   D N   1 
ATOM   11809 C  CA  . GLN   D  1 204 ? 23.082  53.518  -42.417  1.00 55.66  ? 505  GLN   D CA  1 
ATOM   11810 C  C   . GLN   D  1 204 ? 23.088  52.980  -40.987  1.00 52.46  ? 505  GLN   D C   1 
ATOM   11811 O  O   . GLN   D  1 204 ? 22.656  53.667  -40.053  1.00 38.86  ? 505  GLN   D O   1 
ATOM   11812 C  CB  . GLN   D  1 204 ? 21.948  52.884  -43.224  1.00 62.11  ? 505  GLN   D CB  1 
ATOM   11813 C  CG  . GLN   D  1 204 ? 20.660  53.714  -43.200  1.00 75.22  ? 505  GLN   D CG  1 
ATOM   11814 C  CD  . GLN   D  1 204 ? 19.392  52.876  -43.040  1.00 77.43  ? 505  GLN   D CD  1 
ATOM   11815 O  OE1 . GLN   D  1 204 ? 19.271  51.786  -43.603  1.00 69.78  ? 505  GLN   D OE1 1 
ATOM   11816 N  NE2 . GLN   D  1 204 ? 18.438  53.394  -42.264  1.00 81.49  ? 505  GLN   D NE2 1 
ATOM   11817 N  N   . PHE   D  1 205 ? 23.578  51.750  -40.803  1.00 46.96  ? 506  PHE   D N   1 
ATOM   11818 C  CA  . PHE   D  1 205 ? 23.646  51.163  -39.473  1.00 46.13  ? 506  PHE   D CA  1 
ATOM   11819 C  C   . PHE   D  1 205 ? 24.592  51.950  -38.569  1.00 46.39  ? 506  PHE   D C   1 
ATOM   11820 O  O   . PHE   D  1 205 ? 24.315  52.131  -37.379  1.00 47.08  ? 506  PHE   D O   1 
ATOM   11821 C  CB  . PHE   D  1 205 ? 24.083  49.707  -39.574  1.00 42.28  ? 506  PHE   D CB  1 
ATOM   11822 C  CG  . PHE   D  1 205 ? 24.123  49.021  -38.266  1.00 44.35  ? 506  PHE   D CG  1 
ATOM   11823 C  CD1 . PHE   D  1 205 ? 22.949  48.584  -37.668  1.00 51.28  ? 506  PHE   D CD1 1 
ATOM   11824 C  CD2 . PHE   D  1 205 ? 25.324  48.847  -37.588  1.00 45.95  ? 506  PHE   D CD2 1 
ATOM   11825 C  CE1 . PHE   D  1 205 ? 22.976  47.959  -36.422  1.00 40.18  ? 506  PHE   D CE1 1 
ATOM   11826 C  CE2 . PHE   D  1 205 ? 25.353  48.219  -36.354  1.00 38.27  ? 506  PHE   D CE2 1 
ATOM   11827 C  CZ  . PHE   D  1 205 ? 24.176  47.776  -35.773  1.00 39.48  ? 506  PHE   D CZ  1 
ATOM   11828 N  N   . THR   D  1 206 ? 25.708  52.425  -39.123  1.00 44.83  ? 507  THR   D N   1 
ATOM   11829 C  CA  . THR   D  1 206 ? 26.612  53.298  -38.383  1.00 45.20  ? 507  THR   D CA  1 
ATOM   11830 C  C   . THR   D  1 206 ? 25.888  54.545  -37.870  1.00 58.33  ? 507  THR   D C   1 
ATOM   11831 O  O   . THR   D  1 206 ? 26.077  54.950  -36.716  1.00 61.59  ? 507  THR   D O   1 
ATOM   11832 C  CB  . THR   D  1 206 ? 27.806  53.667  -39.272  1.00 39.26  ? 507  THR   D CB  1 
ATOM   11833 O  OG1 . THR   D  1 206 ? 28.509  52.476  -39.657  1.00 34.88  ? 507  THR   D OG1 1 
ATOM   11834 C  CG2 . THR   D  1 206 ? 28.766  54.579  -38.553  1.00 35.86  ? 507  THR   D CG2 1 
ATOM   11835 N  N   . GLU   D  1 207 ? 25.042  55.157  -38.706  1.00 61.58  ? 508  GLU   D N   1 
ATOM   11836 C  CA  . GLU   D  1 207 ? 24.267  56.312  -38.257  1.00 60.69  ? 508  GLU   D CA  1 
ATOM   11837 C  C   . GLU   D  1 207 ? 23.323  55.940  -37.118  1.00 56.70  ? 508  GLU   D C   1 
ATOM   11838 O  O   . GLU   D  1 207 ? 23.132  56.723  -36.179  1.00 53.73  ? 508  GLU   D O   1 
ATOM   11839 C  CB  . GLU   D  1 207 ? 23.469  56.907  -39.423  1.00 66.99  ? 508  GLU   D CB  1 
ATOM   11840 C  CG  . GLU   D  1 207 ? 24.256  57.773  -40.376  1.00 70.07  ? 508  GLU   D CG  1 
ATOM   11841 C  CD  . GLU   D  1 207 ? 23.532  57.972  -41.703  1.00 85.32  ? 508  GLU   D CD  1 
ATOM   11842 O  OE1 . GLU   D  1 207 ? 22.404  57.449  -41.854  1.00 89.33  ? 508  GLU   D OE1 1 
ATOM   11843 O  OE2 . GLU   D  1 207 ? 24.094  58.645  -42.595  1.00 87.21  ? 508  GLU   D OE2 1 
ATOM   11844 N  N   . ILE   D  1 208 ? 22.701  54.761  -37.199  1.00 53.90  ? 509  ILE   D N   1 
ATOM   11845 C  CA  . ILE   D  1 208 ? 21.765  54.341  -36.162  1.00 46.94  ? 509  ILE   D CA  1 
ATOM   11846 C  C   . ILE   D  1 208 ? 22.489  54.199  -34.837  1.00 46.36  ? 509  ILE   D C   1 
ATOM   11847 O  O   . ILE   D  1 208 ? 22.023  54.694  -33.807  1.00 43.34  ? 509  ILE   D O   1 
ATOM   11848 C  CB  . ILE   D  1 208 ? 21.072  53.025  -36.552  1.00 48.95  ? 509  ILE   D CB  1 
ATOM   11849 C  CG1 . ILE   D  1 208 ? 20.270  53.193  -37.837  1.00 60.92  ? 509  ILE   D CG1 1 
ATOM   11850 C  CG2 . ILE   D  1 208 ? 20.157  52.584  -35.455  1.00 41.03  ? 509  ILE   D CG2 1 
ATOM   11851 C  CD1 . ILE   D  1 208 ? 19.592  51.914  -38.275  1.00 62.73  ? 509  ILE   D CD1 1 
ATOM   11852 N  N   . CYS   D  1 209 ? 23.650  53.528  -34.850  1.00 45.29  ? 510  CYS   D N   1 
ATOM   11853 C  CA  . CYS   D  1 209 ? 24.452  53.366  -33.635  1.00 49.30  ? 510  CYS   D CA  1 
ATOM   11854 C  C   . CYS   D  1 209 ? 24.836  54.711  -33.047  1.00 52.99  ? 510  CYS   D C   1 
ATOM   11855 O  O   . CYS   D  1 209 ? 24.654  54.952  -31.849  1.00 54.78  ? 510  CYS   D O   1 
ATOM   11856 C  CB  . CYS   D  1 209 ? 25.721  52.564  -33.922  1.00 52.61  ? 510  CYS   D CB  1 
ATOM   11857 S  SG  . CYS   D  1 209 ? 25.465  50.865  -34.403  1.00 49.21  ? 510  CYS   D SG  1 
ATOM   11858 N  N   . ILE   D  1 210 ? 25.397  55.594  -33.874  1.00 54.68  ? 511  ILE   D N   1 
ATOM   11859 C  CA  . ILE   D  1 210 ? 25.816  56.899  -33.377  1.00 53.98  ? 511  ILE   D CA  1 
ATOM   11860 C  C   . ILE   D  1 210 ? 24.647  57.609  -32.722  1.00 52.49  ? 511  ILE   D C   1 
ATOM   11861 O  O   . ILE   D  1 210 ? 24.769  58.162  -31.621  1.00 58.10  ? 511  ILE   D O   1 
ATOM   11862 C  CB  . ILE   D  1 210 ? 26.421  57.731  -34.518  1.00 50.87  ? 511  ILE   D CB  1 
ATOM   11863 C  CG1 . ILE   D  1 210 ? 27.706  57.068  -35.011  1.00 47.75  ? 511  ILE   D CG1 1 
ATOM   11864 C  CG2 . ILE   D  1 210 ? 26.689  59.136  -34.043  1.00 38.78  ? 511  ILE   D CG2 1 
ATOM   11865 C  CD1 . ILE   D  1 210 ? 28.437  57.872  -36.079  1.00 49.20  ? 511  ILE   D CD1 1 
ATOM   11866 N  N   . GLN   D  1 211 ? 23.481  57.555  -33.361  1.00 51.12  ? 512  GLN   D N   1 
ATOM   11867 C  CA  . GLN   D  1 211 ? 22.300  58.211  -32.814  1.00 58.79  ? 512  GLN   D CA  1 
ATOM   11868 C  C   . GLN   D  1 211 ? 21.914  57.621  -31.465  1.00 61.15  ? 512  GLN   D C   1 
ATOM   11869 O  O   . GLN   D  1 211 ? 21.455  58.342  -30.569  1.00 58.47  ? 512  GLN   D O   1 
ATOM   11870 C  CB  . GLN   D  1 211 ? 21.145  58.087  -33.800  1.00 66.49  ? 512  GLN   D CB  1 
ATOM   11871 C  CG  . GLN   D  1 211 ? 19.880  58.747  -33.336  1.00 78.33  ? 512  GLN   D CG  1 
ATOM   11872 C  CD  . GLN   D  1 211 ? 18.777  58.573  -34.337  1.00 93.42  ? 512  GLN   D CD  1 
ATOM   11873 O  OE1 . GLN   D  1 211 ? 18.967  57.953  -35.387  1.00 97.79  ? 512  GLN   D OE1 1 
ATOM   11874 N  NE2 . GLN   D  1 211 ? 17.610  59.114  -34.024  1.00 98.19  ? 512  GLN   D NE2 1 
ATOM   11875 N  N   . GLN   D  1 212 ? 22.087  56.313  -31.307  1.00 54.23  ? 513  GLN   D N   1 
ATOM   11876 C  CA  . GLN   D  1 212 ? 21.769  55.611  -30.075  1.00 57.61  ? 513  GLN   D CA  1 
ATOM   11877 C  C   . GLN   D  1 212 ? 22.816  55.802  -28.990  1.00 53.34  ? 513  GLN   D C   1 
ATOM   11878 O  O   . GLN   D  1 212 ? 22.686  55.185  -27.931  1.00 50.96  ? 513  GLN   D O   1 
ATOM   11879 C  CB  . GLN   D  1 212 ? 21.610  54.110  -30.347  1.00 58.18  ? 513  GLN   D CB  1 
ATOM   11880 C  CG  . GLN   D  1 212 ? 20.388  53.724  -31.142  1.00 57.55  ? 513  GLN   D CG  1 
ATOM   11881 C  CD  . GLN   D  1 212 ? 19.124  54.349  -30.605  1.00 71.47  ? 513  GLN   D CD  1 
ATOM   11882 O  OE1 . GLN   D  1 212 ? 18.305  54.860  -31.372  1.00 80.38  ? 513  GLN   D OE1 1 
ATOM   11883 N  NE2 . GLN   D  1 212 ? 18.949  54.311  -29.282  1.00 73.09  ? 513  GLN   D NE2 1 
ATOM   11884 N  N   . GLY   D  1 213 ? 23.862  56.591  -29.232  1.00 50.97  ? 514  GLY   D N   1 
ATOM   11885 C  CA  . GLY   D  1 213 ? 24.872  56.865  -28.222  1.00 47.80  ? 514  GLY   D CA  1 
ATOM   11886 C  C   . GLY   D  1 213 ? 26.283  56.435  -28.569  1.00 51.58  ? 514  GLY   D C   1 
ATOM   11887 O  O   . GLY   D  1 213 ? 27.224  56.845  -27.876  1.00 55.12  ? 514  GLY   D O   1 
ATOM   11888 N  N   . TRP   D  1 214 ? 26.493  55.642  -29.614  1.00 55.90  ? 515  TRP   D N   1 
ATOM   11889 C  CA  . TRP   D  1 214 ? 27.841  55.190  -29.931  1.00 55.90  ? 515  TRP   D CA  1 
ATOM   11890 C  C   . TRP   D  1 214 ? 28.751  56.363  -30.276  1.00 62.27  ? 515  TRP   D C   1 
ATOM   11891 O  O   . TRP   D  1 214 ? 28.398  57.235  -31.078  1.00 54.19  ? 515  TRP   D O   1 
ATOM   11892 C  CB  . TRP   D  1 214 ? 27.819  54.195  -31.088  1.00 56.01  ? 515  TRP   D CB  1 
ATOM   11893 C  CG  . TRP   D  1 214 ? 29.112  53.474  -31.238  1.00 53.78  ? 515  TRP   D CG  1 
ATOM   11894 C  CD1 . TRP   D  1 214 ? 29.765  52.760  -30.276  1.00 52.68  ? 515  TRP   D CD1 1 
ATOM   11895 C  CD2 . TRP   D  1 214 ? 29.921  53.394  -32.412  1.00 48.87  ? 515  TRP   D CD2 1 
ATOM   11896 N  NE1 . TRP   D  1 214 ? 30.927  52.237  -30.781  1.00 51.67  ? 515  TRP   D NE1 1 
ATOM   11897 C  CE2 . TRP   D  1 214 ? 31.047  52.612  -32.091  1.00 50.87  ? 515  TRP   D CE2 1 
ATOM   11898 C  CE3 . TRP   D  1 214 ? 29.802  53.900  -33.700  1.00 45.46  ? 515  TRP   D CE3 1 
ATOM   11899 C  CZ2 . TRP   D  1 214 ? 32.042  52.327  -33.013  1.00 52.41  ? 515  TRP   D CZ2 1 
ATOM   11900 C  CZ3 . TRP   D  1 214 ? 30.781  53.604  -34.608  1.00 54.84  ? 515  TRP   D CZ3 1 
ATOM   11901 C  CH2 . TRP   D  1 214 ? 31.893  52.831  -34.261  1.00 47.75  ? 515  TRP   D CH2 1 
ATOM   11902 N  N   . LYS   D  1 215 ? 29.929  56.374  -29.660  1.00 62.56  ? 516  LYS   D N   1 
ATOM   11903 C  CA  . LYS   D  1 215 ? 30.947  57.366  -29.943  1.00 58.56  ? 516  LYS   D CA  1 
ATOM   11904 C  C   . LYS   D  1 215 ? 31.966  56.735  -30.870  1.00 55.69  ? 516  LYS   D C   1 
ATOM   11905 O  O   . LYS   D  1 215 ? 32.746  55.885  -30.427  1.00 54.56  ? 516  LYS   D O   1 
ATOM   11906 C  CB  . LYS   D  1 215 ? 31.609  57.834  -28.652  1.00 69.35  ? 516  LYS   D CB  1 
ATOM   11907 C  CG  . LYS   D  1 215 ? 30.608  58.341  -27.622  1.00 76.91  ? 516  LYS   D CG  1 
ATOM   11908 C  CD  . LYS   D  1 215 ? 30.268  59.800  -27.851  1.00 81.81  ? 516  LYS   D CD  1 
ATOM   11909 C  CE  . LYS   D  1 215 ? 28.939  60.166  -27.225  1.00 83.52  ? 516  LYS   D CE  1 
ATOM   11910 N  NZ  . LYS   D  1 215 ? 27.818  59.855  -28.153  1.00 80.30  ? 516  LYS   D NZ  1 
ATOM   11911 N  N   . PRO   D  1 216 ? 32.002  57.108  -32.144  1.00 61.79  ? 517  PRO   D N   1 
ATOM   11912 C  CA  . PRO   D  1 216 ? 32.802  56.375  -33.119  1.00 51.00  ? 517  PRO   D CA  1 
ATOM   11913 C  C   . PRO   D  1 216 ? 34.227  56.896  -33.175  1.00 50.08  ? 517  PRO   D C   1 
ATOM   11914 O  O   . PRO   D  1 216 ? 34.461  58.103  -33.032  1.00 49.61  ? 517  PRO   D O   1 
ATOM   11915 C  CB  . PRO   D  1 216 ? 32.066  56.660  -34.428  1.00 51.28  ? 517  PRO   D CB  1 
ATOM   11916 C  CG  . PRO   D  1 216 ? 31.556  58.045  -34.241  1.00 58.81  ? 517  PRO   D CG  1 
ATOM   11917 C  CD  . PRO   D  1 216 ? 31.213  58.182  -32.774  1.00 60.55  ? 517  PRO   D CD  1 
ATOM   11918 N  N   . PRO   D  1 217 ? 35.212  56.022  -33.404  1.00 50.51  ? 518  PRO   D N   1 
ATOM   11919 C  CA  . PRO   D  1 217 ? 36.577  56.512  -33.662  1.00 52.65  ? 518  PRO   D CA  1 
ATOM   11920 C  C   . PRO   D  1 217 ? 36.717  57.276  -34.974  1.00 55.81  ? 518  PRO   D C   1 
ATOM   11921 O  O   . PRO   D  1 217 ? 37.703  58.006  -35.140  1.00 61.78  ? 518  PRO   D O   1 
ATOM   11922 C  CB  . PRO   D  1 217 ? 37.415  55.226  -33.679  1.00 49.33  ? 518  PRO   D CB  1 
ATOM   11923 C  CG  . PRO   D  1 217 ? 36.595  54.226  -32.965  1.00 41.44  ? 518  PRO   D CG  1 
ATOM   11924 C  CD  . PRO   D  1 217 ? 35.172  54.559  -33.267  1.00 38.37  ? 518  PRO   D CD  1 
ATOM   11925 N  N   . ARG   D  1 218 ? 35.757  57.156  -35.892  1.00 62.46  ? 519  ARG   D N   1 
ATOM   11926 C  CA  . ARG   D  1 218 ? 35.863  57.679  -37.257  1.00 62.33  ? 519  ARG   D CA  1 
ATOM   11927 C  C   . ARG   D  1 218 ? 37.208  57.288  -37.877  1.00 67.46  ? 519  ARG   D C   1 
ATOM   11928 O  O   . ARG   D  1 218 ? 38.092  58.112  -38.106  1.00 77.71  ? 519  ARG   D O   1 
ATOM   11929 C  CB  . ARG   D  1 218 ? 35.649  59.196  -37.291  1.00 62.34  ? 519  ARG   D CB  1 
ATOM   11930 C  CG  . ARG   D  1 218 ? 34.405  59.667  -36.550  1.00 66.34  ? 519  ARG   D CG  1 
ATOM   11931 C  CD  . ARG   D  1 218 ? 33.889  61.005  -37.073  1.00 67.75  ? 519  ARG   D CD  1 
ATOM   11932 N  NE  . ARG   D  1 218 ? 32.972  60.808  -38.196  1.00 75.83  ? 519  ARG   D NE  1 
ATOM   11933 C  CZ  . ARG   D  1 218 ? 31.649  60.755  -38.072  1.00 75.70  ? 519  ARG   D CZ  1 
ATOM   11934 N  NH1 . ARG   D  1 218 ? 30.878  60.567  -39.136  1.00 74.11  ? 519  ARG   D NH1 1 
ATOM   11935 N  NH2 . ARG   D  1 218 ? 31.095  60.905  -36.876  1.00 73.94  ? 519  ARG   D NH2 1 
ATOM   11936 N  N   . GLY   D  1 219 ? 37.350  55.975  -38.086  1.00 62.17  ? 520  GLY   D N   1 
ATOM   11937 C  CA  . GLY   D  1 219 ? 38.487  55.417  -38.788  1.00 57.22  ? 520  GLY   D CA  1 
ATOM   11938 C  C   . GLY   D  1 219 ? 38.010  54.483  -39.886  1.00 57.74  ? 520  GLY   D C   1 
ATOM   11939 O  O   . GLY   D  1 219 ? 36.810  54.337  -40.120  1.00 56.38  ? 520  GLY   D O   1 
ATOM   11940 N  N   . ARG   D  1 220 ? 38.978  53.838  -40.544  1.00 58.25  ? 521  ARG   D N   1 
ATOM   11941 C  CA  . ARG   D  1 220 ? 38.643  52.985  -41.682  1.00 51.35  ? 521  ARG   D CA  1 
ATOM   11942 C  C   . ARG   D  1 220 ? 38.116  51.610  -41.270  1.00 52.53  ? 521  ARG   D C   1 
ATOM   11943 O  O   . ARG   D  1 220 ? 37.348  51.000  -42.025  1.00 56.05  ? 521  ARG   D O   1 
ATOM   11944 C  CB  . ARG   D  1 220 ? 39.853  52.803  -42.598  1.00 55.10  ? 521  ARG   D CB  1 
ATOM   11945 C  CG  . ARG   D  1 220 ? 39.524  52.053  -43.883  1.00 58.66  ? 521  ARG   D CG  1 
ATOM   11946 C  CD  . ARG   D  1 220 ? 39.851  52.885  -45.108  1.00 71.53  ? 521  ARG   D CD  1 
ATOM   11947 N  NE  . ARG   D  1 220 ? 41.104  52.465  -45.728  1.00 79.70  ? 521  ARG   D NE  1 
ATOM   11948 C  CZ  . ARG   D  1 220 ? 41.196  51.868  -46.914  1.00 87.50  ? 521  ARG   D CZ  1 
ATOM   11949 N  NH1 . ARG   D  1 220 ? 40.107  51.628  -47.632  1.00 89.83  ? 521  ARG   D NH1 1 
ATOM   11950 N  NH2 . ARG   D  1 220 ? 42.384  51.518  -47.391  1.00 91.60  ? 521  ARG   D NH2 1 
ATOM   11951 N  N   . PHE   D  1 221 ? 38.518  51.098  -40.107  1.00 43.47  ? 522  PHE   D N   1 
ATOM   11952 C  CA  . PHE   D  1 221 ? 38.196  49.731  -39.707  1.00 43.35  ? 522  PHE   D CA  1 
ATOM   11953 C  C   . PHE   D  1 221 ? 37.797  49.694  -38.225  1.00 49.15  ? 522  PHE   D C   1 
ATOM   11954 O  O   . PHE   D  1 221 ? 38.320  48.913  -37.429  1.00 50.48  ? 522  PHE   D O   1 
ATOM   11955 C  CB  . PHE   D  1 221 ? 39.363  48.781  -39.997  1.00 44.01  ? 522  PHE   D CB  1 
ATOM   11956 C  CG  . PHE   D  1 221 ? 39.770  48.718  -41.459  1.00 50.25  ? 522  PHE   D CG  1 
ATOM   11957 C  CD1 . PHE   D  1 221 ? 38.928  48.163  -42.413  1.00 56.01  ? 522  PHE   D CD1 1 
ATOM   11958 C  CD2 . PHE   D  1 221 ? 41.003  49.202  -41.872  1.00 53.51  ? 522  PHE   D CD2 1 
ATOM   11959 C  CE1 . PHE   D  1 221 ? 39.302  48.102  -43.761  1.00 54.54  ? 522  PHE   D CE1 1 
ATOM   11960 C  CE2 . PHE   D  1 221 ? 41.389  49.142  -43.218  1.00 58.15  ? 522  PHE   D CE2 1 
ATOM   11961 C  CZ  . PHE   D  1 221 ? 40.532  48.592  -44.162  1.00 56.42  ? 522  PHE   D CZ  1 
ATOM   11962 N  N   . ASP   D  1 222 ? 36.851  50.552  -37.843  1.00 42.81  ? 523  ASP   D N   1 
ATOM   11963 C  CA  . ASP   D  1 222 ? 36.245  50.492  -36.522  1.00 46.31  ? 523  ASP   D CA  1 
ATOM   11964 C  C   . ASP   D  1 222 ? 35.270  49.326  -36.471  1.00 48.11  ? 523  ASP   D C   1 
ATOM   11965 O  O   . ASP   D  1 222 ? 34.288  49.307  -37.220  1.00 51.23  ? 523  ASP   D O   1 
ATOM   11966 C  CB  . ASP   D  1 222 ? 35.511  51.793  -36.200  1.00 44.78  ? 523  ASP   D CB  1 
ATOM   11967 C  CG  . ASP   D  1 222 ? 36.344  53.019  -36.484  1.00 51.70  ? 523  ASP   D CG  1 
ATOM   11968 O  OD1 . ASP   D  1 222 ? 37.576  52.889  -36.651  1.00 57.86  ? 523  ASP   D OD1 1 
ATOM   11969 O  OD2 . ASP   D  1 222 ? 35.756  54.115  -36.542  1.00 57.23  ? 523  ASP   D OD2 1 
ATOM   11970 N  N   . VAL   D  1 223 ? 35.533  48.352  -35.599  1.00 42.63  ? 524  VAL   D N   1 
ATOM   11971 C  CA  . VAL   D  1 223 ? 34.532  47.321  -35.352  1.00 39.89  ? 524  VAL   D CA  1 
ATOM   11972 C  C   . VAL   D  1 223 ? 33.295  47.974  -34.748  1.00 42.78  ? 524  VAL   D C   1 
ATOM   11973 O  O   . VAL   D  1 223 ? 33.386  48.715  -33.761  1.00 43.00  ? 524  VAL   D O   1 
ATOM   11974 C  CB  . VAL   D  1 223 ? 35.103  46.224  -34.443  1.00 33.90  ? 524  VAL   D CB  1 
ATOM   11975 C  CG1 . VAL   D  1 223 ? 34.004  45.302  -33.991  1.00 31.41  ? 524  VAL   D CG1 1 
ATOM   11976 C  CG2 . VAL   D  1 223 ? 36.226  45.461  -35.164  1.00 32.80  ? 524  VAL   D CG2 1 
ATOM   11977 N  N   . LEU   D  1 224 ? 32.138  47.749  -35.371  1.00 33.52  ? 525  LEU   D N   1 
ATOM   11978 C  CA  . LEU   D  1 224 ? 30.920  48.392  -34.911  1.00 36.76  ? 525  LEU   D CA  1 
ATOM   11979 C  C   . LEU   D  1 224 ? 30.481  47.795  -33.579  1.00 37.37  ? 525  LEU   D C   1 
ATOM   11980 O  O   . LEU   D  1 224 ? 30.897  46.694  -33.224  1.00 34.87  ? 525  LEU   D O   1 
ATOM   11981 C  CB  . LEU   D  1 224 ? 29.799  48.216  -35.926  1.00 35.30  ? 525  LEU   D CB  1 
ATOM   11982 C  CG  . LEU   D  1 224 ? 29.718  49.130  -37.150  1.00 38.28  ? 525  LEU   D CG  1 
ATOM   11983 C  CD1 . LEU   D  1 224 ? 29.016  48.332  -38.213  1.00 35.03  ? 525  LEU   D CD1 1 
ATOM   11984 C  CD2 . LEU   D  1 224 ? 28.967  50.432  -36.845  1.00 30.45  ? 525  LEU   D CD2 1 
ATOM   11985 N  N   . PRO   D  1 225 ? 29.630  48.492  -32.834  1.00 37.84  ? 526  PRO   D N   1 
ATOM   11986 C  CA  . PRO   D  1 225 ? 29.072  47.902  -31.615  1.00 43.39  ? 526  PRO   D CA  1 
ATOM   11987 C  C   . PRO   D  1 225 ? 27.907  46.995  -31.950  1.00 41.74  ? 526  PRO   D C   1 
ATOM   11988 O  O   . PRO   D  1 225 ? 27.309  47.073  -33.024  1.00 41.69  ? 526  PRO   D O   1 
ATOM   11989 C  CB  . PRO   D  1 225 ? 28.600  49.120  -30.811  1.00 44.50  ? 526  PRO   D CB  1 
ATOM   11990 C  CG  . PRO   D  1 225 ? 28.246  50.127  -31.867  1.00 42.95  ? 526  PRO   D CG  1 
ATOM   11991 C  CD  . PRO   D  1 225 ? 29.243  49.910  -32.979  1.00 39.63  ? 526  PRO   D CD  1 
ATOM   11992 N  N   . LEU   D  1 226 ? 27.584  46.127  -31.005  1.00 28.26  ? 527  LEU   D N   1 
ATOM   11993 C  CA  . LEU   D  1 226 ? 26.378  45.336  -31.137  1.00 35.78  ? 527  LEU   D CA  1 
ATOM   11994 C  C   . LEU   D  1 226 ? 25.169  46.172  -30.742  1.00 45.53  ? 527  LEU   D C   1 
ATOM   11995 O  O   . LEU   D  1 226 ? 25.225  46.973  -29.802  1.00 52.27  ? 527  LEU   D O   1 
ATOM   11996 C  CB  . LEU   D  1 226 ? 26.465  44.078  -30.286  1.00 35.59  ? 527  LEU   D CB  1 
ATOM   11997 C  CG  . LEU   D  1 226 ? 27.456  43.058  -30.837  1.00 43.76  ? 527  LEU   D CG  1 
ATOM   11998 C  CD1 . LEU   D  1 226 ? 27.582  41.871  -29.899  1.00 42.87  ? 527  LEU   D CD1 1 
ATOM   11999 C  CD2 . LEU   D  1 226 ? 27.007  42.611  -32.218  1.00 33.42  ? 527  LEU   D CD2 1 
ATOM   12000 N  N   . LEU   D  1 227 ? 24.080  45.988  -31.482  1.00 42.34  ? 528  LEU   D N   1 
ATOM   12001 C  CA  . LEU   D  1 227 ? 22.806  46.653  -31.237  1.00 38.22  ? 528  LEU   D CA  1 
ATOM   12002 C  C   . LEU   D  1 227 ? 21.775  45.550  -31.075  1.00 42.43  ? 528  LEU   D C   1 
ATOM   12003 O  O   . LEU   D  1 227 ? 21.334  44.961  -32.074  1.00 38.78  ? 528  LEU   D O   1 
ATOM   12004 C  CB  . LEU   D  1 227 ? 22.434  47.576  -32.385  1.00 33.66  ? 528  LEU   D CB  1 
ATOM   12005 C  CG  . LEU   D  1 227 ? 21.885  48.972  -32.099  1.00 42.81  ? 528  LEU   D CG  1 
ATOM   12006 C  CD1 . LEU   D  1 227 ? 20.827  49.275  -33.138  1.00 28.70  ? 528  LEU   D CD1 1 
ATOM   12007 C  CD2 . LEU   D  1 227 ? 21.381  49.180  -30.618  1.00 28.89  ? 528  LEU   D CD2 1 
ATOM   12008 N  N   . LEU   D  1 228 ? 21.369  45.286  -29.834  1.00 30.61  ? 529  LEU   D N   1 
ATOM   12009 C  CA  . LEU   D  1 228 ? 20.658  44.053  -29.518  1.00 37.28  ? 529  LEU   D CA  1 
ATOM   12010 C  C   . LEU   D  1 228 ? 19.276  44.340  -28.953  1.00 39.38  ? 529  LEU   D C   1 
ATOM   12011 O  O   . LEU   D  1 228 ? 19.117  45.174  -28.052  1.00 38.54  ? 529  LEU   D O   1 
ATOM   12012 C  CB  . LEU   D  1 228 ? 21.453  43.192  -28.541  1.00 44.09  ? 529  LEU   D CB  1 
ATOM   12013 C  CG  . LEU   D  1 228 ? 22.869  42.869  -28.995  1.00 41.57  ? 529  LEU   D CG  1 
ATOM   12014 C  CD1 . LEU   D  1 228 ? 23.585  42.010  -27.949  1.00 38.32  ? 529  LEU   D CD1 1 
ATOM   12015 C  CD2 . LEU   D  1 228 ? 22.822  42.181  -30.340  1.00 37.99  ? 529  LEU   D CD2 1 
ATOM   12016 N  N   . GLN   D  1 229 ? 18.286  43.611  -29.463  1.00 37.84  ? 530  GLN   D N   1 
ATOM   12017 C  CA  . GLN   D  1 229 ? 16.892  43.787  -29.083  1.00 41.78  ? 530  GLN   D CA  1 
ATOM   12018 C  C   . GLN   D  1 229 ? 16.367  42.491  -28.483  1.00 39.41  ? 530  GLN   D C   1 
ATOM   12019 O  O   . GLN   D  1 229 ? 16.420  41.435  -29.128  1.00 38.87  ? 530  GLN   D O   1 
ATOM   12020 C  CB  . GLN   D  1 229 ? 16.066  44.210  -30.297  1.00 46.15  ? 530  GLN   D CB  1 
ATOM   12021 C  CG  . GLN   D  1 229 ? 14.593  43.931  -30.207  1.00 44.29  ? 530  GLN   D CG  1 
ATOM   12022 C  CD  . GLN   D  1 229 ? 13.833  44.563  -31.357  1.00 49.05  ? 530  GLN   D CD  1 
ATOM   12023 O  OE1 . GLN   D  1 229 ? 14.217  44.441  -32.520  1.00 54.78  ? 530  GLN   D OE1 1 
ATOM   12024 N  NE2 . GLN   D  1 229 ? 12.755  45.262  -31.032  1.00 51.92  ? 530  GLN   D NE2 1 
ATOM   12025 N  N   . ALA   D  1 230 ? 15.859  42.583  -27.255  1.00 36.79  ? 531  ALA   D N   1 
ATOM   12026 C  CA  . ALA   D  1 230 ? 15.236  41.475  -26.544  1.00 39.54  ? 531  ALA   D CA  1 
ATOM   12027 C  C   . ALA   D  1 230 ? 13.772  41.790  -26.273  1.00 44.05  ? 531  ALA   D C   1 
ATOM   12028 O  O   . ALA   D  1 230 ? 13.440  42.896  -25.829  1.00 52.69  ? 531  ALA   D O   1 
ATOM   12029 C  CB  . ALA   D  1 230 ? 15.956  41.199  -25.220  1.00 42.09  ? 531  ALA   D CB  1 
ATOM   12030 N  N   . ASN   D  1 231 ? 12.903  40.820  -26.552  1.00 41.87  ? 532  ASN   D N   1 
ATOM   12031 C  CA  . ASN   D  1 231 ? 11.491  40.869  -26.170  1.00 43.92  ? 532  ASN   D CA  1 
ATOM   12032 C  C   . ASN   D  1 231 ? 10.763  42.097  -26.718  1.00 43.84  ? 532  ASN   D C   1 
ATOM   12033 O  O   . ASN   D  1 231 ? 9.817   42.594  -26.105  1.00 43.80  ? 532  ASN   D O   1 
ATOM   12034 C  CB  . ASN   D  1 231 ? 11.337  40.803  -24.648  1.00 49.34  ? 532  ASN   D CB  1 
ATOM   12035 C  CG  . ASN   D  1 231 ? 10.103  40.052  -24.230  1.00 54.10  ? 532  ASN   D CG  1 
ATOM   12036 O  OD1 . ASN   D  1 231 ? 9.756   39.035  -24.827  1.00 58.05  ? 532  ASN   D OD1 1 
ATOM   12037 N  ND2 . ASN   D  1 231 ? 9.417   40.556  -23.203  1.00 65.93  ? 532  ASN   D ND2 1 
ATOM   12038 N  N   . GLY   D  1 232 ? 11.162  42.587  -27.891  1.00 47.25  ? 533  GLY   D N   1 
ATOM   12039 C  CA  . GLY   D  1 232 ? 10.482  43.723  -28.482  1.00 36.19  ? 533  GLY   D CA  1 
ATOM   12040 C  C   . GLY   D  1 232 ? 10.797  45.057  -27.850  1.00 41.89  ? 533  GLY   D C   1 
ATOM   12041 O  O   . GLY   D  1 232 ? 10.126  46.048  -28.158  1.00 46.75  ? 533  GLY   D O   1 
ATOM   12042 N  N   . ASN   D  1 233 ? 11.767  45.116  -26.947  1.00 49.94  ? 534  ASN   D N   1 
ATOM   12043 C  CA  . ASN   D  1 233 ? 12.137  46.401  -26.387  1.00 49.84  ? 534  ASN   D CA  1 
ATOM   12044 C  C   . ASN   D  1 233 ? 13.088  47.125  -27.339  1.00 46.23  ? 534  ASN   D C   1 
ATOM   12045 O  O   . ASN   D  1 233 ? 13.561  46.564  -28.329  1.00 45.65  ? 534  ASN   D O   1 
ATOM   12046 C  CB  . ASN   D  1 233 ? 12.746  46.210  -25.000  1.00 45.13  ? 534  ASN   D CB  1 
ATOM   12047 C  CG  . ASN   D  1 233 ? 11.732  45.661  -24.004  1.00 49.96  ? 534  ASN   D CG  1 
ATOM   12048 O  OD1 . ASN   D  1 233 ? 10.586  46.095  -23.981  1.00 51.93  ? 534  ASN   D OD1 1 
ATOM   12049 N  ND2 . ASN   D  1 233 ? 12.139  44.683  -23.211  1.00 47.06  ? 534  ASN   D ND2 1 
ATOM   12050 N  N   . ASP   D  1 234 ? 13.340  48.395  -27.048  1.00 47.26  ? 535  ASP   D N   1 
ATOM   12051 C  CA  . ASP   D  1 234 ? 14.295  49.138  -27.848  1.00 48.57  ? 535  ASP   D CA  1 
ATOM   12052 C  C   . ASP   D  1 234 ? 15.647  48.442  -27.763  1.00 48.54  ? 535  ASP   D C   1 
ATOM   12053 O  O   . ASP   D  1 234 ? 15.985  47.867  -26.722  1.00 47.14  ? 535  ASP   D O   1 
ATOM   12054 C  CB  . ASP   D  1 234 ? 14.424  50.585  -27.368  1.00 48.70  ? 535  ASP   D CB  1 
ATOM   12055 C  CG  . ASP   D  1 234 ? 13.127  51.374  -27.491  1.00 49.20  ? 535  ASP   D CG  1 
ATOM   12056 O  OD1 . ASP   D  1 234 ? 12.204  50.941  -28.215  1.00 46.30  ? 535  ASP   D OD1 1 
ATOM   12057 O  OD2 . ASP   D  1 234 ? 13.037  52.448  -26.864  1.00 52.84  ? 535  ASP   D OD2 1 
ATOM   12058 N  N   . PRO   D  1 235 ? 16.422  48.434  -28.837  1.00 46.70  ? 536  PRO   D N   1 
ATOM   12059 C  CA  . PRO   D  1 235 ? 17.718  47.757  -28.797  1.00 41.53  ? 536  PRO   D CA  1 
ATOM   12060 C  C   . PRO   D  1 235 ? 18.700  48.538  -27.939  1.00 39.98  ? 536  PRO   D C   1 
ATOM   12061 O  O   . PRO   D  1 235 ? 18.506  49.719  -27.651  1.00 39.86  ? 536  PRO   D O   1 
ATOM   12062 C  CB  . PRO   D  1 235 ? 18.146  47.734  -30.268  1.00 45.30  ? 536  PRO   D CB  1 
ATOM   12063 C  CG  . PRO   D  1 235 ? 17.489  48.931  -30.845  1.00 43.93  ? 536  PRO   D CG  1 
ATOM   12064 C  CD  . PRO   D  1 235 ? 16.166  49.068  -30.139  1.00 47.15  ? 536  PRO   D CD  1 
ATOM   12065 N  N   . GLU   D  1 236 ? 19.777  47.869  -27.536  1.00 43.03  ? 537  GLU   D N   1 
ATOM   12066 C  CA  . GLU   D  1 236 ? 20.770  48.486  -26.664  1.00 43.73  ? 537  GLU   D CA  1 
ATOM   12067 C  C   . GLU   D  1 236 ? 22.174  48.260  -27.223  1.00 46.29  ? 537  GLU   D C   1 
ATOM   12068 O  O   . GLU   D  1 236 ? 22.442  47.250  -27.878  1.00 48.15  ? 537  GLU   D O   1 
ATOM   12069 C  CB  . GLU   D  1 236 ? 20.635  47.928  -25.227  1.00 43.21  ? 537  GLU   D CB  1 
ATOM   12070 C  CG  . GLU   D  1 236 ? 19.200  48.032  -24.661  1.00 46.97  ? 537  GLU   D CG  1 
ATOM   12071 C  CD  . GLU   D  1 236 ? 18.988  47.247  -23.360  1.00 50.70  ? 537  GLU   D CD  1 
ATOM   12072 O  OE1 . GLU   D  1 236 ? 19.919  47.208  -22.540  1.00 49.77  ? 537  GLU   D OE1 1 
ATOM   12073 O  OE2 . GLU   D  1 236 ? 17.898  46.659  -23.165  1.00 50.82  ? 537  GLU   D OE2 1 
ATOM   12074 N  N   . LEU   D  1 237 ? 23.075  49.206  -26.968  1.00 39.82  ? 538  LEU   D N   1 
ATOM   12075 C  CA  . LEU   D  1 237 ? 24.428  49.093  -27.492  1.00 39.23  ? 538  LEU   D CA  1 
ATOM   12076 C  C   . LEU   D  1 237 ? 25.334  48.325  -26.534  1.00 49.36  ? 538  LEU   D C   1 
ATOM   12077 O  O   . LEU   D  1 237 ? 25.149  48.353  -25.316  1.00 49.62  ? 538  LEU   D O   1 
ATOM   12078 C  CB  . LEU   D  1 237 ? 25.016  50.475  -27.781  1.00 36.96  ? 538  LEU   D CB  1 
ATOM   12079 C  CG  . LEU   D  1 237 ? 24.337  51.248  -28.908  1.00 42.55  ? 538  LEU   D CG  1 
ATOM   12080 C  CD1 . LEU   D  1 237 ? 24.790  52.671  -28.873  1.00 44.18  ? 538  LEU   D CD1 1 
ATOM   12081 C  CD2 . LEU   D  1 237 ? 24.659  50.628  -30.258  1.00 44.15  ? 538  LEU   D CD2 1 
ATOM   12082 N  N   . PHE   D  1 238 ? 26.310  47.617  -27.108  1.00 53.86  ? 539  PHE   D N   1 
ATOM   12083 C  CA  . PHE   D  1 238 ? 27.350  46.918  -26.362  1.00 47.76  ? 539  PHE   D CA  1 
ATOM   12084 C  C   . PHE   D  1 238 ? 28.609  46.852  -27.213  1.00 47.08  ? 539  PHE   D C   1 
ATOM   12085 O  O   . PHE   D  1 238 ? 28.533  46.534  -28.403  1.00 47.28  ? 539  PHE   D O   1 
ATOM   12086 C  CB  . PHE   D  1 238 ? 26.945  45.489  -26.003  1.00 46.02  ? 539  PHE   D CB  1 
ATOM   12087 C  CG  . PHE   D  1 238 ? 25.651  45.386  -25.282  1.00 44.31  ? 539  PHE   D CG  1 
ATOM   12088 C  CD1 . PHE   D  1 238 ? 25.598  45.509  -23.904  1.00 48.33  ? 539  PHE   D CD1 1 
ATOM   12089 C  CD2 . PHE   D  1 238 ? 24.487  45.145  -25.977  1.00 47.39  ? 539  PHE   D CD2 1 
ATOM   12090 C  CE1 . PHE   D  1 238 ? 24.392  45.411  -23.236  1.00 46.21  ? 539  PHE   D CE1 1 
ATOM   12091 C  CE2 . PHE   D  1 238 ? 23.281  45.050  -25.325  1.00 49.12  ? 539  PHE   D CE2 1 
ATOM   12092 C  CZ  . PHE   D  1 238 ? 23.231  45.175  -23.956  1.00 47.89  ? 539  PHE   D CZ  1 
ATOM   12093 N  N   . GLN   D  1 239 ? 29.760  47.119  -26.602  1.00 43.10  ? 540  GLN   D N   1 
ATOM   12094 C  CA  . GLN   D  1 239 ? 31.045  46.993  -27.286  1.00 49.99  ? 540  GLN   D CA  1 
ATOM   12095 C  C   . GLN   D  1 239 ? 31.584  45.581  -27.093  1.00 49.27  ? 540  GLN   D C   1 
ATOM   12096 O  O   . GLN   D  1 239 ? 31.860  45.172  -25.960  1.00 39.40  ? 540  GLN   D O   1 
ATOM   12097 C  CB  . GLN   D  1 239 ? 32.055  48.011  -26.755  1.00 56.94  ? 540  GLN   D CB  1 
ATOM   12098 C  CG  . GLN   D  1 239 ? 33.473  47.868  -27.345  1.00 66.47  ? 540  GLN   D CG  1 
ATOM   12099 C  CD  . GLN   D  1 239 ? 34.583  48.050  -26.299  1.00 76.66  ? 540  GLN   D CD  1 
ATOM   12100 O  OE1 . GLN   D  1 239 ? 34.664  47.301  -25.317  1.00 83.73  ? 540  GLN   D OE1 1 
ATOM   12101 N  NE2 . GLN   D  1 239 ? 35.436  49.045  -26.509  1.00 73.55  ? 540  GLN   D NE2 1 
ATOM   12102 N  N   . ILE   D  1 240 ? 31.711  44.835  -28.189  1.00 40.14  ? 541  ILE   D N   1 
ATOM   12103 C  CA  . ILE   D  1 240 ? 32.399  43.535  -28.127  1.00 42.36  ? 541  ILE   D CA  1 
ATOM   12104 C  C   . ILE   D  1 240 ? 33.799  43.752  -27.572  1.00 45.96  ? 541  ILE   D C   1 
ATOM   12105 O  O   . ILE   D  1 240 ? 34.488  44.699  -27.999  1.00 46.38  ? 541  ILE   D O   1 
ATOM   12106 C  CB  . ILE   D  1 240 ? 32.470  42.867  -29.516  1.00 39.17  ? 541  ILE   D CB  1 
ATOM   12107 C  CG1 . ILE   D  1 240 ? 31.091  42.744  -30.154  1.00 41.21  ? 541  ILE   D CG1 1 
ATOM   12108 C  CG2 . ILE   D  1 240 ? 33.093  41.483  -29.409  1.00 31.52  ? 541  ILE   D CG2 1 
ATOM   12109 C  CD1 . ILE   D  1 240 ? 31.077  41.880  -31.414  1.00 38.56  ? 541  ILE   D CD1 1 
ATOM   12110 N  N   . PRO   D  1 241 ? 34.266  42.944  -26.623  1.00 48.87  ? 542  PRO   D N   1 
ATOM   12111 C  CA  . PRO   D  1 241 ? 35.634  43.106  -26.111  1.00 45.83  ? 542  PRO   D CA  1 
ATOM   12112 C  C   . PRO   D  1 241 ? 36.646  42.958  -27.232  1.00 44.05  ? 542  PRO   D C   1 
ATOM   12113 O  O   . PRO   D  1 241 ? 36.615  41.974  -27.990  1.00 41.78  ? 542  PRO   D O   1 
ATOM   12114 C  CB  . PRO   D  1 241 ? 35.766  41.971  -25.086  1.00 40.22  ? 542  PRO   D CB  1 
ATOM   12115 C  CG  . PRO   D  1 241 ? 34.355  41.646  -24.696  1.00 38.72  ? 542  PRO   D CG  1 
ATOM   12116 C  CD  . PRO   D  1 241 ? 33.548  41.852  -25.943  1.00 48.14  ? 542  PRO   D CD  1 
ATOM   12117 N  N   . PRO   D  1 242 ? 37.560  43.916  -27.363  1.00 37.53  ? 543  PRO   D N   1 
ATOM   12118 C  CA  . PRO   D  1 242 ? 38.491  43.900  -28.496  1.00 45.07  ? 543  PRO   D CA  1 
ATOM   12119 C  C   . PRO   D  1 242 ? 39.274  42.604  -28.627  1.00 48.59  ? 543  PRO   D C   1 
ATOM   12120 O  O   . PRO   D  1 242 ? 39.545  42.165  -29.760  1.00 42.18  ? 543  PRO   D O   1 
ATOM   12121 C  CB  . PRO   D  1 242 ? 39.406  45.098  -28.203  1.00 46.34  ? 543  PRO   D CB  1 
ATOM   12122 C  CG  . PRO   D  1 242 ? 38.588  46.003  -27.336  1.00 49.59  ? 543  PRO   D CG  1 
ATOM   12123 C  CD  . PRO   D  1 242 ? 37.723  45.107  -26.511  1.00 41.81  ? 543  PRO   D CD  1 
ATOM   12124 N  N   . GLU   D  1 243 ? 39.622  41.960  -27.507  1.00 40.25  ? 544  GLU   D N   1 
ATOM   12125 C  CA  . GLU   D  1 243 ? 40.399  40.726  -27.566  1.00 32.93  ? 544  GLU   D CA  1 
ATOM   12126 C  C   . GLU   D  1 243 ? 39.601  39.542  -28.110  1.00 37.72  ? 544  GLU   D C   1 
ATOM   12127 O  O   . GLU   D  1 243 ? 40.183  38.476  -28.332  1.00 41.19  ? 544  GLU   D O   1 
ATOM   12128 C  CB  . GLU   D  1 243 ? 40.962  40.389  -26.176  1.00 42.07  ? 544  GLU   D CB  1 
ATOM   12129 C  CG  . GLU   D  1 243 ? 39.919  39.980  -25.116  1.00 34.57  ? 544  GLU   D CG  1 
ATOM   12130 C  CD  . GLU   D  1 243 ? 39.354  41.163  -24.333  1.00 44.28  ? 544  GLU   D CD  1 
ATOM   12131 O  OE1 . GLU   D  1 243 ? 39.641  42.320  -24.706  1.00 46.43  ? 544  GLU   D OE1 1 
ATOM   12132 O  OE2 . GLU   D  1 243 ? 38.630  40.938  -23.330  1.00 50.95  ? 544  GLU   D OE2 1 
ATOM   12133 N  N   . LEU   D  1 244 ? 38.295  39.685  -28.317  1.00 37.69  ? 545  LEU   D N   1 
ATOM   12134 C  CA  . LEU   D  1 244 ? 37.507  38.631  -28.949  1.00 34.58  ? 545  LEU   D CA  1 
ATOM   12135 C  C   . LEU   D  1 244 ? 37.378  38.786  -30.474  1.00 40.48  ? 545  LEU   D C   1 
ATOM   12136 O  O   . LEU   D  1 244 ? 36.865  37.868  -31.126  1.00 37.34  ? 545  LEU   D O   1 
ATOM   12137 C  CB  . LEU   D  1 244 ? 36.104  38.581  -28.332  1.00 32.74  ? 545  LEU   D CB  1 
ATOM   12138 C  CG  . LEU   D  1 244 ? 35.872  38.124  -26.886  1.00 38.88  ? 545  LEU   D CG  1 
ATOM   12139 C  CD1 . LEU   D  1 244 ? 34.377  38.036  -26.649  1.00 34.46  ? 545  LEU   D CD1 1 
ATOM   12140 C  CD2 . LEU   D  1 244 ? 36.534  36.806  -26.563  1.00 41.19  ? 545  LEU   D CD2 1 
ATOM   12141 N  N   . VAL   D  1 245 ? 37.818  39.908  -31.053  1.00 36.39  ? 546  VAL   D N   1 
ATOM   12142 C  CA  . VAL   D  1 245 ? 37.696  40.173  -32.488  1.00 39.91  ? 546  VAL   D CA  1 
ATOM   12143 C  C   . VAL   D  1 245 ? 39.038  39.843  -33.135  1.00 37.49  ? 546  VAL   D C   1 
ATOM   12144 O  O   . VAL   D  1 245 ? 39.961  40.659  -33.131  1.00 34.29  ? 546  VAL   D O   1 
ATOM   12145 C  CB  . VAL   D  1 245 ? 37.294  41.624  -32.774  1.00 38.02  ? 546  VAL   D CB  1 
ATOM   12146 C  CG1 . VAL   D  1 245 ? 37.170  41.851  -34.277  1.00 43.10  ? 546  VAL   D CG1 1 
ATOM   12147 C  CG2 . VAL   D  1 245 ? 35.988  41.966  -32.102  1.00 33.57  ? 546  VAL   D CG2 1 
ATOM   12148 N  N   . LEU   D  1 246 ? 39.166  38.647  -33.693  1.00 31.77  ? 547  LEU   D N   1 
ATOM   12149 C  CA  . LEU   D  1 246 ? 40.402  38.291  -34.370  1.00 34.97  ? 547  LEU   D CA  1 
ATOM   12150 C  C   . LEU   D  1 246 ? 40.409  38.950  -35.751  1.00 37.02  ? 547  LEU   D C   1 
ATOM   12151 O  O   . LEU   D  1 246 ? 39.403  38.915  -36.465  1.00 42.29  ? 547  LEU   D O   1 
ATOM   12152 C  CB  . LEU   D  1 246 ? 40.535  36.775  -34.481  1.00 35.42  ? 547  LEU   D CB  1 
ATOM   12153 C  CG  . LEU   D  1 246 ? 41.644  36.205  -35.370  1.00 39.66  ? 547  LEU   D CG  1 
ATOM   12154 C  CD1 . LEU   D  1 246 ? 42.980  36.282  -34.653  1.00 39.72  ? 547  LEU   D CD1 1 
ATOM   12155 C  CD2 . LEU   D  1 246 ? 41.324  34.779  -35.754  1.00 38.05  ? 547  LEU   D CD2 1 
ATOM   12156 N  N   . GLU   D  1 247 ? 41.522  39.591  -36.100  1.00 36.05  ? 548  GLU   D N   1 
ATOM   12157 C  CA  . GLU   D  1 247 ? 41.659  40.312  -37.360  1.00 38.78  ? 548  GLU   D CA  1 
ATOM   12158 C  C   . GLU   D  1 247 ? 42.950  39.900  -38.060  1.00 40.07  ? 548  GLU   D C   1 
ATOM   12159 O  O   . GLU   D  1 247 ? 43.900  39.423  -37.439  1.00 41.70  ? 548  GLU   D O   1 
ATOM   12160 C  CB  . GLU   D  1 247 ? 41.652  41.833  -37.149  1.00 32.21  ? 548  GLU   D CB  1 
ATOM   12161 C  CG  . GLU   D  1 247 ? 40.302  42.426  -36.797  1.00 39.90  ? 548  GLU   D CG  1 
ATOM   12162 C  CD  . GLU   D  1 247 ? 40.407  43.895  -36.442  1.00 49.35  ? 548  GLU   D CD  1 
ATOM   12163 O  OE1 . GLU   D  1 247 ? 41.317  44.245  -35.678  1.00 56.11  ? 548  GLU   D OE1 1 
ATOM   12164 O  OE2 . GLU   D  1 247 ? 39.605  44.709  -36.938  1.00 54.42  ? 548  GLU   D OE2 1 
ATOM   12165 N  N   . VAL   D  1 248 ? 42.988  40.101  -39.376  1.00 37.20  ? 549  VAL   D N   1 
ATOM   12166 C  CA  . VAL   D  1 248 ? 44.112  39.683  -40.198  1.00 35.01  ? 549  VAL   D CA  1 
ATOM   12167 C  C   . VAL   D  1 248 ? 44.567  40.881  -41.026  1.00 41.76  ? 549  VAL   D C   1 
ATOM   12168 O  O   . VAL   D  1 248 ? 43.809  41.367  -41.873  1.00 32.53  ? 549  VAL   D O   1 
ATOM   12169 C  CB  . VAL   D  1 248 ? 43.752  38.509  -41.125  1.00 36.13  ? 549  VAL   D CB  1 
ATOM   12170 C  CG1 . VAL   D  1 248 ? 44.953  38.118  -42.003  1.00 38.84  ? 549  VAL   D CG1 1 
ATOM   12171 C  CG2 . VAL   D  1 248 ? 43.224  37.325  -40.325  1.00 28.73  ? 549  VAL   D CG2 1 
ATOM   12172 N  N   . PRO   D  1 249 ? 45.774  41.394  -40.820  1.00 29.83  ? 550  PRO   D N   1 
ATOM   12173 C  CA  . PRO   D  1 249 ? 46.280  42.461  -41.685  1.00 44.59  ? 550  PRO   D CA  1 
ATOM   12174 C  C   . PRO   D  1 249 ? 46.697  41.880  -43.031  1.00 48.05  ? 550  PRO   D C   1 
ATOM   12175 O  O   . PRO   D  1 249 ? 47.365  40.846  -43.102  1.00 46.74  ? 550  PRO   D O   1 
ATOM   12176 C  CB  . PRO   D  1 249 ? 47.482  42.996  -40.907  1.00 37.76  ? 550  PRO   D CB  1 
ATOM   12177 C  CG  . PRO   D  1 249 ? 47.989  41.777  -40.168  1.00 31.75  ? 550  PRO   D CG  1 
ATOM   12178 C  CD  . PRO   D  1 249 ? 46.780  40.928  -39.847  1.00 34.21  ? 550  PRO   D CD  1 
ATOM   12179 N  N   . ILE   D  1 250 ? 46.295  42.539  -44.107  1.00 44.09  ? 551  ILE   D N   1 
ATOM   12180 C  CA  . ILE   D  1 250 ? 46.454  41.963  -45.440  1.00 43.06  ? 551  ILE   D CA  1 
ATOM   12181 C  C   . ILE   D  1 250 ? 47.796  42.385  -46.019  1.00 41.51  ? 551  ILE   D C   1 
ATOM   12182 O  O   . ILE   D  1 250 ? 48.052  43.580  -46.204  1.00 49.24  ? 551  ILE   D O   1 
ATOM   12183 C  CB  . ILE   D  1 250 ? 45.295  42.363  -46.364  1.00 40.68  ? 551  ILE   D CB  1 
ATOM   12184 C  CG1 . ILE   D  1 250 ? 43.976  42.021  -45.679  1.00 40.07  ? 551  ILE   D CG1 1 
ATOM   12185 C  CG2 . ILE   D  1 250 ? 45.392  41.629  -47.704  1.00 38.39  ? 551  ILE   D CG2 1 
ATOM   12186 C  CD1 . ILE   D  1 250 ? 43.926  40.610  -45.111  1.00 31.52  ? 551  ILE   D CD1 1 
ATOM   12187 N  N   . ARG   D  1 251 ? 48.657  41.405  -46.301  1.00 38.95  ? 552  ARG   D N   1 
ATOM   12188 C  CA  . ARG   D  1 251 ? 49.902  41.640  -47.029  1.00 44.74  ? 552  ARG   D CA  1 
ATOM   12189 C  C   . ARG   D  1 251 ? 49.959  40.722  -48.255  1.00 45.70  ? 552  ARG   D C   1 
ATOM   12190 O  O   . ARG   D  1 251 ? 49.136  39.820  -48.429  1.00 42.77  ? 552  ARG   D O   1 
ATOM   12191 C  CB  . ARG   D  1 251 ? 51.139  41.443  -46.130  1.00 40.01  ? 552  ARG   D CB  1 
ATOM   12192 C  CG  . ARG   D  1 251 ? 51.251  40.081  -45.440  1.00 46.26  ? 552  ARG   D CG  1 
ATOM   12193 C  CD  . ARG   D  1 251 ? 50.429  39.979  -44.111  1.00 44.94  ? 552  ARG   D CD  1 
ATOM   12194 N  NE  . ARG   D  1 251 ? 50.835  38.805  -43.340  1.00 43.59  ? 552  ARG   D NE  1 
ATOM   12195 C  CZ  . ARG   D  1 251 ? 50.167  38.274  -42.315  1.00 46.45  ? 552  ARG   D CZ  1 
ATOM   12196 N  NH1 . ARG   D  1 251 ? 50.661  37.207  -41.708  1.00 47.80  ? 552  ARG   D NH1 1 
ATOM   12197 N  NH2 . ARG   D  1 251 ? 49.017  38.787  -41.889  1.00 45.04  ? 552  ARG   D NH2 1 
ATOM   12198 N  N   . HIS   D  1 252 ? 50.940  40.963  -49.121  1.00 46.98  ? 553  HIS   D N   1 
ATOM   12199 C  CA  . HIS   D  1 252 ? 51.091  40.191  -50.345  1.00 46.66  ? 553  HIS   D CA  1 
ATOM   12200 C  C   . HIS   D  1 252 ? 52.433  39.464  -50.357  1.00 46.78  ? 553  HIS   D C   1 
ATOM   12201 O  O   . HIS   D  1 252 ? 53.449  40.034  -49.950  1.00 50.39  ? 553  HIS   D O   1 
ATOM   12202 C  CB  . HIS   D  1 252 ? 50.982  41.114  -51.578  1.00 40.02  ? 553  HIS   D CB  1 
ATOM   12203 C  CG  . HIS   D  1 252 ? 50.838  40.389  -52.879  1.00 45.85  ? 553  HIS   D CG  1 
ATOM   12204 N  ND1 . HIS   D  1 252 ? 51.910  39.836  -53.546  1.00 47.09  ? 553  HIS   D ND1 1 
ATOM   12205 C  CD2 . HIS   D  1 252 ? 49.753  40.151  -53.652  1.00 47.17  ? 553  HIS   D CD2 1 
ATOM   12206 C  CE1 . HIS   D  1 252 ? 51.489  39.275  -54.666  1.00 46.08  ? 553  HIS   D CE1 1 
ATOM   12207 N  NE2 . HIS   D  1 252 ? 50.184  39.450  -54.754  1.00 44.01  ? 553  HIS   D NE2 1 
ATOM   12208 N  N   . PRO   D  1 253 ? 52.474  38.214  -50.825  1.00 46.85  ? 554  PRO   D N   1 
ATOM   12209 C  CA  . PRO   D  1 253 ? 53.736  37.457  -50.780  1.00 41.75  ? 554  PRO   D CA  1 
ATOM   12210 C  C   . PRO   D  1 253 ? 54.829  38.017  -51.678  1.00 53.45  ? 554  PRO   D C   1 
ATOM   12211 O  O   . PRO   D  1 253 ? 56.010  37.741  -51.434  1.00 64.80  ? 554  PRO   D O   1 
ATOM   12212 C  CB  . PRO   D  1 253 ? 53.308  36.059  -51.239  1.00 42.59  ? 554  PRO   D CB  1 
ATOM   12213 C  CG  . PRO   D  1 253 ? 52.172  36.342  -52.211  1.00 43.36  ? 554  PRO   D CG  1 
ATOM   12214 C  CD  . PRO   D  1 253 ? 51.411  37.471  -51.535  1.00 47.22  ? 554  PRO   D CD  1 
ATOM   12215 N  N   . LYS   D  1 254 ? 54.482  38.790  -52.703  1.00 44.88  ? 555  LYS   D N   1 
ATOM   12216 C  CA  . LYS   D  1 254 ? 55.454  39.337  -53.643  1.00 55.88  ? 555  LYS   D CA  1 
ATOM   12217 C  C   . LYS   D  1 254 ? 55.557  40.851  -53.577  1.00 55.96  ? 555  LYS   D C   1 
ATOM   12218 O  O   . LYS   D  1 254 ? 56.662  41.394  -53.586  1.00 61.70  ? 555  LYS   D O   1 
ATOM   12219 C  CB  . LYS   D  1 254 ? 55.097  38.922  -55.080  1.00 66.33  ? 555  LYS   D CB  1 
ATOM   12220 C  CG  . LYS   D  1 254 ? 55.105  37.427  -55.328  1.00 73.67  ? 555  LYS   D CG  1 
ATOM   12221 C  CD  . LYS   D  1 254 ? 56.464  36.819  -55.010  1.00 83.56  ? 555  LYS   D CD  1 
ATOM   12222 C  CE  . LYS   D  1 254 ? 56.690  35.574  -55.847  1.00 92.31  ? 555  LYS   D CE  1 
ATOM   12223 N  NZ  . LYS   D  1 254 ? 55.449  34.747  -55.911  1.00 90.68  ? 555  LYS   D NZ  1 
ATOM   12224 N  N   . PHE   D  1 255 ? 54.428  41.545  -53.522  1.00 57.06  ? 556  PHE   D N   1 
ATOM   12225 C  CA  . PHE   D  1 255 ? 54.417  43.001  -53.498  1.00 59.44  ? 556  PHE   D CA  1 
ATOM   12226 C  C   . PHE   D  1 255 ? 54.618  43.467  -52.060  1.00 67.22  ? 556  PHE   D C   1 
ATOM   12227 O  O   . PHE   D  1 255 ? 53.717  43.341  -51.219  1.00 67.17  ? 556  PHE   D O   1 
ATOM   12228 C  CB  . PHE   D  1 255 ? 53.110  43.535  -54.074  1.00 60.42  ? 556  PHE   D CB  1 
ATOM   12229 C  CG  . PHE   D  1 255 ? 52.884  43.175  -55.520  1.00 60.98  ? 556  PHE   D CG  1 
ATOM   12230 C  CD1 . PHE   D  1 255 ? 53.884  43.346  -56.455  1.00 63.38  ? 556  PHE   D CD1 1 
ATOM   12231 C  CD2 . PHE   D  1 255 ? 51.660  42.677  -55.939  1.00 57.76  ? 556  PHE   D CD2 1 
ATOM   12232 C  CE1 . PHE   D  1 255 ? 53.670  43.016  -57.780  1.00 62.00  ? 556  PHE   D CE1 1 
ATOM   12233 C  CE2 . PHE   D  1 255 ? 51.437  42.345  -57.249  1.00 55.36  ? 556  PHE   D CE2 1 
ATOM   12234 C  CZ  . PHE   D  1 255 ? 52.443  42.518  -58.177  1.00 59.04  ? 556  PHE   D CZ  1 
ATOM   12235 N  N   . GLU   D  1 256 ? 55.807  43.996  -51.770  1.00 65.37  ? 557  GLU   D N   1 
ATOM   12236 C  CA  . GLU   D  1 256 ? 56.060  44.496  -50.427  1.00 68.58  ? 557  GLU   D CA  1 
ATOM   12237 C  C   . GLU   D  1 256 ? 55.248  45.749  -50.141  1.00 67.35  ? 557  GLU   D C   1 
ATOM   12238 O  O   . GLU   D  1 256 ? 54.924  46.019  -48.982  1.00 65.51  ? 557  GLU   D O   1 
ATOM   12239 C  CB  . GLU   D  1 256 ? 57.549  44.761  -50.247  1.00 75.43  ? 557  GLU   D CB  1 
ATOM   12240 C  CG  . GLU   D  1 256 ? 58.387  43.531  -50.512  1.00 85.73  ? 557  GLU   D CG  1 
ATOM   12241 C  CD  . GLU   D  1 256 ? 59.765  43.868  -51.037  1.00 97.78  ? 557  GLU   D CD  1 
ATOM   12242 O  OE1 . GLU   D  1 256 ? 60.388  44.819  -50.513  1.00 105.72 ? 557  GLU   D OE1 1 
ATOM   12243 O  OE2 . GLU   D  1 256 ? 60.218  43.187  -51.981  1.00 96.87  ? 557  GLU   D OE2 1 
ATOM   12244 N  N   . TRP   D  1 257 ? 54.892  46.513  -51.177  1.00 64.11  ? 558  TRP   D N   1 
ATOM   12245 C  CA  . TRP   D  1 257 ? 54.095  47.710  -50.945  1.00 62.99  ? 558  TRP   D CA  1 
ATOM   12246 C  C   . TRP   D  1 257 ? 52.701  47.383  -50.443  1.00 64.00  ? 558  TRP   D C   1 
ATOM   12247 O  O   . TRP   D  1 257 ? 52.013  48.280  -49.949  1.00 70.00  ? 558  TRP   D O   1 
ATOM   12248 C  CB  . TRP   D  1 257 ? 53.982  48.552  -52.217  1.00 67.45  ? 558  TRP   D CB  1 
ATOM   12249 C  CG  . TRP   D  1 257 ? 53.720  47.764  -53.476  1.00 67.82  ? 558  TRP   D CG  1 
ATOM   12250 C  CD1 . TRP   D  1 257 ? 54.658  47.283  -54.345  1.00 61.54  ? 558  TRP   D CD1 1 
ATOM   12251 C  CD2 . TRP   D  1 257 ? 52.444  47.381  -54.014  1.00 65.85  ? 558  TRP   D CD2 1 
ATOM   12252 N  NE1 . TRP   D  1 257 ? 54.052  46.619  -55.377  1.00 56.50  ? 558  TRP   D NE1 1 
ATOM   12253 C  CE2 . TRP   D  1 257 ? 52.694  46.667  -55.208  1.00 60.49  ? 558  TRP   D CE2 1 
ATOM   12254 C  CE3 . TRP   D  1 257 ? 51.118  47.566  -53.604  1.00 63.14  ? 558  TRP   D CE3 1 
ATOM   12255 C  CZ2 . TRP   D  1 257 ? 51.666  46.135  -56.000  1.00 55.51  ? 558  TRP   D CZ2 1 
ATOM   12256 C  CZ3 . TRP   D  1 257 ? 50.092  47.037  -54.400  1.00 59.96  ? 558  TRP   D CZ3 1 
ATOM   12257 C  CH2 . TRP   D  1 257 ? 50.379  46.332  -55.582  1.00 54.44  ? 558  TRP   D CH2 1 
ATOM   12258 N  N   . PHE   D  1 258 ? 52.267  46.128  -50.558  1.00 57.03  ? 559  PHE   D N   1 
ATOM   12259 C  CA  . PHE   D  1 258 ? 50.856  45.839  -50.356  1.00 54.01  ? 559  PHE   D CA  1 
ATOM   12260 C  C   . PHE   D  1 258 ? 50.433  46.146  -48.931  1.00 50.61  ? 559  PHE   D C   1 
ATOM   12261 O  O   . PHE   D  1 258 ? 49.372  46.746  -48.713  1.00 46.43  ? 559  PHE   D O   1 
ATOM   12262 C  CB  . PHE   D  1 258 ? 50.545  44.391  -50.706  1.00 50.85  ? 559  PHE   D CB  1 
ATOM   12263 C  CG  . PHE   D  1 258 ? 49.103  44.157  -51.042  1.00 51.78  ? 559  PHE   D CG  1 
ATOM   12264 C  CD1 . PHE   D  1 258 ? 48.149  44.045  -50.032  1.00 44.86  ? 559  PHE   D CD1 1 
ATOM   12265 C  CD2 . PHE   D  1 258 ? 48.695  44.062  -52.375  1.00 53.89  ? 559  PHE   D CD2 1 
ATOM   12266 C  CE1 . PHE   D  1 258 ? 46.818  43.841  -50.345  1.00 45.83  ? 559  PHE   D CE1 1 
ATOM   12267 C  CE2 . PHE   D  1 258 ? 47.365  43.852  -52.703  1.00 49.49  ? 559  PHE   D CE2 1 
ATOM   12268 C  CZ  . PHE   D  1 258 ? 46.421  43.747  -51.692  1.00 50.92  ? 559  PHE   D CZ  1 
ATOM   12269 N  N   . LYS   D  1 259 ? 51.262  45.764  -47.951  1.00 45.92  ? 560  LYS   D N   1 
ATOM   12270 C  CA  . LYS   D  1 259 ? 50.975  46.095  -46.559  1.00 52.49  ? 560  LYS   D CA  1 
ATOM   12271 C  C   . LYS   D  1 259 ? 50.756  47.592  -46.350  1.00 53.33  ? 560  LYS   D C   1 
ATOM   12272 O  O   . LYS   D  1 259 ? 50.020  47.980  -45.434  1.00 44.24  ? 560  LYS   D O   1 
ATOM   12273 C  CB  . LYS   D  1 259 ? 52.102  45.582  -45.647  1.00 53.36  ? 560  LYS   D CB  1 
ATOM   12274 C  CG  . LYS   D  1 259 ? 53.495  46.138  -45.928  1.00 59.88  ? 560  LYS   D CG  1 
ATOM   12275 C  CD  . LYS   D  1 259 ? 54.473  45.745  -44.804  1.00 66.30  ? 560  LYS   D CD  1 
ATOM   12276 C  CE  . LYS   D  1 259 ? 55.861  46.369  -44.980  1.00 68.98  ? 560  LYS   D CE  1 
ATOM   12277 N  NZ  . LYS   D  1 259 ? 56.503  46.017  -46.280  1.00 72.42  ? 560  LYS   D NZ  1 
ATOM   12278 N  N   . ASP   D  1 260 ? 51.337  48.440  -47.201  1.00 52.83  ? 561  ASP   D N   1 
ATOM   12279 C  CA  . ASP   D  1 260 ? 51.160  49.881  -47.067  1.00 58.86  ? 561  ASP   D CA  1 
ATOM   12280 C  C   . ASP   D  1 260 ? 49.779  50.354  -47.489  1.00 54.70  ? 561  ASP   D C   1 
ATOM   12281 O  O   . ASP   D  1 260 ? 49.445  51.523  -47.267  1.00 54.63  ? 561  ASP   D O   1 
ATOM   12282 C  CB  . ASP   D  1 260 ? 52.229  50.616  -47.871  1.00 67.15  ? 561  ASP   D CB  1 
ATOM   12283 C  CG  . ASP   D  1 260 ? 53.618  50.171  -47.500  1.00 77.68  ? 561  ASP   D CG  1 
ATOM   12284 O  OD1 . ASP   D  1 260 ? 53.729  49.404  -46.517  1.00 82.37  ? 561  ASP   D OD1 1 
ATOM   12285 O  OD2 . ASP   D  1 260 ? 54.590  50.569  -48.179  1.00 76.63  ? 561  ASP   D OD2 1 
ATOM   12286 N  N   . LEU   D  1 261 ? 48.965  49.486  -48.082  1.00 49.31  ? 562  LEU   D N   1 
ATOM   12287 C  CA  . LEU   D  1 261 ? 47.584  49.872  -48.315  1.00 51.10  ? 562  LEU   D CA  1 
ATOM   12288 C  C   . LEU   D  1 261 ? 46.818  49.996  -47.003  1.00 54.21  ? 562  LEU   D C   1 
ATOM   12289 O  O   . LEU   D  1 261 ? 45.775  50.661  -46.962  1.00 53.17  ? 562  LEU   D O   1 
ATOM   12290 C  CB  . LEU   D  1 261 ? 46.929  48.870  -49.265  1.00 47.62  ? 562  LEU   D CB  1 
ATOM   12291 C  CG  . LEU   D  1 261 ? 47.643  48.807  -50.627  1.00 49.51  ? 562  LEU   D CG  1 
ATOM   12292 C  CD1 . LEU   D  1 261 ? 47.207  47.606  -51.449  1.00 40.19  ? 562  LEU   D CD1 1 
ATOM   12293 C  CD2 . LEU   D  1 261 ? 47.422  50.087  -51.421  1.00 49.54  ? 562  LEU   D CD2 1 
ATOM   12294 N  N   . GLY   D  1 262 ? 47.335  49.401  -45.929  1.00 53.53  ? 563  GLY   D N   1 
ATOM   12295 C  CA  . GLY   D  1 262 ? 46.712  49.483  -44.621  1.00 48.95  ? 563  GLY   D CA  1 
ATOM   12296 C  C   . GLY   D  1 262 ? 45.482  48.622  -44.443  1.00 53.75  ? 563  GLY   D C   1 
ATOM   12297 O  O   . GLY   D  1 262 ? 44.655  48.904  -43.570  1.00 57.28  ? 563  GLY   D O   1 
ATOM   12298 N  N   . LEU   D  1 263 ? 45.322  47.586  -45.251  1.00 48.65  ? 564  LEU   D N   1 
ATOM   12299 C  CA  . LEU   D  1 263 ? 44.092  46.824  -45.216  1.00 46.47  ? 564  LEU   D CA  1 
ATOM   12300 C  C   . LEU   D  1 263 ? 44.168  45.718  -44.170  1.00 43.36  ? 564  LEU   D C   1 
ATOM   12301 O  O   . LEU   D  1 263 ? 45.223  45.123  -43.922  1.00 41.37  ? 564  LEU   D O   1 
ATOM   12302 C  CB  . LEU   D  1 263 ? 43.781  46.226  -46.590  1.00 45.64  ? 564  LEU   D CB  1 
ATOM   12303 C  CG  . LEU   D  1 263 ? 43.675  47.167  -47.799  1.00 57.15  ? 564  LEU   D CG  1 
ATOM   12304 C  CD1 . LEU   D  1 263 ? 43.936  46.400  -49.092  1.00 51.70  ? 564  LEU   D CD1 1 
ATOM   12305 C  CD2 . LEU   D  1 263 ? 42.320  47.855  -47.866  1.00 56.12  ? 564  LEU   D CD2 1 
ATOM   12306 N  N   . LYS   D  1 264 ? 43.023  45.453  -43.558  1.00 43.29  ? 565  LYS   D N   1 
ATOM   12307 C  CA  . LYS   D  1 264 ? 42.845  44.278  -42.722  1.00 44.48  ? 565  LYS   D CA  1 
ATOM   12308 C  C   . LYS   D  1 264 ? 41.408  43.813  -42.875  1.00 40.53  ? 565  LYS   D C   1 
ATOM   12309 O  O   . LYS   D  1 264 ? 40.576  44.488  -43.492  1.00 48.95  ? 565  LYS   D O   1 
ATOM   12310 C  CB  . LYS   D  1 264 ? 43.174  44.568  -41.257  1.00 48.01  ? 565  LYS   D CB  1 
ATOM   12311 C  CG  . LYS   D  1 264 ? 42.307  45.636  -40.626  1.00 50.58  ? 565  LYS   D CG  1 
ATOM   12312 C  CD  . LYS   D  1 264 ? 42.718  45.848  -39.189  1.00 50.72  ? 565  LYS   D CD  1 
ATOM   12313 C  CE  . LYS   D  1 264 ? 42.364  47.230  -38.702  1.00 54.42  ? 565  LYS   D CE  1 
ATOM   12314 N  NZ  . LYS   D  1 264 ? 41.671  47.123  -37.388  1.00 54.47  ? 565  LYS   D NZ  1 
ATOM   12315 N  N   . TRP   D  1 265 ? 41.131  42.627  -42.349  1.00 35.47  ? 566  TRP   D N   1 
ATOM   12316 C  CA  . TRP   D  1 265 ? 39.762  42.136  -42.278  1.00 40.52  ? 566  TRP   D CA  1 
ATOM   12317 C  C   . TRP   D  1 265 ? 39.611  41.319  -41.005  1.00 49.57  ? 566  TRP   D C   1 
ATOM   12318 O  O   . TRP   D  1 265 ? 40.590  40.969  -40.339  1.00 48.21  ? 566  TRP   D O   1 
ATOM   12319 C  CB  . TRP   D  1 265 ? 39.362  41.309  -43.515  1.00 33.38  ? 566  TRP   D CB  1 
ATOM   12320 C  CG  . TRP   D  1 265 ? 37.880  41.340  -43.766  1.00 27.94  ? 566  TRP   D CG  1 
ATOM   12321 C  CD1 . TRP   D  1 265 ? 36.985  40.314  -43.586  1.00 41.05  ? 566  TRP   D CD1 1 
ATOM   12322 C  CD2 . TRP   D  1 265 ? 37.114  42.466  -44.198  1.00 29.52  ? 566  TRP   D CD2 1 
ATOM   12323 N  NE1 . TRP   D  1 265 ? 35.702  40.736  -43.895  1.00 35.46  ? 566  TRP   D NE1 1 
ATOM   12324 C  CE2 . TRP   D  1 265 ? 35.757  42.052  -44.275  1.00 30.85  ? 566  TRP   D CE2 1 
ATOM   12325 C  CE3 . TRP   D  1 265 ? 37.445  43.784  -44.560  1.00 35.44  ? 566  TRP   D CE3 1 
ATOM   12326 C  CZ2 . TRP   D  1 265 ? 34.734  42.909  -44.687  1.00 33.96  ? 566  TRP   D CZ2 1 
ATOM   12327 C  CZ3 . TRP   D  1 265 ? 36.424  44.641  -44.977  1.00 29.61  ? 566  TRP   D CZ3 1 
ATOM   12328 C  CH2 . TRP   D  1 265 ? 35.080  44.195  -45.033  1.00 34.03  ? 566  TRP   D CH2 1 
ATOM   12329 N  N   . TYR   D  1 266 ? 38.365  41.030  -40.669  1.00 44.81  ? 567  TYR   D N   1 
ATOM   12330 C  CA  . TYR   D  1 266 ? 38.082  40.230  -39.499  1.00 42.27  ? 567  TYR   D CA  1 
ATOM   12331 C  C   . TYR   D  1 266 ? 38.004  38.757  -39.879  1.00 45.09  ? 567  TYR   D C   1 
ATOM   12332 O  O   . TYR   D  1 266 ? 37.731  38.403  -41.026  1.00 48.05  ? 567  TYR   D O   1 
ATOM   12333 C  CB  . TYR   D  1 266 ? 36.788  40.696  -38.857  1.00 32.93  ? 567  TYR   D CB  1 
ATOM   12334 C  CG  . TYR   D  1 266 ? 35.643  40.886  -39.816  1.00 40.66  ? 567  TYR   D CG  1 
ATOM   12335 C  CD1 . TYR   D  1 266 ? 34.763  39.851  -40.072  1.00 38.82  ? 567  TYR   D CD1 1 
ATOM   12336 C  CD2 . TYR   D  1 266 ? 35.419  42.112  -40.445  1.00 38.36  ? 567  TYR   D CD2 1 
ATOM   12337 C  CE1 . TYR   D  1 266 ? 33.697  40.010  -40.926  1.00 30.69  ? 567  TYR   D CE1 1 
ATOM   12338 C  CE2 . TYR   D  1 266 ? 34.339  42.281  -41.307  1.00 38.90  ? 567  TYR   D CE2 1 
ATOM   12339 C  CZ  . TYR   D  1 266 ? 33.487  41.215  -41.543  1.00 34.91  ? 567  TYR   D CZ  1 
ATOM   12340 O  OH  . TYR   D  1 266 ? 32.410  41.334  -42.388  1.00 50.48  ? 567  TYR   D OH  1 
ATOM   12341 N  N   . GLY   D  1 267 ? 38.262  37.894  -38.904  1.00 38.06  ? 568  GLY   D N   1 
ATOM   12342 C  CA  . GLY   D  1 267 ? 38.369  36.485  -39.209  1.00 33.54  ? 568  GLY   D CA  1 
ATOM   12343 C  C   . GLY   D  1 267 ? 37.066  35.717  -39.251  1.00 34.07  ? 568  GLY   D C   1 
ATOM   12344 O  O   . GLY   D  1 267 ? 37.012  34.649  -39.873  1.00 36.20  ? 568  GLY   D O   1 
ATOM   12345 N  N   . LEU   D  1 268 ? 36.013  36.236  -38.615  1.00 30.86  ? 569  LEU   D N   1 
ATOM   12346 C  CA  . LEU   D  1 268 ? 34.816  35.446  -38.322  1.00 34.36  ? 569  LEU   D CA  1 
ATOM   12347 C  C   . LEU   D  1 268 ? 33.603  35.978  -39.079  1.00 40.19  ? 569  LEU   D C   1 
ATOM   12348 O  O   . LEU   D  1 268 ? 33.040  37.015  -38.690  1.00 42.99  ? 569  LEU   D O   1 
ATOM   12349 C  CB  . LEU   D  1 268 ? 34.538  35.451  -36.808  1.00 37.58  ? 569  LEU   D CB  1 
ATOM   12350 C  CG  . LEU   D  1 268 ? 33.385  34.536  -36.382  1.00 37.91  ? 569  LEU   D CG  1 
ATOM   12351 C  CD1 . LEU   D  1 268 ? 33.814  33.078  -36.463  1.00 39.55  ? 569  LEU   D CD1 1 
ATOM   12352 C  CD2 . LEU   D  1 268 ? 32.874  34.860  -35.003  1.00 38.93  ? 569  LEU   D CD2 1 
ATOM   12353 N  N   . PRO   D  1 269 ? 33.146  35.314  -40.147  1.00 33.15  ? 570  PRO   D N   1 
ATOM   12354 C  CA  . PRO   D  1 269 ? 31.909  35.756  -40.815  1.00 31.42  ? 570  PRO   D CA  1 
ATOM   12355 C  C   . PRO   D  1 269 ? 30.708  35.213  -40.061  1.00 28.09  ? 570  PRO   D C   1 
ATOM   12356 O  O   . PRO   D  1 269 ? 30.551  34.000  -39.916  1.00 38.91  ? 570  PRO   D O   1 
ATOM   12357 C  CB  . PRO   D  1 269 ? 32.021  35.145  -42.229  1.00 28.70  ? 570  PRO   D CB  1 
ATOM   12358 C  CG  . PRO   D  1 269 ? 32.798  33.852  -42.010  1.00 26.89  ? 570  PRO   D CG  1 
ATOM   12359 C  CD  . PRO   D  1 269 ? 33.759  34.148  -40.815  1.00 32.62  ? 570  PRO   D CD  1 
ATOM   12360 N  N   . ALA   D  1 270 ? 29.838  36.106  -39.608  1.00 33.19  ? 571  ALA   D N   1 
ATOM   12361 C  CA  . ALA   D  1 270 ? 28.791  35.727  -38.657  1.00 29.38  ? 571  ALA   D CA  1 
ATOM   12362 C  C   . ALA   D  1 270 ? 27.500  36.476  -38.997  1.00 35.16  ? 571  ALA   D C   1 
ATOM   12363 O  O   . ALA   D  1 270 ? 27.305  37.603  -38.544  1.00 33.83  ? 571  ALA   D O   1 
ATOM   12364 C  CB  . ALA   D  1 270 ? 29.266  36.020  -37.235  1.00 30.81  ? 571  ALA   D CB  1 
ATOM   12365 N  N   . VAL   D  1 271 ? 26.619  35.840  -39.773  1.00 37.96  ? 572  VAL   D N   1 
ATOM   12366 C  CA  . VAL   D  1 271 ? 25.409  36.490  -40.270  1.00 30.13  ? 572  VAL   D CA  1 
ATOM   12367 C  C   . VAL   D  1 271 ? 24.363  36.533  -39.169  1.00 33.51  ? 572  VAL   D C   1 
ATOM   12368 O  O   . VAL   D  1 271 ? 24.019  35.501  -38.587  1.00 37.52  ? 572  VAL   D O   1 
ATOM   12369 C  CB  . VAL   D  1 271 ? 24.866  35.749  -41.504  1.00 38.37  ? 572  VAL   D CB  1 
ATOM   12370 C  CG1 . VAL   D  1 271 ? 23.381  36.103  -41.719  1.00 30.05  ? 572  VAL   D CG1 1 
ATOM   12371 C  CG2 . VAL   D  1 271 ? 25.732  36.055  -42.766  1.00 22.15  ? 572  VAL   D CG2 1 
ATOM   12372 N  N   . SER   D  1 272 ? 23.808  37.715  -38.918  1.00 32.72  ? 573  SER   D N   1 
ATOM   12373 C  CA  . SER   D  1 272 ? 22.958  37.890  -37.752  1.00 38.33  ? 573  SER   D CA  1 
ATOM   12374 C  C   . SER   D  1 272 ? 21.589  38.489  -38.064  1.00 41.21  ? 573  SER   D C   1 
ATOM   12375 O  O   . SER   D  1 272 ? 20.817  38.728  -37.127  1.00 45.19  ? 573  SER   D O   1 
ATOM   12376 C  CB  . SER   D  1 272 ? 23.677  38.747  -36.686  1.00 30.98  ? 573  SER   D CB  1 
ATOM   12377 O  OG  . SER   D  1 272 ? 24.234  39.929  -37.248  1.00 29.70  ? 573  SER   D OG  1 
ATOM   12378 N  N   . ASN   D  1 273 ? 21.241  38.710  -39.333  1.00 39.54  ? 574  ASN   D N   1 
ATOM   12379 C  CA  . ASN   D  1 273 ? 19.991  39.400  -39.650  1.00 40.81  ? 574  ASN   D CA  1 
ATOM   12380 C  C   . ASN   D  1 273 ? 18.956  38.497  -40.311  1.00 37.20  ? 574  ASN   D C   1 
ATOM   12381 O  O   . ASN   D  1 273 ? 17.925  38.989  -40.784  1.00 40.07  ? 574  ASN   D O   1 
ATOM   12382 C  CB  . ASN   D  1 273 ? 20.254  40.633  -40.523  1.00 32.43  ? 574  ASN   D CB  1 
ATOM   12383 C  CG  . ASN   D  1 273 ? 20.918  40.287  -41.846  1.00 41.91  ? 574  ASN   D CG  1 
ATOM   12384 O  OD1 . ASN   D  1 273 ? 21.150  39.121  -42.154  1.00 44.64  ? 574  ASN   D OD1 1 
ATOM   12385 N  ND2 . ASN   D  1 273 ? 21.219  41.308  -42.638  1.00 40.38  ? 574  ASN   D ND2 1 
ATOM   12386 N  N   . MET   D  1 274 ? 19.175  37.194  -40.323  1.00 32.01  ? 575  MET   D N   1 
ATOM   12387 C  CA  . MET   D  1 274 ? 18.252  36.281  -40.975  1.00 32.50  ? 575  MET   D CA  1 
ATOM   12388 C  C   . MET   D  1 274 ? 17.340  35.614  -39.960  1.00 41.93  ? 575  MET   D C   1 
ATOM   12389 O  O   . MET   D  1 274 ? 17.538  35.704  -38.750  1.00 53.80  ? 575  MET   D O   1 
ATOM   12390 C  CB  . MET   D  1 274 ? 19.017  35.232  -41.779  1.00 25.16  ? 575  MET   D CB  1 
ATOM   12391 C  CG  . MET   D  1 274 ? 19.757  35.864  -42.967  1.00 38.44  ? 575  MET   D CG  1 
ATOM   12392 S  SD  . MET   D  1 274 ? 20.365  34.607  -44.073  1.00 42.08  ? 575  MET   D SD  1 
ATOM   12393 C  CE  . MET   D  1 274 ? 18.826  34.090  -44.789  1.00 36.16  ? 575  MET   D CE  1 
ATOM   12394 N  N   . LEU   D  1 275 ? 16.332  34.924  -40.475  1.00 39.92  ? 576  LEU   D N   1 
ATOM   12395 C  CA  . LEU   D  1 275 ? 15.322  34.279  -39.656  1.00 36.95  ? 576  LEU   D CA  1 
ATOM   12396 C  C   . LEU   D  1 275 ? 15.424  32.782  -39.856  1.00 40.01  ? 576  LEU   D C   1 
ATOM   12397 O  O   . LEU   D  1 275 ? 15.499  32.308  -40.990  1.00 36.50  ? 576  LEU   D O   1 
ATOM   12398 C  CB  . LEU   D  1 275 ? 13.919  34.771  -40.015  1.00 41.80  ? 576  LEU   D CB  1 
ATOM   12399 C  CG  . LEU   D  1 275 ? 12.773  34.456  -39.050  1.00 40.33  ? 576  LEU   D CG  1 
ATOM   12400 C  CD1 . LEU   D  1 275 ? 11.842  35.651  -38.935  1.00 36.26  ? 576  LEU   D CD1 1 
ATOM   12401 C  CD2 . LEU   D  1 275 ? 11.993  33.242  -39.517  1.00 32.03  ? 576  LEU   D CD2 1 
ATOM   12402 N  N   . LEU   D  1 276 ? 15.425  32.041  -38.758  1.00 38.78  ? 577  LEU   D N   1 
ATOM   12403 C  CA  . LEU   D  1 276 ? 15.475  30.591  -38.799  1.00 34.43  ? 577  LEU   D CA  1 
ATOM   12404 C  C   . LEU   D  1 276 ? 14.064  30.071  -38.577  1.00 40.71  ? 577  LEU   D C   1 
ATOM   12405 O  O   . LEU   D  1 276 ? 13.443  30.378  -37.552  1.00 48.86  ? 577  LEU   D O   1 
ATOM   12406 C  CB  . LEU   D  1 276 ? 16.445  30.060  -37.745  1.00 37.01  ? 577  LEU   D CB  1 
ATOM   12407 C  CG  . LEU   D  1 276 ? 16.320  28.594  -37.365  1.00 40.58  ? 577  LEU   D CG  1 
ATOM   12408 C  CD1 . LEU   D  1 276 ? 16.588  27.729  -38.578  1.00 28.64  ? 577  LEU   D CD1 1 
ATOM   12409 C  CD2 . LEU   D  1 276 ? 17.254  28.235  -36.185  1.00 34.94  ? 577  LEU   D CD2 1 
ATOM   12410 N  N   . GLU   D  1 277 ? 13.548  29.310  -39.542  1.00 41.77  ? 578  GLU   D N   1 
ATOM   12411 C  CA  . GLU   D  1 277 ? 12.204  28.756  -39.448  1.00 43.91  ? 578  GLU   D CA  1 
ATOM   12412 C  C   . GLU   D  1 277 ? 12.271  27.244  -39.269  1.00 44.46  ? 578  GLU   D C   1 
ATOM   12413 O  O   . GLU   D  1 277 ? 12.808  26.536  -40.119  1.00 39.61  ? 578  GLU   D O   1 
ATOM   12414 C  CB  . GLU   D  1 277 ? 11.368  29.126  -40.665  1.00 34.00  ? 578  GLU   D CB  1 
ATOM   12415 C  CG  . GLU   D  1 277 ? 9.910   28.746  -40.556  1.00 42.36  ? 578  GLU   D CG  1 
ATOM   12416 C  CD  . GLU   D  1 277 ? 9.614   27.432  -41.239  1.00 64.25  ? 578  GLU   D CD  1 
ATOM   12417 O  OE1 . GLU   D  1 277 ? 10.304  27.130  -42.235  1.00 75.04  ? 578  GLU   D OE1 1 
ATOM   12418 O  OE2 . GLU   D  1 277 ? 8.703   26.696  -40.792  1.00 69.29  ? 578  GLU   D OE2 1 
ATOM   12419 N  N   . ILE   D  1 278 ? 11.724  26.761  -38.156  1.00 39.02  ? 579  ILE   D N   1 
ATOM   12420 C  CA  . ILE   D  1 278 ? 11.688  25.339  -37.817  1.00 42.21  ? 579  ILE   D CA  1 
ATOM   12421 C  C   . ILE   D  1 278 ? 10.261  24.985  -37.427  1.00 43.53  ? 579  ILE   D C   1 
ATOM   12422 O  O   . ILE   D  1 278 ? 9.744   25.507  -36.423  1.00 48.12  ? 579  ILE   D O   1 
ATOM   12423 C  CB  . ILE   D  1 278 ? 12.631  24.975  -36.654  1.00 35.11  ? 579  ILE   D CB  1 
ATOM   12424 C  CG1 . ILE   D  1 278 ? 14.083  25.357  -36.945  1.00 35.54  ? 579  ILE   D CG1 1 
ATOM   12425 C  CG2 . ILE   D  1 278 ? 12.511  23.509  -36.375  1.00 33.63  ? 579  ILE   D CG2 1 
ATOM   12426 C  CD1 . ILE   D  1 278 ? 14.994  25.189  -35.764  1.00 46.91  ? 579  ILE   D CD1 1 
ATOM   12427 N  N   . GLY   D  1 279 ? 9.646   24.084  -38.190  1.00 35.81  ? 580  GLY   D N   1 
ATOM   12428 C  CA  . GLY   D  1 279 ? 8.326   23.564  -37.852  1.00 38.44  ? 580  GLY   D CA  1 
ATOM   12429 C  C   . GLY   D  1 279 ? 7.270   24.626  -37.649  1.00 45.50  ? 580  GLY   D C   1 
ATOM   12430 O  O   . GLY   D  1 279 ? 6.379   24.469  -36.800  1.00 46.57  ? 580  GLY   D O   1 
ATOM   12431 N  N   . GLY   D  1 280 ? 7.347   25.714  -38.413  1.00 40.38  ? 581  GLY   D N   1 
ATOM   12432 C  CA  . GLY   D  1 280 ? 6.435   26.821  -38.257  1.00 42.47  ? 581  GLY   D CA  1 
ATOM   12433 C  C   . GLY   D  1 280 ? 6.836   27.844  -37.216  1.00 43.47  ? 581  GLY   D C   1 
ATOM   12434 O  O   . GLY   D  1 280 ? 6.256   28.933  -37.191  1.00 49.56  ? 581  GLY   D O   1 
ATOM   12435 N  N   . LEU   D  1 281 ? 7.791   27.537  -36.345  1.00 42.53  ? 582  LEU   D N   1 
ATOM   12436 C  CA  . LEU   D  1 281 ? 8.280   28.535  -35.404  1.00 44.29  ? 582  LEU   D CA  1 
ATOM   12437 C  C   . LEU   D  1 281 ? 9.329   29.408  -36.082  1.00 45.84  ? 582  LEU   D C   1 
ATOM   12438 O  O   . LEU   D  1 281 ? 10.110  28.934  -36.910  1.00 54.39  ? 582  LEU   D O   1 
ATOM   12439 C  CB  . LEU   D  1 281 ? 8.869   27.869  -34.159  1.00 31.67  ? 582  LEU   D CB  1 
ATOM   12440 C  CG  . LEU   D  1 281 ? 7.958   26.821  -33.515  1.00 40.14  ? 582  LEU   D CG  1 
ATOM   12441 C  CD1 . LEU   D  1 281 ? 8.704   26.039  -32.453  1.00 42.50  ? 582  LEU   D CD1 1 
ATOM   12442 C  CD2 . LEU   D  1 281 ? 6.720   27.487  -32.925  1.00 37.01  ? 582  LEU   D CD2 1 
ATOM   12443 N  N   . GLU   D  1 282 ? 9.354   30.683  -35.717  1.00 43.70  ? 583  GLU   D N   1 
ATOM   12444 C  CA  . GLU   D  1 282 ? 10.245  31.658  -36.331  1.00 46.01  ? 583  GLU   D CA  1 
ATOM   12445 C  C   . GLU   D  1 282 ? 11.231  32.171  -35.289  1.00 48.54  ? 583  GLU   D C   1 
ATOM   12446 O  O   . GLU   D  1 282 ? 10.826  32.789  -34.300  1.00 41.72  ? 583  GLU   D O   1 
ATOM   12447 C  CB  . GLU   D  1 282 ? 9.440   32.812  -36.922  1.00 43.55  ? 583  GLU   D CB  1 
ATOM   12448 C  CG  . GLU   D  1 282 ? 8.312   32.360  -37.839  1.00 52.53  ? 583  GLU   D CG  1 
ATOM   12449 C  CD  . GLU   D  1 282 ? 7.555   33.523  -38.441  1.00 57.34  ? 583  GLU   D CD  1 
ATOM   12450 O  OE1 . GLU   D  1 282 ? 7.441   33.576  -39.685  1.00 58.47  ? 583  GLU   D OE1 1 
ATOM   12451 O  OE2 . GLU   D  1 282 ? 7.079   34.387  -37.670  1.00 54.80  ? 583  GLU   D OE2 1 
ATOM   12452 N  N   . PHE   D  1 283 ? 12.520  31.935  -35.517  1.00 45.29  ? 584  PHE   D N   1 
ATOM   12453 C  CA  . PHE   D  1 283 ? 13.562  32.412  -34.612  1.00 33.38  ? 584  PHE   D CA  1 
ATOM   12454 C  C   . PHE   D  1 283 ? 14.201  33.646  -35.241  1.00 34.82  ? 584  PHE   D C   1 
ATOM   12455 O  O   . PHE   D  1 283 ? 15.153  33.554  -36.009  1.00 33.09  ? 584  PHE   D O   1 
ATOM   12456 C  CB  . PHE   D  1 283 ? 14.564  31.299  -34.324  1.00 27.04  ? 584  PHE   D CB  1 
ATOM   12457 C  CG  . PHE   D  1 283 ? 13.957  30.122  -33.597  1.00 32.39  ? 584  PHE   D CG  1 
ATOM   12458 C  CD1 . PHE   D  1 283 ? 13.808  30.144  -32.209  1.00 36.72  ? 584  PHE   D CD1 1 
ATOM   12459 C  CD2 . PHE   D  1 283 ? 13.493  29.014  -34.293  1.00 30.82  ? 584  PHE   D CD2 1 
ATOM   12460 C  CE1 . PHE   D  1 283 ? 13.234  29.065  -31.540  1.00 34.64  ? 584  PHE   D CE1 1 
ATOM   12461 C  CE2 . PHE   D  1 283 ? 12.917  27.935  -33.630  1.00 35.46  ? 584  PHE   D CE2 1 
ATOM   12462 C  CZ  . PHE   D  1 283 ? 12.793  27.958  -32.253  1.00 40.86  ? 584  PHE   D CZ  1 
ATOM   12463 N  N   . SER   D  1 284 ? 13.664  34.818  -34.899  1.00 38.83  ? 585  SER   D N   1 
ATOM   12464 C  CA  . SER   D  1 284 ? 14.071  36.061  -35.546  1.00 40.62  ? 585  SER   D CA  1 
ATOM   12465 C  C   . SER   D  1 284 ? 15.478  36.520  -35.179  1.00 39.19  ? 585  SER   D C   1 
ATOM   12466 O  O   . SER   D  1 284 ? 15.971  37.476  -35.790  1.00 36.17  ? 585  SER   D O   1 
ATOM   12467 C  CB  . SER   D  1 284 ? 13.071  37.172  -35.225  1.00 41.36  ? 585  SER   D CB  1 
ATOM   12468 O  OG  . SER   D  1 284 ? 12.848  37.277  -33.834  1.00 48.07  ? 585  SER   D OG  1 
ATOM   12469 N  N   . ALA   D  1 285 ? 16.137  35.893  -34.206  1.00 36.58  ? 586  ALA   D N   1 
ATOM   12470 C  CA  . ALA   D  1 285 ? 17.515  36.232  -33.862  1.00 38.51  ? 586  ALA   D CA  1 
ATOM   12471 C  C   . ALA   D  1 285 ? 18.295  34.938  -33.688  1.00 43.56  ? 586  ALA   D C   1 
ATOM   12472 O  O   . ALA   D  1 285 ? 18.113  34.229  -32.688  1.00 39.19  ? 586  ALA   D O   1 
ATOM   12473 C  CB  . ALA   D  1 285 ? 17.582  37.094  -32.610  1.00 36.48  ? 586  ALA   D CB  1 
ATOM   12474 N  N   . CYS   D  1 286 ? 19.162  34.629  -34.675  1.00 29.92  ? 587  CYS   D N   1 
ATOM   12475 C  CA  . CYS   D  1 286 ? 19.841  33.343  -34.745  1.00 26.58  ? 587  CYS   D CA  1 
ATOM   12476 C  C   . CYS   D  1 286 ? 21.234  33.435  -35.356  1.00 39.24  ? 587  CYS   D C   1 
ATOM   12477 O  O   . CYS   D  1 286 ? 21.522  32.693  -36.303  1.00 40.11  ? 587  CYS   D O   1 
ATOM   12478 C  CB  . CYS   D  1 286 ? 19.011  32.349  -35.565  1.00 36.31  ? 587  CYS   D CB  1 
ATOM   12479 S  SG  . CYS   D  1 286 ? 18.626  32.897  -37.292  1.00 38.89  ? 587  CYS   D SG  1 
ATOM   12480 N  N   . PRO   D  1 287 ? 22.129  34.288  -34.843  1.00 41.21  ? 588  PRO   D N   1 
ATOM   12481 C  CA  . PRO   D  1 287 ? 23.419  34.486  -35.511  1.00 31.61  ? 588  PRO   D CA  1 
ATOM   12482 C  C   . PRO   D  1 287 ? 24.176  33.185  -35.705  1.00 38.10  ? 588  PRO   D C   1 
ATOM   12483 O  O   . PRO   D  1 287 ? 24.241  32.345  -34.805  1.00 35.56  ? 588  PRO   D O   1 
ATOM   12484 C  CB  . PRO   D  1 287 ? 24.172  35.429  -34.565  1.00 32.40  ? 588  PRO   D CB  1 
ATOM   12485 C  CG  . PRO   D  1 287 ? 23.438  35.400  -33.303  1.00 39.17  ? 588  PRO   D CG  1 
ATOM   12486 C  CD  . PRO   D  1 287 ? 22.015  35.139  -33.648  1.00 44.31  ? 588  PRO   D CD  1 
ATOM   12487 N  N   . PHE   D  1 288 ? 24.761  33.032  -36.902  1.00 37.63  ? 589  PHE   D N   1 
ATOM   12488 C  CA  . PHE   D  1 288 ? 25.538  31.849  -37.246  1.00 33.02  ? 589  PHE   D CA  1 
ATOM   12489 C  C   . PHE   D  1 288 ? 26.837  32.259  -37.920  1.00 30.78  ? 589  PHE   D C   1 
ATOM   12490 O  O   . PHE   D  1 288 ? 26.969  33.350  -38.473  1.00 26.08  ? 589  PHE   D O   1 
ATOM   12491 C  CB  . PHE   D  1 288 ? 24.763  30.867  -38.136  1.00 35.09  ? 589  PHE   D CB  1 
ATOM   12492 C  CG  . PHE   D  1 288 ? 24.207  31.471  -39.412  1.00 40.69  ? 589  PHE   D CG  1 
ATOM   12493 C  CD1 . PHE   D  1 288 ? 24.991  31.558  -40.565  1.00 34.73  ? 589  PHE   D CD1 1 
ATOM   12494 C  CD2 . PHE   D  1 288 ? 22.884  31.914  -39.472  1.00 38.06  ? 589  PHE   D CD2 1 
ATOM   12495 C  CE1 . PHE   D  1 288 ? 24.462  32.087  -41.755  1.00 34.18  ? 589  PHE   D CE1 1 
ATOM   12496 C  CE2 . PHE   D  1 288 ? 22.352  32.440  -40.662  1.00 41.41  ? 589  PHE   D CE2 1 
ATOM   12497 C  CZ  . PHE   D  1 288 ? 23.146  32.521  -41.800  1.00 33.99  ? 589  PHE   D CZ  1 
ATOM   12498 N  N   . SER   D  1 289 ? 27.805  31.360  -37.865  1.00 34.78  ? 590  SER   D N   1 
ATOM   12499 C  CA  . SER   D  1 289 ? 29.134  31.707  -38.314  1.00 33.72  ? 590  SER   D CA  1 
ATOM   12500 C  C   . SER   D  1 289 ? 29.825  30.451  -38.821  1.00 34.36  ? 590  SER   D C   1 
ATOM   12501 O  O   . SER   D  1 289 ? 29.502  29.330  -38.413  1.00 35.76  ? 590  SER   D O   1 
ATOM   12502 C  CB  . SER   D  1 289 ? 29.944  32.349  -37.179  1.00 32.01  ? 590  SER   D CB  1 
ATOM   12503 O  OG  . SER   D  1 289 ? 30.094  31.412  -36.132  1.00 38.47  ? 590  SER   D OG  1 
ATOM   12504 N  N   . GLY   D  1 290 ? 30.782  30.651  -39.717  1.00 35.65  ? 591  GLY   D N   1 
ATOM   12505 C  CA  . GLY   D  1 290 ? 31.648  29.572  -40.144  1.00 32.39  ? 591  GLY   D CA  1 
ATOM   12506 C  C   . GLY   D  1 290 ? 33.034  30.128  -40.363  1.00 43.06  ? 591  GLY   D C   1 
ATOM   12507 O  O   . GLY   D  1 290 ? 33.697  30.551  -39.406  1.00 44.24  ? 591  GLY   D O   1 
ATOM   12508 N  N   . TRP   D  1 291 ? 33.468  30.145  -41.624  1.00 34.12  ? 592  TRP   D N   1 
ATOM   12509 C  CA  . TRP   D  1 291 ? 34.730  30.753  -42.002  1.00 27.21  ? 592  TRP   D CA  1 
ATOM   12510 C  C   . TRP   D  1 291 ? 34.623  31.226  -43.450  1.00 37.61  ? 592  TRP   D C   1 
ATOM   12511 O  O   . TRP   D  1 291 ? 33.786  30.750  -44.228  1.00 31.00  ? 592  TRP   D O   1 
ATOM   12512 C  CB  . TRP   D  1 291 ? 35.905  29.785  -41.809  1.00 25.34  ? 592  TRP   D CB  1 
ATOM   12513 C  CG  . TRP   D  1 291 ? 35.776  28.489  -42.539  1.00 37.05  ? 592  TRP   D CG  1 
ATOM   12514 C  CD1 . TRP   D  1 291 ? 35.985  28.275  -43.881  1.00 39.47  ? 592  TRP   D CD1 1 
ATOM   12515 C  CD2 . TRP   D  1 291 ? 35.408  27.224  -41.989  1.00 39.82  ? 592  TRP   D CD2 1 
ATOM   12516 N  NE1 . TRP   D  1 291 ? 35.760  26.960  -44.187  1.00 39.40  ? 592  TRP   D NE1 1 
ATOM   12517 C  CE2 . TRP   D  1 291 ? 35.410  26.291  -43.046  1.00 41.31  ? 592  TRP   D CE2 1 
ATOM   12518 C  CE3 . TRP   D  1 291 ? 35.081  26.784  -40.704  1.00 41.62  ? 592  TRP   D CE3 1 
ATOM   12519 C  CZ2 . TRP   D  1 291 ? 35.095  24.949  -42.855  1.00 51.87  ? 592  TRP   D CZ2 1 
ATOM   12520 C  CZ3 . TRP   D  1 291 ? 34.773  25.454  -40.517  1.00 41.70  ? 592  TRP   D CZ3 1 
ATOM   12521 C  CH2 . TRP   D  1 291 ? 34.782  24.553  -41.578  1.00 50.16  ? 592  TRP   D CH2 1 
ATOM   12522 N  N   . TYR   D  1 292 ? 35.479  32.176  -43.801  1.00 39.42  ? 593  TYR   D N   1 
ATOM   12523 C  CA  . TYR   D  1 292 ? 35.410  32.812  -45.109  1.00 38.24  ? 593  TYR   D CA  1 
ATOM   12524 C  C   . TYR   D  1 292 ? 35.930  31.930  -46.234  1.00 32.59  ? 593  TYR   D C   1 
ATOM   12525 O  O   . TYR   D  1 292 ? 36.924  31.207  -46.092  1.00 34.46  ? 593  TYR   D O   1 
ATOM   12526 C  CB  . TYR   D  1 292 ? 36.215  34.101  -45.126  1.00 31.01  ? 593  TYR   D CB  1 
ATOM   12527 C  CG  . TYR   D  1 292 ? 35.464  35.321  -44.685  1.00 41.45  ? 593  TYR   D CG  1 
ATOM   12528 C  CD1 . TYR   D  1 292 ? 34.416  35.822  -45.448  1.00 31.46  ? 593  TYR   D CD1 1 
ATOM   12529 C  CD2 . TYR   D  1 292 ? 35.826  36.003  -43.518  1.00 35.24  ? 593  TYR   D CD2 1 
ATOM   12530 C  CE1 . TYR   D  1 292 ? 33.747  36.959  -45.072  1.00 36.46  ? 593  TYR   D CE1 1 
ATOM   12531 C  CE2 . TYR   D  1 292 ? 35.153  37.146  -43.127  1.00 34.21  ? 593  TYR   D CE2 1 
ATOM   12532 C  CZ  . TYR   D  1 292 ? 34.111  37.617  -43.898  1.00 41.52  ? 593  TYR   D CZ  1 
ATOM   12533 O  OH  . TYR   D  1 292 ? 33.439  38.767  -43.540  1.00 39.65  ? 593  TYR   D OH  1 
ATOM   12534 N  N   . MET   D  1 293 ? 35.242  32.013  -47.361  1.00 35.75  ? 594  MET   D N   1 
ATOM   12535 C  CA  . MET   D  1 293 ? 35.870  31.795  -48.653  1.00 30.12  ? 594  MET   D CA  1 
ATOM   12536 C  C   . MET   D  1 293 ? 36.564  33.091  -49.057  1.00 31.28  ? 594  MET   D C   1 
ATOM   12537 O  O   . MET   D  1 293 ? 36.010  34.178  -48.885  1.00 29.16  ? 594  MET   D O   1 
ATOM   12538 C  CB  . MET   D  1 293 ? 34.818  31.379  -49.674  1.00 34.48  ? 594  MET   D CB  1 
ATOM   12539 C  CG  . MET   D  1 293 ? 35.342  31.097  -51.078  1.00 35.31  ? 594  MET   D CG  1 
ATOM   12540 S  SD  . MET   D  1 293 ? 34.048  30.254  -52.021  1.00 37.07  ? 594  MET   D SD  1 
ATOM   12541 C  CE  . MET   D  1 293 ? 33.130  31.665  -52.622  1.00 41.02  ? 594  MET   D CE  1 
ATOM   12542 N  N   . GLY   D  1 294 ? 37.789  32.979  -49.576  1.00 31.89  ? 595  GLY   D N   1 
ATOM   12543 C  CA  . GLY   D  1 294 ? 38.600  34.168  -49.831  1.00 35.37  ? 595  GLY   D CA  1 
ATOM   12544 C  C   . GLY   D  1 294 ? 37.920  35.235  -50.680  1.00 46.90  ? 595  GLY   D C   1 
ATOM   12545 O  O   . GLY   D  1 294 ? 38.086  36.432  -50.426  1.00 46.19  ? 595  GLY   D O   1 
ATOM   12546 N  N   . THR   D  1 295 ? 37.131  34.824  -51.692  1.00 39.07  ? 596  THR   D N   1 
ATOM   12547 C  CA  . THR   D  1 295 ? 36.582  35.799  -52.647  1.00 38.32  ? 596  THR   D CA  1 
ATOM   12548 C  C   . THR   D  1 295 ? 35.548  36.721  -52.015  1.00 37.80  ? 596  THR   D C   1 
ATOM   12549 O  O   . THR   D  1 295 ? 35.335  37.827  -52.521  1.00 34.18  ? 596  THR   D O   1 
ATOM   12550 C  CB  . THR   D  1 295 ? 35.929  35.115  -53.856  1.00 33.15  ? 596  THR   D CB  1 
ATOM   12551 O  OG1 . THR   D  1 295 ? 34.961  34.153  -53.413  1.00 32.81  ? 596  THR   D OG1 1 
ATOM   12552 C  CG2 . THR   D  1 295 ? 36.965  34.458  -54.752  1.00 32.36  ? 596  THR   D CG2 1 
ATOM   12553 N  N   . GLU   D  1 296 ? 34.867  36.274  -50.952  1.00 39.17  ? 597  GLU   D N   1 
ATOM   12554 C  CA  . GLU   D  1 296 ? 33.927  37.138  -50.236  1.00 33.92  ? 597  GLU   D CA  1 
ATOM   12555 C  C   . GLU   D  1 296 ? 34.595  38.439  -49.815  1.00 38.03  ? 597  GLU   D C   1 
ATOM   12556 O  O   . GLU   D  1 296 ? 34.020  39.524  -49.960  1.00 42.92  ? 597  GLU   D O   1 
ATOM   12557 C  CB  . GLU   D  1 296 ? 33.378  36.421  -48.996  1.00 40.21  ? 597  GLU   D CB  1 
ATOM   12558 C  CG  . GLU   D  1 296 ? 32.547  35.165  -49.238  1.00 42.69  ? 597  GLU   D CG  1 
ATOM   12559 C  CD  . GLU   D  1 296 ? 31.939  34.636  -47.928  1.00 40.06  ? 597  GLU   D CD  1 
ATOM   12560 O  OE1 . GLU   D  1 296 ? 30.957  35.245  -47.466  1.00 37.13  ? 597  GLU   D OE1 1 
ATOM   12561 O  OE2 . GLU   D  1 296 ? 32.450  33.644  -47.365  1.00 29.77  ? 597  GLU   D OE2 1 
ATOM   12562 N  N   . ILE   D  1 297 ? 35.802  38.335  -49.256  1.00 39.98  ? 598  ILE   D N   1 
ATOM   12563 C  CA  . ILE   D  1 297 ? 36.585  39.512  -48.893  1.00 39.74  ? 598  ILE   D CA  1 
ATOM   12564 C  C   . ILE   D  1 297 ? 37.251  40.097  -50.126  1.00 39.59  ? 598  ILE   D C   1 
ATOM   12565 O  O   . ILE   D  1 297 ? 37.119  41.289  -50.421  1.00 37.34  ? 598  ILE   D O   1 
ATOM   12566 C  CB  . ILE   D  1 297 ? 37.660  39.160  -47.839  1.00 33.44  ? 598  ILE   D CB  1 
ATOM   12567 C  CG1 . ILE   D  1 297 ? 37.101  38.392  -46.630  1.00 28.42  ? 598  ILE   D CG1 1 
ATOM   12568 C  CG2 . ILE   D  1 297 ? 38.383  40.413  -47.400  1.00 28.41  ? 598  ILE   D CG2 1 
ATOM   12569 C  CD1 . ILE   D  1 297 ? 38.163  37.589  -45.870  1.00 26.31  ? 598  ILE   D CD1 1 
ATOM   12570 N  N   . GLY   D  1 298 ? 38.021  39.259  -50.830  1.00 42.15  ? 599  GLY   D N   1 
ATOM   12571 C  CA  . GLY   D  1 298 ? 38.899  39.753  -51.876  1.00 50.19  ? 599  GLY   D CA  1 
ATOM   12572 C  C   . GLY   D  1 298 ? 38.153  40.368  -53.047  1.00 49.65  ? 599  GLY   D C   1 
ATOM   12573 O  O   . GLY   D  1 298 ? 38.536  41.431  -53.540  1.00 48.28  ? 599  GLY   D O   1 
ATOM   12574 N  N   . VAL   D  1 299 ? 37.068  39.730  -53.487  1.00 49.34  ? 600  VAL   D N   1 
ATOM   12575 C  CA  . VAL   D  1 299 ? 36.340  40.201  -54.662  1.00 48.45  ? 600  VAL   D CA  1 
ATOM   12576 C  C   . VAL   D  1 299 ? 35.251  41.186  -54.282  1.00 46.78  ? 600  VAL   D C   1 
ATOM   12577 O  O   . VAL   D  1 299 ? 35.207  42.308  -54.800  1.00 32.89  ? 600  VAL   D O   1 
ATOM   12578 C  CB  . VAL   D  1 299 ? 35.766  39.013  -55.458  1.00 41.14  ? 600  VAL   D CB  1 
ATOM   12579 C  CG1 . VAL   D  1 299 ? 35.035  39.524  -56.678  1.00 42.77  ? 600  VAL   D CG1 1 
ATOM   12580 C  CG2 . VAL   D  1 299 ? 36.868  38.058  -55.874  1.00 34.60  ? 600  VAL   D CG2 1 
ATOM   12581 N  N   . ARG   D  1 300 ? 34.371  40.791  -53.360  1.00 41.74  ? 601  ARG   D N   1 
ATOM   12582 C  CA  . ARG   D  1 300 ? 33.186  41.596  -53.067  1.00 45.03  ? 601  ARG   D CA  1 
ATOM   12583 C  C   . ARG   D  1 300 ? 33.495  42.729  -52.082  1.00 48.83  ? 601  ARG   D C   1 
ATOM   12584 O  O   . ARG   D  1 300 ? 33.281  43.907  -52.396  1.00 44.82  ? 601  ARG   D O   1 
ATOM   12585 C  CB  . ARG   D  1 300 ? 32.038  40.697  -52.549  1.00 34.13  ? 601  ARG   D CB  1 
ATOM   12586 C  CG  . ARG   D  1 300 ? 31.646  39.493  -53.462  1.00 35.12  ? 601  ARG   D CG  1 
ATOM   12587 C  CD  . ARG   D  1 300 ? 31.209  39.937  -54.902  1.00 37.02  ? 601  ARG   D CD  1 
ATOM   12588 N  NE  . ARG   D  1 300 ? 30.180  40.973  -54.839  1.00 38.80  ? 601  ARG   D NE  1 
ATOM   12589 C  CZ  . ARG   D  1 300 ? 28.901  40.726  -54.584  1.00 35.20  ? 601  ARG   D CZ  1 
ATOM   12590 N  NH1 . ARG   D  1 300 ? 28.479  39.480  -54.414  1.00 34.24  ? 601  ARG   D NH1 1 
ATOM   12591 N  NH2 . ARG   D  1 300 ? 28.040  41.722  -54.510  1.00 33.74  ? 601  ARG   D NH2 1 
ATOM   12592 N  N   . ASP   D  1 301 ? 34.011  42.392  -50.889  1.00 47.90  ? 602  ASP   D N   1 
ATOM   12593 C  CA  . ASP   D  1 301 ? 34.262  43.405  -49.854  1.00 49.96  ? 602  ASP   D CA  1 
ATOM   12594 C  C   . ASP   D  1 301 ? 35.227  44.485  -50.325  1.00 48.70  ? 602  ASP   D C   1 
ATOM   12595 O  O   . ASP   D  1 301 ? 34.962  45.683  -50.157  1.00 44.99  ? 602  ASP   D O   1 
ATOM   12596 C  CB  . ASP   D  1 301 ? 34.792  42.749  -48.577  1.00 39.00  ? 602  ASP   D CB  1 
ATOM   12597 C  CG  . ASP   D  1 301 ? 33.725  41.958  -47.868  1.00 43.12  ? 602  ASP   D CG  1 
ATOM   12598 O  OD1 . ASP   D  1 301 ? 32.557  42.387  -47.940  1.00 42.57  ? 602  ASP   D OD1 1 
ATOM   12599 O  OD2 . ASP   D  1 301 ? 34.040  40.900  -47.284  1.00 45.59  ? 602  ASP   D OD2 1 
ATOM   12600 N  N   . TYR   D  1 302 ? 36.350  44.084  -50.919  1.00 51.86  ? 603  TYR   D N   1 
ATOM   12601 C  CA  . TYR   D  1 302 ? 37.365  45.057  -51.300  1.00 55.39  ? 603  TYR   D CA  1 
ATOM   12602 C  C   . TYR   D  1 302 ? 37.111  45.721  -52.645  1.00 48.58  ? 603  TYR   D C   1 
ATOM   12603 O  O   . TYR   D  1 302 ? 37.498  46.880  -52.823  1.00 51.64  ? 603  TYR   D O   1 
ATOM   12604 C  CB  . TYR   D  1 302 ? 38.744  44.403  -51.326  1.00 56.65  ? 603  TYR   D CB  1 
ATOM   12605 C  CG  . TYR   D  1 302 ? 39.329  44.191  -49.958  1.00 46.61  ? 603  TYR   D CG  1 
ATOM   12606 C  CD1 . TYR   D  1 302 ? 38.667  44.644  -48.831  1.00 44.20  ? 603  TYR   D CD1 1 
ATOM   12607 C  CD2 . TYR   D  1 302 ? 40.542  43.543  -49.797  1.00 42.17  ? 603  TYR   D CD2 1 
ATOM   12608 C  CE1 . TYR   D  1 302 ? 39.201  44.451  -47.571  1.00 51.21  ? 603  TYR   D CE1 1 
ATOM   12609 C  CE2 . TYR   D  1 302 ? 41.083  43.343  -48.552  1.00 51.40  ? 603  TYR   D CE2 1 
ATOM   12610 C  CZ  . TYR   D  1 302 ? 40.411  43.798  -47.436  1.00 52.09  ? 603  TYR   D CZ  1 
ATOM   12611 O  OH  . TYR   D  1 302 ? 40.959  43.608  -46.189  1.00 51.21  ? 603  TYR   D OH  1 
ATOM   12612 N  N   . CYS   D  1 303 ? 36.482  45.029  -53.604  1.00 52.82  ? 604  CYS   D N   1 
ATOM   12613 C  CA  . CYS   D  1 303 ? 36.477  45.512  -54.981  1.00 51.96  ? 604  CYS   D CA  1 
ATOM   12614 C  C   . CYS   D  1 303 ? 35.111  45.888  -55.548  1.00 49.81  ? 604  CYS   D C   1 
ATOM   12615 O  O   . CYS   D  1 303 ? 35.068  46.495  -56.624  1.00 53.08  ? 604  CYS   D O   1 
ATOM   12616 C  CB  . CYS   D  1 303 ? 37.140  44.484  -55.916  1.00 51.07  ? 604  CYS   D CB  1 
ATOM   12617 S  SG  . CYS   D  1 303 ? 38.919  44.229  -55.595  1.00 48.16  ? 604  CYS   D SG  1 
ATOM   12618 N  N   . ASP   D  1 304 ? 34.004  45.567  -54.880  1.00 49.70  ? 605  ASP   D N   1 
ATOM   12619 C  CA  . ASP   D  1 304 ? 32.720  46.109  -55.311  1.00 49.35  ? 605  ASP   D CA  1 
ATOM   12620 C  C   . ASP   D  1 304 ? 32.774  47.633  -55.306  1.00 52.90  ? 605  ASP   D C   1 
ATOM   12621 O  O   . ASP   D  1 304 ? 33.253  48.243  -54.340  1.00 56.49  ? 605  ASP   D O   1 
ATOM   12622 C  CB  . ASP   D  1 304 ? 31.589  45.622  -54.404  1.00 46.86  ? 605  ASP   D CB  1 
ATOM   12623 C  CG  . ASP   D  1 304 ? 31.049  44.264  -54.802  1.00 51.16  ? 605  ASP   D CG  1 
ATOM   12624 O  OD1 . ASP   D  1 304 ? 31.688  43.563  -55.621  1.00 52.58  ? 605  ASP   D OD1 1 
ATOM   12625 O  OD2 . ASP   D  1 304 ? 29.967  43.906  -54.292  1.00 50.79  ? 605  ASP   D OD2 1 
ATOM   12626 N  N   . ASN   D  1 305 ? 32.291  48.247  -56.397  1.00 50.91  ? 606  ASN   D N   1 
ATOM   12627 C  CA  . ASN   D  1 305 ? 32.269  49.708  -56.488  1.00 52.93  ? 606  ASN   D CA  1 
ATOM   12628 C  C   . ASN   D  1 305 ? 31.543  50.337  -55.295  1.00 53.25  ? 606  ASN   D C   1 
ATOM   12629 O  O   . ASN   D  1 305 ? 31.948  51.397  -54.802  1.00 50.79  ? 606  ASN   D O   1 
ATOM   12630 C  CB  . ASN   D  1 305 ? 31.617  50.151  -57.804  1.00 63.79  ? 606  ASN   D CB  1 
ATOM   12631 C  CG  . ASN   D  1 305 ? 32.514  49.916  -59.034  1.00 70.62  ? 606  ASN   D CG  1 
ATOM   12632 O  OD1 . ASN   D  1 305 ? 33.719  50.192  -59.015  1.00 69.70  ? 606  ASN   D OD1 1 
ATOM   12633 N  ND2 . ASN   D  1 305 ? 31.911  49.412  -60.114  1.00 70.20  ? 606  ASN   D ND2 1 
ATOM   12634 N  N   . SER   D  1 306 ? 30.475  49.693  -54.807  1.00 48.96  ? 607  SER   D N   1 
ATOM   12635 C  CA  . SER   D  1 306 ? 29.743  50.179  -53.644  1.00 53.42  ? 607  SER   D CA  1 
ATOM   12636 C  C   . SER   D  1 306 ? 30.422  49.844  -52.320  1.00 54.96  ? 607  SER   D C   1 
ATOM   12637 O  O   . SER   D  1 306 ? 29.895  50.222  -51.271  1.00 49.19  ? 607  SER   D O   1 
ATOM   12638 C  CB  . SER   D  1 306 ? 28.318  49.614  -53.623  1.00 58.62  ? 607  SER   D CB  1 
ATOM   12639 O  OG  . SER   D  1 306 ? 27.490  50.226  -54.602  1.00 71.12  ? 607  SER   D OG  1 
ATOM   12640 N  N   . ARG   D  1 307 ? 31.557  49.144  -52.333  1.00 55.36  ? 608  ARG   D N   1 
ATOM   12641 C  CA  . ARG   D  1 307 ? 32.204  48.732  -51.091  1.00 57.56  ? 608  ARG   D CA  1 
ATOM   12642 C  C   . ARG   D  1 307 ? 33.543  49.441  -50.915  1.00 57.89  ? 608  ARG   D C   1 
ATOM   12643 O  O   . ARG   D  1 307 ? 33.610  50.670  -51.058  1.00 62.16  ? 608  ARG   D O   1 
ATOM   12644 C  CB  . ARG   D  1 307 ? 32.356  47.216  -51.062  1.00 56.71  ? 608  ARG   D CB  1 
ATOM   12645 C  CG  . ARG   D  1 307 ? 31.013  46.502  -51.115  1.00 56.60  ? 608  ARG   D CG  1 
ATOM   12646 C  CD  . ARG   D  1 307 ? 30.155  46.794  -49.871  1.00 60.48  ? 608  ARG   D CD  1 
ATOM   12647 N  NE  . ARG   D  1 307 ? 30.823  46.403  -48.634  1.00 54.89  ? 608  ARG   D NE  1 
ATOM   12648 C  CZ  . ARG   D  1 307 ? 30.977  45.144  -48.235  1.00 51.65  ? 608  ARG   D CZ  1 
ATOM   12649 N  NH1 . ARG   D  1 307 ? 30.517  44.143  -48.974  1.00 41.95  ? 608  ARG   D NH1 1 
ATOM   12650 N  NH2 . ARG   D  1 307 ? 31.604  44.884  -47.099  1.00 48.51  ? 608  ARG   D NH2 1 
ATOM   12651 N  N   . TYR   D  1 308 ? 34.618  48.704  -50.613  1.00 48.30  ? 609  TYR   D N   1 
ATOM   12652 C  CA  . TYR   D  1 308 ? 35.879  49.387  -50.329  1.00 45.82  ? 609  TYR   D CA  1 
ATOM   12653 C  C   . TYR   D  1 308 ? 36.568  49.886  -51.588  1.00 50.26  ? 609  TYR   D C   1 
ATOM   12654 O  O   . TYR   D  1 308 ? 37.444  50.757  -51.489  1.00 49.68  ? 609  TYR   D O   1 
ATOM   12655 C  CB  . TYR   D  1 308 ? 36.821  48.486  -49.526  1.00 49.33  ? 609  TYR   D CB  1 
ATOM   12656 C  CG  . TYR   D  1 308 ? 36.594  48.612  -48.027  1.00 54.48  ? 609  TYR   D CG  1 
ATOM   12657 C  CD1 . TYR   D  1 308 ? 35.660  47.809  -47.369  1.00 49.48  ? 609  TYR   D CD1 1 
ATOM   12658 C  CD2 . TYR   D  1 308 ? 37.297  49.555  -47.275  1.00 54.94  ? 609  TYR   D CD2 1 
ATOM   12659 C  CE1 . TYR   D  1 308 ? 35.441  47.935  -45.989  1.00 52.00  ? 609  TYR   D CE1 1 
ATOM   12660 C  CE2 . TYR   D  1 308 ? 37.088  49.689  -45.910  1.00 50.15  ? 609  TYR   D CE2 1 
ATOM   12661 C  CZ  . TYR   D  1 308 ? 36.160  48.880  -45.272  1.00 57.97  ? 609  TYR   D CZ  1 
ATOM   12662 O  OH  . TYR   D  1 308 ? 35.962  49.016  -43.911  1.00 64.21  ? 609  TYR   D OH  1 
ATOM   12663 N  N   . ASN   D  1 309 ? 36.196  49.345  -52.751  1.00 48.92  ? 610  ASN   D N   1 
ATOM   12664 C  CA  . ASN   D  1 309 ? 36.546  49.868  -54.077  1.00 50.16  ? 610  ASN   D CA  1 
ATOM   12665 C  C   . ASN   D  1 309 ? 38.032  50.230  -54.196  1.00 53.37  ? 610  ASN   D C   1 
ATOM   12666 O  O   . ASN   D  1 309 ? 38.412  51.348  -54.555  1.00 52.31  ? 610  ASN   D O   1 
ATOM   12667 C  CB  . ASN   D  1 309 ? 35.651  51.055  -54.437  1.00 46.75  ? 610  ASN   D CB  1 
ATOM   12668 C  CG  . ASN   D  1 309 ? 35.816  51.482  -55.887  1.00 43.44  ? 610  ASN   D CG  1 
ATOM   12669 O  OD1 . ASN   D  1 309 ? 36.083  50.653  -56.754  1.00 52.50  ? 610  ASN   D OD1 1 
ATOM   12670 N  ND2 . ASN   D  1 309 ? 35.694  52.772  -56.147  1.00 35.85  ? 610  ASN   D ND2 1 
ATOM   12671 N  N   . ILE   D  1 310 ? 38.879  49.240  -53.911  1.00 57.33  ? 611  ILE   D N   1 
ATOM   12672 C  CA  . ILE   D  1 310 ? 40.326  49.441  -53.889  1.00 58.97  ? 611  ILE   D CA  1 
ATOM   12673 C  C   . ILE   D  1 310 ? 40.973  49.041  -55.205  1.00 55.27  ? 611  ILE   D C   1 
ATOM   12674 O  O   . ILE   D  1 310 ? 42.205  48.966  -55.287  1.00 54.54  ? 611  ILE   D O   1 
ATOM   12675 C  CB  . ILE   D  1 310 ? 40.976  48.656  -52.743  1.00 56.10  ? 611  ILE   D CB  1 
ATOM   12676 C  CG1 . ILE   D  1 310 ? 40.788  47.158  -52.992  1.00 58.47  ? 611  ILE   D CG1 1 
ATOM   12677 C  CG2 . ILE   D  1 310 ? 40.375  49.065  -51.404  1.00 54.93  ? 611  ILE   D CG2 1 
ATOM   12678 C  CD1 . ILE   D  1 310 ? 41.866  46.289  -52.394  1.00 61.09  ? 611  ILE   D CD1 1 
ATOM   12679 N  N   . LEU   D  1 311 ? 40.174  48.745  -56.232  1.00 52.73  ? 612  LEU   D N   1 
ATOM   12680 C  CA  . LEU   D  1 311 ? 40.759  48.333  -57.504  1.00 51.10  ? 612  LEU   D CA  1 
ATOM   12681 C  C   . LEU   D  1 311 ? 41.720  49.389  -58.042  1.00 47.02  ? 612  LEU   D C   1 
ATOM   12682 O  O   . LEU   D  1 311 ? 42.874  49.079  -58.347  1.00 52.81  ? 612  LEU   D O   1 
ATOM   12683 C  CB  . LEU   D  1 311 ? 39.669  48.021  -58.525  1.00 45.77  ? 612  LEU   D CB  1 
ATOM   12684 C  CG  . LEU   D  1 311 ? 39.202  46.572  -58.486  1.00 37.07  ? 612  LEU   D CG  1 
ATOM   12685 C  CD1 . LEU   D  1 311 ? 38.124  46.316  -59.530  1.00 36.08  ? 612  LEU   D CD1 1 
ATOM   12686 C  CD2 . LEU   D  1 311 ? 40.356  45.598  -58.637  1.00 31.61  ? 612  LEU   D CD2 1 
ATOM   12687 N  N   . GLU   D  1 312 ? 41.279  50.651  -58.123  1.00 47.77  ? 613  GLU   D N   1 
ATOM   12688 C  CA  . GLU   D  1 312 ? 42.124  51.691  -58.719  1.00 58.68  ? 613  GLU   D CA  1 
ATOM   12689 C  C   . GLU   D  1 312 ? 43.460  51.824  -57.996  1.00 58.86  ? 613  GLU   D C   1 
ATOM   12690 O  O   . GLU   D  1 312 ? 44.510  51.959  -58.635  1.00 63.67  ? 613  GLU   D O   1 
ATOM   12691 C  CB  . GLU   D  1 312 ? 41.407  53.041  -58.715  1.00 73.58  ? 613  GLU   D CB  1 
ATOM   12692 C  CG  . GLU   D  1 312 ? 40.670  53.375  -59.989  1.00 84.86  ? 613  GLU   D CG  1 
ATOM   12693 C  CD  . GLU   D  1 312 ? 40.410  54.862  -60.132  1.00 94.28  ? 613  GLU   D CD  1 
ATOM   12694 O  OE1 . GLU   D  1 312 ? 41.357  55.658  -59.930  1.00 88.88  ? 613  GLU   D OE1 1 
ATOM   12695 O  OE2 . GLU   D  1 312 ? 39.257  55.229  -60.447  1.00 102.54 ? 613  GLU   D OE2 1 
ATOM   12696 N  N   . GLU   D  1 313 ? 43.440  51.804  -56.664  1.00 55.68  ? 614  GLU   D N   1 
ATOM   12697 C  CA  . GLU   D  1 313 ? 44.676  52.023  -55.921  1.00 61.74  ? 614  GLU   D CA  1 
ATOM   12698 C  C   . GLU   D  1 313 ? 45.654  50.880  -56.136  1.00 56.23  ? 614  GLU   D C   1 
ATOM   12699 O  O   . GLU   D  1 313 ? 46.860  51.108  -56.275  1.00 62.08  ? 614  GLU   D O   1 
ATOM   12700 C  CB  . GLU   D  1 313 ? 44.379  52.204  -54.427  1.00 60.14  ? 614  GLU   D CB  1 
ATOM   12701 C  CG  . GLU   D  1 313 ? 45.608  52.541  -53.599  1.00 71.06  ? 614  GLU   D CG  1 
ATOM   12702 C  CD  . GLU   D  1 313 ? 45.265  52.845  -52.151  1.00 85.59  ? 614  GLU   D CD  1 
ATOM   12703 O  OE1 . GLU   D  1 313 ? 46.198  53.026  -51.337  1.00 89.49  ? 614  GLU   D OE1 1 
ATOM   12704 O  OE2 . GLU   D  1 313 ? 44.059  52.907  -51.826  1.00 88.23  ? 614  GLU   D OE2 1 
ATOM   12705 N  N   . VAL   D  1 314 ? 45.155  49.646  -56.161  1.00 53.62  ? 615  VAL   D N   1 
ATOM   12706 C  CA  . VAL   D  1 314 ? 46.037  48.498  -56.324  1.00 48.01  ? 615  VAL   D CA  1 
ATOM   12707 C  C   . VAL   D  1 314 ? 46.628  48.486  -57.721  1.00 49.73  ? 615  VAL   D C   1 
ATOM   12708 O  O   . VAL   D  1 314 ? 47.824  48.229  -57.903  1.00 52.21  ? 615  VAL   D O   1 
ATOM   12709 C  CB  . VAL   D  1 314 ? 45.275  47.198  -56.016  1.00 46.60  ? 615  VAL   D CB  1 
ATOM   12710 C  CG1 . VAL   D  1 314 ? 46.137  45.978  -56.339  1.00 37.70  ? 615  VAL   D CG1 1 
ATOM   12711 C  CG2 . VAL   D  1 314 ? 44.843  47.179  -54.537  1.00 54.04  ? 615  VAL   D CG2 1 
ATOM   12712 N  N   . ALA   D  1 315 ? 45.799  48.768  -58.728  1.00 48.75  ? 616  ALA   D N   1 
ATOM   12713 C  CA  . ALA   D  1 315 ? 46.285  48.830  -60.098  1.00 47.25  ? 616  ALA   D CA  1 
ATOM   12714 C  C   . ALA   D  1 315 ? 47.337  49.918  -60.252  1.00 56.25  ? 616  ALA   D C   1 
ATOM   12715 O  O   . ALA   D  1 315 ? 48.355  49.711  -60.917  1.00 54.52  ? 616  ALA   D O   1 
ATOM   12716 C  CB  . ALA   D  1 315 ? 45.109  49.049  -61.049  1.00 44.05  ? 616  ALA   D CB  1 
ATOM   12717 N  N   . LYS   D  1 316 ? 47.129  51.077  -59.614  1.00 59.80  ? 617  LYS   D N   1 
ATOM   12718 C  CA  . LYS   D  1 316 ? 48.111  52.152  -59.732  1.00 61.06  ? 617  LYS   D CA  1 
ATOM   12719 C  C   . LYS   D  1 316 ? 49.450  51.719  -59.154  1.00 57.67  ? 617  LYS   D C   1 
ATOM   12720 O  O   . LYS   D  1 316 ? 50.482  51.795  -59.828  1.00 52.82  ? 617  LYS   D O   1 
ATOM   12721 C  CB  . LYS   D  1 316 ? 47.604  53.425  -59.053  1.00 63.82  ? 617  LYS   D CB  1 
ATOM   12722 C  CG  . LYS   D  1 316 ? 46.547  54.180  -59.843  1.00 73.09  ? 617  LYS   D CG  1 
ATOM   12723 C  CD  . LYS   D  1 316 ? 46.010  55.363  -59.058  1.00 82.33  ? 617  LYS   D CD  1 
ATOM   12724 C  CE  . LYS   D  1 316 ? 44.979  56.152  -59.853  1.00 85.80  ? 617  LYS   D CE  1 
ATOM   12725 N  NZ  . LYS   D  1 316 ? 44.357  57.203  -58.997  1.00 89.20  ? 617  LYS   D NZ  1 
ATOM   12726 N  N   . LYS   D  1 317 ? 49.448  51.228  -57.913  1.00 61.02  ? 618  LYS   D N   1 
ATOM   12727 C  CA  . LYS   D  1 317 ? 50.671  50.667  -57.352  1.00 63.01  ? 618  LYS   D CA  1 
ATOM   12728 C  C   . LYS   D  1 317 ? 51.243  49.560  -58.229  1.00 64.05  ? 618  LYS   D C   1 
ATOM   12729 O  O   . LYS   D  1 317 ? 52.446  49.288  -58.156  1.00 68.74  ? 618  LYS   D O   1 
ATOM   12730 C  CB  . LYS   D  1 317 ? 50.420  50.136  -55.934  1.00 63.77  ? 618  LYS   D CB  1 
ATOM   12731 C  CG  . LYS   D  1 317 ? 50.172  51.221  -54.881  1.00 67.36  ? 618  LYS   D CG  1 
ATOM   12732 C  CD  . LYS   D  1 317 ? 51.045  51.007  -53.658  1.00 70.28  ? 618  LYS   D CD  1 
ATOM   12733 C  CE  . LYS   D  1 317 ? 52.081  52.103  -53.510  1.00 77.61  ? 618  LYS   D CE  1 
ATOM   12734 N  NZ  . LYS   D  1 317 ? 51.429  53.411  -53.230  1.00 83.30  ? 618  LYS   D NZ  1 
ATOM   12735 N  N   . MET   D  1 318 ? 50.419  48.922  -59.061  1.00 54.70  ? 619  MET   D N   1 
ATOM   12736 C  CA  . MET   D  1 318 ? 50.898  47.858  -59.932  1.00 46.97  ? 619  MET   D CA  1 
ATOM   12737 C  C   . MET   D  1 318 ? 51.424  48.378  -61.261  1.00 53.85  ? 619  MET   D C   1 
ATOM   12738 O  O   . MET   D  1 318 ? 51.924  47.580  -62.061  1.00 54.95  ? 619  MET   D O   1 
ATOM   12739 C  CB  . MET   D  1 318 ? 49.790  46.827  -60.186  1.00 44.64  ? 619  MET   D CB  1 
ATOM   12740 C  CG  . MET   D  1 318 ? 49.604  45.830  -59.050  1.00 43.18  ? 619  MET   D CG  1 
ATOM   12741 S  SD  . MET   D  1 318 ? 48.289  44.631  -59.323  1.00 49.91  ? 619  MET   D SD  1 
ATOM   12742 C  CE  . MET   D  1 318 ? 48.901  43.852  -60.835  1.00 47.81  ? 619  MET   D CE  1 
ATOM   12743 N  N   . ASN   D  1 319 ? 51.326  49.686  -61.506  1.00 57.94  ? 620  ASN   D N   1 
ATOM   12744 C  CA  . ASN   D  1 319 ? 51.748  50.302  -62.768  1.00 66.69  ? 620  ASN   D CA  1 
ATOM   12745 C  C   . ASN   D  1 319 ? 51.000  49.743  -63.977  1.00 58.75  ? 620  ASN   D C   1 
ATOM   12746 O  O   . ASN   D  1 319 ? 51.574  49.587  -65.054  1.00 62.38  ? 620  ASN   D O   1 
ATOM   12747 C  CB  . ASN   D  1 319 ? 53.254  50.161  -62.972  1.00 74.53  ? 620  ASN   D CB  1 
ATOM   12748 C  CG  . ASN   D  1 319 ? 53.994  51.399  -62.572  1.00 83.79  ? 620  ASN   D CG  1 
ATOM   12749 O  OD1 . ASN   D  1 319 ? 54.198  52.304  -63.393  1.00 90.93  ? 620  ASN   D OD1 1 
ATOM   12750 N  ND2 . ASN   D  1 319 ? 54.388  51.469  -61.298  1.00 75.95  ? 620  ASN   D ND2 1 
ATOM   12751 N  N   . LEU   D  1 320 ? 49.721  49.430  -63.814  1.00 56.90  ? 621  LEU   D N   1 
ATOM   12752 C  CA  . LEU   D  1 320 ? 48.944  48.894  -64.915  1.00 58.36  ? 621  LEU   D CA  1 
ATOM   12753 C  C   . LEU   D  1 320 ? 48.423  50.034  -65.790  1.00 62.16  ? 621  LEU   D C   1 
ATOM   12754 O  O   . LEU   D  1 320 ? 48.298  51.181  -65.348  1.00 60.82  ? 621  LEU   D O   1 
ATOM   12755 C  CB  . LEU   D  1 320 ? 47.796  48.043  -64.374  1.00 58.77  ? 621  LEU   D CB  1 
ATOM   12756 C  CG  . LEU   D  1 320 ? 48.232  46.912  -63.436  1.00 52.93  ? 621  LEU   D CG  1 
ATOM   12757 C  CD1 . LEU   D  1 320 ? 47.029  46.112  -62.978  1.00 46.93  ? 621  LEU   D CD1 1 
ATOM   12758 C  CD2 . LEU   D  1 320 ? 49.239  46.000  -64.117  1.00 54.62  ? 621  LEU   D CD2 1 
ATOM   12759 N  N   . ASP   D  1 321 ? 48.153  49.715  -67.059  1.00 65.26  ? 622  ASP   D N   1 
ATOM   12760 C  CA  . ASP   D  1 321 ? 47.575  50.692  -67.981  1.00 63.14  ? 622  ASP   D CA  1 
ATOM   12761 C  C   . ASP   D  1 321 ? 46.088  50.769  -67.708  1.00 61.51  ? 622  ASP   D C   1 
ATOM   12762 O  O   . ASP   D  1 321 ? 45.329  49.878  -68.094  1.00 67.81  ? 622  ASP   D O   1 
ATOM   12763 C  CB  . ASP   D  1 321 ? 47.826  50.313  -69.434  1.00 75.28  ? 622  ASP   D CB  1 
ATOM   12764 C  CG  . ASP   D  1 321 ? 47.073  51.218  -70.407  1.00 82.96  ? 622  ASP   D CG  1 
ATOM   12765 O  OD1 . ASP   D  1 321 ? 46.782  52.379  -70.036  1.00 75.18  ? 622  ASP   D OD1 1 
ATOM   12766 O  OD2 . ASP   D  1 321 ? 46.759  50.764  -71.533  1.00 91.17  ? 622  ASP   D OD2 1 
ATOM   12767 N  N   . MET   D  1 322 ? 45.657  51.835  -67.046  1.00 61.29  ? 623  MET   D N   1 
ATOM   12768 C  CA  . MET   D  1 322 ? 44.255  51.973  -66.693  1.00 65.14  ? 623  MET   D CA  1 
ATOM   12769 C  C   . MET   D  1 322 ? 43.491  52.843  -67.682  1.00 72.63  ? 623  MET   D C   1 
ATOM   12770 O  O   . MET   D  1 322 ? 42.378  53.289  -67.377  1.00 76.38  ? 623  MET   D O   1 
ATOM   12771 C  CB  . MET   D  1 322 ? 44.133  52.513  -65.277  1.00 56.93  ? 623  MET   D CB  1 
ATOM   12772 C  CG  . MET   D  1 322 ? 44.757  51.577  -64.265  1.00 63.76  ? 623  MET   D CG  1 
ATOM   12773 S  SD  . MET   D  1 322 ? 44.927  52.297  -62.633  1.00 69.45  ? 623  MET   D SD  1 
ATOM   12774 C  CE  . MET   D  1 322 ? 43.273  52.911  -62.365  1.00 69.57  ? 623  MET   D CE  1 
ATOM   12775 N  N   . ARG   D  1 323 ? 44.060  53.073  -68.868  1.00 70.68  ? 624  ARG   D N   1 
ATOM   12776 C  CA  . ARG   D  1 323 ? 43.402  53.918  -69.855  1.00 79.66  ? 624  ARG   D CA  1 
ATOM   12777 C  C   . ARG   D  1 323 ? 42.324  53.163  -70.625  1.00 80.65  ? 624  ARG   D C   1 
ATOM   12778 O  O   . ARG   D  1 323 ? 41.298  53.749  -70.985  1.00 93.45  ? 624  ARG   D O   1 
ATOM   12779 C  CB  . ARG   D  1 323 ? 44.432  54.507  -70.816  1.00 85.96  ? 624  ARG   D CB  1 
ATOM   12780 C  CG  . ARG   D  1 323 ? 45.281  55.616  -70.216  1.00 89.88  ? 624  ARG   D CG  1 
ATOM   12781 C  CD  . ARG   D  1 323 ? 46.405  55.984  -71.168  1.00 97.40  ? 624  ARG   D CD  1 
ATOM   12782 N  NE  . ARG   D  1 323 ? 47.070  54.779  -71.655  1.00 103.15 ? 624  ARG   D NE  1 
ATOM   12783 C  CZ  . ARG   D  1 323 ? 47.984  54.753  -72.620  1.00 105.90 ? 624  ARG   D CZ  1 
ATOM   12784 N  NH1 . ARG   D  1 323 ? 48.362  55.877  -73.220  1.00 108.14 ? 624  ARG   D NH1 1 
ATOM   12785 N  NH2 . ARG   D  1 323 ? 48.518  53.592  -72.983  1.00 103.42 ? 624  ARG   D NH2 1 
ATOM   12786 N  N   . LYS   D  1 324 ? 42.518  51.875  -70.886  1.00 71.60  ? 625  LYS   D N   1 
ATOM   12787 C  CA  . LYS   D  1 324 ? 41.532  51.104  -71.632  1.00 71.28  ? 625  LYS   D CA  1 
ATOM   12788 C  C   . LYS   D  1 324 ? 41.143  49.859  -70.850  1.00 65.53  ? 625  LYS   D C   1 
ATOM   12789 O  O   . LYS   D  1 324 ? 42.003  49.182  -70.280  1.00 69.74  ? 625  LYS   D O   1 
ATOM   12790 C  CB  . LYS   D  1 324 ? 42.060  50.720  -73.025  1.00 70.75  ? 625  LYS   D CB  1 
ATOM   12791 C  CG  . LYS   D  1 324 ? 43.338  49.900  -73.005  1.00 76.55  ? 625  LYS   D CG  1 
ATOM   12792 C  CD  . LYS   D  1 324 ? 44.351  50.419  -74.006  1.00 81.23  ? 625  LYS   D CD  1 
ATOM   12793 C  CE  . LYS   D  1 324 ? 45.531  49.472  -74.114  1.00 83.42  ? 625  LYS   D CE  1 
ATOM   12794 N  NZ  . LYS   D  1 324 ? 45.144  48.176  -74.735  1.00 83.21  ? 625  LYS   D NZ  1 
ATOM   12795 N  N   . THR   D  1 325 ? 39.836  49.567  -70.834  1.00 59.17  ? 626  THR   D N   1 
ATOM   12796 C  CA  . THR   D  1 325 ? 39.338  48.375  -70.149  1.00 52.61  ? 626  THR   D CA  1 
ATOM   12797 C  C   . THR   D  1 325 ? 39.983  47.110  -70.701  1.00 52.95  ? 626  THR   D C   1 
ATOM   12798 O  O   . THR   D  1 325 ? 40.253  46.165  -69.948  1.00 41.55  ? 626  THR   D O   1 
ATOM   12799 C  CB  . THR   D  1 325 ? 37.814  48.278  -70.280  1.00 54.03  ? 626  THR   D CB  1 
ATOM   12800 O  OG1 . THR   D  1 325 ? 37.459  48.117  -71.663  1.00 64.45  ? 626  THR   D OG1 1 
ATOM   12801 C  CG2 . THR   D  1 325 ? 37.149  49.524  -69.755  1.00 50.60  ? 626  THR   D CG2 1 
ATOM   12802 N  N   . SER   D  1 326 ? 40.225  47.071  -72.022  1.00 50.45  ? 627  SER   D N   1 
ATOM   12803 C  CA  . SER   D  1 326 ? 40.735  45.862  -72.657  1.00 53.19  ? 627  SER   D CA  1 
ATOM   12804 C  C   . SER   D  1 326 ? 42.154  45.521  -72.221  1.00 52.98  ? 627  SER   D C   1 
ATOM   12805 O  O   . SER   D  1 326 ? 42.653  44.453  -72.589  1.00 61.09  ? 627  SER   D O   1 
ATOM   12806 C  CB  . SER   D  1 326 ? 40.663  45.981  -74.190  1.00 51.84  ? 627  SER   D CB  1 
ATOM   12807 O  OG  . SER   D  1 326 ? 40.962  47.296  -74.626  1.00 62.97  ? 627  SER   D OG  1 
ATOM   12808 N  N   . SER   D  1 327 ? 42.819  46.391  -71.462  1.00 41.66  ? 628  SER   D N   1 
ATOM   12809 C  CA  . SER   D  1 327 ? 44.059  45.980  -70.815  1.00 51.42  ? 628  SER   D CA  1 
ATOM   12810 C  C   . SER   D  1 327 ? 43.811  44.973  -69.693  1.00 46.93  ? 628  SER   D C   1 
ATOM   12811 O  O   . SER   D  1 327 ? 44.758  44.321  -69.250  1.00 48.44  ? 628  SER   D O   1 
ATOM   12812 C  CB  . SER   D  1 327 ? 44.796  47.196  -70.255  1.00 58.23  ? 628  SER   D CB  1 
ATOM   12813 O  OG  . SER   D  1 327 ? 44.311  47.519  -68.963  1.00 61.88  ? 628  SER   D OG  1 
ATOM   12814 N  N   . LEU   D  1 328 ? 42.562  44.832  -69.244  1.00 39.97  ? 629  LEU   D N   1 
ATOM   12815 C  CA  . LEU   D  1 328 ? 42.179  43.939  -68.138  1.00 45.92  ? 629  LEU   D CA  1 
ATOM   12816 C  C   . LEU   D  1 328 ? 42.920  44.254  -66.834  1.00 49.06  ? 629  LEU   D C   1 
ATOM   12817 O  O   . LEU   D  1 328 ? 43.232  43.359  -66.046  1.00 51.36  ? 629  LEU   D O   1 
ATOM   12818 C  CB  . LEU   D  1 328 ? 42.357  42.463  -68.515  1.00 43.43  ? 629  LEU   D CB  1 
ATOM   12819 C  CG  . LEU   D  1 328 ? 41.520  42.004  -69.719  1.00 45.53  ? 629  LEU   D CG  1 
ATOM   12820 C  CD1 . LEU   D  1 328 ? 41.386  40.495  -69.749  1.00 40.17  ? 629  LEU   D CD1 1 
ATOM   12821 C  CD2 . LEU   D  1 328 ? 40.155  42.673  -69.721  1.00 36.90  ? 629  LEU   D CD2 1 
ATOM   12822 N  N   . TRP   D  1 329 ? 43.183  45.536  -66.583  1.00 55.49  ? 630  TRP   D N   1 
ATOM   12823 C  CA  . TRP   D  1 329 ? 43.847  45.906  -65.334  1.00 53.83  ? 630  TRP   D CA  1 
ATOM   12824 C  C   . TRP   D  1 329 ? 42.992  45.554  -64.120  1.00 56.01  ? 630  TRP   D C   1 
ATOM   12825 O  O   . TRP   D  1 329 ? 43.514  45.079  -63.103  1.00 59.42  ? 630  TRP   D O   1 
ATOM   12826 C  CB  . TRP   D  1 329 ? 44.200  47.395  -65.339  1.00 52.14  ? 630  TRP   D CB  1 
ATOM   12827 C  CG  . TRP   D  1 329 ? 43.037  48.348  -65.452  1.00 50.75  ? 630  TRP   D CG  1 
ATOM   12828 C  CD1 . TRP   D  1 329 ? 42.503  48.860  -66.599  1.00 53.39  ? 630  TRP   D CD1 1 
ATOM   12829 C  CD2 . TRP   D  1 329 ? 42.295  48.934  -64.371  1.00 51.06  ? 630  TRP   D CD2 1 
ATOM   12830 N  NE1 . TRP   D  1 329 ? 41.462  49.714  -66.302  1.00 49.92  ? 630  TRP   D NE1 1 
ATOM   12831 C  CE2 . TRP   D  1 329 ? 41.316  49.774  -64.941  1.00 55.77  ? 630  TRP   D CE2 1 
ATOM   12832 C  CE3 . TRP   D  1 329 ? 42.350  48.815  -62.977  1.00 56.53  ? 630  TRP   D CE3 1 
ATOM   12833 C  CZ2 . TRP   D  1 329 ? 40.407  50.497  -64.163  1.00 50.27  ? 630  TRP   D CZ2 1 
ATOM   12834 C  CZ3 . TRP   D  1 329 ? 41.448  49.531  -62.210  1.00 53.37  ? 630  TRP   D CZ3 1 
ATOM   12835 C  CH2 . TRP   D  1 329 ? 40.488  50.358  -62.807  1.00 51.92  ? 630  TRP   D CH2 1 
ATOM   12836 N  N   . LYS   D  1 330 ? 41.679  45.780  -64.202  1.00 54.32  ? 631  LYS   D N   1 
ATOM   12837 C  CA  . LYS   D  1 330 ? 40.794  45.399  -63.107  1.00 47.34  ? 631  LYS   D CA  1 
ATOM   12838 C  C   . LYS   D  1 330 ? 40.938  43.923  -62.784  1.00 53.60  ? 631  LYS   D C   1 
ATOM   12839 O  O   . LYS   D  1 330 ? 41.140  43.539  -61.624  1.00 56.12  ? 631  LYS   D O   1 
ATOM   12840 C  CB  . LYS   D  1 330 ? 39.343  45.717  -63.458  1.00 39.88  ? 631  LYS   D CB  1 
ATOM   12841 C  CG  . LYS   D  1 330 ? 39.021  47.180  -63.348  1.00 49.82  ? 631  LYS   D CG  1 
ATOM   12842 C  CD  . LYS   D  1 330 ? 37.541  47.438  -63.479  1.00 47.04  ? 631  LYS   D CD  1 
ATOM   12843 C  CE  . LYS   D  1 330 ? 37.283  48.918  -63.333  1.00 46.74  ? 631  LYS   D CE  1 
ATOM   12844 N  NZ  . LYS   D  1 330 ? 35.842  49.243  -63.360  1.00 53.05  ? 631  LYS   D NZ  1 
ATOM   12845 N  N   . ASP   D  1 331 ? 40.828  43.083  -63.812  1.00 53.00  ? 632  ASP   D N   1 
ATOM   12846 C  CA  . ASP   D  1 331 ? 40.945  41.639  -63.638  1.00 50.11  ? 632  ASP   D CA  1 
ATOM   12847 C  C   . ASP   D  1 331 ? 42.274  41.270  -62.990  1.00 46.55  ? 632  ASP   D C   1 
ATOM   12848 O  O   . ASP   D  1 331 ? 42.332  40.427  -62.087  1.00 46.99  ? 632  ASP   D O   1 
ATOM   12849 C  CB  . ASP   D  1 331 ? 40.802  40.957  -65.005  1.00 50.82  ? 632  ASP   D CB  1 
ATOM   12850 C  CG  . ASP   D  1 331 ? 39.605  41.485  -65.808  1.00 41.71  ? 632  ASP   D CG  1 
ATOM   12851 O  OD1 . ASP   D  1 331 ? 39.721  42.559  -66.442  1.00 41.31  ? 632  ASP   D OD1 1 
ATOM   12852 O  OD2 . ASP   D  1 331 ? 38.543  40.837  -65.794  1.00 35.25  ? 632  ASP   D OD2 1 
ATOM   12853 N  N   . GLN   D  1 332 ? 43.356  41.895  -63.456  1.00 48.58  ? 633  GLN   D N   1 
ATOM   12854 C  CA  . GLN   D  1 332 ? 44.693  41.552  -62.994  1.00 49.17  ? 633  GLN   D CA  1 
ATOM   12855 C  C   . GLN   D  1 332 ? 44.887  41.975  -61.551  1.00 49.71  ? 633  GLN   D C   1 
ATOM   12856 O  O   . GLN   D  1 332 ? 45.470  41.241  -60.743  1.00 42.27  ? 633  GLN   D O   1 
ATOM   12857 C  CB  . GLN   D  1 332 ? 45.713  42.247  -63.872  1.00 53.92  ? 633  GLN   D CB  1 
ATOM   12858 C  CG  . GLN   D  1 332 ? 46.838  41.411  -64.371  1.00 60.91  ? 633  GLN   D CG  1 
ATOM   12859 C  CD  . GLN   D  1 332 ? 47.647  42.175  -65.397  1.00 64.93  ? 633  GLN   D CD  1 
ATOM   12860 O  OE1 . GLN   D  1 332 ? 47.390  43.354  -65.649  1.00 57.45  ? 633  GLN   D OE1 1 
ATOM   12861 N  NE2 . GLN   D  1 332 ? 48.613  41.508  -66.007  1.00 81.86  ? 633  GLN   D NE2 1 
ATOM   12862 N  N   . ALA   D  1 333 ? 44.420  43.176  -61.227  1.00 48.10  ? 634  ALA   D N   1 
ATOM   12863 C  CA  . ALA   D  1 333 ? 44.528  43.686  -59.876  1.00 45.67  ? 634  ALA   D CA  1 
ATOM   12864 C  C   . ALA   D  1 333 ? 43.629  42.905  -58.925  1.00 47.77  ? 634  ALA   D C   1 
ATOM   12865 O  O   . ALA   D  1 333 ? 43.967  42.750  -57.751  1.00 41.92  ? 634  ALA   D O   1 
ATOM   12866 C  CB  . ALA   D  1 333 ? 44.201  45.180  -59.868  1.00 35.37  ? 634  ALA   D CB  1 
ATOM   12867 N  N   . LEU   D  1 334 ? 42.512  42.370  -59.430  1.00 45.18  ? 635  LEU   D N   1 
ATOM   12868 C  CA  . LEU   D  1 334 ? 41.613  41.576  -58.597  1.00 40.84  ? 635  LEU   D CA  1 
ATOM   12869 C  C   . LEU   D  1 334 ? 42.249  40.248  -58.183  1.00 50.16  ? 635  LEU   D C   1 
ATOM   12870 O  O   . LEU   D  1 334 ? 42.074  39.811  -57.034  1.00 43.81  ? 635  LEU   D O   1 
ATOM   12871 C  CB  . LEU   D  1 334 ? 40.288  41.344  -59.329  1.00 38.58  ? 635  LEU   D CB  1 
ATOM   12872 C  CG  . LEU   D  1 334 ? 39.232  40.386  -58.757  1.00 34.91  ? 635  LEU   D CG  1 
ATOM   12873 C  CD1 . LEU   D  1 334 ? 38.472  40.984  -57.580  1.00 32.61  ? 635  LEU   D CD1 1 
ATOM   12874 C  CD2 . LEU   D  1 334 ? 38.266  39.959  -59.854  1.00 36.64  ? 635  LEU   D CD2 1 
ATOM   12875 N  N   . VAL   D  1 335 ? 42.987  39.587  -59.092  1.00 50.51  ? 636  VAL   D N   1 
ATOM   12876 C  CA  . VAL   D  1 335 ? 43.633  38.319  -58.734  1.00 44.11  ? 636  VAL   D CA  1 
ATOM   12877 C  C   . VAL   D  1 335 ? 44.656  38.547  -57.627  1.00 43.40  ? 636  VAL   D C   1 
ATOM   12878 O  O   . VAL   D  1 335 ? 44.708  37.800  -56.641  1.00 38.70  ? 636  VAL   D O   1 
ATOM   12879 C  CB  . VAL   D  1 335 ? 44.284  37.645  -59.962  1.00 45.65  ? 636  VAL   D CB  1 
ATOM   12880 C  CG1 . VAL   D  1 335 ? 44.974  36.334  -59.549  1.00 31.79  ? 636  VAL   D CG1 1 
ATOM   12881 C  CG2 . VAL   D  1 335 ? 43.264  37.351  -61.045  1.00 30.23  ? 636  VAL   D CG2 1 
ATOM   12882 N  N   . GLU   D  1 336 ? 45.484  39.591  -57.776  1.00 47.78  ? 637  GLU   D N   1 
ATOM   12883 C  CA  . GLU   D  1 336 ? 46.531  39.869  -56.794  1.00 50.99  ? 637  GLU   D CA  1 
ATOM   12884 C  C   . GLU   D  1 336 ? 45.942  40.159  -55.419  1.00 49.99  ? 637  GLU   D C   1 
ATOM   12885 O  O   . GLU   D  1 336 ? 46.512  39.764  -54.396  1.00 41.58  ? 637  GLU   D O   1 
ATOM   12886 C  CB  . GLU   D  1 336 ? 47.392  41.052  -57.243  1.00 49.24  ? 637  GLU   D CB  1 
ATOM   12887 C  CG  . GLU   D  1 336 ? 48.181  40.842  -58.521  1.00 52.14  ? 637  GLU   D CG  1 
ATOM   12888 C  CD  . GLU   D  1 336 ? 49.202  39.732  -58.397  1.00 50.68  ? 637  GLU   D CD  1 
ATOM   12889 O  OE1 . GLU   D  1 336 ? 49.451  39.232  -57.280  1.00 48.98  ? 637  GLU   D OE1 1 
ATOM   12890 O  OE2 . GLU   D  1 336 ? 49.754  39.345  -59.431  1.00 49.68  ? 637  GLU   D OE2 1 
ATOM   12891 N  N   . ILE   D  1 337 ? 44.823  40.883  -55.380  1.00 53.13  ? 638  ILE   D N   1 
ATOM   12892 C  CA  . ILE   D  1 337 ? 44.155  41.175  -54.119  1.00 41.55  ? 638  ILE   D CA  1 
ATOM   12893 C  C   . ILE   D  1 337 ? 43.725  39.886  -53.445  1.00 48.75  ? 638  ILE   D C   1 
ATOM   12894 O  O   . ILE   D  1 337 ? 43.866  39.723  -52.224  1.00 50.15  ? 638  ILE   D O   1 
ATOM   12895 C  CB  . ILE   D  1 337 ? 42.966  42.117  -54.368  1.00 37.71  ? 638  ILE   D CB  1 
ATOM   12896 C  CG1 . ILE   D  1 337 ? 43.488  43.487  -54.778  1.00 43.86  ? 638  ILE   D CG1 1 
ATOM   12897 C  CG2 . ILE   D  1 337 ? 42.066  42.231  -53.149  1.00 36.38  ? 638  ILE   D CG2 1 
ATOM   12898 C  CD1 . ILE   D  1 337 ? 42.442  44.338  -55.440  1.00 46.95  ? 638  ILE   D CD1 1 
ATOM   12899 N  N   . ASN   D  1 338 ? 43.217  38.941  -54.231  1.00 44.24  ? 639  ASN   D N   1 
ATOM   12900 C  CA  . ASN   D  1 338 ? 42.702  37.703  -53.666  1.00 41.65  ? 639  ASN   D CA  1 
ATOM   12901 C  C   . ASN   D  1 338 ? 43.822  36.765  -53.238  1.00 41.75  ? 639  ASN   D C   1 
ATOM   12902 O  O   . ASN   D  1 338 ? 43.637  35.974  -52.301  1.00 38.20  ? 639  ASN   D O   1 
ATOM   12903 C  CB  . ASN   D  1 338 ? 41.753  37.053  -54.671  1.00 32.10  ? 639  ASN   D CB  1 
ATOM   12904 C  CG  . ASN   D  1 338 ? 40.368  37.645  -54.591  1.00 40.06  ? 639  ASN   D CG  1 
ATOM   12905 O  OD1 . ASN   D  1 338 ? 39.519  37.158  -53.843  1.00 49.41  ? 639  ASN   D OD1 1 
ATOM   12906 N  ND2 . ASN   D  1 338 ? 40.146  38.731  -55.309  1.00 42.34  ? 639  ASN   D ND2 1 
ATOM   12907 N  N   . ILE   D  1 339 ? 44.979  36.850  -53.905  1.00 40.83  ? 640  ILE   D N   1 
ATOM   12908 C  CA  . ILE   D  1 339 ? 46.177  36.152  -53.450  1.00 40.47  ? 640  ILE   D CA  1 
ATOM   12909 C  C   . ILE   D  1 339 ? 46.595  36.679  -52.089  1.00 47.20  ? 640  ILE   D C   1 
ATOM   12910 O  O   . ILE   D  1 339 ? 46.948  35.909  -51.188  1.00 50.74  ? 640  ILE   D O   1 
ATOM   12911 C  CB  . ILE   D  1 339 ? 47.312  36.296  -54.485  1.00 39.15  ? 640  ILE   D CB  1 
ATOM   12912 C  CG1 . ILE   D  1 339 ? 47.017  35.423  -55.703  1.00 37.92  ? 640  ILE   D CG1 1 
ATOM   12913 C  CG2 . ILE   D  1 339 ? 48.677  35.933  -53.882  1.00 31.92  ? 640  ILE   D CG2 1 
ATOM   12914 C  CD1 . ILE   D  1 339 ? 47.814  35.780  -56.923  1.00 38.05  ? 640  ILE   D CD1 1 
ATOM   12915 N  N   . ALA   D  1 340 ? 46.527  38.000  -51.916  1.00 45.20  ? 641  ALA   D N   1 
ATOM   12916 C  CA  . ALA   D  1 340 ? 46.945  38.618  -50.666  1.00 49.86  ? 641  ALA   D CA  1 
ATOM   12917 C  C   . ALA   D  1 340 ? 46.067  38.160  -49.501  1.00 48.45  ? 641  ALA   D C   1 
ATOM   12918 O  O   . ALA   D  1 340 ? 46.572  37.803  -48.426  1.00 42.31  ? 641  ALA   D O   1 
ATOM   12919 C  CB  . ALA   D  1 340 ? 46.918  40.141  -50.814  1.00 43.56  ? 641  ALA   D CB  1 
ATOM   12920 N  N   . VAL   D  1 341 ? 44.748  38.165  -49.706  1.00 38.41  ? 642  VAL   D N   1 
ATOM   12921 C  CA  . VAL   D  1 341 ? 43.805  37.744  -48.672  1.00 41.61  ? 642  VAL   D CA  1 
ATOM   12922 C  C   . VAL   D  1 341 ? 44.108  36.318  -48.228  1.00 40.68  ? 642  VAL   D C   1 
ATOM   12923 O  O   . VAL   D  1 341 ? 44.235  36.039  -47.030  1.00 37.19  ? 642  VAL   D O   1 
ATOM   12924 C  CB  . VAL   D  1 341 ? 42.357  37.886  -49.184  1.00 42.13  ? 642  VAL   D CB  1 
ATOM   12925 C  CG1 . VAL   D  1 341 ? 41.367  37.360  -48.170  1.00 38.76  ? 642  VAL   D CG1 1 
ATOM   12926 C  CG2 . VAL   D  1 341 ? 42.049  39.346  -49.509  1.00 36.36  ? 642  VAL   D CG2 1 
ATOM   12927 N  N   . LEU   D  1 342 ? 44.252  35.396  -49.189  1.00 40.15  ? 643  LEU   D N   1 
ATOM   12928 C  CA  . LEU   D  1 342 ? 44.510  33.996  -48.846  1.00 42.30  ? 643  LEU   D CA  1 
ATOM   12929 C  C   . LEU   D  1 342 ? 45.864  33.826  -48.166  1.00 46.12  ? 643  LEU   D C   1 
ATOM   12930 O  O   . LEU   D  1 342 ? 45.999  33.041  -47.221  1.00 41.95  ? 643  LEU   D O   1 
ATOM   12931 C  CB  . LEU   D  1 342 ? 44.428  33.109  -50.092  1.00 37.40  ? 643  LEU   D CB  1 
ATOM   12932 C  CG  . LEU   D  1 342 ? 43.038  32.978  -50.710  1.00 38.52  ? 643  LEU   D CG  1 
ATOM   12933 C  CD1 . LEU   D  1 342 ? 43.099  32.596  -52.214  1.00 47.97  ? 643  LEU   D CD1 1 
ATOM   12934 C  CD2 . LEU   D  1 342 ? 42.192  32.002  -49.940  1.00 25.86  ? 643  LEU   D CD2 1 
ATOM   12935 N  N   . TYR   D  1 343 ? 46.880  34.544  -48.641  1.00 45.97  ? 644  TYR   D N   1 
ATOM   12936 C  CA  . TYR   D  1 343 ? 48.207  34.427  -48.053  1.00 40.71  ? 644  TYR   D CA  1 
ATOM   12937 C  C   . TYR   D  1 343 ? 48.229  34.981  -46.637  1.00 46.17  ? 644  TYR   D C   1 
ATOM   12938 O  O   . TYR   D  1 343 ? 48.893  34.429  -45.750  1.00 47.42  ? 644  TYR   D O   1 
ATOM   12939 C  CB  . TYR   D  1 343 ? 49.214  35.167  -48.923  1.00 36.46  ? 644  TYR   D CB  1 
ATOM   12940 C  CG  . TYR   D  1 343 ? 50.571  35.397  -48.292  1.00 36.07  ? 644  TYR   D CG  1 
ATOM   12941 C  CD1 . TYR   D  1 343 ? 51.494  34.371  -48.192  1.00 38.66  ? 644  TYR   D CD1 1 
ATOM   12942 C  CD2 . TYR   D  1 343 ? 50.948  36.660  -47.842  1.00 43.53  ? 644  TYR   D CD2 1 
ATOM   12943 C  CE1 . TYR   D  1 343 ? 52.745  34.580  -47.634  1.00 45.53  ? 644  TYR   D CE1 1 
ATOM   12944 C  CE2 . TYR   D  1 343 ? 52.197  36.883  -47.291  1.00 49.87  ? 644  TYR   D CE2 1 
ATOM   12945 C  CZ  . TYR   D  1 343 ? 53.095  35.837  -47.186  1.00 54.10  ? 644  TYR   D CZ  1 
ATOM   12946 O  OH  . TYR   D  1 343 ? 54.347  36.041  -46.635  1.00 58.46  ? 644  TYR   D OH  1 
ATOM   12947 N  N   . SER   D  1 344 ? 47.516  36.078  -46.419  1.00 46.95  ? 645  SER   D N   1 
ATOM   12948 C  CA  . SER   D  1 344 ? 47.527  36.725  -45.122  1.00 41.78  ? 645  SER   D CA  1 
ATOM   12949 C  C   . SER   D  1 344 ? 46.865  35.844  -44.070  1.00 45.68  ? 645  SER   D C   1 
ATOM   12950 O  O   . SER   D  1 344 ? 47.438  35.602  -42.999  1.00 43.26  ? 645  SER   D O   1 
ATOM   12951 C  CB  . SER   D  1 344 ? 46.844  38.082  -45.234  1.00 36.86  ? 645  SER   D CB  1 
ATOM   12952 O  OG  . SER   D  1 344 ? 47.694  38.984  -45.919  1.00 46.44  ? 645  SER   D OG  1 
ATOM   12953 N  N   . PHE   D  1 345 ? 45.666  35.338  -44.370  1.00 39.19  ? 646  PHE   D N   1 
ATOM   12954 C  CA  . PHE   D  1 345 ? 44.976  34.446  -43.442  1.00 40.17  ? 646  PHE   D CA  1 
ATOM   12955 C  C   . PHE   D  1 345 ? 45.798  33.193  -43.160  1.00 46.71  ? 646  PHE   D C   1 
ATOM   12956 O  O   . PHE   D  1 345 ? 45.907  32.752  -42.006  1.00 44.48  ? 646  PHE   D O   1 
ATOM   12957 C  CB  . PHE   D  1 345 ? 43.603  34.066  -44.000  1.00 34.65  ? 646  PHE   D CB  1 
ATOM   12958 C  CG  . PHE   D  1 345 ? 42.508  35.049  -43.664  1.00 34.54  ? 646  PHE   D CG  1 
ATOM   12959 C  CD1 . PHE   D  1 345 ? 42.620  36.386  -44.023  1.00 31.89  ? 646  PHE   D CD1 1 
ATOM   12960 C  CD2 . PHE   D  1 345 ? 41.361  34.629  -42.996  1.00 32.73  ? 646  PHE   D CD2 1 
ATOM   12961 C  CE1 . PHE   D  1 345 ? 41.620  37.289  -43.730  1.00 34.98  ? 646  PHE   D CE1 1 
ATOM   12962 C  CE2 . PHE   D  1 345 ? 40.353  35.525  -42.687  1.00 33.08  ? 646  PHE   D CE2 1 
ATOM   12963 C  CZ  . PHE   D  1 345 ? 40.479  36.862  -43.055  1.00 39.32  ? 646  PHE   D CZ  1 
ATOM   12964 N  N   . GLN   D  1 346 ? 46.390  32.607  -44.203  1.00 47.03  ? 647  GLN   D N   1 
ATOM   12965 C  CA  . GLN   D  1 346 ? 47.116  31.358  -44.017  1.00 47.11  ? 647  GLN   D CA  1 
ATOM   12966 C  C   . GLN   D  1 346 ? 48.348  31.558  -43.149  1.00 48.44  ? 647  GLN   D C   1 
ATOM   12967 O  O   . GLN   D  1 346 ? 48.656  30.709  -42.308  1.00 50.72  ? 647  GLN   D O   1 
ATOM   12968 C  CB  . GLN   D  1 346 ? 47.485  30.755  -45.369  1.00 43.98  ? 647  GLN   D CB  1 
ATOM   12969 C  CG  . GLN   D  1 346 ? 46.331  29.985  -46.006  1.00 48.91  ? 647  GLN   D CG  1 
ATOM   12970 C  CD  . GLN   D  1 346 ? 46.515  29.751  -47.506  1.00 54.29  ? 647  GLN   D CD  1 
ATOM   12971 O  OE1 . GLN   D  1 346 ? 47.531  30.122  -48.092  1.00 53.20  ? 647  GLN   D OE1 1 
ATOM   12972 N  NE2 . GLN   D  1 346 ? 45.523  29.127  -48.125  1.00 57.10  ? 647  GLN   D NE2 1 
ATOM   12973 N  N   . SER   D  1 347 ? 49.050  32.680  -43.329  1.00 41.21  ? 648  SER   D N   1 
ATOM   12974 C  CA  . SER   D  1 347 ? 50.250  32.944  -42.550  1.00 38.35  ? 648  SER   D CA  1 
ATOM   12975 C  C   . SER   D  1 347 ? 49.922  33.156  -41.071  1.00 49.69  ? 648  SER   D C   1 
ATOM   12976 O  O   . SER   D  1 347 ? 50.651  32.674  -40.198  1.00 48.85  ? 648  SER   D O   1 
ATOM   12977 C  CB  . SER   D  1 347 ? 50.985  34.156  -43.117  1.00 45.52  ? 648  SER   D CB  1 
ATOM   12978 O  OG  . SER   D  1 347 ? 51.297  33.961  -44.486  1.00 53.69  ? 648  SER   D OG  1 
ATOM   12979 N  N   . ASP   D  1 348 ? 48.823  33.861  -40.769  1.00 44.99  ? 649  ASP   D N   1 
ATOM   12980 C  CA  . ASP   D  1 348 ? 48.333  34.008  -39.399  1.00 45.29  ? 649  ASP   D CA  1 
ATOM   12981 C  C   . ASP   D  1 348 ? 47.519  32.805  -38.914  1.00 47.92  ? 649  ASP   D C   1 
ATOM   12982 O  O   . ASP   D  1 348 ? 46.796  32.940  -37.928  1.00 43.85  ? 649  ASP   D O   1 
ATOM   12983 C  CB  . ASP   D  1 348 ? 47.484  35.276  -39.272  1.00 39.68  ? 649  ASP   D CB  1 
ATOM   12984 C  CG  . ASP   D  1 348 ? 48.284  36.531  -39.497  1.00 44.87  ? 649  ASP   D CG  1 
ATOM   12985 O  OD1 . ASP   D  1 348 ? 49.526  36.435  -39.606  1.00 33.97  ? 649  ASP   D OD1 1 
ATOM   12986 O  OD2 . ASP   D  1 348 ? 47.671  37.617  -39.569  1.00 54.50  ? 649  ASP   D OD2 1 
ATOM   12987 N  N   . LYS   D  1 349 ? 47.604  31.665  -39.593  1.00 43.39  ? 650  LYS   D N   1 
ATOM   12988 C  CA  . LYS   D  1 349 ? 46.858  30.449  -39.268  1.00 39.56  ? 650  LYS   D CA  1 
ATOM   12989 C  C   . LYS   D  1 349 ? 45.409  30.721  -38.844  1.00 42.05  ? 650  LYS   D C   1 
ATOM   12990 O  O   . LYS   D  1 349 ? 44.897  30.159  -37.872  1.00 40.38  ? 650  LYS   D O   1 
ATOM   12991 C  CB  . LYS   D  1 349 ? 47.600  29.641  -38.214  1.00 44.35  ? 650  LYS   D CB  1 
ATOM   12992 C  CG  . LYS   D  1 349 ? 48.965  29.177  -38.698  1.00 42.00  ? 650  LYS   D CG  1 
ATOM   12993 C  CD  . LYS   D  1 349 ? 49.844  28.790  -37.511  1.00 52.91  ? 650  LYS   D CD  1 
ATOM   12994 C  CE  . LYS   D  1 349 ? 50.906  27.763  -37.887  1.00 68.08  ? 650  LYS   D CE  1 
ATOM   12995 N  NZ  . LYS   D  1 349 ? 51.399  27.041  -36.670  1.00 79.76  ? 650  LYS   D NZ  1 
ATOM   12996 N  N   . VAL   D  1 350 ? 44.724  31.549  -39.631  1.00 47.19  ? 651  VAL   D N   1 
ATOM   12997 C  CA  . VAL   D  1 350 ? 43.289  31.792  -39.508  1.00 43.66  ? 651  VAL   D CA  1 
ATOM   12998 C  C   . VAL   D  1 350 ? 42.580  31.089  -40.669  1.00 43.90  ? 651  VAL   D C   1 
ATOM   12999 O  O   . VAL   D  1 350 ? 42.902  31.332  -41.839  1.00 42.24  ? 651  VAL   D O   1 
ATOM   13000 C  CB  . VAL   D  1 350 ? 42.980  33.301  -39.495  1.00 27.97  ? 651  VAL   D CB  1 
ATOM   13001 C  CG1 . VAL   D  1 350 ? 41.470  33.548  -39.510  1.00 27.66  ? 651  VAL   D CG1 1 
ATOM   13002 C  CG2 . VAL   D  1 350 ? 43.628  33.951  -38.303  1.00 32.70  ? 651  VAL   D CG2 1 
ATOM   13003 N  N   . THR   D  1 351 ? 41.606  30.236  -40.335  1.00 38.54  ? 652  THR   D N   1 
ATOM   13004 C  CA  . THR   D  1 351 ? 40.922  29.389  -41.303  1.00 37.22  ? 652  THR   D CA  1 
ATOM   13005 C  C   . THR   D  1 351 ? 40.313  30.193  -42.441  1.00 40.74  ? 652  THR   D C   1 
ATOM   13006 O  O   . THR   D  1 351 ? 39.549  31.139  -42.213  1.00 37.06  ? 652  THR   D O   1 
ATOM   13007 C  CB  . THR   D  1 351 ? 39.804  28.602  -40.626  1.00 36.06  ? 652  THR   D CB  1 
ATOM   13008 O  OG1 . THR   D  1 351 ? 40.300  27.918  -39.467  1.00 44.39  ? 652  THR   D OG1 1 
ATOM   13009 C  CG2 . THR   D  1 351 ? 39.203  27.607  -41.629  1.00 31.47  ? 652  THR   D CG2 1 
ATOM   13010 N  N   . ILE   D  1 352 ? 40.604  29.765  -43.671  1.00 37.32  ? 653  ILE   D N   1 
ATOM   13011 C  CA  . ILE   D  1 352 ? 39.993  30.325  -44.871  1.00 30.52  ? 653  ILE   D CA  1 
ATOM   13012 C  C   . ILE   D  1 352 ? 40.021  29.247  -45.944  1.00 39.91  ? 653  ILE   D C   1 
ATOM   13013 O  O   . ILE   D  1 352 ? 40.840  28.326  -45.898  1.00 37.86  ? 653  ILE   D O   1 
ATOM   13014 C  CB  . ILE   D  1 352 ? 40.742  31.604  -45.313  1.00 35.01  ? 653  ILE   D CB  1 
ATOM   13015 C  CG1 . ILE   D  1 352 ? 39.909  32.445  -46.299  1.00 29.66  ? 653  ILE   D CG1 1 
ATOM   13016 C  CG2 . ILE   D  1 352 ? 42.122  31.237  -45.875  1.00 32.08  ? 653  ILE   D CG2 1 
ATOM   13017 C  CD1 . ILE   D  1 352 ? 40.369  33.885  -46.382  1.00 24.56  ? 653  ILE   D CD1 1 
ATOM   13018 N  N   . VAL   D  1 353 ? 39.107  29.359  -46.915  1.00 39.65  ? 654  VAL   D N   1 
ATOM   13019 C  CA  . VAL   D  1 353 ? 39.043  28.455  -48.059  1.00 38.78  ? 654  VAL   D CA  1 
ATOM   13020 C  C   . VAL   D  1 353 ? 39.037  29.277  -49.349  1.00 41.51  ? 654  VAL   D C   1 
ATOM   13021 O  O   . VAL   D  1 353 ? 38.304  30.267  -49.465  1.00 34.34  ? 654  VAL   D O   1 
ATOM   13022 C  CB  . VAL   D  1 353 ? 37.812  27.528  -47.990  1.00 43.01  ? 654  VAL   D CB  1 
ATOM   13023 C  CG1 . VAL   D  1 353 ? 36.520  28.303  -48.061  1.00 37.70  ? 654  VAL   D CG1 1 
ATOM   13024 C  CG2 . VAL   D  1 353 ? 37.874  26.475  -49.082  1.00 39.96  ? 654  VAL   D CG2 1 
ATOM   13025 N  N   . ASP   D  1 354 ? 39.878  28.885  -50.304  1.00 35.70  ? 655  ASP   D N   1 
ATOM   13026 C  CA  . ASP   D  1 354 ? 39.897  29.562  -51.589  1.00 40.83  ? 655  ASP   D CA  1 
ATOM   13027 C  C   . ASP   D  1 354 ? 38.755  29.034  -52.457  1.00 38.92  ? 655  ASP   D C   1 
ATOM   13028 O  O   . ASP   D  1 354 ? 38.197  27.963  -52.201  1.00 34.71  ? 655  ASP   D O   1 
ATOM   13029 C  CB  . ASP   D  1 354 ? 41.250  29.375  -52.276  1.00 40.11  ? 655  ASP   D CB  1 
ATOM   13030 C  CG  . ASP   D  1 354 ? 41.505  27.938  -52.656  1.00 48.77  ? 655  ASP   D CG  1 
ATOM   13031 O  OD1 . ASP   D  1 354 ? 40.967  27.508  -53.701  1.00 37.13  ? 655  ASP   D OD1 1 
ATOM   13032 O  OD2 . ASP   D  1 354 ? 42.208  27.228  -51.898  1.00 60.25  ? 655  ASP   D OD2 1 
ATOM   13033 N  N   . HIS   D  1 355 ? 38.395  29.807  -53.487  1.00 42.88  ? 656  HIS   D N   1 
ATOM   13034 C  CA  . HIS   D  1 355 ? 37.180  29.475  -54.231  1.00 41.33  ? 656  HIS   D CA  1 
ATOM   13035 C  C   . HIS   D  1 355 ? 37.306  28.147  -54.960  1.00 33.46  ? 656  HIS   D C   1 
ATOM   13036 O  O   . HIS   D  1 355 ? 36.315  27.428  -55.099  1.00 41.65  ? 656  HIS   D O   1 
ATOM   13037 C  CB  . HIS   D  1 355 ? 36.791  30.597  -55.202  1.00 37.48  ? 656  HIS   D CB  1 
ATOM   13038 C  CG  . HIS   D  1 355 ? 37.912  31.115  -56.047  1.00 39.86  ? 656  HIS   D CG  1 
ATOM   13039 N  ND1 . HIS   D  1 355 ? 38.811  32.057  -55.596  1.00 38.92  ? 656  HIS   D ND1 1 
ATOM   13040 C  CD2 . HIS   D  1 355 ? 38.235  30.878  -57.341  1.00 35.16  ? 656  HIS   D CD2 1 
ATOM   13041 C  CE1 . HIS   D  1 355 ? 39.665  32.352  -56.561  1.00 35.35  ? 656  HIS   D CE1 1 
ATOM   13042 N  NE2 . HIS   D  1 355 ? 39.342  31.641  -57.626  1.00 37.27  ? 656  HIS   D NE2 1 
ATOM   13043 N  N   . HIS   D  1 356 ? 38.508  27.776  -55.378  1.00 31.63  ? 657  HIS   D N   1 
ATOM   13044 C  CA  . HIS   D  1 356 ? 38.681  26.486  -56.035  1.00 39.83  ? 657  HIS   D CA  1 
ATOM   13045 C  C   . HIS   D  1 356 ? 38.397  25.339  -55.081  1.00 42.17  ? 657  HIS   D C   1 
ATOM   13046 O  O   . HIS   D  1 356 ? 37.551  24.478  -55.356  1.00 44.70  ? 657  HIS   D O   1 
ATOM   13047 C  CB  . HIS   D  1 356 ? 40.089  26.392  -56.603  1.00 32.74  ? 657  HIS   D CB  1 
ATOM   13048 C  CG  . HIS   D  1 356 ? 40.389  27.484  -57.570  1.00 38.69  ? 657  HIS   D CG  1 
ATOM   13049 N  ND1 . HIS   D  1 356 ? 39.789  27.554  -58.807  1.00 36.54  ? 657  HIS   D ND1 1 
ATOM   13050 C  CD2 . HIS   D  1 356 ? 41.179  28.577  -57.468  1.00 38.73  ? 657  HIS   D CD2 1 
ATOM   13051 C  CE1 . HIS   D  1 356 ? 40.221  28.630  -59.438  1.00 39.31  ? 657  HIS   D CE1 1 
ATOM   13052 N  NE2 . HIS   D  1 356 ? 41.068  29.265  -58.649  1.00 40.20  ? 657  HIS   D NE2 1 
ATOM   13053 N  N   . SER   D  1 357 ? 39.099  25.313  -53.949  1.00 35.05  ? 658  SER   D N   1 
ATOM   13054 C  CA  . SER   D  1 357 ? 38.869  24.254  -52.972  1.00 37.43  ? 658  SER   D CA  1 
ATOM   13055 C  C   . SER   D  1 357 ? 37.409  24.220  -52.511  1.00 36.58  ? 658  SER   D C   1 
ATOM   13056 O  O   . SER   D  1 357 ? 36.824  23.140  -52.354  1.00 34.32  ? 658  SER   D O   1 
ATOM   13057 C  CB  . SER   D  1 357 ? 39.818  24.431  -51.784  1.00 41.55  ? 658  SER   D CB  1 
ATOM   13058 O  OG  . SER   D  1 357 ? 39.640  23.370  -50.861  1.00 52.92  ? 658  SER   D OG  1 
ATOM   13059 N  N   . ALA   D  1 358 ? 36.793  25.390  -52.308  1.00 35.44  ? 659  ALA   D N   1 
ATOM   13060 C  CA  . ALA   D  1 358 ? 35.411  25.420  -51.831  1.00 25.49  ? 659  ALA   D CA  1 
ATOM   13061 C  C   . ALA   D  1 358 ? 34.439  24.830  -52.848  1.00 35.67  ? 659  ALA   D C   1 
ATOM   13062 O  O   . ALA   D  1 358 ? 33.481  24.146  -52.466  1.00 34.59  ? 659  ALA   D O   1 
ATOM   13063 C  CB  . ALA   D  1 358 ? 35.001  26.851  -51.487  1.00 27.88  ? 659  ALA   D CB  1 
ATOM   13064 N  N   . THR   D  1 359 ? 34.646  25.095  -54.149  1.00 35.42  ? 660  THR   D N   1 
ATOM   13065 C  CA  . THR   D  1 359 ? 33.669  24.624  -55.130  1.00 28.08  ? 660  THR   D CA  1 
ATOM   13066 C  C   . THR   D  1 359 ? 33.855  23.147  -55.434  1.00 30.36  ? 660  THR   D C   1 
ATOM   13067 O  O   . THR   D  1 359 ? 32.874  22.428  -55.655  1.00 34.89  ? 660  THR   D O   1 
ATOM   13068 C  CB  . THR   D  1 359 ? 33.761  25.434  -56.417  1.00 32.04  ? 660  THR   D CB  1 
ATOM   13069 O  OG1 . THR   D  1 359 ? 35.110  25.440  -56.878  1.00 38.06  ? 660  THR   D OG1 1 
ATOM   13070 C  CG2 . THR   D  1 359 ? 33.294  26.850  -56.185  1.00 28.24  ? 660  THR   D CG2 1 
ATOM   13071 N  N   . GLU   D  1 360 ? 35.103  22.678  -55.453  1.00 36.58  ? 661  GLU   D N   1 
ATOM   13072 C  CA  . GLU   D  1 360 ? 35.339  21.245  -55.547  1.00 42.11  ? 661  GLU   D CA  1 
ATOM   13073 C  C   . GLU   D  1 360 ? 34.669  20.502  -54.392  1.00 44.08  ? 661  GLU   D C   1 
ATOM   13074 O  O   . GLU   D  1 360 ? 34.042  19.454  -54.593  1.00 43.74  ? 661  GLU   D O   1 
ATOM   13075 C  CB  . GLU   D  1 360 ? 36.841  20.973  -55.570  1.00 42.43  ? 661  GLU   D CB  1 
ATOM   13076 C  CG  . GLU   D  1 360 ? 37.204  19.510  -55.720  1.00 53.72  ? 661  GLU   D CG  1 
ATOM   13077 C  CD  . GLU   D  1 360 ? 38.704  19.268  -55.617  1.00 77.74  ? 661  GLU   D CD  1 
ATOM   13078 O  OE1 . GLU   D  1 360 ? 39.473  20.258  -55.607  1.00 87.04  ? 661  GLU   D OE1 1 
ATOM   13079 O  OE2 . GLU   D  1 360 ? 39.113  18.087  -55.542  1.00 82.83  ? 661  GLU   D OE2 1 
ATOM   13080 N  N   . SER   D  1 361 ? 34.772  21.034  -53.174  1.00 42.45  ? 662  SER   D N   1 
ATOM   13081 C  CA  A SER   D  1 361 ? 34.158  20.337  -52.052  0.67 40.22  ? 662  SER   D CA  1 
ATOM   13082 C  CA  B SER   D  1 361 ? 34.156  20.361  -52.034  0.33 40.15  ? 662  SER   D CA  1 
ATOM   13083 C  C   . SER   D  1 361 ? 32.644  20.328  -52.184  1.00 40.84  ? 662  SER   D C   1 
ATOM   13084 O  O   . SER   D  1 361 ? 32.001  19.307  -51.908  1.00 39.05  ? 662  SER   D O   1 
ATOM   13085 C  CB  A SER   D  1 361 ? 34.598  20.968  -50.732  0.67 38.38  ? 662  SER   D CB  1 
ATOM   13086 C  CB  B SER   D  1 361 ? 34.551  21.051  -50.726  0.33 38.63  ? 662  SER   D CB  1 
ATOM   13087 O  OG  A SER   D  1 361 ? 35.963  20.688  -50.469  0.67 37.95  ? 662  SER   D OG  1 
ATOM   13088 O  OG  B SER   D  1 361 ? 33.649  22.099  -50.385  0.33 37.40  ? 662  SER   D OG  1 
ATOM   13089 N  N   . PHE   D  1 362 ? 32.059  21.438  -52.639  1.00 38.65  ? 663  PHE   D N   1 
ATOM   13090 C  CA  . PHE   D  1 362 ? 30.617  21.467  -52.833  1.00 33.85  ? 663  PHE   D CA  1 
ATOM   13091 C  C   . PHE   D  1 362 ? 30.168  20.440  -53.871  1.00 37.18  ? 663  PHE   D C   1 
ATOM   13092 O  O   . PHE   D  1 362 ? 29.113  19.812  -53.697  1.00 36.45  ? 663  PHE   D O   1 
ATOM   13093 C  CB  . PHE   D  1 362 ? 30.153  22.863  -53.236  1.00 40.57  ? 663  PHE   D CB  1 
ATOM   13094 C  CG  . PHE   D  1 362 ? 28.688  22.936  -53.476  1.00 41.32  ? 663  PHE   D CG  1 
ATOM   13095 C  CD1 . PHE   D  1 362 ? 27.807  23.032  -52.402  1.00 34.00  ? 663  PHE   D CD1 1 
ATOM   13096 C  CD2 . PHE   D  1 362 ? 28.177  22.868  -54.777  1.00 33.93  ? 663  PHE   D CD2 1 
ATOM   13097 C  CE1 . PHE   D  1 362 ? 26.441  23.066  -52.605  1.00 36.60  ? 663  PHE   D CE1 1 
ATOM   13098 C  CE2 . PHE   D  1 362 ? 26.817  22.904  -54.995  1.00 34.16  ? 663  PHE   D CE2 1 
ATOM   13099 C  CZ  . PHE   D  1 362 ? 25.939  23.005  -53.918  1.00 44.98  ? 663  PHE   D CZ  1 
ATOM   13100 N  N   . ILE   D  1 363 ? 30.944  20.246  -54.957  1.00 32.46  ? 664  ILE   D N   1 
ATOM   13101 C  CA  . ILE   D  1 363 ? 30.558  19.231  -55.943  1.00 36.61  ? 664  ILE   D CA  1 
ATOM   13102 C  C   . ILE   D  1 363 ? 30.544  17.848  -55.298  1.00 38.23  ? 664  ILE   D C   1 
ATOM   13103 O  O   . ILE   D  1 363 ? 29.584  17.086  -55.462  1.00 38.59  ? 664  ILE   D O   1 
ATOM   13104 C  CB  . ILE   D  1 363 ? 31.472  19.265  -57.186  1.00 38.46  ? 664  ILE   D CB  1 
ATOM   13105 C  CG1 . ILE   D  1 363 ? 31.208  20.524  -58.016  1.00 38.96  ? 664  ILE   D CG1 1 
ATOM   13106 C  CG2 . ILE   D  1 363 ? 31.202  18.049  -58.081  1.00 25.97  ? 664  ILE   D CG2 1 
ATOM   13107 C  CD1 . ILE   D  1 363 ? 29.888  20.504  -58.743  1.00 31.60  ? 664  ILE   D CD1 1 
ATOM   13108 N  N   . LYS   D  1 364 ? 31.596  17.518  -54.530  1.00 40.30  ? 665  LYS   D N   1 
ATOM   13109 C  CA  . LYS   D  1 364 ? 31.596  16.285  -53.736  1.00 43.72  ? 665  LYS   D CA  1 
ATOM   13110 C  C   . LYS   D  1 364 ? 30.363  16.206  -52.845  1.00 39.29  ? 665  LYS   D C   1 
ATOM   13111 O  O   . LYS   D  1 364 ? 29.696  15.168  -52.774  1.00 34.93  ? 665  LYS   D O   1 
ATOM   13112 C  CB  . LYS   D  1 364 ? 32.862  16.192  -52.877  1.00 45.18  ? 665  LYS   D CB  1 
ATOM   13113 C  CG  . LYS   D  1 364 ? 34.182  16.253  -53.632  1.00 51.66  ? 665  LYS   D CG  1 
ATOM   13114 C  CD  . LYS   D  1 364 ? 34.581  14.910  -54.232  1.00 59.88  ? 665  LYS   D CD  1 
ATOM   13115 C  CE  . LYS   D  1 364 ? 35.950  14.438  -53.717  1.00 67.88  ? 665  LYS   D CE  1 
ATOM   13116 N  NZ  . LYS   D  1 364 ? 37.028  15.487  -53.727  1.00 64.07  ? 665  LYS   D NZ  1 
ATOM   13117 N  N   . HIS   D  1 365 ? 30.052  17.300  -52.146  1.00 42.42  ? 666  HIS   D N   1 
ATOM   13118 C  CA  . HIS   D  1 365 ? 28.893  17.309  -51.261  1.00 40.70  ? 666  HIS   D CA  1 
ATOM   13119 C  C   . HIS   D  1 365 ? 27.604  17.107  -52.047  1.00 44.32  ? 666  HIS   D C   1 
ATOM   13120 O  O   . HIS   D  1 365 ? 26.722  16.338  -51.635  1.00 33.86  ? 666  HIS   D O   1 
ATOM   13121 C  CB  . HIS   D  1 365 ? 28.862  18.625  -50.491  1.00 35.26  ? 666  HIS   D CB  1 
ATOM   13122 C  CG  . HIS   D  1 365 ? 27.574  18.892  -49.774  1.00 36.46  ? 666  HIS   D CG  1 
ATOM   13123 N  ND1 . HIS   D  1 365 ? 27.189  18.195  -48.650  1.00 37.42  ? 666  HIS   D ND1 1 
ATOM   13124 C  CD2 . HIS   D  1 365 ? 26.600  19.807  -50.002  1.00 34.64  ? 666  HIS   D CD2 1 
ATOM   13125 C  CE1 . HIS   D  1 365 ? 26.031  18.664  -48.219  1.00 33.60  ? 666  HIS   D CE1 1 
ATOM   13126 N  NE2 . HIS   D  1 365 ? 25.645  19.634  -49.027  1.00 37.10  ? 666  HIS   D NE2 1 
ATOM   13127 N  N   . MET   D  1 366 ? 27.487  17.774  -53.198  1.00 45.43  ? 667  MET   D N   1 
ATOM   13128 C  CA  . MET   D  1 366 ? 26.277  17.647  -54.005  1.00 39.74  ? 667  MET   D CA  1 
ATOM   13129 C  C   . MET   D  1 366 ? 26.018  16.193  -54.392  1.00 41.35  ? 667  MET   D C   1 
ATOM   13130 O  O   . MET   D  1 366 ? 24.918  15.670  -54.165  1.00 36.98  ? 667  MET   D O   1 
ATOM   13131 C  CB  . MET   D  1 366 ? 26.377  18.539  -55.238  1.00 46.31  ? 667  MET   D CB  1 
ATOM   13132 C  CG  . MET   D  1 366 ? 25.044  18.791  -55.911  1.00 50.96  ? 667  MET   D CG  1 
ATOM   13133 S  SD  . MET   D  1 366 ? 25.196  20.061  -57.173  1.00 51.70  ? 667  MET   D SD  1 
ATOM   13134 C  CE  . MET   D  1 366 ? 23.827  19.584  -58.238  1.00 56.47  ? 667  MET   D CE  1 
ATOM   13135 N  N   . GLU   D  1 367 ? 27.022  15.508  -54.958  1.00 46.93  ? 668  GLU   D N   1 
ATOM   13136 C  CA  . GLU   D  1 367 ? 26.768  14.129  -55.382  1.00 57.16  ? 668  GLU   D CA  1 
ATOM   13137 C  C   . GLU   D  1 367 ? 26.424  13.244  -54.190  1.00 51.00  ? 668  GLU   D C   1 
ATOM   13138 O  O   . GLU   D  1 367 ? 25.540  12.386  -54.286  1.00 48.54  ? 668  GLU   D O   1 
ATOM   13139 C  CB  . GLU   D  1 367 ? 27.943  13.530  -56.174  1.00 65.75  ? 668  GLU   D CB  1 
ATOM   13140 C  CG  . GLU   D  1 367 ? 29.185  14.371  -56.332  1.00 70.99  ? 668  GLU   D CG  1 
ATOM   13141 C  CD  . GLU   D  1 367 ? 29.745  14.353  -57.753  1.00 75.07  ? 668  GLU   D CD  1 
ATOM   13142 O  OE1 . GLU   D  1 367 ? 28.950  14.328  -58.716  1.00 72.85  ? 668  GLU   D OE1 1 
ATOM   13143 O  OE2 . GLU   D  1 367 ? 30.986  14.363  -57.906  1.00 76.98  ? 668  GLU   D OE2 1 
ATOM   13144 N  N   . ASN   D  1 368 ? 27.094  13.445  -53.052  1.00 54.94  ? 669  ASN   D N   1 
ATOM   13145 C  CA  . ASN   D  1 368 ? 26.749  12.663  -51.868  1.00 44.84  ? 669  ASN   D CA  1 
ATOM   13146 C  C   . ASN   D  1 368 ? 25.308  12.915  -51.447  1.00 39.50  ? 669  ASN   D C   1 
ATOM   13147 O  O   . ASN   D  1 368 ? 24.575  11.969  -51.123  1.00 41.70  ? 669  ASN   D O   1 
ATOM   13148 C  CB  . ASN   D  1 368 ? 27.702  12.975  -50.716  1.00 53.79  ? 669  ASN   D CB  1 
ATOM   13149 C  CG  . ASN   D  1 368 ? 27.380  12.168  -49.473  1.00 55.74  ? 669  ASN   D CG  1 
ATOM   13150 O  OD1 . ASN   D  1 368 ? 27.411  10.931  -49.503  1.00 60.06  ? 669  ASN   D OD1 1 
ATOM   13151 N  ND2 . ASN   D  1 368 ? 27.036  12.859  -48.379  1.00 48.49  ? 669  ASN   D ND2 1 
ATOM   13152 N  N   . GLU   D  1 369 ? 24.878  14.186  -51.465  1.00 39.96  ? 670  GLU   D N   1 
ATOM   13153 C  CA  . GLU   D  1 369 ? 23.498  14.512  -51.112  1.00 38.35  ? 670  GLU   D CA  1 
ATOM   13154 C  C   . GLU   D  1 369 ? 22.491  13.879  -52.074  1.00 41.74  ? 670  GLU   D C   1 
ATOM   13155 O  O   . GLU   D  1 369 ? 21.415  13.440  -51.653  1.00 41.40  ? 670  GLU   D O   1 
ATOM   13156 C  CB  . GLU   D  1 369 ? 23.317  16.029  -51.064  1.00 39.06  ? 670  GLU   D CB  1 
ATOM   13157 C  CG  . GLU   D  1 369 ? 23.984  16.671  -49.893  1.00 40.36  ? 670  GLU   D CG  1 
ATOM   13158 C  CD  . GLU   D  1 369 ? 23.256  16.372  -48.605  1.00 44.27  ? 670  GLU   D CD  1 
ATOM   13159 O  OE1 . GLU   D  1 369 ? 22.460  17.229  -48.158  1.00 44.76  ? 670  GLU   D OE1 1 
ATOM   13160 O  OE2 . GLU   D  1 369 ? 23.472  15.273  -48.055  1.00 46.34  ? 670  GLU   D OE2 1 
ATOM   13161 N  N   . TYR   D  1 370 ? 22.803  13.825  -53.369  1.00 42.84  ? 671  TYR   D N   1 
ATOM   13162 C  CA  . TYR   D  1 370 ? 21.901  13.099  -54.258  1.00 52.87  ? 671  TYR   D CA  1 
ATOM   13163 C  C   . TYR   D  1 370 ? 21.871  11.614  -53.905  1.00 49.28  ? 671  TYR   D C   1 
ATOM   13164 O  O   . TYR   D  1 370 ? 20.799  11.001  -53.869  1.00 44.47  ? 671  TYR   D O   1 
ATOM   13165 C  CB  . TYR   D  1 370 ? 22.292  13.317  -55.722  1.00 51.00  ? 671  TYR   D CB  1 
ATOM   13166 C  CG  . TYR   D  1 370 ? 21.701  14.582  -56.333  1.00 56.27  ? 671  TYR   D CG  1 
ATOM   13167 C  CD1 . TYR   D  1 370 ? 22.282  15.826  -56.107  1.00 55.45  ? 671  TYR   D CD1 1 
ATOM   13168 C  CD2 . TYR   D  1 370 ? 20.566  14.531  -57.142  1.00 53.49  ? 671  TYR   D CD2 1 
ATOM   13169 C  CE1 . TYR   D  1 370 ? 21.746  16.987  -56.664  1.00 50.69  ? 671  TYR   D CE1 1 
ATOM   13170 C  CE2 . TYR   D  1 370 ? 20.022  15.689  -57.698  1.00 43.65  ? 671  TYR   D CE2 1 
ATOM   13171 C  CZ  . TYR   D  1 370 ? 20.619  16.912  -57.458  1.00 47.88  ? 671  TYR   D CZ  1 
ATOM   13172 O  OH  . TYR   D  1 370 ? 20.098  18.059  -58.008  1.00 44.10  ? 671  TYR   D OH  1 
ATOM   13173 N  N   . ARG   D  1 371 ? 23.031  11.027  -53.603  1.00 46.31  ? 672  ARG   D N   1 
ATOM   13174 C  CA  . ARG   D  1 371 ? 23.083  9.597   -53.322  1.00 53.85  ? 672  ARG   D CA  1 
ATOM   13175 C  C   . ARG   D  1 371 ? 22.268  9.241   -52.078  1.00 54.66  ? 672  ARG   D C   1 
ATOM   13176 O  O   . ARG   D  1 371 ? 21.433  8.332   -52.109  1.00 59.47  ? 672  ARG   D O   1 
ATOM   13177 C  CB  . ARG   D  1 371 ? 24.538  9.151   -53.168  1.00 71.84  ? 672  ARG   D CB  1 
ATOM   13178 C  CG  . ARG   D  1 371 ? 24.789  7.701   -53.576  1.00 87.67  ? 672  ARG   D CG  1 
ATOM   13179 C  CD  . ARG   D  1 371 ? 26.281  7.347   -53.599  1.00 98.91  ? 672  ARG   D CD  1 
ATOM   13180 N  NE  . ARG   D  1 371 ? 27.102  8.332   -54.313  1.00 103.82 ? 672  ARG   D NE  1 
ATOM   13181 C  CZ  . ARG   D  1 371 ? 28.106  9.017   -53.762  1.00 101.85 ? 672  ARG   D CZ  1 
ATOM   13182 N  NH1 . ARG   D  1 371 ? 28.427  8.819   -52.488  1.00 97.74  ? 672  ARG   D NH1 1 
ATOM   13183 N  NH2 . ARG   D  1 371 ? 28.799  9.895   -54.484  1.00 99.47  ? 672  ARG   D NH2 1 
ATOM   13184 N  N   . CYS   D  1 372 ? 22.479  9.951   -50.972  1.00 49.39  ? 673  CYS   D N   1 
ATOM   13185 C  CA  . CYS   D  1 372 ? 21.879  9.526   -49.714  1.00 53.89  ? 673  CYS   D CA  1 
ATOM   13186 C  C   . CYS   D  1 372 ? 20.588  10.263  -49.363  1.00 48.93  ? 673  CYS   D C   1 
ATOM   13187 O  O   . CYS   D  1 372 ? 19.847  9.794   -48.499  1.00 46.09  ? 673  CYS   D O   1 
ATOM   13188 C  CB  . CYS   D  1 372 ? 22.894  9.685   -48.579  1.00 56.92  ? 673  CYS   D CB  1 
ATOM   13189 S  SG  . CYS   D  1 372 ? 23.093  11.380  -48.017  1.00 58.26  ? 673  CYS   D SG  1 
ATOM   13190 N  N   . ARG   D  1 373 ? 20.293  11.389  -50.013  1.00 49.34  ? 674  ARG   D N   1 
ATOM   13191 C  CA  . ARG   D  1 373 ? 19.094  12.175  -49.743  1.00 36.52  ? 674  ARG   D CA  1 
ATOM   13192 C  C   . ARG   D  1 373 ? 18.199  12.372  -50.965  1.00 47.52  ? 674  ARG   D C   1 
ATOM   13193 O  O   . ARG   D  1 373 ? 17.046  12.791  -50.804  1.00 49.39  ? 674  ARG   D O   1 
ATOM   13194 C  CB  . ARG   D  1 373 ? 19.491  13.551  -49.176  1.00 35.69  ? 674  ARG   D CB  1 
ATOM   13195 C  CG  . ARG   D  1 373 ? 18.379  14.323  -48.465  1.00 33.16  ? 674  ARG   D CG  1 
ATOM   13196 C  CD  . ARG   D  1 373 ? 18.840  15.727  -48.103  1.00 32.12  ? 674  ARG   D CD  1 
ATOM   13197 N  NE  . ARG   D  1 373 ? 17.888  16.409  -47.231  1.00 38.77  ? 674  ARG   D NE  1 
ATOM   13198 C  CZ  . ARG   D  1 373 ? 17.830  17.728  -47.071  1.00 43.86  ? 674  ARG   D CZ  1 
ATOM   13199 N  NH1 . ARG   D  1 373 ? 18.657  18.522  -47.744  1.00 43.33  ? 674  ARG   D NH1 1 
ATOM   13200 N  NH2 . ARG   D  1 373 ? 16.937  18.257  -46.247  1.00 35.42  ? 674  ARG   D NH2 1 
ATOM   13201 N  N   . GLY   D  1 374 ? 18.679  12.090  -52.174  1.00 44.50  ? 675  GLY   D N   1 
ATOM   13202 C  CA  . GLY   D  1 374 ? 17.835  12.222  -53.341  1.00 48.03  ? 675  GLY   D CA  1 
ATOM   13203 C  C   . GLY   D  1 374 ? 17.803  13.607  -53.936  1.00 51.37  ? 675  GLY   D C   1 
ATOM   13204 O  O   . GLY   D  1 374 ? 16.881  13.927  -54.700  1.00 52.73  ? 675  GLY   D O   1 
ATOM   13205 N  N   . GLY   D  1 375 ? 18.772  14.438  -53.607  1.00 46.10  ? 676  GLY   D N   1 
ATOM   13206 C  CA  . GLY   D  1 375 ? 18.857  15.753  -54.197  1.00 51.02  ? 676  GLY   D CA  1 
ATOM   13207 C  C   . GLY   D  1 375 ? 19.605  16.692  -53.278  1.00 51.09  ? 676  GLY   D C   1 
ATOM   13208 O  O   . GLY   D  1 375 ? 20.037  16.329  -52.184  1.00 45.19  ? 676  GLY   D O   1 
ATOM   13209 N  N   . CYS   D  1 376 ? 19.745  17.909  -53.753  1.00 47.49  ? 677  CYS   D N   1 
ATOM   13210 C  CA  . CYS   D  1 376 ? 20.420  18.952  -53.012  1.00 40.48  ? 677  CYS   D CA  1 
ATOM   13211 C  C   . CYS   D  1 376 ? 20.083  20.280  -53.662  1.00 43.74  ? 677  CYS   D C   1 
ATOM   13212 O  O   . CYS   D  1 376 ? 20.623  20.597  -54.722  1.00 49.09  ? 677  CYS   D O   1 
ATOM   13213 C  CB  . CYS   D  1 376 ? 21.924  18.711  -53.003  1.00 37.84  ? 677  CYS   D CB  1 
ATOM   13214 S  SG  . CYS   D  1 376 ? 22.855  20.073  -52.310  1.00 40.06  ? 677  CYS   D SG  1 
ATOM   13215 N  N   . PRO   D  1 377 ? 19.203  21.077  -53.080  1.00 41.93  ? 678  PRO   D N   1 
ATOM   13216 C  CA  . PRO   D  1 377 ? 18.800  22.313  -53.756  1.00 35.83  ? 678  PRO   D CA  1 
ATOM   13217 C  C   . PRO   D  1 377 ? 19.956  23.299  -53.771  1.00 41.93  ? 678  PRO   D C   1 
ATOM   13218 O  O   . PRO   D  1 377 ? 20.681  23.447  -52.785  1.00 41.71  ? 678  PRO   D O   1 
ATOM   13219 C  CB  . PRO   D  1 377 ? 17.627  22.814  -52.907  1.00 38.72  ? 678  PRO   D CB  1 
ATOM   13220 C  CG  . PRO   D  1 377 ? 17.952  22.301  -51.518  1.00 36.20  ? 678  PRO   D CG  1 
ATOM   13221 C  CD  . PRO   D  1 377 ? 18.740  21.021  -51.680  1.00 31.55  ? 678  PRO   D CD  1 
ATOM   13222 N  N   . ALA   D  1 378 ? 20.146  23.956  -54.915  1.00 43.44  ? 679  ALA   D N   1 
ATOM   13223 C  CA  . ALA   D  1 378 ? 21.343  24.762  -55.126  1.00 42.81  ? 679  ALA   D CA  1 
ATOM   13224 C  C   . ALA   D  1 378 ? 21.023  25.934  -56.039  1.00 40.78  ? 679  ALA   D C   1 
ATOM   13225 O  O   . ALA   D  1 378 ? 20.279  25.789  -57.015  1.00 34.11  ? 679  ALA   D O   1 
ATOM   13226 C  CB  . ALA   D  1 378 ? 22.486  23.930  -55.727  1.00 38.72  ? 679  ALA   D CB  1 
ATOM   13227 N  N   . ASP   D  1 379 ? 21.601  27.086  -55.716  1.00 34.28  ? 680  ASP   D N   1 
ATOM   13228 C  CA  . ASP   D  1 379 ? 21.373  28.330  -56.445  1.00 33.88  ? 680  ASP   D CA  1 
ATOM   13229 C  C   . ASP   D  1 379 ? 22.676  28.709  -57.140  1.00 38.25  ? 680  ASP   D C   1 
ATOM   13230 O  O   . ASP   D  1 379 ? 23.557  29.340  -56.541  1.00 37.59  ? 680  ASP   D O   1 
ATOM   13231 C  CB  . ASP   D  1 379 ? 20.875  29.430  -55.514  1.00 39.34  ? 680  ASP   D CB  1 
ATOM   13232 C  CG  . ASP   D  1 379 ? 20.438  30.679  -56.261  1.00 46.21  ? 680  ASP   D CG  1 
ATOM   13233 O  OD1 . ASP   D  1 379 ? 20.828  30.854  -57.445  1.00 48.22  ? 680  ASP   D OD1 1 
ATOM   13234 O  OD2 . ASP   D  1 379 ? 19.709  31.491  -55.661  1.00 42.01  ? 680  ASP   D OD2 1 
ATOM   13235 N  N   . TRP   D  1 380 ? 22.760  28.328  -58.421  1.00 32.91  ? 681  TRP   D N   1 
ATOM   13236 C  CA  . TRP   D  1 380 ? 23.932  28.555  -59.266  1.00 28.42  ? 681  TRP   D CA  1 
ATOM   13237 C  C   . TRP   D  1 380 ? 24.391  30.013  -59.235  1.00 22.79  ? 681  TRP   D C   1 
ATOM   13238 O  O   . TRP   D  1 380 ? 25.587  30.300  -59.144  1.00 25.70  ? 681  TRP   D O   1 
ATOM   13239 C  CB  . TRP   D  1 380 ? 23.557  28.129  -60.700  1.00 30.53  ? 681  TRP   D CB  1 
ATOM   13240 C  CG  . TRP   D  1 380 ? 24.686  27.972  -61.677  1.00 32.30  ? 681  TRP   D CG  1 
ATOM   13241 C  CD1 . TRP   D  1 380 ? 25.274  26.792  -62.072  1.00 23.82  ? 681  TRP   D CD1 1 
ATOM   13242 C  CD2 . TRP   D  1 380 ? 25.357  29.017  -62.400  1.00 30.67  ? 681  TRP   D CD2 1 
ATOM   13243 N  NE1 . TRP   D  1 380 ? 26.271  27.048  -62.986  1.00 38.60  ? 681  TRP   D NE1 1 
ATOM   13244 C  CE2 . TRP   D  1 380 ? 26.332  28.398  -63.222  1.00 30.24  ? 681  TRP   D CE2 1 
ATOM   13245 C  CE3 . TRP   D  1 380 ? 25.227  30.410  -62.437  1.00 28.55  ? 681  TRP   D CE3 1 
ATOM   13246 C  CZ2 . TRP   D  1 380 ? 27.181  29.125  -64.058  1.00 31.80  ? 681  TRP   D CZ2 1 
ATOM   13247 C  CZ3 . TRP   D  1 380 ? 26.070  31.144  -63.294  1.00 32.79  ? 681  TRP   D CZ3 1 
ATOM   13248 C  CH2 . TRP   D  1 380 ? 27.038  30.493  -64.085  1.00 37.40  ? 681  TRP   D CH2 1 
ATOM   13249 N  N   . VAL   D  1 381 ? 23.446  30.945  -59.370  1.00 33.33  ? 682  VAL   D N   1 
ATOM   13250 C  CA  . VAL   D  1 381 ? 23.739  32.373  -59.343  1.00 32.05  ? 682  VAL   D CA  1 
ATOM   13251 C  C   . VAL   D  1 381 ? 24.537  32.759  -58.109  1.00 34.73  ? 682  VAL   D C   1 
ATOM   13252 O  O   . VAL   D  1 381 ? 25.363  33.680  -58.153  1.00 37.23  ? 682  VAL   D O   1 
ATOM   13253 C  CB  . VAL   D  1 381 ? 22.411  33.148  -59.432  1.00 30.53  ? 682  VAL   D CB  1 
ATOM   13254 C  CG1 . VAL   D  1 381 ? 22.648  34.632  -59.388  1.00 31.03  ? 682  VAL   D CG1 1 
ATOM   13255 C  CG2 . VAL   D  1 381 ? 21.646  32.745  -60.692  1.00 29.83  ? 682  VAL   D CG2 1 
ATOM   13256 N  N   . TRP   D  1 382 ? 24.306  32.071  -56.990  1.00 39.94  ? 683  TRP   D N   1 
ATOM   13257 C  CA  . TRP   D  1 382 ? 25.049  32.300  -55.756  1.00 37.28  ? 683  TRP   D CA  1 
ATOM   13258 C  C   . TRP   D  1 382 ? 26.195  31.318  -55.552  1.00 30.85  ? 683  TRP   D C   1 
ATOM   13259 O  O   . TRP   D  1 382 ? 27.208  31.692  -54.955  1.00 33.57  ? 683  TRP   D O   1 
ATOM   13260 C  CB  . TRP   D  1 382 ? 24.102  32.235  -54.542  1.00 36.73  ? 683  TRP   D CB  1 
ATOM   13261 C  CG  . TRP   D  1 382 ? 23.328  33.492  -54.375  1.00 38.02  ? 683  TRP   D CG  1 
ATOM   13262 C  CD1 . TRP   D  1 382 ? 22.410  34.014  -55.243  1.00 40.15  ? 683  TRP   D CD1 1 
ATOM   13263 C  CD2 . TRP   D  1 382 ? 23.419  34.412  -53.289  1.00 43.78  ? 683  TRP   D CD2 1 
ATOM   13264 N  NE1 . TRP   D  1 382 ? 21.924  35.200  -54.762  1.00 40.38  ? 683  TRP   D NE1 1 
ATOM   13265 C  CE2 . TRP   D  1 382 ? 22.521  35.465  -53.557  1.00 49.46  ? 683  TRP   D CE2 1 
ATOM   13266 C  CE3 . TRP   D  1 382 ? 24.164  34.445  -52.105  1.00 46.44  ? 683  TRP   D CE3 1 
ATOM   13267 C  CZ2 . TRP   D  1 382 ? 22.350  36.543  -52.685  1.00 55.34  ? 683  TRP   D CZ2 1 
ATOM   13268 C  CZ3 . TRP   D  1 382 ? 23.994  35.521  -51.236  1.00 49.16  ? 683  TRP   D CZ3 1 
ATOM   13269 C  CH2 . TRP   D  1 382 ? 23.095  36.552  -51.534  1.00 47.76  ? 683  TRP   D CH2 1 
ATOM   13270 N  N   . ILE   D  1 383 ? 26.067  30.071  -56.027  1.00 30.27  ? 684  ILE   D N   1 
ATOM   13271 C  CA  . ILE   D  1 383 ? 27.123  29.085  -55.789  1.00 32.13  ? 684  ILE   D CA  1 
ATOM   13272 C  C   . ILE   D  1 383 ? 28.371  29.404  -56.619  1.00 39.27  ? 684  ILE   D C   1 
ATOM   13273 O  O   . ILE   D  1 383 ? 29.498  29.207  -56.152  1.00 41.95  ? 684  ILE   D O   1 
ATOM   13274 C  CB  . ILE   D  1 383 ? 26.601  27.663  -56.062  1.00 30.07  ? 684  ILE   D CB  1 
ATOM   13275 C  CG1 . ILE   D  1 383 ? 25.441  27.313  -55.127  1.00 33.45  ? 684  ILE   D CG1 1 
ATOM   13276 C  CG2 . ILE   D  1 383 ? 27.718  26.638  -55.915  1.00 31.02  ? 684  ILE   D CG2 1 
ATOM   13277 C  CD1 . ILE   D  1 383 ? 25.827  27.314  -53.631  1.00 37.25  ? 684  ILE   D CD1 1 
ATOM   13278 N  N   . VAL   D  1 384 ? 28.203  29.901  -57.849  1.00 39.15  ? 685  VAL   D N   1 
ATOM   13279 C  CA  . VAL   D  1 384 ? 29.378  30.195  -58.691  1.00 38.51  ? 685  VAL   D CA  1 
ATOM   13280 C  C   . VAL   D  1 384 ? 30.134  31.388  -58.110  1.00 30.73  ? 685  VAL   D C   1 
ATOM   13281 O  O   . VAL   D  1 384 ? 29.518  32.432  -57.829  1.00 34.95  ? 685  VAL   D O   1 
ATOM   13282 C  CB  . VAL   D  1 384 ? 28.950  30.458  -60.150  1.00 42.71  ? 685  VAL   D CB  1 
ATOM   13283 C  CG1 . VAL   D  1 384 ? 30.129  30.985  -60.993  1.00 23.68  ? 685  VAL   D CG1 1 
ATOM   13284 C  CG2 . VAL   D  1 384 ? 28.407  29.185  -60.765  1.00 43.45  ? 685  VAL   D CG2 1 
ATOM   13285 N  N   . PRO   D  1 385 ? 31.441  31.280  -57.890  1.00 34.64  ? 686  PRO   D N   1 
ATOM   13286 C  CA  . PRO   D  1 385 ? 32.192  32.373  -57.244  1.00 34.17  ? 686  PRO   D CA  1 
ATOM   13287 C  C   . PRO   D  1 385 ? 32.170  33.632  -58.091  1.00 41.77  ? 686  PRO   D C   1 
ATOM   13288 O  O   . PRO   D  1 385 ? 32.015  33.559  -59.316  1.00 43.28  ? 686  PRO   D O   1 
ATOM   13289 C  CB  . PRO   D  1 385 ? 33.615  31.810  -57.131  1.00 26.51  ? 686  PRO   D CB  1 
ATOM   13290 C  CG  . PRO   D  1 385 ? 33.436  30.327  -57.150  1.00 39.05  ? 686  PRO   D CG  1 
ATOM   13291 C  CD  . PRO   D  1 385 ? 32.221  30.036  -57.977  1.00 38.59  ? 686  PRO   D CD  1 
ATOM   13292 N  N   . PRO   D  1 386 ? 32.361  34.803  -57.480  1.00 41.70  ? 687  PRO   D N   1 
ATOM   13293 C  CA  . PRO   D  1 386 ? 32.270  36.068  -58.223  1.00 38.40  ? 687  PRO   D CA  1 
ATOM   13294 C  C   . PRO   D  1 386 ? 33.482  36.396  -59.087  1.00 38.45  ? 687  PRO   D C   1 
ATOM   13295 O  O   . PRO   D  1 386 ? 33.512  37.485  -59.676  1.00 36.55  ? 687  PRO   D O   1 
ATOM   13296 C  CB  . PRO   D  1 386 ? 32.128  37.099  -57.098  1.00 38.03  ? 687  PRO   D CB  1 
ATOM   13297 C  CG  . PRO   D  1 386 ? 32.976  36.511  -56.019  1.00 36.34  ? 687  PRO   D CG  1 
ATOM   13298 C  CD  . PRO   D  1 386 ? 32.725  35.022  -56.070  1.00 33.89  ? 687  PRO   D CD  1 
ATOM   13299 N  N   . MET   D  1 387 ? 34.482  35.516  -59.166  1.00 40.74  ? 688  MET   D N   1 
ATOM   13300 C  CA  . MET   D  1 387 ? 35.580  35.656  -60.115  1.00 36.62  ? 688  MET   D CA  1 
ATOM   13301 C  C   . MET   D  1 387 ? 35.932  34.272  -60.636  1.00 44.49  ? 688  MET   D C   1 
ATOM   13302 O  O   . MET   D  1 387 ? 35.623  33.258  -60.001  1.00 38.75  ? 688  MET   D O   1 
ATOM   13303 C  CB  . MET   D  1 387 ? 36.821  36.308  -59.483  1.00 36.75  ? 688  MET   D CB  1 
ATOM   13304 C  CG  . MET   D  1 387 ? 37.536  35.426  -58.444  1.00 43.82  ? 688  MET   D CG  1 
ATOM   13305 S  SD  . MET   D  1 387 ? 39.129  36.087  -57.866  1.00 46.65  ? 688  MET   D SD  1 
ATOM   13306 C  CE  . MET   D  1 387 ? 40.169  35.864  -59.315  1.00 48.38  ? 688  MET   D CE  1 
ATOM   13307 N  N   . SER   D  1 388 ? 36.576  34.234  -61.811  1.00 42.71  ? 689  SER   D N   1 
ATOM   13308 C  CA  . SER   D  1 388 ? 37.086  32.978  -62.378  1.00 35.25  ? 689  SER   D CA  1 
ATOM   13309 C  C   . SER   D  1 388 ? 36.020  31.884  -62.427  1.00 35.76  ? 689  SER   D C   1 
ATOM   13310 O  O   . SER   D  1 388 ? 36.311  30.705  -62.224  1.00 41.75  ? 689  SER   D O   1 
ATOM   13311 C  CB  . SER   D  1 388 ? 38.297  32.473  -61.596  1.00 35.68  ? 689  SER   D CB  1 
ATOM   13312 O  OG  . SER   D  1 388 ? 39.267  33.480  -61.426  1.00 43.08  ? 689  SER   D OG  1 
ATOM   13313 N  N   . GLY   D  1 389 ? 34.779  32.279  -62.713  1.00 33.79  ? 690  GLY   D N   1 
ATOM   13314 C  CA  . GLY   D  1 389 ? 33.657  31.357  -62.606  1.00 32.04  ? 690  GLY   D CA  1 
ATOM   13315 C  C   . GLY   D  1 389 ? 33.849  30.045  -63.351  1.00 42.06  ? 690  GLY   D C   1 
ATOM   13316 O  O   . GLY   D  1 389 ? 33.754  28.964  -62.759  1.00 36.84  ? 690  GLY   D O   1 
ATOM   13317 N  N   . SER   D  1 390 ? 34.114  30.110  -64.672  1.00 34.52  ? 691  SER   D N   1 
ATOM   13318 C  CA  . SER   D  1 390 ? 34.112  28.863  -65.433  1.00 34.91  ? 691  SER   D CA  1 
ATOM   13319 C  C   . SER   D  1 390 ? 35.360  28.013  -65.217  1.00 37.89  ? 691  SER   D C   1 
ATOM   13320 O  O   . SER   D  1 390 ? 35.381  26.857  -65.646  1.00 43.32  ? 691  SER   D O   1 
ATOM   13321 C  CB  . SER   D  1 390 ? 33.924  29.127  -66.934  1.00 37.16  ? 691  SER   D CB  1 
ATOM   13322 O  OG  . SER   D  1 390 ? 35.073  29.711  -67.490  1.00 31.55  ? 691  SER   D OG  1 
ATOM   13323 N  N   . ILE   D  1 391 ? 36.391  28.511  -64.546  1.00 43.89  ? 692  ILE   D N   1 
ATOM   13324 C  CA  . ILE   D  1 391 ? 37.484  27.600  -64.248  1.00 43.79  ? 692  ILE   D CA  1 
ATOM   13325 C  C   . ILE   D  1 391 ? 37.258  26.933  -62.891  1.00 34.59  ? 692  ILE   D C   1 
ATOM   13326 O  O   . ILE   D  1 391 ? 38.147  26.241  -62.388  1.00 35.71  ? 692  ILE   D O   1 
ATOM   13327 C  CB  . ILE   D  1 391 ? 38.856  28.292  -64.300  1.00 47.36  ? 692  ILE   D CB  1 
ATOM   13328 C  CG1 . ILE   D  1 391 ? 38.979  29.333  -63.201  1.00 46.86  ? 692  ILE   D CG1 1 
ATOM   13329 C  CG2 . ILE   D  1 391 ? 39.126  28.846  -65.708  1.00 45.54  ? 692  ILE   D CG2 1 
ATOM   13330 C  CD1 . ILE   D  1 391 ? 40.402  29.665  -62.868  1.00 43.85  ? 692  ILE   D CD1 1 
ATOM   13331 N  N   . THR   D  1 392 ? 36.054  27.092  -62.311  1.00 34.86  ? 693  THR   D N   1 
ATOM   13332 C  CA  . THR   D  1 392 ? 35.715  26.306  -61.129  1.00 43.18  ? 693  THR   D CA  1 
ATOM   13333 C  C   . THR   D  1 392 ? 34.654  25.273  -61.489  1.00 41.59  ? 693  THR   D C   1 
ATOM   13334 O  O   . THR   D  1 392 ? 33.848  25.500  -62.398  1.00 40.55  ? 693  THR   D O   1 
ATOM   13335 C  CB  . THR   D  1 392 ? 35.218  27.168  -59.957  1.00 40.27  ? 693  THR   D CB  1 
ATOM   13336 O  OG1 . THR   D  1 392 ? 33.907  27.675  -60.230  1.00 42.17  ? 693  THR   D OG1 1 
ATOM   13337 C  CG2 . THR   D  1 392 ? 36.157  28.321  -59.742  1.00 36.32  ? 693  THR   D CG2 1 
ATOM   13338 N  N   . PRO   D  1 393 ? 34.635  24.117  -60.817  1.00 38.25  ? 694  PRO   D N   1 
ATOM   13339 C  CA  . PRO   D  1 393 ? 33.784  23.016  -61.302  1.00 40.07  ? 694  PRO   D CA  1 
ATOM   13340 C  C   . PRO   D  1 393 ? 32.293  23.266  -61.171  1.00 42.06  ? 694  PRO   D C   1 
ATOM   13341 O  O   . PRO   D  1 393 ? 31.541  22.674  -61.950  1.00 40.25  ? 694  PRO   D O   1 
ATOM   13342 C  CB  . PRO   D  1 393 ? 34.228  21.819  -60.456  1.00 34.86  ? 694  PRO   D CB  1 
ATOM   13343 C  CG  . PRO   D  1 393 ? 34.825  22.435  -59.232  1.00 40.43  ? 694  PRO   D CG  1 
ATOM   13344 C  CD  . PRO   D  1 393 ? 35.500  23.692  -59.707  1.00 34.87  ? 694  PRO   D CD  1 
ATOM   13345 N  N   . VAL   D  1 394 ? 31.836  24.121  -60.243  1.00 43.42  ? 695  VAL   D N   1 
ATOM   13346 C  CA  . VAL   D  1 394 ? 30.400  24.383  -60.129  1.00 40.82  ? 695  VAL   D CA  1 
ATOM   13347 C  C   . VAL   D  1 394 ? 29.835  25.100  -61.365  1.00 38.24  ? 695  VAL   D C   1 
ATOM   13348 O  O   . VAL   D  1 394 ? 28.630  24.984  -61.653  1.00 27.49  ? 695  VAL   D O   1 
ATOM   13349 C  CB  . VAL   D  1 394 ? 30.076  25.195  -58.857  1.00 43.14  ? 695  VAL   D CB  1 
ATOM   13350 C  CG1 . VAL   D  1 394 ? 30.273  24.349  -57.578  1.00 34.33  ? 695  VAL   D CG1 1 
ATOM   13351 C  CG2 . VAL   D  1 394 ? 30.903  26.456  -58.795  1.00 23.32  ? 695  VAL   D CG2 1 
ATOM   13352 N  N   . PHE   D  1 395 ? 30.666  25.839  -62.111  1.00 35.00  ? 696  PHE   D N   1 
ATOM   13353 C  CA  . PHE   D  1 395 ? 30.155  26.544  -63.293  1.00 30.57  ? 696  PHE   D CA  1 
ATOM   13354 C  C   . PHE   D  1 395 ? 29.502  25.583  -64.282  1.00 37.98  ? 696  PHE   D C   1 
ATOM   13355 O  O   . PHE   D  1 395 ? 28.468  25.902  -64.885  1.00 40.66  ? 696  PHE   D O   1 
ATOM   13356 C  CB  . PHE   D  1 395 ? 31.281  27.328  -63.968  1.00 33.18  ? 696  PHE   D CB  1 
ATOM   13357 C  CG  . PHE   D  1 395 ? 30.848  28.103  -65.179  1.00 39.34  ? 696  PHE   D CG  1 
ATOM   13358 C  CD1 . PHE   D  1 395 ? 30.768  27.493  -66.432  1.00 40.15  ? 696  PHE   D CD1 1 
ATOM   13359 C  CD2 . PHE   D  1 395 ? 30.548  29.445  -65.077  1.00 34.25  ? 696  PHE   D CD2 1 
ATOM   13360 C  CE1 . PHE   D  1 395 ? 30.362  28.210  -67.554  1.00 38.32  ? 696  PHE   D CE1 1 
ATOM   13361 C  CE2 . PHE   D  1 395 ? 30.147  30.174  -66.203  1.00 38.57  ? 696  PHE   D CE2 1 
ATOM   13362 C  CZ  . PHE   D  1 395 ? 30.055  29.546  -67.439  1.00 36.88  ? 696  PHE   D CZ  1 
ATOM   13363 N  N   . HIS   D  1 396 ? 30.070  24.392  -64.443  1.00 41.41  ? 697  HIS   D N   1 
ATOM   13364 C  CA  . HIS   D  1 396 ? 29.596  23.433  -65.433  1.00 36.83  ? 697  HIS   D CA  1 
ATOM   13365 C  C   . HIS   D  1 396 ? 28.606  22.433  -64.867  1.00 41.28  ? 697  HIS   D C   1 
ATOM   13366 O  O   . HIS   D  1 396 ? 28.211  21.498  -65.585  1.00 30.97  ? 697  HIS   D O   1 
ATOM   13367 C  CB  . HIS   D  1 396 ? 30.785  22.703  -66.035  1.00 36.83  ? 697  HIS   D CB  1 
ATOM   13368 C  CG  . HIS   D  1 396 ? 31.927  23.611  -66.329  1.00 38.79  ? 697  HIS   D CG  1 
ATOM   13369 N  ND1 . HIS   D  1 396 ? 32.102  24.207  -67.556  1.00 39.60  ? 697  HIS   D ND1 1 
ATOM   13370 C  CD2 . HIS   D  1 396 ? 32.919  24.079  -65.534  1.00 41.14  ? 697  HIS   D CD2 1 
ATOM   13371 C  CE1 . HIS   D  1 396 ? 33.172  24.981  -67.516  1.00 43.65  ? 697  HIS   D CE1 1 
ATOM   13372 N  NE2 . HIS   D  1 396 ? 33.684  24.925  -66.298  1.00 37.21  ? 697  HIS   D NE2 1 
ATOM   13373 N  N   . GLN   D  1 397 ? 28.185  22.627  -63.615  1.00 36.44  ? 698  GLN   D N   1 
ATOM   13374 C  CA  . GLN   D  1 397 ? 27.264  21.732  -62.926  1.00 35.26  ? 698  GLN   D CA  1 
ATOM   13375 C  C   . GLN   D  1 397 ? 25.842  22.287  -62.969  1.00 36.97  ? 698  GLN   D C   1 
ATOM   13376 O  O   . GLN   D  1 397 ? 25.563  23.334  -62.373  1.00 43.30  ? 698  GLN   D O   1 
ATOM   13377 C  CB  . GLN   D  1 397 ? 27.691  21.549  -61.470  1.00 38.61  ? 698  GLN   D CB  1 
ATOM   13378 C  CG  . GLN   D  1 397 ? 26.701  20.732  -60.687  1.00 40.08  ? 698  GLN   D CG  1 
ATOM   13379 C  CD  . GLN   D  1 397 ? 26.721  19.284  -61.110  1.00 37.48  ? 698  GLN   D CD  1 
ATOM   13380 O  OE1 . GLN   D  1 397 ? 27.788  18.672  -61.191  1.00 40.99  ? 698  GLN   D OE1 1 
ATOM   13381 N  NE2 . GLN   D  1 397 ? 25.546  18.720  -61.375  1.00 34.59  ? 698  GLN   D NE2 1 
ATOM   13382 N  N   . GLU   D  1 398 ? 24.937  21.561  -63.623  1.00 33.40  ? 699  GLU   D N   1 
ATOM   13383 C  CA  . GLU   D  1 398 ? 23.517  21.878  -63.531  1.00 32.90  ? 699  GLU   D CA  1 
ATOM   13384 C  C   . GLU   D  1 398 ? 23.004  21.674  -62.100  1.00 39.43  ? 699  GLU   D C   1 
ATOM   13385 O  O   . GLU   D  1 398 ? 23.380  20.718  -61.417  1.00 30.53  ? 699  GLU   D O   1 
ATOM   13386 C  CB  . GLU   D  1 398 ? 22.717  21.013  -64.503  1.00 32.39  ? 699  GLU   D CB  1 
ATOM   13387 C  CG  . GLU   D  1 398 ? 22.674  21.563  -65.924  1.00 33.17  ? 699  GLU   D CG  1 
ATOM   13388 C  CD  . GLU   D  1 398 ? 21.980  20.627  -66.895  1.00 43.35  ? 699  GLU   D CD  1 
ATOM   13389 O  OE1 . GLU   D  1 398 ? 21.815  21.016  -68.083  1.00 48.65  ? 699  GLU   D OE1 1 
ATOM   13390 O  OE2 . GLU   D  1 398 ? 21.607  19.505  -66.475  1.00 41.93  ? 699  GLU   D OE2 1 
ATOM   13391 N  N   . MET   D  1 399 ? 22.122  22.573  -61.661  1.00 42.21  ? 700  MET   D N   1 
ATOM   13392 C  CA  . MET   D  1 399 ? 21.628  22.610  -60.287  1.00 38.64  ? 700  MET   D CA  1 
ATOM   13393 C  C   . MET   D  1 399 ? 20.130  22.873  -60.263  1.00 40.44  ? 700  MET   D C   1 
ATOM   13394 O  O   . MET   D  1 399 ? 19.635  23.754  -60.971  1.00 49.14  ? 700  MET   D O   1 
ATOM   13395 C  CB  . MET   D  1 399 ? 22.319  23.705  -59.480  1.00 32.27  ? 700  MET   D CB  1 
ATOM   13396 C  CG  . MET   D  1 399 ? 23.762  23.439  -59.182  1.00 31.01  ? 700  MET   D CG  1 
ATOM   13397 S  SD  . MET   D  1 399 ? 24.488  24.974  -58.633  1.00 38.03  ? 700  MET   D SD  1 
ATOM   13398 C  CE  . MET   D  1 399 ? 26.245  24.609  -58.796  1.00 30.78  ? 700  MET   D CE  1 
ATOM   13399 N  N   . LEU   D  1 400 ? 19.409  22.121  -59.440  1.00 34.60  ? 701  LEU   D N   1 
ATOM   13400 C  CA  . LEU   D  1 400 ? 17.988  22.363  -59.229  1.00 41.59  ? 701  LEU   D CA  1 
ATOM   13401 C  C   . LEU   D  1 400 ? 17.789  23.166  -57.952  1.00 42.34  ? 701  LEU   D C   1 
ATOM   13402 O  O   . LEU   D  1 400 ? 18.338  22.812  -56.899  1.00 30.82  ? 701  LEU   D O   1 
ATOM   13403 C  CB  . LEU   D  1 400 ? 17.215  21.051  -59.139  1.00 40.60  ? 701  LEU   D CB  1 
ATOM   13404 C  CG  . LEU   D  1 400 ? 17.048  20.324  -60.451  1.00 39.63  ? 701  LEU   D CG  1 
ATOM   13405 C  CD1 . LEU   D  1 400 ? 16.326  19.045  -60.156  1.00 44.85  ? 701  LEU   D CD1 1 
ATOM   13406 C  CD2 . LEU   D  1 400 ? 16.284  21.215  -61.430  1.00 34.40  ? 701  LEU   D CD2 1 
ATOM   13407 N  N   . ASN   D  1 401 ? 16.995  24.230  -58.042  1.00 45.24  ? 702  ASN   D N   1 
ATOM   13408 C  CA  . ASN   D  1 401 ? 16.741  25.106  -56.908  1.00 42.66  ? 702  ASN   D CA  1 
ATOM   13409 C  C   . ASN   D  1 401 ? 15.297  24.957  -56.443  1.00 46.22  ? 702  ASN   D C   1 
ATOM   13410 O  O   . ASN   D  1 401 ? 14.371  25.029  -57.258  1.00 38.51  ? 702  ASN   D O   1 
ATOM   13411 C  CB  . ASN   D  1 401 ? 17.035  26.564  -57.258  1.00 31.83  ? 702  ASN   D CB  1 
ATOM   13412 C  CG  . ASN   D  1 401 ? 17.093  27.435  -56.046  1.00 41.18  ? 702  ASN   D CG  1 
ATOM   13413 O  OD1 . ASN   D  1 401 ? 17.298  26.942  -54.940  1.00 46.29  ? 702  ASN   D OD1 1 
ATOM   13414 N  ND2 . ASN   D  1 401 ? 16.893  28.731  -56.226  1.00 40.42  ? 702  ASN   D ND2 1 
ATOM   13415 N  N   . TYR   D  1 402 ? 15.117  24.744  -55.134  1.00 39.87  ? 703  TYR   D N   1 
ATOM   13416 C  CA  . TYR   D  1 402 ? 13.804  24.636  -54.510  1.00 32.40  ? 703  TYR   D CA  1 
ATOM   13417 C  C   . TYR   D  1 402 ? 13.976  24.815  -53.004  1.00 43.46  ? 703  TYR   D C   1 
ATOM   13418 O  O   . TYR   D  1 402 ? 15.091  24.760  -52.478  1.00 42.05  ? 703  TYR   D O   1 
ATOM   13419 C  CB  . TYR   D  1 402 ? 13.112  23.308  -54.842  1.00 34.74  ? 703  TYR   D CB  1 
ATOM   13420 C  CG  . TYR   D  1 402 ? 13.994  22.099  -54.688  1.00 40.53  ? 703  TYR   D CG  1 
ATOM   13421 C  CD1 . TYR   D  1 402 ? 14.077  21.423  -53.469  1.00 34.58  ? 703  TYR   D CD1 1 
ATOM   13422 C  CD2 . TYR   D  1 402 ? 14.748  21.625  -55.755  1.00 35.20  ? 703  TYR   D CD2 1 
ATOM   13423 C  CE1 . TYR   D  1 402 ? 14.889  20.309  -53.313  1.00 38.01  ? 703  TYR   D CE1 1 
ATOM   13424 C  CE2 . TYR   D  1 402 ? 15.564  20.514  -55.618  1.00 37.69  ? 703  TYR   D CE2 1 
ATOM   13425 C  CZ  . TYR   D  1 402 ? 15.633  19.855  -54.393  1.00 43.49  ? 703  TYR   D CZ  1 
ATOM   13426 O  OH  . TYR   D  1 402 ? 16.439  18.744  -54.261  1.00 36.23  ? 703  TYR   D OH  1 
ATOM   13427 N  N   . ARG   D  1 403 ? 12.859  25.054  -52.320  1.00 38.11  ? 704  ARG   D N   1 
ATOM   13428 C  CA  . ARG   D  1 403 ? 12.870  25.585  -50.961  1.00 42.20  ? 704  ARG   D CA  1 
ATOM   13429 C  C   . ARG   D  1 403 ? 12.324  24.522  -50.010  1.00 42.75  ? 704  ARG   D C   1 
ATOM   13430 O  O   . ARG   D  1 403 ? 11.120  24.245  -50.004  1.00 42.67  ? 704  ARG   D O   1 
ATOM   13431 C  CB  . ARG   D  1 403 ? 12.067  26.881  -50.892  1.00 44.01  ? 704  ARG   D CB  1 
ATOM   13432 C  CG  . ARG   D  1 403 ? 12.077  27.564  -49.544  1.00 64.49  ? 704  ARG   D CG  1 
ATOM   13433 C  CD  . ARG   D  1 403 ? 11.586  29.015  -49.623  1.00 74.49  ? 704  ARG   D CD  1 
ATOM   13434 N  NE  . ARG   D  1 403 ? 12.645  29.933  -50.040  1.00 86.62  ? 704  ARG   D NE  1 
ATOM   13435 C  CZ  . ARG   D  1 403 ? 13.656  30.322  -49.264  1.00 92.17  ? 704  ARG   D CZ  1 
ATOM   13436 N  NH1 . ARG   D  1 403 ? 13.758  29.869  -48.024  1.00 94.32  ? 704  ARG   D NH1 1 
ATOM   13437 N  NH2 . ARG   D  1 403 ? 14.577  31.161  -49.727  1.00 94.00  ? 704  ARG   D NH2 1 
ATOM   13438 N  N   . LEU   D  1 404 ? 13.219  23.897  -49.248  1.00 36.18  ? 705  LEU   D N   1 
ATOM   13439 C  CA  . LEU   D  1 404 ? 12.836  22.962  -48.197  1.00 34.12  ? 705  LEU   D CA  1 
ATOM   13440 C  C   . LEU   D  1 404 ? 12.857  23.676  -46.848  1.00 38.62  ? 705  LEU   D C   1 
ATOM   13441 O  O   . LEU   D  1 404 ? 13.500  24.718  -46.669  1.00 35.02  ? 705  LEU   D O   1 
ATOM   13442 C  CB  . LEU   D  1 404 ? 13.774  21.752  -48.129  1.00 28.20  ? 705  LEU   D CB  1 
ATOM   13443 C  CG  . LEU   D  1 404 ? 14.034  20.907  -49.368  1.00 40.30  ? 705  LEU   D CG  1 
ATOM   13444 C  CD1 . LEU   D  1 404 ? 15.199  19.953  -49.109  1.00 39.54  ? 705  LEU   D CD1 1 
ATOM   13445 C  CD2 . LEU   D  1 404 ? 12.779  20.152  -49.766  1.00 46.40  ? 705  LEU   D CD2 1 
ATOM   13446 N  N   . THR   D  1 405 ? 12.176  23.076  -45.887  1.00 42.02  ? 706  THR   D N   1 
ATOM   13447 C  CA  . THR   D  1 405 ? 12.186  23.594  -44.532  1.00 41.03  ? 706  THR   D CA  1 
ATOM   13448 C  C   . THR   D  1 405 ? 12.630  22.501  -43.557  1.00 36.25  ? 706  THR   D C   1 
ATOM   13449 O  O   . THR   D  1 405 ? 12.446  21.311  -43.842  1.00 27.47  ? 706  THR   D O   1 
ATOM   13450 C  CB  . THR   D  1 405 ? 10.796  24.128  -44.168  1.00 41.65  ? 706  THR   D CB  1 
ATOM   13451 O  OG1 . THR   D  1 405 ? 10.826  24.688  -42.852  1.00 50.60  ? 706  THR   D OG1 1 
ATOM   13452 C  CG2 . THR   D  1 405 ? 9.743   23.032  -44.243  1.00 26.56  ? 706  THR   D CG2 1 
ATOM   13453 N  N   . PRO   D  1 406 ? 13.284  22.853  -42.426  1.00 42.41  ? 707  PRO   D N   1 
ATOM   13454 C  CA  . PRO   D  1 406 ? 13.717  24.166  -41.930  1.00 38.02  ? 707  PRO   D CA  1 
ATOM   13455 C  C   . PRO   D  1 406 ? 14.554  24.927  -42.942  1.00 39.52  ? 707  PRO   D C   1 
ATOM   13456 O  O   . PRO   D  1 406 ? 15.266  24.311  -43.728  1.00 39.98  ? 707  PRO   D O   1 
ATOM   13457 C  CB  . PRO   D  1 406 ? 14.568  23.819  -40.705  1.00 38.82  ? 707  PRO   D CB  1 
ATOM   13458 C  CG  . PRO   D  1 406 ? 14.084  22.522  -40.262  1.00 43.70  ? 707  PRO   D CG  1 
ATOM   13459 C  CD  . PRO   D  1 406 ? 13.647  21.777  -41.481  1.00 39.84  ? 707  PRO   D CD  1 
ATOM   13460 N  N   . SER   D  1 407 ? 14.452  26.248  -42.928  1.00 41.88  ? 708  SER   D N   1 
ATOM   13461 C  CA  . SER   D  1 407 ? 15.247  27.072  -43.817  1.00 48.23  ? 708  SER   D CA  1 
ATOM   13462 C  C   . SER   D  1 407 ? 15.626  28.356  -43.102  1.00 43.40  ? 708  SER   D C   1 
ATOM   13463 O  O   . SER   D  1 407 ? 14.980  28.760  -42.133  1.00 50.12  ? 708  SER   D O   1 
ATOM   13464 C  CB  . SER   D  1 407 ? 14.492  27.400  -45.108  1.00 50.74  ? 708  SER   D CB  1 
ATOM   13465 O  OG  . SER   D  1 407 ? 13.431  28.289  -44.840  1.00 53.94  ? 708  SER   D OG  1 
ATOM   13466 N  N   . PHE   D  1 408 ? 16.697  28.980  -43.582  1.00 36.41  ? 709  PHE   D N   1 
ATOM   13467 C  CA  . PHE   D  1 408 ? 17.001  30.361  -43.240  1.00 28.37  ? 709  PHE   D CA  1 
ATOM   13468 C  C   . PHE   D  1 408 ? 16.301  31.277  -44.231  1.00 36.29  ? 709  PHE   D C   1 
ATOM   13469 O  O   . PHE   D  1 408 ? 16.171  30.950  -45.412  1.00 40.16  ? 709  PHE   D O   1 
ATOM   13470 C  CB  . PHE   D  1 408 ? 18.513  30.615  -43.226  1.00 25.79  ? 709  PHE   D CB  1 
ATOM   13471 C  CG  . PHE   D  1 408 ? 19.217  29.960  -42.069  1.00 32.06  ? 709  PHE   D CG  1 
ATOM   13472 C  CD1 . PHE   D  1 408 ? 19.089  30.469  -40.776  1.00 37.40  ? 709  PHE   D CD1 1 
ATOM   13473 C  CD2 . PHE   D  1 408 ? 19.989  28.816  -42.265  1.00 27.57  ? 709  PHE   D CD2 1 
ATOM   13474 C  CE1 . PHE   D  1 408 ? 19.725  29.844  -39.698  1.00 38.22  ? 709  PHE   D CE1 1 
ATOM   13475 C  CE2 . PHE   D  1 408 ? 20.621  28.198  -41.202  1.00 33.26  ? 709  PHE   D CE2 1 
ATOM   13476 C  CZ  . PHE   D  1 408 ? 20.489  28.713  -39.912  1.00 35.55  ? 709  PHE   D CZ  1 
ATOM   13477 N  N   . GLU   D  1 409 ? 15.814  32.404  -43.732  1.00 38.31  ? 710  GLU   D N   1 
ATOM   13478 C  CA  . GLU   D  1 409 ? 14.960  33.306  -44.483  1.00 36.20  ? 710  GLU   D CA  1 
ATOM   13479 C  C   . GLU   D  1 409 ? 15.427  34.731  -44.251  1.00 42.79  ? 710  GLU   D C   1 
ATOM   13480 O  O   . GLU   D  1 409 ? 15.982  35.051  -43.199  1.00 46.17  ? 710  GLU   D O   1 
ATOM   13481 C  CB  . GLU   D  1 409 ? 13.488  33.201  -44.057  1.00 33.39  ? 710  GLU   D CB  1 
ATOM   13482 C  CG  . GLU   D  1 409 ? 12.836  31.846  -44.209  1.00 43.49  ? 710  GLU   D CG  1 
ATOM   13483 C  CD  . GLU   D  1 409 ? 12.576  31.463  -45.669  1.00 58.50  ? 710  GLU   D CD  1 
ATOM   13484 O  OE1 . GLU   D  1 409 ? 12.514  32.365  -46.549  1.00 56.92  ? 710  GLU   D OE1 1 
ATOM   13485 O  OE2 . GLU   D  1 409 ? 12.436  30.246  -45.931  1.00 57.92  ? 710  GLU   D OE2 1 
ATOM   13486 N  N   . TYR   D  1 410 ? 15.171  35.592  -45.228  1.00 42.63  ? 711  TYR   D N   1 
ATOM   13487 C  CA  . TYR   D  1 410 ? 15.375  37.010  -45.015  1.00 46.01  ? 711  TYR   D CA  1 
ATOM   13488 C  C   . TYR   D  1 410 ? 14.202  37.589  -44.246  1.00 40.35  ? 711  TYR   D C   1 
ATOM   13489 O  O   . TYR   D  1 410 ? 13.077  37.100  -44.320  1.00 41.16  ? 711  TYR   D O   1 
ATOM   13490 C  CB  . TYR   D  1 410 ? 15.520  37.765  -46.332  1.00 45.42  ? 711  TYR   D CB  1 
ATOM   13491 C  CG  . TYR   D  1 410 ? 16.581  37.230  -47.246  1.00 55.68  ? 711  TYR   D CG  1 
ATOM   13492 C  CD1 . TYR   D  1 410 ? 17.927  37.447  -46.986  1.00 62.13  ? 711  TYR   D CD1 1 
ATOM   13493 C  CD2 . TYR   D  1 410 ? 16.236  36.528  -48.387  1.00 67.66  ? 711  TYR   D CD2 1 
ATOM   13494 C  CE1 . TYR   D  1 410 ? 18.901  36.966  -47.838  1.00 71.60  ? 711  TYR   D CE1 1 
ATOM   13495 C  CE2 . TYR   D  1 410 ? 17.196  36.049  -49.246  1.00 76.82  ? 711  TYR   D CE2 1 
ATOM   13496 C  CZ  . TYR   D  1 410 ? 18.524  36.270  -48.968  1.00 76.54  ? 711  TYR   D CZ  1 
ATOM   13497 O  OH  . TYR   D  1 410 ? 19.470  35.788  -49.829  1.00 80.83  ? 711  TYR   D OH  1 
ATOM   13498 N  N   . GLN   D  1 411 ? 14.474  38.644  -43.507  1.00 40.38  ? 712  GLN   D N   1 
ATOM   13499 C  CA  . GLN   D  1 411 ? 13.435  39.389  -42.820  1.00 48.09  ? 712  GLN   D CA  1 
ATOM   13500 C  C   . GLN   D  1 411 ? 13.746  40.865  -42.996  1.00 42.31  ? 712  GLN   D C   1 
ATOM   13501 O  O   . GLN   D  1 411 ? 14.898  41.235  -43.248  1.00 43.87  ? 712  GLN   D O   1 
ATOM   13502 C  CB  . GLN   D  1 411 ? 13.360  39.013  -41.328  1.00 43.81  ? 712  GLN   D CB  1 
ATOM   13503 C  CG  . GLN   D  1 411 ? 14.656  39.161  -40.591  1.00 46.79  ? 712  GLN   D CG  1 
ATOM   13504 C  CD  . GLN   D  1 411 ? 14.565  38.668  -39.154  1.00 41.83  ? 712  GLN   D CD  1 
ATOM   13505 O  OE1 . GLN   D  1 411 ? 13.479  38.593  -38.571  1.00 35.08  ? 712  GLN   D OE1 1 
ATOM   13506 N  NE2 . GLN   D  1 411 ? 15.711  38.308  -38.588  1.00 34.59  ? 712  GLN   D NE2 1 
ATOM   13507 N  N   . PRO   D  1 412 ? 12.744  41.729  -42.890  1.00 45.22  ? 713  PRO   D N   1 
ATOM   13508 C  CA  . PRO   D  1 412 ? 13.023  43.162  -42.992  1.00 50.31  ? 713  PRO   D CA  1 
ATOM   13509 C  C   . PRO   D  1 412 ? 13.983  43.614  -41.901  1.00 47.23  ? 713  PRO   D C   1 
ATOM   13510 O  O   . PRO   D  1 412 ? 14.105  42.984  -40.846  1.00 46.57  ? 713  PRO   D O   1 
ATOM   13511 C  CB  . PRO   D  1 412 ? 11.641  43.816  -42.843  1.00 53.71  ? 713  PRO   D CB  1 
ATOM   13512 C  CG  . PRO   D  1 412 ? 10.741  42.752  -42.301  1.00 52.69  ? 713  PRO   D CG  1 
ATOM   13513 C  CD  . PRO   D  1 412 ? 11.307  41.444  -42.755  1.00 49.66  ? 713  PRO   D CD  1 
ATOM   13514 N  N   . ASP   D  1 413 ? 14.702  44.692  -42.204  1.00 49.94  ? 714  ASP   D N   1 
ATOM   13515 C  CA  . ASP   D  1 413 ? 15.574  45.331  -41.234  1.00 49.24  ? 714  ASP   D CA  1 
ATOM   13516 C  C   . ASP   D  1 413 ? 14.754  45.838  -40.052  1.00 57.39  ? 714  ASP   D C   1 
ATOM   13517 O  O   . ASP   D  1 413 ? 13.654  46.375  -40.244  1.00 56.06  ? 714  ASP   D O   1 
ATOM   13518 C  CB  . ASP   D  1 413 ? 16.326  46.492  -41.880  1.00 51.10  ? 714  ASP   D CB  1 
ATOM   13519 C  CG  . ASP   D  1 413 ? 17.325  46.028  -42.916  1.00 59.20  ? 714  ASP   D CG  1 
ATOM   13520 O  OD1 . ASP   D  1 413 ? 17.945  44.966  -42.709  1.00 58.28  ? 714  ASP   D OD1 1 
ATOM   13521 O  OD2 . ASP   D  1 413 ? 17.484  46.723  -43.942  1.00 66.08  ? 714  ASP   D OD2 1 
ATOM   13522 N  N   . PRO   D  1 414 ? 15.268  45.716  -38.822  1.00 53.09  ? 715  PRO   D N   1 
ATOM   13523 C  CA  . PRO   D  1 414 ? 14.420  45.990  -37.654  1.00 52.60  ? 715  PRO   D CA  1 
ATOM   13524 C  C   . PRO   D  1 414 ? 14.013  47.439  -37.550  1.00 52.94  ? 715  PRO   D C   1 
ATOM   13525 O  O   . PRO   D  1 414 ? 12.940  47.732  -37.010  1.00 49.84  ? 715  PRO   D O   1 
ATOM   13526 C  CB  . PRO   D  1 414 ? 15.301  45.577  -36.466  1.00 44.86  ? 715  PRO   D CB  1 
ATOM   13527 C  CG  . PRO   D  1 414 ? 16.504  44.892  -37.057  1.00 42.44  ? 715  PRO   D CG  1 
ATOM   13528 C  CD  . PRO   D  1 414 ? 16.660  45.441  -38.433  1.00 47.60  ? 715  PRO   D CD  1 
ATOM   13529 N  N   . TRP   D  1 415 ? 14.839  48.357  -38.044  1.00 52.88  ? 716  TRP   D N   1 
ATOM   13530 C  CA  . TRP   D  1 415 ? 14.513  49.771  -37.976  1.00 53.05  ? 716  TRP   D CA  1 
ATOM   13531 C  C   . TRP   D  1 415 ? 13.479  50.186  -39.009  1.00 60.22  ? 716  TRP   D C   1 
ATOM   13532 O  O   . TRP   D  1 415 ? 13.077  51.353  -39.030  1.00 62.01  ? 716  TRP   D O   1 
ATOM   13533 C  CB  . TRP   D  1 415 ? 15.780  50.603  -38.138  1.00 52.98  ? 716  TRP   D CB  1 
ATOM   13534 C  CG  . TRP   D  1 415 ? 16.518  50.341  -39.397  1.00 54.79  ? 716  TRP   D CG  1 
ATOM   13535 C  CD1 . TRP   D  1 415 ? 16.290  50.915  -40.618  1.00 55.79  ? 716  TRP   D CD1 1 
ATOM   13536 C  CD2 . TRP   D  1 415 ? 17.630  49.456  -39.571  1.00 52.64  ? 716  TRP   D CD2 1 
ATOM   13537 N  NE1 . TRP   D  1 415 ? 17.187  50.433  -41.543  1.00 53.62  ? 716  TRP   D NE1 1 
ATOM   13538 C  CE2 . TRP   D  1 415 ? 18.021  49.538  -40.925  1.00 56.23  ? 716  TRP   D CE2 1 
ATOM   13539 C  CE3 . TRP   D  1 415 ? 18.334  48.602  -38.715  1.00 56.82  ? 716  TRP   D CE3 1 
ATOM   13540 C  CZ2 . TRP   D  1 415 ? 19.082  48.798  -41.440  1.00 56.88  ? 716  TRP   D CZ2 1 
ATOM   13541 C  CZ3 . TRP   D  1 415 ? 19.386  47.868  -39.229  1.00 58.58  ? 716  TRP   D CZ3 1 
ATOM   13542 C  CH2 . TRP   D  1 415 ? 19.750  47.971  -40.582  1.00 59.25  ? 716  TRP   D CH2 1 
ATOM   13543 N  N   . ASN   D  1 416 ? 13.043  49.271  -39.869  1.00 61.78  ? 717  ASN   D N   1 
ATOM   13544 C  CA  . ASN   D  1 416 ? 11.892  49.532  -40.718  1.00 61.95  ? 717  ASN   D CA  1 
ATOM   13545 C  C   . ASN   D  1 416 ? 10.583  49.116  -40.063  1.00 60.09  ? 717  ASN   D C   1 
ATOM   13546 O  O   . ASN   D  1 416 ? 9.525   49.612  -40.456  1.00 64.99  ? 717  ASN   D O   1 
ATOM   13547 C  CB  . ASN   D  1 416 ? 12.058  48.816  -42.062  1.00 56.83  ? 717  ASN   D CB  1 
ATOM   13548 C  CG  . ASN   D  1 416 ? 13.227  49.359  -42.864  1.00 53.23  ? 717  ASN   D CG  1 
ATOM   13549 O  OD1 . ASN   D  1 416 ? 13.590  50.530  -42.735  1.00 52.61  ? 717  ASN   D OD1 1 
ATOM   13550 N  ND2 . ASN   D  1 416 ? 13.828  48.509  -43.691  1.00 52.71  ? 717  ASN   D ND2 1 
ATOM   13551 N  N   . THR   D  1 417 ? 10.633  48.245  -39.062  1.00 57.86  ? 718  THR   D N   1 
ATOM   13552 C  CA  . THR   D  1 417 ? 9.436   47.764  -38.388  1.00 61.56  ? 718  THR   D CA  1 
ATOM   13553 C  C   . THR   D  1 417 ? 9.302   48.239  -36.952  1.00 62.14  ? 718  THR   D C   1 
ATOM   13554 O  O   . THR   D  1 417 ? 8.178   48.424  -36.486  1.00 67.44  ? 718  THR   D O   1 
ATOM   13555 C  CB  . THR   D  1 417 ? 9.408   46.234  -38.396  1.00 65.86  ? 718  THR   D CB  1 
ATOM   13556 O  OG1 . THR   D  1 417 ? 9.701   45.780  -39.718  1.00 74.17  ? 718  THR   D OG1 1 
ATOM   13557 C  CG2 . THR   D  1 417 ? 8.035   45.729  -38.007  1.00 69.91  ? 718  THR   D CG2 1 
ATOM   13558 N  N   . HIS   D  1 418 ? 10.410  48.452  -36.247  1.00 59.64  ? 719  HIS   D N   1 
ATOM   13559 C  CA  . HIS   D  1 418 ? 10.345  48.717  -34.815  1.00 63.69  ? 719  HIS   D CA  1 
ATOM   13560 C  C   . HIS   D  1 418 ? 9.691   50.062  -34.531  1.00 64.58  ? 719  HIS   D C   1 
ATOM   13561 O  O   . HIS   D  1 418 ? 10.036  51.076  -35.142  1.00 71.74  ? 719  HIS   D O   1 
ATOM   13562 C  CB  . HIS   D  1 418 ? 11.741  48.686  -34.198  1.00 61.09  ? 719  HIS   D CB  1 
ATOM   13563 C  CG  . HIS   D  1 418 ? 11.735  48.900  -32.720  1.00 60.66  ? 719  HIS   D CG  1 
ATOM   13564 N  ND1 . HIS   D  1 418 ? 11.284  47.944  -31.837  1.00 61.48  ? 719  HIS   D ND1 1 
ATOM   13565 C  CD2 . HIS   D  1 418 ? 12.085  49.972  -31.971  1.00 62.11  ? 719  HIS   D CD2 1 
ATOM   13566 C  CE1 . HIS   D  1 418 ? 11.373  48.412  -30.605  1.00 62.76  ? 719  HIS   D CE1 1 
ATOM   13567 N  NE2 . HIS   D  1 418 ? 11.855  49.641  -30.659  1.00 61.34  ? 719  HIS   D NE2 1 
ATOM   13568 N  N   . VAL   D  1 419 ? 8.747   50.072  -33.598  1.00 67.14  ? 720  VAL   D N   1 
ATOM   13569 C  CA  . VAL   D  1 419 ? 8.176   51.312  -33.087  1.00 73.52  ? 720  VAL   D CA  1 
ATOM   13570 C  C   . VAL   D  1 419 ? 8.752   51.567  -31.697  1.00 69.77  ? 720  VAL   D C   1 
ATOM   13571 O  O   . VAL   D  1 419 ? 8.710   50.695  -30.818  1.00 65.64  ? 720  VAL   D O   1 
ATOM   13572 C  CB  . VAL   D  1 419 ? 6.636   51.267  -33.086  1.00 76.07  ? 720  VAL   D CB  1 
ATOM   13573 C  CG1 . VAL   D  1 419 ? 6.115   51.320  -34.523  1.00 71.35  ? 720  VAL   D CG1 1 
ATOM   13574 C  CG2 . VAL   D  1 419 ? 6.109   50.021  -32.368  1.00 72.95  ? 720  VAL   D CG2 1 
ATOM   13575 N  N   . TRP   D  1 420 ? 9.313   52.758  -31.511  1.00 69.06  ? 721  TRP   D N   1 
ATOM   13576 C  CA  . TRP   D  1 420 ? 10.126  53.079  -30.348  1.00 71.01  ? 721  TRP   D CA  1 
ATOM   13577 C  C   . TRP   D  1 420 ? 9.273   53.522  -29.166  1.00 79.33  ? 721  TRP   D C   1 
ATOM   13578 O  O   . TRP   D  1 420 ? 8.241   54.181  -29.327  1.00 81.92  ? 721  TRP   D O   1 
ATOM   13579 C  CB  . TRP   D  1 420 ? 11.128  54.178  -30.699  1.00 66.24  ? 721  TRP   D CB  1 
ATOM   13580 C  CG  . TRP   D  1 420 ? 12.146  53.734  -31.685  1.00 57.11  ? 721  TRP   D CG  1 
ATOM   13581 C  CD1 . TRP   D  1 420 ? 11.985  53.607  -33.043  1.00 55.15  ? 721  TRP   D CD1 1 
ATOM   13582 C  CD2 . TRP   D  1 420 ? 13.488  53.338  -31.402  1.00 49.22  ? 721  TRP   D CD2 1 
ATOM   13583 N  NE1 . TRP   D  1 420 ? 13.149  53.161  -33.617  1.00 41.66  ? 721  TRP   D NE1 1 
ATOM   13584 C  CE2 . TRP   D  1 420 ? 14.088  52.985  -32.634  1.00 46.97  ? 721  TRP   D CE2 1 
ATOM   13585 C  CE3 . TRP   D  1 420 ? 14.244  53.252  -30.230  1.00 50.13  ? 721  TRP   D CE3 1 
ATOM   13586 C  CZ2 . TRP   D  1 420 ? 15.406  52.551  -32.724  1.00 49.68  ? 721  TRP   D CZ2 1 
ATOM   13587 C  CZ3 . TRP   D  1 420 ? 15.550  52.817  -30.317  1.00 55.90  ? 721  TRP   D CZ3 1 
ATOM   13588 C  CH2 . TRP   D  1 420 ? 16.122  52.474  -31.560  1.00 53.74  ? 721  TRP   D CH2 1 
ATOM   13589 N  N   . LYS   D  1 421 ? 9.738   53.167  -27.968  1.00 82.69  ? 722  LYS   D N   1 
ATOM   13590 C  CA  . LYS   D  1 421 ? 9.063   53.506  -26.716  1.00 84.23  ? 722  LYS   D CA  1 
ATOM   13591 C  C   . LYS   D  1 421 ? 9.886   54.464  -25.844  1.00 76.06  ? 722  LYS   D C   1 
ATOM   13592 O  O   . LYS   D  1 421 ? 11.036  54.812  -26.143  1.00 69.17  ? 722  LYS   D O   1 
ATOM   13593 C  CB  . LYS   D  1 421 ? 8.748   52.226  -25.940  1.00 90.06  ? 722  LYS   D CB  1 
ATOM   13594 C  CG  . LYS   D  1 421 ? 9.912   51.236  -25.875  1.00 91.84  ? 722  LYS   D CG  1 
ATOM   13595 C  CD  . LYS   D  1 421 ? 9.422   49.795  -25.739  1.00 92.16  ? 722  LYS   D CD  1 
ATOM   13596 C  CE  . LYS   D  1 421 ? 8.733   49.320  -27.019  1.00 89.18  ? 722  LYS   D CE  1 
ATOM   13597 N  NZ  . LYS   D  1 421 ? 7.911   48.095  -26.796  1.00 84.29  ? 722  LYS   D NZ  1 
HETATM 13598 C  CHA . HEM   E  2 .   ? -33.421 9.419   -34.384  1.00 39.81  ? 801  HEM   A CHA 1 
HETATM 13599 C  CHB . HEM   E  2 .   ? -29.003 11.296  -34.656  1.00 39.89  ? 801  HEM   A CHB 1 
HETATM 13600 C  CHC . HEM   E  2 .   ? -30.253 12.952  -39.075  1.00 42.24  ? 801  HEM   A CHC 1 
HETATM 13601 C  CHD . HEM   E  2 .   ? -34.849 11.673  -38.479  1.00 38.60  ? 801  HEM   A CHD 1 
HETATM 13602 C  C1A . HEM   E  2 .   ? -32.085 9.640   -34.142  1.00 32.52  ? 801  HEM   A C1A 1 
HETATM 13603 C  C2A . HEM   E  2 .   ? -31.229 8.939   -33.207  1.00 40.95  ? 801  HEM   A C2A 1 
HETATM 13604 C  C3A . HEM   E  2 .   ? -29.998 9.449   -33.274  1.00 34.56  ? 801  HEM   A C3A 1 
HETATM 13605 C  C4A . HEM   E  2 .   ? -30.038 10.502  -34.255  1.00 36.55  ? 801  HEM   A C4A 1 
HETATM 13606 C  CMA . HEM   E  2 .   ? -28.762 9.026   -32.448  1.00 28.27  ? 801  HEM   A CMA 1 
HETATM 13607 C  CAA . HEM   E  2 .   ? -31.671 7.786   -32.305  1.00 43.88  ? 801  HEM   A CAA 1 
HETATM 13608 C  CBA . HEM   E  2 .   ? -31.453 6.561   -33.181  1.00 45.44  ? 801  HEM   A CBA 1 
HETATM 13609 C  CGA . HEM   E  2 .   ? -31.474 5.343   -32.307  1.00 55.86  ? 801  HEM   A CGA 1 
HETATM 13610 O  O1A . HEM   E  2 .   ? -31.065 5.471   -31.126  1.00 54.79  ? 801  HEM   A O1A 1 
HETATM 13611 O  O2A . HEM   E  2 .   ? -31.880 4.256   -32.796  1.00 65.64  ? 801  HEM   A O2A 1 
HETATM 13612 C  C1B . HEM   E  2 .   ? -28.971 11.877  -35.904  1.00 37.65  ? 801  HEM   A C1B 1 
HETATM 13613 C  C2B . HEM   E  2 .   ? -27.804 12.506  -36.488  1.00 34.80  ? 801  HEM   A C2B 1 
HETATM 13614 C  C3B . HEM   E  2 .   ? -28.140 12.974  -37.696  1.00 40.51  ? 801  HEM   A C3B 1 
HETATM 13615 C  C4B . HEM   E  2 .   ? -29.542 12.648  -37.932  1.00 41.57  ? 801  HEM   A C4B 1 
HETATM 13616 C  CMB . HEM   E  2 .   ? -26.417 12.616  -35.803  1.00 31.72  ? 801  HEM   A CMB 1 
HETATM 13617 C  CAB . HEM   E  2 .   ? -27.152 13.701  -38.644  1.00 45.55  ? 801  HEM   A CAB 1 
HETATM 13618 C  CBB . HEM   E  2 .   ? -27.538 14.582  -39.564  1.00 47.05  ? 801  HEM   A CBB 1 
HETATM 13619 C  C1C . HEM   E  2 .   ? -31.592 12.754  -39.345  1.00 38.25  ? 801  HEM   A C1C 1 
HETATM 13620 C  C2C . HEM   E  2 .   ? -32.293 13.067  -40.582  1.00 38.85  ? 801  HEM   A C2C 1 
HETATM 13621 C  C3C . HEM   E  2 .   ? -33.581 12.712  -40.420  1.00 45.16  ? 801  HEM   A C3C 1 
HETATM 13622 C  C4C . HEM   E  2 .   ? -33.715 12.170  -39.076  1.00 38.68  ? 801  HEM   A C4C 1 
HETATM 13623 C  CMC . HEM   E  2 .   ? -31.615 13.680  -41.822  1.00 33.82  ? 801  HEM   A CMC 1 
HETATM 13624 C  CAC . HEM   E  2 .   ? -34.768 12.838  -41.408  1.00 47.81  ? 801  HEM   A CAC 1 
HETATM 13625 C  CBC . HEM   E  2 .   ? -34.747 13.611  -42.502  1.00 50.92  ? 801  HEM   A CBC 1 
HETATM 13626 C  C1D . HEM   E  2 .   ? -34.849 10.951  -37.304  1.00 41.62  ? 801  HEM   A C1D 1 
HETATM 13627 C  C2D . HEM   E  2 .   ? -36.007 10.359  -36.675  1.00 34.43  ? 801  HEM   A C2D 1 
HETATM 13628 C  C3D . HEM   E  2 .   ? -35.595 9.758   -35.563  1.00 41.40  ? 801  HEM   A C3D 1 
HETATM 13629 C  C4D . HEM   E  2 .   ? -34.174 9.917   -35.430  1.00 37.98  ? 801  HEM   A C4D 1 
HETATM 13630 C  CMD . HEM   E  2 .   ? -37.459 10.424  -37.196  1.00 36.10  ? 801  HEM   A CMD 1 
HETATM 13631 C  CAD . HEM   E  2 .   ? -36.460 9.017   -34.545  1.00 46.36  ? 801  HEM   A CAD 1 
HETATM 13632 C  CBD . HEM   E  2 .   ? -37.013 7.739   -35.123  1.00 51.48  ? 801  HEM   A CBD 1 
HETATM 13633 C  CGD . HEM   E  2 .   ? -37.858 7.185   -34.011  1.00 54.46  ? 801  HEM   A CGD 1 
HETATM 13634 O  O1D . HEM   E  2 .   ? -38.827 7.896   -33.591  1.00 49.64  ? 801  HEM   A O1D 1 
HETATM 13635 O  O2D . HEM   E  2 .   ? -37.546 6.042   -33.571  1.00 47.64  ? 801  HEM   A O2D 1 
HETATM 13636 N  NA  . HEM   E  2 .   ? -31.318 10.591  -34.758  1.00 39.74  ? 801  HEM   A NA  1 
HETATM 13637 N  NB  . HEM   E  2 .   ? -30.030 11.986  -36.800  1.00 34.55  ? 801  HEM   A NB  1 
HETATM 13638 N  NC  . HEM   E  2 .   ? -32.492 12.222  -38.470  1.00 39.51  ? 801  HEM   A NC  1 
HETATM 13639 N  ND  . HEM   E  2 .   ? -33.742 10.658  -36.517  1.00 35.82  ? 801  HEM   A ND  1 
HETATM 13640 FE FE  . HEM   E  2 .   ? -32.014 11.579  -36.540  1.00 34.95  ? 801  HEM   A FE  1 
HETATM 13641 N  N1  . H4B   F  3 .   ? -33.134 5.768   -27.024  1.00 51.89  ? 802  H4B   A N1  1 
HETATM 13642 C  C2  . H4B   F  3 .   ? -32.622 5.646   -28.279  1.00 54.39  ? 802  H4B   A C2  1 
HETATM 13643 N  N2  . H4B   F  3 .   ? -31.917 6.669   -28.840  1.00 46.70  ? 802  H4B   A N2  1 
HETATM 13644 N  N3  . H4B   F  3 .   ? -32.808 4.507   -28.988  1.00 51.22  ? 802  H4B   A N3  1 
HETATM 13645 C  C4  . H4B   F  3 .   ? -33.501 3.477   -28.459  1.00 49.96  ? 802  H4B   A C4  1 
HETATM 13646 O  O4  . H4B   F  3 .   ? -33.672 2.436   -29.123  1.00 50.31  ? 802  H4B   A O4  1 
HETATM 13647 C  C4A . H4B   F  3 .   ? -34.047 3.589   -27.193  1.00 51.70  ? 802  H4B   A C4A 1 
HETATM 13648 C  C8A . H4B   F  3 .   ? -33.843 4.755   -26.472  1.00 53.07  ? 802  H4B   A C8A 1 
HETATM 13649 N  N5  . H4B   F  3 .   ? -34.760 2.575   -26.638  1.00 50.11  ? 802  H4B   A N5  1 
HETATM 13650 N  N8  . H4B   F  3 .   ? -34.354 4.884   -25.216  1.00 46.04  ? 802  H4B   A N8  1 
HETATM 13651 C  C6  . H4B   F  3 .   ? -35.682 2.892   -25.544  1.00 45.75  ? 802  H4B   A C6  1 
HETATM 13652 C  C7  . H4B   F  3 .   ? -34.991 3.771   -24.511  1.00 39.45  ? 802  H4B   A C7  1 
HETATM 13653 C  C9  . H4B   F  3 .   ? -36.246 1.632   -24.892  1.00 39.34  ? 802  H4B   A C9  1 
HETATM 13654 O  O9  . H4B   F  3 .   ? -35.124 0.836   -24.507  1.00 44.61  ? 802  H4B   A O9  1 
HETATM 13655 C  C10 . H4B   F  3 .   ? -37.163 1.903   -23.686  1.00 41.47  ? 802  H4B   A C10 1 
HETATM 13656 C  C11 . H4B   F  3 .   ? -37.666 0.585   -23.105  1.00 39.16  ? 802  H4B   A C11 1 
HETATM 13657 O  O10 . H4B   F  3 .   ? -38.308 2.696   -24.044  1.00 47.57  ? 802  H4B   A O10 1 
HETATM 13658 C  C11 . A1A0A G  4 .   ? -31.411 6.038   -36.904  1.00 53.47  ? 803  A1A0A A C11 1 
HETATM 13659 C  C12 . A1A0A G  4 .   ? -30.762 4.823   -36.874  1.00 63.55  ? 803  A1A0A A C12 1 
HETATM 13660 C  C15 . A1A0A G  4 .   ? -33.316 5.044   -35.844  1.00 65.43  ? 803  A1A0A A C15 1 
HETATM 13661 N  N02 . A1A0A G  4 .   ? -27.572 8.853   -37.005  1.00 36.02  ? 803  A1A0A A N02 1 
HETATM 13662 C  C03 . A1A0A G  4 .   ? -29.304 9.277   -38.614  1.00 39.94  ? 803  A1A0A A C03 1 
HETATM 13663 C  C04 . A1A0A G  4 .   ? -30.545 8.925   -39.126  1.00 47.82  ? 803  A1A0A A C04 1 
HETATM 13664 C  C06 . A1A0A G  4 .   ? -30.683 7.183   -37.501  1.00 46.65  ? 803  A1A0A A C06 1 
HETATM 13665 C  C22 . A1A0A G  4 .   ? -36.602 4.329   -36.522  1.00 96.90  ? 803  A1A0A A C22 1 
HETATM 13666 C  C23 . A1A0A G  4 .   ? -36.938 3.109   -37.363  1.00 101.33 ? 803  A1A0A A C23 1 
HETATM 13667 C  C02 . A1A0A G  4 .   ? -28.782 8.552   -37.542  1.00 41.63  ? 803  A1A0A A C02 1 
HETATM 13668 C  C05 . A1A0A G  4 .   ? -31.237 7.872   -38.558  1.00 42.34  ? 803  A1A0A A C05 1 
HETATM 13669 C  C07 . A1A0A G  4 .   ? -31.159 9.656   -40.298  1.00 51.34  ? 803  A1A0A A C07 1 
HETATM 13670 C  C13 . A1A0A G  4 .   ? -31.374 3.714   -36.339  1.00 71.66  ? 803  A1A0A A C13 1 
HETATM 13671 C  C14 . A1A0A G  4 .   ? -32.659 3.818   -35.823  1.00 70.12  ? 803  A1A0A A C14 1 
HETATM 13672 C  C16 . A1A0A G  4 .   ? -32.699 6.160   -36.393  1.00 51.64  ? 803  A1A0A A C16 1 
HETATM 13673 C  C17 . A1A0A G  4 .   ? -34.710 5.141   -35.275  1.00 79.22  ? 803  A1A0A A C17 1 
HETATM 13674 C  C24 . A1A0A G  4 .   ? -37.229 1.918   -36.461  1.00 109.24 ? 803  A1A0A A C24 1 
HETATM 13675 C  C25 . A1A0A G  4 .   ? -36.212 1.751   -35.324  1.00 105.29 ? 803  A1A0A A C25 1 
HETATM 13676 C  C26 . A1A0A G  4 .   ? -35.849 3.071   -34.653  1.00 98.66  ? 803  A1A0A A C26 1 
HETATM 13677 F  F12 . A1A0A G  4 .   ? -29.523 4.713   -37.369  1.00 57.67  ? 803  A1A0A A F12 1 
HETATM 13678 F  F13 . A1A0A G  4 .   ? -30.706 2.551   -36.335  1.00 75.64  ? 803  A1A0A A F13 1 
HETATM 13679 F  F27 . A1A0A G  4 .   ? -37.217 0.822   -37.200  1.00 114.58 ? 803  A1A0A A F27 1 
HETATM 13680 F  F28 . A1A0A G  4 .   ? -38.430 2.112   -35.950  1.00 112.77 ? 803  A1A0A A F28 1 
HETATM 13681 N  N01 . A1A0A G  4 .   ? -29.474 7.522   -37.024  1.00 44.67  ? 803  A1A0A A N01 1 
HETATM 13682 N  N21 . A1A0A G  4 .   ? -35.421 3.953   -35.742  1.00 91.87  ? 803  A1A0A A N21 1 
HETATM 13683 C  C1  . GOL   H  5 .   ? -46.322 25.883  -35.460  1.00 80.84  ? 804  GOL   A C1  1 
HETATM 13684 O  O1  . GOL   H  5 .   ? -47.646 25.462  -35.707  1.00 83.75  ? 804  GOL   A O1  1 
HETATM 13685 C  C2  . GOL   H  5 .   ? -45.556 25.948  -36.776  1.00 76.28  ? 804  GOL   A C2  1 
HETATM 13686 O  O2  . GOL   H  5 .   ? -44.884 24.727  -36.982  1.00 61.76  ? 804  GOL   A O2  1 
HETATM 13687 C  C3  . GOL   H  5 .   ? -44.551 27.094  -36.723  1.00 85.42  ? 804  GOL   A C3  1 
HETATM 13688 O  O3  . GOL   H  5 .   ? -43.244 26.575  -36.611  1.00 90.90  ? 804  GOL   A O3  1 
HETATM 13689 C  C1  . GOL   I  5 .   ? -32.169 21.935  -50.393  1.00 75.40  ? 805  GOL   A C1  1 
HETATM 13690 O  O1  . GOL   I  5 .   ? -31.998 22.098  -48.996  1.00 79.42  ? 805  GOL   A O1  1 
HETATM 13691 C  C2  . GOL   I  5 .   ? -33.602 21.485  -50.683  1.00 74.53  ? 805  GOL   A C2  1 
HETATM 13692 O  O2  . GOL   I  5 .   ? -33.651 20.330  -51.506  1.00 61.09  ? 805  GOL   A O2  1 
HETATM 13693 C  C3  . GOL   I  5 .   ? -34.376 22.637  -51.320  1.00 84.23  ? 805  GOL   A C3  1 
HETATM 13694 O  O3  . GOL   I  5 .   ? -34.551 23.664  -50.366  1.00 87.94  ? 805  GOL   A O3  1 
HETATM 13695 ZN ZN  . ZN    J  6 .   ? -45.731 11.389  -19.957  1.00 40.94  ? 801  ZN    B ZN  1 
HETATM 13696 C  CHA . HEM   K  2 .   ? -34.381 7.616   -5.136   1.00 37.58  ? 802  HEM   B CHA 1 
HETATM 13697 C  CHB . HEM   K  2 .   ? -31.415 3.845   -4.678   1.00 43.32  ? 802  HEM   B CHB 1 
HETATM 13698 C  CHC . HEM   K  2 .   ? -33.435 2.942   -0.307   1.00 33.30  ? 802  HEM   B CHC 1 
HETATM 13699 C  CHD . HEM   K  2 .   ? -36.788 6.313   -1.085   1.00 31.65  ? 802  HEM   B CHD 1 
HETATM 13700 C  C1A . HEM   K  2 .   ? -33.306 6.786   -5.337   1.00 37.32  ? 802  HEM   B C1A 1 
HETATM 13701 C  C2A . HEM   K  2 .   ? -32.203 6.962   -6.260   1.00 45.01  ? 802  HEM   B C2A 1 
HETATM 13702 C  C3A . HEM   K  2 .   ? -31.376 5.925   -6.134   1.00 38.96  ? 802  HEM   B C3A 1 
HETATM 13703 C  C4A . HEM   K  2 .   ? -31.935 5.040   -5.132   1.00 42.37  ? 802  HEM   B C4A 1 
HETATM 13704 C  CMA . HEM   K  2 .   ? -30.070 5.695   -6.929   1.00 39.24  ? 802  HEM   B CMA 1 
HETATM 13705 C  CAA . HEM   K  2 .   ? -31.982 8.153   -7.210   1.00 56.19  ? 802  HEM   B CAA 1 
HETATM 13706 C  CBA . HEM   K  2 .   ? -31.285 9.215   -6.367   1.00 67.40  ? 802  HEM   B CBA 1 
HETATM 13707 C  CGA . HEM   K  2 .   ? -30.563 10.193  -7.242   1.00 71.35  ? 802  HEM   B CGA 1 
HETATM 13708 O  O1A . HEM   K  2 .   ? -30.120 9.762   -8.328   1.00 76.97  ? 802  HEM   B O1A 1 
HETATM 13709 O  O2A . HEM   K  2 .   ? -30.420 11.382  -6.852   1.00 72.19  ? 802  HEM   B O2A 1 
HETATM 13710 C  C1B . HEM   K  2 .   ? -31.694 3.271   -3.440   1.00 40.41  ? 802  HEM   B C1B 1 
HETATM 13711 C  C2B . HEM   K  2 .   ? -31.027 2.121   -2.881   1.00 36.68  ? 802  HEM   B C2B 1 
HETATM 13712 C  C3B . HEM   K  2 .   ? -31.575 1.851   -1.695   1.00 44.11  ? 802  HEM   B C3B 1 
HETATM 13713 C  C4B . HEM   K  2 .   ? -32.629 2.834   -1.441   1.00 40.23  ? 802  HEM   B C4B 1 
HETATM 13714 C  CMB . HEM   K  2 .   ? -29.880 1.336   -3.564   1.00 33.33  ? 802  HEM   B CMB 1 
HETATM 13715 C  CAB . HEM   K  2 .   ? -31.110 0.689   -0.778   1.00 49.50  ? 802  HEM   B CAB 1 
HETATM 13716 C  CBB . HEM   K  2 .   ? -31.719 0.371   0.376    1.00 44.18  ? 802  HEM   B CBB 1 
HETATM 13717 C  C1C . HEM   K  2 .   ? -34.497 3.794   -0.089   1.00 27.47  ? 802  HEM   B C1C 1 
HETATM 13718 C  C2C . HEM   K  2 .   ? -35.303 3.931   1.138    1.00 37.90  ? 802  HEM   B C2C 1 
HETATM 13719 C  C3C . HEM   K  2 .   ? -36.234 4.879   0.920    1.00 40.09  ? 802  HEM   B C3C 1 
HETATM 13720 C  C4C . HEM   K  2 .   ? -36.049 5.351   -0.448   1.00 36.33  ? 802  HEM   B C4C 1 
HETATM 13721 C  CMC . HEM   K  2 .   ? -35.064 3.123   2.439    1.00 24.35  ? 802  HEM   B CMC 1 
HETATM 13722 C  CAC . HEM   K  2 .   ? -37.353 5.408   1.849    1.00 40.48  ? 802  HEM   B CAC 1 
HETATM 13723 C  CBC . HEM   K  2 .   ? -37.749 4.779   2.965    1.00 44.23  ? 802  HEM   B CBC 1 
HETATM 13724 C  C1D . HEM   K  2 .   ? -36.411 6.958   -2.237   1.00 34.38  ? 802  HEM   B C1D 1 
HETATM 13725 C  C2D . HEM   K  2 .   ? -37.109 8.070   -2.832   1.00 34.94  ? 802  HEM   B C2D 1 
HETATM 13726 C  C3D . HEM   K  2 .   ? -36.460 8.426   -3.948   1.00 40.27  ? 802  HEM   B C3D 1 
HETATM 13727 C  C4D . HEM   K  2 .   ? -35.304 7.556   -4.103   1.00 40.14  ? 802  HEM   B C4D 1 
HETATM 13728 C  CMD . HEM   K  2 .   ? -38.393 8.728   -2.289   1.00 35.69  ? 802  HEM   B CMD 1 
HETATM 13729 C  CAD . HEM   K  2 .   ? -36.896 9.560   -4.899   1.00 31.89  ? 802  HEM   B CAD 1 
HETATM 13730 C  CBD . HEM   K  2 .   ? -36.387 10.878  -4.357   1.00 46.37  ? 802  HEM   B CBD 1 
HETATM 13731 C  CGD . HEM   K  2 .   ? -36.819 11.949  -5.321   1.00 64.82  ? 802  HEM   B CGD 1 
HETATM 13732 O  O1D . HEM   K  2 .   ? -37.921 11.800  -5.947   1.00 57.21  ? 802  HEM   B O1D 1 
HETATM 13733 O  O2D . HEM   K  2 .   ? -36.052 12.948  -5.447   1.00 73.02  ? 802  HEM   B O2D 1 
HETATM 13734 N  NA  . HEM   K  2 .   ? -33.105 5.603   -4.675   1.00 41.95  ? 802  HEM   B NA  1 
HETATM 13735 N  NB  . HEM   K  2 .   ? -32.675 3.669   -2.544   1.00 31.12  ? 802  HEM   B NB  1 
HETATM 13736 N  NC  . HEM   K  2 .   ? -34.995 4.679   -1.005   1.00 35.70  ? 802  HEM   B NC  1 
HETATM 13737 N  ND  . HEM   K  2 .   ? -35.311 6.660   -3.032   1.00 31.43  ? 802  HEM   B ND  1 
HETATM 13738 FE FE  . HEM   K  2 .   ? -34.228 4.971   -2.967   1.00 35.37  ? 802  HEM   B FE  1 
HETATM 13739 N  N1  . H4B   L  3 .   ? -32.047 10.387  -12.494  1.00 67.03  ? 803  H4B   B N1  1 
HETATM 13740 C  C2  . H4B   L  3 .   ? -31.586 10.227  -11.231  1.00 66.40  ? 803  H4B   B C2  1 
HETATM 13741 N  N2  . H4B   L  3 .   ? -31.457 8.974   -10.726  1.00 60.03  ? 803  H4B   B N2  1 
HETATM 13742 N  N3  . H4B   L  3 .   ? -31.260 11.309  -10.481  1.00 66.89  ? 803  H4B   B N3  1 
HETATM 13743 C  C4  . H4B   L  3 .   ? -31.388 12.560  -10.981  1.00 59.93  ? 803  H4B   B C4  1 
HETATM 13744 O  O4  . H4B   L  3 .   ? -31.083 13.544  -10.284  1.00 53.42  ? 803  H4B   B O4  1 
HETATM 13745 C  C4A . H4B   L  3 .   ? -31.869 12.742  -12.268  1.00 61.85  ? 803  H4B   B C4A 1 
HETATM 13746 C  C8A . H4B   L  3 .   ? -32.194 11.626  -13.023  1.00 64.00  ? 803  H4B   B C8A 1 
HETATM 13747 N  N5  . H4B   L  3 .   ? -32.025 13.980  -12.794  1.00 58.63  ? 803  H4B   B N5  1 
HETATM 13748 N  N8  . H4B   L  3 .   ? -32.669 11.762  -14.282  1.00 56.86  ? 803  H4B   B N8  1 
HETATM 13749 C  C6  . H4B   L  3 .   ? -32.977 14.128  -13.883  1.00 55.65  ? 803  H4B   B C6  1 
HETATM 13750 C  C7  . H4B   L  3 .   ? -32.735 13.060  -14.934  1.00 56.68  ? 803  H4B   B C7  1 
HETATM 13751 C  C9  . H4B   L  3 .   ? -32.931 15.501  -14.547  1.00 54.86  ? 803  H4B   B C9  1 
HETATM 13752 O  O9  . H4B   L  3 .   ? -31.593 15.856  -14.901  1.00 50.44  ? 803  H4B   B O9  1 
HETATM 13753 C  C10 . H4B   L  3 .   ? -33.755 15.488  -15.821  1.00 53.88  ? 803  H4B   B C10 1 
HETATM 13754 C  C11 . H4B   L  3 .   ? -33.670 16.859  -16.480  1.00 45.87  ? 803  H4B   B C11 1 
HETATM 13755 O  O10 . H4B   L  3 .   ? -35.112 15.158  -15.499  1.00 62.83  ? 803  H4B   B O10 1 
HETATM 13756 C  C11 . A1A0A M  4 .   ? -30.812 9.438   -2.534   1.00 43.38  ? 804  A1A0A B C11 1 
HETATM 13757 C  C12 . A1A0A M  4 .   ? -29.619 10.131  -2.517   1.00 51.87  ? 804  A1A0A B C12 1 
HETATM 13758 C  C15 . A1A0A M  4 .   ? -31.872 11.331  -3.559   1.00 60.90  ? 804  A1A0A B C15 1 
HETATM 13759 N  N02 . A1A0A M  4 .   ? -28.894 5.037   -2.306   1.00 37.23  ? 804  A1A0A B N02 1 
HETATM 13760 C  C03 . A1A0A M  4 .   ? -30.592 5.605   -0.767   1.00 38.53  ? 804  A1A0A B C03 1 
HETATM 13761 C  C04 . A1A0A M  4 .   ? -31.483 6.535   -0.265   1.00 39.09  ? 804  A1A0A B C04 1 
HETATM 13762 C  C06 . A1A0A M  4 .   ? -30.763 8.078   -1.935   1.00 42.03  ? 804  A1A0A B C06 1 
HETATM 13763 C  C22 . A1A0A M  4 .   ? -34.094 13.562  -2.669   1.00 93.14  ? 804  A1A0A B C22 1 
HETATM 13764 C  C23 . A1A0A M  4 .   ? -33.939 14.943  -2.053   1.00 99.86  ? 804  A1A0A B C23 1 
HETATM 13765 C  C02 . A1A0A M  4 .   ? -29.787 5.942   -1.845   1.00 38.08  ? 804  A1A0A B C02 1 
HETATM 13766 C  C05 . A1A0A M  4 .   ? -31.571 7.780   -0.846   1.00 30.99  ? 804  A1A0A B C05 1 
HETATM 13767 C  C07 . A1A0A M  4 .   ? -32.366 6.182   0.905    1.00 49.75  ? 804  A1A0A B C07 1 
HETATM 13768 C  C13 . A1A0A M  4 .   ? -29.521 11.410  -3.014   1.00 60.34  ? 804  A1A0A B C13 1 
HETATM 13769 C  C14 . A1A0A M  4 .   ? -30.657 12.016  -3.536   1.00 63.97  ? 804  A1A0A B C14 1 
HETATM 13770 C  C16 . A1A0A M  4 .   ? -31.961 10.031  -3.052   1.00 50.81  ? 804  A1A0A B C16 1 
HETATM 13771 C  C17 . A1A0A M  4 .   ? -33.083 12.021  -4.141   1.00 73.19  ? 804  A1A0A B C17 1 
HETATM 13772 C  C24 . A1A0A M  4 .   ? -34.191 15.993  -3.123   1.00 98.71  ? 804  A1A0A B C24 1 
HETATM 13773 C  C25 . A1A0A M  4 .   ? -33.286 15.763  -4.329   1.00 91.43  ? 804  A1A0A B C25 1 
HETATM 13774 C  C26 . A1A0A M  4 .   ? -33.391 14.326  -4.826   1.00 85.31  ? 804  A1A0A B C26 1 
HETATM 13775 F  F12 . A1A0A M  4 .   ? -28.531 9.543   -2.006   1.00 57.31  ? 804  A1A0A B F12 1 
HETATM 13776 F  F13 . A1A0A M  4 .   ? -28.328 12.040  -2.990   1.00 65.92  ? 804  A1A0A B F13 1 
HETATM 13777 F  F27 . A1A0A M  4 .   ? -33.952 17.191  -2.623   1.00 102.59 ? 804  A1A0A B F27 1 
HETATM 13778 F  F28 . A1A0A M  4 .   ? -35.457 15.897  -3.487   1.00 97.93  ? 804  A1A0A B F28 1 
HETATM 13779 N  N01 . A1A0A M  4 .   ? -29.866 7.171   -2.387   1.00 36.47  ? 804  A1A0A B N01 1 
HETATM 13780 N  N21 . A1A0A M  4 .   ? -33.077 13.421  -3.714   1.00 81.21  ? 804  A1A0A B N21 1 
HETATM 13781 C  C1  . GOL   N  5 .   ? -53.294 0.644   -3.753   1.00 71.31  ? 805  GOL   B C1  1 
HETATM 13782 O  O1  . GOL   N  5 .   ? -52.806 1.932   -3.438   1.00 70.95  ? 805  GOL   B O1  1 
HETATM 13783 C  C2  . GOL   N  5 .   ? -53.211 -0.259  -2.526   1.00 72.00  ? 805  GOL   B C2  1 
HETATM 13784 O  O2  . GOL   N  5 .   ? -51.985 -0.973  -2.505   1.00 63.45  ? 805  GOL   B O2  1 
HETATM 13785 C  C3  . GOL   N  5 .   ? -54.448 -1.167  -2.445   1.00 78.32  ? 805  GOL   B C3  1 
HETATM 13786 O  O3  . GOL   N  5 .   ? -54.148 -2.509  -2.778   1.00 78.44  ? 805  GOL   B O3  1 
HETATM 13787 C  CHA . HEM   O  2 .   ? 24.753  33.657  -77.244  1.00 30.52  ? 801  HEM   C CHA 1 
HETATM 13788 C  CHB . HEM   O  2 .   ? 27.780  37.402  -77.702  1.00 39.48  ? 801  HEM   C CHB 1 
HETATM 13789 C  CHC . HEM   O  2 .   ? 25.873  38.272  -82.125  1.00 42.99  ? 801  HEM   C CHC 1 
HETATM 13790 C  CHD . HEM   O  2 .   ? 22.499  34.940  -81.352  1.00 30.49  ? 801  HEM   C CHD 1 
HETATM 13791 C  C1A . HEM   O  2 .   ? 25.843  34.479  -77.042  1.00 34.05  ? 801  HEM   C C1A 1 
HETATM 13792 C  C2A . HEM   O  2 .   ? 26.936  34.282  -76.101  1.00 44.06  ? 801  HEM   C C2A 1 
HETATM 13793 C  C3A . HEM   O  2 .   ? 27.779  35.313  -76.225  1.00 43.79  ? 801  HEM   C C3A 1 
HETATM 13794 C  C4A . HEM   O  2 .   ? 27.248  36.209  -77.248  1.00 41.20  ? 801  HEM   C C4A 1 
HETATM 13795 C  CMA . HEM   O  2 .   ? 29.085  35.522  -75.425  1.00 34.28  ? 801  HEM   C CMA 1 
HETATM 13796 C  CAA . HEM   O  2 .   ? 27.117  33.076  -75.153  1.00 49.74  ? 801  HEM   C CAA 1 
HETATM 13797 C  CBA . HEM   O  2 .   ? 27.857  32.004  -75.963  1.00 60.50  ? 801  HEM   C CBA 1 
HETATM 13798 C  CGA . HEM   O  2 .   ? 28.515  30.976  -75.085  1.00 65.27  ? 801  HEM   C CGA 1 
HETATM 13799 O  O1A . HEM   O  2 .   ? 29.159  31.378  -74.088  1.00 68.04  ? 801  HEM   C O1A 1 
HETATM 13800 O  O2A . HEM   O  2 .   ? 28.415  29.760  -75.387  1.00 68.03  ? 801  HEM   C O2A 1 
HETATM 13801 C  C1B . HEM   O  2 .   ? 27.552  37.966  -78.957  1.00 40.62  ? 801  HEM   C C1B 1 
HETATM 13802 C  C2B . HEM   O  2 .   ? 28.278  39.065  -79.550  1.00 32.31  ? 801  HEM   C C2B 1 
HETATM 13803 C  C3B . HEM   O  2 .   ? 27.747  39.317  -80.747  1.00 44.21  ? 801  HEM   C C3B 1 
HETATM 13804 C  C4B . HEM   O  2 .   ? 26.662  38.376  -80.986  1.00 43.94  ? 801  HEM   C C4B 1 
HETATM 13805 C  CMB . HEM   O  2 .   ? 29.448  39.853  -78.921  1.00 32.53  ? 801  HEM   C CMB 1 
HETATM 13806 C  CAB . HEM   O  2 .   ? 28.274  40.421  -81.690  1.00 39.73  ? 801  HEM   C CAB 1 
HETATM 13807 C  CBB . HEM   O  2 .   ? 27.661  40.747  -82.830  1.00 50.21  ? 801  HEM   C CBB 1 
HETATM 13808 C  C1C . HEM   O  2 .   ? 24.793  37.445  -82.334  1.00 35.54  ? 801  HEM   C C1C 1 
HETATM 13809 C  C2C . HEM   O  2 .   ? 23.957  37.370  -83.534  1.00 40.54  ? 801  HEM   C C2C 1 
HETATM 13810 C  C3C . HEM   O  2 .   ? 23.016  36.431  -83.316  1.00 41.72  ? 801  HEM   C C3C 1 
HETATM 13811 C  C4C . HEM   O  2 .   ? 23.236  35.910  -81.972  1.00 37.16  ? 801  HEM   C C4C 1 
HETATM 13812 C  CMC . HEM   O  2 .   ? 24.193  38.232  -84.795  1.00 29.86  ? 801  HEM   C CMC 1 
HETATM 13813 C  CAC . HEM   O  2 .   ? 21.862  35.945  -84.226  1.00 43.01  ? 801  HEM   C CAC 1 
HETATM 13814 C  CBC . HEM   O  2 .   ? 21.484  36.591  -85.335  1.00 47.69  ? 801  HEM   C CBC 1 
HETATM 13815 C  C1D . HEM   O  2 .   ? 22.821  34.305  -80.188  1.00 37.62  ? 801  HEM   C C1D 1 
HETATM 13816 C  C2D . HEM   O  2 .   ? 22.070  33.229  -79.595  1.00 42.71  ? 801  HEM   C C2D 1 
HETATM 13817 C  C3D . HEM   O  2 .   ? 22.682  32.868  -78.463  1.00 41.98  ? 801  HEM   C C3D 1 
HETATM 13818 C  C4D . HEM   O  2 .   ? 23.851  33.712  -78.291  1.00 39.67  ? 801  HEM   C C4D 1 
HETATM 13819 C  CMD . HEM   O  2 .   ? 20.779  32.612  -80.178  1.00 45.40  ? 801  HEM   C CMD 1 
HETATM 13820 C  CAD . HEM   O  2 .   ? 22.199  31.767  -77.492  1.00 32.63  ? 801  HEM   C CAD 1 
HETATM 13821 C  CBD . HEM   O  2 .   ? 22.692  30.414  -77.941  1.00 51.49  ? 801  HEM   C CBD 1 
HETATM 13822 C  CGD . HEM   O  2 .   ? 22.154  29.429  -76.936  1.00 64.49  ? 801  HEM   C CGD 1 
HETATM 13823 O  O1D . HEM   O  2 .   ? 21.007  29.635  -76.430  1.00 58.66  ? 801  HEM   C O1D 1 
HETATM 13824 O  O2D . HEM   O  2 .   ? 22.882  28.438  -76.658  1.00 68.21  ? 801  HEM   C O2D 1 
HETATM 13825 N  NA  . HEM   O  2 .   ? 26.071  35.661  -77.701  1.00 43.32  ? 801  HEM   C NA  1 
HETATM 13826 N  NB  . HEM   O  2 .   ? 26.574  37.583  -79.862  1.00 30.32  ? 801  HEM   C NB  1 
HETATM 13827 N  NC  . HEM   O  2 .   ? 24.314  36.545  -81.423  1.00 37.09  ? 801  HEM   C NC  1 
HETATM 13828 N  ND  . HEM   O  2 .   ? 23.899  34.583  -79.370  1.00 35.32  ? 801  HEM   C ND  1 
HETATM 13829 FE FE  . HEM   O  2 .   ? 25.025  36.266  -79.442  1.00 34.75  ? 801  HEM   C FE  1 
HETATM 13830 N  N1  . H4B   P  3 .   ? 27.130  30.770  -69.982  1.00 49.56  ? 802  H4B   C N1  1 
HETATM 13831 C  C2  . H4B   P  3 .   ? 27.575  30.929  -71.254  1.00 45.00  ? 802  H4B   C C2  1 
HETATM 13832 N  N2  . H4B   P  3 .   ? 27.637  32.187  -71.780  1.00 41.65  ? 802  H4B   C N2  1 
HETATM 13833 N  N3  . H4B   P  3 .   ? 27.942  29.843  -71.991  1.00 46.75  ? 802  H4B   C N3  1 
HETATM 13834 C  C4  . H4B   P  3 .   ? 27.875  28.596  -71.461  1.00 54.28  ? 802  H4B   C C4  1 
HETATM 13835 O  O4  . H4B   P  3 .   ? 28.221  27.600  -72.131  1.00 52.68  ? 802  H4B   C O4  1 
HETATM 13836 C  C4A . H4B   P  3 .   ? 27.409  28.424  -70.161  1.00 55.88  ? 802  H4B   C C4A 1 
HETATM 13837 C  C8A . H4B   P  3 .   ? 27.042  29.540  -69.426  1.00 50.44  ? 802  H4B   C C8A 1 
HETATM 13838 N  N5  . H4B   P  3 .   ? 27.313  27.194  -69.601  1.00 53.11  ? 802  H4B   C N5  1 
HETATM 13839 N  N8  . H4B   P  3 .   ? 26.583  29.414  -68.159  1.00 47.35  ? 802  H4B   C N8  1 
HETATM 13840 C  C6  . H4B   P  3 .   ? 26.340  27.045  -68.532  1.00 49.72  ? 802  H4B   C C6  1 
HETATM 13841 C  C7  . H4B   P  3 .   ? 26.567  28.126  -67.484  1.00 46.95  ? 802  H4B   C C7  1 
HETATM 13842 C  C9  . H4B   P  3 .   ? 26.344  25.656  -67.890  1.00 47.05  ? 802  H4B   C C9  1 
HETATM 13843 O  O9  . H4B   P  3 .   ? 27.665  25.245  -67.527  1.00 45.01  ? 802  H4B   C O9  1 
HETATM 13844 C  C10 . H4B   P  3 .   ? 25.464  25.681  -66.654  1.00 50.89  ? 802  H4B   C C10 1 
HETATM 13845 C  C11 . H4B   P  3 .   ? 25.479  24.335  -65.930  1.00 43.38  ? 802  H4B   C C11 1 
HETATM 13846 O  O10 . H4B   P  3 .   ? 24.145  26.042  -67.083  1.00 55.85  ? 802  H4B   C O10 1 
HETATM 13847 C  C11 . A1A0A Q  4 .   ? 28.408  31.808  -79.864  1.00 48.75  ? 803  A1A0A C C11 1 
HETATM 13848 C  C12 . A1A0A Q  4 .   ? 29.567  31.062  -79.904  1.00 57.22  ? 803  A1A0A C C12 1 
HETATM 13849 C  C15 . A1A0A Q  4 .   ? 27.238  29.968  -78.870  1.00 59.38  ? 803  A1A0A C C15 1 
HETATM 13850 N  N02 . A1A0A Q  4 .   ? 30.401  36.173  -80.072  1.00 40.24  ? 803  A1A0A C N02 1 
HETATM 13851 C  C03 . A1A0A Q  4 .   ? 28.681  35.619  -81.646  1.00 45.24  ? 803  A1A0A C C03 1 
HETATM 13852 C  C04 . A1A0A Q  4 .   ? 27.779  34.685  -82.130  1.00 43.97  ? 803  A1A0A C C04 1 
HETATM 13853 C  C06 . A1A0A Q  4 .   ? 28.503  33.168  -80.452  1.00 45.75  ? 803  A1A0A C C06 1 
HETATM 13854 C  C22 . A1A0A Q  4 .   ? 25.280  27.603  -79.794  1.00 86.96  ? 803  A1A0A C C22 1 
HETATM 13855 C  C23 . A1A0A Q  4 .   ? 25.598  26.171  -80.198  1.00 90.98  ? 803  A1A0A C C23 1 
HETATM 13856 C  C02 . A1A0A Q  4 .   ? 29.492  35.288  -80.560  1.00 44.84  ? 803  A1A0A C C02 1 
HETATM 13857 C  C05 . A1A0A Q  4 .   ? 27.695  33.453  -81.539  1.00 41.18  ? 803  A1A0A C C05 1 
HETATM 13858 C  C07 . A1A0A Q  4 .   ? 26.882  34.989  -83.289  1.00 55.01  ? 803  A1A0A C C07 1 
HETATM 13859 C  C13 . A1A0A Q  4 .   ? 29.591  29.775  -79.424  1.00 63.68  ? 803  A1A0A C C13 1 
HETATM 13860 C  C14 . A1A0A Q  4 .   ? 28.421  29.223  -78.904  1.00 67.08  ? 803  A1A0A C C14 1 
HETATM 13861 C  C16 . A1A0A Q  4 .   ? 27.225  31.277  -79.354  1.00 47.31  ? 803  A1A0A C C16 1 
HETATM 13862 C  C17 . A1A0A Q  4 .   ? 25.985  29.342  -78.299  1.00 69.58  ? 803  A1A0A C C17 1 
HETATM 13863 C  C24 . A1A0A Q  4 .   ? 25.096  25.232  -79.112  1.00 91.57  ? 803  A1A0A C C24 1 
HETATM 13864 C  C25 . A1A0A Q  4 .   ? 25.632  25.642  -77.742  1.00 85.14  ? 803  A1A0A C C25 1 
HETATM 13865 C  C26 . A1A0A Q  4 .   ? 25.432  27.127  -77.463  1.00 77.17  ? 803  A1A0A C C26 1 
HETATM 13866 F  F12 . A1A0A Q  4 .   ? 30.684  31.608  -80.416  1.00 61.31  ? 803  A1A0A C F12 1 
HETATM 13867 F  F13 . A1A0A Q  4 .   ? 30.749  29.088  -79.472  1.00 66.28  ? 803  A1A0A C F13 1 
HETATM 13868 F  F27 . A1A0A Q  4 .   ? 25.489  23.997  -79.370  1.00 94.68  ? 803  A1A0A C F27 1 
HETATM 13869 F  F28 . A1A0A Q  4 .   ? 23.777  25.299  -79.122  1.00 93.03  ? 803  A1A0A C F28 1 
HETATM 13870 N  N01 . A1A0A Q  4 .   ? 29.405  34.065  -80.008  1.00 41.13  ? 803  A1A0A C N01 1 
HETATM 13871 N  N21 . A1A0A Q  4 .   ? 26.023  27.896  -78.563  1.00 76.10  ? 803  A1A0A C N21 1 
HETATM 13872 C  C1  . GOL   R  5 .   ? 6.601   41.040  -78.614  1.00 81.10  ? 804  GOL   C C1  1 
HETATM 13873 O  O1  . GOL   R  5 .   ? 6.406   39.733  -79.112  1.00 77.96  ? 804  GOL   C O1  1 
HETATM 13874 C  C2  . GOL   R  5 .   ? 6.531   42.078  -79.735  1.00 82.73  ? 804  GOL   C C2  1 
HETATM 13875 O  O2  . GOL   R  5 .   ? 7.722   42.844  -79.789  1.00 76.11  ? 804  GOL   C O2  1 
HETATM 13876 C  C3  . GOL   R  5 .   ? 5.338   42.993  -79.467  1.00 86.41  ? 804  GOL   C C3  1 
HETATM 13877 O  O3  . GOL   R  5 .   ? 5.688   44.327  -79.755  1.00 89.35  ? 804  GOL   C O3  1 
HETATM 13878 C  C1  . GOL   S  5 .   ? 20.017  44.994  -92.977  1.00 67.92  ? 805  GOL   C C1  1 
HETATM 13879 O  O1  . GOL   S  5 .   ? 19.925  45.660  -91.728  1.00 76.86  ? 805  GOL   C O1  1 
HETATM 13880 C  C2  . GOL   S  5 .   ? 18.832  44.048  -93.148  1.00 54.77  ? 805  GOL   C C2  1 
HETATM 13881 O  O2  . GOL   S  5 .   ? 19.126  42.986  -94.042  1.00 54.98  ? 805  GOL   C O2  1 
HETATM 13882 C  C3  . GOL   S  5 .   ? 17.613  44.842  -93.588  1.00 58.36  ? 805  GOL   C C3  1 
HETATM 13883 O  O3  . GOL   S  5 .   ? 17.638  46.098  -92.950  1.00 63.42  ? 805  GOL   C O3  1 
HETATM 13884 ZN ZN  . ZN    T  6 .   ? 13.483  29.846  -62.487  1.00 41.74  ? 806  ZN    C ZN  1 
HETATM 13885 C  CHA . HEM   U  2 .   ? 25.773  31.797  -48.012  1.00 40.85  ? 801  HEM   D CHA 1 
HETATM 13886 C  CHB . HEM   U  2 .   ? 30.236  29.995  -47.703  1.00 46.20  ? 801  HEM   D CHB 1 
HETATM 13887 C  CHC . HEM   U  2 .   ? 28.961  28.296  -43.307  1.00 43.45  ? 801  HEM   D CHC 1 
HETATM 13888 C  CHD . HEM   U  2 .   ? 24.356  29.480  -43.965  1.00 31.93  ? 801  HEM   D CHD 1 
HETATM 13889 C  C1A . HEM   U  2 .   ? 27.116  31.592  -48.238  1.00 39.34  ? 801  HEM   D C1A 1 
HETATM 13890 C  C2A . HEM   U  2 .   ? 27.963  32.310  -49.173  1.00 41.26  ? 801  HEM   D C2A 1 
HETATM 13891 C  C3A . HEM   U  2 .   ? 29.206  31.821  -49.090  1.00 39.87  ? 801  HEM   D C3A 1 
HETATM 13892 C  C4A . HEM   U  2 .   ? 29.180  30.768  -48.108  1.00 40.17  ? 801  HEM   D C4A 1 
HETATM 13893 C  CMA . HEM   U  2 .   ? 30.449  32.257  -49.891  1.00 40.33  ? 801  HEM   D CMA 1 
HETATM 13894 C  CAA . HEM   U  2 .   ? 27.498  33.457  -50.071  1.00 41.86  ? 801  HEM   D CAA 1 
HETATM 13895 C  CBA . HEM   U  2 .   ? 27.779  34.700  -49.236  1.00 50.88  ? 801  HEM   D CBA 1 
HETATM 13896 C  CGA . HEM   U  2 .   ? 27.828  35.900  -50.137  1.00 58.66  ? 801  HEM   D CGA 1 
HETATM 13897 O  O1A . HEM   U  2 .   ? 28.510  35.810  -51.188  1.00 53.69  ? 801  HEM   D O1A 1 
HETATM 13898 O  O2A . HEM   U  2 .   ? 27.199  36.934  -49.794  1.00 64.05  ? 801  HEM   D O2A 1 
HETATM 13899 C  C1B . HEM   U  2 .   ? 30.282  29.393  -46.460  1.00 42.84  ? 801  HEM   D C1B 1 
HETATM 13900 C  C2B . HEM   U  2 .   ? 31.438  28.757  -45.864  1.00 42.26  ? 801  HEM   D C2B 1 
HETATM 13901 C  C3B . HEM   U  2 .   ? 31.092  28.276  -44.673  1.00 42.04  ? 801  HEM   D C3B 1 
HETATM 13902 C  C4B . HEM   U  2 .   ? 29.690  28.601  -44.440  1.00 40.96  ? 801  HEM   D C4B 1 
HETATM 13903 C  CMB . HEM   U  2 .   ? 32.845  28.629  -46.486  1.00 40.33  ? 801  HEM   D CMB 1 
HETATM 13904 C  CAB . HEM   U  2 .   ? 32.108  27.552  -43.759  1.00 45.07  ? 801  HEM   D CAB 1 
HETATM 13905 C  CBB . HEM   U  2 .   ? 31.753  26.698  -42.801  1.00 46.68  ? 801  HEM   D CBB 1 
HETATM 13906 C  C1C . HEM   U  2 .   ? 27.617  28.483  -43.050  1.00 37.17  ? 801  HEM   D C1C 1 
HETATM 13907 C  C2C . HEM   U  2 .   ? 26.911  28.169  -41.813  1.00 38.13  ? 801  HEM   D C2C 1 
HETATM 13908 C  C3C . HEM   U  2 .   ? 25.617  28.494  -41.986  1.00 45.62  ? 801  HEM   D C3C 1 
HETATM 13909 C  C4C . HEM   U  2 .   ? 25.488  29.014  -43.343  1.00 37.59  ? 801  HEM   D C4C 1 
HETATM 13910 C  CMC . HEM   U  2 .   ? 27.608  27.580  -40.581  1.00 35.75  ? 801  HEM   D CMC 1 
HETATM 13911 C  CAC . HEM   U  2 .   ? 24.421  28.352  -41.009  1.00 49.97  ? 801  HEM   D CAC 1 
HETATM 13912 C  CBC . HEM   U  2 .   ? 24.461  27.607  -39.895  1.00 47.65  ? 801  HEM   D CBC 1 
HETATM 13913 C  C1D . HEM   U  2 .   ? 24.360  30.236  -45.111  1.00 40.39  ? 801  HEM   D C1D 1 
HETATM 13914 C  C2D . HEM   U  2 .   ? 23.202  30.876  -45.686  1.00 36.10  ? 801  HEM   D C2D 1 
HETATM 13915 C  C3D . HEM   U  2 .   ? 23.604  31.505  -46.791  1.00 45.79  ? 801  HEM   D C3D 1 
HETATM 13916 C  C4D . HEM   U  2 .   ? 25.022  31.294  -46.966  1.00 43.89  ? 801  HEM   D C4D 1 
HETATM 13917 C  CMD . HEM   U  2 .   ? 21.783  30.805  -45.095  1.00 40.93  ? 801  HEM   D CMD 1 
HETATM 13918 C  CAD . HEM   U  2 .   ? 22.763  32.306  -47.794  1.00 53.80  ? 801  HEM   D CAD 1 
HETATM 13919 C  CBD . HEM   U  2 .   ? 22.142  33.551  -47.218  1.00 59.05  ? 801  HEM   D CBD 1 
HETATM 13920 C  CGD . HEM   U  2 .   ? 21.213  34.010  -48.308  1.00 61.83  ? 801  HEM   D CGD 1 
HETATM 13921 O  O1D . HEM   U  2 .   ? 20.310  33.198  -48.697  1.00 54.43  ? 801  HEM   D O1D 1 
HETATM 13922 O  O2D . HEM   U  2 .   ? 21.393  35.180  -48.764  1.00 56.00  ? 801  HEM   D O2D 1 
HETATM 13923 N  NA  . HEM   U  2 .   ? 27.895  30.657  -47.610  1.00 41.96  ? 801  HEM   D NA  1 
HETATM 13924 N  NB  . HEM   U  2 .   ? 29.223  29.282  -45.567  1.00 36.43  ? 801  HEM   D NB  1 
HETATM 13925 N  NC  . HEM   U  2 .   ? 26.716  28.982  -43.935  1.00 33.01  ? 801  HEM   D NC  1 
HETATM 13926 N  ND  . HEM   U  2 .   ? 25.459  30.503  -45.925  1.00 34.65  ? 801  HEM   D ND  1 
HETATM 13927 FE FE  . HEM   U  2 .   ? 27.198  29.608  -45.873  1.00 34.63  ? 801  HEM   D FE  1 
HETATM 13928 N  N1  . H4B   V  3 .   ? 26.148  35.584  -55.316  1.00 51.70  ? 802  H4B   D N1  1 
HETATM 13929 C  C2  . H4B   V  3 .   ? 26.627  35.715  -54.050  1.00 54.83  ? 802  H4B   D C2  1 
HETATM 13930 N  N2  . H4B   V  3 .   ? 27.360  34.713  -53.493  1.00 47.65  ? 802  H4B   D N2  1 
HETATM 13931 N  N3  . H4B   V  3 .   ? 26.376  36.840  -53.336  1.00 50.69  ? 802  H4B   D N3  1 
HETATM 13932 C  C4  . H4B   V  3 .   ? 25.644  37.836  -53.877  1.00 46.53  ? 802  H4B   D C4  1 
HETATM 13933 O  O4  . H4B   V  3 .   ? 25.408  38.863  -53.216  1.00 50.61  ? 802  H4B   D O4  1 
HETATM 13934 C  C4A . H4B   V  3 .   ? 25.133  37.711  -55.158  1.00 46.02  ? 802  H4B   D C4A 1 
HETATM 13935 C  C8A . H4B   V  3 .   ? 25.402  36.560  -55.885  1.00 51.35  ? 802  H4B   D C8A 1 
HETATM 13936 N  N5  . H4B   V  3 .   ? 24.381  38.693  -55.718  1.00 42.62  ? 802  H4B   D N5  1 
HETATM 13937 N  N8  . H4B   V  3 .   ? 24.924  36.411  -57.163  1.00 47.34  ? 802  H4B   D N8  1 
HETATM 13938 C  C6  . H4B   V  3 .   ? 23.498  38.336  -56.835  1.00 46.84  ? 802  H4B   D C6  1 
HETATM 13939 C  C7  . H4B   V  3 .   ? 24.246  37.498  -57.874  1.00 39.20  ? 802  H4B   D C7  1 
HETATM 13940 C  C9  . H4B   V  3 .   ? 22.875  39.572  -57.481  1.00 41.06  ? 802  H4B   D C9  1 
HETATM 13941 O  O9  . H4B   V  3 .   ? 23.926  40.457  -57.871  1.00 41.99  ? 802  H4B   D O9  1 
HETATM 13942 C  C10 . H4B   V  3 .   ? 22.019  39.261  -58.707  1.00 45.53  ? 802  H4B   D C10 1 
HETATM 13943 C  C11 . H4B   V  3 .   ? 21.383  40.560  -59.204  1.00 40.43  ? 802  H4B   D C11 1 
HETATM 13944 O  O10 . H4B   V  3 .   ? 21.005  38.300  -58.389  1.00 43.87  ? 802  H4B   D O10 1 
HETATM 13945 C  C11 . A1A0A W  4 .   ? 27.761  35.174  -45.502  1.00 53.32  ? 803  A1A0A D C11 1 
HETATM 13946 C  C12 . A1A0A W  4 .   ? 28.422  36.387  -45.508  1.00 58.37  ? 803  A1A0A D C12 1 
HETATM 13947 C  C15 . A1A0A W  4 .   ? 25.829  36.203  -46.499  1.00 64.79  ? 803  A1A0A D C15 1 
HETATM 13948 N  N02 . A1A0A W  4 .   ? 31.646  32.385  -45.361  1.00 38.46  ? 803  A1A0A D N02 1 
HETATM 13949 C  C03 . A1A0A W  4 .   ? 29.928  32.003  -43.753  1.00 41.67  ? 803  A1A0A D C03 1 
HETATM 13950 C  C04 . A1A0A W  4 .   ? 28.693  32.345  -43.245  1.00 46.75  ? 803  A1A0A D C04 1 
HETATM 13951 C  C06 . A1A0A W  4 .   ? 28.523  34.040  -44.919  1.00 46.04  ? 803  A1A0A D C06 1 
HETATM 13952 C  C22 . A1A0A W  4 .   ? 22.331  37.040  -46.151  1.00 91.33  ? 803  A1A0A D C22 1 
HETATM 13953 C  C23 . A1A0A W  4 .   ? 21.895  38.201  -45.267  1.00 91.86  ? 803  A1A0A D C23 1 
HETATM 13954 C  C02 . A1A0A W  4 .   ? 30.441  32.707  -44.845  1.00 40.21  ? 803  A1A0A D C02 1 
HETATM 13955 C  C05 . A1A0A W  4 .   ? 27.989  33.375  -43.835  1.00 44.34  ? 803  A1A0A D C05 1 
HETATM 13956 C  C07 . A1A0A W  4 .   ? 28.103  31.626  -42.058  1.00 56.03  ? 803  A1A0A D C07 1 
HETATM 13957 C  C13 . A1A0A W  4 .   ? 27.804  37.508  -46.005  1.00 67.29  ? 803  A1A0A D C13 1 
HETATM 13958 C  C14 . A1A0A W  4 .   ? 26.510  37.415  -46.494  1.00 68.57  ? 803  A1A0A D C14 1 
HETATM 13959 C  C16 . A1A0A W  4 .   ? 26.457  35.065  -45.993  1.00 52.98  ? 803  A1A0A D C16 1 
HETATM 13960 C  C17 . A1A0A W  4 .   ? 24.418  36.150  -47.051  1.00 76.06  ? 803  A1A0A D C17 1 
HETATM 13961 C  C24 . A1A0A W  4 .   ? 22.051  39.556  -45.961  1.00 104.92 ? 803  A1A0A D C24 1 
HETATM 13962 C  C25 . A1A0A W  4 .   ? 23.252  39.658  -46.911  1.00 103.87 ? 803  A1A0A D C25 1 
HETATM 13963 C  C26 . A1A0A W  4 .   ? 23.552  38.363  -47.657  1.00 97.47  ? 803  A1A0A D C26 1 
HETATM 13964 F  F12 . A1A0A W  4 .   ? 29.679  36.473  -45.030  1.00 51.80  ? 803  A1A0A D F12 1 
HETATM 13965 F  F13 . A1A0A W  4 .   ? 28.466  38.676  -46.004  1.00 76.64  ? 803  A1A0A D F13 1 
HETATM 13966 F  F27 . A1A0A W  4 .   ? 22.203  40.486  -45.036  1.00 109.22 ? 803  A1A0A D F27 1 
HETATM 13967 F  F28 . A1A0A W  4 .   ? 20.945  39.792  -46.642  1.00 110.36 ? 803  A1A0A D F28 1 
HETATM 13968 N  N01 . A1A0A W  4 .   ? 29.744  33.715  -45.386  1.00 35.24  ? 803  A1A0A D N01 1 
HETATM 13969 N  N21 . A1A0A W  4 .   ? 23.690  37.349  -46.607  1.00 89.20  ? 803  A1A0A D N21 1 
HETATM 13970 C  C1  . GOL   X  5 .   ? 12.853  16.016  -46.601  1.00 70.89  ? 804  GOL   D C1  1 
HETATM 13971 O  O1  . GOL   X  5 .   ? 12.378  17.243  -46.084  1.00 73.06  ? 804  GOL   D O1  1 
HETATM 13972 C  C2  . GOL   X  5 .   ? 13.806  15.395  -45.584  1.00 71.04  ? 804  GOL   D C2  1 
HETATM 13973 O  O2  . GOL   X  5 .   ? 14.612  16.393  -45.003  1.00 63.18  ? 804  GOL   D O2  1 
HETATM 13974 C  C3  . GOL   X  5 .   ? 14.701  14.345  -46.232  1.00 73.39  ? 804  GOL   D C3  1 
HETATM 13975 O  O3  . GOL   X  5 .   ? 15.937  14.340  -45.547  1.00 71.74  ? 804  GOL   D O3  1 
HETATM 13976 O  O   . HOH   Y  7 .   ? -38.676 -14.350 -49.100  1.00 74.51  ? 901  HOH   A O   1 
HETATM 13977 O  O   . HOH   Y  7 .   ? -44.885 38.927  -45.901  1.00 64.32  ? 902  HOH   A O   1 
HETATM 13978 O  O   . HOH   Y  7 .   ? -44.495 8.926   -63.335  1.00 47.03  ? 903  HOH   A O   1 
HETATM 13979 O  O   . HOH   Y  7 .   ? -38.877 5.025   -26.374  1.00 39.26  ? 904  HOH   A O   1 
HETATM 13980 O  O   . HOH   Y  7 .   ? -13.409 3.217   -44.944  1.00 44.91  ? 905  HOH   A O   1 
HETATM 13981 O  O   . HOH   Y  7 .   ? -45.868 7.408   -59.543  1.00 44.38  ? 906  HOH   A O   1 
HETATM 13982 O  O   . HOH   Y  7 .   ? -28.042 -1.666  -38.381  1.00 47.21  ? 907  HOH   A O   1 
HETATM 13983 O  O   . HOH   Y  7 .   ? -40.466 10.068  -23.071  1.00 40.65  ? 908  HOH   A O   1 
HETATM 13984 O  O   . HOH   Y  7 .   ? -42.315 10.510  -31.413  1.00 52.85  ? 909  HOH   A O   1 
HETATM 13985 O  O   . HOH   Y  7 .   ? -26.568 20.844  -19.340  1.00 47.38  ? 910  HOH   A O   1 
HETATM 13986 O  O   . HOH   Y  7 .   ? -18.620 -11.126 -27.154  1.00 50.78  ? 911  HOH   A O   1 
HETATM 13987 O  O   . HOH   Y  7 .   ? -40.802 15.485  -20.534  1.00 45.80  ? 912  HOH   A O   1 
HETATM 13988 O  O   . HOH   Y  7 .   ? -51.446 15.051  -15.506  1.00 47.74  ? 913  HOH   A O   1 
HETATM 13989 O  O   . HOH   Y  7 .   ? -15.304 -10.924 -37.419  1.00 58.67  ? 914  HOH   A O   1 
HETATM 13990 O  O   . HOH   Y  7 .   ? -27.768 18.414  -42.879  1.00 50.62  ? 915  HOH   A O   1 
HETATM 13991 O  O   . HOH   Y  7 .   ? -56.886 30.095  -43.291  1.00 61.13  ? 916  HOH   A O   1 
HETATM 13992 O  O   . HOH   Y  7 .   ? -60.042 22.142  -46.747  1.00 61.27  ? 917  HOH   A O   1 
HETATM 13993 O  O   . HOH   Y  7 .   ? -32.888 0.413   -38.252  1.00 46.08  ? 918  HOH   A O   1 
HETATM 13994 O  O   . HOH   Y  7 .   ? -20.360 15.729  -43.757  1.00 45.52  ? 919  HOH   A O   1 
HETATM 13995 O  O   . HOH   Y  7 .   ? -55.878 15.114  -56.865  1.00 59.83  ? 920  HOH   A O   1 
HETATM 13996 O  O   . HOH   Y  7 .   ? -21.044 -10.817 -32.945  1.00 57.93  ? 921  HOH   A O   1 
HETATM 13997 O  O   . HOH   Y  7 .   ? -25.824 -1.625  -25.372  1.00 35.32  ? 922  HOH   A O   1 
HETATM 13998 O  O   . HOH   Y  7 .   ? -33.813 -6.583  -62.156  1.00 54.35  ? 923  HOH   A O   1 
HETATM 13999 O  O   . HOH   Y  7 .   ? -31.423 25.364  -34.519  1.00 42.52  ? 924  HOH   A O   1 
HETATM 14000 O  O   . HOH   Y  7 .   ? -42.475 -3.250  -59.341  1.00 39.49  ? 925  HOH   A O   1 
HETATM 14001 O  O   . HOH   Y  7 .   ? -24.104 -9.164  -49.362  1.00 51.79  ? 926  HOH   A O   1 
HETATM 14002 O  O   . HOH   Y  7 .   ? -40.199 4.748   -45.626  1.00 35.83  ? 927  HOH   A O   1 
HETATM 14003 O  O   . HOH   Y  7 .   ? -29.731 3.950   -27.830  1.00 36.49  ? 928  HOH   A O   1 
HETATM 14004 O  O   . HOH   Y  7 .   ? -26.706 6.243   -29.682  1.00 39.34  ? 929  HOH   A O   1 
HETATM 14005 O  O   . HOH   Y  7 .   ? -42.783 -7.388  -37.531  1.00 51.55  ? 930  HOH   A O   1 
HETATM 14006 O  O   . HOH   Y  7 .   ? -30.767 23.984  -39.644  1.00 44.65  ? 931  HOH   A O   1 
HETATM 14007 O  O   . HOH   Y  7 .   ? -22.365 4.221   -48.844  1.00 35.62  ? 932  HOH   A O   1 
HETATM 14008 O  O   . HOH   Y  7 .   ? -48.064 15.140  -53.709  1.00 41.48  ? 933  HOH   A O   1 
HETATM 14009 O  O   . HOH   Y  7 .   ? -14.575 -2.186  -8.593   1.00 49.94  ? 934  HOH   A O   1 
HETATM 14010 O  O   . HOH   Y  7 .   ? -17.099 14.572  -33.129  1.00 48.04  ? 935  HOH   A O   1 
HETATM 14011 O  O   . HOH   Y  7 .   ? -21.515 8.277   -40.265  1.00 36.40  ? 936  HOH   A O   1 
HETATM 14012 O  O   . HOH   Y  7 .   ? -43.343 16.638  -32.717  1.00 35.99  ? 937  HOH   A O   1 
HETATM 14013 O  O   . HOH   Y  7 .   ? -15.473 13.507  -35.044  1.00 55.63  ? 938  HOH   A O   1 
HETATM 14014 O  O   . HOH   Y  7 .   ? -26.963 10.991  -45.436  1.00 30.01  ? 939  HOH   A O   1 
HETATM 14015 O  O   . HOH   Y  7 .   ? -38.905 23.171  -32.481  1.00 45.36  ? 940  HOH   A O   1 
HETATM 14016 O  O   . HOH   Y  7 .   ? -26.935 -4.172  -39.498  1.00 33.32  ? 941  HOH   A O   1 
HETATM 14017 O  O   . HOH   Y  7 .   ? -42.842 11.126  -24.197  1.00 39.23  ? 942  HOH   A O   1 
HETATM 14018 O  O   . HOH   Y  7 .   ? -21.164 4.902   -58.939  1.00 55.41  ? 943  HOH   A O   1 
HETATM 14019 O  O   . HOH   Y  7 .   ? -53.693 22.091  -60.119  1.00 53.35  ? 944  HOH   A O   1 
HETATM 14020 O  O   . HOH   Y  7 .   ? -40.017 7.643   -25.552  1.00 43.27  ? 945  HOH   A O   1 
HETATM 14021 O  O   . HOH   Y  7 .   ? -24.856 -6.031  -20.260  1.00 40.18  ? 946  HOH   A O   1 
HETATM 14022 O  O   . HOH   Y  7 .   ? -45.664 27.116  -53.385  1.00 48.95  ? 947  HOH   A O   1 
HETATM 14023 O  O   . HOH   Y  7 .   ? -47.179 11.262  -53.966  1.00 42.54  ? 948  HOH   A O   1 
HETATM 14024 O  O   . HOH   Y  7 .   ? -27.412 1.604   -36.897  1.00 50.67  ? 949  HOH   A O   1 
HETATM 14025 O  O   . HOH   Y  7 .   ? -27.415 -4.833  -51.709  1.00 32.96  ? 950  HOH   A O   1 
HETATM 14026 O  O   . HOH   Y  7 .   ? -28.167 2.419   -43.505  1.00 31.12  ? 951  HOH   A O   1 
HETATM 14027 O  O   . HOH   Y  7 .   ? -45.171 -1.312  -60.062  1.00 41.68  ? 952  HOH   A O   1 
HETATM 14028 O  O   . HOH   Y  7 .   ? -31.062 25.283  -21.544  1.00 39.45  ? 953  HOH   A O   1 
HETATM 14029 O  O   . HOH   Y  7 .   ? -38.555 20.401  -24.890  1.00 39.68  ? 954  HOH   A O   1 
HETATM 14030 O  O   . HOH   Y  7 .   ? -31.514 11.129  -30.769  1.00 54.92  ? 955  HOH   A O   1 
HETATM 14031 O  O   . HOH   Y  7 .   ? -40.947 -0.533  -44.259  1.00 52.46  ? 956  HOH   A O   1 
HETATM 14032 O  O   . HOH   Y  7 .   ? -21.802 18.466  -33.347  1.00 51.69  ? 957  HOH   A O   1 
HETATM 14033 O  O   . HOH   Y  7 .   ? -39.716 -3.293  -61.510  1.00 36.07  ? 958  HOH   A O   1 
HETATM 14034 O  O   . HOH   Y  7 .   ? -24.203 -4.570  -51.940  1.00 44.96  ? 959  HOH   A O   1 
HETATM 14035 O  O   . HOH   Y  7 .   ? -33.056 9.861   -54.962  1.00 36.74  ? 960  HOH   A O   1 
HETATM 14036 O  O   . HOH   Y  7 .   ? -48.107 26.688  -52.689  1.00 40.79  ? 961  HOH   A O   1 
HETATM 14037 O  O   . HOH   Y  7 .   ? -51.928 9.806   -48.393  1.00 40.13  ? 962  HOH   A O   1 
HETATM 14038 O  O   . HOH   Y  7 .   ? -39.256 20.836  -12.497  1.00 44.02  ? 963  HOH   A O   1 
HETATM 14039 O  O   . HOH   Y  7 .   ? -20.409 16.076  -22.649  1.00 43.09  ? 964  HOH   A O   1 
HETATM 14040 O  O   . HOH   Y  7 .   ? -41.479 13.904  -36.838  1.00 35.71  ? 965  HOH   A O   1 
HETATM 14041 O  O   . HOH   Y  7 .   ? -15.719 13.800  -50.781  1.00 43.36  ? 966  HOH   A O   1 
HETATM 14042 O  O   . HOH   Y  7 .   ? -6.657  -2.237  -33.657  1.00 50.20  ? 967  HOH   A O   1 
HETATM 14043 O  O   . HOH   Y  7 .   ? -28.632 4.312   -30.596  1.00 33.18  ? 968  HOH   A O   1 
HETATM 14044 O  O   . HOH   Y  7 .   ? -43.034 -3.915  -56.453  1.00 35.40  ? 969  HOH   A O   1 
HETATM 14045 O  O   . HOH   Y  7 .   ? -41.305 1.926   -46.378  1.00 38.50  ? 970  HOH   A O   1 
HETATM 14046 O  O   . HOH   Y  7 .   ? -22.402 3.104   -46.171  1.00 41.39  ? 971  HOH   A O   1 
HETATM 14047 O  O   . HOH   Y  7 .   ? -50.608 -1.654  -50.365  1.00 47.83  ? 972  HOH   A O   1 
HETATM 14048 O  O   . HOH   Y  7 .   ? -44.266 7.050   -50.070  1.00 50.66  ? 973  HOH   A O   1 
HETATM 14049 O  O   . HOH   Y  7 .   ? -54.096 10.845  -43.035  1.00 48.27  ? 974  HOH   A O   1 
HETATM 14050 O  O   . HOH   Y  7 .   ? -18.511 6.117   -30.074  1.00 43.36  ? 975  HOH   A O   1 
HETATM 14051 O  O   . HOH   Y  7 .   ? -35.916 15.882  -56.636  1.00 49.09  ? 976  HOH   A O   1 
HETATM 14052 O  O   . HOH   Y  7 .   ? -12.091 -4.908  -35.497  1.00 43.34  ? 977  HOH   A O   1 
HETATM 14053 O  O   . HOH   Y  7 .   ? -54.154 3.699   -56.467  1.00 49.35  ? 978  HOH   A O   1 
HETATM 14054 O  O   . HOH   Y  7 .   ? -47.655 4.594   -51.142  1.00 34.17  ? 979  HOH   A O   1 
HETATM 14055 O  O   . HOH   Y  7 .   ? -36.341 21.205  -33.763  1.00 33.17  ? 980  HOH   A O   1 
HETATM 14056 O  O   . HOH   Y  7 .   ? -30.195 -2.396  -31.086  1.00 37.97  ? 981  HOH   A O   1 
HETATM 14057 O  O   . HOH   Y  7 .   ? -48.653 18.262  -41.825  1.00 40.88  ? 982  HOH   A O   1 
HETATM 14058 O  O   . HOH   Y  7 .   ? -32.826 29.680  -36.509  1.00 47.35  ? 983  HOH   A O   1 
HETATM 14059 O  O   . HOH   Y  7 .   ? -31.058 -3.465  -45.427  1.00 39.57  ? 984  HOH   A O   1 
HETATM 14060 O  O   . HOH   Y  7 .   ? -25.985 17.607  -45.121  1.00 42.19  ? 985  HOH   A O   1 
HETATM 14061 O  O   . HOH   Y  7 .   ? -27.526 17.827  -47.197  1.00 41.14  ? 986  HOH   A O   1 
HETATM 14062 O  O   . HOH   Y  7 .   ? -28.501 -3.286  -46.985  1.00 38.59  ? 987  HOH   A O   1 
HETATM 14063 O  O   . HOH   Y  7 .   ? -32.740 10.050  -59.109  1.00 49.67  ? 988  HOH   A O   1 
HETATM 14064 O  O   . HOH   Y  7 .   ? -42.025 10.677  -28.525  1.00 41.67  ? 989  HOH   A O   1 
HETATM 14065 O  O   . HOH   Y  7 .   ? -45.318 9.421   -24.446  1.00 52.69  ? 990  HOH   A O   1 
HETATM 14066 O  O   . HOH   Y  7 .   ? -26.618 11.098  -56.819  1.00 41.44  ? 991  HOH   A O   1 
HETATM 14067 O  O   . HOH   Y  7 .   ? -13.513 -12.361 -33.670  1.00 52.30  ? 992  HOH   A O   1 
HETATM 14068 O  O   . HOH   Y  7 .   ? -49.555 8.276   -55.200  1.00 40.59  ? 993  HOH   A O   1 
HETATM 14069 O  O   . HOH   Y  7 .   ? -34.246 -5.183  -41.197  1.00 51.91  ? 994  HOH   A O   1 
HETATM 14070 O  O   . HOH   Y  7 .   ? -29.200 10.936  -28.779  1.00 39.00  ? 995  HOH   A O   1 
HETATM 14071 O  O   . HOH   Y  7 .   ? -41.889 1.955   -38.867  1.00 45.51  ? 996  HOH   A O   1 
HETATM 14072 O  O   . HOH   Y  7 .   ? -51.976 3.107   -51.527  1.00 46.07  ? 997  HOH   A O   1 
HETATM 14073 O  O   . HOH   Y  7 .   ? -37.764 30.918  -24.190  1.00 46.78  ? 998  HOH   A O   1 
HETATM 14074 O  O   . HOH   Y  7 .   ? -20.398 -7.858  -7.855   1.00 54.39  ? 999  HOH   A O   1 
HETATM 14075 O  O   . HOH   Y  7 .   ? -39.074 14.591  -22.635  1.00 40.19  ? 1000 HOH   A O   1 
HETATM 14076 O  O   . HOH   Y  7 .   ? -9.345  2.099   -43.952  1.00 53.66  ? 1001 HOH   A O   1 
HETATM 14077 O  O   . HOH   Y  7 .   ? -43.560 14.782  -34.891  1.00 46.60  ? 1002 HOH   A O   1 
HETATM 14078 O  O   . HOH   Y  7 .   ? -19.281 16.458  -54.246  1.00 55.07  ? 1003 HOH   A O   1 
HETATM 14079 O  O   . HOH   Y  7 .   ? -34.042 20.370  -54.380  1.00 50.89  ? 1004 HOH   A O   1 
HETATM 14080 O  O   . HOH   Y  7 .   ? -28.085 18.909  -32.927  1.00 43.34  ? 1005 HOH   A O   1 
HETATM 14081 O  O   . HOH   Y  7 .   ? -47.929 -1.236  -46.553  1.00 50.71  ? 1006 HOH   A O   1 
HETATM 14082 O  O   . HOH   Y  7 .   ? -19.087 -10.842 -44.564  1.00 51.15  ? 1007 HOH   A O   1 
HETATM 14083 O  O   . HOH   Y  7 .   ? -31.474 7.453   -22.532  1.00 34.33  ? 1008 HOH   A O   1 
HETATM 14084 O  O   . HOH   Y  7 .   ? -39.689 25.057  -49.773  1.00 42.62  ? 1009 HOH   A O   1 
HETATM 14085 O  O   . HOH   Y  7 .   ? -45.606 28.302  -39.779  1.00 47.57  ? 1010 HOH   A O   1 
HETATM 14086 O  O   . HOH   Y  7 .   ? -38.122 5.881   -43.637  1.00 50.14  ? 1011 HOH   A O   1 
HETATM 14087 O  O   . HOH   Y  7 .   ? -40.770 11.678  -35.599  1.00 35.26  ? 1012 HOH   A O   1 
HETATM 14088 O  O   . HOH   Y  7 .   ? -21.012 18.024  -24.424  1.00 61.12  ? 1013 HOH   A O   1 
HETATM 14089 O  O   . HOH   Y  7 .   ? -38.564 -10.821 -54.388  1.00 46.59  ? 1014 HOH   A O   1 
HETATM 14090 O  O   . HOH   Y  7 .   ? -30.292 6.335   -26.044  1.00 43.64  ? 1015 HOH   A O   1 
HETATM 14091 O  O   . HOH   Y  7 .   ? -19.812 8.586   -29.642  1.00 42.97  ? 1016 HOH   A O   1 
HETATM 14092 O  O   . HOH   Y  7 .   ? -17.622 17.150  -33.548  1.00 63.00  ? 1017 HOH   A O   1 
HETATM 14093 O  O   . HOH   Y  7 .   ? -11.251 -4.917  -38.744  1.00 59.68  ? 1018 HOH   A O   1 
HETATM 14094 O  O   . HOH   Y  7 .   ? -33.366 25.394  -20.345  1.00 39.15  ? 1019 HOH   A O   1 
HETATM 14095 O  O   . HOH   Y  7 .   ? -22.813 18.424  -19.042  1.00 44.87  ? 1020 HOH   A O   1 
HETATM 14096 O  O   . HOH   Y  7 .   ? -8.042  12.159  -40.695  1.00 56.53  ? 1021 HOH   A O   1 
HETATM 14097 O  O   . HOH   Y  7 .   ? -5.553  3.264   -38.582  1.00 52.76  ? 1022 HOH   A O   1 
HETATM 14098 O  O   . HOH   Y  7 .   ? -11.989 2.158   -20.728  1.00 46.81  ? 1023 HOH   A O   1 
HETATM 14099 O  O   . HOH   Y  7 .   ? -35.434 -8.623  -39.241  1.00 40.14  ? 1024 HOH   A O   1 
HETATM 14100 O  O   . HOH   Y  7 .   ? -33.093 -4.108  -43.445  1.00 50.93  ? 1025 HOH   A O   1 
HETATM 14101 O  O   . HOH   Y  7 .   ? -40.637 13.063  -59.607  1.00 51.34  ? 1026 HOH   A O   1 
HETATM 14102 O  O   . HOH   Y  7 .   ? -47.811 36.111  -43.040  1.00 56.91  ? 1027 HOH   A O   1 
HETATM 14103 O  O   . HOH   Y  7 .   ? -19.057 15.974  -36.880  1.00 49.66  ? 1028 HOH   A O   1 
HETATM 14104 O  O   . HOH   Y  7 .   ? -31.877 -2.999  -35.075  1.00 34.76  ? 1029 HOH   A O   1 
HETATM 14105 O  O   . HOH   Y  7 .   ? -44.903 21.879  -58.013  1.00 38.18  ? 1030 HOH   A O   1 
HETATM 14106 O  O   . HOH   Y  7 .   ? -42.036 13.331  -32.548  1.00 56.04  ? 1031 HOH   A O   1 
HETATM 14107 O  O   . HOH   Y  7 .   ? -39.416 11.115  -32.916  1.00 39.80  ? 1032 HOH   A O   1 
HETATM 14108 O  O   . HOH   Y  7 .   ? -53.402 17.357  -15.892  1.00 49.63  ? 1033 HOH   A O   1 
HETATM 14109 O  O   . HOH   Y  7 .   ? -18.722 18.943  -25.104  1.00 57.64  ? 1034 HOH   A O   1 
HETATM 14110 O  O   . HOH   Y  7 .   ? -28.114 24.867  -20.722  1.00 53.98  ? 1035 HOH   A O   1 
HETATM 14111 O  O   . HOH   Y  7 .   ? -47.253 18.952  -58.016  1.00 55.07  ? 1036 HOH   A O   1 
HETATM 14112 O  O   . HOH   Y  7 .   ? -53.372 16.888  -59.697  1.00 66.04  ? 1037 HOH   A O   1 
HETATM 14113 O  O   . HOH   Y  7 .   ? -24.090 6.408   -60.942  1.00 46.57  ? 1038 HOH   A O   1 
HETATM 14114 O  O   . HOH   Y  7 .   ? -28.975 -13.198 -55.313  1.00 50.09  ? 1039 HOH   A O   1 
HETATM 14115 O  O   . HOH   Y  7 .   ? -52.146 3.218   -28.759  1.00 69.07  ? 1040 HOH   A O   1 
HETATM 14116 O  O   . HOH   Y  7 .   ? -24.341 -24.617 -36.180  1.00 47.31  ? 1041 HOH   A O   1 
HETATM 14117 O  O   . HOH   Y  7 .   ? -15.714 16.640  -50.180  1.00 54.83  ? 1042 HOH   A O   1 
HETATM 14118 O  O   . HOH   Y  7 .   ? -19.445 -5.111  -15.605  1.00 44.85  ? 1043 HOH   A O   1 
HETATM 14119 O  O   . HOH   Y  7 .   ? -21.719 -12.617 -35.517  1.00 43.54  ? 1044 HOH   A O   1 
HETATM 14120 O  O   . HOH   Y  7 .   ? -53.380 5.224   -41.058  1.00 54.87  ? 1045 HOH   A O   1 
HETATM 14121 O  O   . HOH   Y  7 .   ? -42.094 -0.073  -36.757  1.00 47.99  ? 1046 HOH   A O   1 
HETATM 14122 O  O   . HOH   Y  7 .   ? -19.486 -2.810  -50.137  1.00 51.06  ? 1047 HOH   A O   1 
HETATM 14123 O  O   . HOH   Y  7 .   ? -54.312 9.907   -46.739  1.00 54.19  ? 1048 HOH   A O   1 
HETATM 14124 O  O   . HOH   Y  7 .   ? -45.207 36.363  -53.707  1.00 54.05  ? 1049 HOH   A O   1 
HETATM 14125 O  O   . HOH   Y  7 .   ? -48.077 5.443   -59.338  1.00 51.70  ? 1050 HOH   A O   1 
HETATM 14126 O  O   . HOH   Y  7 .   ? -21.464 6.202   -52.576  1.00 53.04  ? 1051 HOH   A O   1 
HETATM 14127 O  O   . HOH   Y  7 .   ? -24.518 16.358  -36.002  1.00 45.36  ? 1052 HOH   A O   1 
HETATM 14128 O  O   . HOH   Y  7 .   ? -50.038 20.375  -40.592  1.00 38.06  ? 1053 HOH   A O   1 
HETATM 14129 O  O   . HOH   Y  7 .   ? -49.099 -3.912  -49.321  1.00 59.02  ? 1054 HOH   A O   1 
HETATM 14130 O  O   . HOH   Y  7 .   ? -23.593 20.008  -51.115  1.00 60.43  ? 1055 HOH   A O   1 
HETATM 14131 O  O   . HOH   Y  7 .   ? -48.163 11.152  -57.343  1.00 60.37  ? 1056 HOH   A O   1 
HETATM 14132 O  O   . HOH   Y  7 .   ? -28.923 8.071   -28.450  1.00 51.97  ? 1057 HOH   A O   1 
HETATM 14133 O  O   . HOH   Y  7 .   ? -36.496 -19.586 -53.675  1.00 57.45  ? 1058 HOH   A O   1 
HETATM 14134 O  O   . HOH   Y  7 .   ? -39.893 29.205  -37.473  1.00 56.44  ? 1059 HOH   A O   1 
HETATM 14135 O  O   . HOH   Y  7 .   ? -67.596 10.967  -51.588  1.00 54.73  ? 1060 HOH   A O   1 
HETATM 14136 O  O   . HOH   Y  7 .   ? -46.931 15.230  -58.251  1.00 50.65  ? 1061 HOH   A O   1 
HETATM 14137 O  O   . HOH   Y  7 .   ? -55.144 20.745  -59.096  1.00 50.27  ? 1062 HOH   A O   1 
HETATM 14138 O  O   . HOH   Y  7 .   ? -4.525  -5.197  -23.731  1.00 48.44  ? 1063 HOH   A O   1 
HETATM 14139 O  O   . HOH   Y  7 .   ? -28.143 -7.341  -19.096  1.00 55.73  ? 1064 HOH   A O   1 
HETATM 14140 O  O   . HOH   Y  7 .   ? -28.393 2.898   -33.225  1.00 59.16  ? 1065 HOH   A O   1 
HETATM 14141 O  O   . HOH   Y  7 .   ? -49.274 27.038  -55.421  1.00 48.02  ? 1066 HOH   A O   1 
HETATM 14142 O  O   . HOH   Y  7 .   ? -24.134 -8.547  -59.376  1.00 55.00  ? 1067 HOH   A O   1 
HETATM 14143 O  O   . HOH   Y  7 .   ? -22.381 18.543  -44.348  1.00 62.96  ? 1068 HOH   A O   1 
HETATM 14144 O  O   . HOH   Y  7 .   ? -43.260 24.463  -56.678  1.00 60.33  ? 1069 HOH   A O   1 
HETATM 14145 O  O   . HOH   Y  7 .   ? -23.117 -12.316 -32.958  1.00 62.63  ? 1070 HOH   A O   1 
HETATM 14146 O  O   . HOH   Y  7 .   ? -25.124 17.526  -33.418  1.00 64.31  ? 1071 HOH   A O   1 
HETATM 14147 O  O   . HOH   Y  7 .   ? -1.194  -1.251  -25.272  1.00 64.74  ? 1072 HOH   A O   1 
HETATM 14148 O  O   . HOH   Y  7 .   ? -37.772 24.931  -51.714  1.00 44.01  ? 1073 HOH   A O   1 
HETATM 14149 O  O   . HOH   Y  7 .   ? -43.591 8.557   -26.048  1.00 56.00  ? 1074 HOH   A O   1 
HETATM 14150 O  O   . HOH   Y  7 .   ? -28.146 11.454  -60.684  1.00 61.63  ? 1075 HOH   A O   1 
HETATM 14151 O  O   . HOH   Y  7 .   ? -14.487 6.653   -50.329  1.00 46.49  ? 1076 HOH   A O   1 
HETATM 14152 O  O   . HOH   Y  7 .   ? -38.411 24.948  -47.100  1.00 50.94  ? 1077 HOH   A O   1 
HETATM 14153 O  O   . HOH   Y  7 .   ? -53.895 23.370  -26.223  1.00 53.51  ? 1078 HOH   A O   1 
HETATM 14154 O  O   . HOH   Y  7 .   ? -32.438 -3.679  -32.557  1.00 51.19  ? 1079 HOH   A O   1 
HETATM 14155 O  O   . HOH   Y  7 .   ? -38.123 25.686  -44.205  1.00 42.31  ? 1080 HOH   A O   1 
HETATM 14156 O  O   . HOH   Y  7 .   ? -50.069 6.385   -56.918  1.00 45.24  ? 1081 HOH   A O   1 
HETATM 14157 O  O   . HOH   Y  7 .   ? -32.857 0.342   -35.307  1.00 53.54  ? 1082 HOH   A O   1 
HETATM 14158 O  O   . HOH   Y  7 .   ? -38.512 27.410  -42.806  1.00 49.51  ? 1083 HOH   A O   1 
HETATM 14159 O  O   . HOH   Y  7 .   ? -28.932 12.639  -57.523  1.00 38.52  ? 1084 HOH   A O   1 
HETATM 14160 O  O   . HOH   Y  7 .   ? -42.009 -10.250 -58.426  1.00 54.36  ? 1085 HOH   A O   1 
HETATM 14161 O  O   . HOH   Y  7 .   ? -17.413 5.870   -51.374  1.00 50.31  ? 1086 HOH   A O   1 
HETATM 14162 O  O   . HOH   Y  7 .   ? -54.102 4.689   -23.189  1.00 56.62  ? 1087 HOH   A O   1 
HETATM 14163 O  O   . HOH   Y  7 .   ? -32.739 11.391  -57.133  1.00 41.41  ? 1088 HOH   A O   1 
HETATM 14164 O  O   . HOH   Y  7 .   ? -50.118 10.411  -59.136  1.00 53.85  ? 1089 HOH   A O   1 
HETATM 14165 O  O   . HOH   Y  7 .   ? -20.848 18.157  -41.619  1.00 55.00  ? 1090 HOH   A O   1 
HETATM 14166 O  O   . HOH   Y  7 .   ? -55.648 20.892  -27.284  1.00 58.76  ? 1091 HOH   A O   1 
HETATM 14167 O  O   . HOH   Z  7 .   ? -40.509 10.090  -16.308  1.00 38.32  ? 901  HOH   B O   1 
HETATM 14168 O  O   . HOH   Z  7 .   ? -50.695 9.099   -11.142  1.00 42.63  ? 902  HOH   B O   1 
HETATM 14169 O  O   . HOH   Z  7 .   ? -29.484 3.097   6.235    1.00 34.55  ? 903  HOH   B O   1 
HETATM 14170 O  O   . HOH   Z  7 .   ? -42.708 -1.422  -5.652   1.00 37.16  ? 904  HOH   B O   1 
HETATM 14171 O  O   . HOH   Z  7 .   ? -50.125 10.673  14.135   1.00 48.95  ? 905  HOH   B O   1 
HETATM 14172 O  O   . HOH   Z  7 .   ? -27.591 20.941  1.296    1.00 54.80  ? 906  HOH   B O   1 
HETATM 14173 O  O   . HOH   Z  7 .   ? -43.175 5.764   -18.927  1.00 53.80  ? 907  HOH   B O   1 
HETATM 14174 O  O   . HOH   Z  7 .   ? -69.343 13.833  13.463   1.00 55.03  ? 908  HOH   B O   1 
HETATM 14175 O  O   . HOH   Z  7 .   ? -52.598 -6.502  -13.558  1.00 53.20  ? 909  HOH   B O   1 
HETATM 14176 O  O   . HOH   Z  7 .   ? -22.476 6.748   9.541    1.00 31.02  ? 910  HOH   B O   1 
HETATM 14177 O  O   . HOH   Z  7 .   ? -5.850  19.210  -34.580  1.00 52.37  ? 911  HOH   B O   1 
HETATM 14178 O  O   . HOH   Z  7 .   ? -39.502 -7.488  -17.718  1.00 41.45  ? 912  HOH   B O   1 
HETATM 14179 O  O   . HOH   Z  7 .   ? -39.623 -6.416  0.618    1.00 43.34  ? 913  HOH   B O   1 
HETATM 14180 O  O   . HOH   Z  7 .   ? -16.462 16.631  -14.014  1.00 50.59  ? 914  HOH   B O   1 
HETATM 14181 O  O   . HOH   Z  7 .   ? -46.818 5.672   -7.112   1.00 43.79  ? 915  HOH   B O   1 
HETATM 14182 O  O   . HOH   Z  7 .   ? -55.928 0.477   13.357   1.00 40.34  ? 916  HOH   B O   1 
HETATM 14183 O  O   . HOH   Z  7 .   ? -35.686 20.182  4.299    1.00 47.28  ? 917  HOH   B O   1 
HETATM 14184 O  O   . HOH   Z  7 .   ? -44.320 -0.322  -27.253  1.00 40.24  ? 918  HOH   B O   1 
HETATM 14185 O  O   . HOH   Z  7 .   ? -46.637 20.088  13.525   1.00 46.55  ? 919  HOH   B O   1 
HETATM 14186 O  O   . HOH   Z  7 .   ? -44.520 15.542  20.181   1.00 40.93  ? 920  HOH   B O   1 
HETATM 14187 O  O   . HOH   Z  7 .   ? -26.941 6.837   -9.990   1.00 39.43  ? 921  HOH   B O   1 
HETATM 14188 O  O   . HOH   Z  7 .   ? -14.580 14.609  6.567    1.00 53.52  ? 922  HOH   B O   1 
HETATM 14189 O  O   . HOH   Z  7 .   ? -43.205 7.503   -2.618   1.00 40.03  ? 923  HOH   B O   1 
HETATM 14190 O  O   . HOH   Z  7 .   ? -44.599 3.633   18.020   1.00 46.41  ? 924  HOH   B O   1 
HETATM 14191 O  O   . HOH   Z  7 .   ? -26.182 -4.524  4.511    1.00 39.18  ? 925  HOH   B O   1 
HETATM 14192 O  O   . HOH   Z  7 .   ? -34.318 7.595   15.364   1.00 41.13  ? 926  HOH   B O   1 
HETATM 14193 O  O   . HOH   Z  7 .   ? -41.157 5.603   -16.752  1.00 30.18  ? 927  HOH   B O   1 
HETATM 14194 O  O   . HOH   Z  7 .   ? -23.695 2.979   0.881    1.00 31.76  ? 928  HOH   B O   1 
HETATM 14195 O  O   . HOH   Z  7 .   ? -64.372 21.304  9.225    1.00 46.54  ? 929  HOH   B O   1 
HETATM 14196 O  O   . HOH   Z  7 .   ? -28.259 10.085  -11.628  1.00 35.72  ? 930  HOH   B O   1 
HETATM 14197 O  O   . HOH   Z  7 .   ? -26.357 11.348  4.221    1.00 40.33  ? 931  HOH   B O   1 
HETATM 14198 O  O   . HOH   Z  7 .   ? -33.848 -6.316  -20.116  1.00 42.95  ? 932  HOH   B O   1 
HETATM 14199 O  O   . HOH   Z  7 .   ? -25.946 17.730  5.772    1.00 38.59  ? 933  HOH   B O   1 
HETATM 14200 O  O   . HOH   Z  7 .   ? -27.761 19.392  3.564    1.00 58.77  ? 934  HOH   B O   1 
HETATM 14201 O  O   . HOH   Z  7 .   ? -44.254 19.068  11.526   1.00 42.64  ? 935  HOH   B O   1 
HETATM 14202 O  O   . HOH   Z  7 .   ? -55.767 8.545   1.432    1.00 46.73  ? 936  HOH   B O   1 
HETATM 14203 O  O   . HOH   Z  7 .   ? -24.103 16.802  7.556    1.00 48.71  ? 937  HOH   B O   1 
HETATM 14204 O  O   . HOH   Z  7 .   ? -44.161 0.091   -14.690  1.00 40.03  ? 938  HOH   B O   1 
HETATM 14205 O  O   . HOH   Z  7 .   ? -4.940  4.223   -5.238   1.00 49.04  ? 939  HOH   B O   1 
HETATM 14206 O  O   . HOH   Z  7 .   ? -46.089 -1.806  -7.062   1.00 49.72  ? 940  HOH   B O   1 
HETATM 14207 O  O   . HOH   Z  7 .   ? -34.432 -3.177  -6.421   1.00 45.51  ? 941  HOH   B O   1 
HETATM 14208 O  O   . HOH   Z  7 .   ? -22.105 17.204  11.958   1.00 42.04  ? 942  HOH   B O   1 
HETATM 14209 O  O   . HOH   Z  7 .   ? -47.547 13.129  14.435   1.00 39.28  ? 943  HOH   B O   1 
HETATM 14210 O  O   . HOH   Z  7 .   ? -41.631 -6.437  -19.186  1.00 43.16  ? 944  HOH   B O   1 
HETATM 14211 O  O   . HOH   Z  7 .   ? -27.496 24.956  -0.379   1.00 43.97  ? 945  HOH   B O   1 
HETATM 14212 O  O   . HOH   Z  7 .   ? -17.911 17.310  -22.949  1.00 61.20  ? 946  HOH   B O   1 
HETATM 14213 O  O   . HOH   Z  7 .   ? -19.550 15.718  12.271   1.00 48.64  ? 947  HOH   B O   1 
HETATM 14214 O  O   . HOH   Z  7 .   ? -43.062 15.183  10.586   1.00 42.25  ? 948  HOH   B O   1 
HETATM 14215 O  O   . HOH   Z  7 .   ? -41.895 10.694  -11.157  1.00 42.49  ? 949  HOH   B O   1 
HETATM 14216 O  O   . HOH   Z  7 .   ? -10.941 18.049  -11.823  1.00 47.15  ? 950  HOH   B O   1 
HETATM 14217 O  O   . HOH   Z  7 .   ? -54.501 20.038  10.323   1.00 53.15  ? 951  HOH   B O   1 
HETATM 14218 O  O   . HOH   Z  7 .   ? -37.751 13.239  -13.878  1.00 47.28  ? 952  HOH   B O   1 
HETATM 14219 O  O   . HOH   Z  7 .   ? -25.106 11.460  -2.759   1.00 51.70  ? 953  HOH   B O   1 
HETATM 14220 O  O   . HOH   Z  7 .   ? -33.973 -2.895  3.647    1.00 43.93  ? 954  HOH   B O   1 
HETATM 14221 O  O   . HOH   Z  7 .   ? -21.721 16.231  -0.071   1.00 50.66  ? 955  HOH   B O   1 
HETATM 14222 O  O   . HOH   Z  7 .   ? -62.674 8.250   1.069    1.00 43.31  ? 956  HOH   B O   1 
HETATM 14223 O  O   . HOH   Z  7 .   ? -33.234 5.053   -8.529   1.00 53.86  ? 957  HOH   B O   1 
HETATM 14224 O  O   . HOH   Z  7 .   ? -27.506 9.003   -8.900   1.00 44.96  ? 958  HOH   B O   1 
HETATM 14225 O  O   . HOH   Z  7 .   ? -42.893 10.004  -15.646  1.00 43.91  ? 959  HOH   B O   1 
HETATM 14226 O  O   . HOH   Z  7 .   ? -16.122 20.604  2.510    1.00 45.06  ? 960  HOH   B O   1 
HETATM 14227 O  O   . HOH   Z  7 .   ? -43.861 14.229  24.296   1.00 48.06  ? 961  HOH   B O   1 
HETATM 14228 O  O   . HOH   Z  7 .   ? -31.601 8.072   -17.016  1.00 40.64  ? 962  HOH   B O   1 
HETATM 14229 O  O   . HOH   Z  7 .   ? -38.272 18.145  -0.793   1.00 38.62  ? 963  HOH   B O   1 
HETATM 14230 O  O   . HOH   Z  7 .   ? -23.173 18.703  -14.829  1.00 75.25  ? 964  HOH   B O   1 
HETATM 14231 O  O   . HOH   Z  7 .   ? -37.741 14.976  6.157    1.00 37.73  ? 965  HOH   B O   1 
HETATM 14232 O  O   . HOH   Z  7 .   ? -39.945 -7.832  -4.996   1.00 46.60  ? 966  HOH   B O   1 
HETATM 14233 O  O   . HOH   Z  7 .   ? -37.474 18.198  6.851    1.00 35.86  ? 967  HOH   B O   1 
HETATM 14234 O  O   . HOH   Z  7 .   ? -16.838 19.364  9.748    1.00 41.32  ? 968  HOH   B O   1 
HETATM 14235 O  O   . HOH   Z  7 .   ? -22.027 1.602   -9.637   1.00 47.16  ? 969  HOH   B O   1 
HETATM 14236 O  O   . HOH   Z  7 .   ? -55.824 -7.025  -11.276  1.00 35.61  ? 970  HOH   B O   1 
HETATM 14237 O  O   . HOH   Z  7 .   ? -24.391 14.479  -1.592   1.00 62.59  ? 971  HOH   B O   1 
HETATM 14238 O  O   . HOH   Z  7 .   ? -25.487 15.903  -8.543   1.00 40.72  ? 972  HOH   B O   1 
HETATM 14239 O  O   . HOH   Z  7 .   ? -52.990 5.234   -4.148   1.00 56.06  ? 973  HOH   B O   1 
HETATM 14240 O  O   . HOH   Z  7 .   ? -30.316 16.129  -11.201  1.00 50.48  ? 974  HOH   B O   1 
HETATM 14241 O  O   . HOH   Z  7 .   ? -29.933 8.686   -13.368  1.00 36.19  ? 975  HOH   B O   1 
HETATM 14242 O  O   . HOH   Z  7 .   ? -50.139 2.249   -1.577   1.00 45.51  ? 976  HOH   B O   1 
HETATM 14243 O  O   . HOH   Z  7 .   ? -41.965 25.712  21.271   1.00 58.39  ? 977  HOH   B O   1 
HETATM 14244 O  O   . HOH   Z  7 .   ? -36.785 13.158  3.910    1.00 38.57  ? 978  HOH   B O   1 
HETATM 14245 O  O   . HOH   Z  7 .   ? -33.823 -2.356  7.947    1.00 49.94  ? 979  HOH   B O   1 
HETATM 14246 O  O   . HOH   Z  7 .   ? -13.737 21.223  -4.823   1.00 58.83  ? 980  HOH   B O   1 
HETATM 14247 O  O   . HOH   Z  7 .   ? -37.124 -8.928  -18.520  1.00 48.53  ? 981  HOH   B O   1 
HETATM 14248 O  O   . HOH   Z  7 .   ? -18.756 25.795  15.362   1.00 49.44  ? 982  HOH   B O   1 
HETATM 14249 O  O   . HOH   Z  7 .   ? -12.009 17.667  -24.823  1.00 47.24  ? 983  HOH   B O   1 
HETATM 14250 O  O   . HOH   Z  7 .   ? -11.541 2.835   -18.229  1.00 57.25  ? 984  HOH   B O   1 
HETATM 14251 O  O   . HOH   Z  7 .   ? -27.431 -6.454  -14.761  1.00 46.35  ? 985  HOH   B O   1 
HETATM 14252 O  O   . HOH   Z  7 .   ? -36.414 23.772  19.682   1.00 35.85  ? 986  HOH   B O   1 
HETATM 14253 O  O   . HOH   Z  7 .   ? -33.221 30.532  -1.542   1.00 52.62  ? 987  HOH   B O   1 
HETATM 14254 O  O   . HOH   Z  7 .   ? -40.483 8.680   -6.657   1.00 43.03  ? 988  HOH   B O   1 
HETATM 14255 O  O   . HOH   Z  7 .   ? -14.949 6.724   9.226    1.00 42.64  ? 989  HOH   B O   1 
HETATM 14256 O  O   . HOH   Z  7 .   ? -32.181 -3.180  5.688    1.00 36.07  ? 990  HOH   B O   1 
HETATM 14257 O  O   . HOH   Z  7 .   ? -29.922 -6.426  8.532    1.00 55.54  ? 991  HOH   B O   1 
HETATM 14258 O  O   . HOH   Z  7 .   ? -22.050 7.900   6.849    1.00 34.56  ? 992  HOH   B O   1 
HETATM 14259 O  O   . HOH   Z  7 .   ? -49.299 23.306  17.076   1.00 61.36  ? 993  HOH   B O   1 
HETATM 14260 O  O   . HOH   Z  7 .   ? -55.405 14.226  16.869   1.00 47.81  ? 994  HOH   B O   1 
HETATM 14261 O  O   . HOH   Z  7 .   ? -11.874 18.039  4.962    1.00 56.79  ? 995  HOH   B O   1 
HETATM 14262 O  O   . HOH   Z  7 .   ? -50.032 -4.308  10.173   1.00 58.95  ? 996  HOH   B O   1 
HETATM 14263 O  O   . HOH   Z  7 .   ? -14.526 12.893  -23.496  1.00 46.28  ? 997  HOH   B O   1 
HETATM 14264 O  O   . HOH   Z  7 .   ? -39.902 -1.335  11.650   1.00 41.47  ? 998  HOH   B O   1 
HETATM 14265 O  O   . HOH   Z  7 .   ? -31.217 4.498   -10.405  1.00 36.88  ? 999  HOH   B O   1 
HETATM 14266 O  O   . HOH   Z  7 .   ? -50.661 2.334   18.448   1.00 40.57  ? 1000 HOH   B O   1 
HETATM 14267 O  O   . HOH   Z  7 .   ? -52.227 7.446   1.881    1.00 47.45  ? 1001 HOH   B O   1 
HETATM 14268 O  O   . HOH   Z  7 .   ? -19.695 2.840   -8.963   1.00 39.87  ? 1002 HOH   B O   1 
HETATM 14269 O  O   . HOH   Z  7 .   ? -19.405 3.935   16.195   1.00 69.18  ? 1003 HOH   B O   1 
HETATM 14270 O  O   . HOH   Z  7 .   ? -42.216 10.402  -8.010   1.00 43.05  ? 1004 HOH   B O   1 
HETATM 14271 O  O   . HOH   Z  7 .   ? -23.277 -6.903  11.164   1.00 48.23  ? 1005 HOH   B O   1 
HETATM 14272 O  O   . HOH   Z  7 .   ? -29.272 3.120   17.707   1.00 54.41  ? 1006 HOH   B O   1 
HETATM 14273 O  O   . HOH   Z  7 .   ? -22.789 -5.174  -6.151   1.00 61.87  ? 1007 HOH   B O   1 
HETATM 14274 O  O   . HOH   Z  7 .   ? -42.041 9.252   -4.500   1.00 44.51  ? 1008 HOH   B O   1 
HETATM 14275 O  O   . HOH   Z  7 .   ? -40.860 -3.381  10.706   1.00 38.74  ? 1009 HOH   B O   1 
HETATM 14276 O  O   . HOH   Z  7 .   ? -26.233 6.390   -18.936  1.00 48.84  ? 1010 HOH   B O   1 
HETATM 14277 O  O   . HOH   Z  7 .   ? -47.659 13.851  17.411   1.00 48.09  ? 1011 HOH   B O   1 
HETATM 14278 O  O   . HOH   Z  7 .   ? -16.009 33.766  13.166   1.00 56.04  ? 1012 HOH   B O   1 
HETATM 14279 O  O   . HOH   Z  7 .   ? -45.571 7.965   -4.849   1.00 48.63  ? 1013 HOH   B O   1 
HETATM 14280 O  O   . HOH   Z  7 .   ? -29.479 -5.010  5.334    1.00 53.17  ? 1014 HOH   B O   1 
HETATM 14281 O  O   . HOH   Z  7 .   ? -44.259 8.672   -7.275   1.00 62.01  ? 1015 HOH   B O   1 
HETATM 14282 O  O   . HOH   Z  7 .   ? -40.463 28.375  21.952   1.00 55.92  ? 1016 HOH   B O   1 
HETATM 14283 O  O   . HOH   Z  7 .   ? -42.267 -12.649 -15.503  1.00 56.58  ? 1017 HOH   B O   1 
HETATM 14284 O  O   . HOH   Z  7 .   ? -45.036 -4.868  7.880    1.00 50.85  ? 1018 HOH   B O   1 
HETATM 14285 O  O   . HOH   Z  7 .   ? -16.305 23.164  14.115   1.00 65.66  ? 1019 HOH   B O   1 
HETATM 14286 O  O   . HOH   Z  7 .   ? -51.128 -3.235  0.265    1.00 55.05  ? 1020 HOH   B O   1 
HETATM 14287 O  O   . HOH   Z  7 .   ? -26.181 19.027  -11.921  1.00 58.78  ? 1021 HOH   B O   1 
HETATM 14288 O  O   . HOH   Z  7 .   ? -53.364 15.747  18.402   1.00 52.64  ? 1022 HOH   B O   1 
HETATM 14289 O  O   . HOH   Z  7 .   ? -15.564 16.288  8.921    1.00 49.61  ? 1023 HOH   B O   1 
HETATM 14290 O  O   . HOH   Z  7 .   ? -6.798  -0.712  -0.461   1.00 55.24  ? 1024 HOH   B O   1 
HETATM 14291 O  O   . HOH   Z  7 .   ? -65.236 3.828   17.944   1.00 42.11  ? 1025 HOH   B O   1 
HETATM 14292 O  O   . HOH   Z  7 .   ? -29.451 6.372   -11.142  1.00 45.74  ? 1026 HOH   B O   1 
HETATM 14293 O  O   . HOH   Z  7 .   ? -45.197 -12.205 -22.692  1.00 57.74  ? 1027 HOH   B O   1 
HETATM 14294 O  O   . HOH   Z  7 .   ? -43.208 18.368  -7.185   1.00 66.27  ? 1028 HOH   B O   1 
HETATM 14295 O  O   . HOH   Z  7 .   ? -34.478 -7.944  -17.861  1.00 55.64  ? 1029 HOH   B O   1 
HETATM 14296 O  O   . HOH   Z  7 .   ? -35.206 24.051  22.870   1.00 57.81  ? 1030 HOH   B O   1 
HETATM 14297 O  O   . HOH   Z  7 .   ? -46.499 -2.998  7.778    1.00 41.16  ? 1031 HOH   B O   1 
HETATM 14298 O  O   . HOH   Z  7 .   ? -33.055 -4.278  -28.045  1.00 56.69  ? 1032 HOH   B O   1 
HETATM 14299 O  O   . HOH   Z  7 .   ? -26.826 11.371  -6.568   1.00 65.18  ? 1033 HOH   B O   1 
HETATM 14300 O  O   . HOH   Z  7 .   ? -27.525 13.520  -7.930   1.00 38.71  ? 1034 HOH   B O   1 
HETATM 14301 O  O   . HOH   Z  7 .   ? -30.380 -2.918  -3.480   1.00 42.70  ? 1035 HOH   B O   1 
HETATM 14302 O  O   . HOH   Z  7 .   ? -57.084 0.631   15.973   1.00 42.97  ? 1036 HOH   B O   1 
HETATM 14303 O  O   . HOH   Z  7 .   ? -47.802 -5.163  3.778    1.00 54.73  ? 1037 HOH   B O   1 
HETATM 14304 O  O   . HOH   Z  7 .   ? -50.207 0.161   -23.544  1.00 59.49  ? 1038 HOH   B O   1 
HETATM 14305 O  O   . HOH   Z  7 .   ? -30.567 19.559  -2.438   1.00 55.28  ? 1039 HOH   B O   1 
HETATM 14306 O  O   . HOH   Z  7 .   ? -54.182 0.621   19.729   1.00 61.20  ? 1040 HOH   B O   1 
HETATM 14307 O  O   . HOH   Z  7 .   ? -46.497 -3.756  4.916    1.00 42.48  ? 1041 HOH   B O   1 
HETATM 14308 O  O   . HOH   Z  7 .   ? -31.871 3.980   21.742   1.00 55.67  ? 1042 HOH   B O   1 
HETATM 14309 O  O   . HOH   Z  7 .   ? -58.394 8.233   -11.899  1.00 50.31  ? 1043 HOH   B O   1 
HETATM 14310 O  O   . HOH   Z  7 .   ? -3.894  2.708   -3.158   1.00 49.74  ? 1044 HOH   B O   1 
HETATM 14311 O  O   . HOH   Z  7 .   ? -21.349 25.268  16.158   1.00 56.42  ? 1045 HOH   B O   1 
HETATM 14312 O  O   . HOH   Z  7 .   ? -25.095 -8.604  -14.452  1.00 51.37  ? 1046 HOH   B O   1 
HETATM 14313 O  O   . HOH   Z  7 .   ? -58.023 20.616  21.930   1.00 57.84  ? 1047 HOH   B O   1 
HETATM 14314 O  O   . HOH   Z  7 .   ? -27.388 -5.642  -0.291   1.00 52.54  ? 1048 HOH   B O   1 
HETATM 14315 O  O   . HOH   Z  7 .   ? -12.451 -6.569  -2.784   1.00 62.23  ? 1049 HOH   B O   1 
HETATM 14316 O  O   . HOH   Z  7 .   ? -33.181 3.620   18.973   1.00 58.74  ? 1050 HOH   B O   1 
HETATM 14317 O  O   . HOH   Z  7 .   ? -57.527 6.633   -13.307  1.00 57.97  ? 1051 HOH   B O   1 
HETATM 14318 O  O   . HOH   Z  7 .   ? -35.141 5.722   17.689   1.00 63.05  ? 1052 HOH   B O   1 
HETATM 14319 O  O   . HOH   AA 7 .   ? -1.666  48.778  -86.246  1.00 45.89  ? 901  HOH   C O   1 
HETATM 14320 O  O   . HOH   AA 7 .   ? 8.416   32.029  -71.216  1.00 50.23  ? 902  HOH   C O   1 
HETATM 14321 O  O   . HOH   AA 7 .   ? 59.920  29.238  -61.563  1.00 62.51  ? 903  HOH   C O   1 
HETATM 14322 O  O   . HOH   AA 7 .   ? 46.405  11.443  -84.739  1.00 62.95  ? 904  HOH   C O   1 
HETATM 14323 O  O   . HOH   AA 7 .   ? 18.728  31.125  -66.176  1.00 41.90  ? 905  HOH   C O   1 
HETATM 14324 O  O   . HOH   AA 7 .   ? 29.653  38.083  -88.514  1.00 28.81  ? 906  HOH   C O   1 
HETATM 14325 O  O   . HOH   AA 7 .   ? 16.584  42.805  -76.678  1.00 31.57  ? 907  HOH   C O   1 
HETATM 14326 O  O   . HOH   AA 7 .   ? 36.732  34.555  -91.854  1.00 34.11  ? 908  HOH   C O   1 
HETATM 14327 O  O   . HOH   AA 7 .   ? 3.060   21.841  -68.463  1.00 63.81  ? 909  HOH   C O   1 
HETATM 14328 O  O   . HOH   AA 7 .   ? 42.657  24.639  -68.332  1.00 43.68  ? 910  HOH   C O   1 
HETATM 14329 O  O   . HOH   AA 7 .   ? 32.968  30.073  -86.399  1.00 35.99  ? 911  HOH   C O   1 
HETATM 14330 O  O   . HOH   AA 7 .   ? 18.619  33.822  -104.810 1.00 48.23  ? 912  HOH   C O   1 
HETATM 14331 O  O   . HOH   AA 7 .   ? 14.598  37.622  -100.502 1.00 38.27  ? 913  HOH   C O   1 
HETATM 14332 O  O   . HOH   AA 7 .   ? 31.589  32.032  -73.624  1.00 49.11  ? 914  HOH   C O   1 
HETATM 14333 O  O   . HOH   AA 7 .   ? 9.164   30.639  -96.375  1.00 47.33  ? 915  HOH   C O   1 
HETATM 14334 O  O   . HOH   AA 7 .   ? 23.598  20.901  -86.540  1.00 38.12  ? 916  HOH   C O   1 
HETATM 14335 O  O   . HOH   AA 7 .   ? 12.668  20.700  -95.743  1.00 43.45  ? 917  HOH   C O   1 
HETATM 14336 O  O   . HOH   AA 7 .   ? 28.768  25.169  -71.380  1.00 50.38  ? 918  HOH   C O   1 
HETATM 14337 O  O   . HOH   AA 7 .   ? 35.103  24.584  -89.998  1.00 46.96  ? 919  HOH   C O   1 
HETATM 14338 O  O   . HOH   AA 7 .   ? 33.221  23.426  -88.172  1.00 36.27  ? 920  HOH   C O   1 
HETATM 14339 O  O   . HOH   AA 7 .   ? 24.994  33.722  -97.815  1.00 33.54  ? 921  HOH   C O   1 
HETATM 14340 O  O   . HOH   AA 7 .   ? 23.168  17.700  -102.106 1.00 36.64  ? 922  HOH   C O   1 
HETATM 14341 O  O   . HOH   AA 7 .   ? 43.052  20.810  -85.118  1.00 46.20  ? 923  HOH   C O   1 
HETATM 14342 O  O   . HOH   AA 7 .   ? 17.535  47.591  -63.178  1.00 46.25  ? 924  HOH   C O   1 
HETATM 14343 O  O   . HOH   AA 7 .   ? 31.906  16.332  -82.082  1.00 48.00  ? 925  HOH   C O   1 
HETATM 14344 O  O   . HOH   AA 7 .   ? 40.102  24.229  -63.186  1.00 48.41  ? 926  HOH   C O   1 
HETATM 14345 O  O   . HOH   AA 7 .   ? 35.473  38.238  -83.361  1.00 38.59  ? 927  HOH   C O   1 
HETATM 14346 O  O   . HOH   AA 7 .   ? 33.163  14.995  -79.687  1.00 51.89  ? 928  HOH   C O   1 
HETATM 14347 O  O   . HOH   AA 7 .   ? 30.295  46.865  -61.721  1.00 56.50  ? 929  HOH   C O   1 
HETATM 14348 O  O   . HOH   AA 7 .   ? 20.390  49.378  -80.029  1.00 55.69  ? 930  HOH   C O   1 
HETATM 14349 O  O   . HOH   AA 7 .   ? 31.475  19.961  -83.636  1.00 54.73  ? 931  HOH   C O   1 
HETATM 14350 O  O   . HOH   AA 7 .   ? 54.087  37.052  -77.072  1.00 55.11  ? 932  HOH   C O   1 
HETATM 14351 O  O   . HOH   AA 7 .   ? 35.064  26.857  -80.870  1.00 61.12  ? 933  HOH   C O   1 
HETATM 14352 O  O   . HOH   AA 7 .   ? 21.224  26.138  -88.635  1.00 40.06  ? 934  HOH   C O   1 
HETATM 14353 O  O   . HOH   AA 7 .   ? 33.755  25.257  -74.017  1.00 40.21  ? 935  HOH   C O   1 
HETATM 14354 O  O   . HOH   AA 7 .   ? 20.897  23.046  -81.491  1.00 37.86  ? 936  HOH   C O   1 
HETATM 14355 O  O   . HOH   AA 7 .   ? 46.042  22.999  -67.873  1.00 41.69  ? 937  HOH   C O   1 
HETATM 14356 O  O   . HOH   AA 7 .   ? 32.307  34.216  -72.493  1.00 33.87  ? 938  HOH   C O   1 
HETATM 14357 O  O   . HOH   AA 7 .   ? 19.673  48.903  -64.804  1.00 45.67  ? 939  HOH   C O   1 
HETATM 14358 O  O   . HOH   AA 7 .   ? 12.549  35.166  -75.278  1.00 35.85  ? 940  HOH   C O   1 
HETATM 14359 O  O   . HOH   AA 7 .   ? 13.234  42.932  -75.334  1.00 44.03  ? 941  HOH   C O   1 
HETATM 14360 O  O   . HOH   AA 7 .   ? 11.686  28.221  -96.614  1.00 38.99  ? 942  HOH   C O   1 
HETATM 14361 O  O   . HOH   AA 7 .   ? 37.348  24.946  -82.334  1.00 46.99  ? 943  HOH   C O   1 
HETATM 14362 O  O   . HOH   AA 7 .   ? 49.093  38.619  -87.172  1.00 53.71  ? 944  HOH   C O   1 
HETATM 14363 O  O   . HOH   AA 7 .   ? 6.682   47.903  -68.724  1.00 42.44  ? 945  HOH   C O   1 
HETATM 14364 O  O   . HOH   AA 7 .   ? 25.042  34.489  -102.422 1.00 52.24  ? 946  HOH   C O   1 
HETATM 14365 O  O   . HOH   AA 7 .   ? 15.685  33.593  -79.737  1.00 47.46  ? 947  HOH   C O   1 
HETATM 14366 O  O   . HOH   AA 7 .   ? 7.074   33.820  -84.195  1.00 64.86  ? 948  HOH   C O   1 
HETATM 14367 O  O   . HOH   AA 7 .   ? 3.128   40.710  -95.751  1.00 45.72  ? 949  HOH   C O   1 
HETATM 14368 O  O   . HOH   AA 7 .   ? 33.119  45.526  -86.824  1.00 38.28  ? 950  HOH   C O   1 
HETATM 14369 O  O   . HOH   AA 7 .   ? 17.292  30.949  -71.231  1.00 41.03  ? 951  HOH   C O   1 
HETATM 14370 O  O   . HOH   AA 7 .   ? 16.090  35.276  -63.611  1.00 56.04  ? 952  HOH   C O   1 
HETATM 14371 O  O   . HOH   AA 7 .   ? 18.067  35.675  -65.567  1.00 35.67  ? 953  HOH   C O   1 
HETATM 14372 O  O   . HOH   AA 7 .   ? 19.300  49.045  -77.493  1.00 47.89  ? 954  HOH   C O   1 
HETATM 14373 O  O   . HOH   AA 7 .   ? 50.477  25.067  -80.343  1.00 59.67  ? 955  HOH   C O   1 
HETATM 14374 O  O   . HOH   AA 7 .   ? 14.921  41.154  -67.574  1.00 36.33  ? 956  HOH   C O   1 
HETATM 14375 O  O   . HOH   AA 7 .   ? 3.767   33.535  -99.422  1.00 40.45  ? 957  HOH   C O   1 
HETATM 14376 O  O   . HOH   AA 7 .   ? 15.009  22.262  -93.829  1.00 45.05  ? 958  HOH   C O   1 
HETATM 14377 O  O   . HOH   AA 7 .   ? 37.317  39.868  -72.830  1.00 40.36  ? 959  HOH   C O   1 
HETATM 14378 O  O   . HOH   AA 7 .   ? 16.255  25.889  -92.869  1.00 41.88  ? 960  HOH   C O   1 
HETATM 14379 O  O   . HOH   AA 7 .   ? 39.038  25.489  -100.207 1.00 46.28  ? 961  HOH   C O   1 
HETATM 14380 O  O   . HOH   AA 7 .   ? 26.068  36.101  -73.747  1.00 59.50  ? 962  HOH   C O   1 
HETATM 14381 O  O   . HOH   AA 7 .   ? 25.349  19.015  -104.191 1.00 54.92  ? 963  HOH   C O   1 
HETATM 14382 O  O   . HOH   AA 7 .   ? 48.330  23.391  -70.626  1.00 66.66  ? 964  HOH   C O   1 
HETATM 14383 O  O   . HOH   AA 7 .   ? 19.231  37.767  -99.699  1.00 39.20  ? 965  HOH   C O   1 
HETATM 14384 O  O   . HOH   AA 7 .   ? 40.446  15.456  -97.552  1.00 62.89  ? 966  HOH   C O   1 
HETATM 14385 O  O   . HOH   AA 7 .   ? 14.896  41.556  -55.088  1.00 40.43  ? 967  HOH   C O   1 
HETATM 14386 O  O   . HOH   AA 7 .   ? -3.509  33.029  -83.409  1.00 54.70  ? 968  HOH   C O   1 
HETATM 14387 O  O   . HOH   AA 7 .   ? 24.849  44.522  -76.074  1.00 37.68  ? 969  HOH   C O   1 
HETATM 14388 O  O   . HOH   AA 7 .   ? 40.012  10.986  -83.486  1.00 74.23  ? 970  HOH   C O   1 
HETATM 14389 O  O   . HOH   AA 7 .   ? 27.791  33.324  -65.492  1.00 52.82  ? 971  HOH   C O   1 
HETATM 14390 O  O   . HOH   AA 7 .   ? 5.272   45.920  -72.934  1.00 49.73  ? 972  HOH   C O   1 
HETATM 14391 O  O   . HOH   AA 7 .   ? 31.875  47.520  -67.526  1.00 48.84  ? 973  HOH   C O   1 
HETATM 14392 O  O   . HOH   AA 7 .   ? 45.625  20.046  -77.539  1.00 64.44  ? 974  HOH   C O   1 
HETATM 14393 O  O   . HOH   AA 7 .   ? 27.194  44.282  -88.119  1.00 41.31  ? 975  HOH   C O   1 
HETATM 14394 O  O   . HOH   AA 7 .   ? 37.269  23.841  -94.389  1.00 39.18  ? 976  HOH   C O   1 
HETATM 14395 O  O   . HOH   AA 7 .   ? 39.483  38.294  -73.345  1.00 39.39  ? 977  HOH   C O   1 
HETATM 14396 O  O   . HOH   AA 7 .   ? 17.194  15.635  -103.572 1.00 63.85  ? 978  HOH   C O   1 
HETATM 14397 O  O   . HOH   AA 7 .   ? 29.244  32.459  -69.054  1.00 28.41  ? 979  HOH   C O   1 
HETATM 14398 O  O   . HOH   AA 7 .   ? 21.947  23.048  -89.258  1.00 38.39  ? 980  HOH   C O   1 
HETATM 14399 O  O   . HOH   AA 7 .   ? 3.399   48.374  -71.048  1.00 50.80  ? 981  HOH   C O   1 
HETATM 14400 O  O   . HOH   AA 7 .   ? 30.851  31.307  -70.844  1.00 37.08  ? 982  HOH   C O   1 
HETATM 14401 O  O   . HOH   AA 7 .   ? 11.344  43.874  -92.745  1.00 46.55  ? 983  HOH   C O   1 
HETATM 14402 O  O   . HOH   AA 7 .   ? 44.239  34.234  -91.585  1.00 39.06  ? 984  HOH   C O   1 
HETATM 14403 O  O   . HOH   AA 7 .   ? 26.205  10.297  -80.882  1.00 47.87  ? 985  HOH   C O   1 
HETATM 14404 O  O   . HOH   AA 7 .   ? 30.598  45.085  -98.804  1.00 50.30  ? 986  HOH   C O   1 
HETATM 14405 O  O   . HOH   AA 7 .   ? 33.975  29.649  -79.758  1.00 48.73  ? 987  HOH   C O   1 
HETATM 14406 O  O   . HOH   AA 7 .   ? 3.543   27.125  -99.393  1.00 56.24  ? 988  HOH   C O   1 
HETATM 14407 O  O   . HOH   AA 7 .   ? 36.428  23.023  -66.821  1.00 68.92  ? 989  HOH   C O   1 
HETATM 14408 O  O   . HOH   AA 7 .   ? 37.174  33.361  -89.087  1.00 34.94  ? 990  HOH   C O   1 
HETATM 14409 O  O   . HOH   AA 7 .   ? 31.652  21.770  -85.950  1.00 51.42  ? 991  HOH   C O   1 
HETATM 14410 O  O   . HOH   AA 7 .   ? 22.459  28.246  -86.174  1.00 36.24  ? 992  HOH   C O   1 
HETATM 14411 O  O   . HOH   AA 7 .   ? 8.473   38.828  -100.684 1.00 48.54  ? 993  HOH   C O   1 
HETATM 14412 O  O   . HOH   AA 7 .   ? 10.650  12.266  -101.024 1.00 64.75  ? 994  HOH   C O   1 
HETATM 14413 O  O   . HOH   AA 7 .   ? 27.966  6.152   -92.085  1.00 59.10  ? 995  HOH   C O   1 
HETATM 14414 O  O   . HOH   AA 7 .   ? -6.024  39.506  -87.336  1.00 49.24  ? 996  HOH   C O   1 
HETATM 14415 O  O   . HOH   AA 7 .   ? 22.201  50.314  -63.880  1.00 59.19  ? 997  HOH   C O   1 
HETATM 14416 O  O   . HOH   AA 7 .   ? 40.457  36.235  -94.378  1.00 41.81  ? 998  HOH   C O   1 
HETATM 14417 O  O   . HOH   AA 7 .   ? 39.449  24.908  -65.875  1.00 58.15  ? 999  HOH   C O   1 
HETATM 14418 O  O   . HOH   AA 7 .   ? -10.438 27.448  -95.464  1.00 56.02  ? 1000 HOH   C O   1 
HETATM 14419 O  O   . HOH   AA 7 .   ? 44.566  28.312  -58.919  1.00 48.33  ? 1001 HOH   C O   1 
HETATM 14420 O  O   . HOH   AA 7 .   ? 4.528   43.576  -82.676  1.00 55.72  ? 1002 HOH   C O   1 
HETATM 14421 O  O   . HOH   AA 7 .   ? 8.442   48.778  -87.971  1.00 55.70  ? 1003 HOH   C O   1 
HETATM 14422 O  O   . HOH   AA 7 .   ? 29.595  38.291  -99.935  1.00 41.33  ? 1004 HOH   C O   1 
HETATM 14423 O  O   . HOH   AA 7 .   ? 13.620  33.449  -77.536  1.00 42.35  ? 1005 HOH   C O   1 
HETATM 14424 O  O   . HOH   AA 7 .   ? 28.081  36.692  -71.921  1.00 36.98  ? 1006 HOH   C O   1 
HETATM 14425 O  O   . HOH   AA 7 .   ? 43.524  24.739  -91.364  1.00 48.93  ? 1007 HOH   C O   1 
HETATM 14426 O  O   . HOH   AA 7 .   ? -1.213  32.459  -80.062  1.00 55.28  ? 1008 HOH   C O   1 
HETATM 14427 O  O   . HOH   AA 7 .   ? 47.309  23.090  -87.468  1.00 47.21  ? 1009 HOH   C O   1 
HETATM 14428 O  O   . HOH   AA 7 .   ? 59.237  38.548  -71.820  1.00 51.64  ? 1010 HOH   C O   1 
HETATM 14429 O  O   . HOH   AA 7 .   ? 25.533  20.144  -85.092  1.00 45.77  ? 1011 HOH   C O   1 
HETATM 14430 O  O   . HOH   AA 7 .   ? 17.222  32.012  -78.034  1.00 40.62  ? 1012 HOH   C O   1 
HETATM 14431 O  O   . HOH   AA 7 .   ? 4.157   21.173  -92.503  1.00 52.22  ? 1013 HOH   C O   1 
HETATM 14432 O  O   . HOH   AA 7 .   ? 9.184   45.677  -92.285  1.00 55.31  ? 1014 HOH   C O   1 
HETATM 14433 O  O   . HOH   AA 7 .   ? 6.170   36.585  -78.367  1.00 43.58  ? 1015 HOH   C O   1 
HETATM 14434 O  O   . HOH   AA 7 .   ? 43.080  41.230  -90.614  1.00 58.67  ? 1016 HOH   C O   1 
HETATM 14435 O  O   . HOH   AA 7 .   ? 34.539  34.906  -103.645 1.00 43.46  ? 1017 HOH   C O   1 
HETATM 14436 O  O   . HOH   AA 7 .   ? 39.982  25.278  -94.387  1.00 58.16  ? 1018 HOH   C O   1 
HETATM 14437 O  O   . HOH   AA 7 .   ? 15.020  32.676  -75.395  1.00 58.95  ? 1019 HOH   C O   1 
HETATM 14438 O  O   . HOH   AA 7 .   ? 19.094  32.218  -76.037  1.00 44.11  ? 1020 HOH   C O   1 
HETATM 14439 O  O   . HOH   AA 7 .   ? 8.180   44.474  -82.551  1.00 43.34  ? 1021 HOH   C O   1 
HETATM 14440 O  O   . HOH   AA 7 .   ? 47.528  38.370  -64.058  1.00 52.64  ? 1022 HOH   C O   1 
HETATM 14441 O  O   . HOH   AA 7 .   ? 36.515  46.458  -76.452  1.00 47.50  ? 1023 HOH   C O   1 
HETATM 14442 O  O   . HOH   AA 7 .   ? 24.033  15.181  -104.890 1.00 64.42  ? 1024 HOH   C O   1 
HETATM 14443 O  O   . HOH   AA 7 .   ? 11.227  27.394  -99.691  1.00 50.29  ? 1025 HOH   C O   1 
HETATM 14444 O  O   . HOH   AA 7 .   ? 42.813  22.048  -92.037  1.00 43.90  ? 1026 HOH   C O   1 
HETATM 14445 O  O   . HOH   AA 7 .   ? 29.230  44.095  -78.998  1.00 46.10  ? 1027 HOH   C O   1 
HETATM 14446 O  O   . HOH   AA 7 .   ? 56.765  27.113  -75.845  1.00 57.68  ? 1028 HOH   C O   1 
HETATM 14447 O  O   . HOH   AA 7 .   ? 9.375   41.396  -58.690  1.00 58.92  ? 1029 HOH   C O   1 
HETATM 14448 O  O   . HOH   AA 7 .   ? 14.347  46.431  -90.171  1.00 56.38  ? 1030 HOH   C O   1 
HETATM 14449 O  O   . HOH   AA 7 .   ? 52.349  42.217  -82.433  1.00 52.92  ? 1031 HOH   C O   1 
HETATM 14450 O  O   . HOH   AA 7 .   ? 16.875  11.559  -92.345  1.00 61.48  ? 1032 HOH   C O   1 
HETATM 14451 O  O   . HOH   AA 7 .   ? 32.877  22.195  -70.463  1.00 52.87  ? 1033 HOH   C O   1 
HETATM 14452 O  O   . HOH   AA 7 .   ? 29.843  46.560  -87.435  1.00 59.75  ? 1034 HOH   C O   1 
HETATM 14453 O  O   . HOH   AA 7 .   ? 24.916  49.285  -64.505  1.00 47.93  ? 1035 HOH   C O   1 
HETATM 14454 O  O   . HOH   AA 7 .   ? 32.092  30.231  -76.931  1.00 71.41  ? 1036 HOH   C O   1 
HETATM 14455 O  O   . HOH   AA 7 .   ? 24.392  20.906  -79.825  1.00 61.64  ? 1037 HOH   C O   1 
HETATM 14456 O  O   . HOH   AA 7 .   ? 31.738  27.803  -74.502  1.00 50.19  ? 1038 HOH   C O   1 
HETATM 14457 O  O   . HOH   AA 7 .   ? 38.402  21.580  -61.841  1.00 48.71  ? 1039 HOH   C O   1 
HETATM 14458 O  O   . HOH   AA 7 .   ? 19.014  28.242  -60.795  1.00 37.16  ? 1040 HOH   C O   1 
HETATM 14459 O  O   . HOH   AA 7 .   ? 2.090   35.266  -69.505  1.00 60.67  ? 1041 HOH   C O   1 
HETATM 14460 O  O   . HOH   AA 7 .   ? 29.855  35.051  -71.297  1.00 45.01  ? 1042 HOH   C O   1 
HETATM 14461 O  O   . HOH   AA 7 .   ? 40.386  7.555   -87.061  1.00 71.35  ? 1043 HOH   C O   1 
HETATM 14462 O  O   . HOH   AA 7 .   ? 12.772  44.741  -87.429  1.00 48.50  ? 1044 HOH   C O   1 
HETATM 14463 O  O   . HOH   AA 7 .   ? 27.915  21.685  -79.950  1.00 55.98  ? 1045 HOH   C O   1 
HETATM 14464 O  O   . HOH   AA 7 .   ? 60.677  36.172  -72.678  1.00 56.53  ? 1046 HOH   C O   1 
HETATM 14465 O  O   . HOH   AA 7 .   ? 2.193   40.724  -98.433  1.00 50.27  ? 1047 HOH   C O   1 
HETATM 14466 O  O   . HOH   AA 7 .   ? 11.447  46.563  -86.338  1.00 45.82  ? 1048 HOH   C O   1 
HETATM 14467 O  O   . HOH   AA 7 .   ? 2.161   39.381  -61.733  1.00 56.70  ? 1049 HOH   C O   1 
HETATM 14468 O  O   . HOH   AA 7 .   ? 12.924  44.468  -90.293  1.00 45.38  ? 1050 HOH   C O   1 
HETATM 14469 O  O   . HOH   AA 7 .   ? 40.579  38.979  -94.425  1.00 51.36  ? 1051 HOH   C O   1 
HETATM 14470 O  O   . HOH   AA 7 .   ? 24.906  51.006  -81.004  1.00 59.75  ? 1052 HOH   C O   1 
HETATM 14471 O  O   . HOH   AA 7 .   ? 26.131  37.501  -101.698 1.00 56.50  ? 1053 HOH   C O   1 
HETATM 14472 O  O   . HOH   AA 7 .   ? 29.827  47.654  -90.856  1.00 61.83  ? 1054 HOH   C O   1 
HETATM 14473 O  O   . HOH   AA 7 .   ? 16.540  53.821  -67.193  1.00 56.41  ? 1055 HOH   C O   1 
HETATM 14474 O  O   . HOH   AA 7 .   ? 0.630   33.368  -70.061  1.00 70.82  ? 1056 HOH   C O   1 
HETATM 14475 O  O   . HOH   AA 7 .   ? 37.641  16.810  -98.098  1.00 49.82  ? 1057 HOH   C O   1 
HETATM 14476 O  O   . HOH   AA 7 .   ? 24.333  35.535  -100.085 1.00 53.89  ? 1058 HOH   C O   1 
HETATM 14477 O  O   . HOH   AA 7 .   ? 47.933  8.565   -84.924  1.00 61.60  ? 1059 HOH   C O   1 
HETATM 14478 O  O   . HOH   AA 7 .   ? 45.356  39.548  -90.814  1.00 45.44  ? 1060 HOH   C O   1 
HETATM 14479 O  O   . HOH   AA 7 .   ? 43.627  40.058  -93.169  1.00 57.70  ? 1061 HOH   C O   1 
HETATM 14480 O  O   . HOH   AA 7 .   ? 26.937  40.264  -100.220 1.00 50.55  ? 1062 HOH   C O   1 
HETATM 14481 O  O   . HOH   BA 7 .   ? 33.262  42.689  -56.966  1.00 46.55  ? 901  HOH   D O   1 
HETATM 14482 O  O   . HOH   BA 7 .   ? 34.932  52.192  -58.961  1.00 45.32  ? 902  HOH   D O   1 
HETATM 14483 O  O   . HOH   BA 7 .   ? 38.476  51.906  -49.326  1.00 49.89  ? 903  HOH   D O   1 
HETATM 14484 O  O   . HOH   BA 7 .   ? 34.876  50.307  -32.783  1.00 43.75  ? 904  HOH   D O   1 
HETATM 14485 O  O   . HOH   BA 7 .   ? 2.173   10.666  -39.732  1.00 70.97  ? 905  HOH   D O   1 
HETATM 14486 O  O   . HOH   BA 7 .   ? 38.255  36.174  -23.624  1.00 59.91  ? 906  HOH   D O   1 
HETATM 14487 O  O   . HOH   BA 7 .   ? 26.881  39.149  -50.833  1.00 54.13  ? 907  HOH   D O   1 
HETATM 14488 O  O   . HOH   BA 7 .   ? 51.200  37.487  -57.596  1.00 46.29  ? 908  HOH   D O   1 
HETATM 14489 O  O   . HOH   BA 7 .   ? 7.560   26.094  -67.037  1.00 41.75  ? 909  HOH   D O   1 
HETATM 14490 O  O   . HOH   BA 7 .   ? 29.563  37.234  -54.575  1.00 43.14  ? 910  HOH   D O   1 
HETATM 14491 O  O   . HOH   BA 7 .   ? 26.173  40.980  -44.383  1.00 45.15  ? 911  HOH   D O   1 
HETATM 14492 O  O   . HOH   BA 7 .   ? 40.638  52.454  -54.970  1.00 54.82  ? 912  HOH   D O   1 
HETATM 14493 O  O   . HOH   BA 7 .   ? 18.378  25.765  -61.856  1.00 42.20  ? 913  HOH   D O   1 
HETATM 14494 O  O   . HOH   BA 7 .   ? 14.481  32.506  -18.966  1.00 49.66  ? 914  HOH   D O   1 
HETATM 14495 O  O   . HOH   BA 7 .   ? 18.131  13.512  -32.416  1.00 51.83  ? 915  HOH   D O   1 
HETATM 14496 O  O   . HOH   BA 7 .   ? 37.795  32.977  -42.133  1.00 31.29  ? 916  HOH   D O   1 
HETATM 14497 O  O   . HOH   BA 7 .   ? 31.080  42.971  -43.854  1.00 52.14  ? 917  HOH   D O   1 
HETATM 14498 O  O   . HOH   BA 7 .   ? 30.370  47.051  -57.580  1.00 50.86  ? 918  HOH   D O   1 
HETATM 14499 O  O   . HOH   BA 7 .   ? 38.864  25.460  -38.548  1.00 40.21  ? 919  HOH   D O   1 
HETATM 14500 O  O   . HOH   BA 7 .   ? 45.826  37.740  -37.626  1.00 42.14  ? 920  HOH   D O   1 
HETATM 14501 O  O   . HOH   BA 7 .   ? 9.301   36.769  -29.025  1.00 40.47  ? 921  HOH   D O   1 
HETATM 14502 O  O   . HOH   BA 7 .   ? 18.561  41.877  -38.087  1.00 46.39  ? 922  HOH   D O   1 
HETATM 14503 O  O   . HOH   BA 7 .   ? 32.337  45.523  -42.973  1.00 38.28  ? 923  HOH   D O   1 
HETATM 14504 O  O   . HOH   BA 7 .   ? 1.501   25.366  -69.773  1.00 67.08  ? 924  HOH   D O   1 
HETATM 14505 O  O   . HOH   BA 7 .   ? 31.501  22.802  -39.678  1.00 45.61  ? 925  HOH   D O   1 
HETATM 14506 O  O   . HOH   BA 7 .   ? 11.977  29.912  -28.409  1.00 40.58  ? 926  HOH   D O   1 
HETATM 14507 O  O   . HOH   BA 7 .   ? 32.556  34.952  -52.803  1.00 31.42  ? 927  HOH   D O   1 
HETATM 14508 O  O   . HOH   BA 7 .   ? 37.744  48.702  -34.256  1.00 48.53  ? 928  HOH   D O   1 
HETATM 14509 O  O   . HOH   BA 7 .   ? 32.677  20.346  -63.209  1.00 41.09  ? 929  HOH   D O   1 
HETATM 14510 O  O   . HOH   BA 7 .   ? 28.097  16.094  -60.800  1.00 40.12  ? 930  HOH   D O   1 
HETATM 14511 O  O   . HOH   BA 7 .   ? 21.064  31.589  -19.176  1.00 49.71  ? 931  HOH   D O   1 
HETATM 14512 O  O   . HOH   BA 7 .   ? 28.118  44.617  -37.107  1.00 36.71  ? 932  HOH   D O   1 
HETATM 14513 O  O   . HOH   BA 7 .   ? 42.065  26.501  -49.364  1.00 47.69  ? 933  HOH   D O   1 
HETATM 14514 O  O   . HOH   BA 7 .   ? 27.629  30.227  -51.407  1.00 50.38  ? 934  HOH   D O   1 
HETATM 14515 O  O   . HOH   BA 7 .   ? 32.319  30.194  -37.017  1.00 36.97  ? 935  HOH   D O   1 
HETATM 14516 O  O   . HOH   BA 7 .   ? 30.849  36.869  -51.865  1.00 45.06  ? 936  HOH   D O   1 
HETATM 14517 O  O   . HOH   BA 7 .   ? 36.760  37.034  -33.651  1.00 26.33  ? 937  HOH   D O   1 
HETATM 14518 O  O   . HOH   BA 7 .   ? 19.478  33.925  -56.729  1.00 39.12  ? 938  HOH   D O   1 
HETATM 14519 O  O   . HOH   BA 7 .   ? 10.989  26.122  -28.772  1.00 39.54  ? 939  HOH   D O   1 
HETATM 14520 O  O   . HOH   BA 7 .   ? 30.983  38.708  -38.875  1.00 37.74  ? 940  HOH   D O   1 
HETATM 14521 O  O   . HOH   BA 7 .   ? 27.745  15.792  -47.622  1.00 36.25  ? 941  HOH   D O   1 
HETATM 14522 O  O   . HOH   BA 7 .   ? 26.289  31.507  -27.477  1.00 37.18  ? 942  HOH   D O   1 
HETATM 14523 O  O   . HOH   BA 7 .   ? 20.707  20.895  -57.392  1.00 35.31  ? 943  HOH   D O   1 
HETATM 14524 O  O   . HOH   BA 7 .   ? 17.733  3.143   -34.550  1.00 58.41  ? 944  HOH   D O   1 
HETATM 14525 O  O   . HOH   BA 7 .   ? 15.782  24.537  -49.768  1.00 27.89  ? 945  HOH   D O   1 
HETATM 14526 O  O   . HOH   BA 7 .   ? 20.280  17.960  -50.052  1.00 42.57  ? 946  HOH   D O   1 
HETATM 14527 O  O   . HOH   BA 7 .   ? 19.937  20.379  -69.912  1.00 36.54  ? 947  HOH   D O   1 
HETATM 14528 O  O   . HOH   BA 7 .   ? 43.996  52.153  -45.316  1.00 59.88  ? 948  HOH   D O   1 
HETATM 14529 O  O   . HOH   BA 7 .   ? 19.303  36.508  -36.832  1.00 37.15  ? 949  HOH   D O   1 
HETATM 14530 O  O   . HOH   BA 7 .   ? 17.915  27.410  -45.457  1.00 32.99  ? 950  HOH   D O   1 
HETATM 14531 O  O   . HOH   BA 7 .   ? 13.512  12.990  -42.424  1.00 37.68  ? 951  HOH   D O   1 
HETATM 14532 O  O   . HOH   BA 7 .   ? 38.732  25.285  -59.873  1.00 43.60  ? 952  HOH   D O   1 
HETATM 14533 O  O   . HOH   BA 7 .   ? 25.697  15.313  -46.056  1.00 50.40  ? 953  HOH   D O   1 
HETATM 14534 O  O   . HOH   BA 7 .   ? 10.641  23.052  -40.683  1.00 45.62  ? 954  HOH   D O   1 
HETATM 14535 O  O   . HOH   BA 7 .   ? 29.854  30.345  -53.702  1.00 42.60  ? 955  HOH   D O   1 
HETATM 14536 O  O   . HOH   BA 7 .   ? 14.495  19.455  -44.172  1.00 42.24  ? 956  HOH   D O   1 
HETATM 14537 O  O   . HOH   BA 7 .   ? 16.540  30.412  -58.349  1.00 44.56  ? 957  HOH   D O   1 
HETATM 14538 O  O   . HOH   BA 7 .   ? 19.365  23.315  -24.600  1.00 44.16  ? 958  HOH   D O   1 
HETATM 14539 O  O   . HOH   BA 7 .   ? 13.092  33.635  -22.775  1.00 38.44  ? 959  HOH   D O   1 
HETATM 14540 O  O   . HOH   BA 7 .   ? 36.797  38.096  -36.340  1.00 28.31  ? 960  HOH   D O   1 
HETATM 14541 O  O   . HOH   BA 7 .   ? 14.941  34.410  -32.241  1.00 44.23  ? 961  HOH   D O   1 
HETATM 14542 O  O   . HOH   BA 7 .   ? 53.520  38.296  -43.511  1.00 49.53  ? 962  HOH   D O   1 
HETATM 14543 O  O   . HOH   BA 7 .   ? 19.497  44.660  -20.927  1.00 41.93  ? 963  HOH   D O   1 
HETATM 14544 O  O   . HOH   BA 7 .   ? 39.946  52.102  -37.995  1.00 48.61  ? 964  HOH   D O   1 
HETATM 14545 O  O   . HOH   BA 7 .   ? 31.942  46.023  -30.777  1.00 39.00  ? 965  HOH   D O   1 
HETATM 14546 O  O   . HOH   BA 7 .   ? 31.186  16.428  -61.793  1.00 56.44  ? 966  HOH   D O   1 
HETATM 14547 O  O   . HOH   BA 7 .   ? 30.749  64.488  -53.606  1.00 54.72  ? 967  HOH   D O   1 
HETATM 14548 O  O   . HOH   BA 7 .   ? 29.267  43.575  -51.353  1.00 42.01  ? 968  HOH   D O   1 
HETATM 14549 O  O   . HOH   BA 7 .   ? 22.927  19.939  -48.586  1.00 39.36  ? 969  HOH   D O   1 
HETATM 14550 O  O   . HOH   BA 7 .   ? 17.973  39.373  -36.053  1.00 36.41  ? 970  HOH   D O   1 
HETATM 14551 O  O   . HOH   BA 7 .   ? 7.383   38.079  -30.937  1.00 45.72  ? 971  HOH   D O   1 
HETATM 14552 O  O   . HOH   BA 7 .   ? 4.829   19.489  -22.922  1.00 59.00  ? 972  HOH   D O   1 
HETATM 14553 O  O   . HOH   BA 7 .   ? 23.602  50.110  -43.039  1.00 49.17  ? 973  HOH   D O   1 
HETATM 14554 O  O   . HOH   BA 7 .   ? 28.960  34.760  -56.428  1.00 51.60  ? 974  HOH   D O   1 
HETATM 14555 O  O   . HOH   BA 7 .   ? 49.655  39.299  -38.599  1.00 52.24  ? 975  HOH   D O   1 
HETATM 14556 O  O   . HOH   BA 7 .   ? 30.983  22.419  -49.525  1.00 46.28  ? 976  HOH   D O   1 
HETATM 14557 O  O   . HOH   BA 7 .   ? 52.612  43.424  -48.601  1.00 38.16  ? 977  HOH   D O   1 
HETATM 14558 O  O   . HOH   BA 7 .   ? 40.751  35.251  -52.228  1.00 28.39  ? 978  HOH   D O   1 
HETATM 14559 O  O   . HOH   BA 7 .   ? 22.219  51.570  -25.766  1.00 50.16  ? 979  HOH   D O   1 
HETATM 14560 O  O   . HOH   BA 7 .   ? 19.428  16.282  -32.697  1.00 44.32  ? 980  HOH   D O   1 
HETATM 14561 O  O   . HOH   BA 7 .   ? 37.447  22.668  -49.179  1.00 52.72  ? 981  HOH   D O   1 
HETATM 14562 O  O   . HOH   BA 7 .   ? 27.641  33.797  -59.764  1.00 38.13  ? 982  HOH   D O   1 
HETATM 14563 O  O   . HOH   BA 7 .   ? 16.090  45.085  -26.023  1.00 37.74  ? 983  HOH   D O   1 
HETATM 14564 O  O   . HOH   BA 7 .   ? 17.419  39.354  -43.514  1.00 45.29  ? 984  HOH   D O   1 
HETATM 14565 O  O   . HOH   BA 7 .   ? 31.784  39.485  -45.700  1.00 40.04  ? 985  HOH   D O   1 
HETATM 14566 O  O   . HOH   BA 7 .   ? 11.441  42.156  -35.833  1.00 39.96  ? 986  HOH   D O   1 
HETATM 14567 O  O   . HOH   BA 7 .   ? 20.368  26.665  -59.701  1.00 37.03  ? 987  HOH   D O   1 
HETATM 14568 O  O   . HOH   BA 7 .   ? 30.830  44.681  -35.388  1.00 37.43  ? 988  HOH   D O   1 
HETATM 14569 O  O   . HOH   BA 7 .   ? 25.887  15.781  -62.190  1.00 42.31  ? 989  HOH   D O   1 
HETATM 14570 O  O   . HOH   BA 7 .   ? 11.627  36.494  -31.193  1.00 38.58  ? 990  HOH   D O   1 
HETATM 14571 O  O   . HOH   BA 7 .   ? 10.567  42.914  -21.637  1.00 55.29  ? 991  HOH   D O   1 
HETATM 14572 O  O   . HOH   BA 7 .   ? 38.328  36.279  -62.780  1.00 43.93  ? 992  HOH   D O   1 
HETATM 14573 O  O   . HOH   BA 7 .   ? 23.320  25.127  -25.791  1.00 49.71  ? 993  HOH   D O   1 
HETATM 14574 O  O   . HOH   BA 7 .   ? 43.507  27.074  -31.682  1.00 51.23  ? 994  HOH   D O   1 
HETATM 14575 O  O   . HOH   BA 7 .   ? 33.347  23.696  -37.496  1.00 39.38  ? 995  HOH   D O   1 
HETATM 14576 O  O   . HOH   BA 7 .   ? 39.409  32.466  -52.791  1.00 37.59  ? 996  HOH   D O   1 
HETATM 14577 O  O   . HOH   BA 7 .   ? 17.301  29.407  -17.567  1.00 50.91  ? 997  HOH   D O   1 
HETATM 14578 O  O   . HOH   BA 7 .   ? 13.657  34.603  -48.010  1.00 51.67  ? 998  HOH   D O   1 
HETATM 14579 O  O   . HOH   BA 7 .   ? 18.466  29.696  -46.690  1.00 43.09  ? 999  HOH   D O   1 
HETATM 14580 O  O   . HOH   BA 7 .   ? 5.374   37.296  -25.681  1.00 62.82  ? 1000 HOH   D O   1 
HETATM 14581 O  O   . HOH   BA 7 .   ? 5.295   30.468  -39.474  1.00 46.07  ? 1001 HOH   D O   1 
HETATM 14582 O  O   . HOH   BA 7 .   ? 11.169  14.746  -29.632  1.00 46.45  ? 1002 HOH   D O   1 
HETATM 14583 O  O   . HOH   BA 7 .   ? 36.434  22.959  -63.310  1.00 52.26  ? 1003 HOH   D O   1 
HETATM 14584 O  O   . HOH   BA 7 .   ? 11.551  5.245   -39.171  1.00 53.78  ? 1004 HOH   D O   1 
HETATM 14585 O  O   . HOH   BA 7 .   ? 9.864   33.225  -27.003  1.00 46.73  ? 1005 HOH   D O   1 
HETATM 14586 O  O   . HOH   BA 7 .   ? 33.169  34.714  -63.132  1.00 66.47  ? 1006 HOH   D O   1 
HETATM 14587 O  O   . HOH   BA 7 .   ? 20.502  27.794  -20.847  1.00 66.24  ? 1007 HOH   D O   1 
HETATM 14588 O  O   . HOH   BA 7 .   ? 40.144  25.482  -45.472  1.00 56.10  ? 1008 HOH   D O   1 
HETATM 14589 O  O   . HOH   BA 7 .   ? 21.077  35.204  -38.770  1.00 46.50  ? 1009 HOH   D O   1 
HETATM 14590 O  O   . HOH   BA 7 .   ? 42.940  24.551  -32.258  1.00 54.55  ? 1010 HOH   D O   1 
HETATM 14591 O  O   . HOH   BA 7 .   ? 36.360  53.213  -48.245  1.00 53.02  ? 1011 HOH   D O   1 
HETATM 14592 O  O   . HOH   BA 7 .   ? 27.086  44.199  -47.427  1.00 48.23  ? 1012 HOH   D O   1 
HETATM 14593 O  O   . HOH   BA 7 .   ? 33.064  48.526  -30.799  1.00 50.39  ? 1013 HOH   D O   1 
HETATM 14594 O  O   . HOH   BA 7 .   ? 19.955  30.084  -49.422  1.00 38.23  ? 1014 HOH   D O   1 
HETATM 14595 O  O   . HOH   BA 7 .   ? 47.107  38.847  -61.520  1.00 47.62  ? 1015 HOH   D O   1 
HETATM 14596 O  O   . HOH   BA 7 .   ? 24.922  46.616  -41.630  1.00 56.90  ? 1016 HOH   D O   1 
HETATM 14597 O  O   . HOH   BA 7 .   ? 13.561  39.040  -17.032  1.00 62.97  ? 1017 HOH   D O   1 
HETATM 14598 O  O   . HOH   BA 7 .   ? 40.510  33.618  -30.311  1.00 59.69  ? 1018 HOH   D O   1 
HETATM 14599 O  O   . HOH   BA 7 .   ? 38.547  49.117  -74.701  1.00 57.13  ? 1019 HOH   D O   1 
HETATM 14600 O  O   . HOH   BA 7 .   ? 14.661  10.653  -43.886  1.00 65.63  ? 1020 HOH   D O   1 
HETATM 14601 O  O   . HOH   BA 7 .   ? 25.404  21.096  -31.191  1.00 38.77  ? 1021 HOH   D O   1 
HETATM 14602 O  O   . HOH   BA 7 .   ? 41.013  24.264  -48.264  1.00 56.03  ? 1022 HOH   D O   1 
HETATM 14603 O  O   . HOH   BA 7 .   ? 35.185  35.132  -21.589  1.00 54.74  ? 1023 HOH   D O   1 
HETATM 14604 O  O   . HOH   BA 7 .   ? 12.011  25.974  -24.185  1.00 53.35  ? 1024 HOH   D O   1 
HETATM 14605 O  O   . HOH   BA 7 .   ? 43.589  27.329  -38.095  1.00 50.63  ? 1025 HOH   D O   1 
HETATM 14606 O  O   . HOH   BA 7 .   ? 34.863  24.886  -46.352  1.00 40.58  ? 1026 HOH   D O   1 
HETATM 14607 O  O   . HOH   BA 7 .   ? 40.392  22.595  -57.488  1.00 64.39  ? 1027 HOH   D O   1 
HETATM 14608 O  O   . HOH   BA 7 .   ? 14.481  19.201  -24.357  1.00 39.14  ? 1028 HOH   D O   1 
HETATM 14609 O  O   . HOH   BA 7 .   ? 24.793  32.413  -21.350  1.00 45.70  ? 1029 HOH   D O   1 
HETATM 14610 O  O   . HOH   BA 7 .   ? 21.507  10.355  -58.269  1.00 52.56  ? 1030 HOH   D O   1 
HETATM 14611 O  O   . HOH   BA 7 .   ? 31.608  22.949  -35.238  1.00 37.48  ? 1031 HOH   D O   1 
HETATM 14612 O  O   . HOH   BA 7 .   ? 18.414  27.984  -22.775  1.00 40.37  ? 1032 HOH   D O   1 
HETATM 14613 O  O   . HOH   BA 7 .   ? 0.171   23.579  -65.453  1.00 47.13  ? 1033 HOH   D O   1 
HETATM 14614 O  O   . HOH   BA 7 .   ? 11.751  22.108  -24.327  1.00 52.70  ? 1034 HOH   D O   1 
HETATM 14615 O  O   . HOH   BA 7 .   ? 38.351  53.414  -57.900  1.00 62.43  ? 1035 HOH   D O   1 
HETATM 14616 O  O   . HOH   BA 7 .   ? 39.741  46.562  -66.766  1.00 35.87  ? 1036 HOH   D O   1 
HETATM 14617 O  O   . HOH   BA 7 .   ? 37.828  35.051  -29.802  1.00 44.01  ? 1037 HOH   D O   1 
HETATM 14618 O  O   . HOH   BA 7 .   ? 54.783  46.390  -58.557  1.00 52.45  ? 1038 HOH   D O   1 
HETATM 14619 O  O   . HOH   BA 7 .   ? 26.304  18.588  -32.246  1.00 55.59  ? 1039 HOH   D O   1 
HETATM 14620 O  O   . HOH   BA 7 .   ? 34.995  65.867  -46.037  1.00 52.00  ? 1040 HOH   D O   1 
HETATM 14621 O  O   . HOH   BA 7 .   ? 30.111  54.320  -27.051  1.00 45.41  ? 1041 HOH   D O   1 
HETATM 14622 O  O   . HOH   BA 7 .   ? 13.744  4.772   -28.315  1.00 47.76  ? 1042 HOH   D O   1 
HETATM 14623 O  O   . HOH   BA 7 .   ? 17.348  41.651  -45.630  1.00 59.43  ? 1043 HOH   D O   1 
HETATM 14624 O  O   . HOH   BA 7 .   ? 54.773  43.057  -46.610  1.00 49.78  ? 1044 HOH   D O   1 
HETATM 14625 O  O   . HOH   BA 7 .   ? 5.988   21.734  -44.053  1.00 44.55  ? 1045 HOH   D O   1 
HETATM 14626 O  O   . HOH   BA 7 .   ? 30.789  38.381  -48.943  1.00 66.31  ? 1046 HOH   D O   1 
HETATM 14627 O  O   . HOH   BA 7 .   ? 13.812  44.120  -50.245  1.00 54.06  ? 1047 HOH   D O   1 
HETATM 14628 O  O   . HOH   BA 7 .   ? 38.810  28.474  -27.190  1.00 58.52  ? 1048 HOH   D O   1 
HETATM 14629 O  O   . HOH   BA 7 .   ? 23.986  27.327  -24.261  1.00 43.86  ? 1049 HOH   D O   1 
HETATM 14630 O  O   . HOH   BA 7 .   ? 16.028  17.117  -25.419  1.00 61.70  ? 1050 HOH   D O   1 
HETATM 14631 O  O   . HOH   BA 7 .   ? 30.478  33.103  -54.021  1.00 37.20  ? 1051 HOH   D O   1 
HETATM 14632 O  O   . HOH   BA 7 .   ? 37.196  18.571  -62.046  1.00 57.91  ? 1052 HOH   D O   1 
HETATM 14633 O  O   . HOH   BA 7 .   ? 11.358  35.966  -22.889  1.00 52.03  ? 1053 HOH   D O   1 
HETATM 14634 O  O   . HOH   BA 7 .   ? 10.892  44.780  -34.495  1.00 61.60  ? 1054 HOH   D O   1 
HETATM 14635 O  O   . HOH   BA 7 .   ? 15.637  32.720  -56.584  1.00 54.43  ? 1055 HOH   D O   1 
HETATM 14636 O  O   . HOH   BA 7 .   ? 41.154  55.325  -56.014  1.00 60.08  ? 1056 HOH   D O   1 
HETATM 14637 O  O   . HOH   BA 7 .   ? 10.381  31.129  -23.411  1.00 56.61  ? 1057 HOH   D O   1 
HETATM 14638 O  O   . HOH   BA 7 .   ? 9.268   34.939  -25.019  1.00 43.75  ? 1058 HOH   D O   1 
HETATM 14639 O  O   . HOH   BA 7 .   ? 29.126  34.398  -62.170  1.00 53.74  ? 1059 HOH   D O   1 
HETATM 14640 O  O   . HOH   BA 7 .   ? 26.169  40.952  -46.953  1.00 51.57  ? 1060 HOH   D O   1 
HETATM 14641 O  O   . HOH   BA 7 .   ? 26.236  30.030  -25.019  1.00 58.98  ? 1061 HOH   D O   1 
HETATM 14642 O  O   . HOH   BA 7 .   ? 44.126  42.386  -25.998  1.00 42.44  ? 1062 HOH   D O   1 
HETATM 14643 O  O   . HOH   BA 7 .   ? 38.301  23.141  -40.585  1.00 55.36  ? 1063 HOH   D O   1 
HETATM 14644 O  O   . HOH   BA 7 .   ? 4.905   37.103  -59.056  1.00 60.88  ? 1064 HOH   D O   1 
HETATM 14645 O  O   . HOH   BA 7 .   ? 35.161  18.555  -59.432  1.00 62.70  ? 1065 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   . ARG A 3   ? 1.2084 1.3206 1.1766 0.1770  0.0325  -0.0502 304 ARG A N   
2     C CA  . ARG A 3   ? 1.2681 1.3457 1.2259 0.1827  0.0253  -0.0524 304 ARG A CA  
3     C C   . ARG A 3   ? 1.2755 1.3202 1.2265 0.1701  0.0230  -0.0495 304 ARG A C   
4     O O   . ARG A 3   ? 1.3560 1.3726 1.3014 0.1676  0.0186  -0.0475 304 ARG A O   
5     C CB  . ARG A 3   ? 1.3353 1.4059 1.2805 0.2033  0.0207  -0.0630 304 ARG A CB  
6     C CG  . ARG A 3   ? 1.4547 1.4874 1.3864 0.2110  0.0130  -0.0653 304 ARG A CG  
7     C CD  . ARG A 3   ? 1.6167 1.6475 1.5369 0.2340  0.0087  -0.0756 304 ARG A CD  
8     N NE  . ARG A 3   ? 1.7628 1.7480 1.6634 0.2403  0.0015  -0.0801 304 ARG A NE  
9     C CZ  . ARG A 3   ? 1.8388 1.8051 1.7254 0.2462  -0.0011 -0.0886 304 ARG A CZ  
10    N NH1 . ARG A 3   ? 1.7979 1.7885 1.6878 0.2478  0.0029  -0.0934 304 ARG A NH1 
11    N NH2 . ARG A 3   ? 1.8990 1.8215 1.7673 0.2502  -0.0077 -0.0923 304 ARG A NH2 
12    N N   . PHE A 4   ? 1.1435 1.1931 1.0947 0.1620  0.0262  -0.0493 305 PHE A N   
13    C CA  . PHE A 4   ? 1.0273 1.0525 0.9741 0.1494  0.0246  -0.0468 305 PHE A CA  
14    C C   . PHE A 4   ? 0.8585 0.9033 0.8128 0.1383  0.0303  -0.0421 305 PHE A C   
15    O O   . PHE A 4   ? 0.8010 0.8716 0.7581 0.1428  0.0346  -0.0437 305 PHE A O   
16    C CB  . PHE A 4   ? 1.1685 1.1669 1.0996 0.1560  0.0191  -0.0558 305 PHE A CB  
17    C CG  . PHE A 4   ? 1.3506 1.3214 1.2707 0.1659  0.0128  -0.0599 305 PHE A CG  
18    C CD1 . PHE A 4   ? 1.3558 1.2965 1.2715 0.1572  0.0093  -0.0558 305 PHE A CD1 
19    C CD2 . PHE A 4   ? 1.4460 1.4202 1.3588 0.1847  0.0105  -0.0678 305 PHE A CD2 
20    C CE1 . PHE A 4   ? 1.3430 1.2554 1.2463 0.1663  0.0036  -0.0588 305 PHE A CE1 
21    C CE2 . PHE A 4   ? 1.4386 1.3843 1.3389 0.1952  0.0043  -0.0713 305 PHE A CE2 
22    C CZ  . PHE A 4   ? 1.3750 1.2887 1.2701 0.1856  0.0009  -0.0664 305 PHE A CZ  
23    N N   . LEU A 5   ? 0.7455 0.7783 0.7023 0.1242  0.0306  -0.0360 306 LEU A N   
24    C CA  . LEU A 5   ? 0.6295 0.6752 0.5906 0.1144  0.0350  -0.0314 306 LEU A CA  
25    C C   . LEU A 5   ? 0.6692 0.6928 0.6247 0.1061  0.0316  -0.0320 306 LEU A C   
26    O O   . LEU A 5   ? 0.7650 0.7668 0.7188 0.1015  0.0280  -0.0308 306 LEU A O   
27    C CB  . LEU A 5   ? 0.5610 0.6220 0.5341 0.1047  0.0399  -0.0217 306 LEU A CB  
28    C CG  . LEU A 5   ? 0.5864 0.6767 0.5667 0.1092  0.0449  -0.0204 306 LEU A CG  
29    C CD1 . LEU A 5   ? 0.5318 0.6330 0.5229 0.0980  0.0492  -0.0112 306 LEU A CD1 
30    C CD2 . LEU A 5   ? 0.5953 0.7036 0.5720 0.1131  0.0486  -0.0234 306 LEU A CD2 
31    N N   . LYS A 6   ? 0.7139 0.7443 0.6663 0.1041  0.0327  -0.0339 307 LYS A N   
32    C CA  . LYS A 6   ? 0.6502 0.6640 0.5978 0.0964  0.0294  -0.0355 307 LYS A CA  
33    C C   . LYS A 6   ? 0.5492 0.5741 0.5033 0.0860  0.0330  -0.0276 307 LYS A C   
34    O O   . LYS A 6   ? 0.5724 0.6180 0.5301 0.0867  0.0381  -0.0234 307 LYS A O   
35    C CB  . LYS A 6   ? 0.6872 0.6972 0.6240 0.1032  0.0262  -0.0455 307 LYS A CB  
36    C CG  . LYS A 6   ? 0.7838 0.7710 0.7105 0.1112  0.0205  -0.0542 307 LYS A CG  
37    C CD  . LYS A 6   ? 0.9458 0.9266 0.8610 0.1159  0.0169  -0.0646 307 LYS A CD  
38    C CE  . LYS A 6   ? 1.0527 1.0168 0.9566 0.1288  0.0125  -0.0741 307 LYS A CE  
39    N NZ  . LYS A 6   ? 1.0950 1.0312 0.9961 0.1262  0.0087  -0.0726 307 LYS A NZ  
40    N N   . VAL A 7   ? 0.5311 0.5418 0.4860 0.0766  0.0306  -0.0254 308 VAL A N   
41    C CA  . VAL A 7   ? 0.5364 0.5548 0.4955 0.0681  0.0327  -0.0195 308 VAL A CA  
42    C C   . VAL A 7   ? 0.5709 0.5797 0.5244 0.0643  0.0282  -0.0252 308 VAL A C   
43    O O   . VAL A 7   ? 0.6545 0.6451 0.6031 0.0636  0.0236  -0.0312 308 VAL A O   
44    C CB  . VAL A 7   ? 0.4736 0.4884 0.4409 0.0597  0.0344  -0.0108 308 VAL A CB  
45    C CG1 . VAL A 7   ? 0.4732 0.4997 0.4465 0.0620  0.0389  -0.0053 308 VAL A CG1 
46    C CG2 . VAL A 7   ? 0.5098 0.5031 0.4761 0.0553  0.0302  -0.0124 308 VAL A CG2 
47    N N   . LYS A 8   ? 0.5756 0.5965 0.5293 0.0616  0.0294  -0.0233 309 LYS A N   
48    C CA  . LYS A 8   ? 0.5867 0.6047 0.5355 0.0587  0.0252  -0.0295 309 LYS A CA  
49    C C   . LYS A 8   ? 0.5991 0.6233 0.5531 0.0509  0.0258  -0.0236 309 LYS A C   
50    O O   . LYS A 8   ? 0.5675 0.6034 0.5250 0.0512  0.0301  -0.0157 309 LYS A O   
51    C CB  . LYS A 8   ? 0.5080 0.5380 0.4492 0.0669  0.0251  -0.0355 309 LYS A CB  
52    C CG  . LYS A 8   ? 0.6422 0.6741 0.5784 0.0643  0.0208  -0.0418 309 LYS A CG  
53    C CD  . LYS A 8   ? 0.6179 0.6606 0.5450 0.0735  0.0204  -0.0486 309 LYS A CD  
54    C CE  . LYS A 8   ? 0.7039 0.7479 0.6256 0.0708  0.0151  -0.0565 309 LYS A CE  
55    N NZ  . LYS A 8   ? 0.7089 0.7686 0.6220 0.0795  0.0155  -0.0610 309 LYS A NZ  
56    N N   . ASN A 9   ? 0.6339 0.6501 0.5879 0.0438  0.0216  -0.0275 310 ASN A N   
57    C CA  . ASN A 9   ? 0.6023 0.6279 0.5603 0.0379  0.0212  -0.0242 310 ASN A CA  
58    C C   . ASN A 9   ? 0.5976 0.6355 0.5497 0.0413  0.0187  -0.0302 310 ASN A C   
59    O O   . ASN A 9   ? 0.6111 0.6428 0.5579 0.0406  0.0142  -0.0397 310 ASN A O   
60    C CB  . ASN A 9   ? 0.5797 0.5944 0.5417 0.0277  0.0183  -0.0252 310 ASN A CB  
61    C CG  . ASN A 9   ? 0.6036 0.6309 0.5715 0.0227  0.0188  -0.0208 310 ASN A CG  
62    O OD1 . ASN A 9   ? 0.5598 0.6002 0.5260 0.0235  0.0167  -0.0241 310 ASN A OD1 
63    N ND2 . ASN A 9   ? 0.6541 0.6782 0.6284 0.0183  0.0212  -0.0138 310 ASN A ND2 
64    N N   . TRP A 10  ? 0.6248 0.6786 0.5766 0.0452  0.0215  -0.0248 311 TRP A N   
65    C CA  . TRP A 10  ? 0.5599 0.6271 0.5048 0.0504  0.0196  -0.0294 311 TRP A CA  
66    C C   . TRP A 10  ? 0.5614 0.6354 0.5073 0.0453  0.0148  -0.0338 311 TRP A C   
67    O O   . TRP A 10  ? 0.5552 0.6398 0.4951 0.0491  0.0118  -0.0397 311 TRP A O   
68    C CB  . TRP A 10  ? 0.5115 0.5915 0.4535 0.0570  0.0248  -0.0210 311 TRP A CB  
69    C CG  . TRP A 10  ? 0.5461 0.6252 0.4852 0.0627  0.0289  -0.0200 311 TRP A CG  
70    C CD1 . TRP A 10  ? 0.5185 0.5925 0.4627 0.0619  0.0333  -0.0137 311 TRP A CD1 
71    C CD2 . TRP A 10  ? 0.5339 0.6193 0.4647 0.0704  0.0287  -0.0264 311 TRP A CD2 
72    N NE1 . TRP A 10  ? 0.4976 0.5762 0.4379 0.0684  0.0360  -0.0156 311 TRP A NE1 
73    C CE2 . TRP A 10  ? 0.4854 0.5709 0.4174 0.0740  0.0335  -0.0233 311 TRP A CE2 
74    C CE3 . TRP A 10  ? 0.6891 0.7816 0.6117 0.0747  0.0249  -0.0348 311 TRP A CE3 
75    C CZ2 . TRP A 10  ? 0.5520 0.6451 0.4772 0.0823  0.0349  -0.0282 311 TRP A CZ2 
76    C CZ3 . TRP A 10  ? 0.6760 0.7743 0.5909 0.0831  0.0263  -0.0397 311 TRP A CZ3 
77    C CH2 . TRP A 10  ? 0.6009 0.6998 0.5172 0.0870  0.0314  -0.0363 311 TRP A CH2 
78    N N   . GLU A 11  ? 0.5164 0.5865 0.4700 0.0371  0.0139  -0.0314 312 GLU A N   
79    C CA  . GLU A 11  ? 0.6174 0.6953 0.5742 0.0304  0.0093  -0.0363 312 GLU A CA  
80    C C   . GLU A 11  ? 0.6844 0.7496 0.6401 0.0223  0.0045  -0.0464 312 GLU A C   
81    O O   . GLU A 11  ? 0.7080 0.7812 0.6618 0.0191  -0.0004 -0.0547 312 GLU A O   
82    C CB  . GLU A 11  ? 0.6561 0.7372 0.6216 0.0255  0.0113  -0.0287 312 GLU A CB  
83    C CG  . GLU A 11  ? 0.6836 0.7783 0.6537 0.0195  0.0072  -0.0327 312 GLU A CG  
84    C CD  . GLU A 11  ? 0.7112 0.8076 0.6900 0.0143  0.0093  -0.0263 312 GLU A CD  
85    O OE1 . GLU A 11  ? 0.6924 0.7774 0.6734 0.0146  0.0135  -0.0190 312 GLU A OE1 
86    O OE2 . GLU A 11  ? 0.7692 0.8801 0.7529 0.0098  0.0065  -0.0292 312 GLU A OE2 
87    N N   . THR A 12  ? 0.6028 0.6477 0.5587 0.0191  0.0056  -0.0461 313 THR A N   
88    C CA  . THR A 12  ? 0.5535 0.5809 0.5070 0.0106  0.0014  -0.0542 313 THR A CA  
89    C C   . THR A 12  ? 0.6845 0.6973 0.6278 0.0165  -0.0005 -0.0617 313 THR A C   
90    O O   . THR A 12  ? 0.8031 0.8005 0.7414 0.0102  -0.0049 -0.0701 313 THR A O   
91    C CB  . THR A 12  ? 0.5938 0.6050 0.5522 0.0031  0.0034  -0.0486 313 THR A CB  
92    O OG1 . THR A 12  ? 0.6601 0.6599 0.6161 0.0107  0.0068  -0.0442 313 THR A OG1 
93    C CG2 . THR A 12  ? 0.5962 0.6209 0.5643 -0.0013 0.0060  -0.0407 313 THR A CG2 
94    N N   . GLU A 13  ? 0.6928 0.7089 0.6326 0.0280  0.0028  -0.0590 314 GLU A N   
95    C CA  . GLU A 13  ? 0.6782 0.6829 0.6087 0.0365  0.0019  -0.0652 314 GLU A CA  
96    C C   . GLU A 13  ? 0.7219 0.7039 0.6517 0.0360  0.0027  -0.0636 314 GLU A C   
97    O O   . GLU A 13  ? 0.7037 0.6759 0.6257 0.0446  0.0020  -0.0686 314 GLU A O   
98    C CB  . GLU A 13  ? 0.8364 0.8364 0.7576 0.0359  -0.0041 -0.0782 314 GLU A CB  
99    C CG  . GLU A 13  ? 0.8627 0.8851 0.7832 0.0366  -0.0061 -0.0816 314 GLU A CG  
100   C CD  . GLU A 13  ? 1.0173 1.0529 0.9304 0.0497  -0.0045 -0.0834 314 GLU A CD  
101   O OE1 . GLU A 13  ? 1.0898 1.1306 1.0044 0.0573  0.0012  -0.0755 314 GLU A OE1 
102   O OE2 . GLU A 13  ? 1.0827 1.1240 0.9882 0.0521  -0.0087 -0.0931 314 GLU A OE2 
103   N N   . VAL A 14  ? 0.6479 0.6218 0.5846 0.0276  0.0039  -0.0570 315 VAL A N   
104   C CA  . VAL A 14  ? 0.7040 0.6567 0.6391 0.0278  0.0045  -0.0548 315 VAL A CA  
105   C C   . VAL A 14  ? 0.7445 0.7031 0.6803 0.0395  0.0086  -0.0501 315 VAL A C   
106   O O   . VAL A 14  ? 0.7444 0.7220 0.6865 0.0424  0.0130  -0.0432 315 VAL A O   
107   C CB  . VAL A 14  ? 0.7429 0.6903 0.6856 0.0168  0.0058  -0.0474 315 VAL A CB  
108   C CG1 . VAL A 14  ? 0.6649 0.5922 0.6056 0.0183  0.0067  -0.0437 315 VAL A CG1 
109   C CG2 . VAL A 14  ? 0.7617 0.7037 0.7038 0.0039  0.0019  -0.0525 315 VAL A CG2 
110   N N   . VAL A 15  ? 0.7720 0.7141 0.7009 0.0463  0.0073  -0.0539 316 VAL A N   
111   C CA  . VAL A 15  ? 0.7453 0.6944 0.6752 0.0575  0.0109  -0.0506 316 VAL A CA  
112   C C   . VAL A 15  ? 0.7004 0.6308 0.6299 0.0579  0.0105  -0.0475 316 VAL A C   
113   O O   . VAL A 15  ? 0.7304 0.6365 0.6509 0.0573  0.0062  -0.0529 316 VAL A O   
114   C CB  . VAL A 15  ? 0.6739 0.6269 0.5950 0.0696  0.0097  -0.0592 316 VAL A CB  
115   C CG1 . VAL A 15  ? 0.6182 0.5842 0.5424 0.0803  0.0141  -0.0553 316 VAL A CG1 
116   C CG2 . VAL A 15  ? 0.6419 0.6122 0.5616 0.0692  0.0095  -0.0628 316 VAL A CG2 
117   N N   . LEU A 16  ? 0.7500 0.6908 0.6879 0.0593  0.0147  -0.0390 317 LEU A N   
118   C CA  . LEU A 16  ? 0.6623 0.5897 0.6007 0.0606  0.0147  -0.0350 317 LEU A CA  
119   C C   . LEU A 16  ? 0.6384 0.5768 0.5776 0.0732  0.0169  -0.0350 317 LEU A C   
120   O O   . LEU A 16  ? 0.6410 0.6016 0.5839 0.0779  0.0203  -0.0346 317 LEU A O   
121   C CB  . LEU A 16  ? 0.5486 0.4799 0.4965 0.0509  0.0174  -0.0256 317 LEU A CB  
122   C CG  . LEU A 16  ? 0.5795 0.5105 0.5296 0.0390  0.0165  -0.0250 317 LEU A CG  
123   C CD1 . LEU A 16  ? 0.4566 0.3968 0.4168 0.0317  0.0200  -0.0157 317 LEU A CD1 
124   C CD2 . LEU A 16  ? 0.6436 0.5498 0.5852 0.0329  0.0118  -0.0303 317 LEU A CD2 
125   N N   . THR A 17  ? 0.5405 0.4641 0.4758 0.0787  0.0149  -0.0352 318 THR A N   
126   C CA  . THR A 17  ? 0.6002 0.5341 0.5355 0.0919  0.0161  -0.0366 318 THR A CA  
127   C C   . THR A 17  ? 0.6779 0.6162 0.6211 0.0907  0.0181  -0.0288 318 THR A C   
128   O O   . THR A 17  ? 0.7279 0.6458 0.6672 0.0888  0.0153  -0.0269 318 THR A O   
129   C CB  . THR A 17  ? 0.6437 0.5571 0.5655 0.1032  0.0110  -0.0454 318 THR A CB  
130   O OG1 . THR A 17  ? 0.6978 0.6060 0.6115 0.1036  0.0087  -0.0536 318 THR A OG1 
131   C CG2 . THR A 17  ? 0.5667 0.4952 0.4893 0.1183  0.0123  -0.0475 318 THR A CG2 
132   N N   . ASP A 18  ? 0.6447 0.6092 0.5982 0.0917  0.0229  -0.0243 319 ASP A N   
133   C CA  . ASP A 18  ? 0.6233 0.5951 0.5852 0.0894  0.0250  -0.0173 319 ASP A CA  
134   C C   . ASP A 18  ? 0.6490 0.6276 0.6099 0.1026  0.0240  -0.0204 319 ASP A C   
135   O O   . ASP A 18  ? 0.5985 0.5995 0.5627 0.1098  0.0267  -0.0230 319 ASP A O   
136   C CB  . ASP A 18  ? 0.5863 0.5809 0.5590 0.0818  0.0305  -0.0109 319 ASP A CB  
137   C CG  . ASP A 18  ? 0.5773 0.5765 0.5582 0.0769  0.0323  -0.0039 319 ASP A CG  
138   O OD1 . ASP A 18  ? 0.6343 0.6422 0.6178 0.0839  0.0322  -0.0044 319 ASP A OD1 
139   O OD2 . ASP A 18  ? 0.5903 0.5851 0.5747 0.0666  0.0334  0.0016  319 ASP A OD2 
140   N N   . THR A 19  ? 0.6159 0.5762 0.5720 0.1061  0.0202  -0.0200 320 THR A N   
141   C CA  . THR A 19  ? 0.6354 0.6041 0.5919 0.1185  0.0190  -0.0216 320 THR A CA  
142   C C   . THR A 19  ? 0.6621 0.6419 0.6286 0.1135  0.0208  -0.0144 320 THR A C   
143   O O   . THR A 19  ? 0.7254 0.7234 0.6967 0.1218  0.0212  -0.0152 320 THR A O   
144   C CB  . THR A 19  ? 0.6821 0.6220 0.6240 0.1286  0.0128  -0.0265 320 THR A CB  
145   O OG1 . THR A 19  ? 0.7282 0.6438 0.6663 0.1196  0.0107  -0.0211 320 THR A OG1 
146   C CG2 . THR A 19  ? 0.7028 0.6279 0.6332 0.1328  0.0104  -0.0344 320 THR A CG2 
147   N N   . LEU A 20  ? 0.5305 0.5013 0.5002 0.1002  0.0218  -0.0080 321 LEU A N   
148   C CA  . LEU A 20  ? 0.5822 0.5593 0.5593 0.0952  0.0228  -0.0017 321 LEU A CA  
149   C C   . LEU A 20  ? 0.5858 0.5944 0.5757 0.0933  0.0275  0.0004  321 LEU A C   
150   O O   . LEU A 20  ? 0.5140 0.5330 0.5098 0.0938  0.0275  0.0030  321 LEU A O   
151   C CB  . LEU A 20  ? 0.5228 0.4846 0.5000 0.0817  0.0233  0.0040  321 LEU A CB  
152   C CG  . LEU A 20  ? 0.5717 0.5398 0.5567 0.0740  0.0250  0.0107  321 LEU A CG  
153   C CD1 . LEU A 20  ? 0.5383 0.5000 0.5197 0.0813  0.0214  0.0113  321 LEU A CD1 
154   C CD2 . LEU A 20  ? 0.5483 0.5033 0.5327 0.0615  0.0260  0.0152  321 LEU A CD2 
155   N N   . HIS A 21  ? 0.5599 0.5839 0.5535 0.0909  0.0314  -0.0006 322 HIS A N   
156   C CA  . HIS A 21  ? 0.4525 0.5047 0.4569 0.0872  0.0365  0.0020  322 HIS A CA  
157   C C   . HIS A 21  ? 0.5088 0.5815 0.5176 0.0973  0.0361  -0.0013 322 HIS A C   
158   O O   . HIS A 21  ? 0.5613 0.6574 0.5799 0.0927  0.0399  0.0013  322 HIS A O   
159   C CB  . HIS A 21  ? 0.5008 0.5642 0.5052 0.0848  0.0406  0.0012  322 HIS A CB  
160   C CG  . HIS A 21  ? 0.5141 0.5842 0.5130 0.0971  0.0397  -0.0063 322 HIS A CG  
161   N ND1 . HIS A 21  ? 0.5761 0.6262 0.5642 0.1027  0.0358  -0.0116 322 HIS A ND1 
162   C CD2 . HIS A 21  ? 0.5401 0.6353 0.5426 0.1050  0.0422  -0.0097 322 HIS A CD2 
163   C CE1 . HIS A 21  ? 0.5891 0.6502 0.5736 0.1144  0.0357  -0.0184 322 HIS A CE1 
164   N NE2 . HIS A 21  ? 0.5877 0.6774 0.5811 0.1163  0.0397  -0.0172 322 HIS A NE2 
165   N N   . LEU A 22  ? 0.5812 0.6460 0.5824 0.1109  0.0316  -0.0072 323 LEU A N   
166   C CA  . LEU A 22  ? 0.6349 0.7207 0.6401 0.1224  0.0306  -0.0108 323 LEU A CA  
167   C C   . LEU A 22  ? 0.6843 0.7731 0.6952 0.1197  0.0289  -0.0069 323 LEU A C   
168   O O   . LEU A 22  ? 0.6756 0.7901 0.6943 0.1248  0.0294  -0.0085 323 LEU A O   
169   C CB  . LEU A 22  ? 0.6416 0.7145 0.6351 0.1394  0.0256  -0.0183 323 LEU A CB  
170   C CG  . LEU A 22  ? 0.7161 0.7847 0.7024 0.1431  0.0266  -0.0234 323 LEU A CG  
171   C CD1 . LEU A 22  ? 0.6663 0.7146 0.6383 0.1593  0.0208  -0.0311 323 LEU A CD1 
172   C CD2 . LEU A 22  ? 0.7161 0.8200 0.7114 0.1433  0.0325  -0.0249 323 LEU A CD2 
173   N N   . LYS A 23  ? 0.6596 0.7248 0.6671 0.1114  0.0271  -0.0019 324 LYS A N   
174   C CA  . LYS A 23  ? 0.6748 0.7408 0.6862 0.1084  0.0253  0.0018  324 LYS A CA  
175   C C   . LYS A 23  ? 0.7144 0.7990 0.7380 0.0946  0.0299  0.0066  324 LYS A C   
176   O O   . LYS A 23  ? 0.7559 0.8479 0.7844 0.0925  0.0287  0.0085  324 LYS A O   
177   C CB  . LYS A 23  ? 0.6443 0.6770 0.6455 0.1056  0.0216  0.0051  324 LYS A CB  
178   C CG  . LYS A 23  ? 0.7610 0.7714 0.7483 0.1194  0.0159  0.0012  324 LYS A CG  
179   C CD  . LYS A 23  ? 0.8788 0.8986 0.8657 0.1318  0.0120  -0.0004 324 LYS A CD  
180   C CE  . LYS A 23  ? 1.0055 1.0288 0.9858 0.1499  0.0090  -0.0077 324 LYS A CE  
181   N NZ  . LYS A 23  ? 1.0808 1.0700 1.0450 0.1547  0.0059  -0.0102 324 LYS A NZ  
182   N N   . SER A 24  ? 0.7548 0.8457 0.7820 0.0854  0.0350  0.0085  325 SER A N   
183   C CA  . SER A 24  ? 0.7236 0.8284 0.7602 0.0722  0.0393  0.0132  325 SER A CA  
184   C C   . SER A 24  ? 0.7697 0.9063 0.8164 0.0741  0.0410  0.0110  325 SER A C   
185   O O   . SER A 24  ? 0.7052 0.8576 0.7525 0.0852  0.0403  0.0058  325 SER A O   
186   C CB  . SER A 24  ? 0.6476 0.7512 0.6840 0.0635  0.0442  0.0159  325 SER A CB  
187   O OG  . SER A 24  ? 0.6912 0.8162 0.7303 0.0670  0.0478  0.0131  325 SER A OG  
188   N N   . THR A 25  ? 0.8732 1.0197 0.9276 0.0630  0.0430  0.0145  326 THR A N   
189   C CA  . THR A 25  ? 1.0308 1.2091 1.0957 0.0629  0.0443  0.0121  326 THR A CA  
190   C C   . THR A 25  ? 1.0651 1.2549 1.1379 0.0465  0.0491  0.0163  326 THR A C   
191   O O   . THR A 25  ? 1.1538 1.3664 1.2355 0.0432  0.0492  0.0148  326 THR A O   
192   C CB  . THR A 25  ? 1.0968 1.2787 1.1626 0.0717  0.0383  0.0093  326 THR A CB  
193   O OG1 . THR A 25  ? 1.1255 1.2782 1.1837 0.0703  0.0345  0.0125  326 THR A OG1 
194   C CG2 . THR A 25  ? 1.0773 1.2678 1.1399 0.0900  0.0349  0.0031  326 THR A CG2 
195   N N   . LEU A 26  ? 0.9959 1.1705 1.0650 0.0363  0.0528  0.0212  327 LEU A N   
196   C CA  . LEU A 26  ? 0.9602 1.1408 1.0343 0.0210  0.0571  0.0254  327 LEU A CA  
197   C C   . LEU A 26  ? 0.9190 1.0931 0.9886 0.0145  0.0626  0.0294  327 LEU A C   
198   O O   . LEU A 26  ? 1.0163 1.1756 1.0784 0.0206  0.0620  0.0295  327 LEU A O   
199   C CB  . LEU A 26  ? 0.9650 1.1275 1.0376 0.0143  0.0542  0.0280  327 LEU A CB  
200   C CG  . LEU A 26  ? 0.9309 1.0661 0.9959 0.0192  0.0493  0.0290  327 LEU A CG  
201   C CD1 . LEU A 26  ? 0.8431 0.9718 0.9095 0.0111  0.0476  0.0308  327 LEU A CD1 
202   C CD2 . LEU A 26  ? 0.9285 1.0604 0.9899 0.0337  0.0442  0.0250  327 LEU A CD2 
203   N N   . GLU A 27  ? 0.7690 0.9541 0.8424 0.0020  0.0677  0.0328  328 GLU A N   
204   C CA  . GLU A 27  ? 0.7489 0.9347 0.8182 -0.0033 0.0737  0.0366  328 GLU A CA  
205   C C   . GLU A 27  ? 0.7015 0.8581 0.7606 -0.0042 0.0733  0.0409  328 GLU A C   
206   O O   . GLU A 27  ? 0.7782 0.9153 0.8347 -0.0073 0.0706  0.0428  328 GLU A O   
207   C CB  . GLU A 27  ? 0.8224 1.0212 0.8961 -0.0185 0.0791  0.0403  328 GLU A CB  
208   C CG  . GLU A 27  ? 0.9158 1.1496 0.9981 -0.0197 0.0831  0.0375  328 GLU A CG  
209   C CD  . GLU A 27  ? 1.0627 1.3064 1.1484 -0.0375 0.0887  0.0417  328 GLU A CD  
210   O OE1 . GLU A 27  ? 1.1218 1.3528 1.2080 -0.0470 0.0870  0.0434  328 GLU A OE1 
211   O OE2 . GLU A 27  ? 1.1016 1.3651 1.1888 -0.0424 0.0948  0.0432  328 GLU A OE2 
212   N N   . THR A 28  ? 0.5885 0.7443 0.6418 -0.0010 0.0762  0.0420  329 THR A N   
213   C CA  . THR A 28  ? 0.5386 0.6723 0.5826 -0.0035 0.0771  0.0467  329 THR A CA  
214   C C   . THR A 28  ? 0.4801 0.6129 0.5208 -0.0153 0.0829  0.0532  329 THR A C   
215   O O   . THR A 28  ? 0.6408 0.7537 0.6736 -0.0182 0.0832  0.0577  329 THR A O   
216   C CB  . THR A 28  ? 0.7038 0.8355 0.7417 0.0062  0.0766  0.0445  329 THR A CB  
217   O OG1 . THR A 28  ? 0.6467 0.7991 0.6847 0.0065  0.0817  0.0445  329 THR A OG1 
218   C CG2 . THR A 28  ? 0.6721 0.8006 0.7109 0.0177  0.0708  0.0380  329 THR A CG2 
219   N N   . GLY A 29  ? 0.4877 0.6418 0.5335 -0.0219 0.0875  0.0539  330 GLY A N   
220   C CA  . GLY A 29  ? 0.4406 0.5943 0.4816 -0.0335 0.0937  0.0604  330 GLY A CA  
221   C C   . GLY A 29  ? 0.5557 0.7224 0.5920 -0.0310 0.0988  0.0621  330 GLY A C   
222   O O   . GLY A 29  ? 0.5750 0.7499 0.6092 -0.0412 0.1051  0.0670  330 GLY A O   
223   N N   . CYS A 30  ? 0.4467 0.6155 0.4808 -0.0181 0.0964  0.0580  331 CYS A N   
224   C CA  . CYS A 30  ? 0.3748 0.5572 0.4038 -0.0144 0.1009  0.0586  331 CYS A CA  
225   C C   . CYS A 30  ? 0.4230 0.6385 0.4612 -0.0132 0.1040  0.0544  331 CYS A C   
226   O O   . CYS A 30  ? 0.4477 0.6752 0.4961 -0.0114 0.1010  0.0494  331 CYS A O   
227   C CB  . CYS A 30  ? 0.3352 0.5082 0.3581 -0.0010 0.0967  0.0546  331 CYS A CB  
228   S SG  . CYS A 30  ? 0.4466 0.5864 0.4598 -0.0005 0.0928  0.0583  331 CYS A SG  
229   N N   . THR A 31  ? 0.4279 0.6596 0.4620 -0.0135 0.1099  0.0563  332 THR A N   
230   C CA  . THR A 31  ? 0.4770 0.7430 0.5185 -0.0095 0.1131  0.0515  332 THR A CA  
231   C C   . THR A 31  ? 0.4480 0.7187 0.4825 0.0044  0.1127  0.0474  332 THR A C   
232   O O   . THR A 31  ? 0.5150 0.7635 0.5395 0.0091  0.1102  0.0487  332 THR A O   
233   C CB  . THR A 31  ? 0.6264 0.9128 0.6701 -0.0244 0.1217  0.0573  332 THR A CB  
234   O OG1 . THR A 31  ? 0.6606 0.9461 0.6924 -0.0258 0.1275  0.0629  332 THR A OG1 
235   C CG2 . THR A 31  ? 0.5825 0.8533 0.6275 -0.0406 0.1224  0.0633  332 THR A CG2 
236   N N   . GLU A 32  ? 0.3652 0.6665 0.4049 0.0114  0.1151  0.0419  333 GLU A N   
237   C CA  . GLU A 32  ? 0.5385 0.8453 0.5707 0.0251  0.1149  0.0371  333 GLU A CA  
238   C C   . GLU A 32  ? 0.5755 0.8785 0.5957 0.0200  0.1207  0.0441  333 GLU A C   
239   O O   . GLU A 32  ? 0.6512 0.9481 0.6621 0.0304  0.1190  0.0412  333 GLU A O   
240   C CB  . GLU A 32  ? 0.5888 0.9309 0.6286 0.0345  0.1165  0.0294  333 GLU A CB  
241   C CG  . GLU A 32  ? 0.7350 1.0818 0.7857 0.0410  0.1104  0.0226  333 GLU A CG  
242   C CD  . GLU A 32  ? 0.8250 1.1997 0.8799 0.0567  0.1095  0.0129  333 GLU A CD  
243   O OE1 . GLU A 32  ? 0.8208 1.1816 0.8711 0.0721  0.1027  0.0057  333 GLU A OE1 
244   O OE2 . GLU A 32  ? 0.8765 1.2866 0.9389 0.0536  0.1155  0.0124  333 GLU A OE2 
245   N N   . TYR A 33  ? 0.5634 0.8677 0.5821 0.0043  0.1272  0.0534  334 TYR A N   
246   C CA  . TYR A 33  ? 0.5143 0.8150 0.5199 -0.0005 0.1333  0.0611  334 TYR A CA  
247   C C   . TYR A 33  ? 0.5140 0.7822 0.5101 -0.0101 0.1330  0.0703  334 TYR A C   
248   O O   . TYR A 33  ? 0.5527 0.8149 0.5361 -0.0135 0.1376  0.0776  334 TYR A O   
249   C CB  . TYR A 33  ? 0.4671 0.7991 0.4751 -0.0101 0.1429  0.0651  334 TYR A CB  
250   C CG  . TYR A 33  ? 0.6479 1.0143 0.6614 0.0022  0.1444  0.0563  334 TYR A CG  
251   C CD1 . TYR A 33  ? 0.5936 0.9679 0.5963 0.0118  0.1468  0.0550  334 TYR A CD1 
252   C CD2 . TYR A 33  ? 0.6547 1.0456 0.6832 0.0053  0.1428  0.0489  334 TYR A CD2 
253   C CE1 . TYR A 33  ? 0.7330 1.1380 0.7397 0.0242  0.1479  0.0463  334 TYR A CE1 
254   C CE2 . TYR A 33  ? 0.6233 1.0453 0.6561 0.0183  0.1437  0.0404  334 TYR A CE2 
255   C CZ  . TYR A 33  ? 0.7653 1.1939 0.7871 0.0278  0.1464  0.0390  334 TYR A CZ  
256   O OH  . TYR A 33  ? 0.8752 1.3345 0.9001 0.0419  0.1473  0.0298  334 TYR A OH  
257   N N   . ILE A 34  ? 0.6220 0.8691 0.6228 -0.0136 0.1276  0.0704  335 ILE A N   
258   C CA  . ILE A 34  ? 0.5874 0.8029 0.5779 -0.0197 0.1266  0.0780  335 ILE A CA  
259   C C   . ILE A 34  ? 0.6081 0.8021 0.6027 -0.0143 0.1181  0.0736  335 ILE A C   
260   O O   . ILE A 34  ? 0.7498 0.9491 0.7560 -0.0142 0.1147  0.0685  335 ILE A O   
261   C CB  . ILE A 34  ? 0.6746 0.8861 0.6630 -0.0373 0.1328  0.0872  335 ILE A CB  
262   C CG1 . ILE A 34  ? 0.7903 0.9695 0.7749 -0.0428 0.1289  0.0912  335 ILE A CG1 
263   C CG2 . ILE A 34  ? 0.6747 0.9149 0.6764 -0.0462 0.1369  0.0849  335 ILE A CG2 
264   C CD1 . ILE A 34  ? 0.8835 1.0481 0.8569 -0.0566 0.1348  0.1019  335 ILE A CD1 
265   N N   . CYS A 35  ? 0.5177 0.6890 0.5023 -0.0092 0.1146  0.0755  336 CYS A N   
266   C CA  . CYS A 35  ? 0.4925 0.6431 0.4796 -0.0050 0.1072  0.0723  336 CYS A CA  
267   C C   . CYS A 35  ? 0.5024 0.6310 0.4855 -0.0149 0.1077  0.0795  336 CYS A C   
268   O O   . CYS A 35  ? 0.4687 0.5873 0.4403 -0.0196 0.1116  0.0873  336 CYS A O   
269   C CB  . CYS A 35  ? 0.4485 0.5897 0.4280 0.0063  0.1028  0.0691  336 CYS A CB  
270   S SG  . CYS A 35  ? 0.4772 0.5955 0.4594 0.0106  0.0943  0.0652  336 CYS A SG  
271   N N   . MET A 36  ? 0.4553 0.5758 0.4467 -0.0175 0.1037  0.0770  337 MET A N   
272   C CA  . MET A 36  ? 0.4940 0.5925 0.4820 -0.0254 0.1030  0.0821  337 MET A CA  
273   C C   . MET A 36  ? 0.5261 0.6068 0.5141 -0.0184 0.0962  0.0790  337 MET A C   
274   O O   . MET A 36  ? 0.5209 0.5879 0.5108 -0.0227 0.0940  0.0798  337 MET A O   
275   C CB  . MET A 36  ? 0.5020 0.6073 0.4989 -0.0364 0.1047  0.0821  337 MET A CB  
276   C CG  . MET A 36  ? 0.6755 0.8029 0.6742 -0.0442 0.1117  0.0845  337 MET A CG  
277   S SD  . MET A 36  ? 0.7856 0.9148 0.7889 -0.0625 0.1157  0.0882  337 MET A SD  
278   C CE  . MET A 36  ? 0.8232 0.9933 0.8373 -0.0653 0.1210  0.0848  337 MET A CE  
279   N N   . GLY A 37  ? 0.4286 0.5103 0.4140 -0.0080 0.0931  0.0752  338 GLY A N   
280   C CA  . GLY A 37  ? 0.4531 0.5210 0.4388 -0.0019 0.0870  0.0719  338 GLY A CA  
281   C C   . GLY A 37  ? 0.4501 0.4973 0.4290 -0.0044 0.0860  0.0769  338 GLY A C   
282   O O   . GLY A 37  ? 0.5875 0.6250 0.5691 -0.0018 0.0814  0.0742  338 GLY A O   
283   N N   . SER A 38  ? 0.3972 0.4366 0.3661 -0.0090 0.0901  0.0842  339 SER A N   
284   C CA  . SER A 38  ? 0.4616 0.4797 0.4222 -0.0097 0.0889  0.0888  339 SER A CA  
285   C C   . SER A 38  ? 0.4798 0.4864 0.4396 -0.0201 0.0913  0.0930  339 SER A C   
286   O O   . SER A 38  ? 0.5751 0.5622 0.5261 -0.0206 0.0908  0.0971  339 SER A O   
287   C CB  . SER A 38  ? 0.5009 0.5125 0.4472 -0.0050 0.0906  0.0943  339 SER A CB  
288   O OG  . SER A 38  ? 0.4417 0.4558 0.3802 -0.0110 0.0968  0.1006  339 SER A OG  
289   N N   . ILE A 39  ? 0.4371 0.4559 0.4056 -0.0279 0.0937  0.0915  340 ILE A N   
290   C CA  . ILE A 39  ? 0.5077 0.5171 0.4769 -0.0387 0.0952  0.0939  340 ILE A CA  
291   C C   . ILE A 39  ? 0.5169 0.5180 0.4926 -0.0365 0.0898  0.0892  340 ILE A C   
292   O O   . ILE A 39  ? 0.4891 0.5015 0.4747 -0.0311 0.0862  0.0831  340 ILE A O   
293   C CB  . ILE A 39  ? 0.5745 0.6041 0.5523 -0.0478 0.0992  0.0929  340 ILE A CB  
294   C CG1 . ILE A 39  ? 0.5576 0.5980 0.5288 -0.0499 0.1053  0.0975  340 ILE A CG1 
295   C CG2 . ILE A 39  ? 0.4906 0.5125 0.4708 -0.0601 0.1000  0.0938  340 ILE A CG2 
296   C CD1 . ILE A 39  ? 0.5770 0.5964 0.5312 -0.0533 0.1087  0.1063  340 ILE A CD1 
297   N N   . MET A 40  ? 0.5021 0.4823 0.4708 -0.0401 0.0891  0.0921  341 MET A N   
298   C CA  . MET A 40  ? 0.6178 0.5902 0.5911 -0.0369 0.0841  0.0879  341 MET A CA  
299   C C   . MET A 40  ? 0.6389 0.6227 0.6243 -0.0429 0.0829  0.0832  341 MET A C   
300   O O   . MET A 40  ? 0.7622 0.7524 0.7556 -0.0376 0.0789  0.0781  341 MET A O   
301   C CB  . MET A 40  ? 0.7147 0.6623 0.6766 -0.0375 0.0834  0.0914  341 MET A CB  
302   C CG  . MET A 40  ? 0.8762 0.8191 0.8421 -0.0310 0.0783  0.0868  341 MET A CG  
303   S SD  . MET A 40  ? 1.0714 0.9885 1.0234 -0.0262 0.0768  0.0898  341 MET A SD  
304   C CE  . MET A 40  ? 0.9748 0.8887 0.9149 -0.0187 0.0787  0.0952  341 MET A CE  
305   N N   . HIS A 41  ? 0.6812 0.6678 0.6676 -0.0541 0.0861  0.0849  342 HIS A N   
306   C CA  . HIS A 41  ? 0.7543 0.7557 0.7527 -0.0599 0.0850  0.0801  342 HIS A CA  
307   C C   . HIS A 41  ? 0.7441 0.7664 0.7476 -0.0672 0.0897  0.0809  342 HIS A C   
308   O O   . HIS A 41  ? 0.7500 0.7689 0.7498 -0.0792 0.0935  0.0844  342 HIS A O   
309   C CB  . HIS A 41  ? 0.8410 0.8274 0.8371 -0.0680 0.0836  0.0798  342 HIS A CB  
310   C CG  . HIS A 41  ? 0.9881 0.9509 0.9754 -0.0622 0.0805  0.0805  342 HIS A CG  
311   N ND1 . HIS A 41  ? 0.9924 0.9557 0.9836 -0.0525 0.0760  0.0767  342 HIS A ND1 
312   C CD2 . HIS A 41  ? 1.0289 0.9672 1.0032 -0.0647 0.0814  0.0843  342 HIS A CD2 
313   C CE1 . HIS A 41  ? 0.9858 0.9289 0.9680 -0.0492 0.0745  0.0780  342 HIS A CE1 
314   N NE2 . HIS A 41  ? 1.0085 0.9356 0.9800 -0.0556 0.0774  0.0824  342 HIS A NE2 
315   N N   . PRO A 42  ? 0.8218 0.8664 0.8334 -0.0606 0.0895  0.0775  343 PRO A N   
316   C CA  . PRO A 42  ? 0.8123 0.8805 0.8291 -0.0663 0.0943  0.0778  343 PRO A CA  
317   C C   . PRO A 42  ? 0.8524 0.9379 0.8803 -0.0756 0.0944  0.0742  343 PRO A C   
318   O O   . PRO A 42  ? 0.9366 1.0282 0.9728 -0.0712 0.0895  0.0686  343 PRO A O   
319   C CB  . PRO A 42  ? 0.8431 0.9277 0.8645 -0.0537 0.0929  0.0738  343 PRO A CB  
320   C CG  . PRO A 42  ? 0.8517 0.9176 0.8673 -0.0436 0.0885  0.0733  343 PRO A CG  
321   C CD  . PRO A 42  ? 0.8488 0.8963 0.8632 -0.0474 0.0854  0.0735  343 PRO A CD  
322   N N   . PRO A 49  ? 1.6085 1.7113 1.6799 -0.1553 0.0483  0.0168  350 PRO A N   
323   C CA  . PRO A 49  ? 1.6456 1.7512 1.7176 -0.1423 0.0416  0.0124  350 PRO A CA  
324   C C   . PRO A 49  ? 1.6901 1.8345 1.7767 -0.1390 0.0374  0.0064  350 PRO A C   
325   O O   . PRO A 49  ? 1.6551 1.8062 1.7430 -0.1240 0.0328  0.0049  350 PRO A O   
326   C CB  . PRO A 49  ? 1.6252 1.7069 1.6872 -0.1508 0.0386  0.0088  350 PRO A CB  
327   C CG  . PRO A 49  ? 1.6009 1.6751 1.6604 -0.1708 0.0430  0.0095  350 PRO A CG  
328   C CD  . PRO A 49  ? 1.5966 1.6714 1.6566 -0.1702 0.0498  0.0170  350 PRO A CD  
329   N N   . GLU A 50  ? 1.7919 1.9620 1.8887 -0.1528 0.0391  0.0032  351 GLU A N   
330   C CA  . GLU A 50  ? 1.8209 2.0321 1.9324 -0.1500 0.0353  -0.0029 351 GLU A CA  
331   C C   . GLU A 50  ? 1.7603 1.9924 1.8791 -0.1350 0.0367  -0.0004 351 GLU A C   
332   O O   . GLU A 50  ? 1.7482 2.0150 1.8787 -0.1292 0.0334  -0.0053 351 GLU A O   
333   C CB  . GLU A 50  ? 1.8564 2.0907 1.9772 -0.1709 0.0372  -0.0073 351 GLU A CB  
334   C CG  . GLU A 50  ? 1.8306 2.1017 1.9639 -0.1721 0.0308  -0.0164 351 GLU A CG  
335   C CD  . GLU A 50  ? 1.7943 2.0495 1.9204 -0.1728 0.0240  -0.0217 351 GLU A CD  
336   O OE1 . GLU A 50  ? 1.7624 2.0121 1.8843 -0.1553 0.0188  -0.0222 351 GLU A OE1 
337   O OE2 . GLU A 50  ? 1.7841 2.0315 1.9078 -0.1913 0.0238  -0.0254 351 GLU A OE2 
338   N N   . ASP A 51  ? 1.6659 1.8781 1.7777 -0.1277 0.0412  0.0066  352 ASP A N   
339   C CA  . ASP A 51  ? 1.5368 1.7646 1.6535 -0.1132 0.0425  0.0086  352 ASP A CA  
340   C C   . ASP A 51  ? 1.3505 1.5758 1.4648 -0.0937 0.0363  0.0073  352 ASP A C   
341   O O   . ASP A 51  ? 1.3500 1.5693 1.4613 -0.0803 0.0372  0.0106  352 ASP A O   
342   C CB  . ASP A 51  ? 1.5357 1.7422 1.6446 -0.1127 0.0490  0.0162  352 ASP A CB  
343   C CG  . ASP A 51  ? 1.5133 1.7350 1.6273 -0.1269 0.0560  0.0182  352 ASP A CG  
344   O OD1 . ASP A 51  ? 1.5149 1.7267 1.6257 -0.1445 0.0586  0.0190  352 ASP A OD1 
345   O OD2 . ASP A 51  ? 1.4794 1.7218 1.5995 -0.1205 0.0589  0.0191  352 ASP A OD2 
346   N N   . VAL A 52  ? 1.1207 1.3493 1.2351 -0.0924 0.0301  0.0024  353 VAL A N   
347   C CA  . VAL A 52  ? 0.9252 1.1536 1.0367 -0.0744 0.0242  0.0013  353 VAL A CA  
348   C C   . VAL A 52  ? 0.7482 1.0116 0.8703 -0.0640 0.0220  -0.0022 353 VAL A C   
349   O O   . VAL A 52  ? 0.7132 1.0085 0.8470 -0.0720 0.0221  -0.0070 353 VAL A O   
350   C CB  . VAL A 52  ? 0.8995 1.1208 1.0064 -0.0755 0.0182  -0.0026 353 VAL A CB  
351   C CG1 . VAL A 52  ? 0.8671 1.0539 0.9627 -0.0845 0.0203  0.0002  353 VAL A CG1 
352   C CG2 . VAL A 52  ? 0.8547 1.1081 0.9725 -0.0848 0.0147  -0.0102 353 VAL A CG2 
353   N N   . ALA A 53  ? 0.6688 0.9265 0.7865 -0.0462 0.0200  0.0000  354 ALA A N   
354   C CA  . ALA A 53  ? 0.6419 0.9280 0.7674 -0.0339 0.0187  -0.0026 354 ALA A CA  
355   C C   . ALA A 53  ? 0.6768 0.9941 0.8102 -0.0301 0.0122  -0.0096 354 ALA A C   
356   O O   . ALA A 53  ? 0.7160 1.0256 0.8444 -0.0286 0.0069  -0.0113 354 ALA A O   
357   C CB  . ALA A 53  ? 0.5945 0.8616 0.7107 -0.0158 0.0173  0.0010  354 ALA A CB  
358   N N   . THR A 54  ? 0.7411 1.0955 0.8866 -0.0282 0.0126  -0.0139 355 THR A N   
359   C CA  . THR A 54  ? 0.7868 1.1752 0.9405 -0.0217 0.0060  -0.0209 355 THR A CA  
360   C C   . THR A 54  ? 0.8241 1.2076 0.9700 0.0024  -0.0001 -0.0207 355 THR A C   
361   O O   . THR A 54  ? 0.8028 1.1590 0.9383 0.0128  0.0014  -0.0155 355 THR A O   
362   C CB  . THR A 54  ? 0.7707 1.2038 0.9406 -0.0269 0.0086  -0.0260 355 THR A CB  
363   O OG1 . THR A 54  ? 0.8053 1.2460 0.9755 -0.0112 0.0104  -0.0248 355 THR A OG1 
364   C CG2 . THR A 54  ? 0.7687 1.2015 0.9438 -0.0509 0.0161  -0.0243 355 THR A CG2 
365   N N   . LYS A 55  ? 0.8530 1.2634 1.0034 0.0112  -0.0072 -0.0266 356 LYS A N   
366   C CA  . LYS A 55  ? 0.7964 1.2038 0.9385 0.0350  -0.0134 -0.0265 356 LYS A CA  
367   C C   . LYS A 55  ? 0.7078 1.1180 0.8496 0.0484  -0.0106 -0.0251 356 LYS A C   
368   O O   . LYS A 55  ? 0.6617 1.0402 0.7904 0.0598  -0.0105 -0.0201 356 LYS A O   
369   C CB  . LYS A 55  ? 0.8041 1.2478 0.9530 0.0426  -0.0213 -0.0339 356 LYS A CB  
370   C CG  . LYS A 55  ? 0.7453 1.1745 0.8850 0.0432  -0.0276 -0.0340 356 LYS A CG  
371   C CD  . LYS A 55  ? 0.7394 1.2082 0.8865 0.0515  -0.0356 -0.0418 356 LYS A CD  
372   C CE  . LYS A 55  ? 0.8402 1.3001 0.9807 0.0466  -0.0411 -0.0432 356 LYS A CE  
373   N NZ  . LYS A 55  ? 0.8797 1.3814 1.0282 0.0529  -0.0494 -0.0517 356 LYS A NZ  
374   N N   . ASP A 56  ? 0.7570 1.2056 0.9131 0.0465  -0.0080 -0.0299 357 ASP A N   
375   C CA  . ASP A 56  ? 0.7675 1.2231 0.9235 0.0610  -0.0058 -0.0300 357 ASP A CA  
376   C C   . ASP A 56  ? 0.6683 1.0891 0.8163 0.0557  0.0012  -0.0232 357 ASP A C   
377   O O   . ASP A 56  ? 0.7184 1.1253 0.8583 0.0710  0.0012  -0.0216 357 ASP A O   
378   C CB  . ASP A 56  ? 0.8698 1.3767 1.0437 0.0576  -0.0034 -0.0365 357 ASP A CB  
379   C CG  . ASP A 56  ? 0.8922 1.4383 1.0756 0.0626  -0.0106 -0.0441 357 ASP A CG  
380   O OD1 . ASP A 56  ? 0.7898 1.3252 0.9636 0.0778  -0.0185 -0.0445 357 ASP A OD1 
381   O OD2 . ASP A 56  ? 0.9645 1.5528 1.1645 0.0508  -0.0084 -0.0494 357 ASP A OD2 
382   N N   . GLN A 57  ? 0.5392 0.9443 0.6882 0.0350  0.0066  -0.0195 358 GLN A N   
383   C CA  . GLN A 57  ? 0.4546 0.8248 0.5946 0.0307  0.0124  -0.0129 358 GLN A CA  
384   C C   . GLN A 57  ? 0.5312 0.8617 0.6550 0.0425  0.0087  -0.0085 358 GLN A C   
385   O O   . GLN A 57  ? 0.4989 0.8083 0.6146 0.0501  0.0108  -0.0052 358 GLN A O   
386   C CB  . GLN A 57  ? 0.5774 0.9373 0.7198 0.0075  0.0180  -0.0098 358 GLN A CB  
387   C CG  . GLN A 57  ? 0.7431 1.1343 0.8987 -0.0063 0.0241  -0.0119 358 GLN A CG  
388   C CD  . GLN A 57  ? 0.8138 1.1876 0.9683 -0.0285 0.0299  -0.0078 358 GLN A CD  
389   O OE1 . GLN A 57  ? 0.8194 1.1783 0.9706 -0.0381 0.0277  -0.0075 358 GLN A OE1 
390   N NE2 . GLN A 57  ? 0.8269 1.2012 0.9826 -0.0360 0.0373  -0.0045 358 GLN A NE2 
391   N N   . LEU A 58  ? 0.5197 0.8402 0.6382 0.0436  0.0032  -0.0085 359 LEU A N   
392   C CA  . LEU A 58  ? 0.5583 0.8399 0.6611 0.0504  0.0008  -0.0033 359 LEU A CA  
393   C C   . LEU A 58  ? 0.5069 0.7811 0.6003 0.0722  -0.0039 -0.0033 359 LEU A C   
394   O O   . LEU A 58  ? 0.4622 0.7032 0.5428 0.0774  -0.0035 0.0015  359 LEU A O   
395   C CB  . LEU A 58  ? 0.4674 0.7417 0.5668 0.0441  -0.0031 -0.0033 359 LEU A CB  
396   C CG  . LEU A 58  ? 0.4986 0.7332 0.5830 0.0451  -0.0036 0.0026  359 LEU A CG  
397   C CD1 . LEU A 58  ? 0.4865 0.6962 0.5677 0.0358  0.0032  0.0077  359 LEU A CD1 
398   C CD2 . LEU A 58  ? 0.5354 0.7676 0.6178 0.0375  -0.0068 0.0017  359 LEU A CD2 
399   N N   . PHE A 59  ? 0.5226 0.8267 0.6213 0.0851  -0.0085 -0.0088 360 PHE A N   
400   C CA  . PHE A 59  ? 0.6080 0.9036 0.6956 0.1073  -0.0138 -0.0091 360 PHE A CA  
401   C C   . PHE A 59  ? 0.6517 0.9223 0.7308 0.1136  -0.0104 -0.0060 360 PHE A C   
402   O O   . PHE A 59  ? 0.7392 0.9751 0.8030 0.1209  -0.0124 -0.0016 360 PHE A O   
403   C CB  . PHE A 59  ? 0.7716 1.1085 0.8683 0.1205  -0.0183 -0.0163 360 PHE A CB  
404   C CG  . PHE A 59  ? 0.8756 1.2312 0.9746 0.1225  -0.0250 -0.0195 360 PHE A CG  
405   C CD1 . PHE A 59  ? 0.8552 1.1867 0.9387 0.1336  -0.0311 -0.0163 360 PHE A CD1 
406   C CD2 . PHE A 59  ? 0.8874 1.2860 1.0037 0.1133  -0.0252 -0.0257 360 PHE A CD2 
407   C CE1 . PHE A 59  ? 0.8136 1.1635 0.8984 0.1364  -0.0376 -0.0194 360 PHE A CE1 
408   C CE2 . PHE A 59  ? 0.8074 1.2250 0.9259 0.1153  -0.0319 -0.0294 360 PHE A CE2 
409   C CZ  . PHE A 59  ? 0.7576 1.1510 0.8602 0.1274  -0.0382 -0.0264 360 PHE A CZ  
410   N N   . PRO A 60  ? 0.6583 0.9445 0.7462 0.1103  -0.0050 -0.0081 361 PRO A N   
411   C CA  . PRO A 60  ? 0.5882 0.8512 0.6668 0.1182  -0.0028 -0.0062 361 PRO A CA  
412   C C   . PRO A 60  ? 0.4969 0.7222 0.5670 0.1066  0.0011  0.0003  361 PRO A C   
413   O O   . PRO A 60  ? 0.6062 0.8029 0.6639 0.1145  0.0005  0.0027  361 PRO A O   
414   C CB  . PRO A 60  ? 0.6013 0.8958 0.6925 0.1162  0.0022  -0.0105 361 PRO A CB  
415   C CG  . PRO A 60  ? 0.6133 0.9338 0.7191 0.0980  0.0055  -0.0113 361 PRO A CG  
416   C CD  . PRO A 60  ? 0.6201 0.9429 0.7253 0.0975  -0.0003 -0.0118 361 PRO A CD  
417   N N   . LEU A 61  ? 0.4417 0.6659 0.5177 0.0883  0.0047  0.0030  362 LEU A N   
418   C CA  . LEU A 61  ? 0.4768 0.6672 0.5448 0.0786  0.0080  0.0089  362 LEU A CA  
419   C C   . LEU A 61  ? 0.5409 0.7022 0.5947 0.0856  0.0033  0.0123  362 LEU A C   
420   O O   . LEU A 61  ? 0.5572 0.6892 0.6008 0.0861  0.0046  0.0162  362 LEU A O   
421   C CB  . LEU A 61  ? 0.4210 0.6153 0.4966 0.0594  0.0122  0.0107  362 LEU A CB  
422   C CG  . LEU A 61  ? 0.4750 0.6936 0.5628 0.0489  0.0178  0.0088  362 LEU A CG  
423   C CD1 . LEU A 61  ? 0.4604 0.6730 0.5513 0.0303  0.0214  0.0115  362 LEU A CD1 
424   C CD2 . LEU A 61  ? 0.5356 0.7473 0.6208 0.0530  0.0218  0.0097  362 LEU A CD2 
425   N N   . ALA A 62  ? 0.5259 0.6957 0.5787 0.0904  -0.0019 0.0111  363 ALA A N   
426   C CA  . ALA A 62  ? 0.5566 0.6994 0.5946 0.0972  -0.0062 0.0150  363 ALA A CA  
427   C C   . ALA A 62  ? 0.5953 0.7236 0.6214 0.1150  -0.0097 0.0149  363 ALA A C   
428   O O   . ALA A 62  ? 0.6576 0.7532 0.6698 0.1171  -0.0100 0.0195  363 ALA A O   
429   C CB  . ALA A 62  ? 0.5985 0.7547 0.6375 0.0980  -0.0110 0.0136  363 ALA A CB  
430   N N   . LYS A 63  ? 0.6112 0.7631 0.6420 0.1277  -0.0122 0.0095  364 LYS A N   
431   C CA  . LYS A 63  ? 0.6162 0.7524 0.6345 0.1455  -0.0155 0.0088  364 LYS A CA  
432   C C   . LYS A 63  ? 0.6243 0.7330 0.6361 0.1411  -0.0111 0.0114  364 LYS A C   
433   O O   . LYS A 63  ? 0.6265 0.7021 0.6224 0.1471  -0.0132 0.0147  364 LYS A O   
434   C CB  . LYS A 63  ? 0.6226 0.7918 0.6487 0.1595  -0.0178 0.0017  364 LYS A CB  
435   C CG  . LYS A 63  ? 0.6595 0.8107 0.6701 0.1808  -0.0224 0.0003  364 LYS A CG  
436   C CD  . LYS A 63  ? 0.7695 0.9473 0.7876 0.1921  -0.0218 -0.0067 364 LYS A CD  
437   C CE  . LYS A 63  ? 0.8501 1.0202 0.8540 0.2176  -0.0288 -0.0098 364 LYS A CE  
438   N NZ  . LYS A 63  ? 0.8770 1.0012 0.8608 0.2245  -0.0297 -0.0069 364 LYS A NZ  
439   N N   . GLU A 64  ? 0.5966 0.7184 0.6202 0.1297  -0.0051 0.0101  365 GLU A N   
440   C CA  . GLU A 64  ? 0.5879 0.6874 0.6065 0.1251  -0.0011 0.0119  365 GLU A CA  
441   C C   . GLU A 64  ? 0.5786 0.6434 0.5863 0.1169  -0.0006 0.0182  365 GLU A C   
442   O O   . GLU A 64  ? 0.4788 0.5156 0.4738 0.1214  -0.0015 0.0198  365 GLU A O   
443   C CB  . GLU A 64  ? 0.6532 0.7731 0.6858 0.1123  0.0054  0.0107  365 GLU A CB  
444   C CG  . GLU A 64  ? 0.7989 0.9038 0.8277 0.1103  0.0093  0.0110  365 GLU A CG  
445   C CD  . GLU A 64  ? 0.9630 1.0830 1.0034 0.0954  0.0160  0.0118  365 GLU A CD  
446   O OE1 . GLU A 64  ? 0.9887 1.0965 1.0260 0.0921  0.0193  0.0126  365 GLU A OE1 
447   O OE2 . GLU A 64  ? 0.9264 1.0693 0.9779 0.0869  0.0179  0.0116  365 GLU A OE2 
448   N N   . PHE A 65  ? 0.6095 0.6761 0.6215 0.1047  0.0007  0.0215  366 PHE A N   
449   C CA  . PHE A 65  ? 0.6106 0.6483 0.6135 0.0964  0.0019  0.0272  366 PHE A CA  
450   C C   . PHE A 65  ? 0.5225 0.5365 0.5091 0.1067  -0.0032 0.0300  366 PHE A C   
451   O O   . PHE A 65  ? 0.5992 0.5847 0.5744 0.1052  -0.0026 0.0335  366 PHE A O   
452   C CB  . PHE A 65  ? 0.6467 0.6923 0.6570 0.0826  0.0042  0.0293  366 PHE A CB  
453   C CG  . PHE A 65  ? 0.6113 0.6313 0.6119 0.0764  0.0047  0.0348  366 PHE A CG  
454   C CD1 . PHE A 65  ? 0.6282 0.6307 0.6263 0.0684  0.0087  0.0375  366 PHE A CD1 
455   C CD2 . PHE A 65  ? 0.5446 0.5595 0.5384 0.0790  0.0012  0.0370  366 PHE A CD2 
456   C CE1 . PHE A 65  ? 0.6355 0.6176 0.6254 0.0626  0.0095  0.0422  366 PHE A CE1 
457   C CE2 . PHE A 65  ? 0.6513 0.6444 0.6358 0.0732  0.0022  0.0421  366 PHE A CE2 
458   C CZ  . PHE A 65  ? 0.6808 0.6582 0.6639 0.0648  0.0065  0.0446  366 PHE A CZ  
459   N N   . ILE A 66  ? 0.5645 0.5897 0.5491 0.1171  -0.0082 0.0286  367 ILE A N   
460   C CA  . ILE A 66  ? 0.5839 0.5851 0.5510 0.1276  -0.0132 0.0320  367 ILE A CA  
461   C C   . ILE A 66  ? 0.6182 0.5975 0.5729 0.1390  -0.0149 0.0312  367 ILE A C   
462   O O   . ILE A 66  ? 0.5826 0.5290 0.5210 0.1400  -0.0160 0.0357  367 ILE A O   
463   C CB  . ILE A 66  ? 0.5851 0.6055 0.5524 0.1382  -0.0188 0.0301  367 ILE A CB  
464   C CG1 . ILE A 66  ? 0.5711 0.6074 0.5477 0.1258  -0.0175 0.0311  367 ILE A CG1 
465   C CG2 . ILE A 66  ? 0.5846 0.5786 0.5312 0.1517  -0.0243 0.0340  367 ILE A CG2 
466   C CD1 . ILE A 66  ? 0.5273 0.5376 0.4942 0.1157  -0.0155 0.0377  367 ILE A CD1 
467   N N   . ASP A 67  ? 0.5397 0.5366 0.5014 0.1471  -0.0150 0.0251  368 ASP A N   
468   C CA  . ASP A 67  ? 0.5592 0.5359 0.5094 0.1580  -0.0165 0.0230  368 ASP A CA  
469   C C   . ASP A 67  ? 0.5921 0.5428 0.5377 0.1457  -0.0122 0.0259  368 ASP A C   
470   O O   . ASP A 67  ? 0.7062 0.6248 0.6356 0.1499  -0.0141 0.0276  368 ASP A O   
471   C CB  . ASP A 67  ? 0.5424 0.5476 0.5030 0.1675  -0.0163 0.0155  368 ASP A CB  
472   C CG  . ASP A 67  ? 0.6180 0.6480 0.5808 0.1835  -0.0215 0.0116  368 ASP A CG  
473   O OD1 . ASP A 67  ? 0.5730 0.5940 0.5261 0.1903  -0.0263 0.0146  368 ASP A OD1 
474   O OD2 . ASP A 67  ? 0.6323 0.6928 0.6065 0.1896  -0.0208 0.0054  368 ASP A OD2 
475   N N   . GLN A 68  ? 0.5251 0.4895 0.4845 0.1303  -0.0067 0.0263  369 GLN A N   
476   C CA  . GLN A 68  ? 0.5882 0.5330 0.5452 0.1184  -0.0027 0.0285  369 GLN A CA  
477   C C   . GLN A 68  ? 0.6778 0.5938 0.6224 0.1118  -0.0032 0.0350  369 GLN A C   
478   O O   . GLN A 68  ? 0.7186 0.6074 0.6520 0.1094  -0.0031 0.0365  369 GLN A O   
479   C CB  . GLN A 68  ? 0.5816 0.5489 0.5553 0.1047  0.0029  0.0281  369 GLN A CB  
480   C CG  . GLN A 68  ? 0.7324 0.6861 0.7061 0.0930  0.0071  0.0297  369 GLN A CG  
481   C CD  . GLN A 68  ? 0.8116 0.7829 0.7987 0.0794  0.0121  0.0312  369 GLN A CD  
482   O OE1 . GLN A 68  ? 0.8239 0.7842 0.8105 0.0688  0.0150  0.0342  369 GLN A OE1 
483   N NE2 . GLN A 68  ? 0.6705 0.6692 0.6692 0.0797  0.0131  0.0290  369 GLN A NE2 
484   N N   . TYR A 69  ? 0.6545 0.5765 0.6004 0.1086  -0.0039 0.0386  370 TYR A N   
485   C CA  . TYR A 69  ? 0.6823 0.5797 0.6163 0.1022  -0.0039 0.0451  370 TYR A CA  
486   C C   . TYR A 69  ? 0.6386 0.5068 0.5526 0.1134  -0.0085 0.0471  370 TYR A C   
487   O O   . TYR A 69  ? 0.6415 0.4815 0.5433 0.1071  -0.0075 0.0514  370 TYR A O   
488   C CB  . TYR A 69  ? 0.6019 0.5135 0.5408 0.0978  -0.0039 0.0478  370 TYR A CB  
489   C CG  . TYR A 69  ? 0.7351 0.6229 0.6598 0.0942  -0.0044 0.0545  370 TYR A CG  
490   C CD1 . TYR A 69  ? 0.8061 0.6824 0.7303 0.0802  0.0001  0.0583  370 TYR A CD1 
491   C CD2 . TYR A 69  ? 0.7386 0.6160 0.6495 0.1052  -0.0093 0.0571  370 TYR A CD2 
492   C CE1 . TYR A 69  ? 0.7559 0.6125 0.6672 0.0761  0.0003  0.0645  370 TYR A CE1 
493   C CE2 . TYR A 69  ? 0.7873 0.6426 0.6839 0.1014  -0.0093 0.0639  370 TYR A CE2 
494   C CZ  . TYR A 69  ? 0.8190 0.6644 0.7161 0.0863  -0.0042 0.0676  370 TYR A CZ  
495   O OH  . TYR A 69  ? 0.8614 0.6871 0.7446 0.0814  -0.0034 0.0746  370 TYR A OH  
496   N N   . TYR A 70  ? 0.6420 0.5159 0.5515 0.1299  -0.0135 0.0443  371 TYR A N   
497   C CA  . TYR A 70  ? 0.7175 0.5594 0.6052 0.1413  -0.0181 0.0466  371 TYR A CA  
498   C C   . TYR A 70  ? 0.7960 0.6168 0.6762 0.1436  -0.0179 0.0434  371 TYR A C   
499   O O   . TYR A 70  ? 0.8330 0.6184 0.6939 0.1458  -0.0200 0.0465  371 TYR A O   
500   C CB  . TYR A 70  ? 0.7126 0.5651 0.5954 0.1602  -0.0242 0.0447  371 TYR A CB  
501   C CG  . TYR A 70  ? 0.7551 0.6097 0.6340 0.1584  -0.0257 0.0502  371 TYR A CG  
502   C CD1 . TYR A 70  ? 0.7744 0.5960 0.6321 0.1599  -0.0277 0.0574  371 TYR A CD1 
503   C CD2 . TYR A 70  ? 0.7085 0.5970 0.6044 0.1533  -0.0246 0.0485  371 TYR A CD2 
504   C CE1 . TYR A 70  ? 0.8410 0.6655 0.6947 0.1580  -0.0287 0.0625  371 TYR A CE1 
505   C CE2 . TYR A 70  ? 0.7456 0.6363 0.6377 0.1512  -0.0259 0.0529  371 TYR A CE2 
506   C CZ  . TYR A 70  ? 0.7987 0.6583 0.6698 0.1541  -0.0280 0.0599  371 TYR A CZ  
507   O OH  . TYR A 70  ? 0.7875 0.6510 0.6544 0.1525  -0.0293 0.0642  371 TYR A OH  
508   N N   . SER A 71  ? 0.7573 0.5978 0.6513 0.1423  -0.0154 0.0372  372 SER A N   
509   C CA  . SER A 71  ? 0.8428 0.6634 0.7301 0.1420  -0.0149 0.0339  372 SER A CA  
510   C C   . SER A 71  ? 0.8356 0.6343 0.7189 0.1241  -0.0111 0.0386  372 SER A C   
511   O O   . SER A 71  ? 0.8724 0.6380 0.7395 0.1234  -0.0126 0.0396  372 SER A O   
512   C CB  . SER A 71  ? 0.9256 0.7746 0.8287 0.1438  -0.0125 0.0267  372 SER A CB  
513   O OG  . SER A 71  ? 1.0592 0.8923 0.9586 0.1386  -0.0108 0.0239  372 SER A OG  
514   N N   . SER A 72  ? 0.7722 0.5886 0.6694 0.1096  -0.0065 0.0413  373 SER A N   
515   C CA  . SER A 72  ? 0.7677 0.5697 0.6638 0.0928  -0.0026 0.0451  373 SER A CA  
516   C C   . SER A 72  ? 0.9246 0.6931 0.8017 0.0899  -0.0041 0.0513  373 SER A C   
517   O O   . SER A 72  ? 0.9995 0.7484 0.8705 0.0786  -0.0021 0.0529  373 SER A O   
518   C CB  . SER A 72  ? 0.7042 0.5304 0.6162 0.0809  0.0018  0.0474  373 SER A CB  
519   O OG  . SER A 72  ? 0.7684 0.5921 0.6755 0.0803  0.0010  0.0530  373 SER A OG  
520   N N   . ILE A 73  ? 0.8933 0.6556 0.7606 0.0990  -0.0075 0.0551  374 ILE A N   
521   C CA  . ILE A 73  ? 0.9337 0.6649 0.7819 0.0957  -0.0085 0.0623  374 ILE A CA  
522   C C   . ILE A 73  ? 1.0027 0.7034 0.8294 0.1105  -0.0141 0.0619  374 ILE A C   
523   O O   . ILE A 73  ? 1.0125 0.6882 0.8209 0.1128  -0.0161 0.0684  374 ILE A O   
524   C CB  . ILE A 73  ? 0.8853 0.6278 0.7347 0.0940  -0.0080 0.0681  374 ILE A CB  
525   C CG1 . ILE A 73  ? 0.8213 0.5811 0.6722 0.1114  -0.0128 0.0657  374 ILE A CG1 
526   C CG2 . ILE A 73  ? 0.8329 0.6004 0.7007 0.0791  -0.0025 0.0684  374 ILE A CG2 
527   C CD1 . ILE A 73  ? 0.7618 0.5278 0.6091 0.1124  -0.0139 0.0712  374 ILE A CD1 
528   N N   . LYS A 74  ? 1.0620 0.7639 0.8897 0.1213  -0.0165 0.0546  375 LYS A N   
529   C CA  . LYS A 74  ? 1.1515 0.8223 0.9579 0.1365  -0.0220 0.0529  375 LYS A CA  
530   C C   . LYS A 74  ? 1.1168 0.7824 0.9106 0.1522  -0.0270 0.0569  375 LYS A C   
531   O O   . LYS A 74  ? 1.2873 0.9163 1.0573 0.1581  -0.0304 0.0614  375 LYS A O   
532   C CB  . LYS A 74  ? 1.2078 0.8368 0.9961 0.1255  -0.0213 0.0559  375 LYS A CB  
533   C CG  . LYS A 74  ? 1.2204 0.8528 1.0190 0.1119  -0.0177 0.0508  375 LYS A CG  
534   C CD  . LYS A 74  ? 1.3661 0.9744 1.1517 0.1217  -0.0215 0.0438  375 LYS A CD  
535   C CE  . LYS A 74  ? 1.3748 0.9914 1.1719 0.1095  -0.0183 0.0377  375 LYS A CE  
536   N NZ  . LYS A 74  ? 1.3260 0.9883 1.1494 0.1067  -0.0145 0.0346  375 LYS A NZ  
537   N N   . ARG A 75  ? 0.9859 0.6882 0.7952 0.1585  -0.0274 0.0555  376 ARG A N   
538   C CA  . ARG A 75  ? 0.9393 0.6444 0.7394 0.1751  -0.0327 0.0577  376 ARG A CA  
539   C C   . ARG A 75  ? 0.8789 0.6208 0.6935 0.1910  -0.0356 0.0497  376 ARG A C   
540   O O   . ARG A 75  ? 0.8524 0.6131 0.6688 0.2013  -0.0390 0.0504  376 ARG A O   
541   C CB  . ARG A 75  ? 0.9511 0.6646 0.7534 0.1658  -0.0309 0.0651  376 ARG A CB  
542   C CG  . ARG A 75  ? 0.9720 0.6513 0.7583 0.1514  -0.0280 0.0740  376 ARG A CG  
543   C CD  . ARG A 75  ? 1.0354 0.6712 0.7919 0.1628  -0.0328 0.0785  376 ARG A CD  
544   N NE  . ARG A 75  ? 1.1126 0.7210 0.8528 0.1507  -0.0305 0.0886  376 ARG A NE  
545   C CZ  . ARG A 75  ? 1.1528 0.7340 0.8849 0.1341  -0.0264 0.0922  376 ARG A CZ  
546   N NH1 . ARG A 75  ? 1.1455 0.7052 0.8628 0.1234  -0.0240 0.1018  376 ARG A NH1 
547   N NH2 . ARG A 75  ? 1.1659 0.7425 0.9043 0.1279  -0.0248 0.0861  376 ARG A NH2 
548   N N   . PHE A 76  ? 0.8516 0.6056 0.6764 0.1931  -0.0344 0.0420  377 PHE A N   
549   C CA  . PHE A 76  ? 0.7498 0.5418 0.5894 0.2067  -0.0362 0.0344  377 PHE A CA  
550   C C   . PHE A 76  ? 0.8809 0.6637 0.7042 0.2318  -0.0437 0.0321  377 PHE A C   
551   O O   . PHE A 76  ? 0.9347 0.6801 0.7364 0.2411  -0.0470 0.0322  377 PHE A O   
552   C CB  . PHE A 76  ? 0.8245 0.6293 0.6765 0.2029  -0.0327 0.0272  377 PHE A CB  
553   C CG  . PHE A 76  ? 0.7985 0.6466 0.6682 0.2132  -0.0331 0.0197  377 PHE A CG  
554   C CD1 . PHE A 76  ? 0.8115 0.6631 0.6738 0.2357  -0.0382 0.0137  377 PHE A CD1 
555   C CD2 . PHE A 76  ? 0.7230 0.6083 0.6161 0.2004  -0.0282 0.0188  377 PHE A CD2 
556   C CE1 . PHE A 76  ? 0.8174 0.7125 0.6968 0.2446  -0.0381 0.0067  377 PHE A CE1 
557   C CE2 . PHE A 76  ? 0.7363 0.6620 0.6454 0.2080  -0.0279 0.0124  377 PHE A CE2 
558   C CZ  . PHE A 76  ? 0.8005 0.7329 0.7036 0.2298  -0.0327 0.0063  377 PHE A CZ  
559   N N   . GLY A 77  ? 0.8491 0.6663 0.6821 0.2432  -0.0467 0.0297  378 GLY A N   
560   C CA  . GLY A 77  ? 0.8483 0.6616 0.6667 0.2682  -0.0542 0.0279  378 GLY A CA  
561   C C   . GLY A 77  ? 0.9391 0.7254 0.7368 0.2729  -0.0584 0.0365  378 GLY A C   
562   O O   . GLY A 77  ? 0.9782 0.7630 0.7631 0.2947  -0.0652 0.0356  378 GLY A O   
563   N N   . SER A 78  ? 0.9090 0.6757 0.7028 0.2538  -0.0545 0.0446  379 SER A N   
564   C CA  . SER A 78  ? 0.9330 0.6701 0.7045 0.2568  -0.0576 0.0537  379 SER A CA  
565   C C   . SER A 78  ? 0.9409 0.7100 0.7191 0.2651  -0.0612 0.0543  379 SER A C   
566   O O   . SER A 78  ? 0.8518 0.6660 0.6544 0.2622  -0.0599 0.0487  379 SER A O   
567   C CB  . SER A 78  ? 0.9942 0.7073 0.7620 0.2329  -0.0517 0.0617  379 SER A CB  
568   O OG  . SER A 78  ? 0.9165 0.6645 0.7080 0.2165  -0.0467 0.0616  379 SER A OG  
569   N N   . LYS A 79  ? 0.8961 0.6402 0.6512 0.2751  -0.0659 0.0614  380 LYS A N   
570   C CA  . LYS A 79  ? 0.9444 0.7157 0.7030 0.2826  -0.0698 0.0627  380 LYS A CA  
571   C C   . LYS A 79  ? 0.8562 0.6576 0.6374 0.2608  -0.0641 0.0634  380 LYS A C   
572   O O   . LYS A 79  ? 0.9050 0.7496 0.7056 0.2625  -0.0653 0.0580  380 LYS A O   
573   C CB  . LYS A 79  ? 1.0865 0.8201 0.8140 0.2931  -0.0746 0.0722  380 LYS A CB  
574   C CG  . LYS A 79  ? 1.1581 0.9169 0.8832 0.3100  -0.0815 0.0721  380 LYS A CG  
575   C CD  . LYS A 79  ? 1.3337 1.0529 1.0266 0.3174  -0.0851 0.0832  380 LYS A CD  
576   C CE  . LYS A 79  ? 1.4358 1.1530 1.1110 0.3467  -0.0945 0.0815  380 LYS A CE  
577   N NZ  . LYS A 79  ? 1.4349 1.2013 1.1245 0.3581  -0.0998 0.0768  380 LYS A NZ  
578   N N   . ALA A 80  ? 0.7586 0.5380 0.5377 0.2398  -0.0577 0.0695  381 ALA A N   
579   C CA  . ALA A 80  ? 0.7745 0.5794 0.5735 0.2198  -0.0521 0.0699  381 ALA A CA  
580   C C   . ALA A 80  ? 0.8184 0.6619 0.6459 0.2133  -0.0489 0.0609  381 ALA A C   
581   O O   . ALA A 80  ? 0.8108 0.6878 0.6564 0.2055  -0.0475 0.0583  381 ALA A O   
582   C CB  . ALA A 80  ? 0.7454 0.5201 0.5368 0.1999  -0.0458 0.0774  381 ALA A CB  
583   N N   . HIS A 81  ? 0.7834 0.6213 0.6140 0.2158  -0.0477 0.0562  382 HIS A N   
584   C CA  . HIS A 81  ? 0.7848 0.6586 0.6404 0.2109  -0.0446 0.0480  382 HIS A CA  
585   C C   . HIS A 81  ? 0.7206 0.6353 0.5884 0.2242  -0.0492 0.0416  382 HIS A C   
586   O O   . HIS A 81  ? 0.6986 0.6486 0.5875 0.2142  -0.0466 0.0381  382 HIS A O   
587   C CB  . HIS A 81  ? 0.7598 0.6182 0.6126 0.2147  -0.0434 0.0440  382 HIS A CB  
588   C CG  . HIS A 81  ? 0.7802 0.6731 0.6563 0.2102  -0.0398 0.0362  382 HIS A CG  
589   N ND1 . HIS A 81  ? 0.7796 0.6684 0.6555 0.2169  -0.0394 0.0307  382 HIS A ND1 
590   C CD2 . HIS A 81  ? 0.7256 0.6560 0.6246 0.1992  -0.0363 0.0332  382 HIS A CD2 
591   C CE1 . HIS A 81  ? 0.7049 0.6286 0.6028 0.2104  -0.0355 0.0251  382 HIS A CE1 
592   N NE2 . HIS A 81  ? 0.7561 0.7044 0.6680 0.1991  -0.0335 0.0267  382 HIS A NE2 
593   N N   . MET A 82  ? 0.6927 0.6032 0.5470 0.2467  -0.0562 0.0401  383 MET A N   
594   C CA  . MET A 82  ? 0.7571 0.7099 0.6237 0.2608  -0.0608 0.0329  383 MET A CA  
595   C C   . MET A 82  ? 0.7895 0.7654 0.6624 0.2562  -0.0628 0.0346  383 MET A C   
596   O O   . MET A 82  ? 0.7764 0.7957 0.6700 0.2538  -0.0629 0.0283  383 MET A O   
597   C CB  . MET A 82  ? 0.7949 0.7358 0.6433 0.2879  -0.0683 0.0309  383 MET A CB  
598   C CG  . MET A 82  ? 1.0034 0.9304 0.8486 0.2949  -0.0671 0.0264  383 MET A CG  
599   S SD  . MET A 82  ? 1.0702 1.0519 0.9463 0.2927  -0.0636 0.0153  383 MET A SD  
600   C CE  . MET A 82  ? 1.0384 0.9914 0.9116 0.2841  -0.0577 0.0142  383 MET A CE  
601   N N   . GLU A 83  ? 0.8064 0.7544 0.6614 0.2542  -0.0641 0.0429  384 GLU A N   
602   C CA  . GLU A 83  ? 0.7988 0.7677 0.6583 0.2501  -0.0661 0.0441  384 GLU A CA  
603   C C   . GLU A 83  ? 0.7973 0.7871 0.6786 0.2264  -0.0594 0.0425  384 GLU A C   
604   O O   . GLU A 83  ? 0.7943 0.8203 0.6913 0.2228  -0.0607 0.0378  384 GLU A O   
605   C CB  . GLU A 83  ? 0.8509 0.7836 0.6845 0.2534  -0.0686 0.0539  384 GLU A CB  
606   C CG  . GLU A 83  ? 0.9924 0.9066 0.8026 0.2791  -0.0765 0.0557  384 GLU A CG  
607   C CD  . GLU A 83  ? 1.1547 1.0304 0.9370 0.2817  -0.0784 0.0664  384 GLU A CD  
608   O OE1 . GLU A 83  ? 1.1589 1.0207 0.9401 0.2627  -0.0729 0.0725  384 GLU A OE1 
609   O OE2 . GLU A 83  ? 1.2434 1.1030 1.0042 0.3032  -0.0854 0.0688  384 GLU A OE2 
610   N N   . ARG A 84  ? 0.7630 0.7306 0.6453 0.2101  -0.0525 0.0459  385 ARG A N   
611   C CA  . ARG A 84  ? 0.7454 0.7307 0.6474 0.1891  -0.0461 0.0442  385 ARG A CA  
612   C C   . ARG A 84  ? 0.7060 0.7325 0.6311 0.1883  -0.0455 0.0352  385 ARG A C   
613   O O   . ARG A 84  ? 0.6597 0.7136 0.6002 0.1777  -0.0443 0.0322  385 ARG A O   
614   C CB  . ARG A 84  ? 0.7468 0.7036 0.6461 0.1751  -0.0394 0.0483  385 ARG A CB  
615   C CG  . ARG A 84  ? 0.7318 0.7035 0.6492 0.1548  -0.0328 0.0469  385 ARG A CG  
616   C CD  . ARG A 84  ? 0.6877 0.6712 0.6077 0.1473  -0.0332 0.0484  385 ARG A CD  
617   N NE  . ARG A 84  ? 0.7173 0.7083 0.6509 0.1285  -0.0270 0.0478  385 ARG A NE  
618   C CZ  . ARG A 84  ? 0.6375 0.6477 0.5799 0.1203  -0.0268 0.0459  385 ARG A CZ  
619   N NH1 . ARG A 84  ? 0.6902 0.7161 0.6303 0.1287  -0.0326 0.0440  385 ARG A NH1 
620   N NH2 . ARG A 84  ? 0.5295 0.5429 0.4822 0.1045  -0.0213 0.0454  385 ARG A NH2 
621   N N   . LEU A 85  ? 0.7482 0.7796 0.6753 0.1996  -0.0465 0.0309  386 LEU A N   
622   C CA  . LEU A 85  ? 0.7381 0.8092 0.6866 0.1988  -0.0452 0.0226  386 LEU A CA  
623   C C   . LEU A 85  ? 0.7939 0.9037 0.7526 0.2039  -0.0501 0.0177  386 LEU A C   
624   O O   . LEU A 85  ? 0.7881 0.9290 0.7662 0.1911  -0.0473 0.0134  386 LEU A O   
625   C CB  . LEU A 85  ? 0.7447 0.8140 0.6899 0.2142  -0.0466 0.0187  386 LEU A CB  
626   C CG  . LEU A 85  ? 0.7569 0.8360 0.7162 0.2048  -0.0402 0.0149  386 LEU A CG  
627   C CD1 . LEU A 85  ? 0.8037 0.9158 0.7853 0.1866  -0.0355 0.0122  386 LEU A CD1 
628   C CD2 . LEU A 85  ? 0.7642 0.8031 0.7124 0.1964  -0.0360 0.0201  386 LEU A CD2 
629   N N   . GLU A 86  ? 0.8841 0.9928 0.8296 0.2228  -0.0576 0.0181  387 GLU A N   
630   C CA  . GLU A 86  ? 0.8908 1.0394 0.8465 0.2283  -0.0629 0.0126  387 GLU A CA  
631   C C   . GLU A 86  ? 0.7545 0.9059 0.7128 0.2132  -0.0623 0.0151  387 GLU A C   
632   O O   . GLU A 86  ? 0.7557 0.9439 0.7298 0.2074  -0.0637 0.0093  387 GLU A O   
633   C CB  . GLU A 86  ? 1.0360 1.1844 0.9763 0.2547  -0.0717 0.0118  387 GLU A CB  
634   C CG  . GLU A 86  ? 1.1517 1.2688 1.0685 0.2615  -0.0761 0.0196  387 GLU A CG  
635   C CD  . GLU A 86  ? 1.2074 1.3394 1.1142 0.2862  -0.0858 0.0172  387 GLU A CD  
636   O OE1 . GLU A 86  ? 1.2207 1.3986 1.1440 0.2888  -0.0893 0.0096  387 GLU A OE1 
637   O OE2 . GLU A 86  ? 1.2133 1.3114 1.0954 0.3029  -0.0900 0.0227  387 GLU A OE2 
638   N N   . GLU A 87  ? 0.6648 0.7787 0.6081 0.2058  -0.0599 0.0232  388 GLU A N   
639   C CA  . GLU A 87  ? 0.6554 0.7706 0.6014 0.1901  -0.0581 0.0253  388 GLU A CA  
640   C C   . GLU A 87  ? 0.7390 0.8746 0.7069 0.1696  -0.0518 0.0209  388 GLU A C   
641   O O   . GLU A 87  ? 0.7722 0.9305 0.7503 0.1602  -0.0526 0.0173  388 GLU A O   
642   C CB  . GLU A 87  ? 0.6629 0.7350 0.5896 0.1854  -0.0555 0.0348  388 GLU A CB  
643   C CG  . GLU A 87  ? 0.7516 0.8247 0.6784 0.1723  -0.0543 0.0368  388 GLU A CG  
644   C CD  . GLU A 87  ? 0.7619 0.7965 0.6724 0.1649  -0.0502 0.0459  388 GLU A CD  
645   O OE1 . GLU A 87  ? 0.7664 0.7781 0.6745 0.1599  -0.0452 0.0491  388 GLU A OE1 
646   O OE2 . GLU A 87  ? 0.7771 0.8057 0.6772 0.1639  -0.0518 0.0495  388 GLU A OE2 
647   N N   . VAL A 88  ? 0.6189 0.7451 0.5929 0.1625  -0.0457 0.0213  389 VAL A N   
648   C CA  . VAL A 88  ? 0.5498 0.6939 0.5430 0.1442  -0.0397 0.0177  389 VAL A CA  
649   C C   . VAL A 88  ? 0.5905 0.7791 0.6013 0.1454  -0.0422 0.0093  389 VAL A C   
650   O O   . VAL A 88  ? 0.5465 0.7554 0.5702 0.1310  -0.0406 0.0058  389 VAL A O   
651   C CB  . VAL A 88  ? 0.5510 0.6782 0.5460 0.1390  -0.0334 0.0195  389 VAL A CB  
652   C CG1 . VAL A 88  ? 0.5426 0.6934 0.5572 0.1235  -0.0279 0.0152  389 VAL A CG1 
653   C CG2 . VAL A 88  ? 0.5610 0.6493 0.5427 0.1319  -0.0298 0.0271  389 VAL A CG2 
654   N N   . ASN A 89  ? 0.7134 0.9177 0.7246 0.1624  -0.0461 0.0056  390 ASN A N   
655   C CA  . ASN A 89  ? 0.7713 1.0218 0.8001 0.1644  -0.0482 -0.0028 390 ASN A CA  
656   C C   . ASN A 89  ? 0.7471 1.0215 0.7799 0.1626  -0.0537 -0.0063 390 ASN A C   
657   O O   . ASN A 89  ? 0.7788 1.0868 0.8292 0.1506  -0.0527 -0.0123 390 ASN A O   
658   C CB  . ASN A 89  ? 0.9000 1.1612 0.9255 0.1866  -0.0522 -0.0060 390 ASN A CB  
659   C CG  . ASN A 89  ? 1.0204 1.2862 1.0547 0.1842  -0.0463 -0.0080 390 ASN A CG  
660   O OD1 . ASN A 89  ? 1.1234 1.4262 1.1713 0.1891  -0.0467 -0.0148 390 ASN A OD1 
661   N ND2 . ASN A 89  ? 0.9509 1.1812 0.9776 0.1766  -0.0408 -0.0025 390 ASN A ND2 
662   N N   . LYS A 90  ? 0.7068 0.9640 0.7226 0.1740  -0.0595 -0.0026 391 LYS A N   
663   C CA  . LYS A 90  ? 0.7191 0.9971 0.7366 0.1731  -0.0652 -0.0058 391 LYS A CA  
664   C C   . LYS A 90  ? 0.6574 0.9364 0.6841 0.1493  -0.0607 -0.0065 391 LYS A C   
665   O O   . LYS A 90  ? 0.7147 1.0266 0.7550 0.1409  -0.0627 -0.0134 391 LYS A O   
666   C CB  . LYS A 90  ? 0.8450 1.0974 0.8393 0.1884  -0.0712 0.0000  391 LYS A CB  
667   C CG  . LYS A 90  ? 0.9464 1.2037 0.9304 0.2146  -0.0781 -0.0008 391 LYS A CG  
668   C CD  . LYS A 90  ? 1.0316 1.2583 0.9900 0.2283  -0.0834 0.0065  391 LYS A CD  
669   C CE  . LYS A 90  ? 1.0622 1.2913 1.0080 0.2559  -0.0910 0.0059  391 LYS A CE  
670   N NZ  . LYS A 90  ? 1.0828 1.2782 1.0011 0.2689  -0.0958 0.0141  391 LYS A NZ  
671   N N   . GLU A 91  ? 0.5350 0.7781 0.5539 0.1384  -0.0547 0.0001  392 GLU A N   
672   C CA  . GLU A 91  ? 0.5379 0.7787 0.5638 0.1173  -0.0503 -0.0005 392 GLU A CA  
673   C C   . GLU A 91  ? 0.6121 0.8814 0.6591 0.1030  -0.0462 -0.0068 392 GLU A C   
674   O O   . GLU A 91  ? 0.6484 0.9362 0.7049 0.0898  -0.0467 -0.0117 392 GLU A O   
675   C CB  . GLU A 91  ? 0.5671 0.7672 0.5821 0.1098  -0.0442 0.0075  392 GLU A CB  
676   C CG  . GLU A 91  ? 0.5844 0.7567 0.5793 0.1169  -0.0468 0.0139  392 GLU A CG  
677   C CD  . GLU A 91  ? 0.6694 0.8089 0.6571 0.1053  -0.0403 0.0203  392 GLU A CD  
678   O OE1 . GLU A 91  ? 0.7215 0.8619 0.7136 0.0914  -0.0378 0.0189  392 GLU A OE1 
679   O OE2 . GLU A 91  ? 0.7692 0.8823 0.7466 0.1102  -0.0378 0.0265  392 GLU A OE2 
680   N N   . ILE A 92  ? 0.6217 0.8940 0.6751 0.1050  -0.0422 -0.0067 393 ILE A N   
681   C CA  . ILE A 92  ? 0.6333 0.9317 0.7054 0.0911  -0.0376 -0.0116 393 ILE A CA  
682   C C   . ILE A 92  ? 0.7800 1.1238 0.8655 0.0923  -0.0427 -0.0202 393 ILE A C   
683   O O   . ILE A 92  ? 0.8643 1.2294 0.9636 0.0753  -0.0405 -0.0249 393 ILE A O   
684   C CB  . ILE A 92  ? 0.5287 0.8224 0.6033 0.0956  -0.0326 -0.0098 393 ILE A CB  
685   C CG1 . ILE A 92  ? 0.5408 0.7908 0.6022 0.0937  -0.0281 -0.0019 393 ILE A CG1 
686   C CG2 . ILE A 92  ? 0.5778 0.8979 0.6705 0.0807  -0.0271 -0.0140 393 ILE A CG2 
687   C CD1 . ILE A 92  ? 0.3551 0.5975 0.4175 0.0972  -0.0234 -0.0003 393 ILE A CD1 
688   N N   . ASP A 93  ? 0.8198 1.1788 0.9010 0.1123  -0.0498 -0.0225 394 ASP A N   
689   C CA  . ASP A 93  ? 0.7699 1.1750 0.8637 0.1151  -0.0557 -0.0311 394 ASP A CA  
690   C C   . ASP A 93  ? 0.7108 1.1214 0.8049 0.1035  -0.0592 -0.0340 394 ASP A C   
691   O O   . ASP A 93  ? 0.7103 1.1525 0.8200 0.0891  -0.0592 -0.0410 394 ASP A O   
692   C CB  . ASP A 93  ? 0.8574 1.2741 0.9435 0.1416  -0.0633 -0.0325 394 ASP A CB  
693   C CG  . ASP A 93  ? 0.9751 1.4243 1.0737 0.1505  -0.0625 -0.0375 394 ASP A CG  
694   O OD1 . ASP A 93  ? 1.0371 1.4864 1.1450 0.1391  -0.0548 -0.0370 394 ASP A OD1 
695   O OD2 . ASP A 93  ? 0.9954 1.4713 1.0941 0.1696  -0.0696 -0.0421 394 ASP A OD2 
696   N N   . THR A 94  ? 0.6301 1.0107 0.7066 0.1093  -0.0623 -0.0290 395 THR A N   
697   C CA  . THR A 94  ? 0.7239 1.1083 0.7988 0.0998  -0.0660 -0.0320 395 THR A CA  
698   C C   . THR A 94  ? 0.8196 1.1934 0.9017 0.0750  -0.0593 -0.0325 395 THR A C   
699   O O   . THR A 94  ? 0.9022 1.3017 0.9970 0.0605  -0.0601 -0.0398 395 THR A O   
700   C CB  . THR A 94  ? 0.7200 1.0732 0.7730 0.1119  -0.0699 -0.0257 395 THR A CB  
701   O OG1 . THR A 94  ? 0.8249 1.1460 0.8651 0.1237  -0.0670 -0.0173 395 THR A OG1 
702   C CG2 . THR A 94  ? 0.6260 1.0039 0.6746 0.1280  -0.0799 -0.0300 395 THR A CG2 
703   N N   . THR A 95  ? 0.7863 1.1218 0.8597 0.0699  -0.0527 -0.0249 396 THR A N   
704   C CA  . THR A 95  ? 0.6601 0.9763 0.7337 0.0502  -0.0476 -0.0240 396 THR A CA  
705   C C   . THR A 95  ? 0.7422 1.0579 0.8273 0.0356  -0.0396 -0.0236 396 THR A C   
706   O O   . THR A 95  ? 0.8050 1.1048 0.8902 0.0194  -0.0352 -0.0230 396 THR A O   
707   C CB  . THR A 95  ? 0.5986 0.8732 0.6538 0.0541  -0.0458 -0.0159 396 THR A CB  
708   O OG1 . THR A 95  ? 0.6600 0.9124 0.7117 0.0583  -0.0402 -0.0092 396 THR A OG1 
709   C CG2 . THR A 95  ? 0.5213 0.7931 0.5622 0.0709  -0.0531 -0.0144 396 THR A CG2 
710   N N   . SER A 96  ? 0.6533 0.9847 0.7465 0.0418  -0.0376 -0.0238 397 SER A N   
711   C CA  . SER A 96  ? 0.6904 1.0226 0.7935 0.0301  -0.0298 -0.0227 397 SER A CA  
712   C C   . SER A 96  ? 0.6035 0.8955 0.6963 0.0283  -0.0237 -0.0146 397 SER A C   
713   O O   . SER A 96  ? 0.5451 0.8324 0.6436 0.0169  -0.0171 -0.0131 397 SER A O   
714   C CB  . SER A 96  ? 0.7595 1.1091 0.8748 0.0083  -0.0274 -0.0281 397 SER A CB  
715   O OG  . SER A 96  ? 0.7950 1.1846 0.9209 0.0087  -0.0334 -0.0363 397 SER A OG  
716   N N   . THR A 97  ? 0.6148 0.8788 0.6923 0.0390  -0.0257 -0.0093 398 THR A N   
717   C CA  . THR A 97  ? 0.5511 0.7786 0.6184 0.0379  -0.0205 -0.0019 398 THR A CA  
718   C C   . THR A 97  ? 0.5964 0.8037 0.6479 0.0537  -0.0245 0.0027  398 THR A C   
719   O O   . THR A 97  ? 0.6241 0.8447 0.6722 0.0651  -0.0310 0.0004  398 THR A O   
720   C CB  . THR A 97  ? 0.5236 0.7330 0.5892 0.0215  -0.0165 -0.0008 398 THR A CB  
721   O OG1 . THR A 97  ? 0.5619 0.7394 0.6184 0.0217  -0.0118 0.0060  398 THR A OG1 
722   C CG2 . THR A 97  ? 0.4698 0.6780 0.5287 0.0206  -0.0217 -0.0032 398 THR A CG2 
723   N N   . TYR A 98  ? 0.5320 0.7074 0.5734 0.0542  -0.0205 0.0094  399 TYR A N   
724   C CA  . TYR A 98  ? 0.5623 0.7154 0.5875 0.0670  -0.0234 0.0147  399 TYR A CA  
725   C C   . TYR A 98  ? 0.5557 0.6776 0.5715 0.0595  -0.0188 0.0206  399 TYR A C   
726   O O   . TYR A 98  ? 0.5740 0.6909 0.5955 0.0465  -0.0137 0.0206  399 TYR A O   
727   C CB  . TYR A 98  ? 0.5504 0.7006 0.5719 0.0817  -0.0245 0.0164  399 TYR A CB  
728   C CG  . TYR A 98  ? 0.5651 0.7003 0.5883 0.0780  -0.0184 0.0193  399 TYR A CG  
729   C CD1 . TYR A 98  ? 0.5722 0.7249 0.6098 0.0696  -0.0143 0.0158  399 TYR A CD1 
730   C CD2 . TYR A 98  ? 0.5619 0.6662 0.5719 0.0828  -0.0169 0.0254  399 TYR A CD2 
731   C CE1 . TYR A 98  ? 0.5108 0.6506 0.5490 0.0670  -0.0090 0.0183  399 TYR A CE1 
732   C CE2 . TYR A 98  ? 0.6118 0.7036 0.6233 0.0795  -0.0118 0.0273  399 TYR A CE2 
733   C CZ  . TYR A 98  ? 0.5577 0.6676 0.5832 0.0722  -0.0080 0.0237  399 TYR A CZ  
734   O OH  . TYR A 98  ? 0.6037 0.7023 0.6300 0.0697  -0.0033 0.0254  399 TYR A OH  
735   N N   . GLN A 99  ? 0.4534 0.5546 0.4539 0.0680  -0.0208 0.0258  400 GLN A N   
736   C CA  . GLN A 99  ? 0.5016 0.5757 0.4922 0.0621  -0.0167 0.0315  400 GLN A CA  
737   C C   . GLN A 99  ? 0.5781 0.6293 0.5595 0.0686  -0.0147 0.0374  400 GLN A C   
738   O O   . GLN A 99  ? 0.6395 0.6860 0.6118 0.0814  -0.0187 0.0393  400 GLN A O   
739   C CB  . GLN A 99  ? 0.5962 0.6649 0.5753 0.0643  -0.0201 0.0331  400 GLN A CB  
740   C CG  . GLN A 99  ? 0.5862 0.6736 0.5723 0.0567  -0.0221 0.0269  400 GLN A CG  
741   C CD  . GLN A 99  ? 0.6215 0.7060 0.6162 0.0418  -0.0165 0.0251  400 GLN A CD  
742   O OE1 . GLN A 99  ? 0.7314 0.7957 0.7204 0.0371  -0.0120 0.0293  400 GLN A OE1 
743   N NE2 . GLN A 99  ? 0.5236 0.6284 0.5317 0.0345  -0.0168 0.0189  400 GLN A NE2 
744   N N   . LEU A 100 ? 0.5105 0.5466 0.4932 0.0600  -0.0088 0.0402  401 LEU A N   
745   C CA  . LEU A 100 ? 0.5272 0.5397 0.5002 0.0638  -0.0069 0.0457  401 LEU A CA  
746   C C   . LEU A 100 ? 0.5984 0.5915 0.5552 0.0665  -0.0079 0.0514  401 LEU A C   
747   O O   . LEU A 100 ? 0.6750 0.6690 0.6296 0.0610  -0.0073 0.0519  401 LEU A O   
748   C CB  . LEU A 100 ? 0.3836 0.3875 0.3624 0.0535  -0.0006 0.0467  401 LEU A CB  
749   C CG  . LEU A 100 ? 0.3729 0.3933 0.3659 0.0502  0.0014  0.0422  401 LEU A CG  
750   C CD1 . LEU A 100 ? 0.3622 0.3740 0.3595 0.0399  0.0074  0.0436  401 LEU A CD1 
751   C CD2 . LEU A 100 ? 0.4032 0.4274 0.3961 0.0612  -0.0010 0.0407  401 LEU A CD2 
752   N N   . LYS A 101 ? 0.5999 0.5748 0.5443 0.0750  -0.0094 0.0558  402 LYS A N   
753   C CA  . LYS A 101 ? 0.4949 0.4461 0.4231 0.0744  -0.0083 0.0628  402 LYS A CA  
754   C C   . LYS A 101 ? 0.5774 0.5175 0.5081 0.0618  -0.0018 0.0653  402 LYS A C   
755   O O   . LYS A 101 ? 0.6596 0.6054 0.6020 0.0559  0.0014  0.0623  402 LYS A O   
756   C CB  . LYS A 101 ? 0.5291 0.4602 0.4428 0.0854  -0.0112 0.0668  402 LYS A CB  
757   C CG  . LYS A 101 ? 0.7598 0.7010 0.6689 0.1005  -0.0182 0.0646  402 LYS A CG  
758   C CD  . LYS A 101 ? 0.9061 0.8312 0.7953 0.1075  -0.0214 0.0709  402 LYS A CD  
759   C CE  . LYS A 101 ? 0.9845 0.9312 0.8740 0.1171  -0.0277 0.0675  402 LYS A CE  
760   N NZ  . LYS A 101 ? 1.0356 1.0033 0.9354 0.1275  -0.0320 0.0608  402 LYS A NZ  
761   N N   . ASP A 102 ? 0.6518 0.5765 0.5707 0.0580  0.0003  0.0709  403 ASP A N   
762   C CA  . ASP A 102 ? 0.6254 0.5423 0.5465 0.0466  0.0063  0.0731  403 ASP A CA  
763   C C   . ASP A 102 ? 0.5717 0.4761 0.4939 0.0450  0.0084  0.0739  403 ASP A C   
764   O O   . ASP A 102 ? 0.6209 0.5295 0.5532 0.0375  0.0123  0.0719  403 ASP A O   
765   C CB  . ASP A 102 ? 0.7365 0.6408 0.6439 0.0434  0.0082  0.0793  403 ASP A CB  
766   C CG  . ASP A 102 ? 0.8722 0.7894 0.7781 0.0444  0.0065  0.0779  403 ASP A CG  
767   O OD1 . ASP A 102 ? 0.7947 0.7299 0.7108 0.0464  0.0038  0.0718  403 ASP A OD1 
768   O OD2 . ASP A 102 ? 0.9769 0.8862 0.8709 0.0428  0.0080  0.0828  403 ASP A OD2 
769   N N   . THR A 103 ? 0.5982 0.4860 0.5088 0.0524  0.0057  0.0768  404 THR A N   
770   C CA  . THR A 103 ? 0.6350 0.5091 0.5449 0.0515  0.0070  0.0768  404 THR A CA  
771   C C   . THR A 103 ? 0.5884 0.4788 0.5139 0.0523  0.0072  0.0703  404 THR A C   
772   O O   . THR A 103 ? 0.5830 0.4709 0.5143 0.0459  0.0105  0.0691  404 THR A O   
773   C CB  . THR A 103 ? 0.6558 0.5093 0.5496 0.0618  0.0028  0.0798  404 THR A CB  
774   O OG1 . THR A 103 ? 0.6501 0.5162 0.5437 0.0743  -0.0026 0.0772  404 THR A OG1 
775   C CG2 . THR A 103 ? 0.7761 0.6073 0.6524 0.0580  0.0041  0.0876  404 THR A CG2 
776   N N   . GLU A 104 ? 0.6035 0.5118 0.5356 0.0602  0.0036  0.0660  405 GLU A N   
777   C CA  . GLU A 104 ? 0.5143 0.4399 0.4607 0.0608  0.0040  0.0602  405 GLU A CA  
778   C C   . GLU A 104 ? 0.5745 0.5122 0.5334 0.0492  0.0087  0.0585  405 GLU A C   
779   O O   . GLU A 104 ? 0.5770 0.5199 0.5447 0.0458  0.0113  0.0559  405 GLU A O   
780   C CB  . GLU A 104 ? 0.4449 0.3903 0.3959 0.0708  -0.0007 0.0559  405 GLU A CB  
781   C CG  . GLU A 104 ? 0.4570 0.3921 0.3945 0.0848  -0.0062 0.0574  405 GLU A CG  
782   C CD  . GLU A 104 ? 0.5443 0.5026 0.4863 0.0940  -0.0111 0.0535  405 GLU A CD  
783   O OE1 . GLU A 104 ? 0.6359 0.5919 0.5699 0.1081  -0.0161 0.0529  405 GLU A OE1 
784   O OE2 . GLU A 104 ? 0.6273 0.6058 0.5802 0.0873  -0.0104 0.0508  405 GLU A OE2 
785   N N   . LEU A 105 ? 0.5412 0.4828 0.5000 0.0437  0.0097  0.0598  406 LEU A N   
786   C CA  . LEU A 105 ? 0.5752 0.5255 0.5437 0.0338  0.0138  0.0583  406 LEU A CA  
787   C C   . LEU A 105 ? 0.6133 0.5515 0.5809 0.0272  0.0181  0.0606  406 LEU A C   
788   O O   . LEU A 105 ? 0.5327 0.4771 0.5093 0.0226  0.0209  0.0585  406 LEU A O   
789   C CB  . LEU A 105 ? 0.5289 0.4833 0.4949 0.0307  0.0135  0.0589  406 LEU A CB  
790   C CG  . LEU A 105 ? 0.4913 0.4528 0.4652 0.0219  0.0171  0.0568  406 LEU A CG  
791   C CD1 . LEU A 105 ? 0.4971 0.4756 0.4820 0.0205  0.0161  0.0516  406 LEU A CD1 
792   C CD2 . LEU A 105 ? 0.5239 0.4824 0.4911 0.0193  0.0177  0.0585  406 LEU A CD2 
793   N N   . ILE A 106 ? 0.5799 0.5016 0.5366 0.0263  0.0187  0.0652  407 ILE A N   
794   C CA  . ILE A 106 ? 0.5071 0.4190 0.4632 0.0194  0.0225  0.0671  407 ILE A CA  
795   C C   . ILE A 106 ? 0.4967 0.4061 0.4565 0.0214  0.0223  0.0645  407 ILE A C   
796   O O   . ILE A 106 ? 0.4587 0.3707 0.4248 0.0160  0.0253  0.0632  407 ILE A O   
797   C CB  . ILE A 106 ? 0.5242 0.4189 0.4668 0.0173  0.0231  0.0726  407 ILE A CB  
798   C CG1 . ILE A 106 ? 0.4998 0.3992 0.4397 0.0135  0.0248  0.0749  407 ILE A CG1 
799   C CG2 . ILE A 106 ? 0.5223 0.4061 0.4636 0.0107  0.0260  0.0739  407 ILE A CG2 
800   C CD1 . ILE A 106 ? 0.5102 0.3946 0.4351 0.0133  0.0247  0.0809  407 ILE A CD1 
801   N N   . TYR A 107 ? 0.5085 0.4130 0.4637 0.0302  0.0186  0.0636  408 TYR A N   
802   C CA  . TYR A 107 ? 0.5649 0.4667 0.5221 0.0337  0.0180  0.0605  408 TYR A CA  
803   C C   . TYR A 107 ? 0.5947 0.5163 0.5658 0.0325  0.0197  0.0561  408 TYR A C   
804   O O   . TYR A 107 ? 0.4637 0.3856 0.4390 0.0295  0.0219  0.0544  408 TYR A O   
805   C CB  . TYR A 107 ? 0.5335 0.4273 0.4820 0.0455  0.0132  0.0599  408 TYR A CB  
806   C CG  . TYR A 107 ? 0.5361 0.4327 0.4882 0.0516  0.0122  0.0552  408 TYR A CG  
807   C CD1 . TYR A 107 ? 0.5375 0.4565 0.5006 0.0565  0.0115  0.0507  408 TYR A CD1 
808   C CD2 . TYR A 107 ? 0.4706 0.3481 0.4147 0.0519  0.0120  0.0551  408 TYR A CD2 
809   C CE1 . TYR A 107 ? 0.5528 0.4764 0.5190 0.0623  0.0111  0.0463  408 TYR A CE1 
810   C CE2 . TYR A 107 ? 0.5501 0.4304 0.4967 0.0581  0.0110  0.0501  408 TYR A CE2 
811   C CZ  . TYR A 107 ? 0.5886 0.4927 0.5463 0.0638  0.0107  0.0459  408 TYR A CZ  
812   O OH  . TYR A 107 ? 0.6530 0.5615 0.6126 0.0705  0.0101  0.0410  408 TYR A OH  
813   N N   . GLY A 108 ? 0.5467 0.4848 0.5242 0.0346  0.0186  0.0543  409 GLY A N   
814   C CA  . GLY A 108 ? 0.3945 0.3509 0.3843 0.0319  0.0205  0.0508  409 GLY A CA  
815   C C   . GLY A 108 ? 0.4456 0.4026 0.4401 0.0224  0.0248  0.0518  409 GLY A C   
816   O O   . GLY A 108 ? 0.4908 0.4534 0.4913 0.0204  0.0271  0.0501  409 GLY A O   
817   N N   . ALA A 109 ? 0.3971 0.3485 0.3882 0.0174  0.0260  0.0545  410 ALA A N   
818   C CA  . ALA A 109 ? 0.4809 0.4335 0.4758 0.0101  0.0298  0.0550  410 ALA A CA  
819   C C   . ALA A 109 ? 0.5053 0.4504 0.4992 0.0080  0.0318  0.0557  410 ALA A C   
820   O O   . ALA A 109 ? 0.4520 0.4020 0.4510 0.0048  0.0343  0.0547  410 ALA A O   
821   C CB  . ALA A 109 ? 0.4787 0.4281 0.4695 0.0066  0.0306  0.0572  410 ALA A CB  
822   N N   . LYS A 110 ? 0.3393 0.2718 0.3256 0.0095  0.0305  0.0573  411 LYS A N   
823   C CA  . LYS A 110 ? 0.5157 0.4410 0.5007 0.0066  0.0319  0.0571  411 LYS A CA  
824   C C   . LYS A 110 ? 0.5870 0.5172 0.5764 0.0105  0.0314  0.0535  411 LYS A C   
825   O O   . LYS A 110 ? 0.5587 0.4911 0.5512 0.0075  0.0333  0.0523  411 LYS A O   
826   C CB  . LYS A 110 ? 0.4957 0.4039 0.4702 0.0063  0.0304  0.0595  411 LYS A CB  
827   C CG  . LYS A 110 ? 0.5097 0.4136 0.4792 0.0009  0.0320  0.0635  411 LYS A CG  
828   C CD  . LYS A 110 ? 0.5136 0.3988 0.4711 -0.0004 0.0309  0.0667  411 LYS A CD  
829   C CE  . LYS A 110 ? 0.5595 0.4432 0.5128 -0.0074 0.0335  0.0709  411 LYS A CE  
830   N NZ  . LYS A 110 ? 0.6929 0.5585 0.6350 -0.0122 0.0337  0.0744  411 LYS A NZ  
831   N N   . HIS A 111 ? 0.5720 0.5057 0.5615 0.0176  0.0288  0.0516  412 HIS A N   
832   C CA  . HIS A 111 ? 0.5809 0.5206 0.5739 0.0219  0.0286  0.0480  412 HIS A CA  
833   C C   . HIS A 111 ? 0.5883 0.5447 0.5910 0.0191  0.0315  0.0468  412 HIS A C   
834   O O   . HIS A 111 ? 0.4998 0.4603 0.5052 0.0189  0.0331  0.0450  412 HIS A O   
835   C CB  . HIS A 111 ? 0.4154 0.3546 0.4049 0.0317  0.0250  0.0460  412 HIS A CB  
836   C CG  . HIS A 111 ? 0.5391 0.4582 0.5175 0.0355  0.0224  0.0462  412 HIS A CG  
837   N ND1 . HIS A 111 ? 0.5325 0.4346 0.5016 0.0324  0.0216  0.0500  412 HIS A ND1 
838   C CD2 . HIS A 111 ? 0.5204 0.4320 0.4942 0.0416  0.0207  0.0428  412 HIS A CD2 
839   C CE1 . HIS A 111 ? 0.6296 0.5131 0.5886 0.0356  0.0194  0.0494  412 HIS A CE1 
840   N NE2 . HIS A 111 ? 0.5328 0.4211 0.4943 0.0417  0.0186  0.0447  412 HIS A NE2 
841   N N   . ALA A 112 ? 0.5804 0.5453 0.5872 0.0164  0.0322  0.0479  413 ALA A N   
842   C CA  . ALA A 112 ? 0.5576 0.5338 0.5713 0.0119  0.0352  0.0476  413 ALA A CA  
843   C C   . ALA A 112 ? 0.5197 0.4913 0.5330 0.0073  0.0380  0.0489  413 ALA A C   
844   O O   . ALA A 112 ? 0.4325 0.4106 0.4491 0.0058  0.0404  0.0485  413 ALA A O   
845   C CB  . ALA A 112 ? 0.4682 0.4493 0.4840 0.0085  0.0352  0.0484  413 ALA A CB  
846   N N   . TRP A 113 ? 0.4900 0.4515 0.4987 0.0051  0.0379  0.0506  414 TRP A N   
847   C CA  . TRP A 113 ? 0.4619 0.4216 0.4706 0.0017  0.0400  0.0512  414 TRP A CA  
848   C C   . TRP A 113 ? 0.4912 0.4489 0.4987 0.0038  0.0394  0.0489  414 TRP A C   
849   O O   . TRP A 113 ? 0.5036 0.4663 0.5132 0.0031  0.0410  0.0481  414 TRP A O   
850   C CB  . TRP A 113 ? 0.4751 0.4281 0.4801 -0.0019 0.0402  0.0532  414 TRP A CB  
851   C CG  . TRP A 113 ? 0.4892 0.4437 0.4949 -0.0051 0.0421  0.0534  414 TRP A CG  
852   C CD1 . TRP A 113 ? 0.4335 0.3941 0.4421 -0.0047 0.0436  0.0524  414 TRP A CD1 
853   C CD2 . TRP A 113 ? 0.5248 0.4763 0.5280 -0.0089 0.0428  0.0545  414 TRP A CD2 
854   N NE1 . TRP A 113 ? 0.3020 0.2642 0.3102 -0.0071 0.0446  0.0525  414 TRP A NE1 
855   C CE2 . TRP A 113 ? 0.5782 0.5359 0.5839 -0.0102 0.0442  0.0536  414 TRP A CE2 
856   C CE3 . TRP A 113 ? 0.4421 0.3875 0.4410 -0.0115 0.0424  0.0565  414 TRP A CE3 
857   C CZ2 . TRP A 113 ? 0.5150 0.4754 0.5204 -0.0141 0.0452  0.0539  414 TRP A CZ2 
858   C CZ3 . TRP A 113 ? 0.3810 0.3279 0.3790 -0.0164 0.0439  0.0573  414 TRP A CZ3 
859   C CH2 . TRP A 113 ? 0.4830 0.4386 0.4850 -0.0177 0.0452  0.0557  414 TRP A CH2 
860   N N   . ARG A 114 ? 0.4412 0.3907 0.4442 0.0070  0.0368  0.0478  415 ARG A N   
861   C CA  . ARG A 114 ? 0.3972 0.3424 0.3976 0.0098  0.0356  0.0448  415 ARG A CA  
862   C C   . ARG A 114 ? 0.5351 0.4922 0.5399 0.0138  0.0366  0.0423  415 ARG A C   
863   O O   . ARG A 114 ? 0.3794 0.3372 0.3834 0.0147  0.0369  0.0398  415 ARG A O   
864   C CB  . ARG A 114 ? 0.3822 0.3146 0.3754 0.0141  0.0323  0.0440  415 ARG A CB  
865   C CG  . ARG A 114 ? 0.4628 0.3841 0.4501 0.0158  0.0305  0.0409  415 ARG A CG  
866   C CD  . ARG A 114 ? 0.4559 0.3623 0.4343 0.0219  0.0270  0.0403  415 ARG A CD  
867   N NE  . ARG A 114 ? 0.4965 0.3881 0.4672 0.0230  0.0249  0.0369  415 ARG A NE  
868   C CZ  . ARG A 114 ? 0.5512 0.4241 0.5111 0.0281  0.0216  0.0361  415 ARG A CZ  
869   N NH1 . ARG A 114 ? 0.5018 0.3597 0.4540 0.0283  0.0197  0.0323  415 ARG A NH1 
870   N NH2 . ARG A 114 ? 0.5240 0.3920 0.4797 0.0332  0.0198  0.0389  415 ARG A NH2 
871   N N   . ASN A 115 ? 0.4995 0.4667 0.5086 0.0158  0.0372  0.0427  416 ASN A N   
872   C CA  . ASN A 115 ? 0.4949 0.4756 0.5083 0.0189  0.0386  0.0407  416 ASN A CA  
873   C C   . ASN A 115 ? 0.4982 0.4872 0.5155 0.0139  0.0423  0.0427  416 ASN A C   
874   O O   . ASN A 115 ? 0.5852 0.5859 0.6057 0.0149  0.0443  0.0420  416 ASN A O   
875   C CB  . ASN A 115 ? 0.4338 0.4235 0.4503 0.0228  0.0373  0.0399  416 ASN A CB  
876   C CG  . ASN A 115 ? 0.4454 0.4277 0.4567 0.0308  0.0334  0.0375  416 ASN A CG  
877   O OD1 . ASN A 115 ? 0.4478 0.4182 0.4529 0.0337  0.0318  0.0358  416 ASN A OD1 
878   N ND2 . ASN A 115 ? 0.4487 0.4379 0.4618 0.0347  0.0314  0.0371  416 ASN A ND2 
879   N N   . ALA A 116 ? 0.4638 0.4473 0.4803 0.0088  0.0434  0.0454  417 ALA A N   
880   C CA  . ALA A 116 ? 0.4605 0.4486 0.4785 0.0051  0.0465  0.0477  417 ALA A CA  
881   C C   . ALA A 116 ? 0.4681 0.4588 0.4845 0.0064  0.0478  0.0470  417 ALA A C   
882   O O   . ALA A 116 ? 0.4020 0.3881 0.4160 0.0056  0.0474  0.0470  417 ALA A O   
883   C CB  . ALA A 116 ? 0.4280 0.4094 0.4446 0.0012  0.0468  0.0502  417 ALA A CB  
884   N N   . SER A 117 ? 0.4934 0.4935 0.5111 0.0083  0.0495  0.0461  418 SER A N   
885   C CA  A SER A 117 ? 0.4512 0.4545 0.4663 0.0107  0.0504  0.0448  418 SER A CA  
886   C CA  B SER A 117 ? 0.4489 0.4527 0.4641 0.0106  0.0506  0.0450  418 SER A CA  
887   C C   . SER A 117 ? 0.5105 0.5113 0.5228 0.0083  0.0519  0.0477  418 SER A C   
888   O O   . SER A 117 ? 0.5549 0.5565 0.5644 0.0104  0.0514  0.0462  418 SER A O   
889   C CB  A SER A 117 ? 0.3942 0.4099 0.4109 0.0129  0.0527  0.0440  418 SER A CB  
890   C CB  B SER A 117 ? 0.4049 0.4212 0.4219 0.0120  0.0533  0.0448  418 SER A CB  
891   O OG  A SER A 117 ? 0.4035 0.4242 0.4214 0.0083  0.0562  0.0480  418 SER A OG  
892   O OG  B SER A 117 ? 0.3781 0.4001 0.3972 0.0168  0.0517  0.0410  418 SER A OG  
893   N N   . ARG A 118 ? 0.4745 0.4721 0.4868 0.0047  0.0534  0.0514  419 ARG A N   
894   C CA  . ARG A 118 ? 0.3899 0.3845 0.3983 0.0042  0.0547  0.0541  419 ARG A CA  
895   C C   . ARG A 118 ? 0.4677 0.4570 0.4754 0.0042  0.0527  0.0536  419 ARG A C   
896   O O   . ARG A 118 ? 0.5126 0.5008 0.5170 0.0052  0.0533  0.0554  419 ARG A O   
897   C CB  . ARG A 118 ? 0.4036 0.3953 0.4103 0.0009  0.0574  0.0582  419 ARG A CB  
898   C CG  . ARG A 118 ? 0.3669 0.3655 0.3734 -0.0006 0.0605  0.0596  419 ARG A CG  
899   C CD  . ARG A 118 ? 0.3485 0.3417 0.3519 -0.0057 0.0633  0.0638  419 ARG A CD  
900   N NE  . ARG A 118 ? 0.5204 0.5211 0.5227 -0.0080 0.0668  0.0658  419 ARG A NE  
901   C CZ  . ARG A 118 ? 0.5816 0.5798 0.5815 -0.0145 0.0700  0.0694  419 ARG A CZ  
902   N NH1 . ARG A 118 ? 0.5645 0.5511 0.5624 -0.0186 0.0696  0.0708  419 ARG A NH1 
903   N NH2 . ARG A 118 ? 0.5756 0.5828 0.5746 -0.0172 0.0737  0.0713  419 ARG A NH2 
904   N N   . CYS A 119 ? 0.4670 0.4533 0.4771 0.0032  0.0504  0.0515  420 CYS A N   
905   C CA  . CYS A 119 ? 0.4150 0.3982 0.4247 0.0019  0.0492  0.0514  420 CYS A CA  
906   C C   . CYS A 119 ? 0.3749 0.3601 0.3843 0.0021  0.0473  0.0482  420 CYS A C   
907   O O   . CYS A 119 ? 0.3818 0.3646 0.3913 0.0022  0.0457  0.0455  420 CYS A O   
908   C CB  . CYS A 119 ? 0.4533 0.4313 0.4644 -0.0005 0.0483  0.0517  420 CYS A CB  
909   S SG  . CYS A 119 ? 0.4613 0.4373 0.4719 -0.0031 0.0473  0.0516  420 CYS A SG  
910   N N   . VAL A 120 ? 0.4462 0.4359 0.4549 0.0025  0.0473  0.0481  421 VAL A N   
911   C CA  . VAL A 120 ? 0.3732 0.3669 0.3821 0.0015  0.0453  0.0445  421 VAL A CA  
912   C C   . VAL A 120 ? 0.4907 0.4817 0.5011 -0.0035 0.0441  0.0435  421 VAL A C   
913   O O   . VAL A 120 ? 0.4067 0.3988 0.4171 -0.0065 0.0424  0.0401  421 VAL A O   
914   C CB  . VAL A 120 ? 0.5463 0.5490 0.5537 0.0047  0.0455  0.0446  421 VAL A CB  
915   C CG1 . VAL A 120 ? 0.2983 0.3041 0.3063 0.0050  0.0462  0.0466  421 VAL A CG1 
916   C CG2 . VAL A 120 ? 0.4984 0.5077 0.5057 0.0043  0.0432  0.0400  421 VAL A CG2 
917   N N   . GLY A 121 ? 0.5066 0.4936 0.5177 -0.0051 0.0452  0.0462  422 GLY A N   
918   C CA  . GLY A 121 ? 0.3233 0.3087 0.3349 -0.0101 0.0448  0.0460  422 GLY A CA  
919   C C   . GLY A 121 ? 0.4744 0.4486 0.4839 -0.0130 0.0435  0.0459  422 GLY A C   
920   O O   . GLY A 121 ? 0.5602 0.5309 0.5687 -0.0173 0.0437  0.0472  422 GLY A O   
921   N N   . ARG A 122 ? 0.4540 0.4226 0.4620 -0.0102 0.0423  0.0444  423 ARG A N   
922   C CA  . ARG A 122 ? 0.4525 0.4096 0.4572 -0.0102 0.0409  0.0446  423 ARG A CA  
923   C C   . ARG A 122 ? 0.4792 0.4264 0.4796 -0.0149 0.0390  0.0428  423 ARG A C   
924   O O   . ARG A 122 ? 0.4673 0.4023 0.4630 -0.0142 0.0376  0.0434  423 ARG A O   
925   C CB  . ARG A 122 ? 0.3933 0.3499 0.3977 -0.0044 0.0401  0.0431  423 ARG A CB  
926   C CG  . ARG A 122 ? 0.4459 0.4087 0.4534 -0.0015 0.0419  0.0454  423 ARG A CG  
927   C CD  . ARG A 122 ? 0.4618 0.4272 0.4697 0.0034  0.0415  0.0435  423 ARG A CD  
928   N NE  . ARG A 122 ? 0.4763 0.4495 0.4849 0.0050  0.0427  0.0421  423 ARG A NE  
929   C CZ  . ARG A 122 ? 0.5452 0.5225 0.5535 0.0093  0.0426  0.0397  423 ARG A CZ  
930   N NH1 . ARG A 122 ? 0.3138 0.2885 0.3214 0.0130  0.0411  0.0380  423 ARG A NH1 
931   N NH2 . ARG A 122 ? 0.4834 0.4682 0.4913 0.0107  0.0440  0.0389  423 ARG A NH2 
932   N N   . ILE A 123 ? 0.4341 0.3857 0.4354 -0.0197 0.0388  0.0406  424 ILE A N   
933   C CA  . ILE A 123 ? 0.4512 0.3920 0.4478 -0.0266 0.0374  0.0392  424 ILE A CA  
934   C C   . ILE A 123 ? 0.5176 0.4524 0.5117 -0.0313 0.0387  0.0436  424 ILE A C   
935   O O   . ILE A 123 ? 0.5649 0.4856 0.5526 -0.0363 0.0377  0.0441  424 ILE A O   
936   C CB  . ILE A 123 ? 0.4749 0.4249 0.4739 -0.0326 0.0370  0.0357  424 ILE A CB  
937   C CG1 . ILE A 123 ? 0.5061 0.4418 0.4990 -0.0406 0.0351  0.0334  424 ILE A CG1 
938   C CG2 . ILE A 123 ? 0.4979 0.4631 0.5024 -0.0363 0.0394  0.0378  424 ILE A CG2 
939   C CD1 . ILE A 123 ? 0.4914 0.4354 0.4864 -0.0473 0.0339  0.0284  424 ILE A CD1 
940   N N   . GLN A 124 ? 0.5842 0.5279 0.5820 -0.0294 0.0409  0.0468  425 GLN A N   
941   C CA  . GLN A 124 ? 0.6485 0.5890 0.6438 -0.0329 0.0424  0.0508  425 GLN A CA  
942   C C   . GLN A 124 ? 0.6783 0.6090 0.6696 -0.0276 0.0415  0.0534  425 GLN A C   
943   O O   . GLN A 124 ? 0.6241 0.5521 0.6124 -0.0295 0.0425  0.0568  425 GLN A O   
944   C CB  . GLN A 124 ? 0.6864 0.6431 0.6872 -0.0331 0.0450  0.0520  425 GLN A CB  
945   C CG  . GLN A 124 ? 0.6658 0.6363 0.6711 -0.0378 0.0458  0.0495  425 GLN A CG  
946   C CD  . GLN A 124 ? 0.6914 0.6627 0.6949 -0.0473 0.0473  0.0509  425 GLN A CD  
947   O OE1 . GLN A 124 ? 0.7119 0.6726 0.7100 -0.0498 0.0480  0.0543  425 GLN A OE1 
948   N NE2 . GLN A 124 ? 0.7252 0.7104 0.7331 -0.0528 0.0479  0.0483  425 GLN A NE2 
949   N N   . TRP A 125 ? 0.5890 0.5160 0.5802 -0.0209 0.0396  0.0516  426 TRP A N   
950   C CA  . TRP A 125 ? 0.4803 0.4047 0.4703 -0.0151 0.0388  0.0533  426 TRP A CA  
951   C C   . TRP A 125 ? 0.6288 0.5401 0.6108 -0.0160 0.0377  0.0564  426 TRP A C   
952   O O   . TRP A 125 ? 0.6883 0.6009 0.6696 -0.0129 0.0375  0.0585  426 TRP A O   
953   C CB  . TRP A 125 ? 0.4630 0.3869 0.4538 -0.0082 0.0369  0.0504  426 TRP A CB  
954   C CG  . TRP A 125 ? 0.5481 0.4571 0.5315 -0.0063 0.0341  0.0487  426 TRP A CG  
955   C CD1 . TRP A 125 ? 0.6247 0.5279 0.6056 -0.0083 0.0331  0.0453  426 TRP A CD1 
956   C CD2 . TRP A 125 ? 0.5458 0.4427 0.5221 -0.0012 0.0316  0.0497  426 TRP A CD2 
957   N NE1 . TRP A 125 ? 0.5640 0.4500 0.5359 -0.0049 0.0302  0.0442  426 TRP A NE1 
958   C CE2 . TRP A 125 ? 0.5416 0.4234 0.5103 0.0000  0.0292  0.0471  426 TRP A CE2 
959   C CE3 . TRP A 125 ? 0.5253 0.4226 0.5003 0.0030  0.0308  0.0523  426 TRP A CE3 
960   C CZ2 . TRP A 125 ? 0.5311 0.3969 0.4902 0.0063  0.0260  0.0474  426 TRP A CZ2 
961   C CZ3 . TRP A 125 ? 0.5229 0.4067 0.4891 0.0091  0.0276  0.0527  426 TRP A CZ3 
962   C CH2 . TRP A 125 ? 0.5824 0.4499 0.5404 0.0111  0.0253  0.0505  426 TRP A CH2 
963   N N   . SER A 126 ? 0.5684 0.4662 0.5434 -0.0203 0.0367  0.0568  427 SER A N   
964   C CA  . SER A 126 ? 0.5524 0.4350 0.5175 -0.0201 0.0356  0.0604  427 SER A CA  
965   C C   . SER A 126 ? 0.5556 0.4411 0.5190 -0.0268 0.0383  0.0647  427 SER A C   
966   O O   . SER A 126 ? 0.5767 0.4525 0.5321 -0.0259 0.0377  0.0685  427 SER A O   
967   C CB  . SER A 126 ? 0.4948 0.3571 0.4501 -0.0219 0.0333  0.0596  427 SER A CB  
968   O OG  . SER A 126 ? 0.5983 0.4586 0.5526 -0.0329 0.0352  0.0598  427 SER A OG  
969   N N   . LYS A 127 ? 0.6015 0.5011 0.5719 -0.0326 0.0413  0.0640  428 LYS A N   
970   C CA  . LYS A 127 ? 0.6246 0.5309 0.5943 -0.0381 0.0443  0.0674  428 LYS A CA  
971   C C   . LYS A 127 ? 0.7665 0.6873 0.7426 -0.0327 0.0453  0.0669  428 LYS A C   
972   O O   . LYS A 127 ? 0.9914 0.9264 0.9747 -0.0332 0.0472  0.0650  428 LYS A O   
973   C CB  . LYS A 127 ? 0.6242 0.5386 0.5972 -0.0476 0.0468  0.0664  428 LYS A CB  
974   C CG  . LYS A 127 ? 0.8108 0.7094 0.7763 -0.0556 0.0460  0.0669  428 LYS A CG  
975   C CD  . LYS A 127 ? 0.9994 0.9030 0.9631 -0.0673 0.0496  0.0697  428 LYS A CD  
976   C CE  . LYS A 127 ? 1.0704 0.9582 1.0218 -0.0700 0.0505  0.0760  428 LYS A CE  
977   N NZ  . LYS A 127 ? 1.0222 0.9247 0.9749 -0.0726 0.0544  0.0794  428 LYS A NZ  
978   N N   . LEU A 128 ? 0.6065 0.5228 0.5791 -0.0270 0.0438  0.0684  429 LEU A N   
979   C CA  . LEU A 128 ? 0.5822 0.5092 0.5597 -0.0221 0.0441  0.0674  429 LEU A CA  
980   C C   . LEU A 128 ? 0.5259 0.4499 0.4968 -0.0210 0.0439  0.0704  429 LEU A C   
981   O O   . LEU A 128 ? 0.6183 0.5313 0.5821 -0.0185 0.0416  0.0724  429 LEU A O   
982   C CB  . LEU A 128 ? 0.3861 0.3143 0.3681 -0.0158 0.0417  0.0645  429 LEU A CB  
983   C CG  . LEU A 128 ? 0.4115 0.3481 0.3973 -0.0122 0.0417  0.0633  429 LEU A CG  
984   C CD1 . LEU A 128 ? 0.4319 0.3782 0.4228 -0.0136 0.0442  0.0620  429 LEU A CD1 
985   C CD2 . LEU A 128 ? 0.3262 0.2639 0.3151 -0.0072 0.0393  0.0612  429 LEU A CD2 
986   N N   . GLN A 129 ? 0.4997 0.4334 0.4720 -0.0218 0.0461  0.0706  430 GLN A N   
987   C CA  . GLN A 129 ? 0.4872 0.4197 0.4527 -0.0206 0.0461  0.0731  430 GLN A CA  
988   C C   . GLN A 129 ? 0.4996 0.4350 0.4673 -0.0143 0.0435  0.0705  430 GLN A C   
989   O O   . GLN A 129 ? 0.5254 0.4688 0.4994 -0.0130 0.0441  0.0674  430 GLN A O   
990   C CB  . GLN A 129 ? 0.6226 0.5652 0.5879 -0.0242 0.0499  0.0738  430 GLN A CB  
991   C CG  . GLN A 129 ? 0.6736 0.6148 0.6299 -0.0242 0.0507  0.0771  430 GLN A CG  
992   C CD  . GLN A 129 ? 0.6854 0.6121 0.6318 -0.0268 0.0497  0.0819  430 GLN A CD  
993   O OE1 . GLN A 129 ? 0.8357 0.7546 0.7756 -0.0220 0.0467  0.0833  430 GLN A OE1 
994   N NE2 . GLN A 129 ? 0.4829 0.4056 0.4274 -0.0343 0.0520  0.0844  430 GLN A NE2 
995   N N   . VAL A 130 ? 0.5023 0.4309 0.4646 -0.0106 0.0404  0.0717  431 VAL A N   
996   C CA  . VAL A 130 ? 0.4924 0.4257 0.4573 -0.0055 0.0375  0.0689  431 VAL A CA  
997   C C   . VAL A 130 ? 0.5511 0.4873 0.5101 -0.0044 0.0372  0.0695  431 VAL A C   
998   O O   . VAL A 130 ? 0.5388 0.4691 0.4886 -0.0042 0.0370  0.0733  431 VAL A O   
999   C CB  . VAL A 130 ? 0.4568 0.3848 0.4203 -0.0006 0.0336  0.0687  431 VAL A CB  
1000  C CG1 . VAL A 130 ? 0.5055 0.4422 0.4728 0.0036  0.0307  0.0653  431 VAL A CG1 
1001  C CG2 . VAL A 130 ? 0.4708 0.3965 0.4396 -0.0009 0.0339  0.0673  431 VAL A CG2 
1002  N N   . PHE A 131 ? 0.6200 0.5640 0.5831 -0.0036 0.0371  0.0658  432 PHE A N   
1003  C CA  . PHE A 131 ? 0.5048 0.4522 0.4624 -0.0021 0.0365  0.0651  432 PHE A CA  
1004  C C   . PHE A 131 ? 0.5355 0.4862 0.4948 0.0013  0.0321  0.0617  432 PHE A C   
1005  O O   . PHE A 131 ? 0.5763 0.5315 0.5427 0.0003  0.0316  0.0577  432 PHE A O   
1006  C CB  . PHE A 131 ? 0.4014 0.3540 0.3608 -0.0038 0.0395  0.0627  432 PHE A CB  
1007  C CG  . PHE A 131 ? 0.4205 0.3743 0.3776 -0.0067 0.0437  0.0657  432 PHE A CG  
1008  C CD1 . PHE A 131 ? 0.5382 0.4906 0.4864 -0.0078 0.0449  0.0698  432 PHE A CD1 
1009  C CD2 . PHE A 131 ? 0.5129 0.4703 0.4761 -0.0086 0.0464  0.0647  432 PHE A CD2 
1010  C CE1 . PHE A 131 ? 0.3616 0.3173 0.3081 -0.0120 0.0491  0.0726  432 PHE A CE1 
1011  C CE2 . PHE A 131 ? 0.3438 0.3058 0.3059 -0.0119 0.0501  0.0670  432 PHE A CE2 
1012  C CZ  . PHE A 131 ? 0.4891 0.4509 0.4433 -0.0142 0.0517  0.0709  432 PHE A CZ  
1013  N N   . ASP A 132 ? 0.4856 0.4347 0.4380 0.0049  0.0290  0.0635  433 ASP A N   
1014  C CA  . ASP A 132 ? 0.4517 0.4070 0.4058 0.0087  0.0243  0.0601  433 ASP A CA  
1015  C C   . ASP A 132 ? 0.5402 0.5017 0.4925 0.0080  0.0234  0.0561  433 ASP A C   
1016  O O   . ASP A 132 ? 0.6193 0.5800 0.5624 0.0099  0.0230  0.0576  433 ASP A O   
1017  C CB  . ASP A 132 ? 0.5056 0.4565 0.4515 0.0144  0.0209  0.0635  433 ASP A CB  
1018  C CG  . ASP A 132 ? 0.5419 0.5024 0.4896 0.0194  0.0155  0.0597  433 ASP A CG  
1019  O OD1 . ASP A 132 ? 0.5117 0.4827 0.4677 0.0170  0.0145  0.0543  433 ASP A OD1 
1020  O OD2 . ASP A 132 ? 0.5723 0.5298 0.5126 0.0259  0.0121  0.0623  433 ASP A OD2 
1021  N N   . ALA A 133 ? 0.4873 0.4539 0.4474 0.0051  0.0231  0.0510  434 ALA A N   
1022  C CA  . ALA A 133 ? 0.4849 0.4552 0.4430 0.0039  0.0217  0.0461  434 ALA A CA  
1023  C C   . ALA A 133 ? 0.3884 0.3679 0.3507 0.0039  0.0168  0.0413  434 ALA A C   
1024  O O   . ALA A 133 ? 0.4366 0.4188 0.4010 0.0003  0.0158  0.0360  434 ALA A O   
1025  C CB  . ALA A 133 ? 0.4541 0.4208 0.4154 -0.0001 0.0251  0.0437  434 ALA A CB  
1026  N N   . ARG A 134 ? 0.3604 0.3447 0.3234 0.0081  0.0137  0.0429  435 ARG A N   
1027  C CA  . ARG A 134 ? 0.3707 0.3679 0.3394 0.0084  0.0091  0.0380  435 ARG A CA  
1028  C C   . ARG A 134 ? 0.5094 0.5128 0.4719 0.0098  0.0050  0.0341  435 ARG A C   
1029  O O   . ARG A 134 ? 0.5421 0.5581 0.5098 0.0085  0.0009  0.0288  435 ARG A O   
1030  C CB  . ARG A 134 ? 0.4338 0.4355 0.4046 0.0144  0.0067  0.0404  435 ARG A CB  
1031  C CG  . ARG A 134 ? 0.4479 0.4504 0.4287 0.0119  0.0093  0.0407  435 ARG A CG  
1032  C CD  . ARG A 134 ? 0.4103 0.4154 0.3913 0.0195  0.0070  0.0429  435 ARG A CD  
1033  N NE  . ARG A 134 ? 0.4642 0.4555 0.4332 0.0250  0.0070  0.0486  435 ARG A NE  
1034  C CZ  . ARG A 134 ? 0.5175 0.5057 0.4811 0.0333  0.0042  0.0512  435 ARG A CZ  
1035  N NH1 . ARG A 134 ? 0.5056 0.5061 0.4758 0.0384  0.0009  0.0480  435 ARG A NH1 
1036  N NH2 . ARG A 134 ? 0.5167 0.4895 0.4676 0.0368  0.0046  0.0570  435 ARG A NH2 
1037  N N   . ASP A 135 ? 0.5195 0.5160 0.4712 0.0119  0.0060  0.0362  436 ASP A N   
1038  C CA  . ASP A 135 ? 0.5558 0.5580 0.5004 0.0135  0.0021  0.0321  436 ASP A CA  
1039  C C   . ASP A 135 ? 0.6195 0.6193 0.5644 0.0076  0.0032  0.0261  436 ASP A C   
1040  O O   . ASP A 135 ? 0.6087 0.6125 0.5473 0.0083  0.0000  0.0215  436 ASP A O   
1041  C CB  . ASP A 135 ? 0.5560 0.5527 0.4869 0.0196  0.0026  0.0375  436 ASP A CB  
1042  C CG  . ASP A 135 ? 0.5901 0.5761 0.5162 0.0174  0.0087  0.0412  436 ASP A CG  
1043  O OD1 . ASP A 135 ? 0.5991 0.5809 0.5325 0.0126  0.0124  0.0403  436 ASP A OD1 
1044  O OD2 . ASP A 135 ? 0.6131 0.5961 0.5279 0.0206  0.0098  0.0451  436 ASP A OD2 
1045  N N   . CYS A 136 ? 0.6045 0.5971 0.5554 0.0023  0.0074  0.0259  437 CYS A N   
1046  C CA  . CYS A 136 ? 0.5615 0.5477 0.5107 -0.0023 0.0087  0.0207  437 CYS A CA  
1047  C C   . CYS A 136 ? 0.6009 0.5935 0.5545 -0.0081 0.0044  0.0131  437 CYS A C   
1048  O O   . CYS A 136 ? 0.4771 0.4792 0.4400 -0.0109 0.0025  0.0123  437 CYS A O   
1049  C CB  . CYS A 136 ? 0.4302 0.4066 0.3839 -0.0052 0.0139  0.0234  437 CYS A CB  
1050  S SG  . CYS A 136 ? 0.5098 0.4737 0.4579 -0.0076 0.0164  0.0189  437 CYS A SG  
1051  N N   . THR A 137 ? 0.4265 0.4148 0.3734 -0.0101 0.0029  0.0069  438 THR A N   
1052  C CA  . THR A 137 ? 0.4734 0.4663 0.4238 -0.0174 -0.0012 -0.0010 438 THR A CA  
1053  C C   . THR A 137 ? 0.4763 0.4540 0.4228 -0.0236 0.0002  -0.0062 438 THR A C   
1054  O O   . THR A 137 ? 0.5083 0.4873 0.4583 -0.0321 -0.0024 -0.0123 438 THR A O   
1055  C CB  . THR A 137 ? 0.5486 0.5539 0.4939 -0.0146 -0.0073 -0.0059 438 THR A CB  
1056  O OG1 . THR A 137 ? 0.4441 0.4411 0.3767 -0.0109 -0.0073 -0.0086 438 THR A OG1 
1057  C CG2 . THR A 137 ? 0.5427 0.5605 0.4888 -0.0067 -0.0092 -0.0004 438 THR A CG2 
1058  N N   . THR A 138 ? 0.4650 0.4287 0.4039 -0.0197 0.0041  -0.0044 439 THR A N   
1059  C CA  . THR A 138 ? 0.5195 0.4666 0.4522 -0.0235 0.0049  -0.0097 439 THR A CA  
1060  C C   . THR A 138 ? 0.4577 0.3918 0.3903 -0.0213 0.0106  -0.0046 439 THR A C   
1061  O O   . THR A 138 ? 0.5219 0.4605 0.4580 -0.0164 0.0139  0.0024  439 THR A O   
1062  C CB  . THR A 138 ? 0.5899 0.5327 0.5096 -0.0187 0.0027  -0.0156 439 THR A CB  
1063  O OG1 . THR A 138 ? 0.6116 0.5556 0.5259 -0.0092 0.0062  -0.0103 439 THR A OG1 
1064  C CG2 . THR A 138 ? 0.5238 0.4803 0.4425 -0.0201 -0.0035 -0.0211 439 THR A CG2 
1065  N N   . ALA A 139 ? 0.4754 0.3923 0.4030 -0.0250 0.0114  -0.0085 440 ALA A N   
1066  C CA  . ALA A 139 ? 0.5263 0.4304 0.4519 -0.0215 0.0162  -0.0043 440 ALA A CA  
1067  C C   . ALA A 139 ? 0.5790 0.4839 0.4977 -0.0109 0.0186  -0.0024 440 ALA A C   
1068  O O   . ALA A 139 ? 0.5131 0.4193 0.4348 -0.0066 0.0227  0.0035  440 ALA A O   
1069  C CB  . ALA A 139 ? 0.5626 0.4455 0.4813 -0.0266 0.0160  -0.0089 440 ALA A CB  
1070  N N   . HIS A 140 ? 0.6170 0.5230 0.5265 -0.0067 0.0163  -0.0076 441 HIS A N   
1071  C CA  . HIS A 140 ? 0.5551 0.4663 0.4582 0.0029  0.0188  -0.0057 441 HIS A CA  
1072  C C   . HIS A 140 ? 0.5875 0.5144 0.4981 0.0047  0.0211  0.0024  441 HIS A C   
1073  O O   . HIS A 140 ? 0.5686 0.4984 0.4792 0.0097  0.0253  0.0070  441 HIS A O   
1074  C CB  . HIS A 140 ? 0.5184 0.4311 0.4106 0.0064  0.0156  -0.0127 441 HIS A CB  
1075  C CG  . HIS A 140 ? 0.5785 0.4738 0.4593 0.0092  0.0148  -0.0203 441 HIS A CG  
1076  N ND1 . HIS A 140 ? 0.6401 0.5215 0.5170 0.0024  0.0108  -0.0276 441 HIS A ND1 
1077  C CD2 . HIS A 140 ? 0.4870 0.3758 0.3588 0.0183  0.0176  -0.0218 441 HIS A CD2 
1078  C CE1 . HIS A 140 ? 0.5125 0.3767 0.3772 0.0074  0.0109  -0.0333 441 HIS A CE1 
1079  N NE2 . HIS A 140 ? 0.6351 0.5042 0.4967 0.0180  0.0150  -0.0300 441 HIS A NE2 
1080  N N   . GLY A 141 ? 0.6238 0.5607 0.5401 0.0008  0.0182  0.0038  442 GLY A N   
1081  C CA  . GLY A 141 ? 0.6029 0.5507 0.5246 0.0025  0.0199  0.0114  442 GLY A CA  
1082  C C   . GLY A 141 ? 0.5341 0.4793 0.4642 0.0011  0.0238  0.0171  442 GLY A C   
1083  O O   . GLY A 141 ? 0.4825 0.4320 0.4135 0.0041  0.0272  0.0229  442 GLY A O   
1084  N N   . MET A 142 ? 0.5912 0.5296 0.5270 -0.0042 0.0234  0.0156  443 MET A N   
1085  C CA  . MET A 142 ? 0.4959 0.4321 0.4390 -0.0054 0.0269  0.0206  443 MET A CA  
1086  C C   . MET A 142 ? 0.5385 0.4697 0.4774 0.0000  0.0309  0.0222  443 MET A C   
1087  O O   . MET A 142 ? 0.4526 0.3884 0.3959 0.0016  0.0340  0.0275  443 MET A O   
1088  C CB  . MET A 142 ? 0.4841 0.4133 0.4319 -0.0122 0.0260  0.0184  443 MET A CB  
1089  C CG  . MET A 142 ? 0.4526 0.3902 0.4066 -0.0182 0.0223  0.0163  443 MET A CG  
1090  S SD  . MET A 142 ? 0.5472 0.4774 0.5061 -0.0282 0.0223  0.0139  443 MET A SD  
1091  C CE  . MET A 142 ? 0.4753 0.4079 0.4426 -0.0273 0.0266  0.0214  443 MET A CE  
1092  N N   . PHE A 143 ? 0.4674 0.3897 0.3975 0.0031  0.0307  0.0171  444 PHE A N   
1093  C CA  . PHE A 143 ? 0.5098 0.4299 0.4352 0.0100  0.0342  0.0178  444 PHE A CA  
1094  C C   . PHE A 143 ? 0.5851 0.5193 0.5106 0.0139  0.0368  0.0218  444 PHE A C   
1095  O O   . PHE A 143 ? 0.6449 0.5843 0.5740 0.0161  0.0403  0.0258  444 PHE A O   
1096  C CB  . PHE A 143 ? 0.5964 0.5046 0.5105 0.0139  0.0328  0.0107  444 PHE A CB  
1097  C CG  . PHE A 143 ? 0.5938 0.5024 0.5017 0.0232  0.0358  0.0100  444 PHE A CG  
1098  C CD1 . PHE A 143 ? 0.4886 0.3911 0.3974 0.0265  0.0381  0.0118  444 PHE A CD1 
1099  C CD2 . PHE A 143 ? 0.5742 0.4912 0.4750 0.0291  0.0364  0.0075  444 PHE A CD2 
1100  C CE1 . PHE A 143 ? 0.4535 0.3593 0.3571 0.0362  0.0406  0.0107  444 PHE A CE1 
1101  C CE2 . PHE A 143 ? 0.5023 0.4231 0.3980 0.0382  0.0394  0.0064  444 PHE A CE2 
1102  C CZ  . PHE A 143 ? 0.5806 0.4965 0.4780 0.0421  0.0414  0.0078  444 PHE A CZ  
1103  N N   . ASN A 144 ? 0.5588 0.4997 0.4799 0.0144  0.0351  0.0209  445 ASN A N   
1104  C CA  . ASN A 144 ? 0.5123 0.4654 0.4323 0.0166  0.0378  0.0256  445 ASN A CA  
1105  C C   . ASN A 144 ? 0.5137 0.4712 0.4427 0.0127  0.0396  0.0327  445 ASN A C   
1106  O O   . ASN A 144 ? 0.5226 0.4863 0.4534 0.0136  0.0434  0.0366  445 ASN A O   
1107  C CB  . ASN A 144 ? 0.5158 0.4737 0.4290 0.0171  0.0351  0.0243  445 ASN A CB  
1108  C CG  . ASN A 144 ? 0.5480 0.5166 0.4569 0.0193  0.0383  0.0294  445 ASN A CG  
1109  O OD1 . ASN A 144 ? 0.6013 0.5736 0.5098 0.0172  0.0373  0.0340  445 ASN A OD1 
1110  N ND2 . ASN A 144 ? 0.4876 0.4613 0.3926 0.0235  0.0422  0.0288  445 ASN A ND2 
1111  N N   . TYR A 145 ? 0.4924 0.4475 0.4270 0.0083  0.0367  0.0338  446 TYR A N   
1112  C CA  . TYR A 145 ? 0.5764 0.5338 0.5186 0.0054  0.0378  0.0395  446 TYR A CA  
1113  C C   . TYR A 145 ? 0.4785 0.4342 0.4264 0.0052  0.0410  0.0409  446 TYR A C   
1114  O O   . TYR A 145 ? 0.4641 0.4240 0.4155 0.0041  0.0435  0.0455  446 TYR A O   
1115  C CB  . TYR A 145 ? 0.5140 0.4701 0.4614 0.0021  0.0340  0.0389  446 TYR A CB  
1116  C CG  . TYR A 145 ? 0.6326 0.5933 0.5769 0.0029  0.0313  0.0411  446 TYR A CG  
1117  C CD1 . TYR A 145 ? 0.5755 0.5377 0.5186 0.0035  0.0331  0.0472  446 TYR A CD1 
1118  C CD2 . TYR A 145 ? 0.3724 0.3356 0.3142 0.0031  0.0268  0.0370  446 TYR A CD2 
1119  C CE1 . TYR A 145 ? 0.4504 0.4142 0.3886 0.0053  0.0305  0.0499  446 TYR A CE1 
1120  C CE2 . TYR A 145 ? 0.3759 0.3437 0.3140 0.0054  0.0239  0.0392  446 TYR A CE2 
1121  C CZ  . TYR A 145 ? 0.4159 0.3830 0.3515 0.0069  0.0259  0.0460  446 TYR A CZ  
1122  O OH  . TYR A 145 ? 0.4866 0.4553 0.4164 0.0101  0.0231  0.0491  446 TYR A OH  
1123  N N   . ILE A 146 ? 0.4454 0.3942 0.3930 0.0062  0.0408  0.0371  447 ILE A N   
1124  C CA  . ILE A 146 ? 0.4604 0.4075 0.4123 0.0069  0.0434  0.0386  447 ILE A CA  
1125  C C   . ILE A 146 ? 0.4775 0.4314 0.4265 0.0119  0.0467  0.0390  447 ILE A C   
1126  O O   . ILE A 146 ? 0.4355 0.3947 0.3894 0.0119  0.0491  0.0419  447 ILE A O   
1127  C CB  . ILE A 146 ? 0.4646 0.3999 0.4157 0.0062  0.0420  0.0352  447 ILE A CB  
1128  C CG1 . ILE A 146 ? 0.4364 0.3700 0.3937 0.0000  0.0398  0.0360  447 ILE A CG1 
1129  C CG2 . ILE A 146 ? 0.4377 0.3698 0.3893 0.0097  0.0445  0.0361  447 ILE A CG2 
1130  C CD1 . ILE A 146 ? 0.4474 0.3698 0.4029 -0.0034 0.0382  0.0325  447 ILE A CD1 
1131  N N   . CYS A 147 ? 0.5231 0.4788 0.4643 0.0162  0.0469  0.0357  448 CYS A N   
1132  C CA  . CYS A 147 ? 0.4260 0.3923 0.3650 0.0211  0.0505  0.0360  448 CYS A CA  
1133  C C   . CYS A 147 ? 0.4245 0.4030 0.3676 0.0170  0.0531  0.0415  448 CYS A C   
1134  O O   . CYS A 147 ? 0.4792 0.4678 0.4259 0.0176  0.0563  0.0433  448 CYS A O   
1135  C CB  . CYS A 147 ? 0.5062 0.4734 0.4352 0.0267  0.0502  0.0312  448 CYS A CB  
1136  S SG  . CYS A 147 ? 0.5493 0.5014 0.4709 0.0333  0.0481  0.0241  448 CYS A SG  
1137  N N   . ASN A 148 ? 0.5220 0.4997 0.4640 0.0127  0.0517  0.0442  449 ASN A N   
1138  C CA  . ASN A 148 ? 0.3598 0.3446 0.3035 0.0081  0.0540  0.0500  449 ASN A CA  
1139  C C   . ASN A 148 ? 0.4060 0.3891 0.3584 0.0040  0.0543  0.0530  449 ASN A C   
1140  O O   . ASN A 148 ? 0.4691 0.4598 0.4244 0.0009  0.0572  0.0561  449 ASN A O   
1141  C CB  . ASN A 148 ? 0.3997 0.3812 0.3378 0.0061  0.0518  0.0523  449 ASN A CB  
1142  C CG  . ASN A 148 ? 0.5253 0.5109 0.4536 0.0101  0.0519  0.0497  449 ASN A CG  
1143  O OD1 . ASN A 148 ? 0.5045 0.4974 0.4298 0.0141  0.0546  0.0470  449 ASN A OD1 
1144  N ND2 . ASN A 148 ? 0.4179 0.3995 0.3407 0.0099  0.0486  0.0501  449 ASN A ND2 
1145  N N   . HIS A 149 ? 0.4702 0.4442 0.4267 0.0035  0.0514  0.0516  450 HIS A N   
1146  C CA  . HIS A 149 ? 0.4188 0.3917 0.3829 0.0008  0.0517  0.0536  450 HIS A CA  
1147  C C   . HIS A 149 ? 0.3431 0.3237 0.3101 0.0029  0.0545  0.0528  450 HIS A C   
1148  O O   . HIS A 149 ? 0.4025 0.3902 0.3734 -0.0003 0.0565  0.0554  450 HIS A O   
1149  C CB  . HIS A 149 ? 0.4900 0.4540 0.4573 0.0006  0.0487  0.0516  450 HIS A CB  
1150  C CG  . HIS A 149 ? 0.5465 0.5093 0.5207 -0.0018 0.0488  0.0535  450 HIS A CG  
1151  N ND1 . HIS A 149 ? 0.4670 0.4257 0.4445 -0.0041 0.0465  0.0543  450 HIS A ND1 
1152  C CD2 . HIS A 149 ? 0.4899 0.4565 0.4681 -0.0015 0.0507  0.0542  450 HIS A CD2 
1153  C CE1 . HIS A 149 ? 0.5098 0.4688 0.4924 -0.0052 0.0473  0.0554  450 HIS A CE1 
1154  N NE2 . HIS A 149 ? 0.5031 0.4667 0.4863 -0.0039 0.0496  0.0554  450 HIS A NE2 
1155  N N   . VAL A 150 ? 0.3966 0.3762 0.3609 0.0086  0.0546  0.0490  451 VAL A N   
1156  C CA  . VAL A 150 ? 0.4279 0.4147 0.3944 0.0128  0.0565  0.0478  451 VAL A CA  
1157  C C   . VAL A 150 ? 0.4916 0.4950 0.4591 0.0120  0.0599  0.0492  451 VAL A C   
1158  O O   . VAL A 150 ? 0.5097 0.5231 0.4829 0.0109  0.0615  0.0501  451 VAL A O   
1159  C CB  . VAL A 150 ? 0.4336 0.4135 0.3940 0.0205  0.0556  0.0433  451 VAL A CB  
1160  C CG1 . VAL A 150 ? 0.3490 0.3391 0.3097 0.0272  0.0577  0.0418  451 VAL A CG1 
1161  C CG2 . VAL A 150 ? 0.3768 0.3406 0.3369 0.0194  0.0529  0.0426  451 VAL A CG2 
1162  N N   . LYS A 151 ? 0.5579 0.5660 0.5201 0.0120  0.0612  0.0492  452 LYS A N   
1163  C CA  . LYS A 151 ? 0.5183 0.5440 0.4810 0.0105  0.0651  0.0506  452 LYS A CA  
1164  C C   . LYS A 151 ? 0.4313 0.4600 0.3987 0.0009  0.0663  0.0556  452 LYS A C   
1165  O O   . LYS A 151 ? 0.5064 0.5495 0.4783 -0.0023 0.0692  0.0565  452 LYS A O   
1166  C CB  . LYS A 151 ? 0.4424 0.4715 0.3966 0.0127  0.0663  0.0497  452 LYS A CB  
1167  C CG  . LYS A 151 ? 0.4420 0.4907 0.3957 0.0102  0.0710  0.0516  452 LYS A CG  
1168  C CD  . LYS A 151 ? 0.4973 0.5505 0.4418 0.0162  0.0721  0.0488  452 LYS A CD  
1169  C CE  . LYS A 151 ? 0.5579 0.6335 0.5011 0.0148  0.0775  0.0502  452 LYS A CE  
1170  N NZ  . LYS A 151 ? 0.5455 0.6245 0.4787 0.0218  0.0781  0.0469  452 LYS A NZ  
1171  N N   . TYR A 152 ? 0.4396 0.4547 0.4053 -0.0037 0.0641  0.0585  453 TYR A N   
1172  C CA  . TYR A 152 ? 0.4838 0.4969 0.4519 -0.0121 0.0647  0.0630  453 TYR A CA  
1173  C C   . TYR A 152 ? 0.4350 0.4500 0.4114 -0.0137 0.0642  0.0621  453 TYR A C   
1174  O O   . TYR A 152 ? 0.3975 0.4220 0.3776 -0.0194 0.0664  0.0635  453 TYR A O   
1175  C CB  . TYR A 152 ? 0.5088 0.5061 0.4727 -0.0140 0.0615  0.0655  453 TYR A CB  
1176  C CG  . TYR A 152 ? 0.5360 0.5271 0.5012 -0.0211 0.0614  0.0695  453 TYR A CG  
1177  C CD1 . TYR A 152 ? 0.5977 0.5895 0.5575 -0.0276 0.0639  0.0740  453 TYR A CD1 
1178  C CD2 . TYR A 152 ? 0.5320 0.5158 0.5027 -0.0215 0.0589  0.0686  453 TYR A CD2 
1179  C CE1 . TYR A 152 ? 0.5853 0.5684 0.5444 -0.0343 0.0637  0.0774  453 TYR A CE1 
1180  C CE2 . TYR A 152 ? 0.5286 0.5054 0.4992 -0.0273 0.0586  0.0714  453 TYR A CE2 
1181  C CZ  . TYR A 152 ? 0.5390 0.5143 0.5035 -0.0338 0.0608  0.0757  453 TYR A CZ  
1182  O OH  . TYR A 152 ? 0.6203 0.5853 0.5828 -0.0401 0.0604  0.0785  453 TYR A OH  
1183  N N   . ALA A 153 ? 0.4589 0.4653 0.4378 -0.0093 0.0613  0.0597  454 ALA A N   
1184  C CA  . ALA A 153 ? 0.4955 0.5026 0.4810 -0.0098 0.0605  0.0589  454 ALA A CA  
1185  C C   . ALA A 153 ? 0.4821 0.5060 0.4715 -0.0079 0.0628  0.0570  454 ALA A C   
1186  O O   . ALA A 153 ? 0.4553 0.4863 0.4499 -0.0124 0.0634  0.0574  454 ALA A O   
1187  C CB  . ALA A 153 ? 0.3192 0.3153 0.3050 -0.0049 0.0577  0.0569  454 ALA A CB  
1188  N N   . THR A 154 ? 0.5297 0.5610 0.5165 -0.0008 0.0639  0.0543  455 THR A N   
1189  C CA  . THR A 154 ? 0.4342 0.4831 0.4245 0.0036  0.0656  0.0518  455 THR A CA  
1190  C C   . THR A 154 ? 0.5292 0.5968 0.5234 -0.0037 0.0689  0.0532  455 THR A C   
1191  O O   . THR A 154 ? 0.5692 0.6504 0.5698 -0.0058 0.0695  0.0522  455 THR A O   
1192  C CB  . THR A 154 ? 0.4311 0.4817 0.4159 0.0142  0.0658  0.0483  455 THR A CB  
1193  O OG1 . THR A 154 ? 0.4953 0.5274 0.4764 0.0193  0.0628  0.0471  455 THR A OG1 
1194  C CG2 . THR A 154 ? 0.3277 0.3984 0.3156 0.0207  0.0674  0.0454  455 THR A CG2 
1195  N N   . ASN A 155 ? 0.5336 0.6030 0.5234 -0.0082 0.0712  0.0555  456 ASN A N   
1196  C CA  . ASN A 155 ? 0.4094 0.4931 0.4013 -0.0182 0.0749  0.0581  456 ASN A CA  
1197  C C   . ASN A 155 ? 0.4884 0.5988 0.4872 -0.0166 0.0773  0.0549  456 ASN A C   
1198  O O   . ASN A 155 ? 0.3788 0.5015 0.3835 -0.0258 0.0788  0.0558  456 ASN A O   
1199  C CB  . ASN A 155 ? 0.3493 0.4205 0.3425 -0.0288 0.0737  0.0616  456 ASN A CB  
1200  C CG  . ASN A 155 ? 0.4580 0.5380 0.4508 -0.0409 0.0773  0.0651  456 ASN A CG  
1201  O OD1 . ASN A 155 ? 0.5614 0.6481 0.5493 -0.0430 0.0806  0.0672  456 ASN A OD1 
1202  N ND2 . ASN A 155 ? 0.4414 0.5211 0.4388 -0.0495 0.0768  0.0656  456 ASN A ND2 
1203  N N   . LYS A 156 ? 0.5527 0.6724 0.5505 -0.0046 0.0773  0.0509  457 LYS A N   
1204  C CA  . LYS A 156 ? 0.5142 0.6620 0.5176 0.0003  0.0794  0.0471  457 LYS A CA  
1205  C C   . LYS A 156 ? 0.4443 0.5999 0.4560 -0.0004 0.0774  0.0454  457 LYS A C   
1206  O O   . LYS A 156 ? 0.3386 0.5207 0.3573 -0.0018 0.0793  0.0432  457 LYS A O   
1207  C CB  . LYS A 156 ? 0.5164 0.6869 0.5213 -0.0080 0.0846  0.0486  457 LYS A CB  
1208  C CG  . LYS A 156 ? 0.5607 0.7282 0.5566 -0.0044 0.0868  0.0494  457 LYS A CG  
1209  C CD  . LYS A 156 ? 0.7096 0.9059 0.7068 -0.0084 0.0924  0.0495  457 LYS A CD  
1210  C CE  . LYS A 156 ? 0.8593 1.0476 0.8500 -0.0205 0.0955  0.0557  457 LYS A CE  
1211  N NZ  . LYS A 156 ? 0.9394 1.1502 0.9262 -0.0197 0.1009  0.0556  457 LYS A NZ  
1212  N N   . GLY A 157 ? 0.4766 0.6109 0.4875 0.0009  0.0735  0.0461  458 GLY A N   
1213  C CA  . GLY A 157 ? 0.4442 0.5828 0.4613 0.0011  0.0712  0.0445  458 GLY A CA  
1214  C C   . GLY A 157 ? 0.5232 0.6532 0.5436 -0.0119 0.0703  0.0471  458 GLY A C   
1215  O O   . GLY A 157 ? 0.5260 0.6533 0.5498 -0.0115 0.0677  0.0459  458 GLY A O   
1216  N N   . ASN A 158 ? 0.4460 0.5705 0.4644 -0.0228 0.0725  0.0505  459 ASN A N   
1217  C CA  . ASN A 158 ? 0.5001 0.6136 0.5197 -0.0348 0.0715  0.0528  459 ASN A CA  
1218  C C   . ASN A 158 ? 0.5079 0.5926 0.5211 -0.0331 0.0689  0.0554  459 ASN A C   
1219  O O   . ASN A 158 ? 0.5442 0.6162 0.5517 -0.0380 0.0697  0.0590  459 ASN A O   
1220  C CB  . ASN A 158 ? 0.4851 0.6075 0.5046 -0.0479 0.0753  0.0555  459 ASN A CB  
1221  C CG  . ASN A 158 ? 0.5175 0.6243 0.5358 -0.0601 0.0742  0.0578  459 ASN A CG  
1222  O OD1 . ASN A 158 ? 0.5179 0.6141 0.5379 -0.0591 0.0707  0.0562  459 ASN A OD1 
1223  N ND2 . ASN A 158 ? 0.4646 0.5686 0.4785 -0.0714 0.0772  0.0618  459 ASN A ND2 
1224  N N   . LEU A 159 ? 0.4416 0.5175 0.4558 -0.0259 0.0657  0.0537  460 LEU A N   
1225  C CA  . LEU A 159 ? 0.4936 0.5474 0.5027 -0.0215 0.0634  0.0551  460 LEU A CA  
1226  C C   . LEU A 159 ? 0.4395 0.4764 0.4459 -0.0293 0.0623  0.0580  460 LEU A C   
1227  O O   . LEU A 159 ? 0.4437 0.4807 0.4523 -0.0369 0.0620  0.0581  460 LEU A O   
1228  C CB  . LEU A 159 ? 0.4482 0.4976 0.4586 -0.0134 0.0609  0.0530  460 LEU A CB  
1229  C CG  . LEU A 159 ? 0.5721 0.6346 0.5828 -0.0036 0.0615  0.0503  460 LEU A CG  
1230  C CD1 . LEU A 159 ? 0.6566 0.7107 0.6658 0.0046  0.0591  0.0493  460 LEU A CD1 
1231  C CD2 . LEU A 159 ? 0.5117 0.5733 0.5171 0.0005  0.0631  0.0504  460 LEU A CD2 
1232  N N   . ARG A 160 ? 0.4197 0.4418 0.4207 -0.0268 0.0613  0.0599  461 ARG A N   
1233  C CA  . ARG A 160 ? 0.4426 0.4481 0.4394 -0.0314 0.0598  0.0627  461 ARG A CA  
1234  C C   . ARG A 160 ? 0.4322 0.4255 0.4278 -0.0250 0.0570  0.0620  461 ARG A C   
1235  O O   . ARG A 160 ? 0.4827 0.4768 0.4770 -0.0191 0.0570  0.0610  461 ARG A O   
1236  C CB  . ARG A 160 ? 0.4313 0.4341 0.4215 -0.0355 0.0617  0.0662  461 ARG A CB  
1237  C CG  . ARG A 160 ? 0.4398 0.4547 0.4304 -0.0439 0.0651  0.0676  461 ARG A CG  
1238  C CD  . ARG A 160 ? 0.5180 0.5271 0.5001 -0.0479 0.0670  0.0720  461 ARG A CD  
1239  N NE  . ARG A 160 ? 0.4594 0.4768 0.4392 -0.0414 0.0684  0.0713  461 ARG A NE  
1240  C CZ  . ARG A 160 ? 0.4857 0.5072 0.4592 -0.0443 0.0714  0.0743  461 ARG A CZ  
1241  N NH1 . ARG A 160 ? 0.4401 0.4565 0.4086 -0.0541 0.0733  0.0789  461 ARG A NH1 
1242  N NH2 . ARG A 160 ? 0.3731 0.4025 0.3442 -0.0374 0.0724  0.0727  461 ARG A NH2 
1243  N N   . SER A 161 ? 0.4237 0.4064 0.4195 -0.0262 0.0548  0.0623  462 SER A N   
1244  C CA  . SER A 161 ? 0.4945 0.4694 0.4905 -0.0207 0.0525  0.0613  462 SER A CA  
1245  C C   . SER A 161 ? 0.4433 0.4093 0.4340 -0.0198 0.0513  0.0632  462 SER A C   
1246  O O   . SER A 161 ? 0.5305 0.4916 0.5164 -0.0233 0.0514  0.0657  462 SER A O   
1247  C CB  . SER A 161 ? 0.4465 0.4169 0.4453 -0.0211 0.0507  0.0601  462 SER A CB  
1248  O OG  . SER A 161 ? 0.5711 0.5310 0.5663 -0.0241 0.0493  0.0615  462 SER A OG  
1249  N N   . ALA A 162 ? 0.4591 0.4232 0.4501 -0.0152 0.0500  0.0618  463 ALA A N   
1250  C CA  . ALA A 162 ? 0.4994 0.4587 0.4858 -0.0138 0.0487  0.0627  463 ALA A CA  
1251  C C   . ALA A 162 ? 0.4912 0.4485 0.4796 -0.0105 0.0467  0.0605  463 ALA A C   
1252  O O   . ALA A 162 ? 0.3712 0.3305 0.3632 -0.0092 0.0473  0.0587  463 ALA A O   
1253  C CB  . ALA A 162 ? 0.3962 0.3604 0.3783 -0.0138 0.0506  0.0632  463 ALA A CB  
1254  N N   . ILE A 163 ? 0.5244 0.4781 0.5100 -0.0094 0.0444  0.0607  464 ILE A N   
1255  C CA  . ILE A 163 ? 0.4805 0.4345 0.4683 -0.0076 0.0424  0.0583  464 ILE A CA  
1256  C C   . ILE A 163 ? 0.5052 0.4590 0.4879 -0.0064 0.0406  0.0579  464 ILE A C   
1257  O O   . ILE A 163 ? 0.5528 0.5044 0.5303 -0.0060 0.0399  0.0603  464 ILE A O   
1258  C CB  . ILE A 163 ? 0.3395 0.2931 0.3315 -0.0069 0.0406  0.0579  464 ILE A CB  
1259  C CG1 . ILE A 163 ? 0.3976 0.3546 0.3932 -0.0068 0.0393  0.0552  464 ILE A CG1 
1260  C CG2 . ILE A 163 ? 0.4075 0.3572 0.3957 -0.0053 0.0384  0.0597  464 ILE A CG2 
1261  C CD1 . ILE A 163 ? 0.4185 0.3788 0.4189 -0.0057 0.0381  0.0544  464 ILE A CD1 
1262  N N   . THR A 164 ? 0.5022 0.4572 0.4853 -0.0062 0.0397  0.0548  465 THR A N   
1263  C CA  . THR A 164 ? 0.5030 0.4590 0.4818 -0.0051 0.0373  0.0532  465 THR A CA  
1264  C C   . THR A 164 ? 0.4076 0.3665 0.3907 -0.0059 0.0344  0.0503  465 THR A C   
1265  O O   . THR A 164 ? 0.3745 0.3331 0.3612 -0.0083 0.0351  0.0480  465 THR A O   
1266  C CB  . THR A 164 ? 0.4960 0.4512 0.4702 -0.0047 0.0385  0.0509  465 THR A CB  
1267  O OG1 . THR A 164 ? 0.4013 0.3576 0.3719 -0.0039 0.0413  0.0535  465 THR A OG1 
1268  C CG2 . THR A 164 ? 0.4461 0.4026 0.4158 -0.0038 0.0354  0.0483  465 THR A CG2 
1269  N N   . ILE A 165 ? 0.3857 0.3480 0.3679 -0.0038 0.0312  0.0504  466 ILE A N   
1270  C CA  . ILE A 165 ? 0.4839 0.4532 0.4717 -0.0042 0.0284  0.0476  466 ILE A CA  
1271  C C   . ILE A 165 ? 0.5463 0.5203 0.5315 -0.0046 0.0252  0.0439  466 ILE A C   
1272  O O   . ILE A 165 ? 0.4990 0.4737 0.4779 -0.0010 0.0229  0.0447  466 ILE A O   
1273  C CB  . ILE A 165 ? 0.4760 0.4476 0.4649 -0.0001 0.0265  0.0496  466 ILE A CB  
1274  C CG1 . ILE A 165 ? 0.4637 0.4303 0.4550 -0.0004 0.0294  0.0522  466 ILE A CG1 
1275  C CG2 . ILE A 165 ? 0.4572 0.4400 0.4521 0.0006  0.0234  0.0462  466 ILE A CG2 
1276  C CD1 . ILE A 165 ? 0.4951 0.4599 0.4851 0.0043  0.0275  0.0539  466 ILE A CD1 
1277  N N   . PHE A 166 ? 0.5378 0.5145 0.5270 -0.0093 0.0249  0.0399  467 PHE A N   
1278  C CA  . PHE A 166 ? 0.4347 0.4157 0.4220 -0.0113 0.0217  0.0352  467 PHE A CA  
1279  C C   . PHE A 166 ? 0.4221 0.4170 0.4156 -0.0115 0.0179  0.0326  467 PHE A C   
1280  O O   . PHE A 166 ? 0.4991 0.4995 0.4980 -0.0093 0.0181  0.0345  467 PHE A O   
1281  C CB  . PHE A 166 ? 0.4436 0.4173 0.4303 -0.0171 0.0235  0.0321  467 PHE A CB  
1282  C CG  . PHE A 166 ? 0.4627 0.4257 0.4416 -0.0147 0.0260  0.0331  467 PHE A CG  
1283  C CD1 . PHE A 166 ? 0.3694 0.3320 0.3403 -0.0116 0.0243  0.0315  467 PHE A CD1 
1284  C CD2 . PHE A 166 ? 0.4313 0.3862 0.4103 -0.0149 0.0299  0.0354  467 PHE A CD2 
1285  C CE1 . PHE A 166 ? 0.3799 0.3353 0.3439 -0.0088 0.0268  0.0320  467 PHE A CE1 
1286  C CE2 . PHE A 166 ? 0.5034 0.4514 0.4757 -0.0117 0.0320  0.0358  467 PHE A CE2 
1287  C CZ  . PHE A 166 ? 0.4709 0.4196 0.4359 -0.0086 0.0306  0.0340  467 PHE A CZ  
1288  N N   . PRO A 167 ? 0.4388 0.4411 0.4314 -0.0132 0.0141  0.0278  468 PRO A N   
1289  C CA  . PRO A 167 ? 0.4692 0.4886 0.4681 -0.0120 0.0099  0.0251  468 PRO A CA  
1290  C C   . PRO A 167 ? 0.4234 0.4517 0.4330 -0.0173 0.0115  0.0239  468 PRO A C   
1291  O O   . PRO A 167 ? 0.4950 0.5178 0.5070 -0.0253 0.0144  0.0227  468 PRO A O   
1292  C CB  . PRO A 167 ? 0.4575 0.4828 0.4534 -0.0149 0.0058  0.0192  468 PRO A CB  
1293  C CG  . PRO A 167 ? 0.4412 0.4521 0.4261 -0.0128 0.0071  0.0204  468 PRO A CG  
1294  C CD  . PRO A 167 ? 0.4647 0.4617 0.4496 -0.0144 0.0127  0.0245  468 PRO A CD  
1295  N N   . GLN A 168 ? 0.4226 0.4644 0.4378 -0.0123 0.0095  0.0243  469 GLN A N   
1296  C CA  . GLN A 168 ? 0.4257 0.4791 0.4512 -0.0159 0.0113  0.0234  469 GLN A CA  
1297  C C   . GLN A 168 ? 0.5329 0.5999 0.5652 -0.0259 0.0101  0.0176  469 GLN A C   
1298  O O   . GLN A 168 ? 0.5982 0.6700 0.6284 -0.0281 0.0064  0.0133  469 GLN A O   
1299  C CB  . GLN A 168 ? 0.4616 0.5279 0.4903 -0.0064 0.0088  0.0241  469 GLN A CB  
1300  C CG  . GLN A 168 ? 0.5315 0.6159 0.5616 -0.0024 0.0028  0.0197  469 GLN A CG  
1301  C CD  . GLN A 168 ? 0.5144 0.6022 0.5406 0.0111  -0.0007 0.0218  469 GLN A CD  
1302  O OE1 . GLN A 168 ? 0.5670 0.6370 0.5838 0.0172  0.0001  0.0268  469 GLN A OE1 
1303  N NE2 . GLN A 168 ? 0.5190 0.6297 0.5519 0.0159  -0.0047 0.0178  469 GLN A NE2 
1304  N N   . ARG A 169 ? 0.5370 0.6110 0.5773 -0.0325 0.0134  0.0174  470 ARG A N   
1305  C CA  . ARG A 169 ? 0.4524 0.5407 0.5001 -0.0439 0.0130  0.0124  470 ARG A CA  
1306  C C   . ARG A 169 ? 0.4179 0.5326 0.4722 -0.0405 0.0074  0.0073  470 ARG A C   
1307  O O   . ARG A 169 ? 0.5045 0.6283 0.5594 -0.0286 0.0050  0.0085  470 ARG A O   
1308  C CB  . ARG A 169 ? 0.5194 0.6112 0.5738 -0.0504 0.0183  0.0145  470 ARG A CB  
1309  C CG  . ARG A 169 ? 0.5603 0.6687 0.6231 -0.0636 0.0190  0.0102  470 ARG A CG  
1310  C CD  . ARG A 169 ? 0.5896 0.6955 0.6554 -0.0705 0.0252  0.0138  470 ARG A CD  
1311  N NE  . ARG A 169 ? 0.5973 0.6763 0.6541 -0.0779 0.0287  0.0166  470 ARG A NE  
1312  C CZ  . ARG A 169 ? 0.7407 0.8058 0.7940 -0.0779 0.0337  0.0219  470 ARG A CZ  
1313  N NH1 . ARG A 169 ? 0.8210 0.8970 0.8793 -0.0716 0.0359  0.0247  470 ARG A NH1 
1314  N NH2 . ARG A 169 ? 0.7059 0.7463 0.7498 -0.0832 0.0363  0.0242  470 ARG A NH2 
1315  N N   . THR A 170 ? 0.3983 0.5243 0.4563 -0.0505 0.0051  0.0014  471 THR A N   
1316  C CA  . THR A 170 ? 0.3480 0.5032 0.4137 -0.0485 -0.0005 -0.0044 471 THR A CA  
1317  C C   . THR A 170 ? 0.3723 0.5498 0.4505 -0.0615 0.0013  -0.0085 471 THR A C   
1318  O O   . THR A 170 ? 0.5034 0.6995 0.5904 -0.0585 0.0030  -0.0077 471 THR A O   
1319  C CB  . THR A 170 ? 0.5015 0.6563 0.5609 -0.0483 -0.0063 -0.0092 471 THR A CB  
1320  O OG1 . THR A 170 ? 0.5774 0.7226 0.6350 -0.0631 -0.0054 -0.0131 471 THR A OG1 
1321  C CG2 . THR A 170 ? 0.4847 0.6182 0.5310 -0.0366 -0.0073 -0.0047 471 THR A CG2 
1322  N N   . ASP A 171 ? 0.4867 0.6627 0.5653 -0.0763 0.0010  -0.0130 472 ASP A N   
1323  C CA  . ASP A 171 ? 0.5416 0.7373 0.6313 -0.0916 0.0033  -0.0167 472 ASP A CA  
1324  C C   . ASP A 171 ? 0.7260 0.8990 0.8119 -0.1042 0.0102  -0.0125 472 ASP A C   
1325  O O   . ASP A 171 ? 0.8530 1.0373 0.9458 -0.1194 0.0129  -0.0147 472 ASP A O   
1326  C CB  . ASP A 171 ? 0.6502 0.8625 0.7435 -0.1016 -0.0021 -0.0254 472 ASP A CB  
1327  C CG  . ASP A 171 ? 0.7428 0.9275 0.8231 -0.1055 -0.0043 -0.0274 472 ASP A CG  
1328  O OD1 . ASP A 171 ? 0.8000 0.9531 0.8694 -0.1025 -0.0008 -0.0220 472 ASP A OD1 
1329  O OD2 . ASP A 171 ? 0.7564 0.9525 0.8374 -0.1110 -0.0098 -0.0350 472 ASP A OD2 
1330  N N   . GLY A 172 ? 0.7047 0.8468 0.7796 -0.0982 0.0133  -0.0064 473 GLY A N   
1331  C CA  . GLY A 172 ? 0.6177 0.7351 0.6864 -0.1082 0.0191  -0.0025 473 GLY A CA  
1332  C C   . GLY A 172 ? 0.6726 0.7689 0.7322 -0.1194 0.0180  -0.0060 473 GLY A C   
1333  O O   . GLY A 172 ? 0.6448 0.7144 0.6955 -0.1250 0.0221  -0.0024 473 GLY A O   
1334  N N   . LYS A 173 ? 0.7021 0.8086 0.7624 -0.1219 0.0121  -0.0132 474 LYS A N   
1335  C CA  . LYS A 173 ? 0.7231 0.8098 0.7739 -0.1318 0.0101  -0.0180 474 LYS A CA  
1336  C C   . LYS A 173 ? 0.6882 0.7552 0.7268 -0.1199 0.0068  -0.0184 474 LYS A C   
1337  O O   . LYS A 173 ? 0.7291 0.7795 0.7585 -0.1257 0.0045  -0.0232 474 LYS A O   
1338  C CB  . LYS A 173 ? 0.7969 0.9083 0.8560 -0.1441 0.0055  -0.0269 474 LYS A CB  
1339  C CG  . LYS A 173 ? 0.9093 1.0333 0.9773 -0.1616 0.0097  -0.0272 474 LYS A CG  
1340  C CD  . LYS A 173 ? 0.9935 1.1584 1.0764 -0.1685 0.0056  -0.0345 474 LYS A CD  
1341  C CE  . LYS A 173 ? 1.0341 1.2149 1.1270 -0.1855 0.0111  -0.0337 474 LYS A CE  
1342  N NZ  . LYS A 173 ? 1.0227 1.2482 1.1319 -0.1925 0.0074  -0.0412 474 LYS A NZ  
1343  N N   . HIS A 174 ? 0.6298 0.6976 0.6674 -0.1038 0.0068  -0.0135 475 HIS A N   
1344  C CA  . HIS A 174 ? 0.6029 0.6555 0.6294 -0.0925 0.0044  -0.0132 475 HIS A CA  
1345  C C   . HIS A 174 ? 0.5906 0.6285 0.6128 -0.0812 0.0085  -0.0051 475 HIS A C   
1346  O O   . HIS A 174 ? 0.5225 0.5602 0.5407 -0.0690 0.0068  -0.0029 475 HIS A O   
1347  C CB  . HIS A 174 ? 0.5760 0.6502 0.6052 -0.0844 -0.0020 -0.0172 475 HIS A CB  
1348  C CG  . HIS A 174 ? 0.6768 0.7685 0.7108 -0.0949 -0.0069 -0.0260 475 HIS A CG  
1349  N ND1 . HIS A 174 ? 0.6969 0.8161 0.7445 -0.1027 -0.0076 -0.0290 475 HIS A ND1 
1350  C CD2 . HIS A 174 ? 0.7157 0.8019 0.7427 -0.0997 -0.0113 -0.0332 475 HIS A CD2 
1351  C CE1 . HIS A 174 ? 0.7242 0.8554 0.7737 -0.1124 -0.0124 -0.0376 475 HIS A CE1 
1352  N NE2 . HIS A 174 ? 0.7636 0.8741 0.8003 -0.1108 -0.0149 -0.0404 475 HIS A NE2 
1353  N N   . ASP A 175 ? 0.6070 0.6327 0.6292 -0.0855 0.0140  -0.0004 476 ASP A N   
1354  C CA  . ASP A 175 ? 0.5336 0.5482 0.5529 -0.0757 0.0179  0.0068  476 ASP A CA  
1355  C C   . ASP A 175 ? 0.5316 0.5242 0.5385 -0.0690 0.0178  0.0077  476 ASP A C   
1356  O O   . ASP A 175 ? 0.5359 0.5140 0.5346 -0.0737 0.0168  0.0038  476 ASP A O   
1357  C CB  . ASP A 175 ? 0.7120 0.7183 0.7327 -0.0819 0.0235  0.0112  476 ASP A CB  
1358  C CG  . ASP A 175 ? 0.6545 0.6844 0.6877 -0.0868 0.0248  0.0115  476 ASP A CG  
1359  O OD1 . ASP A 175 ? 0.5721 0.6251 0.6134 -0.0816 0.0216  0.0094  476 ASP A OD1 
1360  O OD2 . ASP A 175 ? 0.6020 0.6267 0.6359 -0.0953 0.0291  0.0139  476 ASP A OD2 
1361  N N   . PHE A 176 ? 0.5111 0.5019 0.5163 -0.0579 0.0190  0.0125  477 PHE A N   
1362  C CA  . PHE A 176 ? 0.5367 0.5084 0.5319 -0.0518 0.0209  0.0150  477 PHE A CA  
1363  C C   . PHE A 176 ? 0.5942 0.5547 0.5893 -0.0525 0.0260  0.0201  477 PHE A C   
1364  O O   . PHE A 176 ? 0.6265 0.5963 0.6290 -0.0516 0.0279  0.0237  477 PHE A O   
1365  C CB  . PHE A 176 ? 0.4844 0.4609 0.4776 -0.0408 0.0197  0.0176  477 PHE A CB  
1366  C CG  . PHE A 176 ? 0.6066 0.5911 0.5965 -0.0384 0.0148  0.0133  477 PHE A CG  
1367  C CD1 . PHE A 176 ? 0.5489 0.5515 0.5454 -0.0409 0.0107  0.0097  477 PHE A CD1 
1368  C CD2 . PHE A 176 ? 0.5169 0.4924 0.4968 -0.0329 0.0143  0.0128  477 PHE A CD2 
1369  C CE1 . PHE A 176 ? 0.6203 0.6308 0.6130 -0.0378 0.0059  0.0058  477 PHE A CE1 
1370  C CE2 . PHE A 176 ? 0.5741 0.5571 0.5499 -0.0301 0.0099  0.0091  477 PHE A CE2 
1371  C CZ  . PHE A 176 ? 0.5476 0.5476 0.5294 -0.0325 0.0055  0.0056  477 PHE A CZ  
1372  N N   . ARG A 177 ? 0.4606 0.4012 0.4466 -0.0535 0.0279  0.0200  478 ARG A N   
1373  C CA  . ARG A 177 ? 0.5222 0.4511 0.5062 -0.0529 0.0322  0.0248  478 ARG A CA  
1374  C C   . ARG A 177 ? 0.4867 0.3994 0.4604 -0.0453 0.0333  0.0256  478 ARG A C   
1375  O O   . ARG A 177 ? 0.5013 0.4034 0.4666 -0.0452 0.0315  0.0214  478 ARG A O   
1376  C CB  . ARG A 177 ? 0.4869 0.4068 0.4695 -0.0640 0.0339  0.0242  478 ARG A CB  
1377  C CG  . ARG A 177 ? 0.5705 0.5092 0.5644 -0.0719 0.0342  0.0241  478 ARG A CG  
1378  C CD  . ARG A 177 ? 0.6417 0.5923 0.6430 -0.0660 0.0367  0.0293  478 ARG A CD  
1379  N NE  . ARG A 177 ? 0.6657 0.6027 0.6623 -0.0653 0.0410  0.0343  478 ARG A NE  
1380  C CZ  . ARG A 177 ? 0.6227 0.5575 0.6199 -0.0735 0.0442  0.0365  478 ARG A CZ  
1381  N NH1 . ARG A 177 ? 0.5930 0.5395 0.5962 -0.0842 0.0439  0.0340  478 ARG A NH1 
1382  N NH2 . ARG A 177 ? 0.5179 0.4400 0.5093 -0.0712 0.0477  0.0414  478 ARG A NH2 
1383  N N   . VAL A 178 ? 0.4428 0.3546 0.4170 -0.0388 0.0362  0.0305  479 VAL A N   
1384  C CA  . VAL A 178 ? 0.5619 0.4585 0.5268 -0.0327 0.0380  0.0316  479 VAL A CA  
1385  C C   . VAL A 178 ? 0.6266 0.5087 0.5872 -0.0374 0.0403  0.0334  479 VAL A C   
1386  O O   . VAL A 178 ? 0.6169 0.5043 0.5832 -0.0399 0.0425  0.0374  479 VAL A O   
1387  C CB  . VAL A 178 ? 0.6203 0.5242 0.5878 -0.0243 0.0398  0.0355  479 VAL A CB  
1388  C CG1 . VAL A 178 ? 0.5905 0.4819 0.5490 -0.0175 0.0414  0.0359  479 VAL A CG1 
1389  C CG2 . VAL A 178 ? 0.6398 0.5562 0.6101 -0.0207 0.0379  0.0347  479 VAL A CG2 
1390  N N   . TRP A 179 ? 0.6574 0.5202 0.6069 -0.0387 0.0397  0.0305  480 TRP A N   
1391  C CA  . TRP A 179 ? 0.5530 0.3985 0.4959 -0.0438 0.0419  0.0329  480 TRP A CA  
1392  C C   . TRP A 179 ? 0.5273 0.3655 0.4655 -0.0348 0.0446  0.0377  480 TRP A C   
1393  O O   . TRP A 179 ? 0.6415 0.4716 0.5771 -0.0380 0.0470  0.0418  480 TRP A O   
1394  C CB  . TRP A 179 ? 0.4797 0.3032 0.4103 -0.0484 0.0400  0.0281  480 TRP A CB  
1395  C CG  . TRP A 179 ? 0.5340 0.3633 0.4694 -0.0614 0.0380  0.0239  480 TRP A CG  
1396  C CD1 . TRP A 179 ? 0.5388 0.3924 0.4869 -0.0646 0.0360  0.0220  480 TRP A CD1 
1397  C CD2 . TRP A 179 ? 0.5136 0.3249 0.4412 -0.0731 0.0374  0.0211  480 TRP A CD2 
1398  N NE1 . TRP A 179 ? 0.5116 0.3662 0.4613 -0.0771 0.0341  0.0176  480 TRP A NE1 
1399  C CE2 . TRP A 179 ? 0.5320 0.3608 0.4695 -0.0836 0.0351  0.0170  480 TRP A CE2 
1400  C CE3 . TRP A 179 ? 0.5301 0.3110 0.4423 -0.0757 0.0385  0.0216  480 TRP A CE3 
1401  C CZ2 . TRP A 179 ? 0.5705 0.3897 0.5044 -0.0981 0.0341  0.0131  480 TRP A CZ2 
1402  C CZ3 . TRP A 179 ? 0.5928 0.3607 0.5000 -0.0902 0.0377  0.0182  480 TRP A CZ3 
1403  C CH2 . TRP A 179 ? 0.6037 0.3916 0.5223 -0.1020 0.0355  0.0138  480 TRP A CH2 
1404  N N   . ASN A 180 ? 0.5381 0.3802 0.4747 -0.0239 0.0442  0.0373  481 ASN A N   
1405  C CA  . ASN A 180 ? 0.5447 0.3864 0.4794 -0.0150 0.0464  0.0414  481 ASN A CA  
1406  C C   . ASN A 180 ? 0.5464 0.4036 0.4920 -0.0175 0.0483  0.0460  481 ASN A C   
1407  O O   . ASN A 180 ? 0.5374 0.4104 0.4933 -0.0219 0.0476  0.0456  481 ASN A O   
1408  C CB  . ASN A 180 ? 0.4754 0.3256 0.4098 -0.0047 0.0458  0.0397  481 ASN A CB  
1409  C CG  . ASN A 180 ? 0.5409 0.3796 0.4653 -0.0011 0.0438  0.0343  481 ASN A CG  
1410  O OD1 . ASN A 180 ? 0.5609 0.4006 0.4860 -0.0067 0.0417  0.0304  481 ASN A OD1 
1411  N ND2 . ASN A 180 ? 0.5568 0.3856 0.4713 0.0090  0.0442  0.0336  481 ASN A ND2 
1412  N N   . SER A 181 ? 0.4556 0.3081 0.3979 -0.0134 0.0503  0.0501  482 SER A N   
1413  C CA  . SER A 181 ? 0.5061 0.3736 0.4578 -0.0146 0.0520  0.0537  482 SER A CA  
1414  C C   . SER A 181 ? 0.5347 0.4174 0.4924 -0.0070 0.0516  0.0537  482 SER A C   
1415  O O   . SER A 181 ? 0.5300 0.4278 0.4975 -0.0090 0.0516  0.0545  482 SER A O   
1416  C CB  . SER A 181 ? 0.4963 0.3537 0.4420 -0.0150 0.0544  0.0583  482 SER A CB  
1417  O OG  . SER A 181 ? 0.5042 0.3489 0.4389 -0.0057 0.0545  0.0596  482 SER A OG  
1418  N N   . GLN A 182 ? 0.5195 0.3987 0.4712 0.0015  0.0512  0.0525  483 GLN A N   
1419  C CA  . GLN A 182 ? 0.5518 0.4466 0.5093 0.0065  0.0509  0.0516  483 GLN A CA  
1420  C C   . GLN A 182 ? 0.5105 0.4028 0.4632 0.0100  0.0497  0.0477  483 GLN A C   
1421  O O   . GLN A 182 ? 0.4763 0.3530 0.4197 0.0110  0.0489  0.0455  483 GLN A O   
1422  C CB  . GLN A 182 ? 0.5907 0.4915 0.5479 0.0140  0.0519  0.0535  483 GLN A CB  
1423  C CG  . GLN A 182 ? 0.6967 0.6027 0.6587 0.0115  0.0530  0.0569  483 GLN A CG  
1424  C CD  . GLN A 182 ? 0.6898 0.6000 0.6493 0.0195  0.0535  0.0584  483 GLN A CD  
1425  O OE1 . GLN A 182 ? 0.6720 0.5937 0.6340 0.0247  0.0532  0.0569  483 GLN A OE1 
1426  N NE2 . GLN A 182 ? 0.7451 0.6468 0.6992 0.0204  0.0543  0.0614  483 GLN A NE2 
1427  N N   . LEU A 183 ? 0.4818 0.3886 0.4400 0.0115  0.0496  0.0468  484 LEU A N   
1428  C CA  . LEU A 183 ? 0.5457 0.4525 0.4992 0.0149  0.0488  0.0433  484 LEU A CA  
1429  C C   . LEU A 183 ? 0.5609 0.4635 0.5061 0.0248  0.0494  0.0416  484 LEU A C   
1430  O O   . LEU A 183 ? 0.5321 0.4252 0.4686 0.0287  0.0484  0.0380  484 LEU A O   
1431  C CB  . LEU A 183 ? 0.4234 0.3466 0.3835 0.0136  0.0490  0.0437  484 LEU A CB  
1432  C CG  . LEU A 183 ? 0.4215 0.3492 0.3883 0.0061  0.0479  0.0449  484 LEU A CG  
1433  C CD1 . LEU A 183 ? 0.3613 0.3018 0.3317 0.0059  0.0484  0.0461  484 LEU A CD1 
1434  C CD2 . LEU A 183 ? 0.3560 0.2754 0.3196 0.0022  0.0457  0.0421  484 LEU A CD2 
1435  N N   . ILE A 184 ? 0.4629 0.3724 0.4101 0.0298  0.0506  0.0439  485 ILE A N   
1436  C CA  . ILE A 184 ? 0.5329 0.4395 0.4722 0.0407  0.0508  0.0425  485 ILE A CA  
1437  C C   . ILE A 184 ? 0.5650 0.4606 0.5002 0.0428  0.0509  0.0455  485 ILE A C   
1438  O O   . ILE A 184 ? 0.4865 0.3922 0.4289 0.0405  0.0516  0.0486  485 ILE A O   
1439  C CB  . ILE A 184 ? 0.5245 0.4534 0.4695 0.0460  0.0521  0.0420  485 ILE A CB  
1440  C CG1 . ILE A 184 ? 0.5975 0.5371 0.5458 0.0426  0.0526  0.0401  485 ILE A CG1 
1441  C CG2 . ILE A 184 ? 0.5131 0.4416 0.4501 0.0588  0.0520  0.0398  485 ILE A CG2 
1442  C CD1 . ILE A 184 ? 0.6666 0.6290 0.6209 0.0453  0.0545  0.0400  485 ILE A CD1 
1443  N N   . ARG A 185 ? 0.6021 0.4756 0.5247 0.0466  0.0501  0.0448  486 ARG A N   
1444  C CA  . ARG A 185 ? 0.6325 0.4928 0.5467 0.0516  0.0502  0.0478  486 ARG A CA  
1445  C C   . ARG A 185 ? 0.6869 0.5301 0.5858 0.0633  0.0490  0.0450  486 ARG A C   
1446  O O   . ARG A 185 ? 0.6233 0.4607 0.5174 0.0649  0.0480  0.0406  486 ARG A O   
1447  C CB  . ARG A 185 ? 0.6052 0.4483 0.5166 0.0419  0.0506  0.0513  486 ARG A CB  
1448  C CG  . ARG A 185 ? 0.7436 0.5975 0.6675 0.0293  0.0514  0.0528  486 ARG A CG  
1449  C CD  . ARG A 185 ? 0.7907 0.6528 0.7201 0.0274  0.0528  0.0573  486 ARG A CD  
1450  N NE  . ARG A 185 ? 0.8789 0.7271 0.7973 0.0331  0.0533  0.0607  486 ARG A NE  
1451  C CZ  . ARG A 185 ? 0.8894 0.7304 0.8056 0.0276  0.0548  0.0651  486 ARG A CZ  
1452  N NH1 . ARG A 185 ? 0.8220 0.6699 0.7473 0.0165  0.0559  0.0659  486 ARG A NH1 
1453  N NH2 . ARG A 185 ? 0.8519 0.6794 0.7562 0.0339  0.0553  0.0687  486 ARG A NH2 
1454  N N   . TYR A 186 ? 0.5519 0.3859 0.4417 0.0722  0.0487  0.0475  487 TYR A N   
1455  C CA  . TYR A 186 ? 0.6133 0.4269 0.4859 0.0847  0.0472  0.0453  487 TYR A CA  
1456  C C   . TYR A 186 ? 0.6917 0.4703 0.5495 0.0795  0.0468  0.0472  487 TYR A C   
1457  O O   . TYR A 186 ? 0.7719 0.5438 0.6317 0.0689  0.0481  0.0519  487 TYR A O   
1458  C CB  . TYR A 186 ? 0.4962 0.3185 0.3650 0.0994  0.0468  0.0467  487 TYR A CB  
1459  C CG  . TYR A 186 ? 0.6181 0.4752 0.5004 0.1044  0.0472  0.0441  487 TYR A CG  
1460  C CD1 . TYR A 186 ? 0.6729 0.5408 0.5561 0.1099  0.0471  0.0386  487 TYR A CD1 
1461  C CD2 . TYR A 186 ? 0.6117 0.4910 0.5051 0.1032  0.0479  0.0469  487 TYR A CD2 
1462  C CE1 . TYR A 186 ? 0.6792 0.5798 0.5744 0.1132  0.0480  0.0365  487 TYR A CE1 
1463  C CE2 . TYR A 186 ? 0.6443 0.5555 0.5500 0.1060  0.0484  0.0443  487 TYR A CE2 
1464  C CZ  . TYR A 186 ? 0.5735 0.4955 0.4802 0.1106  0.0487  0.0394  487 TYR A CZ  
1465  O OH  . TYR A 186 ? 0.4844 0.4388 0.4029 0.1122  0.0497  0.0370  487 TYR A OH  
1466  N N   . ALA A 187 ? 0.6107 0.3667 0.4529 0.0868  0.0451  0.0433  488 ALA A N   
1467  C CA  . ALA A 187 ? 0.6925 0.4122 0.5186 0.0813  0.0445  0.0444  488 ALA A CA  
1468  C C   . ALA A 187 ? 0.7832 0.4836 0.5958 0.0875  0.0448  0.0505  488 ALA A C   
1469  O O   . ALA A 187 ? 0.6549 0.3668 0.4664 0.1010  0.0445  0.0522  488 ALA A O   
1470  C CB  . ALA A 187 ? 0.6646 0.3637 0.4761 0.0884  0.0422  0.0377  488 ALA A CB  
1471  N N   . GLY A 188 ? 0.8697 0.5410 0.6712 0.0771  0.0454  0.0539  489 GLY A N   
1472  C CA  . GLY A 188 ? 0.8015 0.4472 0.5856 0.0821  0.0459  0.0602  489 GLY A CA  
1473  C C   . GLY A 188 ? 0.9397 0.5421 0.7013 0.0800  0.0447  0.0592  489 GLY A C   
1474  O O   . GLY A 188 ? 0.9825 0.5747 0.7454 0.0653  0.0448  0.0564  489 GLY A O   
1475  N N   . TYR A 189 ? 1.0411 0.6176 0.7810 0.0955  0.0431  0.0611  490 TYR A N   
1476  C CA  . TYR A 189 ? 0.8937 0.4236 0.6082 0.0958  0.0416  0.0603  490 TYR A CA  
1477  C C   . TYR A 189 ? 0.9679 0.4702 0.6631 0.0994  0.0427  0.0693  490 TYR A C   
1478  O O   . TYR A 189 ? 0.9438 0.4525 0.6336 0.1173  0.0417  0.0721  490 TYR A O   
1479  C CB  . TYR A 189 ? 0.7844 0.3040 0.4862 0.1148  0.0380  0.0525  490 TYR A CB  
1480  C CG  . TYR A 189 ? 0.8999 0.4533 0.6201 0.1170  0.0371  0.0442  490 TYR A CG  
1481  C CD1 . TYR A 189 ? 0.9243 0.4725 0.6475 0.1051  0.0364  0.0377  490 TYR A CD1 
1482  C CD2 . TYR A 189 ? 0.9275 0.5180 0.6611 0.1309  0.0370  0.0427  490 TYR A CD2 
1483  C CE1 . TYR A 189 ? 0.8616 0.4401 0.6000 0.1076  0.0357  0.0306  490 TYR A CE1 
1484  C CE2 . TYR A 189 ? 0.9081 0.5288 0.6573 0.1322  0.0367  0.0357  490 TYR A CE2 
1485  C CZ  . TYR A 189 ? 0.8767 0.4905 0.6275 0.1209  0.0361  0.0300  490 TYR A CZ  
1486  O OH  . TYR A 189 ? 0.9017 0.5447 0.6663 0.1224  0.0361  0.0238  490 TYR A OH  
1487  N N   . LYS A 190 ? 0.9282 0.4006 0.6127 0.0825  0.0446  0.0739  491 LYS A N   
1488  C CA  . LYS A 190 ? 1.0394 0.4766 0.7001 0.0852  0.0457  0.0827  491 LYS A CA  
1489  C C   . LYS A 190 ? 1.0217 0.4143 0.6526 0.0999  0.0421  0.0798  491 LYS A C   
1490  O O   . LYS A 190 ? 1.1412 0.5127 0.7652 0.0936  0.0404  0.0732  491 LYS A O   
1491  C CB  . LYS A 190 ? 1.2089 0.6318 0.8690 0.0601  0.0497  0.0888  491 LYS A CB  
1492  C CG  . LYS A 190 ? 1.3947 0.8012 1.0405 0.0598  0.0527  0.1005  491 LYS A CG  
1493  C CD  . LYS A 190 ? 1.4071 0.8575 1.0755 0.0583  0.0553  0.1048  491 LYS A CD  
1494  C CE  . LYS A 190 ? 1.4702 0.9053 1.1241 0.0564  0.0586  0.1163  491 LYS A CE  
1495  N NZ  . LYS A 190 ? 1.5172 0.9242 1.1608 0.0335  0.0626  0.1217  491 LYS A NZ  
1496  N N   . GLN A 191 ? 0.9177 0.2964 0.5305 0.1205  0.0406  0.0843  492 GLN A N   
1497  C CA  . GLN A 191 ? 1.0758 0.4140 0.6595 0.1370  0.0368  0.0820  492 GLN A CA  
1498  C C   . GLN A 191 ? 1.1303 0.4335 0.6968 0.1219  0.0376  0.0870  492 GLN A C   
1499  O O   . GLN A 191 ? 1.2238 0.5297 0.7954 0.1049  0.0416  0.0951  492 GLN A O   
1500  C CB  . GLN A 191 ? 1.1459 0.4984 0.7241 0.1644  0.0340  0.0830  492 GLN A CB  
1501  C CG  . GLN A 191 ? 1.0652 0.4655 0.6666 0.1772  0.0332  0.0772  492 GLN A CG  
1502  C CD  . GLN A 191 ? 1.0880 0.4929 0.6937 0.1813  0.0307  0.0656  492 GLN A CD  
1503  O OE1 . GLN A 191 ? 1.0939 0.5234 0.7215 0.1657  0.0322  0.0608  492 GLN A OE1 
1504  N NE2 . GLN A 191 ? 1.1373 0.5181 0.7209 0.2032  0.0269  0.0608  492 GLN A NE2 
1505  N N   . PRO A 192 ? 1.0714 0.3419 0.6170 0.1276  0.0340  0.0823  493 PRO A N   
1506  C CA  . PRO A 192 ? 1.1576 0.3933 0.6850 0.1145  0.0349  0.0877  493 PRO A CA  
1507  C C   . PRO A 192 ? 1.2294 0.4638 0.7471 0.1227  0.0360  0.0976  493 PRO A C   
1508  O O   . PRO A 192 ? 1.2767 0.4907 0.7850 0.1076  0.0385  0.1047  493 PRO A O   
1509  C CB  . PRO A 192 ? 1.2141 0.4168 0.7203 0.1240  0.0301  0.0795  493 PRO A CB  
1510  C CG  . PRO A 192 ? 1.1508 0.3741 0.6615 0.1488  0.0266  0.0713  493 PRO A CG  
1511  C CD  . PRO A 192 ? 1.0888 0.3524 0.6267 0.1445  0.0294  0.0715  493 PRO A CD  
1512  N N   . ASP A 193 ? 1.1395 0.3959 0.6591 0.1460  0.0342  0.0983  494 ASP A N   
1513  C CA  . ASP A 193 ? 1.1728 0.4289 0.6822 0.1555  0.0347  0.1070  494 ASP A CA  
1514  C C   . ASP A 193 ? 1.1570 0.4404 0.6841 0.1431  0.0395  0.1155  494 ASP A C   
1515  O O   . ASP A 193 ? 1.2562 0.5456 0.7776 0.1514  0.0401  0.1226  494 ASP A O   
1516  C CB  . ASP A 193 ? 1.0943 0.3634 0.5971 0.1866  0.0303  0.1034  494 ASP A CB  
1517  C CG  . ASP A 193 ? 1.1152 0.4303 0.6418 0.1969  0.0304  0.1009  494 ASP A CG  
1518  O OD1 . ASP A 193 ? 1.1277 0.4622 0.6751 0.1818  0.0335  0.1005  494 ASP A OD1 
1519  O OD2 . ASP A 193 ? 1.1655 0.4985 0.6898 0.2206  0.0273  0.0992  494 ASP A OD2 
1520  N N   . GLY A 194 ? 1.0621 0.3620 0.6095 0.1237  0.0429  0.1145  495 GLY A N   
1521  C CA  . GLY A 194 ? 1.0649 0.3927 0.6300 0.1121  0.0474  0.1213  495 GLY A CA  
1522  C C   . GLY A 194 ? 1.0086 0.3758 0.5930 0.1248  0.0471  0.1193  495 GLY A C   
1523  O O   . GLY A 194 ? 1.0409 0.4322 0.6436 0.1121  0.0511  0.1224  495 GLY A O   
1524  N N   . SER A 195 ? 1.0322 0.4079 0.6134 0.1493  0.0427  0.1139  496 SER A N   
1525  C CA  . SER A 195 ? 1.1088 0.5252 0.7098 0.1612  0.0423  0.1113  496 SER A CA  
1526  C C   . SER A 195 ? 1.0602 0.5043 0.6882 0.1458  0.0432  0.1025  496 SER A C   
1527  O O   . SER A 195 ? 1.0908 0.5126 0.7154 0.1309  0.0440  0.0997  496 SER A O   
1528  C CB  . SER A 195 ? 1.1226 0.5460 0.7155 0.1902  0.0372  0.1063  496 SER A CB  
1529  O OG  . SER A 195 ? 1.1521 0.5592 0.7382 0.1955  0.0343  0.0973  496 SER A OG  
1530  N N   . THR A 196 ? 1.0015 0.4947 0.6561 0.1493  0.0429  0.0981  497 THR A N   
1531  C CA  . THR A 196 ? 0.9854 0.5079 0.6659 0.1362  0.0437  0.0906  497 THR A CA  
1532  C C   . THR A 196 ? 1.0030 0.5601 0.6972 0.1526  0.0408  0.0827  497 THR A C   
1533  O O   . THR A 196 ? 1.0547 0.6395 0.7564 0.1644  0.0401  0.0839  497 THR A O   
1534  C CB  . THR A 196 ? 0.9948 0.5458 0.6980 0.1167  0.0476  0.0942  497 THR A CB  
1535  O OG1 . THR A 196 ? 1.0538 0.5770 0.7443 0.1022  0.0508  0.1024  497 THR A OG1 
1536  C CG2 . THR A 196 ? 0.9702 0.5442 0.6961 0.1026  0.0482  0.0869  497 THR A CG2 
1537  N N   . LEU A 197 ? 1.0247 0.5819 0.7225 0.1527  0.0394  0.0743  498 LEU A N   
1538  C CA  . LEU A 197 ? 0.9362 0.5281 0.6482 0.1653  0.0376  0.0665  498 LEU A CA  
1539  C C   . LEU A 197 ? 0.8720 0.5005 0.6127 0.1486  0.0398  0.0636  498 LEU A C   
1540  O O   . LEU A 197 ? 0.9070 0.5262 0.6525 0.1303  0.0414  0.0633  498 LEU A O   
1541  C CB  . LEU A 197 ? 0.9430 0.5138 0.6400 0.1774  0.0347  0.0589  498 LEU A CB  
1542  C CG  . LEU A 197 ? 0.9934 0.6013 0.7054 0.1887  0.0334  0.0505  498 LEU A CG  
1543  C CD1 . LEU A 197 ? 0.9247 0.5635 0.6425 0.2061  0.0324  0.0517  498 LEU A CD1 
1544  C CD2 . LEU A 197 ? 1.0448 0.6303 0.7405 0.2005  0.0308  0.0425  498 LEU A CD2 
1545  N N   . GLY A 198 ? 0.8537 0.5236 0.6129 0.1549  0.0397  0.0615  499 GLY A N   
1546  C CA  . GLY A 198 ? 0.8524 0.5565 0.6375 0.1403  0.0418  0.0596  499 GLY A CA  
1547  C C   . GLY A 198 ? 0.9061 0.6206 0.7026 0.1257  0.0443  0.0659  499 GLY A C   
1548  O O   . GLY A 198 ? 0.9885 0.7023 0.7796 0.1310  0.0444  0.0714  499 GLY A O   
1549  N N   . ASP A 199 ? 0.8323 0.5566 0.6438 0.1080  0.0462  0.0650  500 ASP A N   
1550  C CA  . ASP A 199 ? 0.7928 0.5317 0.6176 0.0946  0.0486  0.0697  500 ASP A CA  
1551  C C   . ASP A 199 ? 0.8449 0.5553 0.6599 0.0812  0.0505  0.0745  500 ASP A C   
1552  O O   . ASP A 199 ? 0.8813 0.5834 0.6991 0.0687  0.0511  0.0720  500 ASP A O   
1553  C CB  . ASP A 199 ? 0.7473 0.5160 0.5944 0.0845  0.0494  0.0657  500 ASP A CB  
1554  C CG  . ASP A 199 ? 0.7359 0.5239 0.5974 0.0740  0.0513  0.0694  500 ASP A CG  
1555  O OD1 . ASP A 199 ? 0.7293 0.5031 0.5850 0.0669  0.0530  0.0747  500 ASP A OD1 
1556  O OD2 . ASP A 199 ? 0.6025 0.4193 0.4804 0.0728  0.0513  0.0669  500 ASP A OD2 
1557  N N   . PRO A 200 ? 0.7836 0.4805 0.5874 0.0825  0.0517  0.0815  501 PRO A N   
1558  C CA  . PRO A 200 ? 0.8013 0.4703 0.5942 0.0689  0.0541  0.0868  501 PRO A CA  
1559  C C   . PRO A 200 ? 0.8245 0.5080 0.6345 0.0492  0.0567  0.0864  501 PRO A C   
1560  O O   . PRO A 200 ? 0.8265 0.4893 0.6300 0.0359  0.0583  0.0880  501 PRO A O   
1561  C CB  . PRO A 200 ? 0.7231 0.3852 0.5045 0.0752  0.0553  0.0947  501 PRO A CB  
1562  C CG  . PRO A 200 ? 0.7071 0.3802 0.4851 0.0964  0.0521  0.0925  501 PRO A CG  
1563  C CD  . PRO A 200 ? 0.6857 0.3917 0.4848 0.0972  0.0507  0.0848  501 PRO A CD  
1564  N N   . ALA A 201 ? 0.8950 0.6134 0.7261 0.0470  0.0569  0.0841  502 ALA A N   
1565  C CA  . ALA A 201 ? 0.7581 0.4926 0.6059 0.0307  0.0588  0.0832  502 ALA A CA  
1566  C C   . ALA A 201 ? 0.8073 0.5355 0.6581 0.0222  0.0577  0.0776  502 ALA A C   
1567  O O   . ALA A 201 ? 0.7501 0.4845 0.6102 0.0077  0.0592  0.0772  502 ALA A O   
1568  C CB  . ALA A 201 ? 0.5855 0.3554 0.4529 0.0326  0.0585  0.0811  502 ALA A CB  
1569  N N   . ASN A 202 ? 0.7758 0.4938 0.6192 0.0313  0.0551  0.0728  503 ASN A N   
1570  C CA  . ASN A 202 ? 0.7758 0.4924 0.6233 0.0245  0.0537  0.0666  503 ASN A CA  
1571  C C   . ASN A 202 ? 0.7872 0.4677 0.6153 0.0228  0.0526  0.0652  503 ASN A C   
1572  O O   . ASN A 202 ? 0.8168 0.4925 0.6442 0.0212  0.0506  0.0589  503 ASN A O   
1573  C CB  . ASN A 202 ? 0.6240 0.3621 0.4807 0.0348  0.0516  0.0610  503 ASN A CB  
1574  C CG  . ASN A 202 ? 0.6390 0.4107 0.5147 0.0337  0.0525  0.0619  503 ASN A CG  
1575  O OD1 . ASN A 202 ? 0.7075 0.4901 0.5942 0.0221  0.0540  0.0636  503 ASN A OD1 
1576  N ND2 . ASN A 202 ? 0.6209 0.4095 0.5005 0.0458  0.0517  0.0604  503 ASN A ND2 
1577  N N   . VAL A 203 ? 0.7390 0.3928 0.5503 0.0226  0.0539  0.0709  504 VAL A N   
1578  C CA  . VAL A 203 ? 0.7158 0.3303 0.5054 0.0219  0.0527  0.0699  504 VAL A CA  
1579  C C   . VAL A 203 ? 0.8488 0.4562 0.6419 0.0033  0.0528  0.0662  504 VAL A C   
1580  O O   . VAL A 203 ? 0.8313 0.4195 0.6148 0.0034  0.0503  0.0601  504 VAL A O   
1581  C CB  . VAL A 203 ? 0.7870 0.3732 0.5568 0.0243  0.0545  0.0780  504 VAL A CB  
1582  C CG1 . VAL A 203 ? 0.7558 0.3011 0.5060 0.0136  0.0546  0.0784  504 VAL A CG1 
1583  C CG2 . VAL A 203 ? 0.8510 0.4318 0.6088 0.0468  0.0524  0.0788  504 VAL A CG2 
1584  N N   . GLN A 204 ? 0.8530 0.4769 0.6598 -0.0126 0.0556  0.0691  505 GLN A N   
1585  C CA  . GLN A 204 ? 0.9095 0.5290 0.7200 -0.0307 0.0555  0.0654  505 GLN A CA  
1586  C C   . GLN A 204 ? 0.9281 0.5678 0.7518 -0.0298 0.0524  0.0569  505 GLN A C   
1587  O O   . GLN A 204 ? 0.9370 0.5627 0.7554 -0.0366 0.0502  0.0509  505 GLN A O   
1588  C CB  . GLN A 204 ? 0.9963 0.6324 0.8189 -0.0468 0.0593  0.0703  505 GLN A CB  
1589  C CG  . GLN A 204 ? 1.1553 0.7753 0.9734 -0.0666 0.0602  0.0689  505 GLN A CG  
1590  C CD  . GLN A 204 ? 1.1823 0.8346 1.0219 -0.0815 0.0617  0.0676  505 GLN A CD  
1591  O OE1 . GLN A 204 ? 1.0270 0.7059 0.8801 -0.0803 0.0641  0.0715  505 GLN A OE1 
1592  N NE2 . GLN A 204 ? 1.2507 0.9016 1.0933 -0.0949 0.0600  0.0616  505 GLN A NE2 
1593  N N   . PHE A 205 ? 0.8092 0.4811 0.6493 -0.0216 0.0521  0.0561  506 PHE A N   
1594  C CA  . PHE A 205 ? 0.7180 0.4081 0.5688 -0.0197 0.0494  0.0489  506 PHE A CA  
1595  C C   . PHE A 205 ? 0.7491 0.4209 0.5857 -0.0073 0.0464  0.0434  506 PHE A C   
1596  O O   . PHE A 205 ? 0.8085 0.4789 0.6450 -0.0103 0.0439  0.0366  506 PHE A O   
1597  C CB  . PHE A 205 ? 0.6740 0.3989 0.5429 -0.0136 0.0500  0.0500  506 PHE A CB  
1598  C CG  . PHE A 205 ? 0.6986 0.4417 0.5774 -0.0122 0.0476  0.0438  506 PHE A CG  
1599  C CD1 . PHE A 205 ? 0.7475 0.5041 0.6375 -0.0245 0.0469  0.0411  506 PHE A CD1 
1600  C CD2 . PHE A 205 ? 0.7140 0.4606 0.5895 0.0014  0.0461  0.0404  506 PHE A CD2 
1601  C CE1 . PHE A 205 ? 0.7036 0.4758 0.6010 -0.0227 0.0445  0.0358  506 PHE A CE1 
1602  C CE2 . PHE A 205 ? 0.6581 0.4210 0.5414 0.0023  0.0442  0.0352  506 PHE A CE2 
1603  C CZ  . PHE A 205 ? 0.6267 0.4013 0.5203 -0.0097 0.0433  0.0331  506 PHE A CZ  
1604  N N   . THR A 206 ? 0.7896 0.4482 0.6137 0.0074  0.0465  0.0459  507 THR A N   
1605  C CA  . THR A 206 ? 0.7535 0.3925 0.5618 0.0206  0.0438  0.0406  507 THR A CA  
1606  C C   . THR A 206 ? 0.8471 0.4510 0.6388 0.0117  0.0421  0.0369  507 THR A C   
1607  O O   . THR A 206 ? 0.8710 0.4664 0.6560 0.0157  0.0392  0.0293  507 THR A O   
1608  C CB  . THR A 206 ? 0.6551 0.2847 0.4514 0.0380  0.0441  0.0445  507 THR A CB  
1609  O OG1 . THR A 206 ? 0.6292 0.2932 0.4415 0.0455  0.0452  0.0467  507 THR A OG1 
1610  C CG2 . THR A 206 ? 0.7032 0.3130 0.4823 0.0533  0.0412  0.0386  507 THR A CG2 
1611  N N   . GLU A 207 ? 0.8718 0.4554 0.6563 -0.0013 0.0440  0.0420  508 GLU A N   
1612  C CA  . GLU A 207 ? 0.9328 0.4824 0.7017 -0.0127 0.0426  0.0385  508 GLU A CA  
1613  C C   . GLU A 207 ? 0.9250 0.4904 0.7069 -0.0268 0.0408  0.0314  508 GLU A C   
1614  O O   . GLU A 207 ? 0.9863 0.5313 0.7572 -0.0296 0.0378  0.0242  508 GLU A O   
1615  C CB  . GLU A 207 ? 0.9764 0.5031 0.7354 -0.0252 0.0457  0.0465  508 GLU A CB  
1616  C CG  . GLU A 207 ? 1.0232 0.5209 0.7609 -0.0115 0.0465  0.0528  508 GLU A CG  
1617  C CD  . GLU A 207 ? 1.2498 0.7330 0.9808 -0.0240 0.0506  0.0625  508 GLU A CD  
1618  O OE1 . GLU A 207 ? 1.2766 0.7787 1.0229 -0.0422 0.0533  0.0644  508 GLU A OE1 
1619  O OE2 . GLU A 207 ? 1.2897 0.7433 0.9997 -0.0149 0.0512  0.0683  508 GLU A OE2 
1620  N N   . ILE A 208 ? 0.8415 0.4428 0.6461 -0.0350 0.0424  0.0331  509 ILE A N   
1621  C CA  . ILE A 208 ? 0.8263 0.4460 0.6438 -0.0464 0.0403  0.0265  509 ILE A CA  
1622  C C   . ILE A 208 ? 0.8932 0.5205 0.7103 -0.0338 0.0369  0.0188  509 ILE A C   
1623  O O   . ILE A 208 ? 1.1210 0.7452 0.9366 -0.0399 0.0338  0.0113  509 ILE A O   
1624  C CB  . ILE A 208 ? 0.8022 0.4590 0.6430 -0.0546 0.0425  0.0301  509 ILE A CB  
1625  C CG1 . ILE A 208 ? 0.8339 0.4855 0.6750 -0.0674 0.0463  0.0373  509 ILE A CG1 
1626  C CG2 . ILE A 208 ? 0.6877 0.3644 0.5409 -0.0644 0.0398  0.0233  509 ILE A CG2 
1627  C CD1 . ILE A 208 ? 0.8100 0.4978 0.6725 -0.0721 0.0487  0.0411  509 ILE A CD1 
1628  N N   . CYS A 209 ? 0.7663 0.4055 0.5851 -0.0165 0.0374  0.0205  510 CYS A N   
1629  C CA  . CYS A 209 ? 0.7654 0.4138 0.5835 -0.0044 0.0348  0.0136  510 CYS A CA  
1630  C C   . CYS A 209 ? 0.8792 0.4935 0.6753 0.0012  0.0319  0.0071  510 CYS A C   
1631  O O   . CYS A 209 ? 0.8981 0.5123 0.6918 0.0006  0.0289  -0.0010 510 CYS A O   
1632  C CB  . CYS A 209 ? 0.7717 0.4402 0.5956 0.0120  0.0364  0.0169  510 CYS A CB  
1633  S SG  . CYS A 209 ? 0.7380 0.4480 0.5872 0.0073  0.0388  0.0218  510 CYS A SG  
1634  N N   . ILE A 210 ? 0.9170 0.5011 0.6956 0.0077  0.0326  0.0104  511 ILE A N   
1635  C CA  . ILE A 210 ? 0.9447 0.4930 0.6998 0.0159  0.0296  0.0043  511 ILE A CA  
1636  C C   . ILE A 210 ? 0.9437 0.4719 0.6921 -0.0008 0.0271  -0.0021 511 ILE A C   
1637  O O   . ILE A 210 ? 1.0091 0.5259 0.7475 0.0034  0.0235  -0.0112 511 ILE A O   
1638  C CB  . ILE A 210 ? 0.9165 0.4342 0.6531 0.0250  0.0308  0.0103  511 ILE A CB  
1639  C CG1 . ILE A 210 ? 0.7965 0.3366 0.5387 0.0445  0.0322  0.0140  511 ILE A CG1 
1640  C CG2 . ILE A 210 ? 0.8024 0.2756 0.5120 0.0301  0.0276  0.0044  511 ILE A CG2 
1641  C CD1 . ILE A 210 ? 0.8523 0.3722 0.5816 0.0523  0.0338  0.0220  511 ILE A CD1 
1642  N N   . GLN A 211 ? 0.9468 0.4730 0.7014 -0.0205 0.0287  0.0021  512 GLN A N   
1643  C CA  . GLN A 211 ? 1.1004 0.6079 0.8487 -0.0383 0.0263  -0.0040 512 GLN A CA  
1644  C C   . GLN A 211 ? 1.1392 0.6746 0.9016 -0.0424 0.0233  -0.0123 512 GLN A C   
1645  O O   . GLN A 211 ? 1.1712 0.6903 0.9243 -0.0495 0.0196  -0.0210 512 GLN A O   
1646  C CB  . GLN A 211 ? 1.1660 0.6694 0.9190 -0.0586 0.0295  0.0030  512 GLN A CB  
1647  C CG  . GLN A 211 ? 1.2971 0.7950 1.0516 -0.0809 0.0276  -0.0027 512 GLN A CG  
1648  C CD  . GLN A 211 ? 1.4217 0.9326 1.1887 -0.0998 0.0316  0.0046  512 GLN A CD  
1649  O OE1 . GLN A 211 ? 1.4115 0.9458 1.1915 -0.0957 0.0353  0.0126  512 GLN A OE1 
1650  N NE2 . GLN A 211 ? 1.5056 1.0022 1.2687 -0.1210 0.0310  0.0015  512 GLN A NE2 
1651  N N   . GLN A 212 ? 1.0918 0.6676 0.8747 -0.0373 0.0246  -0.0100 513 GLN A N   
1652  C CA  . GLN A 212 ? 1.0608 0.6636 0.8552 -0.0373 0.0219  -0.0168 513 GLN A CA  
1653  C C   . GLN A 212 ? 0.9945 0.5925 0.7777 -0.0197 0.0194  -0.0238 513 GLN A C   
1654  O O   . GLN A 212 ? 0.9366 0.5565 0.7274 -0.0181 0.0173  -0.0292 513 GLN A O   
1655  C CB  . GLN A 212 ? 1.0534 0.6979 0.8713 -0.0370 0.0242  -0.0113 513 GLN A CB  
1656  C CG  . GLN A 212 ? 0.9777 0.6367 0.8103 -0.0538 0.0262  -0.0061 513 GLN A CG  
1657  C CD  . GLN A 212 ? 1.0513 0.7036 0.8833 -0.0722 0.0235  -0.0120 513 GLN A CD  
1658  O OE1 . GLN A 212 ? 1.0974 0.7394 0.9289 -0.0866 0.0253  -0.0087 513 GLN A OE1 
1659  N NE2 . GLN A 212 ? 1.0179 0.6776 0.8499 -0.0723 0.0193  -0.0208 513 GLN A NE2 
1660  N N   . GLY A 213 ? 0.9533 0.5254 0.7189 -0.0056 0.0197  -0.0235 514 GLY A N   
1661  C CA  . GLY A 213 ? 0.9477 0.5130 0.7005 0.0115  0.0173  -0.0311 514 GLY A CA  
1662  C C   . GLY A 213 ? 0.9938 0.5779 0.7500 0.0314  0.0197  -0.0275 514 GLY A C   
1663  O O   . GLY A 213 ? 1.0254 0.6088 0.7723 0.0466  0.0182  -0.0338 514 GLY A O   
1664  N N   . TRP A 214 ? 0.9325 0.5350 0.7020 0.0318  0.0234  -0.0181 515 TRP A N   
1665  C CA  . TRP A 214 ? 0.8530 0.4732 0.6255 0.0497  0.0256  -0.0149 515 TRP A CA  
1666  C C   . TRP A 214 ? 0.9035 0.4933 0.6541 0.0659  0.0247  -0.0164 515 TRP A C   
1667  O O   . TRP A 214 ? 0.9709 0.5276 0.7077 0.0620  0.0243  -0.0138 515 TRP A O   
1668  C CB  . TRP A 214 ? 0.8688 0.5108 0.6582 0.0452  0.0292  -0.0050 515 TRP A CB  
1669  C CG  . TRP A 214 ? 0.8629 0.5290 0.6590 0.0606  0.0313  -0.0020 515 TRP A CG  
1670  C CD1 . TRP A 214 ? 0.8515 0.5445 0.6550 0.0692  0.0317  -0.0053 515 TRP A CD1 
1671  C CD2 . TRP A 214 ? 0.8430 0.5102 0.6393 0.0685  0.0335  0.0050  515 TRP A CD2 
1672  N NE1 . TRP A 214 ? 0.8305 0.5422 0.6396 0.0810  0.0340  -0.0012 515 TRP A NE1 
1673  C CE2 . TRP A 214 ? 0.8237 0.5205 0.6287 0.0813  0.0349  0.0048  515 TRP A CE2 
1674  C CE3 . TRP A 214 ? 0.8007 0.4478 0.5903 0.0656  0.0346  0.0113  515 TRP A CE3 
1675  C CZ2 . TRP A 214 ? 0.7199 0.4275 0.5276 0.0912  0.0367  0.0101  515 TRP A CZ2 
1676  C CZ3 . TRP A 214 ? 0.8543 0.5115 0.6459 0.0765  0.0363  0.0169  515 TRP A CZ3 
1677  C CH2 . TRP A 214 ? 0.7902 0.4779 0.5912 0.0892  0.0372  0.0159  515 TRP A CH2 
1678  N N   . LYS A 215 ? 0.8945 0.4956 0.6411 0.0844  0.0244  -0.0205 516 LYS A N   
1679  C CA  . LYS A 215 ? 0.8431 0.4202 0.5696 0.1033  0.0234  -0.0224 516 LYS A CA  
1680  C C   . LYS A 215 ? 0.8552 0.4538 0.5903 0.1145  0.0263  -0.0150 516 LYS A C   
1681  O O   . LYS A 215 ? 0.8776 0.5111 0.6250 0.1234  0.0279  -0.0157 516 LYS A O   
1682  C CB  . LYS A 215 ? 1.0050 0.5825 0.7207 0.1181  0.0211  -0.0327 516 LYS A CB  
1683  C CG  . LYS A 215 ? 1.1121 0.6700 0.8190 0.1074  0.0177  -0.0412 516 LYS A CG  
1684  C CD  . LYS A 215 ? 1.1804 0.6871 0.8639 0.1039  0.0149  -0.0432 516 LYS A CD  
1685  C CE  . LYS A 215 ? 1.2408 0.7326 0.9243 0.0816  0.0126  -0.0469 516 LYS A CE  
1686  N NZ  . LYS A 215 ? 1.2692 0.7707 0.9691 0.0617  0.0152  -0.0377 516 LYS A NZ  
1687  N N   . PRO A 216 ? 0.9996 0.5797 0.7285 0.1141  0.0271  -0.0078 517 PRO A N   
1688  C CA  . PRO A 216 ? 0.8542 0.4587 0.5944 0.1213  0.0298  -0.0004 517 PRO A CA  
1689  C C   . PRO A 216 ? 0.8865 0.4903 0.6145 0.1459  0.0288  -0.0028 517 PRO A C   
1690  O O   . PRO A 216 ? 0.9131 0.4820 0.6178 0.1570  0.0262  -0.0066 517 PRO A O   
1691  C CB  . PRO A 216 ? 0.8587 0.4402 0.5946 0.1099  0.0308  0.0079  517 PRO A CB  
1692  C CG  . PRO A 216 ? 0.9571 0.4910 0.6682 0.1087  0.0281  0.0041  517 PRO A CG  
1693  C CD  . PRO A 216 ? 0.9972 0.5320 0.7072 0.1064  0.0257  -0.0061 517 PRO A CD  
1694  N N   . PRO A 217 ? 0.8751 0.5171 0.6178 0.1554  0.0308  -0.0010 518 PRO A N   
1695  C CA  . PRO A 217 ? 0.8699 0.5150 0.6021 0.1794  0.0298  -0.0030 518 PRO A CA  
1696  C C   . PRO A 217 ? 0.9264 0.5482 0.6453 0.1872  0.0290  0.0034  518 PRO A C   
1697  O O   . PRO A 217 ? 0.9552 0.5734 0.6614 0.2088  0.0274  0.0014  518 PRO A O   
1698  C CB  . PRO A 217 ? 0.7812 0.4777 0.5359 0.1828  0.0325  -0.0026 518 PRO A CB  
1699  C CG  . PRO A 217 ? 0.7452 0.4597 0.5202 0.1611  0.0348  0.0019  518 PRO A CG  
1700  C CD  . PRO A 217 ? 0.7206 0.4051 0.4884 0.1458  0.0334  0.0004  518 PRO A CD  
1701  N N   . ARG A 218 ? 1.0434 0.6494 0.7637 0.1714  0.0301  0.0109  519 ARG A N   
1702  C CA  . ARG A 218 ? 1.0280 0.6111 0.7349 0.1772  0.0298  0.0182  519 ARG A CA  
1703  C C   . ARG A 218 ? 1.0410 0.6529 0.7532 0.1958  0.0299  0.0201  519 ARG A C   
1704  O O   . ARG A 218 ? 1.1214 0.7173 0.8154 0.2160  0.0276  0.0195  519 ARG A O   
1705  C CB  . ARG A 218 ? 1.0996 0.6297 0.7757 0.1847  0.0268  0.0161  519 ARG A CB  
1706  C CG  . ARG A 218 ? 1.1084 0.6097 0.7790 0.1644  0.0265  0.0140  519 ARG A CG  
1707  C CD  . ARG A 218 ? 1.1548 0.6006 0.7974 0.1626  0.0249  0.0170  519 ARG A CD  
1708  N NE  . ARG A 218 ? 1.2674 0.7008 0.9154 0.1357  0.0268  0.0209  519 ARG A NE  
1709  C CZ  . ARG A 218 ? 1.3228 0.7468 0.9705 0.1245  0.0293  0.0307  519 ARG A CZ  
1710  N NH1 . ARG A 218 ? 1.3158 0.7330 0.9699 0.0999  0.0313  0.0333  519 ARG A NH1 
1711  N NH2 . ARG A 218 ? 1.3238 0.7462 0.9642 0.1382  0.0299  0.0377  519 ARG A NH2 
1712  N N   . GLY A 219 ? 1.0255 0.6811 0.7631 0.1889  0.0323  0.0221  520 GLY A N   
1713  C CA  . GLY A 219 ? 1.0040 0.6921 0.7506 0.2020  0.0327  0.0241  520 GLY A CA  
1714  C C   . GLY A 219 ? 0.9660 0.6691 0.7273 0.1888  0.0348  0.0321  520 GLY A C   
1715  O O   . GLY A 219 ? 0.9766 0.6622 0.7388 0.1711  0.0361  0.0365  520 GLY A O   
1716  N N   . ARG A 220 ? 0.9330 0.6698 0.7060 0.1969  0.0352  0.0336  521 ARG A N   
1717  C CA  . ARG A 220 ? 0.7929 0.5435 0.5783 0.1859  0.0368  0.0406  521 ARG A CA  
1718  C C   . ARG A 220 ? 0.7792 0.5606 0.5895 0.1679  0.0395  0.0403  521 ARG A C   
1719  O O   . ARG A 220 ? 0.8635 0.6483 0.6827 0.1546  0.0410  0.0457  521 ARG A O   
1720  C CB  . ARG A 220 ? 0.8576 0.6294 0.6434 0.2023  0.0354  0.0422  521 ARG A CB  
1721  C CG  . ARG A 220 ? 0.9183 0.6894 0.7065 0.1952  0.0362  0.0502  521 ARG A CG  
1722  C CD  . ARG A 220 ? 0.9609 0.7574 0.7509 0.2115  0.0343  0.0506  521 ARG A CD  
1723  N NE  . ARG A 220 ? 0.9665 0.7617 0.7564 0.2067  0.0347  0.0579  521 ARG A NE  
1724  C CZ  . ARG A 220 ? 0.9781 0.7980 0.7719 0.2172  0.0331  0.0589  521 ARG A CZ  
1725  N NH1 . ARG A 220 ? 0.9162 0.7656 0.7153 0.2327  0.0311  0.0531  521 ARG A NH1 
1726  N NH2 . ARG A 220 ? 0.9286 0.7456 0.7213 0.2122  0.0335  0.0654  521 ARG A NH2 
1727  N N   . PHE A 221 ? 0.7410 0.5446 0.5617 0.1678  0.0401  0.0344  522 PHE A N   
1728  C CA  . PHE A 221 ? 0.7402 0.5734 0.5831 0.1526  0.0424  0.0343  522 PHE A CA  
1729  C C   . PHE A 221 ? 0.7011 0.5320 0.5457 0.1459  0.0430  0.0294  522 PHE A C   
1730  O O   . PHE A 221 ? 0.6509 0.5096 0.5075 0.1449  0.0443  0.0260  522 PHE A O   
1731  C CB  . PHE A 221 ? 0.7435 0.6174 0.6008 0.1591  0.0431  0.0332  522 PHE A CB  
1732  C CG  . PHE A 221 ? 0.7879 0.6681 0.6455 0.1640  0.0422  0.0377  522 PHE A CG  
1733  C CD1 . PHE A 221 ? 0.7309 0.6090 0.5957 0.1503  0.0433  0.0433  522 PHE A CD1 
1734  C CD2 . PHE A 221 ? 0.8183 0.7073 0.6684 0.1833  0.0402  0.0361  522 PHE A CD2 
1735  C CE1 . PHE A 221 ? 0.7720 0.6562 0.6362 0.1552  0.0424  0.0472  522 PHE A CE1 
1736  C CE2 . PHE A 221 ? 0.8213 0.7169 0.6709 0.1885  0.0390  0.0402  522 PHE A CE2 
1737  C CZ  . PHE A 221 ? 0.7922 0.6848 0.6486 0.1740  0.0401  0.0458  522 PHE A CZ  
1738  N N   . ASP A 222 ? 0.6911 0.4883 0.5231 0.1405  0.0420  0.0289  523 ASP A N   
1739  C CA  . ASP A 222 ? 0.6682 0.4607 0.5008 0.1328  0.0420  0.0241  523 ASP A CA  
1740  C C   . ASP A 222 ? 0.7243 0.5313 0.5744 0.1136  0.0438  0.0270  523 ASP A C   
1741  O O   . ASP A 222 ? 0.7431 0.5364 0.5940 0.1020  0.0441  0.0315  523 ASP A O   
1742  C CB  . ASP A 222 ? 0.6763 0.4270 0.4887 0.1329  0.0399  0.0222  523 ASP A CB  
1743  C CG  . ASP A 222 ? 0.7514 0.4821 0.5437 0.1528  0.0378  0.0201  523 ASP A CG  
1744  O OD1 . ASP A 222 ? 0.8452 0.5986 0.6399 0.1681  0.0377  0.0184  523 ASP A OD1 
1745  O OD2 . ASP A 222 ? 0.8000 0.4920 0.5734 0.1531  0.0360  0.0200  523 ASP A OD2 
1746  N N   . VAL A 223 ? 0.6482 0.4831 0.5115 0.1106  0.0451  0.0246  524 VAL A N   
1747  C CA  . VAL A 223 ? 0.6019 0.4478 0.4793 0.0939  0.0463  0.0268  524 VAL A CA  
1748  C C   . VAL A 223 ? 0.6172 0.4378 0.4873 0.0844  0.0448  0.0251  524 VAL A C   
1749  O O   . VAL A 223 ? 0.5681 0.3740 0.4264 0.0897  0.0432  0.0197  524 VAL A O   
1750  C CB  . VAL A 223 ? 0.5744 0.4505 0.4635 0.0934  0.0478  0.0245  524 VAL A CB  
1751  C CG1 . VAL A 223 ? 0.5503 0.4341 0.4513 0.0777  0.0485  0.0268  524 VAL A CG1 
1752  C CG2 . VAL A 223 ? 0.4822 0.3847 0.3792 0.1010  0.0493  0.0259  524 VAL A CG2 
1753  N N   . LEU A 224 ? 0.6196 0.4354 0.4961 0.0708  0.0452  0.0290  525 LEU A N   
1754  C CA  . LEU A 224 ? 0.6667 0.4594 0.5362 0.0613  0.0437  0.0271  525 LEU A CA  
1755  C C   . LEU A 224 ? 0.6655 0.4701 0.5413 0.0552  0.0429  0.0228  525 LEU A C   
1756  O O   . LEU A 224 ? 0.5738 0.4038 0.4608 0.0556  0.0441  0.0232  525 LEU A O   
1757  C CB  . LEU A 224 ? 0.6885 0.4741 0.5625 0.0489  0.0445  0.0325  525 LEU A CB  
1758  C CG  . LEU A 224 ? 0.6614 0.4232 0.5229 0.0520  0.0448  0.0364  525 LEU A CG  
1759  C CD1 . LEU A 224 ? 0.6601 0.4294 0.5310 0.0426  0.0468  0.0428  525 LEU A CD1 
1760  C CD2 . LEU A 224 ? 0.6827 0.4103 0.5274 0.0482  0.0432  0.0339  525 LEU A CD2 
1761  N N   . PRO A 225 ? 0.6637 0.4496 0.5313 0.0495  0.0408  0.0185  526 PRO A N   
1762  C CA  . PRO A 225 ? 0.6386 0.4365 0.5122 0.0431  0.0397  0.0147  526 PRO A CA  
1763  C C   . PRO A 225 ? 0.5721 0.3804 0.4591 0.0290  0.0400  0.0184  526 PRO A C   
1764  O O   . PRO A 225 ? 0.6632 0.4624 0.5516 0.0216  0.0405  0.0221  526 PRO A O   
1765  C CB  . PRO A 225 ? 0.5931 0.3653 0.4514 0.0428  0.0368  0.0081  526 PRO A CB  
1766  C CG  . PRO A 225 ? 0.6223 0.3672 0.4709 0.0403  0.0367  0.0107  526 PRO A CG  
1767  C CD  . PRO A 225 ? 0.6351 0.3873 0.4854 0.0503  0.0391  0.0161  526 PRO A CD  
1768  N N   . LEU A 226 ? 0.4854 0.3135 0.3814 0.0258  0.0397  0.0174  527 LEU A N   
1769  C CA  . LEU A 226 ? 0.5361 0.3731 0.4430 0.0137  0.0391  0.0195  527 LEU A CA  
1770  C C   . LEU A 226 ? 0.6621 0.4827 0.5633 0.0048  0.0363  0.0151  527 LEU A C   
1771  O O   . LEU A 226 ? 0.7009 0.5082 0.5908 0.0076  0.0343  0.0092  527 LEU A O   
1772  C CB  . LEU A 226 ? 0.5539 0.4135 0.4694 0.0137  0.0390  0.0196  527 LEU A CB  
1773  C CG  . LEU A 226 ? 0.6431 0.5203 0.5666 0.0185  0.0419  0.0246  527 LEU A CG  
1774  C CD1 . LEU A 226 ? 0.6416 0.5374 0.5706 0.0183  0.0421  0.0251  527 LEU A CD1 
1775  C CD2 . LEU A 226 ? 0.5633 0.4427 0.4954 0.0130  0.0431  0.0298  527 LEU A CD2 
1776  N N   . LEU A 227 ? 0.6904 0.5124 0.5990 -0.0062 0.0364  0.0178  528 LEU A N   
1777  C CA  . LEU A 227 ? 0.6508 0.4620 0.5570 -0.0176 0.0341  0.0141  528 LEU A CA  
1778  C C   . LEU A 227 ? 0.6606 0.4942 0.5810 -0.0254 0.0332  0.0151  528 LEU A C   
1779  O O   . LEU A 227 ? 0.6367 0.4801 0.5667 -0.0292 0.0351  0.0201  528 LEU A O   
1780  C CB  . LEU A 227 ? 0.6763 0.4678 0.5771 -0.0239 0.0356  0.0169  528 LEU A CB  
1781  C CG  . LEU A 227 ? 0.6726 0.4364 0.5591 -0.0297 0.0337  0.0121  528 LEU A CG  
1782  C CD1 . LEU A 227 ? 0.5831 0.3363 0.4699 -0.0424 0.0354  0.0157  528 LEU A CD1 
1783  C CD2 . LEU A 227 ? 0.7161 0.4829 0.6014 -0.0339 0.0297  0.0041  528 LEU A CD2 
1784  N N   . LEU A 228 ? 0.5455 0.3871 0.4663 -0.0267 0.0301  0.0100  529 LEU A N   
1785  C CA  . LEU A 228 ? 0.5767 0.4414 0.5094 -0.0294 0.0289  0.0112  529 LEU A CA  
1786  C C   . LEU A 228 ? 0.6009 0.4688 0.5360 -0.0397 0.0253  0.0061  529 LEU A C   
1787  O O   . LEU A 228 ? 0.4891 0.3463 0.4153 -0.0418 0.0225  -0.0004 529 LEU A O   
1788  C CB  . LEU A 228 ? 0.5174 0.3938 0.4492 -0.0201 0.0285  0.0109  529 LEU A CB  
1789  C CG  . LEU A 228 ? 0.4662 0.3433 0.3972 -0.0110 0.0321  0.0156  529 LEU A CG  
1790  C CD1 . LEU A 228 ? 0.4963 0.3857 0.4259 -0.0036 0.0322  0.0154  529 LEU A CD1 
1791  C CD2 . LEU A 228 ? 0.4672 0.3528 0.4087 -0.0133 0.0345  0.0220  529 LEU A CD2 
1792  N N   . GLN A 229 ? 0.5208 0.4048 0.4679 -0.0459 0.0252  0.0085  530 GLN A N   
1793  C CA  . GLN A 229 ? 0.6130 0.5055 0.5650 -0.0563 0.0219  0.0039  530 GLN A CA  
1794  C C   . GLN A 229 ? 0.5654 0.4825 0.5269 -0.0533 0.0196  0.0044  530 GLN A C   
1795  O O   . GLN A 229 ? 0.4664 0.3949 0.4359 -0.0499 0.0215  0.0098  530 GLN A O   
1796  C CB  . GLN A 229 ? 0.5676 0.4578 0.5248 -0.0671 0.0242  0.0061  530 GLN A CB  
1797  C CG  . GLN A 229 ? 0.5390 0.4486 0.5066 -0.0771 0.0216  0.0029  530 GLN A CG  
1798  C CD  . GLN A 229 ? 0.6716 0.5790 0.6434 -0.0891 0.0245  0.0048  530 GLN A CD  
1799  O OE1 . GLN A 229 ? 0.6931 0.5945 0.6651 -0.0874 0.0287  0.0110  530 GLN A OE1 
1800  N NE2 . GLN A 229 ? 0.6924 0.6052 0.6669 -0.1018 0.0222  -0.0005 530 GLN A NE2 
1801  N N   . ALA A 230 ? 0.5350 0.4591 0.4945 -0.0542 0.0151  -0.0016 531 ALA A N   
1802  C CA  . ALA A 230 ? 0.5849 0.5309 0.5510 -0.0506 0.0120  -0.0015 531 ALA A CA  
1803  C C   . ALA A 230 ? 0.6056 0.5650 0.5777 -0.0600 0.0078  -0.0075 531 ALA A C   
1804  O O   . ALA A 230 ? 0.5733 0.5245 0.5395 -0.0667 0.0052  -0.0143 531 ALA A O   
1805  C CB  . ALA A 230 ? 0.6564 0.6023 0.6138 -0.0411 0.0102  -0.0028 531 ALA A CB  
1806  N N   . ASN A 231 ? 0.6188 0.5989 0.6023 -0.0605 0.0070  -0.0055 532 ASN A N   
1807  C CA  . ASN A 231 ? 0.6481 0.6485 0.6392 -0.0673 0.0024  -0.0112 532 ASN A CA  
1808  C C   . ASN A 231 ? 0.6307 0.6268 0.6243 -0.0825 0.0029  -0.0157 532 ASN A C   
1809  O O   . ASN A 231 ? 0.6593 0.6664 0.6554 -0.0905 -0.0013 -0.0228 532 ASN A O   
1810  C CB  . ASN A 231 ? 0.6979 0.7045 0.6827 -0.0627 -0.0032 -0.0168 532 ASN A CB  
1811  C CG  . ASN A 231 ? 0.7908 0.8249 0.7840 -0.0601 -0.0080 -0.0187 532 ASN A CG  
1812  O OD1 . ASN A 231 ? 0.8343 0.8773 0.8297 -0.0499 -0.0079 -0.0134 532 ASN A OD1 
1813  N ND2 . ASN A 231 ? 0.8670 0.9145 0.8643 -0.0690 -0.0124 -0.0265 532 ASN A ND2 
1814  N N   . GLY A 232 ? 0.6566 0.6371 0.6493 -0.0871 0.0081  -0.0114 533 GLY A N   
1815  C CA  . GLY A 232 ? 0.5737 0.5476 0.5673 -0.1024 0.0094  -0.0142 533 GLY A CA  
1816  C C   . GLY A 232 ? 0.6039 0.5530 0.5842 -0.1085 0.0079  -0.0198 533 GLY A C   
1817  O O   . GLY A 232 ? 0.6392 0.5792 0.6182 -0.1226 0.0087  -0.0225 533 GLY A O   
1818  N N   . ASN A 233 ? 0.6095 0.5472 0.5793 -0.0987 0.0058  -0.0219 534 ASN A N   
1819  C CA  . ASN A 233 ? 0.5920 0.5041 0.5476 -0.1025 0.0043  -0.0277 534 ASN A CA  
1820  C C   . ASN A 233 ? 0.6611 0.5445 0.6073 -0.1018 0.0094  -0.0227 534 ASN A C   
1821  O O   . ASN A 233 ? 0.5499 0.4347 0.5007 -0.0975 0.0139  -0.0148 534 ASN A O   
1822  C CB  . ASN A 233 ? 0.6398 0.5512 0.5868 -0.0913 0.0007  -0.0318 534 ASN A CB  
1823  C CG  . ASN A 233 ? 0.6413 0.5784 0.5948 -0.0928 -0.0051 -0.0377 534 ASN A CG  
1824  O OD1 . ASN A 233 ? 0.6466 0.5927 0.6052 -0.1055 -0.0081 -0.0435 534 ASN A OD1 
1825  N ND2 . ASN A 233 ? 0.6094 0.5595 0.5628 -0.0802 -0.0067 -0.0358 534 ASN A ND2 
1826  N N   . ASP A 234 ? 0.6888 0.5454 0.6208 -0.1060 0.0083  -0.0278 535 ASP A N   
1827  C CA  . ASP A 234 ? 0.7477 0.5747 0.6681 -0.1032 0.0124  -0.0235 535 ASP A CA  
1828  C C   . ASP A 234 ? 0.6976 0.5249 0.6155 -0.0855 0.0146  -0.0185 535 ASP A C   
1829  O O   . ASP A 234 ? 0.7752 0.6154 0.6939 -0.0764 0.0122  -0.0207 535 ASP A O   
1830  C CB  . ASP A 234 ? 0.8205 0.6168 0.7237 -0.1084 0.0100  -0.0308 535 ASP A CB  
1831  C CG  . ASP A 234 ? 0.7382 0.5304 0.6426 -0.1286 0.0085  -0.0354 535 ASP A CG  
1832  O OD1 . ASP A 234 ? 0.7180 0.5270 0.6352 -0.1385 0.0109  -0.0312 535 ASP A OD1 
1833  O OD2 . ASP A 234 ? 0.8139 0.5865 0.7062 -0.1349 0.0049  -0.0436 535 ASP A OD2 
1834  N N   . PRO A 235 ? 0.7404 0.5560 0.6559 -0.0807 0.0191  -0.0114 536 PRO A N   
1835  C CA  . PRO A 235 ? 0.6606 0.4787 0.5746 -0.0650 0.0212  -0.0070 536 PRO A CA  
1836  C C   . PRO A 235 ? 0.6121 0.4102 0.5102 -0.0557 0.0198  -0.0118 536 PRO A C   
1837  O O   . PRO A 235 ? 0.6020 0.3767 0.4878 -0.0605 0.0180  -0.0171 536 PRO A O   
1838  C CB  . PRO A 235 ? 0.6835 0.4950 0.5992 -0.0643 0.0260  0.0011  536 PRO A CB  
1839  C CG  . PRO A 235 ? 0.6715 0.4621 0.5803 -0.0771 0.0265  -0.0001 536 PRO A CG  
1840  C CD  . PRO A 235 ? 0.7109 0.5134 0.6257 -0.0899 0.0228  -0.0066 536 PRO A CD  
1841  N N   . GLU A 236 ? 0.6230 0.4306 0.5210 -0.0422 0.0207  -0.0100 537 GLU A N   
1842  C CA  . GLU A 236 ? 0.5372 0.3318 0.4214 -0.0315 0.0196  -0.0149 537 GLU A CA  
1843  C C   . GLU A 236 ? 0.5228 0.3159 0.4045 -0.0184 0.0234  -0.0096 537 GLU A C   
1844  O O   . GLU A 236 ? 0.5863 0.3962 0.4790 -0.0161 0.0261  -0.0028 537 GLU A O   
1845  C CB  . GLU A 236 ? 0.5783 0.3905 0.4637 -0.0282 0.0163  -0.0199 537 GLU A CB  
1846  C CG  . GLU A 236 ? 0.6098 0.4266 0.4977 -0.0403 0.0117  -0.0262 537 GLU A CG  
1847  C CD  . GLU A 236 ? 0.7126 0.5529 0.6050 -0.0369 0.0088  -0.0287 537 GLU A CD  
1848  O OE1 . GLU A 236 ? 0.7697 0.6144 0.6566 -0.0254 0.0095  -0.0288 537 GLU A OE1 
1849  O OE2 . GLU A 236 ? 0.7422 0.5980 0.6435 -0.0453 0.0059  -0.0303 537 GLU A OE2 
1850  N N   . LEU A 237 ? 0.5820 0.3553 0.4487 -0.0094 0.0232  -0.0132 538 LEU A N   
1851  C CA  . LEU A 237 ? 0.5936 0.3662 0.4570 0.0040  0.0263  -0.0094 538 LEU A CA  
1852  C C   . LEU A 237 ? 0.6981 0.4916 0.5638 0.0145  0.0269  -0.0104 538 LEU A C   
1853  O O   . LEU A 237 ? 0.7794 0.5777 0.6415 0.0149  0.0244  -0.0162 538 LEU A O   
1854  C CB  . LEU A 237 ? 0.6055 0.3471 0.4508 0.0105  0.0258  -0.0127 538 LEU A CB  
1855  C CG  . LEU A 237 ? 0.7098 0.4267 0.5498 0.0010  0.0261  -0.0102 538 LEU A CG  
1856  C CD1 . LEU A 237 ? 0.7930 0.4754 0.6117 0.0078  0.0247  -0.0147 538 LEU A CD1 
1857  C CD2 . LEU A 237 ? 0.6247 0.3502 0.4742 0.0009  0.0299  -0.0008 538 LEU A CD2 
1858  N N   . PHE A 238 ? 0.6410 0.4482 0.5128 0.0223  0.0304  -0.0047 539 PHE A N   
1859  C CA  . PHE A 238 ? 0.6022 0.4298 0.4761 0.0319  0.0322  -0.0044 539 PHE A CA  
1860  C C   . PHE A 238 ? 0.6922 0.5235 0.5668 0.0415  0.0355  -0.0001 539 PHE A C   
1861  O O   . PHE A 238 ? 0.5867 0.4184 0.4685 0.0380  0.0371  0.0057  539 PHE A O   
1862  C CB  . PHE A 238 ? 0.4963 0.3484 0.3835 0.0262  0.0328  -0.0003 539 PHE A CB  
1863  C CG  . PHE A 238 ? 0.5604 0.4137 0.4494 0.0170  0.0294  -0.0034 539 PHE A CG  
1864  C CD1 . PHE A 238 ? 0.6057 0.4638 0.4883 0.0196  0.0271  -0.0089 539 PHE A CD1 
1865  C CD2 . PHE A 238 ? 0.7055 0.5577 0.6028 0.0060  0.0283  -0.0010 539 PHE A CD2 
1866  C CE1 . PHE A 238 ? 0.7368 0.5979 0.6211 0.0116  0.0234  -0.0121 539 PHE A CE1 
1867  C CE2 . PHE A 238 ? 0.7421 0.5986 0.6419 -0.0021 0.0248  -0.0043 539 PHE A CE2 
1868  C CZ  . PHE A 238 ? 0.7892 0.6502 0.6827 0.0007  0.0221  -0.0098 539 PHE A CZ  
1869  N N   . GLN A 239 ? 0.6466 0.4834 0.5144 0.0539  0.0366  -0.0032 540 GLN A N   
1870  C CA  . GLN A 239 ? 0.7011 0.5461 0.5702 0.0641  0.0395  -0.0001 540 GLN A CA  
1871  C C   . GLN A 239 ? 0.6857 0.5610 0.5676 0.0633  0.0426  0.0043  540 GLN A C   
1872  O O   . GLN A 239 ? 0.6273 0.5163 0.5084 0.0654  0.0431  0.0019  540 GLN A O   
1873  C CB  . GLN A 239 ? 0.7255 0.5616 0.5799 0.0789  0.0391  -0.0063 540 GLN A CB  
1874  C CG  . GLN A 239 ? 0.8561 0.7078 0.7127 0.0913  0.0420  -0.0042 540 GLN A CG  
1875  C CD  . GLN A 239 ? 1.0456 0.9142 0.8974 0.1033  0.0433  -0.0093 540 GLN A CD  
1876  O OE1 . GLN A 239 ? 1.1534 1.0422 1.0112 0.0994  0.0448  -0.0092 540 GLN A OE1 
1877  N NE2 . GLN A 239 ? 1.0256 0.8863 0.8658 0.1184  0.0429  -0.0136 540 GLN A NE2 
1878  N N   . ILE A 240 ? 0.6187 0.5033 0.5114 0.0597  0.0445  0.0107  541 ILE A N   
1879  C CA  . ILE A 240 ? 0.6275 0.5386 0.5312 0.0585  0.0475  0.0148  541 ILE A CA  
1880  C C   . ILE A 240 ? 0.6250 0.5505 0.5246 0.0703  0.0497  0.0119  541 ILE A C   
1881  O O   . ILE A 240 ? 0.6239 0.5420 0.5163 0.0809  0.0494  0.0093  541 ILE A O   
1882  C CB  . ILE A 240 ? 0.5599 0.4770 0.4744 0.0540  0.0488  0.0210  541 ILE A CB  
1883  C CG1 . ILE A 240 ? 0.5704 0.4751 0.4890 0.0432  0.0470  0.0235  541 ILE A CG1 
1884  C CG2 . ILE A 240 ? 0.4790 0.4206 0.4036 0.0513  0.0516  0.0247  541 ILE A CG2 
1885  C CD1 . ILE A 240 ? 0.5221 0.4294 0.4488 0.0402  0.0481  0.0288  541 ILE A CD1 
1886  N N   . PRO A 241 ? 0.6089 0.5547 0.5117 0.0697  0.0519  0.0123  542 PRO A N   
1887  C CA  . PRO A 241 ? 0.6069 0.5704 0.5066 0.0804  0.0546  0.0095  542 PRO A CA  
1888  C C   . PRO A 241 ? 0.5300 0.5070 0.4368 0.0848  0.0567  0.0122  542 PRO A C   
1889  O O   . PRO A 241 ? 0.4612 0.4484 0.3793 0.0764  0.0581  0.0178  542 PRO A O   
1890  C CB  . PRO A 241 ? 0.5127 0.4957 0.4163 0.0746  0.0570  0.0115  542 PRO A CB  
1891  C CG  . PRO A 241 ? 0.5296 0.4979 0.4319 0.0653  0.0540  0.0121  542 PRO A CG  
1892  C CD  . PRO A 241 ? 0.5490 0.5017 0.4565 0.0597  0.0518  0.0149  542 PRO A CD  
1893  N N   . PRO A 242 ? 0.4803 0.4575 0.3801 0.0985  0.0567  0.0080  543 PRO A N   
1894  C CA  . PRO A 242 ? 0.5818 0.5698 0.4871 0.1042  0.0577  0.0100  543 PRO A CA  
1895  C C   . PRO A 242 ? 0.6409 0.6606 0.5597 0.0988  0.0614  0.0137  543 PRO A C   
1896  O O   . PRO A 242 ? 0.6181 0.6452 0.5452 0.0964  0.0616  0.0171  543 PRO A O   
1897  C CB  . PRO A 242 ? 0.5424 0.5277 0.4357 0.1220  0.0569  0.0036  543 PRO A CB  
1898  C CG  . PRO A 242 ? 0.5839 0.5420 0.4637 0.1234  0.0541  -0.0009 543 PRO A CG  
1899  C CD  . PRO A 242 ? 0.5780 0.5413 0.4627 0.1103  0.0549  0.0007  543 PRO A CD  
1900  N N   . GLU A 243 ? 0.4473 0.4854 0.3675 0.0963  0.0642  0.0131  544 GLU A N   
1901  C CA  . GLU A 243 ? 0.4459 0.5128 0.3778 0.0889  0.0682  0.0169  544 GLU A CA  
1902  C C   . GLU A 243 ? 0.4610 0.5226 0.4019 0.0735  0.0679  0.0234  544 GLU A C   
1903  O O   . GLU A 243 ? 0.5113 0.5926 0.4617 0.0660  0.0707  0.0269  544 GLU A O   
1904  C CB  . GLU A 243 ? 0.5150 0.6001 0.4442 0.0888  0.0716  0.0154  544 GLU A CB  
1905  C CG  . GLU A 243 ? 0.4216 0.4916 0.3453 0.0809  0.0706  0.0168  544 GLU A CG  
1906  C CD  . GLU A 243 ? 0.5441 0.5946 0.4542 0.0902  0.0676  0.0104  544 GLU A CD  
1907  O OE1 . GLU A 243 ? 0.5708 0.6121 0.4748 0.1021  0.0656  0.0056  544 GLU A OE1 
1908  O OE2 . GLU A 243 ? 0.7049 0.7488 0.6095 0.0860  0.0669  0.0100  544 GLU A OE2 
1909  N N   . LEU A 244 ? 0.4508 0.4872 0.3888 0.0684  0.0647  0.0247  545 LEU A N   
1910  C CA  . LEU A 244 ? 0.4168 0.4478 0.3627 0.0558  0.0641  0.0302  545 LEU A CA  
1911  C C   . LEU A 244 ? 0.4036 0.4267 0.3541 0.0559  0.0623  0.0318  545 LEU A C   
1912  O O   . LEU A 244 ? 0.4462 0.4674 0.4038 0.0465  0.0620  0.0359  545 LEU A O   
1913  C CB  . LEU A 244 ? 0.3753 0.3873 0.3166 0.0497  0.0616  0.0307  545 LEU A CB  
1914  C CG  . LEU A 244 ? 0.5042 0.5205 0.4410 0.0466  0.0626  0.0307  545 LEU A CG  
1915  C CD1 . LEU A 244 ? 0.3787 0.3767 0.3134 0.0404  0.0591  0.0315  545 LEU A CD1 
1916  C CD2 . LEU A 244 ? 0.4095 0.4457 0.3517 0.0398  0.0664  0.0352  545 LEU A CD2 
1917  N N   . VAL A 245 ? 0.3772 0.3953 0.3229 0.0668  0.0611  0.0287  546 VAL A N   
1918  C CA  . VAL A 245 ? 0.5305 0.5398 0.4783 0.0679  0.0593  0.0305  546 VAL A CA  
1919  C C   . VAL A 245 ? 0.5759 0.6090 0.5302 0.0729  0.0609  0.0304  546 VAL A C   
1920  O O   . VAL A 245 ? 0.5419 0.5834 0.4916 0.0852  0.0611  0.0267  546 VAL A O   
1921  C CB  . VAL A 245 ? 0.5590 0.5434 0.4951 0.0764  0.0566  0.0280  546 VAL A CB  
1922  C CG1 . VAL A 245 ? 0.5551 0.5304 0.4923 0.0771  0.0553  0.0309  546 VAL A CG1 
1923  C CG2 . VAL A 245 ? 0.5202 0.4836 0.4504 0.0704  0.0550  0.0272  546 VAL A CG2 
1924  N N   . LEU A 246 ? 0.3574 0.4024 0.3222 0.0637  0.0618  0.0338  547 LEU A N   
1925  C CA  . LEU A 246 ? 0.4238 0.4938 0.3957 0.0669  0.0630  0.0331  547 LEU A CA  
1926  C C   . LEU A 246 ? 0.4642 0.5264 0.4342 0.0742  0.0604  0.0332  547 LEU A C   
1927  O O   . LEU A 246 ? 0.5428 0.5861 0.5119 0.0695  0.0587  0.0360  547 LEU A O   
1928  C CB  . LEU A 246 ? 0.4019 0.4872 0.3847 0.0531  0.0649  0.0361  547 LEU A CB  
1929  C CG  . LEU A 246 ? 0.4081 0.5197 0.4002 0.0523  0.0659  0.0354  547 LEU A CG  
1930  C CD1 . LEU A 246 ? 0.4449 0.5806 0.4366 0.0627  0.0676  0.0313  547 LEU A CD1 
1931  C CD2 . LEU A 246 ? 0.4906 0.6118 0.4909 0.0369  0.0679  0.0384  547 LEU A CD2 
1932  N N   . GLU A 247 ? 0.4341 0.5115 0.4028 0.0865  0.0602  0.0301  548 GLU A N   
1933  C CA  . GLU A 247 ? 0.4996 0.5694 0.4639 0.0961  0.0575  0.0303  548 GLU A CA  
1934  C C   . GLU A 247 ? 0.5395 0.6402 0.5119 0.1009  0.0576  0.0285  548 GLU A C   
1935  O O   . GLU A 247 ? 0.4810 0.6089 0.4590 0.1024  0.0598  0.0256  548 GLU A O   
1936  C CB  . GLU A 247 ? 0.5418 0.5912 0.4910 0.1109  0.0557  0.0278  548 GLU A CB  
1937  C CG  . GLU A 247 ? 0.5396 0.5568 0.4797 0.1064  0.0549  0.0289  548 GLU A CG  
1938  C CD  . GLU A 247 ? 0.5847 0.5799 0.5086 0.1204  0.0530  0.0260  548 GLU A CD  
1939  O OE1 . GLU A 247 ? 0.6290 0.6361 0.5484 0.1333  0.0532  0.0216  548 GLU A OE1 
1940  O OE2 . GLU A 247 ? 0.7040 0.6695 0.6189 0.1188  0.0513  0.0281  548 GLU A OE2 
1941  N N   . VAL A 248 ? 0.4516 0.5491 0.4242 0.1034  0.0553  0.0301  549 VAL A N   
1942  C CA  . VAL A 248 ? 0.4331 0.5595 0.4138 0.1068  0.0546  0.0284  549 VAL A CA  
1943  C C   . VAL A 248 ? 0.5331 0.6546 0.5035 0.1251  0.0516  0.0271  549 VAL A C   
1944  O O   . VAL A 248 ? 0.4948 0.5920 0.4572 0.1274  0.0495  0.0304  549 VAL A O   
1945  C CB  . VAL A 248 ? 0.4341 0.5633 0.4240 0.0933  0.0541  0.0311  549 VAL A CB  
1946  C CG1 . VAL A 248 ? 0.4333 0.5935 0.4314 0.0967  0.0528  0.0284  549 VAL A CG1 
1947  C CG2 . VAL A 248 ? 0.4188 0.5479 0.4164 0.0760  0.0566  0.0329  549 VAL A CG2 
1948  N N   . PRO A 249 ? 0.4876 0.6317 0.4574 0.1389  0.0513  0.0227  550 PRO A N   
1949  C CA  . PRO A 249 ? 0.5208 0.6622 0.4805 0.1578  0.0479  0.0216  550 PRO A CA  
1950  C C   . PRO A 249 ? 0.5458 0.7036 0.5130 0.1555  0.0458  0.0227  550 PRO A C   
1951  O O   . PRO A 249 ? 0.4466 0.6362 0.4285 0.1466  0.0468  0.0207  550 PRO A O   
1952  C CB  . PRO A 249 ? 0.4034 0.5709 0.3627 0.1724  0.0484  0.0158  550 PRO A CB  
1953  C CG  . PRO A 249 ? 0.3927 0.5896 0.3676 0.1576  0.0524  0.0140  550 PRO A CG  
1954  C CD  . PRO A 249 ? 0.3824 0.5575 0.3605 0.1378  0.0543  0.0187  550 PRO A CD  
1955  N N   . ILE A 250 ? 0.5654 0.7007 0.5216 0.1629  0.0429  0.0260  551 ILE A N   
1956  C CA  . ILE A 250 ? 0.5100 0.6563 0.4714 0.1602  0.0407  0.0275  551 ILE A CA  
1957  C C   . ILE A 250 ? 0.5405 0.7144 0.5011 0.1779  0.0376  0.0236  551 ILE A C   
1958  O O   . ILE A 250 ? 0.5472 0.7074 0.4926 0.1966  0.0353  0.0238  551 ILE A O   
1959  C CB  . ILE A 250 ? 0.5182 0.6288 0.4682 0.1585  0.0395  0.0334  551 ILE A CB  
1960  C CG1 . ILE A 250 ? 0.5394 0.6247 0.4902 0.1423  0.0423  0.0367  551 ILE A CG1 
1961  C CG2 . ILE A 250 ? 0.5241 0.6480 0.4800 0.1546  0.0375  0.0345  551 ILE A CG2 
1962  C CD1 . ILE A 250 ? 0.5355 0.6399 0.5029 0.1250  0.0447  0.0351  551 ILE A CD1 
1963  N N   . ARG A 251 ? 0.4960 0.7084 0.4721 0.1722  0.0374  0.0200  552 ARG A N   
1964  C CA  . ARG A 251 ? 0.5428 0.7862 0.5204 0.1871  0.0339  0.0159  552 ARG A CA  
1965  C C   . ARG A 251 ? 0.4702 0.7293 0.4573 0.1773  0.0318  0.0161  552 ARG A C   
1966  O O   . ARG A 251 ? 0.4840 0.7320 0.4772 0.1590  0.0335  0.0186  552 ARG A O   
1967  C CB  . ARG A 251 ? 0.4383 0.7216 0.4265 0.1914  0.0354  0.0095  552 ARG A CB  
1968  C CG  . ARG A 251 ? 0.5457 0.8524 0.5522 0.1693  0.0393  0.0077  552 ARG A CG  
1969  C CD  . ARG A 251 ? 0.5158 0.7995 0.5207 0.1580  0.0438  0.0103  552 ARG A CD  
1970  N NE  . ARG A 251 ? 0.5345 0.8460 0.5553 0.1405  0.0476  0.0082  552 ARG A NE  
1971  C CZ  . ARG A 251 ? 0.6083 0.9081 0.6311 0.1270  0.0516  0.0103  552 ARG A CZ  
1972  N NH1 . ARG A 251 ? 0.6463 0.9724 0.6823 0.1116  0.0550  0.0088  552 ARG A NH1 
1973  N NH2 . ARG A 251 ? 0.5406 0.8028 0.5517 0.1283  0.0523  0.0139  552 ARG A NH2 
1974  N N   . HIS A 252 ? 0.4841 0.7692 0.4716 0.1906  0.0279  0.0128  553 HIS A N   
1975  C CA  . HIS A 252 ? 0.5156 0.8161 0.5102 0.1838  0.0250  0.0121  553 HIS A CA  
1976  C C   . HIS A 252 ? 0.5148 0.8672 0.5263 0.1818  0.0238  0.0047  553 HIS A C   
1977  O O   . HIS A 252 ? 0.5450 0.9228 0.5568 0.1971  0.0228  0.0004  553 HIS A O   
1978  C CB  . HIS A 252 ? 0.4871 0.7703 0.4651 0.2009  0.0206  0.0156  553 HIS A CB  
1979  C CG  . HIS A 252 ? 0.5355 0.8272 0.5177 0.1937  0.0179  0.0157  553 HIS A CG  
1980  N ND1 . HIS A 252 ? 0.5644 0.8979 0.5576 0.1956  0.0144  0.0096  553 HIS A ND1 
1981  C CD2 . HIS A 252 ? 0.5600 0.8246 0.5363 0.1853  0.0180  0.0208  553 HIS A CD2 
1982  C CE1 . HIS A 252 ? 0.5672 0.8976 0.5606 0.1885  0.0122  0.0107  553 HIS A CE1 
1983  N NE2 . HIS A 252 ? 0.5417 0.8308 0.5248 0.1825  0.0145  0.0175  553 HIS A NE2 
1984  N N   . PRO A 253 ? 0.5338 0.9035 0.5593 0.1631  0.0239  0.0025  554 PRO A N   
1985  C CA  . PRO A 253 ? 0.4885 0.9081 0.5314 0.1570  0.0234  -0.0049 554 PRO A CA  
1986  C C   . PRO A 253 ? 0.5336 0.9862 0.5764 0.1753  0.0180  -0.0098 554 PRO A C   
1987  O O   . PRO A 253 ? 0.5934 1.0907 0.6490 0.1758  0.0176  -0.0164 554 PRO A O   
1988  C CB  . PRO A 253 ? 0.5085 0.9280 0.5621 0.1328  0.0242  -0.0053 554 PRO A CB  
1989  C CG  . PRO A 253 ? 0.5812 0.9632 0.6218 0.1354  0.0220  0.0002  554 PRO A CG  
1990  C CD  . PRO A 253 ? 0.6371 0.9826 0.6624 0.1472  0.0241  0.0062  554 PRO A CD  
1991  N N   . LYS A 254 ? 0.4872 0.9207 0.5155 0.1900  0.0137  -0.0066 555 LYS A N   
1992  C CA  . LYS A 254 ? 0.4563 0.9191 0.4823 0.2089  0.0078  -0.0107 555 LYS A CA  
1993  C C   . LYS A 254 ? 0.5626 1.0063 0.5685 0.2368  0.0054  -0.0074 555 LYS A C   
1994  O O   . LYS A 254 ? 0.6355 1.1096 0.6404 0.2561  0.0013  -0.0120 555 LYS A O   
1995  C CB  . LYS A 254 ? 0.6947 1.1573 0.7206 0.2029  0.0038  -0.0106 555 LYS A CB  
1996  C CG  . LYS A 254 ? 0.7708 1.2449 0.8136 0.1750  0.0057  -0.0137 555 LYS A CG  
1997  C CD  . LYS A 254 ? 0.8521 1.3733 0.9082 0.1716  0.0009  -0.0221 555 LYS A CD  
1998  C CE  . LYS A 254 ? 0.9039 1.4750 0.9735 0.1764  0.0008  -0.0295 555 LYS A CE  
1999  N NZ  . LYS A 254 ? 0.8664 1.4560 0.9540 0.1521  0.0058  -0.0329 555 LYS A NZ  
2000  N N   . PHE A 255 ? 0.5930 0.9873 0.5825 0.2396  0.0078  0.0000  556 PHE A N   
2001  C CA  . PHE A 255 ? 0.6291 0.9980 0.5967 0.2648  0.0055  0.0037  556 PHE A CA  
2002  C C   . PHE A 255 ? 0.6475 1.0150 0.6137 0.2720  0.0087  0.0017  556 PHE A C   
2003  O O   . PHE A 255 ? 0.6511 0.9887 0.6150 0.2610  0.0132  0.0052  556 PHE A O   
2004  C CB  . PHE A 255 ? 0.6756 0.9912 0.6249 0.2632  0.0062  0.0128  556 PHE A CB  
2005  C CG  . PHE A 255 ? 0.6099 0.9249 0.5553 0.2623  0.0027  0.0151  556 PHE A CG  
2006  C CD1 . PHE A 255 ? 0.6430 0.9949 0.5915 0.2747  -0.0028 0.0103  556 PHE A CD1 
2007  C CD2 . PHE A 255 ? 0.6152 0.8941 0.5539 0.2495  0.0047  0.0218  556 PHE A CD2 
2008  C CE1 . PHE A 255 ? 0.6079 0.9593 0.5518 0.2743  -0.0062 0.0122  556 PHE A CE1 
2009  C CE2 . PHE A 255 ? 0.5874 0.8662 0.5217 0.2491  0.0018  0.0239  556 PHE A CE2 
2010  C CZ  . PHE A 255 ? 0.5608 0.8751 0.4973 0.2616  -0.0038 0.0191  556 PHE A CZ  
2011  N N   . GLU A 256 ? 0.6908 1.0922 0.6580 0.2916  0.0060  -0.0042 557 GLU A N   
2012  C CA  . GLU A 256 ? 0.6958 1.1005 0.6614 0.3008  0.0087  -0.0072 557 GLU A CA  
2013  C C   . GLU A 256 ? 0.6416 0.9902 0.5841 0.3103  0.0098  -0.0010 557 GLU A C   
2014  O O   . GLU A 256 ? 0.6308 0.9656 0.5729 0.3055  0.0139  -0.0013 557 GLU A O   
2015  C CB  . GLU A 256 ? 0.8034 1.2515 0.7704 0.3250  0.0047  -0.0145 557 GLU A CB  
2016  C CG  . GLU A 256 ? 0.9519 1.4597 0.9443 0.3146  0.0066  -0.0228 557 GLU A CG  
2017  C CD  . GLU A 256 ? 1.1764 1.6929 1.1723 0.3161  0.0115  -0.0261 557 GLU A CD  
2018  O OE1 . GLU A 256 ? 1.2351 1.7152 1.2264 0.3039  0.0161  -0.0217 557 GLU A OE1 
2019  O OE2 . GLU A 256 ? 1.2327 1.7887 1.2334 0.3269  0.0101  -0.0330 557 GLU A OE2 
2020  N N   . TRP A 257 ? 0.6432 0.9587 0.5657 0.3231  0.0062  0.0047  558 TRP A N   
2021  C CA  . TRP A 257 ? 0.6840 0.9464 0.5819 0.3344  0.0065  0.0103  558 TRP A CA  
2022  C C   . TRP A 257 ? 0.6784 0.9007 0.5754 0.3120  0.0114  0.0160  558 TRP A C   
2023  O O   . TRP A 257 ? 0.7709 0.9504 0.6497 0.3178  0.0123  0.0197  558 TRP A O   
2024  C CB  . TRP A 257 ? 0.8148 1.0536 0.6909 0.3527  0.0014  0.0156  558 TRP A CB  
2025  C CG  . TRP A 257 ? 0.8084 1.0543 0.6910 0.3400  0.0001  0.0189  558 TRP A CG  
2026  C CD1 . TRP A 257 ? 0.8195 1.1089 0.7135 0.3436  -0.0039 0.0146  558 TRP A CD1 
2027  C CD2 . TRP A 257 ? 0.8686 1.0784 0.7467 0.3219  0.0025  0.0265  558 TRP A CD2 
2028  N NE1 . TRP A 257 ? 0.8415 1.1226 0.7375 0.3292  -0.0041 0.0189  558 TRP A NE1 
2029  C CE2 . TRP A 257 ? 0.8126 1.0458 0.6991 0.3161  0.0000  0.0263  558 TRP A CE2 
2030  C CE3 . TRP A 257 ? 0.8677 1.0298 0.7358 0.3101  0.0066  0.0330  558 TRP A CE3 
2031  C CZ2 . TRP A 257 ? 0.7579 0.9678 0.6425 0.2999  0.0015  0.0324  558 TRP A CZ2 
2032  C CZ3 . TRP A 257 ? 0.8304 0.9716 0.6978 0.2934  0.0083  0.0391  558 TRP A CZ3 
2033  C CH2 . TRP A 257 ? 0.7430 0.9079 0.6183 0.2891  0.0058  0.0389  558 TRP A CH2 
2034  N N   . PHE A 258 ? 0.6347 0.8688 0.5498 0.2872  0.0142  0.0165  559 PHE A N   
2035  C CA  . PHE A 258 ? 0.6123 0.8074 0.5248 0.2679  0.0179  0.0226  559 PHE A CA  
2036  C C   . PHE A 258 ? 0.6932 0.8714 0.6047 0.2630  0.0218  0.0216  559 PHE A C   
2037  O O   . PHE A 258 ? 0.6830 0.8183 0.5816 0.2588  0.0235  0.0266  559 PHE A O   
2038  C CB  . PHE A 258 ? 0.5211 0.7341 0.4525 0.2446  0.0195  0.0227  559 PHE A CB  
2039  C CG  . PHE A 258 ? 0.5953 0.7703 0.5217 0.2287  0.0219  0.0294  559 PHE A CG  
2040  C CD1 . PHE A 258 ? 0.4795 0.6339 0.4088 0.2142  0.0261  0.0309  559 PHE A CD1 
2041  C CD2 . PHE A 258 ? 0.5911 0.7528 0.5100 0.2286  0.0198  0.0342  559 PHE A CD2 
2042  C CE1 . PHE A 258 ? 0.5140 0.6365 0.4394 0.2003  0.0282  0.0367  559 PHE A CE1 
2043  C CE2 . PHE A 258 ? 0.5688 0.6986 0.4836 0.2143  0.0223  0.0401  559 PHE A CE2 
2044  C CZ  . PHE A 258 ? 0.4967 0.6074 0.4151 0.2003  0.0264  0.0412  559 PHE A CZ  
2045  N N   . LYS A 259 ? 0.6079 0.8205 0.5326 0.2634  0.0234  0.0150  560 LYS A N   
2046  C CA  . LYS A 259 ? 0.6535 0.8530 0.5761 0.2611  0.0269  0.0135  560 LYS A CA  
2047  C C   . LYS A 259 ? 0.6982 0.8588 0.5962 0.2805  0.0251  0.0150  560 LYS A C   
2048  O O   . LYS A 259 ? 0.6512 0.7814 0.5419 0.2750  0.0276  0.0162  560 LYS A O   
2049  C CB  . LYS A 259 ? 0.5617 0.8085 0.5003 0.2624  0.0287  0.0060  560 LYS A CB  
2050  C CG  . LYS A 259 ? 0.5682 0.8490 0.5054 0.2858  0.0249  0.0005  560 LYS A CG  
2051  C CD  . LYS A 259 ? 0.7278 1.0496 0.6769 0.2894  0.0275  -0.0070 560 LYS A CD  
2052  C CE  . LYS A 259 ? 0.7580 1.1202 0.7079 0.3127  0.0236  -0.0132 560 LYS A CE  
2053  N NZ  . LYS A 259 ? 0.7927 1.1853 0.7551 0.3072  0.0206  -0.0136 560 LYS A NZ  
2054  N N   . ASP A 260 ? 0.7232 0.8826 0.6072 0.3031  0.0206  0.0149  561 ASP A N   
2055  C CA  . ASP A 260 ? 0.7925 0.9118 0.6502 0.3232  0.0183  0.0166  561 ASP A CA  
2056  C C   . ASP A 260 ? 0.8131 0.8780 0.6546 0.3138  0.0190  0.0248  561 ASP A C   
2057  O O   . ASP A 260 ? 0.8344 0.8594 0.6535 0.3258  0.0178  0.0266  561 ASP A O   
2058  C CB  . ASP A 260 ? 0.8817 1.0146 0.7280 0.3501  0.0129  0.0149  561 ASP A CB  
2059  C CG  . ASP A 260 ? 1.0177 1.2085 0.8805 0.3602  0.0121  0.0062  561 ASP A CG  
2060  O OD1 . ASP A 260 ? 1.0731 1.2841 0.9490 0.3523  0.0158  0.0012  561 ASP A OD1 
2061  O OD2 . ASP A 260 ? 1.0699 1.2872 0.9326 0.3757  0.0078  0.0044  561 ASP A OD2 
2062  N N   . LEU A 261 ? 0.7205 0.7828 0.5722 0.2930  0.0208  0.0297  562 LEU A N   
2063  C CA  . LEU A 261 ? 0.6969 0.7115 0.5357 0.2817  0.0223  0.0369  562 LEU A CA  
2064  C C   . LEU A 261 ? 0.7938 0.7866 0.6322 0.2708  0.0256  0.0356  562 LEU A C   
2065  O O   . LEU A 261 ? 0.8504 0.7999 0.6737 0.2661  0.0264  0.0402  562 LEU A O   
2066  C CB  . LEU A 261 ? 0.6319 0.6532 0.4830 0.2628  0.0236  0.0414  562 LEU A CB  
2067  C CG  . LEU A 261 ? 0.5964 0.6351 0.4446 0.2746  0.0198  0.0429  562 LEU A CG  
2068  C CD1 . LEU A 261 ? 0.5652 0.6123 0.4250 0.2569  0.0208  0.0464  562 LEU A CD1 
2069  C CD2 . LEU A 261 ? 0.5983 0.6001 0.4184 0.2936  0.0169  0.0480  562 LEU A CD2 
2070  N N   . GLY A 262 ? 0.7078 0.7301 0.5617 0.2668  0.0276  0.0293  563 GLY A N   
2071  C CA  . GLY A 262 ? 0.8059 0.8119 0.6595 0.2581  0.0305  0.0273  563 GLY A CA  
2072  C C   . GLY A 262 ? 0.8449 0.8407 0.7095 0.2324  0.0338  0.0309  563 GLY A C   
2073  O O   . GLY A 262 ? 0.8262 0.7956 0.6849 0.2251  0.0354  0.0311  563 GLY A O   
2074  N N   . LEU A 263 ? 0.7781 0.7945 0.6583 0.2192  0.0346  0.0332  564 LEU A N   
2075  C CA  . LEU A 263 ? 0.6596 0.6638 0.5481 0.1970  0.0372  0.0372  564 LEU A CA  
2076  C C   . LEU A 263 ? 0.5818 0.6123 0.4894 0.1826  0.0402  0.0338  564 LEU A C   
2077  O O   . LEU A 263 ? 0.5441 0.6117 0.4644 0.1845  0.0404  0.0298  564 LEU A O   
2078  C CB  . LEU A 263 ? 0.6746 0.6819 0.5669 0.1907  0.0364  0.0419  564 LEU A CB  
2079  C CG  . LEU A 263 ? 0.7567 0.7394 0.6306 0.2023  0.0339  0.0469  564 LEU A CG  
2080  C CD1 . LEU A 263 ? 0.6106 0.6106 0.4930 0.1966  0.0331  0.0495  564 LEU A CD1 
2081  C CD2 . LEU A 263 ? 0.7533 0.6906 0.6115 0.1967  0.0351  0.0521  564 LEU A CD2 
2082  N N   . LYS A 264 ? 0.6184 0.6295 0.5273 0.1680  0.0424  0.0355  565 LYS A N   
2083  C CA  . LYS A 264 ? 0.6341 0.6631 0.5592 0.1519  0.0452  0.0341  565 LYS A CA  
2084  C C   . LYS A 264 ? 0.5485 0.5554 0.4753 0.1353  0.0463  0.0388  565 LYS A C   
2085  O O   . LYS A 264 ? 0.6937 0.6715 0.6089 0.1360  0.0455  0.0424  565 LYS A O   
2086  C CB  . LYS A 264 ? 0.5591 0.5910 0.4827 0.1549  0.0467  0.0297  565 LYS A CB  
2087  C CG  . LYS A 264 ? 0.6183 0.6125 0.5262 0.1569  0.0463  0.0301  565 LYS A CG  
2088  C CD  . LYS A 264 ? 0.6976 0.6975 0.6033 0.1618  0.0475  0.0248  565 LYS A CD  
2089  C CE  . LYS A 264 ? 0.7818 0.7504 0.6670 0.1757  0.0455  0.0224  565 LYS A CE  
2090  N NZ  . LYS A 264 ? 0.8189 0.7696 0.6998 0.1683  0.0464  0.0203  565 LYS A NZ  
2091  N N   . TRP A 265 ? 0.4314 0.4525 0.3724 0.1202  0.0483  0.0387  566 TRP A N   
2092  C CA  . TRP A 265 ? 0.5028 0.5048 0.4456 0.1055  0.0494  0.0421  566 TRP A CA  
2093  C C   . TRP A 265 ? 0.5971 0.6085 0.5487 0.0950  0.0515  0.0403  566 TRP A C   
2094  O O   . TRP A 265 ? 0.6715 0.7072 0.6299 0.0965  0.0526  0.0373  566 TRP A O   
2095  C CB  . TRP A 265 ? 0.4636 0.4689 0.4130 0.0973  0.0490  0.0455  566 TRP A CB  
2096  C CG  . TRP A 265 ? 0.4660 0.4467 0.4122 0.0875  0.0496  0.0493  566 TRP A CG  
2097  C CD1 . TRP A 265 ? 0.5261 0.5076 0.4815 0.0735  0.0508  0.0505  566 TRP A CD1 
2098  C CD2 . TRP A 265 ? 0.4660 0.4182 0.3987 0.0908  0.0491  0.0523  566 TRP A CD2 
2099  N NE1 . TRP A 265 ? 0.4729 0.4315 0.4226 0.0683  0.0510  0.0537  566 TRP A NE1 
2100  C CE2 . TRP A 265 ? 0.4639 0.4041 0.3998 0.0776  0.0502  0.0550  566 TRP A CE2 
2101  C CE3 . TRP A 265 ? 0.5063 0.4415 0.4236 0.1036  0.0478  0.0532  566 TRP A CE3 
2102  C CZ2 . TRP A 265 ? 0.4452 0.3595 0.3707 0.0754  0.0505  0.0584  566 TRP A CZ2 
2103  C CZ3 . TRP A 265 ? 0.5574 0.4629 0.4627 0.1012  0.0480  0.0571  566 TRP A CZ3 
2104  C CH2 . TRP A 265 ? 0.5362 0.4326 0.4464 0.0864  0.0495  0.0596  566 TRP A CH2 
2105  N N   . TYR A 266 ? 0.4784 0.4714 0.4295 0.0844  0.0521  0.0424  567 TYR A N   
2106  C CA  . TYR A 266 ? 0.4389 0.4396 0.3973 0.0747  0.0538  0.0415  567 TYR A CA  
2107  C C   . TYR A 266 ? 0.4774 0.4940 0.4485 0.0633  0.0546  0.0432  567 TYR A C   
2108  O O   . TYR A 266 ? 0.5443 0.5601 0.5182 0.0607  0.0537  0.0453  567 TYR A O   
2109  C CB  . TYR A 266 ? 0.5182 0.4950 0.4709 0.0688  0.0535  0.0423  567 TYR A CB  
2110  C CG  . TYR A 266 ? 0.5629 0.5199 0.5126 0.0638  0.0526  0.0457  567 TYR A CG  
2111  C CD1 . TYR A 266 ? 0.5640 0.5000 0.5016 0.0707  0.0515  0.0466  567 TYR A CD1 
2112  C CD2 . TYR A 266 ? 0.5021 0.4609 0.4602 0.0523  0.0530  0.0482  567 TYR A CD2 
2113  C CE1 . TYR A 266 ? 0.5567 0.4758 0.4913 0.0649  0.0514  0.0502  567 TYR A CE1 
2114  C CE2 . TYR A 266 ? 0.4475 0.3915 0.4036 0.0479  0.0527  0.0511  567 TYR A CE2 
2115  C CZ  . TYR A 266 ? 0.5526 0.4776 0.4972 0.0534  0.0521  0.0523  567 TYR A CZ  
2116  O OH  . TYR A 266 ? 0.6167 0.5284 0.5593 0.0476  0.0524  0.0556  567 TYR A OH  
2117  N N   . GLY A 267 ? 0.4757 0.5058 0.4533 0.0566  0.0563  0.0423  568 GLY A N   
2118  C CA  . GLY A 267 ? 0.3937 0.4381 0.3817 0.0462  0.0571  0.0435  568 GLY A CA  
2119  C C   . GLY A 267 ? 0.4100 0.4400 0.4000 0.0354  0.0567  0.0464  568 GLY A C   
2120  O O   . GLY A 267 ? 0.4330 0.4689 0.4296 0.0279  0.0566  0.0475  568 GLY A O   
2121  N N   . LEU A 268 ? 0.3853 0.3968 0.3695 0.0348  0.0563  0.0471  569 LEU A N   
2122  C CA  . LEU A 268 ? 0.4854 0.4878 0.4721 0.0253  0.0561  0.0491  569 LEU A CA  
2123  C C   . LEU A 268 ? 0.4924 0.4770 0.4760 0.0245  0.0547  0.0505  569 LEU A C   
2124  O O   . LEU A 268 ? 0.5040 0.4749 0.4808 0.0273  0.0541  0.0499  569 LEU A O   
2125  C CB  . LEU A 268 ? 0.4199 0.4202 0.4035 0.0236  0.0568  0.0484  569 LEU A CB  
2126  C CG  . LEU A 268 ? 0.4469 0.4399 0.4325 0.0149  0.0563  0.0504  569 LEU A CG  
2127  C CD1 . LEU A 268 ? 0.4638 0.4680 0.4552 0.0080  0.0573  0.0521  569 LEU A CD1 
2128  C CD2 . LEU A 268 ? 0.4495 0.4355 0.4296 0.0151  0.0560  0.0494  569 LEU A CD2 
2129  N N   . PRO A 269 ? 0.4692 0.4537 0.4573 0.0202  0.0542  0.0522  570 PRO A N   
2130  C CA  . PRO A 269 ? 0.4231 0.3931 0.4087 0.0185  0.0534  0.0537  570 PRO A CA  
2131  C C   . PRO A 269 ? 0.3594 0.3236 0.3469 0.0118  0.0529  0.0541  570 PRO A C   
2132  O O   . PRO A 269 ? 0.4521 0.4220 0.4446 0.0069  0.0527  0.0546  570 PRO A O   
2133  C CB  . PRO A 269 ? 0.3293 0.3050 0.3190 0.0175  0.0532  0.0549  570 PRO A CB  
2134  C CG  . PRO A 269 ? 0.3794 0.3696 0.3756 0.0140  0.0533  0.0538  570 PRO A CG  
2135  C CD  . PRO A 269 ? 0.3875 0.3853 0.3825 0.0165  0.0543  0.0524  570 PRO A CD  
2136  N N   . ALA A 270 ? 0.4308 0.3830 0.4135 0.0116  0.0524  0.0537  571 ALA A N   
2137  C CA  . ALA A 270 ? 0.4473 0.3960 0.4310 0.0065  0.0515  0.0532  571 ALA A CA  
2138  C C   . ALA A 270 ? 0.5202 0.4579 0.5020 0.0035  0.0509  0.0534  571 ALA A C   
2139  O O   . ALA A 270 ? 0.5555 0.4830 0.5308 0.0047  0.0506  0.0520  571 ALA A O   
2140  C CB  . ALA A 270 ? 0.4328 0.3822 0.4125 0.0087  0.0515  0.0512  571 ALA A CB  
2141  N N   . VAL A 271 ? 0.4927 0.4327 0.4795 -0.0005 0.0508  0.0548  572 VAL A N   
2142  C CA  . VAL A 271 ? 0.4249 0.3582 0.4111 -0.0044 0.0508  0.0552  572 VAL A CA  
2143  C C   . VAL A 271 ? 0.4017 0.3341 0.3889 -0.0088 0.0492  0.0532  572 VAL A C   
2144  O O   . VAL A 271 ? 0.4631 0.4030 0.4548 -0.0098 0.0480  0.0528  572 VAL A O   
2145  C CB  . VAL A 271 ? 0.4929 0.4323 0.4844 -0.0063 0.0515  0.0570  572 VAL A CB  
2146  C CG1 . VAL A 271 ? 0.3677 0.3051 0.3606 -0.0118 0.0517  0.0571  572 VAL A CG1 
2147  C CG2 . VAL A 271 ? 0.3351 0.2742 0.3241 -0.0023 0.0529  0.0588  572 VAL A CG2 
2148  N N   . SER A 272 ? 0.5230 0.4457 0.5055 -0.0116 0.0490  0.0520  573 SER A N   
2149  C CA  . SER A 272 ? 0.5364 0.4588 0.5190 -0.0154 0.0470  0.0491  573 SER A CA  
2150  C C   . SER A 272 ? 0.5436 0.4641 0.5278 -0.0230 0.0468  0.0483  573 SER A C   
2151  O O   . SER A 272 ? 0.5761 0.4986 0.5613 -0.0268 0.0447  0.0453  573 SER A O   
2152  C CB  . SER A 272 ? 0.4722 0.3857 0.4466 -0.0122 0.0462  0.0464  573 SER A CB  
2153  O OG  . SER A 272 ? 0.3642 0.2641 0.3305 -0.0098 0.0475  0.0468  573 SER A OG  
2154  N N   . ASN A 273 ? 0.4420 0.3608 0.4270 -0.0256 0.0490  0.0509  574 ASN A N   
2155  C CA  . ASN A 273 ? 0.4746 0.3923 0.4607 -0.0341 0.0496  0.0505  574 ASN A CA  
2156  C C   . ASN A 273 ? 0.4759 0.4101 0.4718 -0.0370 0.0500  0.0513  574 ASN A C   
2157  O O   . ASN A 273 ? 0.4385 0.3757 0.4367 -0.0446 0.0512  0.0512  574 ASN A O   
2158  C CB  . ASN A 273 ? 0.4535 0.3555 0.4310 -0.0360 0.0521  0.0533  574 ASN A CB  
2159  C CG  . ASN A 273 ? 0.5675 0.4718 0.5451 -0.0310 0.0544  0.0574  574 ASN A CG  
2160  O OD1 . ASN A 273 ? 0.5402 0.4566 0.5239 -0.0261 0.0540  0.0576  574 ASN A OD1 
2161  N ND2 . ASN A 273 ? 0.6175 0.5092 0.5872 -0.0323 0.0568  0.0606  574 ASN A ND2 
2162  N N   . MET A 274 ? 0.4090 0.3539 0.4103 -0.0315 0.0492  0.0517  575 MET A N   
2163  C CA  . MET A 274 ? 0.4913 0.4509 0.5007 -0.0322 0.0494  0.0518  575 MET A CA  
2164  C C   . MET A 274 ? 0.5861 0.5566 0.6007 -0.0328 0.0462  0.0485  575 MET A C   
2165  O O   . MET A 274 ? 0.6876 0.6545 0.6995 -0.0324 0.0438  0.0465  575 MET A O   
2166  C CB  . MET A 274 ? 0.3167 0.2797 0.3275 -0.0257 0.0500  0.0537  575 MET A CB  
2167  C CG  . MET A 274 ? 0.5931 0.5498 0.5997 -0.0251 0.0531  0.0568  575 MET A CG  
2168  S SD  . MET A 274 ? 0.5632 0.5264 0.5721 -0.0189 0.0535  0.0579  575 MET A SD  
2169  C CE  . MET A 274 ? 0.4942 0.4712 0.5097 -0.0212 0.0545  0.0573  575 MET A CE  
2170  N N   . LEU A 275 ? 0.4401 0.4251 0.4618 -0.0327 0.0459  0.0478  576 LEU A N   
2171  C CA  . LEU A 275 ? 0.3559 0.3538 0.3829 -0.0322 0.0426  0.0447  576 LEU A CA  
2172  C C   . LEU A 275 ? 0.4888 0.4936 0.5184 -0.0241 0.0412  0.0450  576 LEU A C   
2173  O O   . LEU A 275 ? 0.4838 0.4927 0.5156 -0.0221 0.0431  0.0462  576 LEU A O   
2174  C CB  . LEU A 275 ? 0.4024 0.4133 0.4354 -0.0398 0.0433  0.0426  576 LEU A CB  
2175  C CG  . LEU A 275 ? 0.4827 0.5114 0.5223 -0.0397 0.0397  0.0385  576 LEU A CG  
2176  C CD1 . LEU A 275 ? 0.4415 0.4770 0.4842 -0.0511 0.0403  0.0359  576 LEU A CD1 
2177  C CD2 . LEU A 275 ? 0.3905 0.4357 0.4365 -0.0333 0.0393  0.0381  576 LEU A CD2 
2178  N N   . LEU A 276 ? 0.5181 0.5229 0.5460 -0.0194 0.0377  0.0439  577 LEU A N   
2179  C CA  . LEU A 276 ? 0.5257 0.5328 0.5535 -0.0116 0.0358  0.0443  577 LEU A CA  
2180  C C   . LEU A 276 ? 0.5637 0.5871 0.5969 -0.0087 0.0329  0.0414  577 LEU A C   
2181  O O   . LEU A 276 ? 0.5261 0.5559 0.5603 -0.0104 0.0303  0.0390  577 LEU A O   
2182  C CB  . LEU A 276 ? 0.3785 0.3743 0.3993 -0.0080 0.0340  0.0458  577 LEU A CB  
2183  C CG  . LEU A 276 ? 0.4743 0.4696 0.4926 -0.0006 0.0312  0.0464  577 LEU A CG  
2184  C CD1 . LEU A 276 ? 0.3070 0.2998 0.3257 0.0026  0.0326  0.0473  577 LEU A CD1 
2185  C CD2 . LEU A 276 ? 0.4522 0.4365 0.4626 0.0009  0.0301  0.0485  577 LEU A CD2 
2186  N N   . GLU A 277 ? 0.5533 0.5844 0.5897 -0.0039 0.0332  0.0409  578 GLU A N   
2187  C CA  . GLU A 277 ? 0.4972 0.5468 0.5394 0.0002  0.0308  0.0376  578 GLU A CA  
2188  C C   . GLU A 277 ? 0.5272 0.5730 0.5649 0.0114  0.0275  0.0376  578 GLU A C   
2189  O O   . GLU A 277 ? 0.4758 0.5150 0.5113 0.0153  0.0288  0.0386  578 GLU A O   
2190  C CB  . GLU A 277 ? 0.5318 0.5959 0.5812 -0.0035 0.0342  0.0365  578 GLU A CB  
2191  C CG  . GLU A 277 ? 0.6244 0.7124 0.6813 0.0000  0.0322  0.0326  578 GLU A CG  
2192  C CD  . GLU A 277 ? 0.7590 0.8514 0.8155 0.0109  0.0314  0.0315  578 GLU A CD  
2193  O OE1 . GLU A 277 ? 0.7729 0.8735 0.8294 0.0204  0.0272  0.0290  578 GLU A OE1 
2194  O OE2 . GLU A 277 ? 0.8411 0.9278 0.8962 0.0106  0.0348  0.0331  578 GLU A OE2 
2195  N N   . ILE A 278 ? 0.5287 0.5775 0.5641 0.0167  0.0231  0.0364  579 ILE A N   
2196  C CA  . ILE A 278 ? 0.4888 0.5310 0.5176 0.0279  0.0195  0.0368  579 ILE A CA  
2197  C C   . ILE A 278 ? 0.5235 0.5854 0.5563 0.0352  0.0154  0.0330  579 ILE A C   
2198  O O   . ILE A 278 ? 0.5774 0.6485 0.6120 0.0331  0.0129  0.0315  579 ILE A O   
2199  C CB  . ILE A 278 ? 0.5397 0.5626 0.5581 0.0288  0.0179  0.0403  579 ILE A CB  
2200  C CG1 . ILE A 278 ? 0.5673 0.5746 0.5829 0.0216  0.0220  0.0436  579 ILE A CG1 
2201  C CG2 . ILE A 278 ? 0.5449 0.5576 0.5544 0.0397  0.0144  0.0414  579 ILE A CG2 
2202  C CD1 . ILE A 278 ? 0.6053 0.5982 0.6123 0.0204  0.0213  0.0467  579 ILE A CD1 
2203  N N   . GLY A 279 ? 0.4471 0.5164 0.4810 0.0443  0.0143  0.0309  580 GLY A N   
2204  C CA  . GLY A 279 ? 0.4268 0.5158 0.4637 0.0541  0.0099  0.0270  580 GLY A CA  
2205  C C   . GLY A 279 ? 0.5276 0.6451 0.5770 0.0474  0.0103  0.0231  580 GLY A C   
2206  O O   . GLY A 279 ? 0.4676 0.6021 0.5194 0.0531  0.0058  0.0199  580 GLY A O   
2207  N N   . GLY A 280 ? 0.5410 0.6643 0.5979 0.0352  0.0154  0.0232  581 GLY A N   
2208  C CA  . GLY A 280 ? 0.5024 0.6487 0.5699 0.0253  0.0164  0.0200  581 GLY A CA  
2209  C C   . GLY A 280 ? 0.4799 0.6184 0.5456 0.0156  0.0156  0.0207  581 GLY A C   
2210  O O   . GLY A 280 ? 0.5171 0.6703 0.5904 0.0048  0.0168  0.0182  581 GLY A O   
2211  N N   . LEU A 281 ? 0.3986 0.5145 0.4539 0.0187  0.0137  0.0238  582 LEU A N   
2212  C CA  . LEU A 281 ? 0.5411 0.6484 0.5934 0.0103  0.0132  0.0242  582 LEU A CA  
2213  C C   . LEU A 281 ? 0.5378 0.6284 0.5885 0.0001  0.0186  0.0273  582 LEU A C   
2214  O O   . LEU A 281 ? 0.5056 0.5827 0.5527 0.0023  0.0215  0.0307  582 LEU A O   
2215  C CB  . LEU A 281 ? 0.5225 0.6147 0.5638 0.0183  0.0093  0.0264  582 LEU A CB  
2216  C CG  . LEU A 281 ? 0.5206 0.6261 0.5604 0.0299  0.0032  0.0240  582 LEU A CG  
2217  C CD1 . LEU A 281 ? 0.6210 0.7064 0.6472 0.0375  0.0003  0.0279  582 LEU A CD1 
2218  C CD2 . LEU A 281 ? 0.4939 0.6227 0.5414 0.0249  0.0002  0.0186  582 LEU A CD2 
2219  N N   . GLU A 282 ? 0.5065 0.5976 0.5590 -0.0108 0.0196  0.0258  583 GLU A N   
2220  C CA  . GLU A 282 ? 0.5166 0.5927 0.5671 -0.0200 0.0244  0.0283  583 GLU A CA  
2221  C C   . GLU A 282 ? 0.5607 0.6183 0.6025 -0.0220 0.0236  0.0293  583 GLU A C   
2222  O O   . GLU A 282 ? 0.5182 0.5797 0.5596 -0.0259 0.0208  0.0260  583 GLU A O   
2223  C CB  . GLU A 282 ? 0.5359 0.6250 0.5940 -0.0317 0.0270  0.0259  583 GLU A CB  
2224  C CG  . GLU A 282 ? 0.5259 0.6348 0.5926 -0.0308 0.0292  0.0252  583 GLU A CG  
2225  C CD  . GLU A 282 ? 0.6588 0.7807 0.7324 -0.0444 0.0323  0.0235  583 GLU A CD  
2226  O OE1 . GLU A 282 ? 0.6650 0.7913 0.7401 -0.0527 0.0303  0.0201  583 GLU A OE1 
2227  O OE2 . GLU A 282 ? 0.7113 0.8384 0.7881 -0.0474 0.0369  0.0254  583 GLU A OE2 
2228  N N   . PHE A 283 ? 0.5195 0.5586 0.5546 -0.0192 0.0259  0.0334  584 PHE A N   
2229  C CA  . PHE A 283 ? 0.4203 0.4431 0.4471 -0.0199 0.0258  0.0346  584 PHE A CA  
2230  C C   . PHE A 283 ? 0.4696 0.4811 0.4947 -0.0275 0.0297  0.0355  584 PHE A C   
2231  O O   . PHE A 283 ? 0.4300 0.4315 0.4526 -0.0261 0.0329  0.0388  584 PHE A O   
2232  C CB  . PHE A 283 ? 0.3761 0.3882 0.3966 -0.0120 0.0257  0.0383  584 PHE A CB  
2233  C CG  . PHE A 283 ? 0.5287 0.5469 0.5472 -0.0041 0.0214  0.0380  584 PHE A CG  
2234  C CD1 . PHE A 283 ? 0.4654 0.4835 0.4787 -0.0026 0.0181  0.0367  584 PHE A CD1 
2235  C CD2 . PHE A 283 ? 0.3894 0.4127 0.4101 0.0025  0.0205  0.0387  584 PHE A CD2 
2236  C CE1 . PHE A 283 ? 0.3904 0.4132 0.4003 0.0055  0.0140  0.0370  584 PHE A CE1 
2237  C CE2 . PHE A 283 ? 0.3843 0.4110 0.4013 0.0110  0.0163  0.0386  584 PHE A CE2 
2238  C CZ  . PHE A 283 ? 0.4479 0.4742 0.4593 0.0125  0.0130  0.0381  584 PHE A CZ  
2239  N N   . SER A 284 ? 0.4424 0.4549 0.4679 -0.0354 0.0292  0.0322  585 SER A N   
2240  C CA  . SER A 284 ? 0.4803 0.4806 0.5029 -0.0429 0.0328  0.0330  585 SER A CA  
2241  C C   . SER A 284 ? 0.4807 0.4616 0.4939 -0.0400 0.0340  0.0349  585 SER A C   
2242  O O   . SER A 284 ? 0.3952 0.3636 0.4043 -0.0437 0.0369  0.0363  585 SER A O   
2243  C CB  . SER A 284 ? 0.4930 0.4975 0.5174 -0.0532 0.0316  0.0287  585 SER A CB  
2244  O OG  . SER A 284 ? 0.5990 0.6083 0.6219 -0.0518 0.0270  0.0245  585 SER A OG  
2245  N N   . ALA A 285 ? 0.4800 0.4583 0.4889 -0.0334 0.0320  0.0350  586 ALA A N   
2246  C CA  . ALA A 285 ? 0.4799 0.4438 0.4807 -0.0300 0.0334  0.0364  586 ALA A CA  
2247  C C   . ALA A 285 ? 0.5413 0.5068 0.5410 -0.0225 0.0333  0.0395  586 ALA A C   
2248  O O   . ALA A 285 ? 0.4840 0.4543 0.4821 -0.0192 0.0306  0.0389  586 ALA A O   
2249  C CB  . ALA A 285 ? 0.4874 0.4451 0.4817 -0.0318 0.0312  0.0324  586 ALA A CB  
2250  N N   . CYS A 286 ? 0.3604 0.3216 0.3603 -0.0202 0.0363  0.0430  587 CYS A N   
2251  C CA  . CYS A 286 ? 0.3351 0.2981 0.3352 -0.0152 0.0366  0.0460  587 CYS A CA  
2252  C C   . CYS A 286 ? 0.4641 0.4205 0.4617 -0.0135 0.0396  0.0484  587 CYS A C   
2253  O O   . CYS A 286 ? 0.5419 0.4999 0.5423 -0.0122 0.0408  0.0505  587 CYS A O   
2254  C CB  . CYS A 286 ? 0.4037 0.3750 0.4101 -0.0144 0.0360  0.0466  587 CYS A CB  
2255  S SG  . CYS A 286 ? 0.4837 0.4561 0.4950 -0.0178 0.0393  0.0475  587 CYS A SG  
2256  N N   . PRO A 287 ? 0.4816 0.4316 0.4738 -0.0128 0.0407  0.0477  588 PRO A N   
2257  C CA  . PRO A 287 ? 0.4112 0.3572 0.4017 -0.0107 0.0434  0.0494  588 PRO A CA  
2258  C C   . PRO A 287 ? 0.4750 0.4255 0.4670 -0.0084 0.0443  0.0519  588 PRO A C   
2259  O O   . PRO A 287 ? 0.4660 0.4187 0.4562 -0.0077 0.0434  0.0525  588 PRO A O   
2260  C CB  . PRO A 287 ? 0.4390 0.3787 0.4226 -0.0088 0.0437  0.0473  588 PRO A CB  
2261  C CG  . PRO A 287 ? 0.4785 0.4208 0.4600 -0.0091 0.0414  0.0456  588 PRO A CG  
2262  C CD  . PRO A 287 ? 0.5042 0.4513 0.4908 -0.0125 0.0392  0.0450  588 PRO A CD  
2263  N N   . PHE A 288 ? 0.3819 0.3333 0.3762 -0.0077 0.0460  0.0533  589 PHE A N   
2264  C CA  . PHE A 288 ? 0.3909 0.3463 0.3868 -0.0070 0.0466  0.0551  589 PHE A CA  
2265  C C   . PHE A 288 ? 0.4016 0.3588 0.3969 -0.0050 0.0487  0.0554  589 PHE A C   
2266  O O   . PHE A 288 ? 0.3930 0.3473 0.3869 -0.0032 0.0495  0.0549  589 PHE A O   
2267  C CB  . PHE A 288 ? 0.4429 0.3999 0.4430 -0.0080 0.0457  0.0558  589 PHE A CB  
2268  C CG  . PHE A 288 ? 0.5599 0.5174 0.5629 -0.0083 0.0465  0.0554  589 PHE A CG  
2269  C CD1 . PHE A 288 ? 0.5401 0.4987 0.5437 -0.0071 0.0481  0.0561  589 PHE A CD1 
2270  C CD2 . PHE A 288 ? 0.5170 0.4754 0.5220 -0.0100 0.0457  0.0544  589 PHE A CD2 
2271  C CE1 . PHE A 288 ? 0.4795 0.4383 0.4843 -0.0073 0.0490  0.0564  589 PHE A CE1 
2272  C CE2 . PHE A 288 ? 0.4960 0.4556 0.5031 -0.0113 0.0470  0.0547  589 PHE A CE2 
2273  C CZ  . PHE A 288 ? 0.4115 0.3704 0.4178 -0.0097 0.0488  0.0559  589 PHE A CZ  
2274  N N   . SER A 289 ? 0.4228 0.3851 0.4188 -0.0054 0.0495  0.0563  590 SER A N   
2275  C CA  . SER A 289 ? 0.4071 0.3751 0.4032 -0.0032 0.0511  0.0560  590 SER A CA  
2276  C C   . SER A 289 ? 0.3983 0.3724 0.3978 -0.0061 0.0515  0.0568  590 SER A C   
2277  O O   . SER A 289 ? 0.3757 0.3475 0.3752 -0.0097 0.0508  0.0578  590 SER A O   
2278  C CB  . SER A 289 ? 0.4051 0.3761 0.3973 -0.0008 0.0522  0.0551  590 SER A CB  
2279  O OG  . SER A 289 ? 0.4993 0.4728 0.4905 -0.0040 0.0524  0.0563  590 SER A OG  
2280  N N   . GLY A 290 ? 0.3920 0.3729 0.3933 -0.0044 0.0523  0.0560  591 GLY A N   
2281  C CA  . GLY A 290 ? 0.3728 0.3611 0.3774 -0.0079 0.0525  0.0558  591 GLY A CA  
2282  C C   . GLY A 290 ? 0.4877 0.4888 0.4936 -0.0053 0.0538  0.0545  591 GLY A C   
2283  O O   . GLY A 290 ? 0.5771 0.5837 0.5814 -0.0039 0.0552  0.0543  591 GLY A O   
2284  N N   . TRP A 291 ? 0.4929 0.5004 0.5015 -0.0040 0.0533  0.0533  592 TRP A N   
2285  C CA  . TRP A 291 ? 0.3699 0.3911 0.3797 0.0006  0.0539  0.0516  592 TRP A CA  
2286  C C   . TRP A 291 ? 0.4722 0.4929 0.4817 0.0053  0.0526  0.0511  592 TRP A C   
2287  O O   . TRP A 291 ? 0.4752 0.4884 0.4850 0.0030  0.0516  0.0516  592 TRP A O   
2288  C CB  . TRP A 291 ? 0.3685 0.4053 0.3828 -0.0050 0.0547  0.0503  592 TRP A CB  
2289  C CG  . TRP A 291 ? 0.4558 0.4913 0.4731 -0.0124 0.0535  0.0497  592 TRP A CG  
2290  C CD1 . TRP A 291 ? 0.4848 0.5255 0.5045 -0.0118 0.0519  0.0476  592 TRP A CD1 
2291  C CD2 . TRP A 291 ? 0.5028 0.5297 0.5193 -0.0208 0.0536  0.0510  592 TRP A CD2 
2292  N NE1 . TRP A 291 ? 0.4954 0.5309 0.5161 -0.0195 0.0508  0.0469  592 TRP A NE1 
2293  C CE2 . TRP A 291 ? 0.5589 0.5849 0.5773 -0.0250 0.0518  0.0491  592 TRP A CE2 
2294  C CE3 . TRP A 291 ? 0.5928 0.6118 0.6060 -0.0247 0.0547  0.0535  592 TRP A CE3 
2295  C CZ2 . TRP A 291 ? 0.6879 0.7032 0.7043 -0.0328 0.0512  0.0497  592 TRP A CZ2 
2296  C CZ3 . TRP A 291 ? 0.6445 0.6532 0.6555 -0.0321 0.0541  0.0547  592 TRP A CZ3 
2297  C CH2 . TRP A 291 ? 0.6873 0.6934 0.6997 -0.0360 0.0523  0.0528  592 TRP A CH2 
2298  N N   . TYR A 292 ? 0.5299 0.5591 0.5379 0.0127  0.0526  0.0501  593 TYR A N   
2299  C CA  . TYR A 292 ? 0.4836 0.5110 0.4888 0.0189  0.0514  0.0503  593 TYR A CA  
2300  C C   . TYR A 292 ? 0.4419 0.4809 0.4516 0.0166  0.0500  0.0484  593 TYR A C   
2301  O O   . TYR A 292 ? 0.4500 0.5041 0.4650 0.0126  0.0499  0.0460  593 TYR A O   
2302  C CB  . TYR A 292 ? 0.4285 0.4599 0.4288 0.0292  0.0514  0.0499  593 TYR A CB  
2303  C CG  . TYR A 292 ? 0.5364 0.5496 0.5286 0.0338  0.0519  0.0519  593 TYR A CG  
2304  C CD1 . TYR A 292 ? 0.4991 0.4969 0.4864 0.0339  0.0517  0.0545  593 TYR A CD1 
2305  C CD2 . TYR A 292 ? 0.4144 0.4257 0.4030 0.0378  0.0527  0.0510  593 TYR A CD2 
2306  C CE1 . TYR A 292 ? 0.5084 0.4888 0.4878 0.0364  0.0522  0.0561  593 TYR A CE1 
2307  C CE2 . TYR A 292 ? 0.4486 0.4415 0.4287 0.0414  0.0528  0.0521  593 TYR A CE2 
2308  C CZ  . TYR A 292 ? 0.5073 0.4843 0.4829 0.0401  0.0525  0.0547  593 TYR A CZ  
2309  O OH  . TYR A 292 ? 0.5393 0.4972 0.5061 0.0419  0.0527  0.0557  593 TYR A OH  
2310  N N   . MET A 293 ? 0.3896 0.4219 0.3966 0.0187  0.0491  0.0494  594 MET A N   
2311  C CA  . MET A 293 ? 0.3431 0.3866 0.3511 0.0213  0.0475  0.0475  594 MET A CA  
2312  C C   . MET A 293 ? 0.3813 0.4286 0.3836 0.0323  0.0471  0.0483  594 MET A C   
2313  O O   . MET A 293 ? 0.4036 0.4368 0.3988 0.0373  0.0480  0.0512  594 MET A O   
2314  C CB  . MET A 293 ? 0.3902 0.4250 0.3966 0.0192  0.0469  0.0482  594 MET A CB  
2315  C CG  . MET A 293 ? 0.3998 0.4454 0.4060 0.0223  0.0450  0.0461  594 MET A CG  
2316  S SD  . MET A 293 ? 0.4160 0.4536 0.4221 0.0175  0.0445  0.0454  594 MET A SD  
2317  C CE  . MET A 293 ? 0.3382 0.3615 0.3363 0.0229  0.0465  0.0506  594 MET A CE  
2318  N N   . GLY A 294 ? 0.3425 0.4087 0.3474 0.0362  0.0454  0.0454  595 GLY A N   
2319  C CA  . GLY A 294 ? 0.3714 0.4434 0.3706 0.0484  0.0446  0.0456  595 GLY A CA  
2320  C C   . GLY A 294 ? 0.4917 0.5470 0.4799 0.0564  0.0444  0.0496  595 GLY A C   
2321  O O   . GLY A 294 ? 0.4981 0.5460 0.4779 0.0661  0.0445  0.0514  595 GLY A O   
2322  N N   . THR A 295 ? 0.4718 0.5201 0.4587 0.0526  0.0443  0.0511  596 THR A N   
2323  C CA  . THR A 295 ? 0.4862 0.5207 0.4620 0.0595  0.0445  0.0553  596 THR A CA  
2324  C C   . THR A 295 ? 0.5062 0.5175 0.4754 0.0581  0.0470  0.0595  596 THR A C   
2325  O O   . THR A 295 ? 0.4043 0.4017 0.3622 0.0644  0.0475  0.0635  596 THR A O   
2326  C CB  . THR A 295 ? 0.4614 0.4967 0.4374 0.0559  0.0442  0.0556  596 THR A CB  
2327  O OG1 . THR A 295 ? 0.4160 0.4453 0.3984 0.0451  0.0456  0.0550  596 THR A OG1 
2328  C CG2 . THR A 295 ? 0.3635 0.4205 0.3435 0.0583  0.0411  0.0512  596 THR A CG2 
2329  N N   . GLU A 296 ? 0.3892 0.3954 0.3644 0.0495  0.0484  0.0588  597 GLU A N   
2330  C CA  . GLU A 296 ? 0.4626 0.4489 0.4319 0.0480  0.0502  0.0618  597 GLU A CA  
2331  C C   . GLU A 296 ? 0.4981 0.4770 0.4580 0.0579  0.0498  0.0626  597 GLU A C   
2332  O O   . GLU A 296 ? 0.5635 0.5230 0.5126 0.0606  0.0507  0.0661  597 GLU A O   
2333  C CB  . GLU A 296 ? 0.5628 0.5484 0.5399 0.0391  0.0510  0.0601  597 GLU A CB  
2334  C CG  . GLU A 296 ? 0.5617 0.5513 0.5465 0.0304  0.0511  0.0592  597 GLU A CG  
2335  C CD  . GLU A 296 ? 0.5648 0.5513 0.5549 0.0233  0.0517  0.0581  597 GLU A CD  
2336  O OE1 . GLU A 296 ? 0.5654 0.5393 0.5525 0.0210  0.0527  0.0599  597 GLU A OE1 
2337  O OE2 . GLU A 296 ? 0.5361 0.5325 0.5326 0.0196  0.0510  0.0557  597 GLU A OE2 
2338  N N   . ILE A 297 ? 0.3897 0.3843 0.3530 0.0635  0.0485  0.0592  598 ILE A N   
2339  C CA  . ILE A 297 ? 0.5577 0.5478 0.5120 0.0751  0.0478  0.0590  598 ILE A CA  
2340  C C   . ILE A 297 ? 0.5286 0.5211 0.4744 0.0866  0.0460  0.0606  598 ILE A C   
2341  O O   . ILE A 297 ? 0.5285 0.5020 0.4603 0.0948  0.0458  0.0638  598 ILE A O   
2342  C CB  . ILE A 297 ? 0.4274 0.4363 0.3892 0.0769  0.0474  0.0545  598 ILE A CB  
2343  C CG1 . ILE A 297 ? 0.3913 0.4006 0.3618 0.0651  0.0491  0.0532  598 ILE A CG1 
2344  C CG2 . ILE A 297 ? 0.4378 0.4406 0.3894 0.0899  0.0468  0.0537  598 ILE A CG2 
2345  C CD1 . ILE A 297 ? 0.4612 0.4909 0.4392 0.0651  0.0494  0.0494  598 ILE A CD1 
2346  N N   . GLY A 298 ? 0.5264 0.5417 0.4797 0.0872  0.0443  0.0581  599 GLY A N   
2347  C CA  . GLY A 298 ? 0.6324 0.6560 0.5785 0.0998  0.0418  0.0584  599 GLY A CA  
2348  C C   . GLY A 298 ? 0.6237 0.6291 0.5576 0.1026  0.0421  0.0639  599 GLY A C   
2349  O O   . GLY A 298 ? 0.6772 0.6747 0.5978 0.1153  0.0407  0.0665  599 GLY A O   
2350  N N   . VAL A 299 ? 0.5745 0.5727 0.5115 0.0914  0.0440  0.0660  600 VAL A N   
2351  C CA  . VAL A 299 ? 0.6024 0.5859 0.5284 0.0926  0.0449  0.0714  600 VAL A CA  
2352  C C   . VAL A 299 ? 0.6437 0.5983 0.5597 0.0888  0.0478  0.0765  600 VAL A C   
2353  O O   . VAL A 299 ? 0.5012 0.4373 0.4014 0.0958  0.0482  0.0815  600 VAL A O   
2354  C CB  . VAL A 299 ? 0.5567 0.5516 0.4913 0.0835  0.0453  0.0702  600 VAL A CB  
2355  C CG1 . VAL A 299 ? 0.4973 0.4798 0.4198 0.0853  0.0467  0.0758  600 VAL A CG1 
2356  C CG2 . VAL A 299 ? 0.6267 0.6490 0.5706 0.0858  0.0421  0.0644  600 VAL A CG2 
2357  N N   . ARG A 300 ? 0.6573 0.6070 0.5814 0.0774  0.0498  0.0753  601 ARG A N   
2358  C CA  . ARG A 300 ? 0.7540 0.6792 0.6705 0.0713  0.0525  0.0795  601 ARG A CA  
2359  C C   . ARG A 300 ? 0.7006 0.6085 0.6080 0.0767  0.0521  0.0795  601 ARG A C   
2360  O O   . ARG A 300 ? 0.6751 0.5607 0.5667 0.0816  0.0527  0.0839  601 ARG A O   
2361  C CB  . ARG A 300 ? 0.6148 0.5436 0.5434 0.0574  0.0543  0.0780  601 ARG A CB  
2362  C CG  . ARG A 300 ? 0.5336 0.4781 0.4706 0.0525  0.0546  0.0771  601 ARG A CG  
2363  C CD  . ARG A 300 ? 0.5155 0.4538 0.4421 0.0543  0.0562  0.0823  601 ARG A CD  
2364  N NE  . ARG A 300 ? 0.5143 0.4302 0.4305 0.0502  0.0592  0.0877  601 ARG A NE  
2365  C CZ  . ARG A 300 ? 0.4047 0.3163 0.3255 0.0392  0.0618  0.0884  601 ARG A CZ  
2366  N NH1 . ARG A 300 ? 0.5369 0.4638 0.4716 0.0328  0.0617  0.0844  601 ARG A NH1 
2367  N NH2 . ARG A 300 ? 0.5462 0.4379 0.4574 0.0346  0.0643  0.0929  601 ARG A NH2 
2368  N N   . ASP A 301 ? 0.6237 0.5408 0.5398 0.0763  0.0512  0.0745  602 ASP A N   
2369  C CA  . ASP A 301 ? 0.6412 0.5427 0.5488 0.0816  0.0507  0.0735  602 ASP A CA  
2370  C C   . ASP A 301 ? 0.6725 0.5650 0.5648 0.0973  0.0489  0.0751  602 ASP A C   
2371  O O   . ASP A 301 ? 0.6293 0.4952 0.5063 0.1012  0.0492  0.0776  602 ASP A O   
2372  C CB  . ASP A 301 ? 0.5610 0.4790 0.4802 0.0805  0.0500  0.0678  602 ASP A CB  
2373  C CG  . ASP A 301 ? 0.5160 0.4381 0.4472 0.0665  0.0515  0.0666  602 ASP A CG  
2374  O OD1 . ASP A 301 ? 0.6292 0.5362 0.5578 0.0583  0.0530  0.0693  602 ASP A OD1 
2375  O OD2 . ASP A 301 ? 0.5807 0.5219 0.5236 0.0637  0.0511  0.0630  602 ASP A OD2 
2376  N N   . TYR A 302 ? 0.7034 0.6175 0.5989 0.1067  0.0468  0.0733  603 TYR A N   
2377  C CA  . TYR A 302 ? 0.6897 0.6007 0.5720 0.1241  0.0443  0.0738  603 TYR A CA  
2378  C C   . TYR A 302 ? 0.7083 0.6036 0.5751 0.1300  0.0441  0.0802  603 TYR A C   
2379  O O   . TYR A 302 ? 0.7682 0.6467 0.6177 0.1437  0.0425  0.0824  603 TYR A O   
2380  C CB  . TYR A 302 ? 0.6747 0.6198 0.5682 0.1317  0.0419  0.0685  603 TYR A CB  
2381  C CG  . TYR A 302 ? 0.5903 0.5477 0.4915 0.1334  0.0417  0.0628  603 TYR A CG  
2382  C CD1 . TYR A 302 ? 0.5684 0.5048 0.4643 0.1306  0.0431  0.0625  603 TYR A CD1 
2383  C CD2 . TYR A 302 ? 0.4923 0.4830 0.4058 0.1372  0.0403  0.0576  603 TYR A CD2 
2384  C CE1 . TYR A 302 ? 0.6094 0.5578 0.5113 0.1328  0.0431  0.0573  603 TYR A CE1 
2385  C CE2 . TYR A 302 ? 0.5553 0.5591 0.4755 0.1384  0.0407  0.0527  603 TYR A CE2 
2386  C CZ  . TYR A 302 ? 0.5756 0.5579 0.4896 0.1367  0.0422  0.0527  603 TYR A CZ  
2387  O OH  . TYR A 302 ? 0.6099 0.6054 0.5295 0.1383  0.0429  0.0479  603 TYR A OH  
2388  N N   . CYS A 303 ? 0.6863 0.5862 0.5575 0.1209  0.0456  0.0832  604 CYS A N   
2389  C CA  . CYS A 303 ? 0.8217 0.7145 0.6795 0.1277  0.0452  0.0887  604 CYS A CA  
2390  C C   . CYS A 303 ? 0.7946 0.6640 0.6433 0.1175  0.0488  0.0957  604 CYS A C   
2391  O O   . CYS A 303 ? 0.7759 0.6345 0.6098 0.1237  0.0489  0.1015  604 CYS A O   
2392  C CB  . CYS A 303 ? 0.7752 0.6996 0.6439 0.1299  0.0431  0.0859  604 CYS A CB  
2393  S SG  . CYS A 303 ? 0.6727 0.6250 0.5460 0.1459  0.0385  0.0794  604 CYS A SG  
2394  N N   . ASP A 304 ? 0.7307 0.5936 0.5876 0.1022  0.0518  0.0954  605 ASP A N   
2395  C CA  . ASP A 304 ? 0.7022 0.5418 0.5492 0.0925  0.0555  0.1018  605 ASP A CA  
2396  C C   . ASP A 304 ? 0.7152 0.5217 0.5389 0.1004  0.0554  0.1070  605 ASP A C   
2397  O O   . ASP A 304 ? 0.8123 0.6086 0.6309 0.1081  0.0533  0.1042  605 ASP A O   
2398  C CB  . ASP A 304 ? 0.6903 0.5276 0.5489 0.0765  0.0580  0.0997  605 ASP A CB  
2399  C CG  . ASP A 304 ? 0.6867 0.5478 0.5630 0.0663  0.0592  0.0973  605 ASP A CG  
2400  O OD1 . ASP A 304 ? 0.6387 0.5209 0.5212 0.0708  0.0577  0.0956  605 ASP A OD1 
2401  O OD2 . ASP A 304 ? 0.6768 0.5349 0.5602 0.0537  0.0615  0.0968  605 ASP A OD2 
2402  N N   . ASN A 305 ? 0.6676 0.4559 0.4761 0.0986  0.0579  0.1148  606 ASN A N   
2403  C CA  . ASN A 305 ? 0.7479 0.5002 0.5315 0.1055  0.0580  0.1206  606 ASN A CA  
2404  C C   . ASN A 305 ? 0.7297 0.4579 0.5104 0.0960  0.0593  0.1192  606 ASN A C   
2405  O O   . ASN A 305 ? 0.7975 0.5001 0.5619 0.1051  0.0574  0.1196  606 ASN A O   
2406  C CB  . ASN A 305 ? 0.9432 0.6799 0.7105 0.1028  0.0611  0.1301  606 ASN A CB  
2407  C CG  . ASN A 305 ? 1.0271 0.7790 0.7885 0.1178  0.0586  0.1322  606 ASN A CG  
2408  O OD1 . ASN A 305 ? 1.0033 0.7523 0.7544 0.1355  0.0545  0.1313  606 ASN A OD1 
2409  N ND2 . ASN A 305 ? 1.1114 0.8806 0.8789 0.1113  0.0609  0.1345  606 ASN A ND2 
2410  N N   . SER A 306 ? 0.6732 0.4097 0.4694 0.0787  0.0620  0.1171  607 SER A N   
2411  C CA  . SER A 306 ? 0.8276 0.5466 0.6242 0.0681  0.0629  0.1146  607 SER A CA  
2412  C C   . SER A 306 ? 0.8717 0.6034 0.6802 0.0729  0.0597  0.1059  607 SER A C   
2413  O O   . SER A 306 ? 0.8138 0.5321 0.6224 0.0654  0.0599  0.1030  607 SER A O   
2414  C CB  . SER A 306 ? 0.8943 0.6210 0.7033 0.0483  0.0669  0.1154  607 SER A CB  
2415  O OG  . SER A 306 ? 1.0753 0.7911 0.8734 0.0418  0.0707  0.1234  607 SER A OG  
2416  N N   . ARG A 307 ? 0.8534 0.6111 0.6718 0.0844  0.0569  0.1017  608 ARG A N   
2417  C CA  . ARG A 307 ? 0.8575 0.6312 0.6884 0.0880  0.0545  0.0939  608 ARG A CA  
2418  C C   . ARG A 307 ? 0.8209 0.5888 0.6396 0.1071  0.0512  0.0920  608 ARG A C   
2419  O O   . ARG A 307 ? 0.9367 0.6733 0.7344 0.1135  0.0507  0.0953  608 ARG A O   
2420  C CB  . ARG A 307 ? 0.8331 0.6426 0.6867 0.0826  0.0546  0.0902  608 ARG A CB  
2421  C CG  . ARG A 307 ? 0.7539 0.5680 0.6188 0.0651  0.0575  0.0911  608 ARG A CG  
2422  C CD  . ARG A 307 ? 0.7494 0.5518 0.6171 0.0550  0.0582  0.0883  608 ARG A CD  
2423  N NE  . ARG A 307 ? 0.7543 0.5686 0.6303 0.0595  0.0559  0.0818  608 ARG A NE  
2424  C CZ  . ARG A 307 ? 0.7150 0.5563 0.6081 0.0577  0.0553  0.0778  608 ARG A CZ  
2425  N NH1 . ARG A 307 ? 0.5764 0.4353 0.4801 0.0523  0.0562  0.0790  608 ARG A NH1 
2426  N NH2 . ARG A 307 ? 0.6541 0.5042 0.5526 0.0614  0.0537  0.0727  608 ARG A NH2 
2427  N N   . TYR A 308 ? 0.6667 0.4631 0.4969 0.1166  0.0488  0.0867  609 TYR A N   
2428  C CA  . TYR A 308 ? 0.6821 0.4754 0.5013 0.1354  0.0456  0.0841  609 TYR A CA  
2429  C C   . TYR A 308 ? 0.8281 0.6180 0.6331 0.1501  0.0438  0.0886  609 TYR A C   
2430  O O   . TYR A 308 ? 0.9481 0.7273 0.7385 0.1672  0.0411  0.0877  609 TYR A O   
2431  C CB  . TYR A 308 ? 0.6975 0.5243 0.5338 0.1399  0.0440  0.0765  609 TYR A CB  
2432  C CG  . TYR A 308 ? 0.7822 0.6032 0.6216 0.1360  0.0444  0.0714  609 TYR A CG  
2433  C CD1 . TYR A 308 ? 0.7722 0.5983 0.6254 0.1189  0.0465  0.0700  609 TYR A CD1 
2434  C CD2 . TYR A 308 ? 0.7298 0.5409 0.5576 0.1506  0.0423  0.0677  609 TYR A CD2 
2435  C CE1 . TYR A 308 ? 0.7473 0.5689 0.6026 0.1157  0.0466  0.0652  609 TYR A CE1 
2436  C CE2 . TYR A 308 ? 0.6600 0.4664 0.4897 0.1475  0.0426  0.0626  609 TYR A CE2 
2437  C CZ  . TYR A 308 ? 0.7396 0.5513 0.5830 0.1297  0.0447  0.0615  609 TYR A CZ  
2438  O OH  . TYR A 308 ? 0.8260 0.6338 0.6706 0.1271  0.0447  0.0565  609 TYR A OH  
2439  N N   . ASN A 309 ? 0.6960 0.4960 0.5046 0.1450  0.0450  0.0929  610 ASN A N   
2440  C CA  . ASN A 309 ? 0.8137 0.6043 0.6054 0.1565  0.0438  0.0990  610 ASN A CA  
2441  C C   . ASN A 309 ? 0.8206 0.6248 0.6065 0.1786  0.0393  0.0959  610 ASN A C   
2442  O O   . ASN A 309 ? 0.7093 0.4902 0.4730 0.1936  0.0374  0.0996  610 ASN A O   
2443  C CB  . ASN A 309 ? 0.7535 0.5001 0.5215 0.1540  0.0458  0.1065  610 ASN A CB  
2444  C CG  . ASN A 309 ? 0.7797 0.5159 0.5312 0.1604  0.0460  0.1146  610 ASN A CG  
2445  O OD1 . ASN A 309 ? 0.8863 0.6467 0.6475 0.1579  0.0464  0.1156  610 ASN A OD1 
2446  N ND2 . ASN A 309 ? 0.7486 0.4476 0.4737 0.1691  0.0456  0.1204  610 ASN A ND2 
2447  N N   . ILE A 310 ? 0.7980 0.6412 0.6037 0.1807  0.0376  0.0892  611 ILE A N   
2448  C CA  . ILE A 310 ? 0.7731 0.6358 0.5769 0.2005  0.0334  0.0848  611 ILE A CA  
2449  C C   . ILE A 310 ? 0.7929 0.6788 0.5976 0.2089  0.0309  0.0861  611 ILE A C   
2450  O O   . ILE A 310 ? 0.7992 0.7081 0.6049 0.2250  0.0271  0.0818  611 ILE A O   
2451  C CB  . ILE A 310 ? 0.8565 0.7490 0.6801 0.1987  0.0330  0.0761  611 ILE A CB  
2452  C CG1 . ILE A 310 ? 0.8637 0.7926 0.7112 0.1861  0.0337  0.0728  611 ILE A CG1 
2453  C CG2 . ILE A 310 ? 0.8394 0.7117 0.6638 0.1887  0.0355  0.0745  611 ILE A CG2 
2454  C CD1 . ILE A 310 ? 0.7953 0.7595 0.6599 0.1885  0.0325  0.0647  611 ILE A CD1 
2455  N N   . LEU A 311 ? 0.6020 0.4850 0.4066 0.1989  0.0327  0.0912  612 LEU A N   
2456  C CA  . LEU A 311 ? 0.6394 0.5436 0.4432 0.2071  0.0300  0.0922  612 LEU A CA  
2457  C C   . LEU A 311 ? 0.7452 0.6392 0.5272 0.2307  0.0261  0.0948  612 LEU A C   
2458  O O   . LEU A 311 ? 0.7747 0.6984 0.5613 0.2445  0.0218  0.0901  612 LEU A O   
2459  C CB  . LEU A 311 ? 0.6120 0.5068 0.4131 0.1947  0.0331  0.0985  612 LEU A CB  
2460  C CG  . LEU A 311 ? 0.5653 0.4814 0.3897 0.1754  0.0355  0.0946  612 LEU A CG  
2461  C CD1 . LEU A 311 ? 0.5725 0.4760 0.3928 0.1631  0.0392  0.1008  612 LEU A CD1 
2462  C CD2 . LEU A 311 ? 0.5180 0.4753 0.3595 0.1787  0.0320  0.0871  612 LEU A CD2 
2463  N N   . GLU A 312 ? 0.8021 0.6537 0.5597 0.2354  0.0273  0.1022  613 GLU A N   
2464  C CA  . GLU A 312 ? 0.8988 0.7344 0.6317 0.2586  0.0235  0.1060  613 GLU A CA  
2465  C C   . GLU A 312 ? 0.9555 0.8100 0.6916 0.2767  0.0192  0.0981  613 GLU A C   
2466  O O   . GLU A 312 ? 0.9479 0.8194 0.6774 0.2966  0.0145  0.0968  613 GLU A O   
2467  C CB  . GLU A 312 ? 1.0316 0.8139 0.7378 0.2576  0.0260  0.1147  613 GLU A CB  
2468  C CG  . GLU A 312 ? 1.2194 0.9767 0.8956 0.2803  0.0225  0.1207  613 GLU A CG  
2469  C CD  . GLU A 312 ? 1.3160 1.0196 0.9653 0.2746  0.0259  0.1311  613 GLU A CD  
2470  O OE1 . GLU A 312 ? 1.3591 1.0509 1.0157 0.2518  0.0311  0.1336  613 GLU A OE1 
2471  O OE2 . GLU A 312 ? 1.2478 0.9216 0.8686 0.2927  0.0234  0.1367  613 GLU A OE2 
2472  N N   . GLU A 313 ? 0.9143 0.7693 0.6614 0.2701  0.0207  0.0924  614 GLU A N   
2473  C CA  . GLU A 313 ? 0.9355 0.8102 0.6867 0.2861  0.0174  0.0845  614 GLU A CA  
2474  C C   . GLU A 313 ? 0.8147 0.7433 0.5873 0.2902  0.0146  0.0775  614 GLU A C   
2475  O O   . GLU A 313 ? 0.8687 0.8172 0.6377 0.3109  0.0102  0.0735  614 GLU A O   
2476  C CB  . GLU A 313 ? 0.9978 0.8651 0.7587 0.2747  0.0204  0.0798  614 GLU A CB  
2477  C CG  . GLU A 313 ? 1.0513 0.8876 0.7919 0.2898  0.0190  0.0789  614 GLU A CG  
2478  C CD  . GLU A 313 ? 1.1814 1.0499 0.9312 0.3052  0.0162  0.0697  614 GLU A CD  
2479  O OE1 . GLU A 313 ? 1.2630 1.1702 1.0224 0.3154  0.0133  0.0664  614 GLU A OE1 
2480  O OE2 . GLU A 313 ? 1.1941 1.0511 0.9419 0.3066  0.0170  0.0653  614 GLU A OE2 
2481  N N   . VAL A 314 ? 0.7256 0.6785 0.5204 0.2706  0.0169  0.0756  615 VAL A N   
2482  C CA  . VAL A 314 ? 0.6481 0.6513 0.4649 0.2702  0.0147  0.0682  615 VAL A CA  
2483  C C   . VAL A 314 ? 0.7437 0.7626 0.5537 0.2824  0.0105  0.0700  615 VAL A C   
2484  O O   . VAL A 314 ? 0.7343 0.7900 0.5519 0.2948  0.0064  0.0639  615 VAL A O   
2485  C CB  . VAL A 314 ? 0.6891 0.7072 0.5293 0.2448  0.0184  0.0657  615 VAL A CB  
2486  C CG1 . VAL A 314 ? 0.6643 0.7296 0.5250 0.2415  0.0162  0.0592  615 VAL A CG1 
2487  C CG2 . VAL A 314 ? 0.7440 0.7554 0.5928 0.2355  0.0217  0.0623  615 VAL A CG2 
2488  N N   . ALA A 315 ? 0.7432 0.7358 0.5386 0.2792  0.0116  0.0782  616 ALA A N   
2489  C CA  . ALA A 315 ? 0.6633 0.6673 0.4489 0.2919  0.0076  0.0808  616 ALA A CA  
2490  C C   . ALA A 315 ? 0.7992 0.8001 0.5657 0.3198  0.0026  0.0809  616 ALA A C   
2491  O O   . ALA A 315 ? 0.7416 0.7753 0.5105 0.3340  -0.0024 0.0771  616 ALA A O   
2492  C CB  . ALA A 315 ? 0.6391 0.6112 0.4098 0.2832  0.0106  0.0905  616 ALA A CB  
2493  N N   . LYS A 316 ? 0.8985 0.8611 0.6460 0.3285  0.0036  0.0846  617 LYS A N   
2494  C CA  . LYS A 316 ? 0.9896 0.9461 0.7172 0.3568  -0.0013 0.0843  617 LYS A CA  
2495  C C   . LYS A 316 ? 0.9463 0.9535 0.6927 0.3680  -0.0052 0.0733  617 LYS A C   
2496  O O   . LYS A 316 ? 0.8468 0.8793 0.5889 0.3878  -0.0106 0.0710  617 LYS A O   
2497  C CB  . LYS A 316 ? 1.0382 0.9462 0.7453 0.3615  0.0006  0.0880  617 LYS A CB  
2498  C CG  . LYS A 316 ? 1.1385 0.9928 0.8156 0.3626  0.0022  0.0997  617 LYS A CG  
2499  C CD  . LYS A 316 ? 1.2013 1.0096 0.8638 0.3599  0.0049  0.1016  617 LYS A CD  
2500  C CE  . LYS A 316 ? 1.2223 0.9786 0.8529 0.3620  0.0060  0.1101  617 LYS A CE  
2501  N NZ  . LYS A 316 ? 1.1819 0.9215 0.8085 0.3452  0.0099  0.1203  617 LYS A NZ  
2502  N N   . LYS A 317 ? 0.8753 0.8994 0.6428 0.3555  -0.0023 0.0664  618 LYS A N   
2503  C CA  . LYS A 317 ? 0.8292 0.9039 0.6162 0.3632  -0.0050 0.0560  618 LYS A CA  
2504  C C   . LYS A 317 ? 0.8555 0.9767 0.6611 0.3577  -0.0075 0.0519  618 LYS A C   
2505  O O   . LYS A 317 ? 0.9110 1.0757 0.7269 0.3700  -0.0115 0.0444  618 LYS A O   
2506  C CB  . LYS A 317 ? 0.7365 0.8196 0.5426 0.3472  -0.0005 0.0504  618 LYS A CB  
2507  C CG  . LYS A 317 ? 0.8289 0.8660 0.6189 0.3481  0.0023  0.0535  618 LYS A CG  
2508  C CD  . LYS A 317 ? 0.7165 0.7696 0.5092 0.3622  0.0014  0.0458  618 LYS A CD  
2509  C CE  . LYS A 317 ? 0.8914 0.9043 0.6536 0.3859  -0.0012 0.0488  618 LYS A CE  
2510  N NZ  . LYS A 317 ? 0.9352 0.9638 0.6971 0.4038  -0.0027 0.0406  618 LYS A NZ  
2511  N N   . MET A 318 ? 0.7703 0.8846 0.5807 0.3390  -0.0053 0.0561  619 MET A N   
2512  C CA  . MET A 318 ? 0.7602 0.9158 0.5866 0.3334  -0.0080 0.0518  619 MET A CA  
2513  C C   . MET A 318 ? 0.7976 0.9585 0.6067 0.3548  -0.0139 0.0545  619 MET A C   
2514  O O   . MET A 318 ? 0.8239 1.0246 0.6451 0.3550  -0.0176 0.0493  619 MET A O   
2515  C CB  . MET A 318 ? 0.6877 0.8352 0.5251 0.3071  -0.0039 0.0544  619 MET A CB  
2516  C CG  . MET A 318 ? 0.6261 0.7864 0.4875 0.2850  0.0005  0.0491  619 MET A CG  
2517  S SD  . MET A 318 ? 0.6830 0.8364 0.5575 0.2562  0.0047  0.0511  619 MET A SD  
2518  C CE  . MET A 318 ? 0.5459 0.7413 0.4290 0.2586  -0.0007 0.0458  619 MET A CE  
2519  N N   . ASN A 319 ? 0.8446 0.9656 0.6247 0.3726  -0.0150 0.0624  620 ASN A N   
2520  C CA  . ASN A 319 ? 0.9761 1.0942 0.7346 0.3946  -0.0204 0.0669  620 ASN A CA  
2521  C C   . ASN A 319 ? 0.9381 1.0482 0.6921 0.3833  -0.0195 0.0730  620 ASN A C   
2522  O O   . ASN A 319 ? 0.8856 1.0170 0.6343 0.3955  -0.0246 0.0726  620 ASN A O   
2523  C CB  . ASN A 319 ? 0.9891 1.1593 0.7570 0.4129  -0.0270 0.0575  620 ASN A CB  
2524  C CG  . ASN A 319 ? 1.0502 1.2094 0.8024 0.4302  -0.0276 0.0538  620 ASN A CG  
2525  O OD1 . ASN A 319 ? 1.2075 1.3358 0.9326 0.4430  -0.0283 0.0582  620 ASN A OD1 
2526  N ND2 . ASN A 319 ? 1.0352 1.2199 0.8034 0.4310  -0.0272 0.0454  620 ASN A ND2 
2527  N N   . LEU A 320 ? 0.8734 0.9542 0.6290 0.3608  -0.0133 0.0784  621 LEU A N   
2528  C CA  . LEU A 320 ? 0.8660 0.9414 0.6187 0.3492  -0.0119 0.0836  621 LEU A CA  
2529  C C   . LEU A 320 ? 0.9478 0.9798 0.6669 0.3619  -0.0118 0.0958  621 LEU A C   
2530  O O   . LEU A 320 ? 0.9714 0.9648 0.6707 0.3709  -0.0105 0.1016  621 LEU A O   
2531  C CB  . LEU A 320 ? 0.8752 0.9408 0.6445 0.3204  -0.0053 0.0838  621 LEU A CB  
2532  C CG  . LEU A 320 ? 0.7790 0.8828 0.5800 0.3054  -0.0048 0.0729  621 LEU A CG  
2533  C CD1 . LEU A 320 ? 0.6283 0.7168 0.4416 0.2792  0.0015  0.0743  621 LEU A CD1 
2534  C CD2 . LEU A 320 ? 0.7876 0.9391 0.6025 0.3078  -0.0099 0.0652  621 LEU A CD2 
2535  N N   . ASP A 321 ? 0.9446 0.9829 0.6563 0.3627  -0.0133 0.0996  622 ASP A N   
2536  C CA  . ASP A 321 ? 0.8741 0.8708 0.5541 0.3704  -0.0119 0.1123  622 ASP A CA  
2537  C C   . ASP A 321 ? 0.8426 0.8016 0.5207 0.3475  -0.0038 0.1194  622 ASP A C   
2538  O O   . ASP A 321 ? 0.9192 0.8904 0.6136 0.3272  -0.0003 0.1178  622 ASP A O   
2539  C CB  . ASP A 321 ? 1.0187 1.0356 0.6921 0.3769  -0.0155 0.1140  622 ASP A CB  
2540  C CG  . ASP A 321 ? 1.1736 1.1476 0.8185 0.3766  -0.0116 0.1262  622 ASP A CG  
2541  O OD1 . ASP A 321 ? 1.2235 1.1560 0.8493 0.3803  -0.0085 0.1314  622 ASP A OD1 
2542  O OD2 . ASP A 321 ? 1.2617 1.2435 0.9043 0.3704  -0.0109 0.1298  622 ASP A OD2 
2543  N N   . MET A 322 ? 0.9083 0.8217 0.5663 0.3508  -0.0010 0.1268  623 MET A N   
2544  C CA  . MET A 322 ? 0.9617 0.8400 0.6181 0.3289  0.0065  0.1330  623 MET A CA  
2545  C C   . MET A 322 ? 1.0494 0.8853 0.6747 0.3305  0.0096  0.1467  623 MET A C   
2546  O O   . MET A 322 ? 1.0921 0.8924 0.7102 0.3150  0.0157  0.1533  623 MET A O   
2547  C CB  . MET A 322 ? 0.9011 0.7597 0.5609 0.3261  0.0083  0.1300  623 MET A CB  
2548  C CG  . MET A 322 ? 0.9561 0.8565 0.6467 0.3223  0.0063  0.1171  623 MET A CG  
2549  S SD  . MET A 322 ? 0.9773 0.8590 0.6695 0.3245  0.0072  0.1128  623 MET A SD  
2550  C CE  . MET A 322 ? 0.9807 0.8083 0.6592 0.3045  0.0146  0.1225  623 MET A CE  
2551  N N   . ARG A 323 ? 1.0614 0.9038 0.6722 0.3447  0.0062  0.1486  624 ARG A N   
2552  C CA  . ARG A 323 ? 1.1973 1.0042 0.7836 0.3415  0.0101  0.1584  624 ARG A CA  
2553  C C   . ARG A 323 ? 1.2319 1.0420 0.8208 0.3245  0.0148  0.1650  624 ARG A C   
2554  O O   . ARG A 323 ? 1.3543 1.1305 0.9269 0.3140  0.0205  0.1741  624 ARG A O   
2555  C CB  . ARG A 323 ? 1.2870 1.1006 0.8578 0.3621  0.0052  0.1570  624 ARG A CB  
2556  C CG  . ARG A 323 ? 1.3298 1.1249 0.8878 0.3784  0.0023  0.1533  624 ARG A CG  
2557  C CD  . ARG A 323 ? 1.4165 1.2318 0.9650 0.4004  -0.0034 0.1494  624 ARG A CD  
2558  N NE  . ARG A 323 ? 1.4477 1.3185 1.0190 0.4050  -0.0082 0.1409  624 ARG A NE  
2559  C CZ  . ARG A 323 ? 1.4641 1.3646 1.0335 0.4215  -0.0135 0.1359  624 ARG A CZ  
2560  N NH1 . ARG A 323 ? 1.4528 1.3321 0.9975 0.4365  -0.0146 0.1390  624 ARG A NH1 
2561  N NH2 . ARG A 323 ? 1.4553 1.4071 1.0475 0.4225  -0.0179 0.1274  624 ARG A NH2 
2562  N N   . LYS A 324 ? 1.1447 0.9961 0.7545 0.3205  0.0129  0.1598  625 LYS A N   
2563  C CA  . LYS A 324 ? 1.1761 1.0353 0.7929 0.3022  0.0179  0.1622  625 LYS A CA  
2564  C C   . LYS A 324 ? 1.1009 0.9906 0.7530 0.2825  0.0196  0.1511  625 LYS A C   
2565  O O   . LYS A 324 ? 1.0755 0.9990 0.7483 0.2867  0.0147  0.1400  625 LYS A O   
2566  C CB  . LYS A 324 ? 1.2460 1.1277 0.8529 0.3143  0.0140  0.1637  625 LYS A CB  
2567  C CG  . LYS A 324 ? 1.2657 1.1902 0.8848 0.3314  0.0052  0.1528  625 LYS A CG  
2568  C CD  . LYS A 324 ? 1.2825 1.2293 0.8929 0.3410  0.0015  0.1533  625 LYS A CD  
2569  C CE  . LYS A 324 ? 1.2467 1.2295 0.8641 0.3603  -0.0071 0.1428  625 LYS A CE  
2570  N NZ  . LYS A 324 ? 1.1560 1.1750 0.8025 0.3568  -0.0110 0.1310  625 LYS A NZ  
2571  N N   . THR A 325 ? 1.0452 0.9228 0.7034 0.2610  0.0267  0.1544  626 THR A N   
2572  C CA  . THR A 325 ? 0.9254 0.8267 0.6146 0.2419  0.0288  0.1450  626 THR A CA  
2573  C C   . THR A 325 ? 0.8566 0.8029 0.5643 0.2434  0.0242  0.1351  626 THR A C   
2574  O O   . THR A 325 ? 0.8099 0.7812 0.5431 0.2352  0.0227  0.1247  626 THR A O   
2575  C CB  . THR A 325 ? 0.8779 0.7614 0.5676 0.2212  0.0367  0.1509  626 THR A CB  
2576  O OG1 . THR A 325 ? 0.9200 0.8001 0.5919 0.2238  0.0386  0.1587  626 THR A OG1 
2577  C CG2 . THR A 325 ? 0.7207 0.5632 0.3988 0.2143  0.0414  0.1580  626 THR A CG2 
2578  N N   . SER A 326 ? 0.8869 0.8430 0.5811 0.2532  0.0219  0.1382  627 SER A N   
2579  C CA  . SER A 326 ? 0.8633 0.8603 0.5733 0.2530  0.0177  0.1287  627 SER A CA  
2580  C C   . SER A 326 ? 0.7547 0.7837 0.4793 0.2640  0.0102  0.1178  627 SER A C   
2581  O O   . SER A 326 ? 0.7499 0.8143 0.4912 0.2609  0.0065  0.1082  627 SER A O   
2582  C CB  . SER A 326 ? 0.8075 0.8065 0.4969 0.2625  0.0167  0.1348  627 SER A CB  
2583  O OG  . SER A 326 ? 0.9047 0.8805 0.5656 0.2814  0.0148  0.1444  627 SER A OG  
2584  N N   . SER A 327 ? 0.7329 0.7514 0.4515 0.2763  0.0078  0.1187  628 SER A N   
2585  C CA  . SER A 327 ? 0.7139 0.7654 0.4508 0.2832  0.0019  0.1075  628 SER A CA  
2586  C C   . SER A 327 ? 0.7436 0.8088 0.5092 0.2635  0.0045  0.0989  628 SER A C   
2587  O O   . SER A 327 ? 0.7866 0.8850 0.5712 0.2642  0.0003  0.0885  628 SER A O   
2588  C CB  . SER A 327 ? 0.6494 0.6860 0.3724 0.3021  -0.0008 0.1102  628 SER A CB  
2589  O OG  . SER A 327 ? 0.7862 0.7936 0.5107 0.2929  0.0041  0.1129  628 SER A OG  
2590  N N   . LEU A 328 ? 0.6918 0.7326 0.4602 0.2460  0.0112  0.1030  629 LEU A N   
2591  C CA  . LEU A 328 ? 0.6787 0.7272 0.4716 0.2276  0.0141  0.0962  629 LEU A CA  
2592  C C   . LEU A 328 ? 0.6542 0.7054 0.4553 0.2323  0.0125  0.0919  629 LEU A C   
2593  O O   . LEU A 328 ? 0.6426 0.7158 0.4660 0.2228  0.0119  0.0833  629 LEU A O   
2594  C CB  . LEU A 328 ? 0.6537 0.7373 0.4671 0.2176  0.0118  0.0865  629 LEU A CB  
2595  C CG  . LEU A 328 ? 0.6108 0.6923 0.4174 0.2118  0.0139  0.0897  629 LEU A CG  
2596  C CD1 . LEU A 328 ? 0.5054 0.6144 0.3332 0.1986  0.0126  0.0795  629 LEU A CD1 
2597  C CD2 . LEU A 328 ? 0.6013 0.6474 0.3976 0.2020  0.0212  0.0993  629 LEU A CD2 
2598  N N   . TRP A 329 ? 0.7106 0.7384 0.4924 0.2473  0.0118  0.0980  630 TRP A N   
2599  C CA  . TRP A 329 ? 0.6882 0.7170 0.4757 0.2533  0.0105  0.0939  630 TRP A CA  
2600  C C   . TRP A 329 ? 0.7007 0.7170 0.5026 0.2344  0.0157  0.0924  630 TRP A C   
2601  O O   . TRP A 329 ? 0.7451 0.7790 0.5637 0.2316  0.0149  0.0851  630 TRP A O   
2602  C CB  . TRP A 329 ? 0.6113 0.6114 0.3725 0.2733  0.0090  0.1011  630 TRP A CB  
2603  C CG  . TRP A 329 ? 0.7088 0.6612 0.4489 0.2684  0.0142  0.1123  630 TRP A CG  
2604  C CD1 . TRP A 329 ? 0.7991 0.7299 0.5175 0.2714  0.0157  0.1219  630 TRP A CD1 
2605  C CD2 . TRP A 329 ? 0.7398 0.6602 0.4774 0.2595  0.0186  0.1150  630 TRP A CD2 
2606  N NE1 . TRP A 329 ? 0.7654 0.6531 0.4686 0.2635  0.0211  0.1306  630 TRP A NE1 
2607  C CE2 . TRP A 329 ? 0.7912 0.6718 0.5060 0.2561  0.0227  0.1262  630 TRP A CE2 
2608  C CE3 . TRP A 329 ? 0.7251 0.6474 0.4772 0.2535  0.0196  0.1090  630 TRP A CE3 
2609  C CZ2 . TRP A 329 ? 0.7496 0.5929 0.4567 0.2462  0.0273  0.1309  630 TRP A CZ2 
2610  C CZ3 . TRP A 329 ? 0.7251 0.6103 0.4689 0.2449  0.0239  0.1135  630 TRP A CZ3 
2611  C CH2 . TRP A 329 ? 0.7158 0.5621 0.4376 0.2411  0.0275  0.1241  630 TRP A CH2 
2612  N N   . LYS A 330 ? 0.7061 0.6945 0.5023 0.2209  0.0212  0.0991  631 LYS A N   
2613  C CA  . LYS A 330 ? 0.7388 0.7167 0.5485 0.2029  0.0258  0.0976  631 LYS A CA  
2614  C C   . LYS A 330 ? 0.7549 0.7654 0.5910 0.1899  0.0253  0.0884  631 LYS A C   
2615  O O   . LYS A 330 ? 0.7053 0.7227 0.5559 0.1833  0.0259  0.0832  631 LYS A O   
2616  C CB  . LYS A 330 ? 0.6739 0.6213 0.4733 0.1908  0.0314  0.1061  631 LYS A CB  
2617  C CG  . LYS A 330 ? 0.7895 0.6973 0.5648 0.1979  0.0333  0.1149  631 LYS A CG  
2618  C CD  . LYS A 330 ? 0.8009 0.6817 0.5681 0.1832  0.0393  0.1227  631 LYS A CD  
2619  C CE  . LYS A 330 ? 0.7998 0.6396 0.5471 0.1854  0.0415  0.1296  631 LYS A CE  
2620  N NZ  . LYS A 330 ? 0.8394 0.6537 0.5775 0.1705  0.0476  0.1378  631 LYS A NZ  
2621  N N   . ASP A 331 ? 0.7241 0.7534 0.5654 0.1858  0.0242  0.0865  632 ASP A N   
2622  C CA  . ASP A 331 ? 0.6447 0.7019 0.5089 0.1731  0.0235  0.0777  632 ASP A CA  
2623  C C   . ASP A 331 ? 0.6085 0.6945 0.4854 0.1790  0.0192  0.0694  632 ASP A C   
2624  O O   . ASP A 331 ? 0.5214 0.6207 0.4165 0.1675  0.0200  0.0633  632 ASP A O   
2625  C CB  . ASP A 331 ? 0.6371 0.7089 0.5015 0.1705  0.0222  0.0764  632 ASP A CB  
2626  C CG  . ASP A 331 ? 0.5544 0.6007 0.4019 0.1689  0.0262  0.0856  632 ASP A CG  
2627  O OD1 . ASP A 331 ? 0.5407 0.5696 0.3679 0.1813  0.0261  0.0931  632 ASP A OD1 
2628  O OD2 . ASP A 331 ? 0.5855 0.6294 0.4396 0.1555  0.0296  0.0854  632 ASP A OD2 
2629  N N   . GLN A 332 ? 0.5654 0.6620 0.4324 0.1972  0.0148  0.0693  633 GLN A N   
2630  C CA  . GLN A 332 ? 0.5113 0.6405 0.3906 0.2040  0.0105  0.0610  633 GLN A CA  
2631  C C   . GLN A 332 ? 0.6096 0.7317 0.4943 0.2031  0.0127  0.0598  633 GLN A C   
2632  O O   . GLN A 332 ? 0.6136 0.7580 0.5170 0.1942  0.0127  0.0528  633 GLN A O   
2633  C CB  . GLN A 332 ? 0.4877 0.6288 0.3532 0.2258  0.0052  0.0617  633 GLN A CB  
2634  C CG  . GLN A 332 ? 0.5806 0.7644 0.4582 0.2281  -0.0002 0.0530  633 GLN A CG  
2635  C CD  . GLN A 332 ? 0.7191 0.9120 0.5801 0.2505  -0.0057 0.0548  633 GLN A CD  
2636  O OE1 . GLN A 332 ? 0.7750 0.9381 0.6135 0.2632  -0.0050 0.0637  633 GLN A OE1 
2637  N NE2 . GLN A 332 ? 0.7931 1.0268 0.6644 0.2553  -0.0113 0.0464  633 GLN A NE2 
2638  N N   . ALA A 333 ? 0.5479 0.6380 0.4154 0.2120  0.0145  0.0666  634 ALA A N   
2639  C CA  . ALA A 333 ? 0.6869 0.7674 0.5574 0.2119  0.0164  0.0653  634 ALA A CA  
2640  C C   . ALA A 333 ? 0.6794 0.7541 0.5651 0.1907  0.0209  0.0638  634 ALA A C   
2641  O O   . ALA A 333 ? 0.6734 0.7574 0.5704 0.1868  0.0218  0.0593  634 ALA A O   
2642  C CB  . ALA A 333 ? 0.7253 0.7678 0.5718 0.2246  0.0172  0.0730  634 ALA A CB  
2643  N N   . LEU A 334 ? 0.6721 0.7330 0.5580 0.1773  0.0238  0.0675  635 LEU A N   
2644  C CA  . LEU A 334 ? 0.5761 0.6322 0.4759 0.1585  0.0276  0.0660  635 LEU A CA  
2645  C C   . LEU A 334 ? 0.6020 0.6910 0.5229 0.1495  0.0262  0.0576  635 LEU A C   
2646  O O   . LEU A 334 ? 0.4257 0.5162 0.3576 0.1401  0.0283  0.0549  635 LEU A O   
2647  C CB  . LEU A 334 ? 0.5598 0.5978 0.4554 0.1478  0.0306  0.0710  635 LEU A CB  
2648  C CG  . LEU A 334 ? 0.5838 0.6175 0.4927 0.1294  0.0342  0.0696  635 LEU A CG  
2649  C CD1 . LEU A 334 ? 0.5214 0.5294 0.4266 0.1250  0.0375  0.0729  635 LEU A CD1 
2650  C CD2 . LEU A 334 ? 0.6017 0.6312 0.5093 0.1216  0.0358  0.0721  635 LEU A CD2 
2651  N N   . VAL A 335 ? 0.5319 0.6472 0.4581 0.1516  0.0227  0.0534  636 VAL A N   
2652  C CA  . VAL A 335 ? 0.4947 0.6401 0.4401 0.1415  0.0214  0.0453  636 VAL A CA  
2653  C C   . VAL A 335 ? 0.5410 0.7029 0.4936 0.1462  0.0209  0.0412  636 VAL A C   
2654  O O   . VAL A 335 ? 0.4136 0.5847 0.3799 0.1341  0.0228  0.0375  636 VAL A O   
2655  C CB  . VAL A 335 ? 0.4873 0.6589 0.4362 0.1434  0.0172  0.0406  636 VAL A CB  
2656  C CG1 . VAL A 335 ? 0.4002 0.5999 0.3685 0.1305  0.0161  0.0322  636 VAL A CG1 
2657  C CG2 . VAL A 335 ? 0.3911 0.5474 0.3325 0.1388  0.0180  0.0442  636 VAL A CG2 
2658  N N   . GLU A 336 ? 0.4815 0.6472 0.4240 0.1644  0.0185  0.0420  637 GLU A N   
2659  C CA  . GLU A 336 ? 0.5407 0.7254 0.4897 0.1708  0.0180  0.0375  637 GLU A CA  
2660  C C   . GLU A 336 ? 0.5657 0.7289 0.5152 0.1643  0.0223  0.0396  637 GLU A C   
2661  O O   . GLU A 336 ? 0.5302 0.7112 0.4922 0.1584  0.0236  0.0350  637 GLU A O   
2662  C CB  . GLU A 336 ? 0.5427 0.7330 0.4784 0.1941  0.0142  0.0381  637 GLU A CB  
2663  C CG  . GLU A 336 ? 0.6320 0.8477 0.5670 0.2025  0.0092  0.0354  637 GLU A CG  
2664  C CD  . GLU A 336 ? 0.6228 0.8833 0.5784 0.1948  0.0070  0.0261  637 GLU A CD  
2665  O OE1 . GLU A 336 ? 0.5533 0.8255 0.5231 0.1835  0.0097  0.0223  637 GLU A OE1 
2666  O OE2 . GLU A 336 ? 0.5442 0.8286 0.5012 0.1997  0.0026  0.0226  637 GLU A OE2 
2667  N N   . ILE A 337 ? 0.6218 0.7478 0.5574 0.1652  0.0246  0.0463  638 ILE A N   
2668  C CA  . ILE A 337 ? 0.5447 0.6496 0.4803 0.1582  0.0284  0.0479  638 ILE A CA  
2669  C C   . ILE A 337 ? 0.5637 0.6777 0.5163 0.1385  0.0309  0.0452  638 ILE A C   
2670  O O   . ILE A 337 ? 0.5357 0.6547 0.4960 0.1332  0.0329  0.0426  638 ILE A O   
2671  C CB  . ILE A 337 ? 0.5185 0.5826 0.4369 0.1595  0.0303  0.0555  638 ILE A CB  
2672  C CG1 . ILE A 337 ? 0.5660 0.6168 0.4652 0.1798  0.0279  0.0583  638 ILE A CG1 
2673  C CG2 . ILE A 337 ? 0.4205 0.4634 0.3405 0.1490  0.0340  0.0566  638 ILE A CG2 
2674  C CD1 . ILE A 337 ? 0.6267 0.6398 0.5072 0.1809  0.0293  0.0664  638 ILE A CD1 
2675  N N   . ASN A 338 ? 0.4978 0.6146 0.4557 0.1281  0.0307  0.0454  639 ASN A N   
2676  C CA  . ASN A 338 ? 0.4678 0.5886 0.4393 0.1102  0.0329  0.0432  639 ASN A CA  
2677  C C   . ASN A 338 ? 0.4830 0.6373 0.4696 0.1050  0.0318  0.0364  639 ASN A C   
2678  O O   . ASN A 338 ? 0.4591 0.6159 0.4556 0.0919  0.0340  0.0347  639 ASN A O   
2679  C CB  . ASN A 338 ? 0.4622 0.5728 0.4328 0.1020  0.0331  0.0453  639 ASN A CB  
2680  C CG  . ASN A 338 ? 0.5041 0.5825 0.4655 0.0989  0.0361  0.0515  639 ASN A CG  
2681  O OD1 . ASN A 338 ? 0.5853 0.6541 0.5525 0.0872  0.0385  0.0518  639 ASN A OD1 
2682  N ND2 . ASN A 338 ? 0.5971 0.6587 0.5435 0.1095  0.0359  0.0564  639 ASN A ND2 
2683  N N   . ILE A 339 ? 0.4299 0.6103 0.4179 0.1148  0.0283  0.0327  640 ILE A N   
2684  C CA  . ILE A 339 ? 0.4143 0.6294 0.4164 0.1104  0.0275  0.0261  640 ILE A CA  
2685  C C   . ILE A 339 ? 0.5081 0.7264 0.5118 0.1139  0.0300  0.0255  640 ILE A C   
2686  O O   . ILE A 339 ? 0.4531 0.6842 0.4681 0.1020  0.0323  0.0228  640 ILE A O   
2687  C CB  . ILE A 339 ? 0.3707 0.6152 0.3735 0.1215  0.0228  0.0218  640 ILE A CB  
2688  C CG1 . ILE A 339 ? 0.4470 0.6951 0.4518 0.1142  0.0204  0.0203  640 ILE A CG1 
2689  C CG2 . ILE A 339 ? 0.3668 0.6494 0.3829 0.1203  0.0223  0.0151  640 ILE A CG2 
2690  C CD1 . ILE A 339 ? 0.4187 0.6952 0.4232 0.1253  0.0153  0.0161  640 ILE A CD1 
2691  N N   . ALA A 340 ? 0.5333 0.7379 0.5241 0.1303  0.0296  0.0282  641 ALA A N   
2692  C CA  . ALA A 340 ? 0.5827 0.7886 0.5724 0.1366  0.0315  0.0272  641 ALA A CA  
2693  C C   . ALA A 340 ? 0.5496 0.7373 0.5429 0.1221  0.0358  0.0292  641 ALA A C   
2694  O O   . ALA A 340 ? 0.4776 0.6801 0.4784 0.1183  0.0380  0.0264  641 ALA A O   
2695  C CB  . ALA A 340 ? 0.4703 0.6553 0.4420 0.1564  0.0301  0.0304  641 ALA A CB  
2696  N N   . VAL A 341 ? 0.3793 0.5365 0.3670 0.1146  0.0369  0.0340  642 VAL A N   
2697  C CA  . VAL A 341 ? 0.4723 0.6115 0.4624 0.1020  0.0403  0.0360  642 VAL A CA  
2698  C C   . VAL A 341 ? 0.4360 0.5949 0.4409 0.0861  0.0418  0.0329  642 VAL A C   
2699  O O   . VAL A 341 ? 0.4766 0.6398 0.4862 0.0805  0.0443  0.0320  642 VAL A O   
2700  C CB  . VAL A 341 ? 0.4582 0.5650 0.4401 0.0974  0.0409  0.0413  642 VAL A CB  
2701  C CG1 . VAL A 341 ? 0.4557 0.5481 0.4419 0.0836  0.0439  0.0427  642 VAL A CG1 
2702  C CG2 . VAL A 341 ? 0.3998 0.4832 0.3655 0.1112  0.0403  0.0448  642 VAL A CG2 
2703  N N   . LEU A 342 ? 0.4486 0.6191 0.4602 0.0787  0.0401  0.0313  643 LEU A N   
2704  C CA  . LEU A 342 ? 0.4578 0.6435 0.4817 0.0627  0.0412  0.0285  643 LEU A CA  
2705  C C   . LEU A 342 ? 0.5316 0.7495 0.5642 0.0628  0.0420  0.0240  643 LEU A C   
2706  O O   . LEU A 342 ? 0.4664 0.6906 0.5060 0.0510  0.0447  0.0233  643 LEU A O   
2707  C CB  . LEU A 342 ? 0.3939 0.5848 0.4216 0.0557  0.0387  0.0267  643 LEU A CB  
2708  C CG  . LEU A 342 ? 0.4184 0.5810 0.4399 0.0520  0.0387  0.0305  643 LEU A CG  
2709  C CD1 . LEU A 342 ? 0.4394 0.6086 0.4606 0.0524  0.0354  0.0284  643 LEU A CD1 
2710  C CD2 . LEU A 342 ? 0.3038 0.4528 0.3293 0.0375  0.0411  0.0317  643 LEU A CD2 
2711  N N   . TYR A 343 ? 0.5769 0.8167 0.6090 0.0763  0.0395  0.0210  644 TYR A N   
2712  C CA  . TYR A 343 ? 0.4579 0.7333 0.4992 0.0773  0.0402  0.0161  644 TYR A CA  
2713  C C   . TYR A 343 ? 0.5614 0.8329 0.6004 0.0806  0.0438  0.0172  644 TYR A C   
2714  O O   . TYR A 343 ? 0.5300 0.8245 0.5779 0.0732  0.0465  0.0146  644 TYR A O   
2715  C CB  . TYR A 343 ? 0.3593 0.6581 0.3991 0.0940  0.0363  0.0126  644 TYR A CB  
2716  C CG  . TYR A 343 ? 0.3216 0.6578 0.3689 0.1003  0.0369  0.0075  644 TYR A CG  
2717  C CD1 . TYR A 343 ? 0.3398 0.7104 0.4020 0.0869  0.0377  0.0027  644 TYR A CD1 
2718  C CD2 . TYR A 343 ? 0.3492 0.6868 0.3882 0.1197  0.0367  0.0072  644 TYR A CD2 
2719  C CE1 . TYR A 343 ? 0.4419 0.8506 0.5121 0.0919  0.0386  -0.0022 644 TYR A CE1 
2720  C CE2 . TYR A 343 ? 0.4480 0.8230 0.4943 0.1268  0.0372  0.0020  644 TYR A CE2 
2721  C CZ  . TYR A 343 ? 0.4784 0.8907 0.5410 0.1125  0.0384  -0.0027 644 TYR A CZ  
2722  O OH  . TYR A 343 ? 0.5429 0.9965 0.6140 0.1183  0.0395  -0.0081 644 TYR A OH  
2723  N N   . SER A 344 ? 0.5400 0.7828 0.5663 0.0914  0.0440  0.0208  645 SER A N   
2724  C CA  . SER A 344 ? 0.4798 0.7181 0.5021 0.0966  0.0467  0.0210  645 SER A CA  
2725  C C   . SER A 344 ? 0.4554 0.6835 0.4821 0.0796  0.0505  0.0231  645 SER A C   
2726  O O   . SER A 344 ? 0.4217 0.6674 0.4537 0.0758  0.0535  0.0213  645 SER A O   
2727  C CB  . SER A 344 ? 0.4262 0.6341 0.4326 0.1117  0.0454  0.0239  645 SER A CB  
2728  O OG  . SER A 344 ? 0.5063 0.7272 0.5073 0.1301  0.0423  0.0215  645 SER A OG  
2729  N N   . PHE A 345 ? 0.3934 0.5943 0.4176 0.0698  0.0504  0.0270  646 PHE A N   
2730  C CA  . PHE A 345 ? 0.4149 0.6049 0.4423 0.0546  0.0534  0.0292  646 PHE A CA  
2731  C C   . PHE A 345 ? 0.4826 0.6991 0.5219 0.0409  0.0552  0.0269  646 PHE A C   
2732  O O   . PHE A 345 ? 0.5218 0.7422 0.5633 0.0329  0.0585  0.0276  646 PHE A O   
2733  C CB  . PHE A 345 ? 0.3796 0.5405 0.4033 0.0474  0.0524  0.0330  646 PHE A CB  
2734  C CG  . PHE A 345 ? 0.4206 0.5521 0.4335 0.0541  0.0524  0.0363  646 PHE A CG  
2735  C CD1 . PHE A 345 ? 0.4406 0.5646 0.4443 0.0693  0.0508  0.0363  646 PHE A CD1 
2736  C CD2 . PHE A 345 ? 0.3697 0.4804 0.3809 0.0450  0.0539  0.0392  646 PHE A CD2 
2737  C CE1 . PHE A 345 ? 0.4577 0.5531 0.4507 0.0737  0.0509  0.0391  646 PHE A CE1 
2738  C CE2 . PHE A 345 ? 0.3352 0.4208 0.3372 0.0498  0.0538  0.0415  646 PHE A CE2 
2739  C CZ  . PHE A 345 ? 0.4865 0.5638 0.4794 0.0634  0.0524  0.0414  646 PHE A CZ  
2740  N N   . GLN A 346 ? 0.4668 0.7012 0.5128 0.0374  0.0530  0.0241  647 GLN A N   
2741  C CA  . GLN A 346 ? 0.4475 0.7055 0.5044 0.0222  0.0545  0.0216  647 GLN A CA  
2742  C C   . GLN A 346 ? 0.4785 0.7690 0.5411 0.0249  0.0572  0.0186  647 GLN A C   
2743  O O   . GLN A 346 ? 0.4978 0.8007 0.5663 0.0113  0.0606  0.0186  647 GLN A O   
2744  C CB  . GLN A 346 ? 0.4101 0.6807 0.4724 0.0185  0.0509  0.0183  647 GLN A CB  
2745  C CG  . GLN A 346 ? 0.4006 0.6443 0.4600 0.0091  0.0494  0.0206  647 GLN A CG  
2746  C CD  . GLN A 346 ? 0.5647 0.8162 0.6258 0.0113  0.0451  0.0173  647 GLN A CD  
2747  O OE1 . GLN A 346 ? 0.5657 0.7967 0.6234 0.0070  0.0435  0.0186  647 GLN A OE1 
2748  N NE2 . GLN A 346 ? 0.5836 0.8661 0.6497 0.0187  0.0431  0.0128  647 GLN A NE2 
2749  N N   . SER A 347 ? 0.4656 0.7705 0.5257 0.0427  0.0557  0.0159  648 SER A N   
2750  C CA  . SER A 347 ? 0.4030 0.7421 0.4687 0.0476  0.0581  0.0122  648 SER A CA  
2751  C C   . SER A 347 ? 0.5674 0.8968 0.6288 0.0460  0.0626  0.0147  648 SER A C   
2752  O O   . SER A 347 ? 0.4545 0.8079 0.5226 0.0375  0.0665  0.0135  648 SER A O   
2753  C CB  . SER A 347 ? 0.3982 0.7519 0.4602 0.0696  0.0548  0.0087  648 SER A CB  
2754  O OG  . SER A 347 ? 0.4990 0.8715 0.5669 0.0705  0.0508  0.0054  648 SER A OG  
2755  N N   . ASP A 348 ? 0.5607 0.8553 0.6105 0.0531  0.0621  0.0183  649 ASP A N   
2756  C CA  . ASP A 348 ? 0.4890 0.7702 0.5334 0.0509  0.0657  0.0207  649 ASP A CA  
2757  C C   . ASP A 348 ? 0.4346 0.6994 0.4806 0.0317  0.0679  0.0250  649 ASP A C   
2758  O O   . ASP A 348 ? 0.5389 0.7860 0.5785 0.0304  0.0700  0.0277  649 ASP A O   
2759  C CB  . ASP A 348 ? 0.4493 0.6996 0.4804 0.0654  0.0638  0.0222  649 ASP A CB  
2760  C CG  . ASP A 348 ? 0.5327 0.7950 0.5587 0.0860  0.0620  0.0182  649 ASP A CG  
2761  O OD1 . ASP A 348 ? 0.4663 0.7645 0.5002 0.0902  0.0623  0.0140  649 ASP A OD1 
2762  O OD2 . ASP A 348 ? 0.6326 0.8684 0.6465 0.0982  0.0602  0.0191  649 ASP A OD2 
2763  N N   . LYS A 349 ? 0.4516 0.7197 0.5045 0.0179  0.0671  0.0254  650 LYS A N   
2764  C CA  . LYS A 349 ? 0.4938 0.7453 0.5469 0.0002  0.0690  0.0294  650 LYS A CA  
2765  C C   . LYS A 349 ? 0.4548 0.6691 0.4980 0.0022  0.0683  0.0337  650 LYS A C   
2766  O O   . LYS A 349 ? 0.5242 0.7265 0.5641 -0.0060 0.0708  0.0371  650 LYS A O   
2767  C CB  . LYS A 349 ? 0.5565 0.8289 0.6139 -0.0110 0.0740  0.0299  650 LYS A CB  
2768  C CG  . LYS A 349 ? 0.6416 0.9533 0.7104 -0.0167 0.0749  0.0254  650 LYS A CG  
2769  C CD  . LYS A 349 ? 0.6958 1.0361 0.7678 -0.0185 0.0801  0.0246  650 LYS A CD  
2770  C CE  . LYS A 349 ? 0.7767 1.1298 0.8546 -0.0407 0.0841  0.0263  650 LYS A CE  
2771  N NZ  . LYS A 349 ? 0.8831 1.2604 0.9718 -0.0493 0.0822  0.0220  650 LYS A NZ  
2772  N N   . VAL A 350 ? 0.5314 0.7278 0.5695 0.0129  0.0648  0.0337  651 VAL A N   
2773  C CA  . VAL A 350 ? 0.4762 0.6393 0.5063 0.0139  0.0637  0.0373  651 VAL A CA  
2774  C C   . VAL A 350 ? 0.4666 0.6158 0.4982 0.0076  0.0610  0.0384  651 VAL A C   
2775  O O   . VAL A 350 ? 0.5095 0.6659 0.5432 0.0124  0.0585  0.0363  651 VAL A O   
2776  C CB  . VAL A 350 ? 0.3699 0.5215 0.3917 0.0299  0.0623  0.0366  651 VAL A CB  
2777  C CG1 . VAL A 350 ? 0.3419 0.4608 0.3564 0.0297  0.0608  0.0398  651 VAL A CG1 
2778  C CG2 . VAL A 350 ? 0.4887 0.6523 0.5079 0.0363  0.0649  0.0349  651 VAL A CG2 
2779  N N   . THR A 351 ? 0.4290 0.5587 0.4586 -0.0022 0.0614  0.0416  652 THR A N   
2780  C CA  . THR A 351 ? 0.3782 0.4955 0.4090 -0.0088 0.0591  0.0422  652 THR A CA  
2781  C C   . THR A 351 ? 0.4822 0.5898 0.5100 0.0009  0.0563  0.0418  652 THR A C   
2782  O O   . THR A 351 ? 0.4946 0.5882 0.5163 0.0092  0.0560  0.0433  652 THR A O   
2783  C CB  . THR A 351 ? 0.4576 0.5525 0.4844 -0.0167 0.0596  0.0458  652 THR A CB  
2784  O OG1 . THR A 351 ? 0.5051 0.6062 0.5324 -0.0258 0.0625  0.0472  652 THR A OG1 
2785  C CG2 . THR A 351 ? 0.3178 0.4012 0.3454 -0.0227 0.0572  0.0456  652 THR A CG2 
2786  N N   . ILE A 352 ? 0.4523 0.5667 0.4838 -0.0010 0.0542  0.0397  653 ILE A N   
2787  C CA  . ILE A 352 ? 0.3859 0.4904 0.4138 0.0063  0.0517  0.0399  653 ILE A CA  
2788  C C   . ILE A 352 ? 0.4482 0.5556 0.4800 -0.0011 0.0497  0.0378  653 ILE A C   
2789  O O   . ILE A 352 ? 0.4327 0.5532 0.4700 -0.0105 0.0499  0.0355  653 ILE A O   
2790  C CB  . ILE A 352 ? 0.3907 0.5073 0.4165 0.0197  0.0507  0.0384  653 ILE A CB  
2791  C CG1 . ILE A 352 ? 0.3372 0.4363 0.3556 0.0282  0.0490  0.0406  653 ILE A CG1 
2792  C CG2 . ILE A 352 ? 0.3901 0.5348 0.4229 0.0192  0.0494  0.0342  653 ILE A CG2 
2793  C CD1 . ILE A 352 ? 0.3190 0.4196 0.3308 0.0424  0.0485  0.0407  653 ILE A CD1 
2794  N N   . VAL A 353 ? 0.4181 0.5125 0.4462 0.0025  0.0479  0.0386  654 VAL A N   
2795  C CA  . VAL A 353 ? 0.4087 0.5045 0.4387 -0.0023 0.0456  0.0361  654 VAL A CA  
2796  C C   . VAL A 353 ? 0.4589 0.5566 0.4852 0.0079  0.0437  0.0357  654 VAL A C   
2797  O O   . VAL A 353 ? 0.3439 0.4284 0.3641 0.0155  0.0443  0.0391  654 VAL A O   
2798  C CB  . VAL A 353 ? 0.4343 0.5096 0.4622 -0.0095 0.0456  0.0375  654 VAL A CB  
2799  C CG1 . VAL A 353 ? 0.3716 0.4292 0.3939 -0.0031 0.0460  0.0409  654 VAL A CG1 
2800  C CG2 . VAL A 353 ? 0.4199 0.4974 0.4495 -0.0155 0.0433  0.0337  654 VAL A CG2 
2801  N N   . ASP A 354 ? 0.4889 0.6034 0.5184 0.0079  0.0412  0.0317  655 ASP A N   
2802  C CA  . ASP A 354 ? 0.4500 0.5662 0.4747 0.0176  0.0392  0.0317  655 ASP A CA  
2803  C C   . ASP A 354 ? 0.4387 0.5383 0.4597 0.0150  0.0386  0.0324  655 ASP A C   
2804  O O   . ASP A 354 ? 0.3770 0.4669 0.4000 0.0059  0.0390  0.0317  655 ASP A O   
2805  C CB  . ASP A 354 ? 0.4996 0.6418 0.5288 0.0195  0.0363  0.0266  655 ASP A CB  
2806  C CG  . ASP A 354 ? 0.5792 0.7290 0.6146 0.0067  0.0348  0.0216  655 ASP A CG  
2807  O OD1 . ASP A 354 ? 0.6525 0.8117 0.6943 -0.0026 0.0359  0.0198  655 ASP A OD1 
2808  O OD2 . ASP A 354 ? 0.4789 0.6238 0.5119 0.0057  0.0326  0.0196  655 ASP A OD2 
2809  N N   . HIS A 355 ? 0.4380 0.5345 0.4527 0.0238  0.0377  0.0340  656 HIS A N   
2810  C CA  . HIS A 355 ? 0.4105 0.4927 0.4212 0.0223  0.0378  0.0351  656 HIS A CA  
2811  C C   . HIS A 355 ? 0.3657 0.4543 0.3799 0.0154  0.0354  0.0296  656 HIS A C   
2812  O O   . HIS A 355 ? 0.4580 0.5341 0.4712 0.0108  0.0356  0.0291  656 HIS A O   
2813  C CB  . HIS A 355 ? 0.3974 0.4751 0.3995 0.0326  0.0380  0.0387  656 HIS A CB  
2814  C CG  . HIS A 355 ? 0.4293 0.5239 0.4290 0.0410  0.0355  0.0369  656 HIS A CG  
2815  N ND1 . HIS A 355 ? 0.4811 0.5841 0.4800 0.0484  0.0352  0.0378  656 HIS A ND1 
2816  C CD2 . HIS A 355 ? 0.4001 0.5053 0.3974 0.0446  0.0328  0.0342  656 HIS A CD2 
2817  C CE1 . HIS A 355 ? 0.4055 0.5243 0.4019 0.0563  0.0324  0.0358  656 HIS A CE1 
2818  N NE2 . HIS A 355 ? 0.4387 0.5592 0.4340 0.0539  0.0308  0.0336  656 HIS A NE2 
2819  N N   . HIS A 356 ? 0.3070 0.4152 0.3252 0.0144  0.0327  0.0247  657 HIS A N   
2820  C CA  . HIS A 356 ? 0.3638 0.4769 0.3847 0.0066  0.0300  0.0186  657 HIS A CA  
2821  C C   . HIS A 356 ? 0.4623 0.5641 0.4867 -0.0054 0.0310  0.0175  657 HIS A C   
2822  O O   . HIS A 356 ? 0.5080 0.5961 0.5297 -0.0094 0.0303  0.0159  657 HIS A O   
2823  C CB  . HIS A 356 ? 0.3113 0.4499 0.3366 0.0068  0.0269  0.0133  657 HIS A CB  
2824  C CG  . HIS A 356 ? 0.4688 0.6178 0.4890 0.0200  0.0254  0.0145  657 HIS A CG  
2825  N ND1 . HIS A 356 ? 0.4261 0.5711 0.4394 0.0253  0.0238  0.0140  657 HIS A ND1 
2826  C CD2 . HIS A 356 ? 0.4539 0.6150 0.4730 0.0299  0.0254  0.0166  657 HIS A CD2 
2827  C CE1 . HIS A 356 ? 0.4541 0.6083 0.4621 0.0373  0.0229  0.0162  657 HIS A CE1 
2828  N NE2 . HIS A 356 ? 0.3997 0.5628 0.4108 0.0408  0.0236  0.0178  657 HIS A NE2 
2829  N N   . SER A 357 ? 0.4726 0.5797 0.5020 -0.0107 0.0326  0.0184  658 SER A N   
2830  C CA  A SER A 357 ? 0.4433 0.5383 0.4742 -0.0221 0.0337  0.0184  658 SER A CA  
2831  C CA  B SER A 357 ? 0.4496 0.5446 0.4806 -0.0221 0.0337  0.0184  658 SER A CA  
2832  C C   . SER A 357 ? 0.4768 0.5478 0.5025 -0.0202 0.0353  0.0226  658 SER A C   
2833  O O   . SER A 357 ? 0.4155 0.4722 0.4388 -0.0260 0.0345  0.0210  658 SER A O   
2834  C CB  A SER A 357 ? 0.4536 0.5591 0.4896 -0.0268 0.0359  0.0199  658 SER A CB  
2835  C CB  B SER A 357 ? 0.4500 0.5554 0.4859 -0.0266 0.0359  0.0199  658 SER A CB  
2836  O OG  A SER A 357 ? 0.4652 0.5583 0.5012 -0.0381 0.0372  0.0205  658 SER A OG  
2837  O OG  B SER A 357 ? 0.4084 0.5401 0.4499 -0.0267 0.0345  0.0159  658 SER A OG  
2838  N N   . ALA A 358 ? 0.5199 0.5863 0.5433 -0.0119 0.0374  0.0275  659 ALA A N   
2839  C CA  . ALA A 358 ? 0.4449 0.4921 0.4647 -0.0107 0.0390  0.0313  659 ALA A CA  
2840  C C   . ALA A 358 ? 0.4877 0.5263 0.5038 -0.0090 0.0376  0.0293  659 ALA A C   
2841  O O   . ALA A 358 ? 0.5005 0.5250 0.5147 -0.0117 0.0377  0.0296  659 ALA A O   
2842  C CB  . ALA A 358 ? 0.3563 0.4013 0.3740 -0.0029 0.0413  0.0362  659 ALA A CB  
2843  N N   . THR A 359 ? 0.4669 0.5142 0.4811 -0.0034 0.0363  0.0274  660 THR A N   
2844  C CA  . THR A 359 ? 0.3884 0.4290 0.3986 -0.0010 0.0353  0.0255  660 THR A CA  
2845  C C   . THR A 359 ? 0.4017 0.4385 0.4118 -0.0079 0.0326  0.0195  660 THR A C   
2846  O O   . THR A 359 ? 0.4596 0.4833 0.4667 -0.0084 0.0322  0.0184  660 THR A O   
2847  C CB  . THR A 359 ? 0.4231 0.4736 0.4297 0.0069  0.0348  0.0255  660 THR A CB  
2848  O OG1 . THR A 359 ? 0.3914 0.4584 0.4001 0.0068  0.0324  0.0219  660 THR A OG1 
2849  C CG2 . THR A 359 ? 0.4065 0.4538 0.4101 0.0135  0.0378  0.0321  660 THR A CG2 
2850  N N   . GLU A 360 ? 0.4361 0.4841 0.4494 -0.0136 0.0305  0.0153  661 GLU A N   
2851  C CA  . GLU A 360 ? 0.5727 0.6143 0.5851 -0.0221 0.0278  0.0095  661 GLU A CA  
2852  C C   . GLU A 360 ? 0.5119 0.5339 0.5225 -0.0276 0.0290  0.0118  661 GLU A C   
2853  O O   . GLU A 360 ? 0.5285 0.5354 0.5341 -0.0295 0.0273  0.0087  661 GLU A O   
2854  C CB  . GLU A 360 ? 0.5999 0.6579 0.6171 -0.0296 0.0259  0.0052  661 GLU A CB  
2855  C CG  . GLU A 360 ? 0.7801 0.8300 0.7952 -0.0398 0.0230  -0.0012 661 GLU A CG  
2856  C CD  . GLU A 360 ? 0.9697 1.0358 0.9906 -0.0505 0.0217  -0.0051 661 GLU A CD  
2857  O OE1 . GLU A 360 ? 1.0175 1.1049 1.0445 -0.0478 0.0228  -0.0034 661 GLU A OE1 
2858  O OE2 . GLU A 360 ? 1.0172 1.0749 1.0362 -0.0616 0.0197  -0.0099 661 GLU A OE2 
2859  N N   . SER A 361 ? 0.4850 0.5063 0.4984 -0.0292 0.0317  0.0170  662 SER A N   
2860  C CA  . SER A 361 ? 0.5114 0.5146 0.5220 -0.0338 0.0326  0.0196  662 SER A CA  
2861  C C   . SER A 361 ? 0.5147 0.5039 0.5209 -0.0265 0.0328  0.0213  662 SER A C   
2862  O O   . SER A 361 ? 0.5050 0.4775 0.5063 -0.0283 0.0316  0.0202  662 SER A O   
2863  C CB  . SER A 361 ? 0.4867 0.4944 0.5008 -0.0361 0.0355  0.0247  662 SER A CB  
2864  O OG  . SER A 361 ? 0.5631 0.5819 0.5808 -0.0452 0.0354  0.0227  662 SER A OG  
2865  N N   . PHE A 362 ? 0.4934 0.4895 0.5008 -0.0181 0.0343  0.0238  663 PHE A N   
2866  C CA  . PHE A 362 ? 0.4825 0.4695 0.4869 -0.0118 0.0349  0.0250  663 PHE A CA  
2867  C C   . PHE A 362 ? 0.4657 0.4464 0.4653 -0.0099 0.0323  0.0195  663 PHE A C   
2868  O O   . PHE A 362 ? 0.5034 0.4722 0.4995 -0.0071 0.0318  0.0190  663 PHE A O   
2869  C CB  . PHE A 362 ? 0.4520 0.4478 0.4578 -0.0050 0.0373  0.0287  663 PHE A CB  
2870  C CG  . PHE A 362 ? 0.5156 0.5061 0.5195 0.0001  0.0382  0.0298  663 PHE A CG  
2871  C CD1 . PHE A 362 ? 0.3693 0.3516 0.3738 0.0000  0.0392  0.0327  663 PHE A CD1 
2872  C CD2 . PHE A 362 ? 0.4157 0.4108 0.4171 0.0052  0.0380  0.0273  663 PHE A CD2 
2873  C CE1 . PHE A 362 ? 0.3745 0.3549 0.3782 0.0046  0.0399  0.0331  663 PHE A CE1 
2874  C CE2 . PHE A 362 ? 0.4511 0.4442 0.4513 0.0097  0.0393  0.0280  663 PHE A CE2 
2875  C CZ  . PHE A 362 ? 0.5872 0.5736 0.5891 0.0093  0.0402  0.0308  663 PHE A CZ  
2876  N N   . ILE A 363 ? 0.4661 0.4553 0.4652 -0.0106 0.0304  0.0147  664 ILE A N   
2877  C CA  . ILE A 363 ? 0.5388 0.5215 0.5324 -0.0089 0.0275  0.0083  664 ILE A CA  
2878  C C   . ILE A 363 ? 0.5745 0.5384 0.5636 -0.0152 0.0253  0.0055  664 ILE A C   
2879  O O   . ILE A 363 ? 0.5386 0.4888 0.5217 -0.0112 0.0238  0.0027  664 ILE A O   
2880  C CB  . ILE A 363 ? 0.4688 0.4652 0.4624 -0.0092 0.0254  0.0032  664 ILE A CB  
2881  C CG1 . ILE A 363 ? 0.4529 0.4640 0.4475 -0.0009 0.0275  0.0062  664 ILE A CG1 
2882  C CG2 . ILE A 363 ? 0.3679 0.3553 0.3549 -0.0094 0.0218  -0.0049 664 ILE A CG2 
2883  C CD1 . ILE A 363 ? 0.4653 0.4729 0.4558 0.0069  0.0286  0.0062  664 ILE A CD1 
2884  N N   . LYS A 364 ? 0.5313 0.4942 0.5225 -0.0249 0.0251  0.0062  665 LYS A N   
2885  C CA  . LYS A 364 ? 0.5918 0.5345 0.5773 -0.0321 0.0235  0.0051  665 LYS A CA  
2886  C C   . LYS A 364 ? 0.5688 0.4966 0.5508 -0.0270 0.0247  0.0098  665 LYS A C   
2887  O O   . LYS A 364 ? 0.5587 0.4666 0.5324 -0.0259 0.0225  0.0076  665 LYS A O   
2888  C CB  . LYS A 364 ? 0.5057 0.4536 0.4950 -0.0440 0.0243  0.0065  665 LYS A CB  
2889  C CG  . LYS A 364 ? 0.5339 0.4909 0.5244 -0.0520 0.0218  -0.0001 665 LYS A CG  
2890  C CD  . LYS A 364 ? 0.7114 0.6849 0.7093 -0.0613 0.0236  0.0020  665 LYS A CD  
2891  C CE  . LYS A 364 ? 0.7359 0.7161 0.7346 -0.0731 0.0210  -0.0047 665 LYS A CE  
2892  N NZ  . LYS A 364 ? 0.6753 0.6753 0.6823 -0.0819 0.0233  -0.0026 665 LYS A NZ  
2893  N N   . HIS A 365 ? 0.5728 0.5097 0.5602 -0.0232 0.0278  0.0158  666 HIS A N   
2894  C CA  . HIS A 365 ? 0.5310 0.4575 0.5162 -0.0183 0.0286  0.0199  666 HIS A CA  
2895  C C   . HIS A 365 ? 0.5524 0.4754 0.5342 -0.0082 0.0275  0.0172  666 HIS A C   
2896  O O   . HIS A 365 ? 0.4244 0.3323 0.4001 -0.0043 0.0259  0.0169  666 HIS A O   
2897  C CB  . HIS A 365 ? 0.4980 0.4368 0.4898 -0.0171 0.0319  0.0258  666 HIS A CB  
2898  C CG  . HIS A 365 ? 0.5506 0.4845 0.5418 -0.0109 0.0327  0.0293  666 HIS A CG  
2899  N ND1 . HIS A 365 ? 0.5407 0.4603 0.5272 -0.0121 0.0320  0.0317  666 HIS A ND1 
2900  C CD2 . HIS A 365 ? 0.5280 0.4704 0.5224 -0.0040 0.0341  0.0307  666 HIS A CD2 
2901  C CE1 . HIS A 365 ? 0.4428 0.3638 0.4304 -0.0055 0.0325  0.0339  666 HIS A CE1 
2902  N NE2 . HIS A 365 ? 0.5003 0.4353 0.4931 -0.0012 0.0340  0.0332  666 HIS A NE2 
2903  N N   . MET A 366 ? 0.4932 0.4309 0.4783 -0.0032 0.0282  0.0152  667 MET A N   
2904  C CA  . MET A 366 ? 0.5230 0.4614 0.5054 0.0061  0.0278  0.0124  667 MET A CA  
2905  C C   . MET A 366 ? 0.5385 0.4601 0.5120 0.0081  0.0241  0.0061  667 MET A C   
2906  O O   . MET A 366 ? 0.5507 0.4625 0.5196 0.0149  0.0230  0.0053  667 MET A O   
2907  C CB  . MET A 366 ? 0.6227 0.5791 0.6085 0.0095  0.0294  0.0114  667 MET A CB  
2908  C CG  . MET A 366 ? 0.6158 0.5788 0.6010 0.0185  0.0306  0.0105  667 MET A CG  
2909  S SD  . MET A 366 ? 0.6259 0.6090 0.6134 0.0212  0.0333  0.0113  667 MET A SD  
2910  C CE  . MET A 366 ? 0.5896 0.5773 0.5737 0.0311  0.0340  0.0078  667 MET A CE  
2911  N N   . GLU A 367 ? 0.6388 0.5564 0.6091 0.0021  0.0218  0.0012  668 GLU A N   
2912  C CA  . GLU A 367 ? 0.7869 0.6856 0.7472 0.0032  0.0179  -0.0054 668 GLU A CA  
2913  C C   . GLU A 367 ? 0.7158 0.5912 0.6689 0.0024  0.0165  -0.0032 668 GLU A C   
2914  O O   . GLU A 367 ? 0.7328 0.5931 0.6773 0.0103  0.0141  -0.0066 668 GLU A O   
2915  C CB  . GLU A 367 ? 0.8834 0.7815 0.8419 -0.0061 0.0155  -0.0108 668 GLU A CB  
2916  C CG  . GLU A 367 ? 0.9308 0.8481 0.8922 -0.0023 0.0154  -0.0152 668 GLU A CG  
2917  C CD  . GLU A 367 ? 1.0313 0.9562 0.9947 -0.0123 0.0136  -0.0190 668 GLU A CD  
2918  O OE1 . GLU A 367 ? 1.0982 1.0156 1.0622 -0.0233 0.0132  -0.0178 668 GLU A OE1 
2919  O OE2 . GLU A 367 ? 0.9903 0.9304 0.9548 -0.0093 0.0128  -0.0232 668 GLU A OE2 
2920  N N   . ASN A 368 ? 0.6448 0.5174 0.6006 -0.0060 0.0181  0.0027  669 ASN A N   
2921  C CA  . ASN A 368 ? 0.6761 0.5264 0.6239 -0.0068 0.0170  0.0059  669 ASN A CA  
2922  C C   . ASN A 368 ? 0.6486 0.4994 0.5961 0.0054  0.0173  0.0085  669 ASN A C   
2923  O O   . ASN A 368 ? 0.6549 0.4863 0.5923 0.0118  0.0146  0.0071  669 ASN A O   
2924  C CB  . ASN A 368 ? 0.7651 0.6165 0.7165 -0.0182 0.0193  0.0120  669 ASN A CB  
2925  C CG  . ASN A 368 ? 0.7539 0.5814 0.6954 -0.0202 0.0184  0.0161  669 ASN A CG  
2926  O OD1 . ASN A 368 ? 0.8731 0.6765 0.8028 -0.0229 0.0155  0.0133  669 ASN A OD1 
2927  N ND2 . ASN A 368 ? 0.6317 0.4646 0.5769 -0.0187 0.0207  0.0227  669 ASN A ND2 
2928  N N   . GLU A 369 ? 0.5653 0.4380 0.5233 0.0088  0.0205  0.0122  670 GLU A N   
2929  C CA  . GLU A 369 ? 0.4776 0.3559 0.4372 0.0194  0.0210  0.0139  670 GLU A CA  
2930  C C   . GLU A 369 ? 0.5706 0.4466 0.5248 0.0306  0.0187  0.0075  670 GLU A C   
2931  O O   . GLU A 369 ? 0.5756 0.4446 0.5251 0.0398  0.0170  0.0071  670 GLU A O   
2932  C CB  . GLU A 369 ? 0.4862 0.3884 0.4575 0.0192  0.0248  0.0178  670 GLU A CB  
2933  C CG  . GLU A 369 ? 0.4518 0.3565 0.4276 0.0114  0.0270  0.0239  670 GLU A CG  
2934  C CD  . GLU A 369 ? 0.5578 0.4525 0.5301 0.0138  0.0261  0.0277  670 GLU A CD  
2935  O OE1 . GLU A 369 ? 0.5800 0.4861 0.5577 0.0180  0.0274  0.0302  670 GLU A OE1 
2936  O OE2 . GLU A 369 ? 0.5568 0.4320 0.5204 0.0113  0.0239  0.0280  670 GLU A OE2 
2937  N N   . TYR A 370 ? 0.4719 0.3557 0.4268 0.0311  0.0186  0.0023  671 TYR A N   
2938  C CA  . TYR A 370 ? 0.6024 0.4825 0.5505 0.0420  0.0163  -0.0046 671 TYR A CA  
2939  C C   . TYR A 370 ? 0.6014 0.4518 0.5356 0.0441  0.0118  -0.0082 671 TYR A C   
2940  O O   . TYR A 370 ? 0.6267 0.4694 0.5542 0.0559  0.0096  -0.0108 671 TYR A O   
2941  C CB  . TYR A 370 ? 0.6493 0.5421 0.5990 0.0416  0.0168  -0.0098 671 TYR A CB  
2942  C CG  . TYR A 370 ? 0.6391 0.5591 0.5983 0.0459  0.0208  -0.0075 671 TYR A CG  
2943  C CD1 . TYR A 370 ? 0.6364 0.5710 0.6049 0.0388  0.0244  -0.0013 671 TYR A CD1 
2944  C CD2 . TYR A 370 ? 0.6613 0.5919 0.6192 0.0570  0.0213  -0.0116 671 TYR A CD2 
2945  C CE1 . TYR A 370 ? 0.6446 0.6005 0.6197 0.0417  0.0283  0.0014  671 TYR A CE1 
2946  C CE2 . TYR A 370 ? 0.6005 0.5555 0.5662 0.0593  0.0256  -0.0089 671 TYR A CE2 
2947  C CZ  . TYR A 370 ? 0.6426 0.6088 0.6165 0.0511  0.0290  -0.0021 671 TYR A CZ  
2948  O OH  . TYR A 370 ? 0.6769 0.6637 0.6567 0.0524  0.0334  0.0011  671 TYR A OH  
2949  N N   . ARG A 371 ? 0.7142 0.5474 0.6433 0.0327  0.0103  -0.0080 672 ARG A N   
2950  C CA  . ARG A 371 ? 0.8143 0.6151 0.7282 0.0324  0.0062  -0.0108 672 ARG A CA  
2951  C C   . ARG A 371 ? 0.8058 0.5930 0.7136 0.0401  0.0051  -0.0062 672 ARG A C   
2952  O O   . ARG A 371 ? 0.8112 0.5812 0.7074 0.0515  0.0017  -0.0102 672 ARG A O   
2953  C CB  . ARG A 371 ? 0.9836 0.7720 0.8953 0.0158  0.0061  -0.0093 672 ARG A CB  
2954  C CG  . ARG A 371 ? 1.1968 0.9716 1.1003 0.0103  0.0028  -0.0176 672 ARG A CG  
2955  C CD  . ARG A 371 ? 1.2944 1.0958 1.2081 0.0080  0.0041  -0.0218 672 ARG A CD  
2956  N NE  . ARG A 371 ? 1.3510 1.1637 1.2646 0.0222  0.0036  -0.0271 672 ARG A NE  
2957  C CZ  . ARG A 371 ? 1.3274 1.1559 1.2440 0.0232  0.0034  -0.0329 672 ARG A CZ  
2958  N NH1 . ARG A 371 ? 1.2941 1.1299 1.2146 0.0113  0.0032  -0.0346 672 ARG A NH1 
2959  N NH2 . ARG A 371 ? 1.2948 1.1335 1.2103 0.0364  0.0034  -0.0372 672 ARG A NH2 
2960  N N   . CYS A 372 ? 0.7848 0.5786 0.6990 0.0347  0.0077  0.0017  673 CYS A N   
2961  C CA  . CYS A 372 ? 0.8436 0.6215 0.7500 0.0402  0.0062  0.0063  673 CYS A CA  
2962  C C   . CYS A 372 ? 0.7953 0.5933 0.7093 0.0521  0.0072  0.0083  673 CYS A C   
2963  O O   . CYS A 372 ? 0.7403 0.5274 0.6473 0.0599  0.0051  0.0109  673 CYS A O   
2964  C CB  . CYS A 372 ? 0.8619 0.6318 0.7680 0.0268  0.0080  0.0137  673 CYS A CB  
2965  S SG  . CYS A 372 ? 0.9018 0.7046 0.8266 0.0202  0.0133  0.0199  673 CYS A SG  
2966  N N   . ARG A 373 ? 0.7694 0.5966 0.6970 0.0535  0.0102  0.0073  674 ARG A N   
2967  C CA  . ARG A 373 ? 0.5334 0.3823 0.4699 0.0614  0.0118  0.0096  674 ARG A CA  
2968  C C   . ARG A 373 ? 0.6342 0.5022 0.5752 0.0718  0.0123  0.0039  674 ARG A C   
2969  O O   . ARG A 373 ? 0.6630 0.5482 0.6099 0.0798  0.0130  0.0045  674 ARG A O   
2970  C CB  . ARG A 373 ? 0.5288 0.3963 0.4781 0.0513  0.0160  0.0156  674 ARG A CB  
2971  C CG  . ARG A 373 ? 0.5230 0.4066 0.4794 0.0562  0.0171  0.0192  674 ARG A CG  
2972  C CD  . ARG A 373 ? 0.4488 0.3492 0.4165 0.0466  0.0211  0.0240  674 ARG A CD  
2973  N NE  . ARG A 373 ? 0.5233 0.4383 0.4972 0.0507  0.0216  0.0264  674 ARG A NE  
2974  C CZ  . ARG A 373 ? 0.5259 0.4595 0.5102 0.0457  0.0250  0.0290  674 ARG A CZ  
2975  N NH1 . ARG A 373 ? 0.5649 0.5045 0.5540 0.0378  0.0281  0.0300  674 ARG A NH1 
2976  N NH2 . ARG A 373 ? 0.4577 0.4037 0.4470 0.0487  0.0250  0.0304  674 ARG A NH2 
2977  N N   . GLY A 374 ? 0.5860 0.4531 0.5245 0.0718  0.0120  -0.0018 675 GLY A N   
2978  C CA  . GLY A 374 ? 0.5999 0.4861 0.5418 0.0817  0.0129  -0.0071 675 GLY A CA  
2979  C C   . GLY A 374 ? 0.6756 0.5895 0.6305 0.0759  0.0179  -0.0049 675 GLY A C   
2980  O O   . GLY A 374 ? 0.6758 0.6087 0.6343 0.0830  0.0196  -0.0083 675 GLY A O   
2981  N N   . GLY A 375 ? 0.6141 0.5307 0.5753 0.0638  0.0203  0.0008  676 GLY A N   
2982  C CA  . GLY A 375 ? 0.6537 0.5919 0.6247 0.0583  0.0246  0.0031  676 GLY A CA  
2983  C C   . GLY A 375 ? 0.7175 0.6579 0.6950 0.0479  0.0268  0.0102  676 GLY A C   
2984  O O   . GLY A 375 ? 0.7250 0.6508 0.6996 0.0439  0.0252  0.0130  676 GLY A O   
2985  N N   . CYS A 376 ? 0.6655 0.6238 0.6508 0.0441  0.0306  0.0130  677 CYS A N   
2986  C CA  . CYS A 376 ? 0.5615 0.5231 0.5524 0.0354  0.0329  0.0190  677 CYS A CA  
2987  C C   . CYS A 376 ? 0.5784 0.5591 0.5758 0.0343  0.0371  0.0215  677 CYS A C   
2988  O O   . CYS A 376 ? 0.5517 0.5378 0.5484 0.0330  0.0383  0.0206  677 CYS A O   
2989  C CB  . CYS A 376 ? 0.5239 0.4750 0.5121 0.0278  0.0318  0.0190  677 CYS A CB  
2990  S SG  . CYS A 376 ? 0.4917 0.4510 0.4866 0.0193  0.0349  0.0251  677 CYS A SG  
2991  N N   . PRO A 377 ? 0.5481 0.5388 0.5509 0.0345  0.0392  0.0248  678 PRO A N   
2992  C CA  . PRO A 377 ? 0.5227 0.5293 0.5301 0.0325  0.0434  0.0275  678 PRO A CA  
2993  C C   . PRO A 377 ? 0.5999 0.6042 0.6078 0.0255  0.0451  0.0317  678 PRO A C   
2994  O O   . PRO A 377 ? 0.5994 0.5947 0.6076 0.0211  0.0441  0.0340  678 PRO A O   
2995  C CB  . PRO A 377 ? 0.5022 0.5175 0.5150 0.0327  0.0446  0.0297  678 PRO A CB  
2996  C CG  . PRO A 377 ? 0.4826 0.4842 0.4940 0.0320  0.0413  0.0303  678 PRO A CG  
2997  C CD  . PRO A 377 ? 0.3890 0.3758 0.3933 0.0354  0.0378  0.0265  678 PRO A CD  
2998  N N   . ALA A 378 ? 0.5222 0.5350 0.5293 0.0252  0.0478  0.0327  679 ALA A N   
2999  C CA  . ALA A 378 ? 0.5006 0.5112 0.5063 0.0211  0.0487  0.0357  679 ALA A CA  
3000  C C   . ALA A 378 ? 0.4487 0.4694 0.4534 0.0209  0.0527  0.0390  679 ALA A C   
3001  O O   . ALA A 378 ? 0.4093 0.4390 0.4124 0.0246  0.0541  0.0371  679 ALA A O   
3002  C CB  . ALA A 378 ? 0.4603 0.4657 0.4622 0.0218  0.0458  0.0317  679 ALA A CB  
3003  N N   . ASP A 379 ? 0.4348 0.4529 0.4393 0.0169  0.0545  0.0440  680 ASP A N   
3004  C CA  . ASP A 379 ? 0.4280 0.4510 0.4296 0.0156  0.0584  0.0487  680 ASP A CA  
3005  C C   . ASP A 379 ? 0.4935 0.5145 0.4896 0.0173  0.0579  0.0498  680 ASP A C   
3006  O O   . ASP A 379 ? 0.5081 0.5226 0.5033 0.0157  0.0571  0.0521  680 ASP A O   
3007  C CB  . ASP A 379 ? 0.5218 0.5406 0.5256 0.0102  0.0604  0.0533  680 ASP A CB  
3008  C CG  . ASP A 379 ? 0.5900 0.6118 0.5900 0.0073  0.0649  0.0583  680 ASP A CG  
3009  O OD1 . ASP A 379 ? 0.5925 0.6163 0.5863 0.0097  0.0664  0.0601  680 ASP A OD1 
3010  O OD2 . ASP A 379 ? 0.5749 0.5965 0.5775 0.0021  0.0669  0.0607  680 ASP A OD2 
3011  N N   . TRP A 380 ? 0.4507 0.4789 0.4428 0.0214  0.0580  0.0476  681 TRP A N   
3012  C CA  . TRP A 380 ? 0.3641 0.3931 0.3508 0.0242  0.0567  0.0475  681 TRP A CA  
3013  C C   . TRP A 380 ? 0.3589 0.3836 0.3410 0.0233  0.0588  0.0541  681 TRP A C   
3014  O O   . TRP A 380 ? 0.3909 0.4136 0.3707 0.0252  0.0567  0.0542  681 TRP A O   
3015  C CB  . TRP A 380 ? 0.4689 0.5075 0.4508 0.0288  0.0573  0.0448  681 TRP A CB  
3016  C CG  . TRP A 380 ? 0.4013 0.4434 0.3778 0.0327  0.0549  0.0427  681 TRP A CG  
3017  C CD1 . TRP A 380 ? 0.4002 0.4446 0.3768 0.0347  0.0507  0.0355  681 TRP A CD1 
3018  C CD2 . TRP A 380 ? 0.4136 0.4575 0.3828 0.0352  0.0561  0.0475  681 TRP A CD2 
3019  N NE1 . TRP A 380 ? 0.4389 0.4890 0.4101 0.0380  0.0492  0.0350  681 TRP A NE1 
3020  C CE2 . TRP A 380 ? 0.4112 0.4612 0.3775 0.0392  0.0523  0.0425  681 TRP A CE2 
3021  C CE3 . TRP A 380 ? 0.4313 0.4709 0.3951 0.0346  0.0598  0.0554  681 TRP A CE3 
3022  C CZ2 . TRP A 380 ? 0.4293 0.4833 0.3880 0.0437  0.0519  0.0453  681 TRP A CZ2 
3023  C CZ3 . TRP A 380 ? 0.4096 0.4503 0.3645 0.0393  0.0596  0.0586  681 TRP A CZ3 
3024  C CH2 . TRP A 380 ? 0.4215 0.4703 0.3741 0.0443  0.0556  0.0536  681 TRP A CH2 
3025  N N   . VAL A 381 ? 0.3799 0.4031 0.3599 0.0206  0.0629  0.0593  682 VAL A N   
3026  C CA  . VAL A 381 ? 0.3931 0.4083 0.3662 0.0198  0.0652  0.0659  682 VAL A CA  
3027  C C   . VAL A 381 ? 0.4465 0.4520 0.4216 0.0187  0.0630  0.0665  682 VAL A C   
3028  O O   . VAL A 381 ? 0.4399 0.4389 0.4083 0.0213  0.0630  0.0699  682 VAL A O   
3029  C CB  . VAL A 381 ? 0.4587 0.4733 0.4300 0.0146  0.0701  0.0707  682 VAL A CB  
3030  C CG1 . VAL A 381 ? 0.4685 0.4707 0.4306 0.0130  0.0725  0.0778  682 VAL A CG1 
3031  C CG2 . VAL A 381 ? 0.4300 0.4573 0.3991 0.0163  0.0727  0.0701  682 VAL A CG2 
3032  N N   . TRP A 382 ? 0.4882 0.4927 0.4715 0.0156  0.0612  0.0630  683 TRP A N   
3033  C CA  . TRP A 382 ? 0.5005 0.4980 0.4863 0.0145  0.0592  0.0628  683 TRP A CA  
3034  C C   . TRP A 382 ? 0.4426 0.4444 0.4320 0.0166  0.0555  0.0580  683 TRP A C   
3035  O O   . TRP A 382 ? 0.4940 0.4933 0.4830 0.0175  0.0542  0.0583  683 TRP A O   
3036  C CB  . TRP A 382 ? 0.4839 0.4774 0.4754 0.0093  0.0597  0.0626  683 TRP A CB  
3037  C CG  . TRP A 382 ? 0.4914 0.4785 0.4795 0.0054  0.0629  0.0672  683 TRP A CG  
3038  C CD1 . TRP A 382 ? 0.4987 0.4887 0.4839 0.0030  0.0664  0.0700  683 TRP A CD1 
3039  C CD2 . TRP A 382 ? 0.5622 0.5386 0.5487 0.0026  0.0631  0.0693  683 TRP A CD2 
3040  N NE1 . TRP A 382 ? 0.5006 0.4814 0.4826 -0.0022 0.0687  0.0740  683 TRP A NE1 
3041  C CE2 . TRP A 382 ? 0.6302 0.6018 0.6126 -0.0021 0.0665  0.0733  683 TRP A CE2 
3042  C CE3 . TRP A 382 ? 0.6095 0.5802 0.5972 0.0034  0.0609  0.0680  683 TRP A CE3 
3043  C CZ2 . TRP A 382 ? 0.7238 0.6831 0.7027 -0.0062 0.0672  0.0755  683 TRP A CZ2 
3044  C CZ3 . TRP A 382 ? 0.6937 0.6533 0.6779 0.0006  0.0617  0.0701  683 TRP A CZ3 
3045  C CH2 . TRP A 382 ? 0.7018 0.6549 0.6815 -0.0042 0.0646  0.0736  683 TRP A CH2 
3046  N N   . ILE A 383 ? 0.3487 0.3566 0.3411 0.0170  0.0538  0.0534  684 ILE A N   
3047  C CA  . ILE A 383 ? 0.3827 0.3932 0.3780 0.0168  0.0503  0.0487  684 ILE A CA  
3048  C C   . ILE A 383 ? 0.4839 0.5008 0.4754 0.0206  0.0490  0.0483  684 ILE A C   
3049  O O   . ILE A 383 ? 0.4612 0.4810 0.4552 0.0199  0.0468  0.0463  684 ILE A O   
3050  C CB  . ILE A 383 ? 0.4220 0.4342 0.4192 0.0165  0.0486  0.0435  684 ILE A CB  
3051  C CG1 . ILE A 383 ? 0.4654 0.4722 0.4662 0.0142  0.0492  0.0436  684 ILE A CG1 
3052  C CG2 . ILE A 383 ? 0.3538 0.3674 0.3525 0.0149  0.0450  0.0385  684 ILE A CG2 
3053  C CD1 . ILE A 383 ? 0.6025 0.6029 0.6064 0.0105  0.0488  0.0455  684 ILE A CD1 
3054  N N   . VAL A 384 ? 0.4519 0.4724 0.4372 0.0249  0.0502  0.0502  685 VAL A N   
3055  C CA  . VAL A 384 ? 0.4588 0.4868 0.4397 0.0299  0.0484  0.0496  685 VAL A CA  
3056  C C   . VAL A 384 ? 0.4767 0.5010 0.4550 0.0324  0.0488  0.0538  685 VAL A C   
3057  O O   . VAL A 384 ? 0.4159 0.4304 0.3899 0.0326  0.0517  0.0592  685 VAL A O   
3058  C CB  . VAL A 384 ? 0.5039 0.5362 0.4771 0.0345  0.0498  0.0512  685 VAL A CB  
3059  C CG1 . VAL A 384 ? 0.3360 0.3758 0.3031 0.0410  0.0477  0.0514  685 VAL A CG1 
3060  C CG2 . VAL A 384 ? 0.5320 0.5693 0.5073 0.0334  0.0488  0.0458  685 VAL A CG2 
3061  N N   . PRO A 385 ? 0.5383 0.5702 0.5189 0.0343  0.0460  0.0511  686 PRO A N   
3062  C CA  . PRO A 385 ? 0.5573 0.5868 0.5351 0.0384  0.0462  0.0542  686 PRO A CA  
3063  C C   . PRO A 385 ? 0.6005 0.6247 0.5669 0.0459  0.0476  0.0596  686 PRO A C   
3064  O O   . PRO A 385 ? 0.5464 0.5745 0.5075 0.0488  0.0476  0.0602  686 PRO A O   
3065  C CB  . PRO A 385 ? 0.4912 0.5359 0.4740 0.0396  0.0427  0.0491  686 PRO A CB  
3066  C CG  . PRO A 385 ? 0.5611 0.6112 0.5506 0.0328  0.0411  0.0436  686 PRO A CG  
3067  C CD  . PRO A 385 ? 0.5296 0.5735 0.5153 0.0325  0.0425  0.0445  686 PRO A CD  
3068  N N   . PRO A 386 ? 0.5381 0.5525 0.4990 0.0495  0.0486  0.0638  687 PRO A N   
3069  C CA  . PRO A 386 ? 0.4899 0.4943 0.4374 0.0564  0.0501  0.0698  687 PRO A CA  
3070  C C   . PRO A 386 ? 0.4799 0.4942 0.4208 0.0670  0.0471  0.0695  687 PRO A C   
3071  O O   . PRO A 386 ? 0.5480 0.5520 0.4756 0.0743  0.0480  0.0750  687 PRO A O   
3072  C CB  . PRO A 386 ? 0.4926 0.4807 0.4366 0.0560  0.0517  0.0732  687 PRO A CB  
3073  C CG  . PRO A 386 ? 0.4089 0.4065 0.3632 0.0548  0.0496  0.0681  687 PRO A CG  
3074  C CD  . PRO A 386 ? 0.3909 0.4014 0.3565 0.0477  0.0485  0.0630  687 PRO A CD  
3075  N N   . MET A 387 ? 0.5431 0.5766 0.4919 0.0682  0.0436  0.0632  688 MET A N   
3076  C CA  . MET A 387 ? 0.5003 0.5481 0.4443 0.0779  0.0402  0.0616  688 MET A CA  
3077  C C   . MET A 387 ? 0.5471 0.6139 0.5005 0.0733  0.0374  0.0544  688 MET A C   
3078  O O   . MET A 387 ? 0.5219 0.5904 0.4858 0.0637  0.0376  0.0503  688 MET A O   
3079  C CB  . MET A 387 ? 0.5490 0.6035 0.4927 0.0861  0.0379  0.0606  688 MET A CB  
3080  C CG  . MET A 387 ? 0.6267 0.6968 0.5852 0.0799  0.0363  0.0540  688 MET A CG  
3081  S SD  . MET A 387 ? 0.5565 0.6408 0.5158 0.0901  0.0338  0.0518  688 MET A SD  
3082  C CE  . MET A 387 ? 0.6122 0.7205 0.5685 0.1001  0.0291  0.0483  688 MET A CE  
3083  N N   . SER A 388 ? 0.4998 0.5795 0.4479 0.0803  0.0345  0.0527  689 SER A N   
3084  C CA  . SER A 388 ? 0.4224 0.5215 0.3783 0.0767  0.0309  0.0447  689 SER A CA  
3085  C C   . SER A 388 ? 0.4566 0.5498 0.4174 0.0666  0.0325  0.0421  689 SER A C   
3086  O O   . SER A 388 ? 0.5654 0.6671 0.5356 0.0592  0.0304  0.0353  689 SER A O   
3087  C CB  . SER A 388 ? 0.3635 0.4791 0.3307 0.0739  0.0280  0.0387  689 SER A CB  
3088  O OG  . SER A 388 ? 0.5010 0.6260 0.4637 0.0851  0.0261  0.0400  689 SER A OG  
3089  N N   . GLY A 389 ? 0.4290 0.5076 0.3827 0.0665  0.0362  0.0475  690 GLY A N   
3090  C CA  . GLY A 389 ? 0.3916 0.4635 0.3500 0.0582  0.0383  0.0458  690 GLY A CA  
3091  C C   . GLY A 389 ? 0.5473 0.6308 0.5094 0.0554  0.0351  0.0378  690 GLY A C   
3092  O O   . GLY A 389 ? 0.5066 0.5888 0.4771 0.0477  0.0342  0.0328  690 GLY A O   
3093  N N   . SER A 390 ? 0.4715 0.5650 0.4263 0.0619  0.0331  0.0363  691 SER A N   
3094  C CA  . SER A 390 ? 0.4498 0.5520 0.4065 0.0593  0.0303  0.0283  691 SER A CA  
3095  C C   . SER A 390 ? 0.4877 0.6032 0.4525 0.0551  0.0252  0.0199  691 SER A C   
3096  O O   . SER A 390 ? 0.4862 0.6065 0.4526 0.0514  0.0223  0.0122  691 SER A O   
3097  C CB  . SER A 390 ? 0.4370 0.5461 0.3823 0.0673  0.0298  0.0290  691 SER A CB  
3098  O OG  . SER A 390 ? 0.3798 0.5031 0.3215 0.0743  0.0259  0.0276  691 SER A OG  
3099  N N   . ILE A 391 ? 0.5030 0.6249 0.4726 0.0554  0.0240  0.0206  692 ILE A N   
3100  C CA  . ILE A 391 ? 0.5066 0.6428 0.4852 0.0492  0.0197  0.0125  692 ILE A CA  
3101  C C   . ILE A 391 ? 0.4325 0.5584 0.4202 0.0383  0.0214  0.0116  692 ILE A C   
3102  O O   . ILE A 391 ? 0.3853 0.5202 0.3808 0.0307  0.0189  0.0060  692 ILE A O   
3103  C CB  . ILE A 391 ? 0.5569 0.7118 0.5367 0.0553  0.0170  0.0121  692 ILE A CB  
3104  C CG1 . ILE A 391 ? 0.4679 0.6163 0.4495 0.0576  0.0200  0.0186  692 ILE A CG1 
3105  C CG2 . ILE A 391 ? 0.4481 0.6134 0.4175 0.0672  0.0147  0.0130  692 ILE A CG2 
3106  C CD1 . ILE A 391 ? 0.5027 0.6712 0.4870 0.0637  0.0171  0.0169  692 ILE A CD1 
3107  N N   . THR A 392 ? 0.4581 0.5654 0.4444 0.0369  0.0256  0.0171  693 THR A N   
3108  C CA  . THR A 392 ? 0.4983 0.5943 0.4913 0.0275  0.0268  0.0163  693 THR A CA  
3109  C C   . THR A 392 ? 0.4616 0.5467 0.4526 0.0242  0.0269  0.0130  693 THR A C   
3110  O O   . THR A 392 ? 0.5197 0.6020 0.5042 0.0298  0.0282  0.0147  693 THR A O   
3111  C CB  . THR A 392 ? 0.5263 0.6105 0.5198 0.0284  0.0309  0.0238  693 THR A CB  
3112  O OG1 . THR A 392 ? 0.5168 0.5909 0.5034 0.0333  0.0339  0.0290  693 THR A OG1 
3113  C CG2 . THR A 392 ? 0.5305 0.6242 0.5247 0.0332  0.0308  0.0266  693 THR A CG2 
3114  N N   . PRO A 393 ? 0.4499 0.5280 0.4454 0.0154  0.0256  0.0086  694 PRO A N   
3115  C CA  . PRO A 393 ? 0.4850 0.5534 0.4772 0.0137  0.0245  0.0038  694 PRO A CA  
3116  C C   . PRO A 393 ? 0.4903 0.5462 0.4794 0.0176  0.0281  0.0085  694 PRO A C   
3117  O O   . PRO A 393 ? 0.4310 0.4843 0.4154 0.0208  0.0277  0.0053  694 PRO A O   
3118  C CB  . PRO A 393 ? 0.4636 0.5246 0.4601 0.0032  0.0225  -0.0008 694 PRO A CB  
3119  C CG  . PRO A 393 ? 0.4258 0.4881 0.4282 -0.0002 0.0247  0.0046  694 PRO A CG  
3120  C CD  . PRO A 393 ? 0.4342 0.5125 0.4368 0.0069  0.0252  0.0078  694 PRO A CD  
3121  N N   . VAL A 394 ? 0.5313 0.5811 0.5229 0.0177  0.0316  0.0155  695 VAL A N   
3122  C CA  . VAL A 394 ? 0.5318 0.5724 0.5215 0.0203  0.0348  0.0193  695 VAL A CA  
3123  C C   . VAL A 394 ? 0.4533 0.5003 0.4368 0.0275  0.0368  0.0216  695 VAL A C   
3124  O O   . VAL A 394 ? 0.3722 0.4160 0.3536 0.0298  0.0389  0.0222  695 VAL A O   
3125  C CB  . VAL A 394 ? 0.5254 0.5591 0.5188 0.0182  0.0378  0.0258  695 VAL A CB  
3126  C CG1 . VAL A 394 ? 0.5082 0.5340 0.5063 0.0112  0.0364  0.0239  695 VAL A CG1 
3127  C CG2 . VAL A 394 ? 0.3184 0.3582 0.3110 0.0211  0.0392  0.0308  695 VAL A CG2 
3128  N N   . PHE A 395 ? 0.4814 0.5384 0.4615 0.0316  0.0363  0.0232  696 PHE A N   
3129  C CA  . PHE A 395 ? 0.4770 0.5392 0.4494 0.0383  0.0384  0.0262  696 PHE A CA  
3130  C C   . PHE A 395 ? 0.5653 0.6303 0.5341 0.0404  0.0373  0.0203  696 PHE A C   
3131  O O   . PHE A 395 ? 0.4685 0.5343 0.4326 0.0440  0.0406  0.0230  696 PHE A O   
3132  C CB  . PHE A 395 ? 0.4308 0.5032 0.3986 0.0435  0.0368  0.0277  696 PHE A CB  
3133  C CG  . PHE A 395 ? 0.5209 0.5976 0.4784 0.0507  0.0388  0.0315  696 PHE A CG  
3134  C CD1 . PHE A 395 ? 0.5089 0.5944 0.4614 0.0541  0.0368  0.0261  696 PHE A CD1 
3135  C CD2 . PHE A 395 ? 0.4424 0.5136 0.3939 0.0539  0.0426  0.0405  696 PHE A CD2 
3136  C CE1 . PHE A 395 ? 0.5310 0.6210 0.4731 0.0607  0.0391  0.0301  696 PHE A CE1 
3137  C CE2 . PHE A 395 ? 0.5344 0.6082 0.4751 0.0597  0.0449  0.0448  696 PHE A CE2 
3138  C CZ  . PHE A 395 ? 0.4497 0.5338 0.3857 0.0633  0.0433  0.0398  696 PHE A CZ  
3139  N N   . HIS A 396 ? 0.5712 0.6376 0.5416 0.0378  0.0329  0.0120  697 HIS A N   
3140  C CA  . HIS A 396 ? 0.5348 0.6033 0.5004 0.0406  0.0311  0.0050  697 HIS A CA  
3141  C C   . HIS A 396 ? 0.5333 0.5902 0.5007 0.0387  0.0316  0.0020  697 HIS A C   
3142  O O   . HIS A 396 ? 0.4518 0.5084 0.4147 0.0417  0.0298  -0.0047 697 HIS A O   
3143  C CB  . HIS A 396 ? 0.4942 0.5697 0.4593 0.0387  0.0256  -0.0032 697 HIS A CB  
3144  C CG  . HIS A 396 ? 0.4383 0.5271 0.4024 0.0413  0.0244  -0.0007 697 HIS A CG  
3145  N ND1 . HIS A 396 ? 0.4313 0.5319 0.3875 0.0487  0.0238  -0.0009 697 HIS A ND1 
3146  C CD2 . HIS A 396 ? 0.4959 0.5887 0.4652 0.0387  0.0239  0.0024  697 HIS A CD2 
3147  C CE1 . HIS A 396 ? 0.4985 0.6091 0.4548 0.0511  0.0225  0.0018  697 HIS A CE1 
3148  N NE2 . HIS A 396 ? 0.4198 0.5265 0.3844 0.0453  0.0226  0.0036  697 HIS A NE2 
3149  N N   . GLN A 397 ? 0.5836 0.6313 0.5567 0.0349  0.0337  0.0066  698 GLN A N   
3150  C CA  . GLN A 397 ? 0.4911 0.5270 0.4659 0.0335  0.0334  0.0040  698 GLN A CA  
3151  C C   . GLN A 397 ? 0.4956 0.5334 0.4703 0.0377  0.0379  0.0086  698 GLN A C   
3152  O O   . GLN A 397 ? 0.4566 0.4949 0.4346 0.0360  0.0413  0.0159  698 GLN A O   
3153  C CB  . GLN A 397 ? 0.4382 0.4638 0.4188 0.0264  0.0325  0.0059  698 GLN A CB  
3154  C CG  . GLN A 397 ? 0.4095 0.4221 0.3907 0.0261  0.0324  0.0048  698 GLN A CG  
3155  C CD  . GLN A 397 ? 0.5218 0.5258 0.4977 0.0270  0.0284  -0.0039 698 GLN A CD  
3156  O OE1 . GLN A 397 ? 0.5017 0.5017 0.4765 0.0216  0.0249  -0.0085 698 GLN A OE1 
3157  N NE2 . GLN A 397 ? 0.4767 0.4783 0.4488 0.0338  0.0288  -0.0068 698 GLN A NE2 
3158  N N   . GLU A 398 ? 0.4144 0.4536 0.3852 0.0431  0.0378  0.0038  699 GLU A N   
3159  C CA  . GLU A 398 ? 0.4691 0.5122 0.4412 0.0465  0.0419  0.0071  699 GLU A CA  
3160  C C   . GLU A 398 ? 0.4415 0.4748 0.4197 0.0431  0.0420  0.0095  699 GLU A C   
3161  O O   . GLU A 398 ? 0.3935 0.4143 0.3721 0.0406  0.0384  0.0060  699 GLU A O   
3162  C CB  . GLU A 398 ? 0.4752 0.5229 0.4421 0.0539  0.0414  0.0003  699 GLU A CB  
3163  C CG  . GLU A 398 ? 0.4288 0.4898 0.3893 0.0584  0.0428  -0.0007 699 GLU A CG  
3164  C CD  . GLU A 398 ? 0.5910 0.6577 0.5460 0.0665  0.0425  -0.0079 699 GLU A CD  
3165  O OE1 . GLU A 398 ? 0.6202 0.6994 0.5691 0.0710  0.0443  -0.0086 699 GLU A OE1 
3166  O OE2 . GLU A 398 ? 0.6066 0.6651 0.5623 0.0693  0.0405  -0.0129 699 GLU A OE2 
3167  N N   . MET A 399 ? 0.5133 0.5521 0.4953 0.0427  0.0463  0.0155  700 MET A N   
3168  C CA  . MET A 399 ? 0.5287 0.5607 0.5164 0.0396  0.0465  0.0183  700 MET A CA  
3169  C C   . MET A 399 ? 0.5376 0.5796 0.5279 0.0427  0.0500  0.0197  700 MET A C   
3170  O O   . MET A 399 ? 0.5993 0.6536 0.5888 0.0431  0.0541  0.0230  700 MET A O   
3171  C CB  . MET A 399 ? 0.5429 0.5715 0.5341 0.0331  0.0479  0.0250  700 MET A CB  
3172  C CG  . MET A 399 ? 0.5232 0.5448 0.5136 0.0296  0.0447  0.0238  700 MET A CG  
3173  S SD  . MET A 399 ? 0.5143 0.5356 0.5072 0.0248  0.0469  0.0314  700 MET A SD  
3174  C CE  . MET A 399 ? 0.3822 0.4029 0.3738 0.0230  0.0431  0.0278  700 MET A CE  
3175  N N   . LEU A 400 ? 0.4334 0.4709 0.4264 0.0448  0.0483  0.0174  701 LEU A N   
3176  C CA  . LEU A 400 ? 0.4773 0.5266 0.4747 0.0472  0.0511  0.0187  701 LEU A CA  
3177  C C   . LEU A 400 ? 0.5521 0.5986 0.5556 0.0408  0.0522  0.0243  701 LEU A C   
3178  O O   . LEU A 400 ? 0.4642 0.4971 0.4682 0.0381  0.0492  0.0247  701 LEU A O   
3179  C CB  . LEU A 400 ? 0.4877 0.5359 0.4835 0.0557  0.0481  0.0119  701 LEU A CB  
3180  C CG  . LEU A 400 ? 0.6119 0.6642 0.6011 0.0637  0.0472  0.0051  701 LEU A CG  
3181  C CD1 . LEU A 400 ? 0.6347 0.6814 0.6212 0.0729  0.0435  -0.0015 701 LEU A CD1 
3182  C CD2 . LEU A 400 ? 0.6339 0.7077 0.6240 0.0650  0.0525  0.0070  701 LEU A CD2 
3183  N N   . ASN A 401 ? 0.5039 0.5636 0.5116 0.0378  0.0565  0.0284  702 ASN A N   
3184  C CA  . ASN A 401 ? 0.4821 0.5400 0.4950 0.0311  0.0577  0.0334  702 ASN A CA  
3185  C C   . ASN A 401 ? 0.5322 0.6027 0.5511 0.0330  0.0583  0.0319  702 ASN A C   
3186  O O   . ASN A 401 ? 0.5083 0.5960 0.5290 0.0343  0.0618  0.0314  702 ASN A O   
3187  C CB  . ASN A 401 ? 0.3645 0.4246 0.3764 0.0240  0.0620  0.0398  702 ASN A CB  
3188  C CG  . ASN A 401 ? 0.5105 0.5616 0.5252 0.0173  0.0618  0.0440  702 ASN A CG  
3189  O OD1 . ASN A 401 ? 0.5161 0.5573 0.5321 0.0179  0.0582  0.0423  702 ASN A OD1 
3190  N ND2 . ASN A 401 ? 0.4301 0.4839 0.4452 0.0108  0.0657  0.0491  702 ASN A ND2 
3191  N N   . TYR A 402 ? 0.4302 0.4935 0.4519 0.0331  0.0551  0.0312  703 TYR A N   
3192  C CA  . TYR A 402 ? 0.4716 0.5480 0.4995 0.0350  0.0551  0.0298  703 TYR A CA  
3193  C C   . TYR A 402 ? 0.4933 0.5602 0.5238 0.0303  0.0528  0.0323  703 TYR A C   
3194  O O   . TYR A 402 ? 0.5562 0.6065 0.5833 0.0269  0.0513  0.0345  703 TYR A O   
3195  C CB  . TYR A 402 ? 0.4021 0.4833 0.4285 0.0465  0.0520  0.0233  703 TYR A CB  
3196  C CG  . TYR A 402 ? 0.4977 0.5582 0.5165 0.0518  0.0474  0.0201  703 TYR A CG  
3197  C CD1 . TYR A 402 ? 0.3952 0.4504 0.4078 0.0543  0.0473  0.0175  703 TYR A CD1 
3198  C CD2 . TYR A 402 ? 0.4416 0.4872 0.4584 0.0537  0.0430  0.0197  703 TYR A CD2 
3199  C CE1 . TYR A 402 ? 0.4254 0.4610 0.4308 0.0574  0.0429  0.0142  703 TYR A CE1 
3200  C CE2 . TYR A 402 ? 0.4143 0.4393 0.4231 0.0568  0.0391  0.0173  703 TYR A CE2 
3201  C CZ  . TYR A 402 ? 0.5310 0.5510 0.5344 0.0582  0.0390  0.0142  703 TYR A CZ  
3202  O OH  . TYR A 402 ? 0.5838 0.5831 0.5791 0.0597  0.0351  0.0113  703 TYR A OH  
3203  N N   . ARG A 403 ? 0.4723 0.5518 0.5088 0.0301  0.0527  0.0317  704 ARG A N   
3204  C CA  . ARG A 403 ? 0.6129 0.6867 0.6521 0.0249  0.0511  0.0340  704 ARG A CA  
3205  C C   . ARG A 403 ? 0.5466 0.6193 0.5857 0.0331  0.0462  0.0305  704 ARG A C   
3206  O O   . ARG A 403 ? 0.5359 0.6264 0.5798 0.0380  0.0456  0.0275  704 ARG A O   
3207  C CB  . ARG A 403 ? 0.6793 0.7677 0.7249 0.0160  0.0547  0.0365  704 ARG A CB  
3208  C CG  . ARG A 403 ? 0.8623 0.9458 0.9103 0.0108  0.0527  0.0379  704 ARG A CG  
3209  C CD  . ARG A 403 ? 1.0225 1.1121 1.0739 -0.0007 0.0565  0.0411  704 ARG A CD  
3210  N NE  . ARG A 403 ? 1.1560 1.2303 1.2014 -0.0064 0.0592  0.0455  704 ARG A NE  
3211  C CZ  . ARG A 403 ? 1.2049 1.2602 1.2454 -0.0074 0.0575  0.0475  704 ARG A CZ  
3212  N NH1 . ARG A 403 ? 1.2492 1.2977 1.2897 -0.0042 0.0534  0.0459  704 ARG A NH1 
3213  N NH2 . ARG A 403 ? 1.1980 1.2420 1.2331 -0.0111 0.0599  0.0512  704 ARG A NH2 
3214  N N   . LEU A 404 ? 0.4589 0.5115 0.4921 0.0349  0.0427  0.0311  705 LEU A N   
3215  C CA  . LEU A 404 ? 0.4614 0.5080 0.4922 0.0416  0.0380  0.0293  705 LEU A CA  
3216  C C   . LEU A 404 ? 0.5196 0.5648 0.5529 0.0356  0.0372  0.0323  705 LEU A C   
3217  O O   . LEU A 404 ? 0.5310 0.5713 0.5653 0.0265  0.0395  0.0357  705 LEU A O   
3218  C CB  . LEU A 404 ? 0.4271 0.4509 0.4483 0.0458  0.0349  0.0287  705 LEU A CB  
3219  C CG  . LEU A 404 ? 0.4404 0.4599 0.4569 0.0509  0.0350  0.0253  705 LEU A CG  
3220  C CD1 . LEU A 404 ? 0.4922 0.4870 0.4996 0.0505  0.0322  0.0256  705 LEU A CD1 
3221  C CD2 . LEU A 404 ? 0.4483 0.4793 0.4647 0.0625  0.0332  0.0203  705 LEU A CD2 
3222  N N   . THR A 405 ? 0.5331 0.5823 0.5666 0.0416  0.0335  0.0305  706 THR A N   
3223  C CA  . THR A 405 ? 0.5141 0.5606 0.5483 0.0373  0.0318  0.0327  706 THR A CA  
3224  C C   . THR A 405 ? 0.4759 0.5037 0.5009 0.0435  0.0274  0.0335  706 THR A C   
3225  O O   . THR A 405 ? 0.3910 0.4118 0.4101 0.0530  0.0248  0.0314  706 THR A O   
3226  C CB  . THR A 405 ? 0.4785 0.5488 0.5212 0.0372  0.0313  0.0304  706 THR A CB  
3227  O OG1 . THR A 405 ? 0.6433 0.7115 0.6866 0.0317  0.0299  0.0321  706 THR A OG1 
3228  C CG2 . THR A 405 ? 0.3181 0.3988 0.3603 0.0502  0.0275  0.0263  706 THR A CG2 
3229  N N   . PRO A 406 ? 0.4645 0.4819 0.4866 0.0385  0.0266  0.0367  707 PRO A N   
3230  C CA  . PRO A 406 ? 0.5073 0.5266 0.5332 0.0283  0.0289  0.0390  707 PRO A CA  
3231  C C   . PRO A 406 ? 0.4454 0.4618 0.4730 0.0211  0.0333  0.0406  707 PRO A C   
3232  O O   . PRO A 406 ? 0.4273 0.4338 0.4509 0.0227  0.0340  0.0409  707 PRO A O   
3233  C CB  . PRO A 406 ? 0.4647 0.4671 0.4828 0.0279  0.0268  0.0419  707 PRO A CB  
3234  C CG  . PRO A 406 ? 0.4847 0.4814 0.4962 0.0378  0.0226  0.0410  707 PRO A CG  
3235  C CD  . PRO A 406 ? 0.4154 0.4151 0.4275 0.0442  0.0227  0.0381  707 PRO A CD  
3236  N N   . SER A 407 ? 0.4658 0.4899 0.4984 0.0133  0.0360  0.0414  708 SER A N   
3237  C CA  . SER A 407 ? 0.5074 0.5278 0.5403 0.0073  0.0400  0.0434  708 SER A CA  
3238  C C   . SER A 407 ? 0.4223 0.4377 0.4548 -0.0003 0.0412  0.0455  708 SER A C   
3239  O O   . SER A 407 ? 0.5635 0.5833 0.5976 -0.0023 0.0395  0.0446  708 SER A O   
3240  C CB  . SER A 407 ? 0.5645 0.5996 0.6025 0.0062  0.0429  0.0423  708 SER A CB  
3241  O OG  . SER A 407 ? 0.6537 0.7036 0.6978 0.0022  0.0432  0.0410  708 SER A OG  
3242  N N   . PHE A 408 ? 0.3388 0.3447 0.3681 -0.0036 0.0437  0.0479  709 PHE A N   
3243  C CA  . PHE A 408 ? 0.3786 0.3799 0.4068 -0.0101 0.0456  0.0495  709 PHE A CA  
3244  C C   . PHE A 408 ? 0.4580 0.4669 0.4890 -0.0150 0.0489  0.0501  709 PHE A C   
3245  O O   . PHE A 408 ? 0.5728 0.5868 0.6047 -0.0131 0.0507  0.0504  709 PHE A O   
3246  C CB  . PHE A 408 ? 0.3056 0.2940 0.3284 -0.0101 0.0465  0.0517  709 PHE A CB  
3247  C CG  . PHE A 408 ? 0.3895 0.3709 0.4091 -0.0078 0.0441  0.0517  709 PHE A CG  
3248  C CD1 . PHE A 408 ? 0.4365 0.4159 0.4547 -0.0097 0.0428  0.0513  709 PHE A CD1 
3249  C CD2 . PHE A 408 ? 0.3091 0.2858 0.3263 -0.0045 0.0433  0.0521  709 PHE A CD2 
3250  C CE1 . PHE A 408 ? 0.4191 0.3928 0.4334 -0.0077 0.0410  0.0518  709 PHE A CE1 
3251  C CE2 . PHE A 408 ? 0.4381 0.4083 0.4516 -0.0037 0.0417  0.0528  709 PHE A CE2 
3252  C CZ  . PHE A 408 ? 0.4186 0.3877 0.4305 -0.0050 0.0407  0.0530  709 PHE A CZ  
3253  N N   . GLU A 409 ? 0.4648 0.4737 0.4963 -0.0216 0.0496  0.0502  710 GLU A N   
3254  C CA  . GLU A 409 ? 0.4231 0.4399 0.4573 -0.0284 0.0526  0.0507  710 GLU A CA  
3255  C C   . GLU A 409 ? 0.5385 0.5415 0.5669 -0.0353 0.0544  0.0528  710 GLU A C   
3256  O O   . GLU A 409 ? 0.5101 0.5027 0.5348 -0.0352 0.0523  0.0521  710 GLU A O   
3257  C CB  . GLU A 409 ? 0.4547 0.4892 0.4964 -0.0309 0.0511  0.0473  710 GLU A CB  
3258  C CG  . GLU A 409 ? 0.5872 0.6362 0.6339 -0.0227 0.0491  0.0447  710 GLU A CG  
3259  C CD  . GLU A 409 ? 0.7298 0.7890 0.7787 -0.0213 0.0525  0.0453  710 GLU A CD  
3260  O OE1 . GLU A 409 ? 0.7330 0.7912 0.7805 -0.0282 0.0566  0.0479  710 GLU A OE1 
3261  O OE2 . GLU A 409 ? 0.7068 0.7739 0.7575 -0.0128 0.0509  0.0431  710 GLU A OE2 
3262  N N   . TYR A 410 ? 0.5908 0.5928 0.6172 -0.0409 0.0582  0.0553  711 TYR A N   
3263  C CA  . TYR A 410 ? 0.5868 0.5742 0.6064 -0.0482 0.0597  0.0571  711 TYR A CA  
3264  C C   . TYR A 410 ? 0.5692 0.5636 0.5930 -0.0573 0.0590  0.0543  711 TYR A C   
3265  O O   . TYR A 410 ? 0.5416 0.5557 0.5741 -0.0595 0.0588  0.0520  711 TYR A O   
3266  C CB  . TYR A 410 ? 0.6052 0.5864 0.6190 -0.0515 0.0642  0.0617  711 TYR A CB  
3267  C CG  . TYR A 410 ? 0.7530 0.7294 0.7626 -0.0430 0.0649  0.0642  711 TYR A CG  
3268  C CD1 . TYR A 410 ? 0.8281 0.7901 0.8314 -0.0372 0.0632  0.0648  711 TYR A CD1 
3269  C CD2 . TYR A 410 ? 0.8800 0.8676 0.8917 -0.0408 0.0672  0.0655  711 TYR A CD2 
3270  C CE1 . TYR A 410 ? 0.9150 0.8751 0.9149 -0.0300 0.0636  0.0666  711 TYR A CE1 
3271  C CE2 . TYR A 410 ? 0.9545 0.9385 0.9621 -0.0335 0.0675  0.0671  711 TYR A CE2 
3272  C CZ  . TYR A 410 ? 0.9616 0.9323 0.9636 -0.0284 0.0655  0.0676  711 TYR A CZ  
3273  O OH  . TYR A 410 ? 1.0037 0.9735 1.0024 -0.0217 0.0655  0.0687  711 TYR A OH  
3274  N N   . GLN A 411 ? 0.6057 0.5846 0.6232 -0.0622 0.0582  0.0539  712 GLN A N   
3275  C CA  . GLN A 411 ? 0.6297 0.6124 0.6494 -0.0729 0.0576  0.0510  712 GLN A CA  
3276  C C   . GLN A 411 ? 0.4669 0.4270 0.4756 -0.0807 0.0600  0.0535  712 GLN A C   
3277  O O   . GLN A 411 ? 0.5164 0.4578 0.5154 -0.0752 0.0608  0.0566  712 GLN A O   
3278  C CB  . GLN A 411 ? 0.6515 0.6381 0.6742 -0.0704 0.0526  0.0460  712 GLN A CB  
3279  C CG  . GLN A 411 ? 0.5869 0.5548 0.6011 -0.0639 0.0505  0.0460  712 GLN A CG  
3280  C CD  . GLN A 411 ? 0.5644 0.5389 0.5813 -0.0603 0.0459  0.0416  712 GLN A CD  
3281  O OE1 . GLN A 411 ? 0.5658 0.5548 0.5891 -0.0649 0.0437  0.0379  712 GLN A OE1 
3282  N NE2 . GLN A 411 ? 0.4604 0.4256 0.4723 -0.0520 0.0445  0.0421  712 GLN A NE2 
3283  N N   . PRO A 412 ? 0.5221 0.4833 0.5313 -0.0935 0.0610  0.0521  713 PRO A N   
3284  C CA  . PRO A 412 ? 0.6797 0.6151 0.6761 -0.1015 0.0629  0.0544  713 PRO A CA  
3285  C C   . PRO A 412 ? 0.7289 0.6433 0.7161 -0.0965 0.0593  0.0517  713 PRO A C   
3286  O O   . PRO A 412 ? 0.6204 0.5426 0.6124 -0.0910 0.0552  0.0472  713 PRO A O   
3287  C CB  . PRO A 412 ? 0.7306 0.6754 0.7314 -0.1177 0.0642  0.0522  713 PRO A CB  
3288  C CG  . PRO A 412 ? 0.6320 0.6079 0.6482 -0.1164 0.0613  0.0471  713 PRO A CG  
3289  C CD  . PRO A 412 ? 0.5791 0.5658 0.6002 -0.1016 0.0607  0.0486  713 PRO A CD  
3290  N N   . ASP A 413 ? 0.7876 0.6746 0.7605 -0.0975 0.0609  0.0547  714 ASP A N   
3291  C CA  . ASP A 413 ? 0.8181 0.6834 0.7804 -0.0922 0.0579  0.0521  714 ASP A CA  
3292  C C   . ASP A 413 ? 0.8402 0.7054 0.8037 -0.1014 0.0546  0.0455  714 ASP A C   
3293  O O   . ASP A 413 ? 0.9137 0.7821 0.8793 -0.1155 0.0558  0.0446  714 ASP A O   
3294  C CB  . ASP A 413 ? 0.8933 0.7284 0.8385 -0.0913 0.0602  0.0565  714 ASP A CB  
3295  C CG  . ASP A 413 ? 0.9061 0.7408 0.8488 -0.0792 0.0621  0.0618  714 ASP A CG  
3296  O OD1 . ASP A 413 ? 0.9073 0.7625 0.8608 -0.0713 0.0611  0.0611  714 ASP A OD1 
3297  O OD2 . ASP A 413 ? 0.9728 0.7862 0.9021 -0.0775 0.0642  0.0665  714 ASP A OD2 
3298  N N   . PRO A 414 ? 0.7954 0.6576 0.7571 -0.0942 0.0505  0.0408  715 PRO A N   
3299  C CA  . PRO A 414 ? 0.6933 0.5599 0.6574 -0.1020 0.0468  0.0338  715 PRO A CA  
3300  C C   . PRO A 414 ? 0.6811 0.5256 0.6346 -0.1154 0.0472  0.0320  715 PRO A C   
3301  O O   . PRO A 414 ? 0.6363 0.4907 0.5953 -0.1279 0.0457  0.0274  715 PRO A O   
3302  C CB  . PRO A 414 ? 0.6844 0.5472 0.6448 -0.0899 0.0431  0.0303  715 PRO A CB  
3303  C CG  . PRO A 414 ? 0.6716 0.5381 0.6333 -0.0769 0.0449  0.0352  715 PRO A CG  
3304  C CD  . PRO A 414 ? 0.7228 0.5801 0.6807 -0.0791 0.0493  0.0414  715 PRO A CD  
3305  N N   . TRP A 415 ? 0.7359 0.5502 0.6735 -0.1130 0.0491  0.0353  716 TRP A N   
3306  C CA  . TRP A 415 ? 0.7481 0.5352 0.6723 -0.1252 0.0492  0.0336  716 TRP A CA  
3307  C C   . TRP A 415 ? 0.8260 0.6162 0.7528 -0.1419 0.0534  0.0374  716 TRP A C   
3308  O O   . TRP A 415 ? 0.9158 0.6867 0.8333 -0.1559 0.0535  0.0354  716 TRP A O   
3309  C CB  . TRP A 415 ? 0.7459 0.4980 0.6505 -0.1158 0.0498  0.0363  716 TRP A CB  
3310  C CG  . TRP A 415 ? 0.7448 0.4942 0.6466 -0.1066 0.0536  0.0446  716 TRP A CG  
3311  C CD1 . TRP A 415 ? 0.7619 0.4974 0.6559 -0.1130 0.0579  0.0515  716 TRP A CD1 
3312  C CD2 . TRP A 415 ? 0.6503 0.4109 0.5562 -0.0895 0.0534  0.0467  716 TRP A CD2 
3313  N NE1 . TRP A 415 ? 0.7252 0.4633 0.6181 -0.0999 0.0600  0.0575  716 TRP A NE1 
3314  C CE2 . TRP A 415 ? 0.7319 0.4857 0.6325 -0.0860 0.0572  0.0544  716 TRP A CE2 
3315  C CE3 . TRP A 415 ? 0.7029 0.4787 0.6158 -0.0777 0.0504  0.0430  716 TRP A CE3 
3316  C CZ2 . TRP A 415 ? 0.6901 0.4530 0.5933 -0.0712 0.0577  0.0576  716 TRP A CZ2 
3317  C CZ3 . TRP A 415 ? 0.7571 0.5413 0.6725 -0.0641 0.0514  0.0466  716 TRP A CZ3 
3318  C CH2 . TRP A 415 ? 0.7914 0.5696 0.7024 -0.0610 0.0548  0.0535  716 TRP A CH2 
3319  N N   . ASN A 416 ? 0.7682 0.5817 0.7066 -0.1413 0.0568  0.0425  717 ASN A N   
3320  C CA  . ASN A 416 ? 0.7529 0.5751 0.6955 -0.1573 0.0612  0.0458  717 ASN A CA  
3321  C C   . ASN A 416 ? 0.7948 0.6477 0.7536 -0.1693 0.0594  0.0397  717 ASN A C   
3322  O O   . ASN A 416 ? 0.8949 0.7574 0.8579 -0.1849 0.0629  0.0412  717 ASN A O   
3323  C CB  . ASN A 416 ? 0.6499 0.4855 0.5974 -0.1508 0.0657  0.0533  717 ASN A CB  
3324  C CG  . ASN A 416 ? 0.7637 0.5700 0.6944 -0.1415 0.0679  0.0599  717 ASN A CG  
3325  O OD1 . ASN A 416 ? 0.8330 0.6061 0.7464 -0.1452 0.0679  0.0608  717 ASN A OD1 
3326  N ND2 . ASN A 416 ? 0.7743 0.5919 0.7090 -0.1288 0.0695  0.0643  717 ASN A ND2 
3327  N N   . THR A 417 ? 0.7833 0.6533 0.7512 -0.1622 0.0543  0.0331  718 THR A N   
3328  C CA  . THR A 417 ? 0.7790 0.6811 0.7627 -0.1709 0.0518  0.0270  718 THR A CA  
3329  C C   . THR A 417 ? 0.8198 0.7205 0.8025 -0.1712 0.0455  0.0183  718 THR A C   
3330  O O   . THR A 417 ? 0.8048 0.7277 0.7977 -0.1817 0.0431  0.0123  718 THR A O   
3331  C CB  . THR A 417 ? 0.6964 0.6327 0.6961 -0.1601 0.0519  0.0282  718 THR A CB  
3332  O OG1 . THR A 417 ? 0.7594 0.6914 0.7571 -0.1423 0.0488  0.0280  718 THR A OG1 
3333  C CG2 . THR A 417 ? 0.5851 0.5272 0.5869 -0.1604 0.0580  0.0359  718 THR A CG2 
3334  N N   . HIS A 418 ? 0.8193 0.6973 0.7905 -0.1596 0.0427  0.0169  719 HIS A N   
3335  C CA  . HIS A 418 ? 0.8328 0.7087 0.8015 -0.1596 0.0368  0.0084  719 HIS A CA  
3336  C C   . HIS A 418 ? 0.9252 0.7812 0.8846 -0.1774 0.0361  0.0038  719 HIS A C   
3337  O O   . HIS A 418 ? 0.9837 0.8091 0.9290 -0.1831 0.0393  0.0076  719 HIS A O   
3338  C CB  . HIS A 418 ? 0.7978 0.6548 0.7557 -0.1426 0.0347  0.0083  719 HIS A CB  
3339  C CG  . HIS A 418 ? 0.7415 0.5941 0.6944 -0.1417 0.0290  -0.0004 719 HIS A CG  
3340  N ND1 . HIS A 418 ? 0.7127 0.5919 0.6760 -0.1365 0.0247  -0.0050 719 HIS A ND1 
3341  C CD2 . HIS A 418 ? 0.7849 0.6091 0.7225 -0.1451 0.0267  -0.0055 719 HIS A CD2 
3342  C CE1 . HIS A 418 ? 0.7848 0.6537 0.7398 -0.1368 0.0201  -0.0126 719 HIS A CE1 
3343  N NE2 . HIS A 418 ? 0.7615 0.5972 0.7011 -0.1421 0.0212  -0.0134 719 HIS A NE2 
3344  N N   . VAL A 419 ? 0.9793 0.8521 0.9456 -0.1864 0.0315  -0.0046 720 VAL A N   
3345  C CA  . VAL A 419 ? 1.0621 0.9161 1.0192 -0.2034 0.0295  -0.0110 720 VAL A CA  
3346  C C   . VAL A 419 ? 1.0297 0.8717 0.9779 -0.1952 0.0233  -0.0191 720 VAL A C   
3347  O O   . VAL A 419 ? 1.0016 0.8685 0.9592 -0.1855 0.0192  -0.0230 720 VAL A O   
3348  C CB  . VAL A 419 ? 1.0309 0.9145 1.0024 -0.2226 0.0292  -0.0153 720 VAL A CB  
3349  C CG1 . VAL A 419 ? 1.0489 0.9064 1.0085 -0.2437 0.0291  -0.0196 720 VAL A CG1 
3350  C CG2 . VAL A 419 ? 0.9349 0.8418 0.9191 -0.2253 0.0351  -0.0075 720 VAL A CG2 
3351  N N   . TRP A 420 ? 1.0712 0.8743 1.0002 -0.1986 0.0226  -0.0215 721 TRP A N   
3352  C CA  . TRP A 420 ? 1.1010 0.8863 1.0176 -0.1865 0.0178  -0.0275 721 TRP A CA  
3353  C C   . TRP A 420 ? 1.1637 0.9589 1.0821 -0.1961 0.0114  -0.0392 721 TRP A C   
3354  O O   . TRP A 420 ? 1.1836 0.9748 1.1013 -0.2160 0.0107  -0.0437 721 TRP A O   
3355  C CB  . TRP A 420 ? 1.0163 0.7547 0.9102 -0.1838 0.0197  -0.0253 721 TRP A CB  
3356  C CG  . TRP A 420 ? 0.8991 0.6304 0.7903 -0.1683 0.0244  -0.0153 721 TRP A CG  
3357  C CD1 . TRP A 420 ? 0.8140 0.5463 0.7088 -0.1718 0.0302  -0.0059 721 TRP A CD1 
3358  C CD2 . TRP A 420 ? 0.8546 0.5799 0.7399 -0.1471 0.0237  -0.0141 721 TRP A CD2 
3359  N NE1 . TRP A 420 ? 0.7396 0.4660 0.6306 -0.1537 0.0326  0.0007  721 TRP A NE1 
3360  C CE2 . TRP A 420 ? 0.8210 0.5437 0.7067 -0.1388 0.0288  -0.0042 721 TRP A CE2 
3361  C CE3 . TRP A 420 ? 0.8270 0.5499 0.7063 -0.1345 0.0194  -0.0206 721 TRP A CE3 
3362  C CZ2 . TRP A 420 ? 0.8962 0.6153 0.7776 -0.1193 0.0295  -0.0009 721 TRP A CZ2 
3363  C CZ3 . TRP A 420 ? 0.8872 0.6069 0.7622 -0.1153 0.0206  -0.0169 721 TRP A CZ3 
3364  C CH2 . TRP A 420 ? 0.8839 0.6020 0.7604 -0.1081 0.0255  -0.0073 721 TRP A CH2 
3365  N N   . LYS A 421 ? 1.2279 1.0368 1.1482 -0.1824 0.0068  -0.0440 722 LYS A N   
3366  C CA  . LYS A 421 ? 1.2631 1.0832 1.1841 -0.1879 0.0000  -0.0554 722 LYS A CA  
3367  C C   . LYS A 421 ? 1.2438 1.0255 1.1434 -0.1901 -0.0032 -0.0631 722 LYS A C   
3368  O O   . LYS A 421 ? 1.2491 1.0284 1.1458 -0.2044 -0.0076 -0.0726 722 LYS A O   
3369  C CB  . LYS A 421 ? 1.2859 1.1348 1.2155 -0.1712 -0.0035 -0.0567 722 LYS A CB  
3370  C CG  . LYS A 421 ? 1.3134 1.1803 1.2537 -0.1573 0.0008  -0.0464 722 LYS A CG  
3371  C CD  . LYS A 421 ? 1.2628 1.1659 1.2229 -0.1643 0.0017  -0.0438 722 LYS A CD  
3372  C CE  . LYS A 421 ? 1.2024 1.1374 1.1728 -0.1515 -0.0021 -0.0449 722 LYS A CE  
3373  N NZ  . LYS A 421 ? 1.1658 1.1374 1.1546 -0.1576 -0.0026 -0.0446 722 LYS A NZ  
3374  N N   . PHE B 4   ? 0.8295 1.1521 0.8229 -0.1653 -0.0160 -0.0531 305 PHE B N   
3375  C CA  . PHE B 4   ? 0.8493 1.1187 0.8279 -0.1732 -0.0114 -0.0554 305 PHE B CA  
3376  C C   . PHE B 4   ? 0.7268 0.9715 0.6952 -0.1623 -0.0137 -0.0556 305 PHE B C   
3377  O O   . PHE B 4   ? 0.7802 1.0408 0.7448 -0.1662 -0.0180 -0.0613 305 PHE B O   
3378  C CB  . PHE B 4   ? 0.9627 1.2255 0.9323 -0.2013 -0.0090 -0.0654 305 PHE B CB  
3379  C CG  . PHE B 4   ? 1.0498 1.3561 1.0309 -0.2162 -0.0088 -0.0676 305 PHE B CG  
3380  C CD1 . PHE B 4   ? 1.0507 1.3571 1.0380 -0.2186 -0.0037 -0.0627 305 PHE B CD1 
3381  C CD2 . PHE B 4   ? 1.0860 1.4361 1.0717 -0.2279 -0.0138 -0.0748 305 PHE B CD2 
3382  C CE1 . PHE B 4   ? 1.0702 1.4206 1.0686 -0.2325 -0.0030 -0.0646 305 PHE B CE1 
3383  C CE2 . PHE B 4   ? 1.1459 1.5416 1.1433 -0.2421 -0.0136 -0.0771 305 PHE B CE2 
3384  C CZ  . PHE B 4   ? 1.1471 1.5434 1.1512 -0.2445 -0.0079 -0.0719 305 PHE B CZ  
3385  N N   . LEU B 5   ? 0.6787 0.8866 0.6424 -0.1495 -0.0107 -0.0496 306 LEU B N   
3386  C CA  . LEU B 5   ? 0.6532 0.8424 0.6099 -0.1359 -0.0123 -0.0473 306 LEU B CA  
3387  C C   . LEU B 5   ? 0.6328 0.7763 0.5744 -0.1408 -0.0082 -0.0511 306 LEU B C   
3388  O O   . LEU B 5   ? 0.6931 0.8116 0.6312 -0.1460 -0.0036 -0.0505 306 LEU B O   
3389  C CB  . LEU B 5   ? 0.5575 0.7472 0.5221 -0.1144 -0.0129 -0.0362 306 LEU B CB  
3390  C CG  . LEU B 5   ? 0.4997 0.7307 0.4773 -0.1067 -0.0165 -0.0319 306 LEU B CG  
3391  C CD1 . LEU B 5   ? 0.4928 0.7161 0.4755 -0.0882 -0.0158 -0.0216 306 LEU B CD1 
3392  C CD2 . LEU B 5   ? 0.4844 0.7438 0.4614 -0.1030 -0.0223 -0.0338 306 LEU B CD2 
3393  N N   . LYS B 6   ? 0.5760 0.7095 0.5077 -0.1377 -0.0099 -0.0549 307 LYS B N   
3394  C CA  . LYS B 6   ? 0.5700 0.6629 0.4857 -0.1391 -0.0065 -0.0592 307 LYS B CA  
3395  C C   . LYS B 6   ? 0.6325 0.7117 0.5486 -0.1200 -0.0059 -0.0517 307 LYS B C   
3396  O O   . LYS B 6   ? 0.6701 0.7706 0.5935 -0.1087 -0.0091 -0.0462 307 LYS B O   
3397  C CB  . LYS B 6   ? 0.6071 0.6987 0.5092 -0.1500 -0.0085 -0.0704 307 LYS B CB  
3398  C CG  . LYS B 6   ? 0.7568 0.8693 0.6587 -0.1707 -0.0105 -0.0788 307 LYS B CG  
3399  C CD  . LYS B 6   ? 0.9539 1.0301 0.8367 -0.1885 -0.0069 -0.0885 307 LYS B CD  
3400  C CE  . LYS B 6   ? 0.9943 1.0855 0.8684 -0.2077 -0.0103 -0.1008 307 LYS B CE  
3401  N NZ  . LYS B 6   ? 1.0603 1.1185 0.9173 -0.2294 -0.0065 -0.1091 307 LYS B NZ  
3402  N N   . VAL B 7   ? 0.6034 0.6474 0.5106 -0.1165 -0.0016 -0.0513 308 VAL B N   
3403  C CA  . VAL B 7   ? 0.5603 0.5916 0.4657 -0.1008 -0.0007 -0.0462 308 VAL B CA  
3404  C C   . VAL B 7   ? 0.6266 0.6305 0.5141 -0.1021 0.0016  -0.0542 308 VAL B C   
3405  O O   . VAL B 7   ? 0.6441 0.6251 0.5197 -0.1129 0.0040  -0.0611 308 VAL B O   
3406  C CB  . VAL B 7   ? 0.6401 0.6588 0.5525 -0.0915 0.0019  -0.0373 308 VAL B CB  
3407  C CG1 . VAL B 7   ? 0.6704 0.7125 0.5978 -0.0906 0.0001  -0.0308 308 VAL B CG1 
3408  C CG2 . VAL B 7   ? 0.6143 0.6005 0.5165 -0.0962 0.0064  -0.0403 308 VAL B CG2 
3409  N N   . LYS B 8   ? 0.5558 0.5613 0.4398 -0.0912 0.0010  -0.0534 309 LYS B N   
3410  C CA  . LYS B 8   ? 0.5264 0.5091 0.3928 -0.0896 0.0031  -0.0613 309 LYS B CA  
3411  C C   . LYS B 8   ? 0.5131 0.4844 0.3791 -0.0739 0.0058  -0.0556 309 LYS B C   
3412  O O   . LYS B 8   ? 0.6783 0.6678 0.5562 -0.0651 0.0047  -0.0470 309 LYS B O   
3413  C CB  . LYS B 8   ? 0.6320 0.6320 0.4920 -0.0924 -0.0001 -0.0682 309 LYS B CB  
3414  C CG  . LYS B 8   ? 0.6817 0.6604 0.5225 -0.0880 0.0020  -0.0767 309 LYS B CG  
3415  C CD  . LYS B 8   ? 0.7421 0.7402 0.5763 -0.0919 -0.0015 -0.0840 309 LYS B CD  
3416  C CE  . LYS B 8   ? 0.7589 0.7422 0.5762 -0.0825 0.0007  -0.0904 309 LYS B CE  
3417  N NZ  . LYS B 8   ? 0.7610 0.7643 0.5710 -0.0860 -0.0028 -0.0976 309 LYS B NZ  
3418  N N   . ASN B 9   ? 0.5560 0.4968 0.4071 -0.0705 0.0094  -0.0606 310 ASN B N   
3419  C CA  . ASN B 9   ? 0.6614 0.5942 0.5093 -0.0550 0.0120  -0.0576 310 ASN B CA  
3420  C C   . ASN B 9   ? 0.7103 0.6453 0.5455 -0.0501 0.0121  -0.0649 310 ASN B C   
3421  O O   . ASN B 9   ? 0.7160 0.6332 0.5342 -0.0563 0.0124  -0.0754 310 ASN B O   
3422  C CB  . ASN B 9   ? 0.6789 0.5788 0.5169 -0.0511 0.0158  -0.0583 310 ASN B CB  
3423  C CG  . ASN B 9   ? 0.7271 0.6238 0.5636 -0.0341 0.0182  -0.0548 310 ASN B CG  
3424  O OD1 . ASN B 9   ? 0.7370 0.6334 0.5632 -0.0259 0.0192  -0.0598 310 ASN B OD1 
3425  N ND2 . ASN B 9   ? 0.6814 0.5776 0.5278 -0.0284 0.0191  -0.0466 310 ASN B ND2 
3426  N N   . TRP B 10  ? 0.7475 0.7039 0.5897 -0.0399 0.0118  -0.0596 311 TRP B N   
3427  C CA  . TRP B 10  ? 0.7204 0.6855 0.5521 -0.0356 0.0117  -0.0657 311 TRP B CA  
3428  C C   . TRP B 10  ? 0.7616 0.7085 0.5787 -0.0226 0.0158  -0.0705 311 TRP B C   
3429  O O   . TRP B 10  ? 0.7928 0.7457 0.5994 -0.0171 0.0164  -0.0763 311 TRP B O   
3430  C CB  . TRP B 10  ? 0.5849 0.5837 0.4293 -0.0320 0.0097  -0.0574 311 TRP B CB  
3431  C CG  . TRP B 10  ? 0.5036 0.5212 0.3578 -0.0421 0.0053  -0.0544 311 TRP B CG  
3432  C CD1 . TRP B 10  ? 0.4585 0.4834 0.3276 -0.0454 0.0036  -0.0459 311 TRP B CD1 
3433  C CD2 . TRP B 10  ? 0.5816 0.6150 0.4309 -0.0489 0.0018  -0.0601 311 TRP B CD2 
3434  N NE1 . TRP B 10  ? 0.5577 0.6027 0.4316 -0.0527 -0.0006 -0.0457 311 TRP B NE1 
3435  C CE2 . TRP B 10  ? 0.6111 0.6627 0.4735 -0.0554 -0.0019 -0.0543 311 TRP B CE2 
3436  C CE3 . TRP B 10  ? 0.7318 0.7666 0.5661 -0.0495 0.0014  -0.0700 311 TRP B CE3 
3437  C CZ2 . TRP B 10  ? 0.6383 0.7118 0.5001 -0.0621 -0.0064 -0.0576 311 TRP B CZ2 
3438  C CZ3 . TRP B 10  ? 0.7377 0.7931 0.5711 -0.0575 -0.0031 -0.0736 311 TRP B CZ3 
3439  C CH2 . TRP B 10  ? 0.7347 0.8104 0.5824 -0.0636 -0.0070 -0.0671 311 TRP B CH2 
3440  N N   . GLU B 11  ? 0.7787 0.7047 0.5941 -0.0164 0.0185  -0.0683 312 GLU B N   
3441  C CA  . GLU B 11  ? 0.7165 0.6222 0.5157 -0.0024 0.0223  -0.0735 312 GLU B CA  
3442  C C   . GLU B 11  ? 0.7707 0.6364 0.5469 -0.0071 0.0235  -0.0842 312 GLU B C   
3443  O O   . GLU B 11  ? 0.8318 0.6798 0.5876 0.0016  0.0256  -0.0932 312 GLU B O   
3444  C CB  . GLU B 11  ? 0.8237 0.7305 0.6327 0.0085  0.0243  -0.0647 312 GLU B CB  
3445  C CG  . GLU B 11  ? 0.9887 0.8957 0.7888 0.0270  0.0277  -0.0665 312 GLU B CG  
3446  C CD  . GLU B 11  ? 1.0525 0.9743 0.8673 0.0360  0.0287  -0.0566 312 GLU B CD  
3447  O OE1 . GLU B 11  ? 0.9271 0.8366 0.7478 0.0325  0.0281  -0.0518 312 GLU B OE1 
3448  O OE2 . GLU B 11  ? 1.1596 1.1073 0.9801 0.0458  0.0301  -0.0537 312 GLU B OE2 
3449  N N   . THR B 12  ? 0.7444 0.5952 0.5223 -0.0212 0.0224  -0.0838 313 THR B N   
3450  C CA  . THR B 12  ? 0.7746 0.5845 0.5300 -0.0286 0.0239  -0.0926 313 THR B CA  
3451  C C   . THR B 12  ? 0.8148 0.6252 0.5653 -0.0487 0.0211  -0.1004 313 THR B C   
3452  O O   . THR B 12  ? 0.8597 0.6357 0.5883 -0.0574 0.0222  -0.1096 313 THR B O   
3453  C CB  . THR B 12  ? 0.7680 0.5575 0.5260 -0.0310 0.0256  -0.0863 313 THR B CB  
3454  O OG1 . THR B 12  ? 0.7212 0.5327 0.4994 -0.0458 0.0229  -0.0802 313 THR B OG1 
3455  C CG2 . THR B 12  ? 0.7556 0.5498 0.5211 -0.0123 0.0276  -0.0780 313 THR B CG2 
3456  N N   . GLU B 13  ? 0.8335 0.6817 0.6031 -0.0565 0.0173  -0.0967 314 GLU B N   
3457  C CA  . GLU B 13  ? 0.8497 0.7088 0.6201 -0.0759 0.0137  -0.1023 314 GLU B CA  
3458  C C   . GLU B 13  ? 0.8192 0.6633 0.5908 -0.0921 0.0141  -0.1016 314 GLU B C   
3459  O O   . GLU B 13  ? 0.8434 0.6911 0.6115 -0.1102 0.0118  -0.1081 314 GLU B O   
3460  C CB  . GLU B 13  ? 0.8546 0.7005 0.6023 -0.0802 0.0131  -0.1162 314 GLU B CB  
3461  C CG  . GLU B 13  ? 0.9872 0.8667 0.7405 -0.0730 0.0106  -0.1166 314 GLU B CG  
3462  C CD  . GLU B 13  ? 1.0565 0.9209 0.7851 -0.0736 0.0105  -0.1307 314 GLU B CD  
3463  O OE1 . GLU B 13  ? 1.1736 1.0493 0.8985 -0.0886 0.0067  -0.1383 314 GLU B OE1 
3464  O OE2 . GLU B 13  ? 0.9541 0.7960 0.6663 -0.0585 0.0141  -0.1347 314 GLU B OE2 
3465  N N   . VAL B 14  ? 0.7513 0.5819 0.5283 -0.0866 0.0168  -0.0935 315 VAL B N   
3466  C CA  . VAL B 14  ? 0.7710 0.5935 0.5519 -0.1016 0.0174  -0.0911 315 VAL B CA  
3467  C C   . VAL B 14  ? 0.7218 0.5872 0.5275 -0.1097 0.0136  -0.0852 315 VAL B C   
3468  O O   . VAL B 14  ? 0.7185 0.6112 0.5418 -0.0985 0.0119  -0.0770 315 VAL B O   
3469  C CB  . VAL B 14  ? 0.8749 0.6740 0.6548 -0.0918 0.0212  -0.0836 315 VAL B CB  
3470  C CG1 . VAL B 14  ? 0.8913 0.6916 0.6802 -0.1057 0.0218  -0.0786 315 VAL B CG1 
3471  C CG2 . VAL B 14  ? 0.8939 0.6465 0.6451 -0.0849 0.0249  -0.0903 315 VAL B CG2 
3472  N N   . VAL B 15  ? 0.7426 0.6141 0.5483 -0.1293 0.0122  -0.0897 316 VAL B N   
3473  C CA  . VAL B 15  ? 0.7263 0.6390 0.5538 -0.1368 0.0086  -0.0849 316 VAL B CA  
3474  C C   . VAL B 15  ? 0.8751 0.7828 0.7081 -0.1480 0.0109  -0.0810 316 VAL B C   
3475  O O   . VAL B 15  ? 0.9442 0.8274 0.7621 -0.1638 0.0132  -0.0873 316 VAL B O   
3476  C CB  . VAL B 15  ? 0.7294 0.6651 0.5547 -0.1504 0.0044  -0.0939 316 VAL B CB  
3477  C CG1 . VAL B 15  ? 0.6233 0.6017 0.4699 -0.1580 0.0009  -0.0891 316 VAL B CG1 
3478  C CG2 . VAL B 15  ? 0.7074 0.6529 0.5285 -0.1384 0.0021  -0.0967 316 VAL B CG2 
3479  N N   . LEU B 16  ? 0.8355 0.7658 0.6886 -0.1406 0.0104  -0.0707 317 LEU B N   
3480  C CA  . LEU B 16  ? 0.7653 0.6981 0.6262 -0.1493 0.0124  -0.0661 317 LEU B CA  
3481  C C   . LEU B 16  ? 0.7265 0.7045 0.6059 -0.1564 0.0086  -0.0645 317 LEU B C   
3482  O O   . LEU B 16  ? 0.8074 0.8138 0.6962 -0.1489 0.0044  -0.0635 317 LEU B O   
3483  C CB  . LEU B 16  ? 0.6923 0.6141 0.5600 -0.1342 0.0149  -0.0561 317 LEU B CB  
3484  C CG  . LEU B 16  ? 0.6466 0.5306 0.4984 -0.1224 0.0180  -0.0564 317 LEU B CG  
3485  C CD1 . LEU B 16  ? 0.5746 0.4590 0.4368 -0.1060 0.0189  -0.0465 317 LEU B CD1 
3486  C CD2 . LEU B 16  ? 0.6270 0.4712 0.4568 -0.1338 0.0220  -0.0620 317 LEU B CD2 
3487  N N   . THR B 17  ? 0.6155 0.6008 0.4992 -0.1703 0.0103  -0.0640 318 THR B N   
3488  C CA  . THR B 17  ? 0.5872 0.6173 0.4868 -0.1788 0.0072  -0.0640 318 THR B CA  
3489  C C   . THR B 17  ? 0.6727 0.7166 0.5869 -0.1741 0.0091  -0.0551 318 THR B C   
3490  O O   . THR B 17  ? 0.6995 0.7243 0.6083 -0.1830 0.0137  -0.0541 318 THR B O   
3491  C CB  . THR B 17  ? 0.6812 0.7152 0.5718 -0.2040 0.0073  -0.0738 318 THR B CB  
3492  O OG1 . THR B 17  ? 0.6746 0.6899 0.5483 -0.2081 0.0057  -0.0830 318 THR B OG1 
3493  C CG2 . THR B 17  ? 0.7386 0.8266 0.6469 -0.2109 0.0032  -0.0743 318 THR B CG2 
3494  N N   . ASP B 18  ? 0.5980 0.6741 0.5288 -0.1603 0.0057  -0.0489 319 ASP B N   
3495  C CA  . ASP B 18  ? 0.5410 0.6273 0.4843 -0.1506 0.0072  -0.0403 319 ASP B CA  
3496  C C   . ASP B 18  ? 0.6017 0.7303 0.5580 -0.1589 0.0059  -0.0407 319 ASP B C   
3497  O O   . ASP B 18  ? 0.5626 0.7261 0.5273 -0.1555 0.0011  -0.0417 319 ASP B O   
3498  C CB  . ASP B 18  ? 0.5184 0.6074 0.4687 -0.1287 0.0045  -0.0329 319 ASP B CB  
3499  C CG  . ASP B 18  ? 0.5539 0.6425 0.5127 -0.1178 0.0064  -0.0246 319 ASP B CG  
3500  O OD1 . ASP B 18  ? 0.4621 0.5789 0.4315 -0.1184 0.0059  -0.0226 319 ASP B OD1 
3501  O OD2 . ASP B 18  ? 0.6002 0.6617 0.5548 -0.1082 0.0082  -0.0205 319 ASP B OD2 
3502  N N   . THR B 19  ? 0.5230 0.6500 0.4802 -0.1696 0.0103  -0.0398 320 THR B N   
3503  C CA  . THR B 19  ? 0.5026 0.6712 0.4740 -0.1735 0.0102  -0.0382 320 THR B CA  
3504  C C   . THR B 19  ? 0.5211 0.6904 0.5008 -0.1584 0.0125  -0.0296 320 THR B C   
3505  O O   . THR B 19  ? 0.4991 0.7061 0.4918 -0.1540 0.0116  -0.0272 320 THR B O   
3506  C CB  . THR B 19  ? 0.5590 0.7320 0.5256 -0.1997 0.0140  -0.0438 320 THR B CB  
3507  O OG1 . THR B 19  ? 0.6023 0.7278 0.5536 -0.2066 0.0196  -0.0430 320 THR B OG1 
3508  C CG2 . THR B 19  ? 0.5377 0.7247 0.4993 -0.2173 0.0109  -0.0534 320 THR B CG2 
3509  N N   . LEU B 20  ? 0.5268 0.6569 0.4987 -0.1500 0.0153  -0.0253 321 LEU B N   
3510  C CA  . LEU B 20  ? 0.6150 0.7435 0.5929 -0.1372 0.0175  -0.0180 321 LEU B CA  
3511  C C   . LEU B 20  ? 0.6024 0.7564 0.5921 -0.1174 0.0132  -0.0134 321 LEU B C   
3512  O O   . LEU B 20  ? 0.4959 0.6626 0.4925 -0.1088 0.0145  -0.0090 321 LEU B O   
3513  C CB  . LEU B 20  ? 0.5688 0.6523 0.5357 -0.1306 0.0203  -0.0147 321 LEU B CB  
3514  C CG  . LEU B 20  ? 0.5628 0.6381 0.5328 -0.1181 0.0225  -0.0079 321 LEU B CG  
3515  C CD1 . LEU B 20  ? 0.4045 0.4883 0.3754 -0.1290 0.0276  -0.0069 321 LEU B CD1 
3516  C CD2 . LEU B 20  ? 0.4546 0.4905 0.4145 -0.1096 0.0234  -0.0053 321 LEU B CD2 
3517  N N   . HIS B 21  ? 0.5139 0.6745 0.5042 -0.1098 0.0083  -0.0141 322 HIS B N   
3518  C CA  . HIS B 21  ? 0.5595 0.7388 0.5574 -0.0906 0.0043  -0.0090 322 HIS B CA  
3519  C C   . HIS B 21  ? 0.5288 0.7527 0.5378 -0.0886 0.0029  -0.0091 322 HIS B C   
3520  O O   . HIS B 21  ? 0.4834 0.7209 0.4971 -0.0708 0.0002  -0.0042 322 HIS B O   
3521  C CB  . HIS B 21  ? 0.4903 0.6696 0.4850 -0.0849 -0.0004 -0.0097 322 HIS B CB  
3522  C CG  . HIS B 21  ? 0.4580 0.6701 0.4557 -0.0947 -0.0035 -0.0155 322 HIS B CG  
3523  N ND1 . HIS B 21  ? 0.4754 0.6809 0.4663 -0.1128 -0.0028 -0.0232 322 HIS B ND1 
3524  C CD2 . HIS B 21  ? 0.4545 0.7074 0.4606 -0.0890 -0.0075 -0.0153 322 HIS B CD2 
3525  C CE1 . HIS B 21  ? 0.5075 0.7493 0.5031 -0.1193 -0.0064 -0.0278 322 HIS B CE1 
3526  N NE2 . HIS B 21  ? 0.5118 0.7846 0.5173 -0.1046 -0.0093 -0.0229 322 HIS B NE2 
3527  N N   . LEU B 22  ? 0.4665 0.7143 0.4790 -0.1064 0.0046  -0.0145 323 LEU B N   
3528  C CA  . LEU B 22  ? 0.4669 0.7621 0.4912 -0.1046 0.0038  -0.0146 323 LEU B CA  
3529  C C   . LEU B 22  ? 0.5774 0.8729 0.6057 -0.0951 0.0077  -0.0097 323 LEU B C   
3530  O O   . LEU B 22  ? 0.6627 0.9959 0.7003 -0.0861 0.0069  -0.0083 323 LEU B O   
3531  C CB  . LEU B 22  ? 0.5152 0.8369 0.5421 -0.1291 0.0052  -0.0219 323 LEU B CB  
3532  C CG  . LEU B 22  ? 0.5714 0.8923 0.5924 -0.1433 0.0020  -0.0289 323 LEU B CG  
3533  C CD1 . LEU B 22  ? 0.5576 0.8999 0.5793 -0.1706 0.0043  -0.0361 323 LEU B CD1 
3534  C CD2 . LEU B 22  ? 0.5784 0.9288 0.6047 -0.1289 -0.0049 -0.0284 323 LEU B CD2 
3535  N N   . LYS B 23  ? 0.5828 0.8387 0.6035 -0.0960 0.0117  -0.0071 324 LYS B N   
3536  C CA  . LYS B 23  ? 0.5052 0.7567 0.5274 -0.0864 0.0152  -0.0026 324 LYS B CA  
3537  C C   . LYS B 23  ? 0.6242 0.8582 0.6443 -0.0629 0.0124  0.0029  324 LYS B C   
3538  O O   . LYS B 23  ? 0.6837 0.9074 0.7027 -0.0537 0.0148  0.0063  324 LYS B O   
3539  C CB  . LYS B 23  ? 0.4834 0.7019 0.4972 -0.1003 0.0210  -0.0027 324 LYS B CB  
3540  C CG  . LYS B 23  ? 0.5489 0.7907 0.5666 -0.1147 0.0264  -0.0039 324 LYS B CG  
3541  C CD  . LYS B 23  ? 0.6043 0.8862 0.6289 -0.1311 0.0254  -0.0094 324 LYS B CD  
3542  C CE  . LYS B 23  ? 0.7662 1.0857 0.7987 -0.1407 0.0301  -0.0096 324 LYS B CE  
3543  N NZ  . LYS B 23  ? 0.7208 1.0158 0.7471 -0.1416 0.0364  -0.0054 324 LYS B NZ  
3544  N N   . SER B 24  ? 0.6165 0.8462 0.6347 -0.0540 0.0073  0.0037  325 SER B N   
3545  C CA  . SER B 24  ? 0.6945 0.9044 0.7084 -0.0342 0.0046  0.0091  325 SER B CA  
3546  C C   . SER B 24  ? 0.7347 0.9693 0.7530 -0.0166 0.0034  0.0120  325 SER B C   
3547  O O   . SER B 24  ? 0.7574 1.0319 0.7830 -0.0150 0.0020  0.0102  325 SER B O   
3548  C CB  . SER B 24  ? 0.7335 0.9359 0.7434 -0.0307 -0.0001 0.0097  325 SER B CB  
3549  O OG  . SER B 24  ? 0.8476 1.0332 0.8524 -0.0130 -0.0027 0.0154  325 SER B OG  
3550  N N   . THR B 25  ? 0.7425 0.9537 0.7552 -0.0026 0.0039  0.0160  326 THR B N   
3551  C CA  . THR B 25  ? 0.8315 1.0605 0.8454 0.0155  0.0034  0.0182  326 THR B CA  
3552  C C   . THR B 25  ? 0.8201 1.0355 0.8260 0.0357  -0.0013 0.0227  326 THR B C   
3553  O O   . THR B 25  ? 0.9080 1.1490 0.9150 0.0507  -0.0038 0.0239  326 THR B O   
3554  C CB  . THR B 25  ? 0.8556 1.0707 0.8675 0.0167  0.0080  0.0186  326 THR B CB  
3555  O OG1 . THR B 25  ? 0.8094 0.9972 0.8185 0.0004  0.0111  0.0176  326 THR B OG1 
3556  C CG2 . THR B 25  ? 0.9154 1.1713 0.9361 0.0158  0.0113  0.0163  326 THR B CG2 
3557  N N   . LEU B 26  ? 0.7140 0.8905 0.7108 0.0366  -0.0026 0.0256  327 LEU B N   
3558  C CA  . LEU B 26  ? 0.6957 0.8527 0.6820 0.0540  -0.0063 0.0305  327 LEU B CA  
3559  C C   . LEU B 26  ? 0.7195 0.8711 0.7021 0.0525  -0.0101 0.0328  327 LEU B C   
3560  O O   . LEU B 26  ? 0.6644 0.8177 0.6512 0.0373  -0.0097 0.0303  327 LEU B O   
3561  C CB  . LEU B 26  ? 0.6847 0.8023 0.6620 0.0563  -0.0049 0.0324  327 LEU B CB  
3562  C CG  . LEU B 26  ? 0.8265 0.9492 0.8060 0.0586  -0.0010 0.0300  327 LEU B CG  
3563  C CD1 . LEU B 26  ? 0.8585 0.9762 0.8436 0.0403  0.0034  0.0270  327 LEU B CD1 
3564  C CD2 . LEU B 26  ? 0.7881 0.8822 0.7551 0.0731  -0.0019 0.0324  327 LEU B CD2 
3565  N N   . GLU B 27  ? 0.6867 0.8303 0.6595 0.0691  -0.0137 0.0378  328 GLU B N   
3566  C CA  . GLU B 27  ? 0.6960 0.8342 0.6632 0.0697  -0.0173 0.0412  328 GLU B CA  
3567  C C   . GLU B 27  ? 0.6963 0.7994 0.6581 0.0586  -0.0164 0.0428  328 GLU B C   
3568  O O   . GLU B 27  ? 0.6852 0.7604 0.6420 0.0584  -0.0147 0.0438  328 GLU B O   
3569  C CB  . GLU B 27  ? 0.5414 0.6752 0.4962 0.0912  -0.0210 0.0472  328 GLU B CB  
3570  C CG  . GLU B 27  ? 0.5912 0.7683 0.5517 0.1030  -0.0233 0.0461  328 GLU B CG  
3571  C CD  . GLU B 27  ? 0.6741 0.8456 0.6203 0.1282  -0.0267 0.0520  328 GLU B CD  
3572  O OE1 . GLU B 27  ? 0.7139 0.9227 0.6641 0.1411  -0.0287 0.0514  328 GLU B OE1 
3573  O OE2 . GLU B 27  ? 0.7435 0.8735 0.6734 0.1351  -0.0274 0.0573  328 GLU B OE2 
3574  N N   . THR B 28  ? 0.6076 0.7152 0.5708 0.0493  -0.0175 0.0425  329 THR B N   
3575  C CA  . THR B 28  ? 0.4885 0.5684 0.4467 0.0403  -0.0168 0.0442  329 THR B CA  
3576  C C   . THR B 28  ? 0.4219 0.4793 0.3664 0.0498  -0.0193 0.0516  329 THR B C   
3577  O O   . THR B 28  ? 0.5514 0.5827 0.4904 0.0441  -0.0183 0.0540  329 THR B O   
3578  C CB  . THR B 28  ? 0.5690 0.6615 0.5322 0.0272  -0.0166 0.0405  329 THR B CB  
3579  O OG1 . THR B 28  ? 0.4972 0.6109 0.4585 0.0330  -0.0202 0.0422  329 THR B OG1 
3580  C CG2 . THR B 28  ? 0.5347 0.6422 0.5083 0.0148  -0.0137 0.0331  329 THR B CG2 
3581  N N   . GLY B 29  ? 0.4481 0.5154 0.3861 0.0641  -0.0225 0.0556  330 GLY B N   
3582  C CA  . GLY B 29  ? 0.5022 0.5493 0.4248 0.0725  -0.0250 0.0634  330 GLY B CA  
3583  C C   . GLY B 29  ? 0.6208 0.6872 0.5422 0.0728  -0.0276 0.0655  330 GLY B C   
3584  O O   . GLY B 29  ? 0.7125 0.7702 0.6203 0.0844  -0.0303 0.0726  330 GLY B O   
3585  N N   . CYS B 30  ? 0.5156 0.6066 0.4490 0.0608  -0.0270 0.0595  331 CYS B N   
3586  C CA  . CYS B 30  ? 0.5566 0.6664 0.4883 0.0599  -0.0296 0.0605  331 CYS B CA  
3587  C C   . CYS B 30  ? 0.5448 0.6892 0.4789 0.0720  -0.0332 0.0599  331 CYS B C   
3588  O O   . CYS B 30  ? 0.6186 0.7780 0.5589 0.0785  -0.0331 0.0572  331 CYS B O   
3589  C CB  . CYS B 30  ? 0.3922 0.5123 0.3333 0.0424  -0.0276 0.0533  331 CYS B CB  
3590  S SG  . CYS B 30  ? 0.4556 0.5428 0.3949 0.0297  -0.0235 0.0534  331 CYS B SG  
3591  N N   . THR B 31  ? 0.5875 0.7466 0.5161 0.0756  -0.0365 0.0626  332 THR B N   
3592  C CA  . THR B 31  ? 0.5936 0.7933 0.5265 0.0839  -0.0404 0.0607  332 THR B CA  
3593  C C   . THR B 31  ? 0.6416 0.8615 0.5770 0.0726  -0.0420 0.0569  332 THR B C   
3594  O O   . THR B 31  ? 0.6438 0.8451 0.5769 0.0603  -0.0398 0.0561  332 THR B O   
3595  C CB  . THR B 31  ? 0.6468 0.8444 0.5654 0.1073  -0.0441 0.0697  332 THR B CB  
3596  O OG1 . THR B 31  ? 0.5745 0.7549 0.4780 0.1100  -0.0458 0.0773  332 THR B OG1 
3597  C CG2 . THR B 31  ? 0.5991 0.7658 0.5102 0.1188  -0.0422 0.0737  332 THR B CG2 
3598  N N   . GLU B 32  ? 0.7039 0.9641 0.6436 0.0774  -0.0461 0.0542  333 GLU B N   
3599  C CA  . GLU B 32  ? 0.7302 1.0105 0.6694 0.0689  -0.0485 0.0507  333 GLU B CA  
3600  C C   . GLU B 32  ? 0.7055 0.9636 0.6282 0.0752  -0.0496 0.0596  333 GLU B C   
3601  O O   . GLU B 32  ? 0.6959 0.9598 0.6167 0.0653  -0.0500 0.0568  333 GLU B O   
3602  C CB  . GLU B 32  ? 0.8076 1.1378 0.7531 0.0749  -0.0535 0.0469  333 GLU B CB  
3603  C CG  . GLU B 32  ? 0.8742 1.2341 0.8370 0.0609  -0.0523 0.0360  333 GLU B CG  
3604  C CD  . GLU B 32  ? 1.0054 1.3698 0.9747 0.0705  -0.0506 0.0372  333 GLU B CD  
3605  O OE1 . GLU B 32  ? 1.0479 1.3837 1.0082 0.0861  -0.0496 0.0453  333 GLU B OE1 
3606  O OE2 . GLU B 32  ? 1.0382 1.4350 1.0211 0.0619  -0.0501 0.0297  333 GLU B OE2 
3607  N N   . TYR B 33  ? 0.6764 0.9069 0.5858 0.0903  -0.0496 0.0702  334 TYR B N   
3608  C CA  . TYR B 33  ? 0.6810 0.8907 0.5727 0.0962  -0.0505 0.0800  334 TYR B CA  
3609  C C   . TYR B 33  ? 0.6733 0.8372 0.5564 0.0899  -0.0460 0.0856  334 TYR B C   
3610  O O   . TYR B 33  ? 0.7226 0.8698 0.5918 0.0902  -0.0458 0.0932  334 TYR B O   
3611  C CB  . TYR B 33  ? 0.7211 0.9350 0.5983 0.1197  -0.0549 0.0895  334 TYR B CB  
3612  C CG  . TYR B 33  ? 0.7303 0.9935 0.6138 0.1277  -0.0602 0.0855  334 TYR B CG  
3613  C CD1 . TYR B 33  ? 0.8591 1.1450 0.7385 0.1254  -0.0634 0.0853  334 TYR B CD1 
3614  C CD2 . TYR B 33  ? 0.6972 0.9872 0.5906 0.1375  -0.0619 0.0815  334 TYR B CD2 
3615  C CE1 . TYR B 33  ? 0.8953 1.2295 0.7805 0.1320  -0.0687 0.0811  334 TYR B CE1 
3616  C CE2 . TYR B 33  ? 0.7374 1.0773 0.6375 0.1440  -0.0669 0.0775  334 TYR B CE2 
3617  C CZ  . TYR B 33  ? 0.8636 1.2255 0.7596 0.1411  -0.0705 0.0773  334 TYR B CZ  
3618  O OH  . TYR B 33  ? 0.9757 1.3904 0.8787 0.1470  -0.0760 0.0728  334 TYR B OH  
3619  N N   . ILE B 34  ? 0.5185 0.6632 0.4088 0.0843  -0.0426 0.0825  335 ILE B N   
3620  C CA  . ILE B 34  ? 0.5454 0.6506 0.4287 0.0771  -0.0387 0.0870  335 ILE B CA  
3621  C C   . ILE B 34  ? 0.5843 0.6862 0.4829 0.0627  -0.0349 0.0780  335 ILE B C   
3622  O O   . ILE B 34  ? 0.6343 0.7460 0.5428 0.0646  -0.0347 0.0728  335 ILE B O   
3623  C CB  . ILE B 34  ? 0.6437 0.7167 0.5112 0.0908  -0.0391 0.0963  335 ILE B CB  
3624  C CG1 . ILE B 34  ? 0.9108 0.9870 0.7612 0.1086  -0.0432 0.1053  335 ILE B CG1 
3625  C CG2 . ILE B 34  ? 0.6036 0.6388 0.4613 0.0813  -0.0357 0.1017  335 ILE B CG2 
3626  C CD1 . ILE B 34  ? 1.0678 1.1364 0.9093 0.1293  -0.0456 0.1090  335 ILE B CD1 
3627  N N   . CYS B 35  ? 0.5176 0.6077 0.4177 0.0489  -0.0317 0.0765  336 CYS B N   
3628  C CA  . CYS B 35  ? 0.4951 0.5765 0.4063 0.0369  -0.0279 0.0696  336 CYS B CA  
3629  C C   . CYS B 35  ? 0.5427 0.5902 0.4469 0.0360  -0.0257 0.0754  336 CYS B C   
3630  O O   . CYS B 35  ? 0.5620 0.5933 0.4543 0.0354  -0.0253 0.0829  336 CYS B O   
3631  C CB  . CYS B 35  ? 0.4360 0.5272 0.3529 0.0238  -0.0259 0.0633  336 CYS B CB  
3632  S SG  . CYS B 35  ? 0.4827 0.5577 0.4091 0.0117  -0.0212 0.0568  336 CYS B SG  
3633  N N   . MET B 36  ? 0.4858 0.5234 0.3965 0.0348  -0.0241 0.0718  337 MET B N   
3634  C CA  . MET B 36  ? 0.5340 0.5411 0.4385 0.0332  -0.0224 0.0758  337 MET B CA  
3635  C C   . MET B 36  ? 0.4833 0.4855 0.3977 0.0208  -0.0190 0.0700  337 MET B C   
3636  O O   . MET B 36  ? 0.5539 0.5353 0.4661 0.0187  -0.0178 0.0712  337 MET B O   
3637  C CB  . MET B 36  ? 0.5438 0.5400 0.4438 0.0452  -0.0238 0.0775  337 MET B CB  
3638  C CG  . MET B 36  ? 0.6446 0.6348 0.5291 0.0598  -0.0270 0.0854  337 MET B CG  
3639  S SD  . MET B 36  ? 0.9465 0.9135 0.8211 0.0743  -0.0279 0.0874  337 MET B SD  
3640  C CE  . MET B 36  ? 0.9232 0.8895 0.7795 0.0938  -0.0319 0.0962  337 MET B CE  
3641  N N   . GLY B 37  ? 0.4893 0.5088 0.4126 0.0128  -0.0176 0.0638  338 GLY B N   
3642  C CA  . GLY B 37  ? 0.5303 0.5470 0.4622 0.0035  -0.0145 0.0577  338 GLY B CA  
3643  C C   . GLY B 37  ? 0.4839 0.4829 0.4127 -0.0025 -0.0124 0.0607  338 GLY B C   
3644  O O   . GLY B 37  ? 0.4320 0.4285 0.3672 -0.0081 -0.0101 0.0561  338 GLY B O   
3645  N N   . SER B 38  ? 0.5077 0.4950 0.4261 -0.0020 -0.0131 0.0686  339 SER B N   
3646  C CA  . SER B 38  ? 0.4736 0.4462 0.3888 -0.0094 -0.0113 0.0717  339 SER B CA  
3647  C C   . SER B 38  ? 0.5420 0.4902 0.4475 -0.0071 -0.0126 0.0773  339 SER B C   
3648  O O   . SER B 38  ? 0.5550 0.4896 0.4547 -0.0146 -0.0116 0.0813  339 SER B O   
3649  C CB  . SER B 38  ? 0.5587 0.5381 0.4689 -0.0147 -0.0101 0.0760  339 SER B CB  
3650  O OG  . SER B 38  ? 0.5780 0.5482 0.4747 -0.0111 -0.0118 0.0846  339 SER B OG  
3651  N N   . ILE B 39  ? 0.4725 0.4152 0.3746 0.0030  -0.0148 0.0777  340 ILE B N   
3652  C CA  . ILE B 39  ? 0.6057 0.5228 0.4975 0.0071  -0.0160 0.0810  340 ILE B CA  
3653  C C   . ILE B 39  ? 0.5722 0.4855 0.4726 0.0039  -0.0148 0.0748  340 ILE B C   
3654  O O   . ILE B 39  ? 0.6402 0.5701 0.5527 0.0051  -0.0139 0.0683  340 ILE B O   
3655  C CB  . ILE B 39  ? 0.6183 0.5334 0.5022 0.0220  -0.0186 0.0834  340 ILE B CB  
3656  C CG1 . ILE B 39  ? 0.5708 0.4903 0.4449 0.0261  -0.0201 0.0902  340 ILE B CG1 
3657  C CG2 . ILE B 39  ? 0.5491 0.4344 0.4199 0.0281  -0.0197 0.0860  340 ILE B CG2 
3658  C CD1 . ILE B 39  ? 0.6241 0.5160 0.4803 0.0216  -0.0199 0.0991  340 ILE B CD1 
3659  N N   . MET B 40  ? 0.5895 0.4804 0.4823 -0.0009 -0.0148 0.0767  341 MET B N   
3660  C CA  . MET B 40  ? 0.6477 0.5351 0.5473 -0.0043 -0.0140 0.0711  341 MET B CA  
3661  C C   . MET B 40  ? 0.6529 0.5392 0.5537 0.0068  -0.0147 0.0674  341 MET B C   
3662  O O   . MET B 40  ? 0.5576 0.4561 0.4696 0.0065  -0.0133 0.0617  341 MET B O   
3663  C CB  . MET B 40  ? 0.7933 0.6582 0.6831 -0.0130 -0.0144 0.0738  341 MET B CB  
3664  C CG  . MET B 40  ? 0.9416 0.8035 0.8371 -0.0164 -0.0141 0.0682  341 MET B CG  
3665  S SD  . MET B 40  ? 0.9747 0.8599 0.8857 -0.0263 -0.0118 0.0642  341 MET B SD  
3666  C CE  . MET B 40  ? 0.8430 0.7270 0.7477 -0.0389 -0.0114 0.0704  341 MET B CE  
3667  N N   . HIS B 41  ? 0.7692 0.6410 0.6574 0.0174  -0.0167 0.0709  342 HIS B N   
3668  C CA  . HIS B 41  ? 0.7693 0.6431 0.6578 0.0301  -0.0173 0.0677  342 HIS B CA  
3669  C C   . HIS B 41  ? 0.6457 0.5296 0.5297 0.0429  -0.0189 0.0710  342 HIS B C   
3670  O O   . HIS B 41  ? 0.6437 0.5085 0.5119 0.0538  -0.0208 0.0752  342 HIS B O   
3671  C CB  . HIS B 41  ? 0.7453 0.5899 0.6204 0.0337  -0.0182 0.0676  342 HIS B CB  
3672  C CG  . HIS B 41  ? 0.8340 0.6653 0.7088 0.0199  -0.0176 0.0662  342 HIS B CG  
3673  N ND1 . HIS B 41  ? 0.8605 0.7054 0.7488 0.0134  -0.0159 0.0606  342 HIS B ND1 
3674  C CD2 . HIS B 41  ? 0.9129 0.7200 0.7750 0.0109  -0.0186 0.0697  342 HIS B CD2 
3675  C CE1 . HIS B 41  ? 0.9011 0.7335 0.7861 0.0023  -0.0162 0.0606  342 HIS B CE1 
3676  N NE2 . HIS B 41  ? 0.9049 0.7152 0.7747 -0.0006 -0.0178 0.0658  342 HIS B NE2 
3677  N N   . PRO B 42  ? 0.7767 0.6904 0.6732 0.0424  -0.0185 0.0689  343 PRO B N   
3678  C CA  . PRO B 42  ? 0.7850 0.7115 0.6770 0.0537  -0.0206 0.0724  343 PRO B CA  
3679  C C   . PRO B 42  ? 0.8089 0.7412 0.6981 0.0703  -0.0219 0.0713  343 PRO B C   
3680  O O   . PRO B 42  ? 0.8060 0.7339 0.6829 0.0838  -0.0243 0.0763  343 PRO B O   
3681  C CB  . PRO B 42  ? 0.6797 0.6375 0.5865 0.0461  -0.0198 0.0687  343 PRO B CB  
3682  C CG  . PRO B 42  ? 0.7228 0.6859 0.6424 0.0357  -0.0170 0.0620  343 PRO B CG  
3683  C CD  . PRO B 42  ? 0.8016 0.7367 0.7146 0.0318  -0.0162 0.0632  343 PRO B CD  
3684  N N   . SER B 43  ? 0.8227 0.7645 0.7215 0.0708  -0.0201 0.0652  344 SER B N   
3685  C CA  . SER B 43  ? 0.7859 0.7424 0.6852 0.0861  -0.0206 0.0632  344 SER B CA  
3686  C C   . SER B 43  ? 0.7944 0.7269 0.6849 0.0924  -0.0198 0.0617  344 SER B C   
3687  O O   . SER B 43  ? 0.7415 0.6565 0.6327 0.0815  -0.0183 0.0596  344 SER B O   
3688  C CB  . SER B 43  ? 0.7140 0.7091 0.6325 0.0809  -0.0188 0.0571  344 SER B CB  
3689  O OG  . SER B 43  ? 0.6931 0.7136 0.6135 0.0956  -0.0198 0.0562  344 SER B OG  
3690  N N   . GLN B 44  ? 0.8977 0.8306 0.7792 0.1112  -0.0211 0.0624  345 GLN B N   
3691  C CA  . GLN B 44  ? 0.9619 0.8801 0.8366 0.1200  -0.0200 0.0592  345 GLN B CA  
3692  C C   . GLN B 44  ? 0.9944 0.9490 0.8813 0.1295  -0.0183 0.0544  345 GLN B C   
3693  O O   . GLN B 44  ? 0.9613 0.9092 0.8414 0.1414  -0.0174 0.0519  345 GLN B O   
3694  C CB  . GLN B 44  ? 0.9560 0.8375 0.8054 0.1356  -0.0224 0.0636  345 GLN B CB  
3695  C CG  . GLN B 44  ? 1.0059 0.8509 0.8412 0.1249  -0.0239 0.0689  345 GLN B CG  
3696  C CD  . GLN B 44  ? 1.1024 0.9137 0.9108 0.1410  -0.0265 0.0749  345 GLN B CD  
3697  O OE1 . GLN B 44  ? 1.1852 0.9971 0.9866 0.1458  -0.0284 0.0813  345 GLN B OE1 
3698  N NE2 . GLN B 44  ? 1.0776 0.8576 0.8688 0.1501  -0.0267 0.0729  345 GLN B NE2 
3699  N N   . HIS B 45  ? 1.0370 1.0306 0.9409 0.1238  -0.0177 0.0529  346 HIS B N   
3700  C CA  . HIS B 45  ? 1.0363 1.0699 0.9540 0.1282  -0.0156 0.0483  346 HIS B CA  
3701  C C   . HIS B 45  ? 1.0284 1.0607 0.9536 0.1183  -0.0116 0.0433  346 HIS B C   
3702  O O   . HIS B 45  ? 1.0204 1.0533 0.9553 0.0998  -0.0097 0.0414  346 HIS B O   
3703  C CB  . HIS B 45  ? 0.9751 1.0466 0.9082 0.1186  -0.0160 0.0473  346 HIS B CB  
3704  C CG  . HIS B 45  ? 0.9778 1.0950 0.9232 0.1247  -0.0149 0.0436  346 HIS B CG  
3705  N ND1 . HIS B 45  ? 0.9585 1.1112 0.9204 0.1099  -0.0136 0.0399  346 HIS B ND1 
3706  C CD2 . HIS B 45  ? 0.9774 1.1121 0.9202 0.1435  -0.0147 0.0428  346 HIS B CD2 
3707  C CE1 . HIS B 45  ? 0.9367 1.1287 0.9068 0.1176  -0.0127 0.0373  346 HIS B CE1 
3708  N NE2 . HIS B 45  ? 0.9372 1.1210 0.8967 0.1390  -0.0132 0.0390  346 HIS B NE2 
3709  N N   . ALA B 46  ? 1.0681 1.0975 0.9871 0.1315  -0.0103 0.0412  347 ALA B N   
3710  C CA  . ALA B 46  ? 1.0035 1.0339 0.9279 0.1246  -0.0063 0.0368  347 ALA B CA  
3711  C C   . ALA B 46  ? 0.9711 1.0466 0.9090 0.1279  -0.0032 0.0335  347 ALA B C   
3712  O O   . ALA B 46  ? 0.9251 1.0291 0.8654 0.1405  -0.0046 0.0341  347 ALA B O   
3713  C CB  . ALA B 46  ? 0.9753 0.9709 0.8824 0.1358  -0.0067 0.0361  347 ALA B CB  
3714  N N   . ARG B 47  ? 1.0687 1.1521 1.0150 0.1159  0.0010  0.0301  348 ARG B N   
3715  C CA  . ARG B 47  ? 1.1470 1.2733 1.1058 0.1157  0.0048  0.0272  348 ARG B CA  
3716  C C   . ARG B 47  ? 1.1708 1.3049 1.1226 0.1359  0.0064  0.0254  348 ARG B C   
3717  O O   . ARG B 47  ? 1.1522 1.3279 1.1134 0.1403  0.0091  0.0235  348 ARG B O   
3718  C CB  . ARG B 47  ? 1.1420 1.2727 1.1108 0.0941  0.0092  0.0251  348 ARG B CB  
3719  C CG  . ARG B 47  ? 1.0988 1.2259 1.0745 0.0751  0.0083  0.0258  348 ARG B CG  
3720  C CD  . ARG B 47  ? 1.1810 1.3273 1.1675 0.0561  0.0129  0.0234  348 ARG B CD  
3721  N NE  . ARG B 47  ? 1.3147 1.5050 1.3105 0.0580  0.0156  0.0214  348 ARG B NE  
3722  C CZ  . ARG B 47  ? 1.3713 1.5887 1.3775 0.0409  0.0186  0.0194  348 ARG B CZ  
3723  N NH1 . ARG B 47  ? 1.3819 1.5833 1.3889 0.0224  0.0192  0.0190  348 ARG B NH1 
3724  N NH2 . ARG B 47  ? 1.4148 1.6756 1.4297 0.0423  0.0210  0.0176  348 ARG B NH2 
3725  N N   . ARG B 48  ? 1.1481 1.2443 1.0826 0.1482  0.0047  0.0257  349 ARG B N   
3726  C CA  . ARG B 48  ? 1.1092 1.2069 1.0336 0.1687  0.0062  0.0233  349 ARG B CA  
3727  C C   . ARG B 48  ? 1.1163 1.1732 1.0184 0.1869  0.0018  0.0249  349 ARG B C   
3728  O O   . ARG B 48  ? 1.1314 1.1493 1.0247 0.1780  -0.0010 0.0271  349 ARG B O   
3729  C CB  . ARG B 48  ? 1.0766 1.1665 1.0009 0.1607  0.0105  0.0199  349 ARG B CB  
3730  C CG  . ARG B 48  ? 1.0241 1.0801 0.9472 0.1409  0.0098  0.0207  349 ARG B CG  
3731  C CD  . ARG B 48  ? 1.0257 1.0606 0.9397 0.1410  0.0119  0.0177  349 ARG B CD  
3732  N NE  . ARG B 48  ? 1.0307 1.0528 0.9281 0.1636  0.0109  0.0153  349 ARG B NE  
3733  C CZ  . ARG B 48  ? 1.1224 1.1666 1.0189 0.1760  0.0147  0.0121  349 ARG B CZ  
3734  N NH1 . ARG B 48  ? 1.1296 1.2103 1.0415 0.1659  0.0199  0.0114  349 ARG B NH1 
3735  N NH2 . ARG B 48  ? 1.2137 1.2426 1.0926 0.1984  0.0135  0.0094  349 ARG B NH2 
3736  N N   . PRO B 49  ? 1.1956 1.2597 1.0869 0.2122  0.0013  0.0240  350 PRO B N   
3737  C CA  . PRO B 49  ? 1.3431 1.3628 1.2090 0.2305  -0.0027 0.0257  350 PRO B CA  
3738  C C   . PRO B 49  ? 1.5286 1.4984 1.3775 0.2259  -0.0030 0.0233  350 PRO B C   
3739  O O   . PRO B 49  ? 1.4775 1.4458 1.3351 0.2077  -0.0005 0.0209  350 PRO B O   
3740  C CB  . PRO B 49  ? 1.3315 1.3756 1.1905 0.2599  -0.0021 0.0240  350 PRO B CB  
3741  C CG  . PRO B 49  ? 1.3011 1.3994 1.1816 0.2546  0.0031  0.0204  350 PRO B CG  
3742  C CD  . PRO B 49  ? 1.2357 1.3519 1.1376 0.2255  0.0041  0.0220  350 PRO B CD  
3743  N N   . GLU B 50  ? 1.8383 1.7665 1.6613 0.2428  -0.0061 0.0238  351 GLU B N   
3744  C CA  . GLU B 50  ? 1.8718 1.7464 1.6755 0.2361  -0.0077 0.0221  351 GLU B CA  
3745  C C   . GLU B 50  ? 1.7541 1.6289 1.5586 0.2321  -0.0044 0.0156  351 GLU B C   
3746  O O   . GLU B 50  ? 1.7426 1.6164 1.5581 0.2101  -0.0033 0.0147  351 GLU B O   
3747  C CB  . GLU B 50  ? 2.0029 1.8335 1.7754 0.2576  -0.0112 0.0232  351 GLU B CB  
3748  C CG  . GLU B 50  ? 2.0473 1.8690 1.8140 0.2617  -0.0148 0.0306  351 GLU B CG  
3749  C CD  . GLU B 50  ? 2.0901 1.8485 1.8266 0.2623  -0.0185 0.0333  351 GLU B CD  
3750  O OE1 . GLU B 50  ? 2.1001 1.8215 1.8188 0.2617  -0.0185 0.0285  351 GLU B OE1 
3751  O OE2 . GLU B 50  ? 2.0967 1.8420 1.8262 0.2624  -0.0213 0.0402  351 GLU B OE2 
3752  N N   . ASP B 51  ? 1.6533 1.5290 1.4448 0.2543  -0.0028 0.0110  352 ASP B N   
3753  C CA  . ASP B 51  ? 1.5853 1.4571 1.3734 0.2525  0.0001  0.0046  352 ASP B CA  
3754  C C   . ASP B 51  ? 1.5233 1.4512 1.3337 0.2521  0.0057  0.0028  352 ASP B C   
3755  O O   . ASP B 51  ? 1.3913 1.3566 1.2247 0.2399  0.0072  0.0064  352 ASP B O   
3756  C CB  . ASP B 51  ? 1.6007 1.4359 1.3584 0.2760  -0.0011 -0.0002 352 ASP B CB  
3757  C CG  . ASP B 51  ? 1.6209 1.3936 1.3545 0.2682  -0.0058 -0.0004 352 ASP B CG  
3758  O OD1 . ASP B 51  ? 1.5363 1.2963 1.2764 0.2437  -0.0067 -0.0005 352 ASP B OD1 
3759  O OD2 . ASP B 51  ? 1.6998 1.4364 1.4069 0.2867  -0.0086 -0.0003 352 ASP B OD2 
3760  N N   . VAL B 52  ? 1.6302 1.5637 1.4328 0.2646  0.0090  -0.0029 353 VAL B N   
3761  C CA  . VAL B 52  ? 1.6215 1.6061 1.4429 0.2624  0.0151  -0.0046 353 VAL B CA  
3762  C C   . VAL B 52  ? 1.6473 1.6817 1.4829 0.2747  0.0167  -0.0020 353 VAL B C   
3763  O O   . VAL B 52  ? 1.7041 1.7428 1.5273 0.3016  0.0160  -0.0034 353 VAL B O   
3764  C CB  . VAL B 52  ? 1.5649 1.5438 1.3719 0.2757  0.0182  -0.0114 353 VAL B CB  
3765  C CG1 . VAL B 52  ? 1.6421 1.5938 1.4220 0.3058  0.0158  -0.0150 353 VAL B CG1 
3766  C CG2 . VAL B 52  ? 1.4717 1.5075 1.2973 0.2753  0.0251  -0.0123 353 VAL B CG2 
3767  N N   . ALA B 53  ? 1.4224 1.4942 1.2829 0.2553  0.0187  0.0015  354 ALA B N   
3768  C CA  . ALA B 53  ? 1.1562 1.2775 1.0325 0.2615  0.0195  0.0040  354 ALA B CA  
3769  C C   . ALA B 53  ? 0.9808 1.1525 0.8645 0.2744  0.0253  0.0006  354 ALA B C   
3770  O O   . ALA B 53  ? 0.8627 1.0387 0.7463 0.2696  0.0300  -0.0025 354 ALA B O   
3771  C CB  . ALA B 53  ? 1.0690 1.2103 0.9675 0.2339  0.0197  0.0079  354 ALA B CB  
3772  N N   . THR B 54  ? 0.8565 1.0691 0.7467 0.2912  0.0251  0.0015  355 THR B N   
3773  C CA  . THR B 54  ? 0.8434 1.1137 0.7441 0.3017  0.0309  -0.0013 355 THR B CA  
3774  C C   . THR B 54  ? 0.7784 1.0934 0.7054 0.2725  0.0356  0.0003  355 THR B C   
3775  O O   . THR B 54  ? 0.7080 1.0117 0.6450 0.2478  0.0338  0.0035  355 THR B O   
3776  C CB  . THR B 54  ? 0.8096 1.1132 0.7086 0.3303  0.0288  -0.0010 355 THR B CB  
3777  O OG1 . THR B 54  ? 0.7221 1.0414 0.6343 0.3198  0.0248  0.0036  355 THR B OG1 
3778  C CG2 . THR B 54  ? 0.7786 1.0335 0.6473 0.3610  0.0247  -0.0026 355 THR B CG2 
3779  N N   . LYS B 55  ? 0.6998 1.0663 0.6369 0.2759  0.0421  -0.0020 356 LYS B N   
3780  C CA  . LYS B 55  ? 0.6976 1.1030 0.6563 0.2469  0.0476  -0.0006 356 LYS B CA  
3781  C C   . LYS B 55  ? 0.6743 1.1085 0.6511 0.2308  0.0449  0.0025  356 LYS B C   
3782  O O   . LYS B 55  ? 0.4414 0.8739 0.4295 0.2011  0.0463  0.0045  356 LYS B O   
3783  C CB  . LYS B 55  ? 0.7805 1.2412 0.7463 0.2546  0.0551  -0.0033 356 LYS B CB  
3784  C CG  . LYS B 55  ? 0.7747 1.2705 0.7593 0.2228  0.0615  -0.0014 356 LYS B CG  
3785  C CD  . LYS B 55  ? 0.7871 1.3420 0.7789 0.2301  0.0694  -0.0036 356 LYS B CD  
3786  C CE  . LYS B 55  ? 0.7884 1.3730 0.7960 0.1961  0.0762  -0.0010 356 LYS B CE  
3787  N NZ  . LYS B 55  ? 0.7580 1.4012 0.7722 0.2007  0.0847  -0.0026 356 LYS B NZ  
3788  N N   . ASP B 56  ? 0.6127 1.0732 0.5911 0.2508  0.0411  0.0027  357 ASP B N   
3789  C CA  . ASP B 56  ? 0.6432 1.1336 0.6379 0.2373  0.0380  0.0050  357 ASP B CA  
3790  C C   . ASP B 56  ? 0.6288 1.0678 0.6187 0.2221  0.0324  0.0081  357 ASP B C   
3791  O O   . ASP B 56  ? 0.6237 1.0811 0.6267 0.2049  0.0303  0.0097  357 ASP B O   
3792  C CB  . ASP B 56  ? 0.6929 1.2241 0.6885 0.2655  0.0346  0.0047  357 ASP B CB  
3793  C CG  . ASP B 56  ? 0.8348 1.3177 0.8066 0.2956  0.0284  0.0058  357 ASP B CG  
3794  O OD1 . ASP B 56  ? 0.9511 1.3702 0.9061 0.2938  0.0267  0.0063  357 ASP B OD1 
3795  O OD2 . ASP B 56  ? 0.8912 1.4005 0.8603 0.3213  0.0251  0.0063  357 ASP B OD2 
3796  N N   . GLN B 57  ? 0.6022 0.9792 0.5734 0.2279  0.0300  0.0085  358 GLN B N   
3797  C CA  . GLN B 57  ? 0.6470 0.9742 0.6127 0.2137  0.0252  0.0114  358 GLN B CA  
3798  C C   . GLN B 57  ? 0.6145 0.9208 0.5852 0.1849  0.0286  0.0115  358 GLN B C   
3799  O O   . GLN B 57  ? 0.5462 0.8451 0.5250 0.1635  0.0270  0.0135  358 GLN B O   
3800  C CB  . GLN B 57  ? 0.7295 1.0021 0.6711 0.2350  0.0206  0.0119  358 GLN B CB  
3801  C CG  . GLN B 57  ? 0.8966 1.1767 0.8301 0.2607  0.0156  0.0137  358 GLN B CG  
3802  C CD  . GLN B 57  ? 0.9747 1.2051 0.8808 0.2860  0.0126  0.0133  358 GLN B CD  
3803  O OE1 . GLN B 57  ? 0.9621 1.1500 0.8555 0.2821  0.0136  0.0114  358 GLN B OE1 
3804  N NE2 . GLN B 57  ? 1.0080 1.2426 0.9032 0.3123  0.0089  0.0151  358 GLN B NE2 
3805  N N   . LEU B 58  ? 0.5669 0.8636 0.5318 0.1851  0.0331  0.0094  359 LEU B N   
3806  C CA  . LEU B 58  ? 0.5754 0.8486 0.5423 0.1603  0.0358  0.0102  359 LEU B CA  
3807  C C   . LEU B 58  ? 0.5121 0.8266 0.4967 0.1373  0.0413  0.0107  359 LEU B C   
3808  O O   . LEU B 58  ? 0.4843 0.7854 0.4744 0.1141  0.0413  0.0126  359 LEU B O   
3809  C CB  . LEU B 58  ? 0.5329 0.7781 0.4854 0.1680  0.0382  0.0079  359 LEU B CB  
3810  C CG  . LEU B 58  ? 0.5150 0.7350 0.4680 0.1444  0.0404  0.0092  359 LEU B CG  
3811  C CD1 . LEU B 58  ? 0.4257 0.6101 0.3778 0.1323  0.0351  0.0117  359 LEU B CD1 
3812  C CD2 . LEU B 58  ? 0.5079 0.7017 0.4460 0.1515  0.0424  0.0068  359 LEU B CD2 
3813  N N   . PHE B 59  ? 0.5557 0.9203 0.5483 0.1430  0.0463  0.0091  360 PHE B N   
3814  C CA  . PHE B 59  ? 0.5106 0.9119 0.5177 0.1185  0.0524  0.0098  360 PHE B CA  
3815  C C   . PHE B 59  ? 0.5130 0.9240 0.5320 0.0966  0.0502  0.0112  360 PHE B C   
3816  O O   . PHE B 59  ? 0.4817 0.8842 0.5041 0.0710  0.0535  0.0125  360 PHE B O   
3817  C CB  . PHE B 59  ? 0.4060 0.8683 0.4219 0.1276  0.0578  0.0079  360 PHE B CB  
3818  C CG  . PHE B 59  ? 0.6082 1.1054 0.6368 0.0997  0.0648  0.0089  360 PHE B CG  
3819  C CD1 . PHE B 59  ? 0.6105 1.0986 0.6337 0.0896  0.0716  0.0100  360 PHE B CD1 
3820  C CD2 . PHE B 59  ? 0.4813 1.0166 0.5251 0.0819  0.0647  0.0090  360 PHE B CD2 
3821  C CE1 . PHE B 59  ? 0.6138 1.1288 0.6456 0.0627  0.0784  0.0117  360 PHE B CE1 
3822  C CE2 . PHE B 59  ? 0.5369 1.0992 0.5898 0.0539  0.0712  0.0099  360 PHE B CE2 
3823  C CZ  . PHE B 59  ? 0.6178 1.1688 0.6642 0.0441  0.0783  0.0116  360 PHE B CZ  
3824  N N   . PRO B 60  ? 0.5200 0.9490 0.5444 0.1053  0.0449  0.0108  361 PRO B N   
3825  C CA  . PRO B 60  ? 0.5279 0.9669 0.5629 0.0831  0.0428  0.0113  361 PRO B CA  
3826  C C   . PRO B 60  ? 0.4845 0.8707 0.5130 0.0658  0.0409  0.0130  361 PRO B C   
3827  O O   . PRO B 60  ? 0.4584 0.8476 0.4931 0.0406  0.0429  0.0130  361 PRO B O   
3828  C CB  . PRO B 60  ? 0.3792 0.8373 0.4164 0.1020  0.0363  0.0111  361 PRO B CB  
3829  C CG  . PRO B 60  ? 0.4775 0.9616 0.5113 0.1304  0.0375  0.0099  361 PRO B CG  
3830  C CD  . PRO B 60  ? 0.4850 0.9320 0.5060 0.1357  0.0411  0.0098  361 PRO B CD  
3831  N N   . LEU B 61  ? 0.5479 0.8859 0.5631 0.0786  0.0372  0.0143  362 LEU B N   
3832  C CA  . LEU B 61  ? 0.5329 0.8233 0.5418 0.0638  0.0359  0.0158  362 LEU B CA  
3833  C C   . LEU B 61  ? 0.6072 0.8892 0.6149 0.0465  0.0422  0.0163  362 LEU B C   
3834  O O   . LEU B 61  ? 0.6415 0.9079 0.6502 0.0258  0.0433  0.0172  362 LEU B O   
3835  C CB  . LEU B 61  ? 0.4643 0.7100 0.4590 0.0809  0.0312  0.0168  362 LEU B CB  
3836  C CG  . LEU B 61  ? 0.5339 0.7801 0.5245 0.1014  0.0253  0.0174  362 LEU B CG  
3837  C CD1 . LEU B 61  ? 0.5264 0.7276 0.5001 0.1173  0.0221  0.0180  362 LEU B CD1 
3838  C CD2 . LEU B 61  ? 0.5309 0.7765 0.5272 0.0905  0.0213  0.0187  362 LEU B CD2 
3839  N N   . ALA B 62  ? 0.6012 0.8919 0.6050 0.0557  0.0464  0.0158  363 ALA B N   
3840  C CA  . ALA B 62  ? 0.5669 0.8512 0.5680 0.0404  0.0528  0.0169  363 ALA B CA  
3841  C C   . ALA B 62  ? 0.5260 0.8413 0.5375 0.0164  0.0576  0.0174  363 ALA B C   
3842  O O   . ALA B 62  ? 0.4854 0.7788 0.4936 -0.0038 0.0600  0.0192  363 ALA B O   
3843  C CB  . ALA B 62  ? 0.5211 0.8170 0.5166 0.0560  0.0568  0.0160  363 ALA B CB  
3844  N N   . LYS B 63  ? 0.4841 0.8508 0.5072 0.0182  0.0590  0.0157  364 LYS B N   
3845  C CA  . LYS B 63  ? 0.5046 0.9046 0.5374 -0.0067 0.0636  0.0156  364 LYS B CA  
3846  C C   . LYS B 63  ? 0.5027 0.8782 0.5354 -0.0264 0.0606  0.0156  364 LYS B C   
3847  O O   . LYS B 63  ? 0.5693 0.9416 0.6011 -0.0511 0.0649  0.0163  364 LYS B O   
3848  C CB  . LYS B 63  ? 0.5300 0.9922 0.5765 -0.0001 0.0638  0.0131  364 LYS B CB  
3849  C CG  . LYS B 63  ? 0.6438 1.1468 0.7008 -0.0280 0.0690  0.0124  364 LYS B CG  
3850  C CD  . LYS B 63  ? 0.7007 1.2559 0.7721 -0.0270 0.0655  0.0093  364 LYS B CD  
3851  C CE  . LYS B 63  ? 0.6408 1.2415 0.7226 -0.0562 0.0709  0.0079  364 LYS B CE  
3852  N NZ  . LYS B 63  ? 0.6199 1.1878 0.6966 -0.0867 0.0714  0.0080  364 LYS B NZ  
3853  N N   . GLU B 64  ? 0.4565 0.8119 0.4881 -0.0156 0.0533  0.0149  365 GLU B N   
3854  C CA  . GLU B 64  ? 0.5372 0.8719 0.5685 -0.0318 0.0501  0.0143  365 GLU B CA  
3855  C C   . GLU B 64  ? 0.4859 0.7701 0.5053 -0.0432 0.0519  0.0164  365 GLU B C   
3856  O O   . GLU B 64  ? 0.4368 0.7102 0.4542 -0.0649 0.0539  0.0161  365 GLU B O   
3857  C CB  . GLU B 64  ? 0.5637 0.8916 0.5959 -0.0153 0.0423  0.0136  365 GLU B CB  
3858  C CG  . GLU B 64  ? 0.7589 1.0790 0.7929 -0.0301 0.0388  0.0121  365 GLU B CG  
3859  C CD  . GLU B 64  ? 0.9760 1.2497 1.0012 -0.0227 0.0339  0.0136  365 GLU B CD  
3860  O OE1 . GLU B 64  ? 1.0422 1.2791 1.0594 -0.0325 0.0357  0.0147  365 GLU B OE1 
3861  O OE2 . GLU B 64  ? 1.0199 1.2948 1.0453 -0.0066 0.0284  0.0141  365 GLU B OE2 
3862  N N   . PHE B 65  ? 0.4782 0.7304 0.4886 -0.0285 0.0509  0.0184  366 PHE B N   
3863  C CA  . PHE B 65  ? 0.5335 0.7414 0.5327 -0.0371 0.0523  0.0205  366 PHE B CA  
3864  C C   . PHE B 65  ? 0.5967 0.8083 0.5922 -0.0551 0.0598  0.0223  366 PHE B C   
3865  O O   . PHE B 65  ? 0.6167 0.8029 0.6051 -0.0716 0.0616  0.0234  366 PHE B O   
3866  C CB  . PHE B 65  ? 0.5214 0.7007 0.5122 -0.0185 0.0497  0.0218  366 PHE B CB  
3867  C CG  . PHE B 65  ? 0.6494 0.7910 0.6290 -0.0254 0.0517  0.0242  366 PHE B CG  
3868  C CD1 . PHE B 65  ? 0.6251 0.7377 0.6006 -0.0348 0.0494  0.0247  366 PHE B CD1 
3869  C CD2 . PHE B 65  ? 0.6919 0.8290 0.6645 -0.0215 0.0557  0.0258  366 PHE B CD2 
3870  C CE1 . PHE B 65  ? 0.6298 0.7099 0.5944 -0.0392 0.0510  0.0271  366 PHE B CE1 
3871  C CE2 . PHE B 65  ? 0.6735 0.7776 0.6351 -0.0266 0.0571  0.0284  366 PHE B CE2 
3872  C CZ  . PHE B 65  ? 0.6082 0.6842 0.5659 -0.0350 0.0547  0.0291  366 PHE B CZ  
3873  N N   . ILE B 66  ? 0.5765 0.8189 0.5751 -0.0516 0.0647  0.0227  367 ILE B N   
3874  C CA  . ILE B 66  ? 0.5749 0.8230 0.5690 -0.0691 0.0726  0.0252  367 ILE B CA  
3875  C C   . ILE B 66  ? 0.5565 0.8212 0.5550 -0.0945 0.0751  0.0242  367 ILE B C   
3876  O O   . ILE B 66  ? 0.4926 0.7344 0.4813 -0.1140 0.0794  0.0264  367 ILE B O   
3877  C CB  . ILE B 66  ? 0.5436 0.8273 0.5411 -0.0587 0.0773  0.0256  367 ILE B CB  
3878  C CG1 . ILE B 66  ? 0.4943 0.7581 0.4850 -0.0336 0.0743  0.0255  367 ILE B CG1 
3879  C CG2 . ILE B 66  ? 0.5129 0.8053 0.5053 -0.0782 0.0862  0.0289  367 ILE B CG2 
3880  C CD1 . ILE B 66  ? 0.4967 0.7206 0.4726 -0.0353 0.0766  0.0289  367 ILE B CD1 
3881  N N   . ASP B 67  ? 0.5764 0.8796 0.5881 -0.0946 0.0723  0.0206  368 ASP B N   
3882  C CA  . ASP B 67  ? 0.6186 0.9366 0.6344 -0.1190 0.0732  0.0182  368 ASP B CA  
3883  C C   . ASP B 67  ? 0.5325 0.8014 0.5373 -0.1298 0.0705  0.0181  368 ASP B C   
3884  O O   . ASP B 67  ? 0.5104 0.7628 0.5063 -0.1528 0.0747  0.0186  368 ASP B O   
3885  C CB  . ASP B 67  ? 0.6083 0.9726 0.6395 -0.1126 0.0685  0.0141  368 ASP B CB  
3886  C CG  . ASP B 67  ? 0.6632 1.0860 0.7060 -0.1083 0.0723  0.0136  368 ASP B CG  
3887  O OD1 . ASP B 67  ? 0.5879 1.0169 0.6271 -0.1134 0.0793  0.0163  368 ASP B OD1 
3888  O OD2 . ASP B 67  ? 0.7111 1.1754 0.7662 -0.0989 0.0684  0.0106  368 ASP B OD2 
3889  N N   . GLN B 68  ? 0.5012 0.7452 0.5049 -0.1131 0.0638  0.0174  369 GLN B N   
3890  C CA  . GLN B 68  ? 0.5203 0.7186 0.5134 -0.1193 0.0613  0.0172  369 GLN B CA  
3891  C C   . GLN B 68  ? 0.6161 0.7755 0.5935 -0.1277 0.0664  0.0211  369 GLN B C   
3892  O O   . GLN B 68  ? 0.6047 0.7397 0.5717 -0.1454 0.0686  0.0208  369 GLN B O   
3893  C CB  . GLN B 68  ? 0.5242 0.7048 0.5184 -0.0977 0.0542  0.0170  369 GLN B CB  
3894  C CG  . GLN B 68  ? 0.6326 0.7693 0.6168 -0.1004 0.0514  0.0169  369 GLN B CG  
3895  C CD  . GLN B 68  ? 0.8029 0.9261 0.7888 -0.0804 0.0450  0.0173  369 GLN B CD  
3896  O OE1 . GLN B 68  ? 0.7751 0.8632 0.7526 -0.0758 0.0435  0.0188  369 GLN B OE1 
3897  N NE2 . GLN B 68  ? 0.8867 1.0384 0.8826 -0.0683 0.0412  0.0161  369 GLN B NE2 
3898  N N   . TYR B 69  ? 0.6493 0.8015 0.6229 -0.1145 0.0684  0.0247  370 TYR B N   
3899  C CA  . TYR B 69  ? 0.6332 0.7477 0.5908 -0.1193 0.0725  0.0290  370 TYR B CA  
3900  C C   . TYR B 69  ? 0.5786 0.6976 0.5289 -0.1428 0.0803  0.0311  370 TYR B C   
3901  O O   . TYR B 69  ? 0.6299 0.7120 0.5643 -0.1548 0.0830  0.0334  370 TYR B O   
3902  C CB  . TYR B 69  ? 0.4750 0.5842 0.4298 -0.1005 0.0727  0.0319  370 TYR B CB  
3903  C CG  . TYR B 69  ? 0.5091 0.5902 0.4479 -0.1071 0.0782  0.0368  370 TYR B CG  
3904  C CD1 . TYR B 69  ? 0.5266 0.5637 0.4518 -0.1070 0.0766  0.0388  370 TYR B CD1 
3905  C CD2 . TYR B 69  ? 0.5145 0.6144 0.4506 -0.1133 0.0852  0.0399  370 TYR B CD2 
3906  C CE1 . TYR B 69  ? 0.5421 0.5528 0.4507 -0.1118 0.0815  0.0439  370 TYR B CE1 
3907  C CE2 . TYR B 69  ? 0.5694 0.6426 0.4889 -0.1193 0.0904  0.0452  370 TYR B CE2 
3908  C CZ  . TYR B 69  ? 0.6107 0.6385 0.5160 -0.1181 0.0883  0.0474  370 TYR B CZ  
3909  O OH  . TYR B 69  ? 0.7358 0.7369 0.6229 -0.1226 0.0933  0.0533  370 TYR B OH  
3910  N N   . TYR B 70  ? 0.5325 0.6957 0.4925 -0.1495 0.0844  0.0306  371 TYR B N   
3911  C CA  . TYR B 70  ? 0.5693 0.7371 0.5215 -0.1749 0.0922  0.0329  371 TYR B CA  
3912  C C   . TYR B 70  ? 0.6118 0.7726 0.5615 -0.1971 0.0915  0.0292  371 TYR B C   
3913  O O   . TYR B 70  ? 0.5677 0.7022 0.5016 -0.2181 0.0966  0.0314  371 TYR B O   
3914  C CB  . TYR B 70  ? 0.6308 0.8519 0.5945 -0.1772 0.0973  0.0334  371 TYR B CB  
3915  C CG  . TYR B 70  ? 0.6840 0.8987 0.6399 -0.1666 0.1021  0.0387  371 TYR B CG  
3916  C CD1 . TYR B 70  ? 0.6425 0.8394 0.5827 -0.1840 0.1101  0.0442  371 TYR B CD1 
3917  C CD2 . TYR B 70  ? 0.6974 0.9203 0.6591 -0.1395 0.0986  0.0381  371 TYR B CD2 
3918  C CE1 . TYR B 70  ? 0.6029 0.7941 0.5347 -0.1741 0.1143  0.0492  371 TYR B CE1 
3919  C CE2 . TYR B 70  ? 0.7117 0.9282 0.6649 -0.1299 0.1027  0.0421  371 TYR B CE2 
3920  C CZ  . TYR B 70  ? 0.6746 0.8766 0.6134 -0.1470 0.1105  0.0477  371 TYR B CZ  
3921  O OH  . TYR B 70  ? 0.6107 0.8074 0.5402 -0.1371 0.1145  0.0518  371 TYR B OH  
3922  N N   . SER B 71  ? 0.6645 0.8441 0.6270 -0.1923 0.0849  0.0237  372 SER B N   
3923  C CA  . SER B 71  ? 0.6948 0.8621 0.6528 -0.2110 0.0831  0.0193  372 SER B CA  
3924  C C   . SER B 71  ? 0.5837 0.6895 0.5218 -0.2116 0.0823  0.0207  372 SER B C   
3925  O O   . SER B 71  ? 0.6177 0.6983 0.5414 -0.2328 0.0852  0.0196  372 SER B O   
3926  C CB  . SER B 71  ? 0.7592 0.9563 0.7335 -0.2016 0.0756  0.0136  372 SER B CB  
3927  O OG  . SER B 71  ? 0.8504 1.1069 0.8415 -0.2043 0.0766  0.0117  372 SER B OG  
3928  N N   . SER B 72  ? 0.5201 0.6010 0.4559 -0.1886 0.0788  0.0231  373 SER B N   
3929  C CA  . SER B 72  ? 0.6033 0.6304 0.5212 -0.1858 0.0778  0.0246  373 SER B CA  
3930  C C   . SER B 72  ? 0.6980 0.6931 0.5949 -0.2022 0.0851  0.0291  373 SER B C   
3931  O O   . SER B 72  ? 0.7396 0.6945 0.6189 -0.2112 0.0857  0.0284  373 SER B O   
3932  C CB  . SER B 72  ? 0.6244 0.6374 0.5441 -0.1596 0.0737  0.0273  373 SER B CB  
3933  O OG  . SER B 72  ? 0.7428 0.7432 0.6530 -0.1561 0.0784  0.0331  373 SER B OG  
3934  N N   . ILE B 73  ? 0.5811 0.5921 0.4775 -0.2058 0.0910  0.0339  374 ILE B N   
3935  C CA  . ILE B 73  ? 0.6020 0.5809 0.4765 -0.2190 0.0982  0.0399  374 ILE B CA  
3936  C C   . ILE B 73  ? 0.6229 0.6184 0.4936 -0.2494 0.1049  0.0395  374 ILE B C   
3937  O O   . ILE B 73  ? 0.7846 0.7673 0.6404 -0.2621 0.1123  0.0454  374 ILE B O   
3938  C CB  . ILE B 73  ? 0.6941 0.6738 0.5664 -0.2037 0.1010  0.0463  374 ILE B CB  
3939  C CG1 . ILE B 73  ? 0.6468 0.6825 0.5381 -0.2020 0.1031  0.0459  374 ILE B CG1 
3940  C CG2 . ILE B 73  ? 0.6080 0.5661 0.4807 -0.1769 0.0944  0.0465  374 ILE B CG2 
3941  C CD1 . ILE B 73  ? 0.6515 0.6918 0.5414 -0.1856 0.1054  0.0509  374 ILE B CD1 
3942  N N   . LYS B 74  ? 0.6777 0.7017 0.5605 -0.2622 0.1023  0.0327  375 LYS B N   
3943  C CA  . LYS B 74  ? 0.8830 0.9225 0.7616 -0.2942 0.1079  0.0311  375 LYS B CA  
3944  C C   . LYS B 74  ? 0.8600 0.9396 0.7455 -0.3025 0.1150  0.0358  375 LYS B C   
3945  O O   . LYS B 74  ? 0.8486 0.9205 0.7200 -0.3277 0.1227  0.0393  375 LYS B O   
3946  C CB  . LYS B 74  ? 0.9984 0.9791 0.8472 -0.3142 0.1117  0.0324  375 LYS B CB  
3947  C CG  . LYS B 74  ? 0.9940 0.9251 0.8303 -0.3006 0.1060  0.0296  375 LYS B CG  
3948  C CD  . LYS B 74  ? 0.9732 0.9189 0.8194 -0.3061 0.0998  0.0203  375 LYS B CD  
3949  C CE  . LYS B 74  ? 0.9552 0.8692 0.7984 -0.2831 0.0929  0.0177  375 LYS B CE  
3950  N NZ  . LYS B 74  ? 0.8101 0.7510 0.6688 -0.2832 0.0863  0.0092  375 LYS B NZ  
3951  N N   . ARG B 75  ? 0.8025 0.9230 0.7082 -0.2807 0.1128  0.0361  376 ARG B N   
3952  C CA  . ARG B 75  ? 0.8706 1.0461 0.7894 -0.2869 0.1182  0.0378  376 ARG B CA  
3953  C C   . ARG B 75  ? 0.9860 1.2195 0.9297 -0.2852 0.1133  0.0306  376 ARG B C   
3954  O O   . ARG B 75  ? 1.0097 1.2534 0.9552 -0.3061 0.1121  0.0255  376 ARG B O   
3955  C CB  . ARG B 75  ? 0.7990 0.9800 0.7203 -0.2624 0.1196  0.0429  376 ARG B CB  
3956  C CG  . ARG B 75  ? 0.8460 0.9691 0.7433 -0.2584 0.1224  0.0496  376 ARG B CG  
3957  C CD  . ARG B 75  ? 1.0917 1.2107 0.9734 -0.2821 0.1326  0.0561  376 ARG B CD  
3958  N NE  . ARG B 75  ? 1.2085 1.2685 1.0635 -0.2995 0.1350  0.0591  376 ARG B NE  
3959  C CZ  . ARG B 75  ? 1.2385 1.2743 1.0715 -0.3179 0.1436  0.0665  376 ARG B CZ  
3960  N NH1 . ARG B 75  ? 1.2357 1.2131 1.0423 -0.3312 0.1452  0.0688  376 ARG B NH1 
3961  N NH2 . ARG B 75  ? 1.2202 1.2893 1.0563 -0.3224 0.1509  0.0716  376 ARG B NH2 
3962  N N   . PHE B 76  ? 0.9679 1.2361 0.9288 -0.2590 0.1100  0.0301  377 PHE B N   
3963  C CA  . PHE B 76  ? 0.8947 1.2224 0.8788 -0.2518 0.1058  0.0245  377 PHE B CA  
3964  C C   . PHE B 76  ? 0.8384 1.2221 0.8313 -0.2733 0.1128  0.0245  377 PHE B C   
3965  O O   . PHE B 76  ? 0.6980 1.0825 0.6847 -0.3047 0.1165  0.0233  377 PHE B O   
3966  C CB  . PHE B 76  ? 0.8692 1.1919 0.8580 -0.2548 0.0981  0.0180  377 PHE B CB  
3967  C CG  . PHE B 76  ? 0.8379 1.2237 0.8490 -0.2488 0.0939  0.0129  377 PHE B CG  
3968  C CD1 . PHE B 76  ? 0.7933 1.1963 0.8165 -0.2172 0.0879  0.0121  377 PHE B CD1 
3969  C CD2 . PHE B 76  ? 0.8838 1.3125 0.9024 -0.2748 0.0961  0.0090  377 PHE B CD2 
3970  C CE1 . PHE B 76  ? 0.8176 1.2784 0.8594 -0.2093 0.0840  0.0080  377 PHE B CE1 
3971  C CE2 . PHE B 76  ? 0.9167 1.4081 0.9560 -0.2678 0.0920  0.0044  377 PHE B CE2 
3972  C CZ  . PHE B 76  ? 0.8994 1.4063 0.9499 -0.2339 0.0860  0.0042  377 PHE B CZ  
3973  N N   . GLY B 77  ? 0.8451 1.2763 0.8517 -0.2567 0.1147  0.0256  378 GLY B N   
3974  C CA  . GLY B 77  ? 0.8280 1.3150 0.8426 -0.2739 0.1224  0.0266  378 GLY B CA  
3975  C C   . GLY B 77  ? 0.7933 1.2606 0.7919 -0.2875 0.1322  0.0339  378 GLY B C   
3976  O O   . GLY B 77  ? 0.8513 1.3670 0.8564 -0.2996 0.1396  0.0357  378 GLY B O   
3977  N N   . SER B 78  ? 0.7035 1.1032 0.6809 -0.2855 0.1327  0.0384  379 SER B N   
3978  C CA  . SER B 78  ? 0.6361 1.0125 0.5955 -0.2967 0.1418  0.0463  379 SER B CA  
3979  C C   . SER B 78  ? 0.6843 1.0966 0.6516 -0.2750 0.1454  0.0490  379 SER B C   
3980  O O   . SER B 78  ? 0.6319 1.0743 0.6154 -0.2476 0.1400  0.0450  379 SER B O   
3981  C CB  . SER B 78  ? 0.6371 0.9357 0.5728 -0.2921 0.1402  0.0504  379 SER B CB  
3982  O OG  . SER B 78  ? 0.5502 0.8323 0.4890 -0.2578 0.1339  0.0500  379 SER B OG  
3983  N N   . LYS B 79  ? 0.6854 1.0920 0.6391 -0.2870 0.1547  0.0561  380 LYS B N   
3984  C CA  . LYS B 79  ? 0.6704 1.1098 0.6292 -0.2671 0.1588  0.0586  380 LYS B CA  
3985  C C   . LYS B 79  ? 0.6699 1.0785 0.6268 -0.2307 0.1515  0.0574  380 LYS B C   
3986  O O   . LYS B 79  ? 0.6558 1.0996 0.6268 -0.2051 0.1485  0.0536  380 LYS B O   
3987  C CB  . LYS B 79  ? 0.6043 1.0354 0.5453 -0.2871 0.1702  0.0673  380 LYS B CB  
3988  C CG  . LYS B 79  ? 0.8261 1.3162 0.7781 -0.2785 0.1756  0.0679  380 LYS B CG  
3989  C CD  . LYS B 79  ? 0.8739 1.3649 0.8161 -0.3030 0.1814  0.0723  380 LYS B CD  
3990  C CE  . LYS B 79  ? 0.8947 1.4309 0.8528 -0.3220 0.1784  0.0662  380 LYS B CE  
3991  N NZ  . LYS B 79  ? 0.8332 1.4425 0.8161 -0.3032 0.1762  0.0604  380 LYS B NZ  
3992  N N   . ALA B 80  ? 0.6558 0.9986 0.5949 -0.2278 0.1482  0.0602  381 ALA B N   
3993  C CA  . ALA B 80  ? 0.5948 0.9083 0.5314 -0.1962 0.1414  0.0591  381 ALA B CA  
3994  C C   . ALA B 80  ? 0.6134 0.9421 0.5677 -0.1763 0.1316  0.0515  381 ALA B C   
3995  O O   . ALA B 80  ? 0.5383 0.8636 0.4956 -0.1486 0.1267  0.0494  381 ALA B O   
3996  C CB  . ALA B 80  ? 0.5882 0.8325 0.5030 -0.1986 0.1396  0.0635  381 ALA B CB  
3997  N N   . HIS B 81  ? 0.6300 0.9741 0.5946 -0.1904 0.1287  0.0474  382 HIS B N   
3998  C CA  . HIS B 81  ? 0.6468 1.0070 0.6272 -0.1718 0.1197  0.0408  382 HIS B CA  
3999  C C   . HIS B 81  ? 0.6840 1.1068 0.6816 -0.1560 0.1204  0.0377  382 HIS B C   
4000  O O   . HIS B 81  ? 0.5884 1.0151 0.5920 -0.1279 0.1145  0.0347  382 HIS B O   
4001  C CB  . HIS B 81  ? 0.6158 0.9742 0.6007 -0.1915 0.1162  0.0372  382 HIS B CB  
4002  C CG  . HIS B 81  ? 0.7491 1.1258 0.7492 -0.1741 0.1073  0.0312  382 HIS B CG  
4003  N ND1 . HIS B 81  ? 0.8112 1.2031 0.8194 -0.1885 0.1038  0.0268  382 HIS B ND1 
4004  C CD2 . HIS B 81  ? 0.8039 1.1838 0.8105 -0.1439 0.1012  0.0291  382 HIS B CD2 
4005  C CE1 . HIS B 81  ? 0.8152 1.2203 0.8347 -0.1670 0.0959  0.0228  382 HIS B CE1 
4006  N NE2 . HIS B 81  ? 0.7800 1.1767 0.7982 -0.1400 0.0944  0.0243  382 HIS B NE2 
4007  N N   . MET B 82  ? 0.7038 1.1759 0.7084 -0.1739 0.1278  0.0385  383 MET B N   
4008  C CA  . MET B 82  ? 0.6622 1.1997 0.6835 -0.1585 0.1290  0.0354  383 MET B CA  
4009  C C   . MET B 82  ? 0.6675 1.2041 0.6831 -0.1326 0.1314  0.0371  383 MET B C   
4010  O O   . MET B 82  ? 0.5799 1.1497 0.6053 -0.1066 0.1286  0.0332  383 MET B O   
4011  C CB  . MET B 82  ? 0.6182 1.2116 0.6482 -0.1859 0.1371  0.0361  383 MET B CB  
4012  C CG  . MET B 82  ? 0.5908 1.1933 0.6276 -0.2117 0.1344  0.0328  383 MET B CG  
4013  S SD  . MET B 82  ? 0.7283 1.3349 0.7786 -0.1872 0.1216  0.0258  383 MET B SD  
4014  C CE  . MET B 82  ? 0.7593 1.4510 0.8302 -0.1649 0.1226  0.0225  383 MET B CE  
4015  N N   . GLU B 83  ? 0.7336 1.2319 0.7318 -0.1384 0.1363  0.0426  384 GLU B N   
4016  C CA  . GLU B 83  ? 0.6908 1.1847 0.6815 -0.1143 0.1381  0.0436  384 GLU B CA  
4017  C C   . GLU B 83  ? 0.5772 1.0310 0.5640 -0.0865 0.1285  0.0403  384 GLU B C   
4018  O O   . GLU B 83  ? 0.5113 0.9753 0.4982 -0.0598 0.1268  0.0374  384 GLU B O   
4019  C CB  . GLU B 83  ? 0.7638 1.2287 0.7359 -0.1290 0.1458  0.0509  384 GLU B CB  
4020  C CG  . GLU B 83  ? 0.8784 1.3794 0.8512 -0.1581 0.1563  0.0552  384 GLU B CG  
4021  C CD  . GLU B 83  ? 0.9881 1.4498 0.9390 -0.1743 0.1634  0.0635  384 GLU B CD  
4022  O OE1 . GLU B 83  ? 1.0213 1.4346 0.9579 -0.1590 0.1600  0.0653  384 GLU B OE1 
4023  O OE2 . GLU B 83  ? 1.0541 1.5333 1.0011 -0.2027 0.1722  0.0683  384 GLU B OE2 
4024  N N   . ARG B 84  ? 0.5702 0.9775 0.5522 -0.0930 0.1223  0.0404  385 ARG B N   
4025  C CA  . ARG B 84  ? 0.5872 0.9582 0.5661 -0.0697 0.1132  0.0374  385 ARG B CA  
4026  C C   . ARG B 84  ? 0.6376 1.0414 0.6308 -0.0491 0.1075  0.0316  385 ARG B C   
4027  O O   . ARG B 84  ? 0.7063 1.0989 0.6962 -0.0232 0.1029  0.0289  385 ARG B O   
4028  C CB  . ARG B 84  ? 0.5994 0.9217 0.5720 -0.0825 0.1085  0.0387  385 ARG B CB  
4029  C CG  . ARG B 84  ? 0.5706 0.8511 0.5374 -0.0624 0.1002  0.0369  385 ARG B CG  
4030  C CD  . ARG B 84  ? 0.6586 0.9077 0.6099 -0.0533 0.1017  0.0398  385 ARG B CD  
4031  N NE  . ARG B 84  ? 0.7111 0.9247 0.6583 -0.0357 0.0933  0.0374  385 ARG B NE  
4032  C CZ  . ARG B 84  ? 0.7024 0.9169 0.6482 -0.0128 0.0898  0.0340  385 ARG B CZ  
4033  N NH1 . ARG B 84  ? 0.7269 0.9756 0.6746 -0.0022 0.0940  0.0324  385 ARG B NH1 
4034  N NH2 . ARG B 84  ? 0.5842 0.7650 0.5254 -0.0009 0.0824  0.0320  385 ARG B NH2 
4035  N N   . LEU B 85  ? 0.6022 1.0462 0.6097 -0.0600 0.1076  0.0296  386 LEU B N   
4036  C CA  . LEU B 85  ? 0.5297 1.0093 0.5500 -0.0394 0.1024  0.0248  386 LEU B CA  
4037  C C   . LEU B 85  ? 0.4950 1.0079 0.5157 -0.0158 0.1057  0.0232  386 LEU B C   
4038  O O   . LEU B 85  ? 0.5086 1.0154 0.5274 0.0122  0.1003  0.0199  386 LEU B O   
4039  C CB  . LEU B 85  ? 0.5052 1.0295 0.5408 -0.0575 0.1028  0.0231  386 LEU B CB  
4040  C CG  . LEU B 85  ? 0.5421 1.0348 0.5772 -0.0765 0.0980  0.0229  386 LEU B CG  
4041  C CD1 . LEU B 85  ? 0.4055 0.9464 0.4555 -0.0932 0.0977  0.0200  386 LEU B CD1 
4042  C CD2 . LEU B 85  ? 0.5312 0.9814 0.5618 -0.0566 0.0887  0.0213  386 LEU B CD2 
4043  N N   . GLU B 86  ? 0.5550 1.1016 0.5765 -0.0268 0.1149  0.0255  387 GLU B N   
4044  C CA  . GLU B 86  ? 0.6273 1.2069 0.6479 -0.0047 0.1191  0.0238  387 GLU B CA  
4045  C C   . GLU B 86  ? 0.6275 1.1590 0.6310 0.0157  0.1168  0.0235  387 GLU B C   
4046  O O   . GLU B 86  ? 0.6362 1.1776 0.6364 0.0440  0.1153  0.0197  387 GLU B O   
4047  C CB  . GLU B 86  ? 0.7450 1.3683 0.7687 -0.0243 0.1301  0.0271  387 GLU B CB  
4048  C CG  . GLU B 86  ? 0.9697 1.6466 1.0104 -0.0468 0.1328  0.0268  387 GLU B CG  
4049  C CD  . GLU B 86  ? 1.1961 1.8949 1.2354 -0.0781 0.1436  0.0319  387 GLU B CD  
4050  O OE1 . GLU B 86  ? 1.2801 1.9745 1.3085 -0.0748 0.1503  0.0351  387 GLU B OE1 
4051  O OE2 . GLU B 86  ? 1.2527 1.9715 1.3002 -0.1068 0.1454  0.0327  387 GLU B OE2 
4052  N N   . GLU B 87  ? 0.6206 1.0997 0.6117 0.0023  0.1164  0.0272  388 GLU B N   
4053  C CA  . GLU B 87  ? 0.7068 1.1408 0.6818 0.0197  0.1135  0.0266  388 GLU B CA  
4054  C C   . GLU B 87  ? 0.6758 1.0825 0.6497 0.0418  0.1034  0.0220  388 GLU B C   
4055  O O   . GLU B 87  ? 0.4424 0.8404 0.4079 0.0665  0.1010  0.0183  388 GLU B O   
4056  C CB  . GLU B 87  ? 0.6821 1.0699 0.6447 0.0003  0.1150  0.0320  388 GLU B CB  
4057  C CG  . GLU B 87  ? 0.6537 1.0056 0.5992 0.0145  0.1142  0.0321  388 GLU B CG  
4058  C CD  . GLU B 87  ? 0.7390 1.0463 0.6721 -0.0027 0.1149  0.0377  388 GLU B CD  
4059  O OE1 . GLU B 87  ? 0.6819 0.9766 0.6186 -0.0226 0.1143  0.0407  388 GLU B OE1 
4060  O OE2 . GLU B 87  ? 0.7615 1.0465 0.6802 0.0045  0.1159  0.0390  388 GLU B OE2 
4061  N N   . VAL B 88  ? 0.6105 1.0025 0.5913 0.0329  0.0976  0.0221  389 VAL B N   
4062  C CA  . VAL B 88  ? 0.5639 0.9313 0.5431 0.0524  0.0885  0.0186  389 VAL B CA  
4063  C C   . VAL B 88  ? 0.5829 0.9882 0.5672 0.0771  0.0874  0.0143  389 VAL B C   
4064  O O   . VAL B 88  ? 0.5865 0.9704 0.5615 0.1010  0.0824  0.0110  389 VAL B O   
4065  C CB  . VAL B 88  ? 0.5824 0.9326 0.5685 0.0375  0.0832  0.0197  389 VAL B CB  
4066  C CG1 . VAL B 88  ? 0.4084 0.7454 0.3948 0.0576  0.0746  0.0165  389 VAL B CG1 
4067  C CG2 . VAL B 88  ? 0.4952 0.7975 0.4718 0.0211  0.0827  0.0232  389 VAL B CG2 
4068  N N   . ASN B 89  ? 0.5632 1.0254 0.5610 0.0721  0.0922  0.0142  390 ASN B N   
4069  C CA  . ASN B 89  ? 0.5551 1.0583 0.5581 0.0974  0.0912  0.0102  390 ASN B CA  
4070  C C   . ASN B 89  ? 0.6464 1.1521 0.6374 0.1208  0.0946  0.0075  390 ASN B C   
4071  O O   . ASN B 89  ? 0.6643 1.1625 0.6475 0.1495  0.0902  0.0035  390 ASN B O   
4072  C CB  . ASN B 89  ? 0.5790 1.1484 0.6003 0.0849  0.0959  0.0106  390 ASN B CB  
4073  C CG  . ASN B 89  ? 0.6908 1.3047 0.7188 0.1122  0.0935  0.0067  390 ASN B CG  
4074  O OD1 . ASN B 89  ? 0.6910 1.3347 0.7162 0.1318  0.0978  0.0045  390 ASN B OD1 
4075  N ND2 . ASN B 89  ? 0.7623 1.3812 0.7979 0.1150  0.0867  0.0060  390 ASN B ND2 
4076  N N   . LYS B 90  ? 0.5663 1.0821 0.5538 0.1095  0.1026  0.0095  391 LYS B N   
4077  C CA  . LYS B 90  ? 0.5496 1.0660 0.5240 0.1309  0.1060  0.0066  391 LYS B CA  
4078  C C   . LYS B 90  ? 0.5259 0.9795 0.4819 0.1466  0.0990  0.0039  391 LYS B C   
4079  O O   . LYS B 90  ? 0.4800 0.9277 0.4242 0.1740  0.0973  -0.0011 391 LYS B O   
4080  C CB  . LYS B 90  ? 0.5839 1.1163 0.5563 0.1124  0.1157  0.0104  391 LYS B CB  
4081  C CG  . LYS B 90  ? 0.7308 1.2371 0.6843 0.1267  0.1177  0.0086  391 LYS B CG  
4082  C CD  . LYS B 90  ? 0.8414 1.3181 0.7869 0.1023  0.1216  0.0144  391 LYS B CD  
4083  C CE  . LYS B 90  ? 0.8324 1.2422 0.7659 0.1017  0.1134  0.0144  391 LYS B CE  
4084  N NZ  . LYS B 90  ? 0.8659 1.2462 0.7820 0.1266  0.1097  0.0089  391 LYS B NZ  
4085  N N   . GLU B 91  ? 0.4740 0.8806 0.4267 0.1294  0.0947  0.0069  392 GLU B N   
4086  C CA  . GLU B 91  ? 0.5658 0.9148 0.5019 0.1399  0.0883  0.0046  392 GLU B CA  
4087  C C   . GLU B 91  ? 0.6723 1.0051 0.6043 0.1624  0.0804  0.0005  392 GLU B C   
4088  O O   . GLU B 91  ? 0.6514 0.9551 0.5669 0.1824  0.0771  -0.0039 392 GLU B O   
4089  C CB  . GLU B 91  ? 0.5082 0.8179 0.4436 0.1161  0.0858  0.0091  392 GLU B CB  
4090  C CG  . GLU B 91  ? 0.6309 0.8931 0.5490 0.1199  0.0830  0.0080  392 GLU B CG  
4091  C CD  . GLU B 91  ? 0.7295 0.9637 0.6471 0.0965  0.0828  0.0132  392 GLU B CD  
4092  O OE1 . GLU B 91  ? 0.7824 0.9749 0.6888 0.0983  0.0778  0.0124  392 GLU B OE1 
4093  O OE2 . GLU B 91  ? 0.7643 1.0183 0.6920 0.0764  0.0875  0.0178  392 GLU B OE2 
4094  N N   . ILE B 92  ? 0.7207 1.0704 0.6658 0.1592  0.0772  0.0018  393 ILE B N   
4095  C CA  . ILE B 92  ? 0.7029 1.0372 0.6427 0.1809  0.0699  -0.0011 393 ILE B CA  
4096  C C   . ILE B 92  ? 0.6722 1.0354 0.6059 0.2104  0.0720  -0.0057 393 ILE B C   
4097  O O   . ILE B 92  ? 0.7050 1.0376 0.6219 0.2338  0.0674  -0.0095 393 ILE B O   
4098  C CB  . ILE B 92  ? 0.6958 1.0438 0.6506 0.1703  0.0662  0.0017  393 ILE B CB  
4099  C CG1 . ILE B 92  ? 0.6258 0.9348 0.5821 0.1458  0.0631  0.0052  393 ILE B CG1 
4100  C CG2 . ILE B 92  ? 0.7399 1.0802 0.6888 0.1950  0.0596  -0.0004 393 ILE B CG2 
4101  C CD1 . ILE B 92  ? 0.6531 0.9822 0.6255 0.1286  0.0616  0.0080  393 ILE B CD1 
4102  N N   . ASP B 93  ? 0.7179 1.1400 0.6637 0.2096  0.0791  -0.0054 394 ASP B N   
4103  C CA  . ASP B 93  ? 0.7193 1.1750 0.6594 0.2380  0.0825  -0.0100 394 ASP B CA  
4104  C C   . ASP B 93  ? 0.8550 1.2729 0.7721 0.2552  0.0827  -0.0145 394 ASP B C   
4105  O O   . ASP B 93  ? 1.0061 1.4219 0.9095 0.2855  0.0812  -0.0197 394 ASP B O   
4106  C CB  . ASP B 93  ? 0.7298 1.2540 0.6864 0.2279  0.0917  -0.0085 394 ASP B CB  
4107  C CG  . ASP B 93  ? 0.8211 1.3975 0.7977 0.2242  0.0912  -0.0069 394 ASP B CG  
4108  O OD1 . ASP B 93  ? 0.9043 1.4730 0.8793 0.2419  0.0843  -0.0082 394 ASP B OD1 
4109  O OD2 . ASP B 93  ? 0.8243 1.4498 0.8175 0.2030  0.0976  -0.0042 394 ASP B OD2 
4110  N N   . THR B 94  ? 0.7426 1.1297 0.6535 0.2371  0.0844  -0.0130 395 THR B N   
4111  C CA  . THR B 94  ? 0.7616 1.1213 0.6517 0.2506  0.0855  -0.0177 395 THR B CA  
4112  C C   . THR B 94  ? 0.8529 1.1437 0.7253 0.2509  0.0777  -0.0197 395 THR B C   
4113  O O   . THR B 94  ? 0.9825 1.2468 0.8353 0.2641  0.0773  -0.0249 395 THR B O   
4114  C CB  . THR B 94  ? 0.7562 1.1377 0.6496 0.2329  0.0940  -0.0150 395 THR B CB  
4115  O OG1 . THR B 94  ? 0.8309 1.1994 0.7348 0.2014  0.0939  -0.0084 395 THR B OG1 
4116  C CG2 . THR B 94  ? 0.6506 1.1017 0.5572 0.2367  0.1026  -0.0144 395 THR B CG2 
4117  N N   . THR B 95  ? 0.7756 1.0383 0.6540 0.2360  0.0716  -0.0161 396 THR B N   
4118  C CA  . THR B 95  ? 0.7112 0.9125 0.5738 0.2358  0.0641  -0.0180 396 THR B CA  
4119  C C   . THR B 95  ? 0.7323 0.9109 0.5967 0.2374  0.0566  -0.0165 396 THR B C   
4120  O O   . THR B 95  ? 0.7828 0.9118 0.6338 0.2369  0.0504  -0.0179 396 THR B O   
4121  C CB  . THR B 95  ? 0.6476 0.8256 0.5117 0.2100  0.0642  -0.0146 396 THR B CB  
4122  O OG1 . THR B 95  ? 0.6380 0.8314 0.5215 0.1872  0.0650  -0.0081 396 THR B OG1 
4123  C CG2 . THR B 95  ? 0.5336 0.7271 0.3926 0.2075  0.0712  -0.0153 396 THR B CG2 
4124  N N   . SER B 96  ? 0.6128 0.8266 0.4930 0.2382  0.0570  -0.0135 397 SER B N   
4125  C CA  . SER B 96  ? 0.7330 0.9301 0.6167 0.2375  0.0505  -0.0110 397 SER B CA  
4126  C C   . SER B 96  ? 0.7614 0.9333 0.6532 0.2100  0.0476  -0.0065 397 SER B C   
4127  O O   . SER B 96  ? 0.8367 0.9853 0.7279 0.2082  0.0417  -0.0046 397 SER B O   
4128  C CB  . SER B 96  ? 0.7685 0.9228 0.6296 0.2610  0.0442  -0.0148 397 SER B CB  
4129  O OG  . SER B 96  ? 0.8637 1.0423 0.7174 0.2897  0.0461  -0.0184 397 SER B OG  
4130  N N   . THR B 97  ? 0.7234 0.8991 0.6213 0.1896  0.0517  -0.0046 398 THR B N   
4131  C CA  . THR B 97  ? 0.7756 0.9320 0.6814 0.1649  0.0496  -0.0002 398 THR B CA  
4132  C C   . THR B 97  ? 0.6685 0.8529 0.5856 0.1454  0.0567  0.0029  398 THR B C   
4133  O O   . THR B 97  ? 0.6094 0.8327 0.5308 0.1496  0.0630  0.0023  398 THR B O   
4134  C CB  . THR B 97  ? 0.7353 0.8386 0.6258 0.1633  0.0443  -0.0018 398 THR B CB  
4135  O OG1 . THR B 97  ? 0.6789 0.7646 0.5771 0.1436  0.0412  0.0022  398 THR B OG1 
4136  C CG2 . THR B 97  ? 0.7634 0.8581 0.6437 0.1621  0.0476  -0.0040 398 THR B CG2 
4137  N N   . TYR B 98  ? 0.5476 0.7127 0.4685 0.1240  0.0561  0.0066  399 TYR B N   
4138  C CA  . TYR B 98  ? 0.6017 0.7812 0.5275 0.1054  0.0626  0.0101  399 TYR B CA  
4139  C C   . TYR B 98  ? 0.5894 0.7293 0.5093 0.0915  0.0599  0.0125  399 TYR B C   
4140  O O   . TYR B 98  ? 0.5686 0.6765 0.4839 0.0942  0.0532  0.0115  399 TYR B O   
4141  C CB  . TYR B 98  ? 0.5954 0.8138 0.5381 0.0907  0.0666  0.0132  399 TYR B CB  
4142  C CG  . TYR B 98  ? 0.5734 0.7787 0.5242 0.0770  0.0622  0.0154  399 TYR B CG  
4143  C CD1 . TYR B 98  ? 0.5548 0.7577 0.5089 0.0876  0.0561  0.0137  399 TYR B CD1 
4144  C CD2 . TYR B 98  ? 0.5801 0.7751 0.5339 0.0541  0.0643  0.0192  399 TYR B CD2 
4145  C CE1 . TYR B 98  ? 0.6212 0.8136 0.5821 0.0753  0.0522  0.0156  399 TYR B CE1 
4146  C CE2 . TYR B 98  ? 0.5441 0.7272 0.5041 0.0426  0.0605  0.0205  399 TYR B CE2 
4147  C CZ  . TYR B 98  ? 0.6419 0.8251 0.6061 0.0530  0.0545  0.0186  399 TYR B CZ  
4148  O OH  . TYR B 98  ? 0.6687 0.8414 0.6384 0.0419  0.0508  0.0197  399 TYR B OH  
4149  N N   . GLN B 99  ? 0.5889 0.7314 0.5078 0.0771  0.0652  0.0160  400 GLN B N   
4150  C CA  . GLN B 99  ? 0.5354 0.6432 0.4471 0.0662  0.0631  0.0186  400 GLN B CA  
4151  C C   . GLN B 99  ? 0.5854 0.6966 0.5044 0.0448  0.0664  0.0238  400 GLN B C   
4152  O O   . GLN B 99  ? 0.6707 0.8102 0.5952 0.0351  0.0731  0.0262  400 GLN B O   
4153  C CB  . GLN B 99  ? 0.4991 0.5976 0.3970 0.0710  0.0658  0.0181  400 GLN B CB  
4154  C CG  . GLN B 99  ? 0.4956 0.5878 0.3831 0.0919  0.0627  0.0119  400 GLN B CG  
4155  C CD  . GLN B 99  ? 0.6538 0.7111 0.5357 0.0977  0.0540  0.0087  400 GLN B CD  
4156  O OE1 . GLN B 99  ? 0.7265 0.7593 0.6071 0.0876  0.0504  0.0108  400 GLN B OE1 
4157  N NE2 . GLN B 99  ? 0.7407 0.7955 0.6184 0.1143  0.0506  0.0038  400 GLN B NE2 
4158  N N   . LEU B 100 ? 0.6322 0.7141 0.5501 0.0370  0.0619  0.0254  401 LEU B N   
4159  C CA  . LEU B 100 ? 0.6159 0.6945 0.5380 0.0181  0.0644  0.0297  401 LEU B CA  
4160  C C   . LEU B 100 ? 0.5877 0.6536 0.4987 0.0095  0.0692  0.0340  401 LEU B C   
4161  O O   . LEU B 100 ? 0.5153 0.5614 0.4157 0.0171  0.0671  0.0338  401 LEU B O   
4162  C CB  . LEU B 100 ? 0.4503 0.5036 0.3746 0.0152  0.0578  0.0294  401 LEU B CB  
4163  C CG  . LEU B 100 ? 0.5077 0.5703 0.4416 0.0216  0.0530  0.0263  401 LEU B CG  
4164  C CD1 . LEU B 100 ? 0.5014 0.5393 0.4363 0.0172  0.0475  0.0267  401 LEU B CD1 
4165  C CD2 . LEU B 100 ? 0.5257 0.6230 0.4709 0.0143  0.0569  0.0265  401 LEU B CD2 
4166  N N   . LYS B 101 ? 0.5416 0.6185 0.4539 -0.0069 0.0755  0.0380  402 LYS B N   
4167  C CA  . LYS B 101 ? 0.5795 0.6366 0.4792 -0.0170 0.0796  0.0435  402 LYS B CA  
4168  C C   . LYS B 101 ? 0.5828 0.6034 0.4766 -0.0178 0.0741  0.0446  402 LYS B C   
4169  O O   . LYS B 101 ? 0.5643 0.5782 0.4657 -0.0167 0.0687  0.0419  402 LYS B O   
4170  C CB  . LYS B 101 ? 0.5724 0.6435 0.4728 -0.0369 0.0872  0.0476  402 LYS B CB  
4171  C CG  . LYS B 101 ? 0.6483 0.7610 0.5552 -0.0385 0.0936  0.0471  402 LYS B CG  
4172  C CD  . LYS B 101 ? 0.6778 0.7962 0.5753 -0.0268 0.0968  0.0479  402 LYS B CD  
4173  C CE  . LYS B 101 ? 0.7973 0.9594 0.6999 -0.0312 0.1049  0.0485  402 LYS B CE  
4174  N NZ  . LYS B 101 ? 0.8895 1.0642 0.7854 -0.0147 0.1070  0.0469  402 LYS B NZ  
4175  N N   . ASP B 102 ? 0.7008 0.6994 0.5803 -0.0190 0.0758  0.0488  403 ASP B N   
4176  C CA  . ASP B 102 ? 0.6406 0.6074 0.5133 -0.0186 0.0712  0.0503  403 ASP B CA  
4177  C C   . ASP B 102 ? 0.5721 0.5301 0.4493 -0.0306 0.0710  0.0509  403 ASP B C   
4178  O O   . ASP B 102 ? 0.5963 0.5408 0.4772 -0.0269 0.0650  0.0487  403 ASP B O   
4179  C CB  . ASP B 102 ? 0.7906 0.7387 0.6458 -0.0195 0.0746  0.0561  403 ASP B CB  
4180  C CG  . ASP B 102 ? 0.9116 0.8604 0.7602 -0.0052 0.0721  0.0545  403 ASP B CG  
4181  O OD1 . ASP B 102 ? 0.9478 0.9083 0.8045 0.0050  0.0677  0.0486  403 ASP B OD1 
4182  O OD2 . ASP B 102 ? 0.9919 0.9280 0.8257 -0.0041 0.0744  0.0592  403 ASP B OD2 
4183  N N   . THR B 103 ? 0.6052 0.5703 0.4809 -0.0461 0.0776  0.0539  404 THR B N   
4184  C CA  . THR B 103 ? 0.6928 0.6476 0.5702 -0.0590 0.0776  0.0538  404 THR B CA  
4185  C C   . THR B 103 ? 0.6577 0.6311 0.5525 -0.0564 0.0725  0.0479  404 THR B C   
4186  O O   . THR B 103 ? 0.6233 0.5825 0.5201 -0.0583 0.0686  0.0462  404 THR B O   
4187  C CB  . THR B 103 ? 0.6860 0.6463 0.5574 -0.0784 0.0858  0.0575  404 THR B CB  
4188  O OG1 . THR B 103 ? 0.7007 0.7000 0.5828 -0.0808 0.0896  0.0560  404 THR B OG1 
4189  C CG2 . THR B 103 ? 0.7543 0.6891 0.6052 -0.0815 0.0907  0.0643  404 THR B CG2 
4190  N N   . GLU B 104 ? 0.6235 0.6284 0.5295 -0.0507 0.0727  0.0450  405 GLU B N   
4191  C CA  . GLU B 104 ? 0.5733 0.5960 0.4939 -0.0461 0.0679  0.0402  405 GLU B CA  
4192  C C   . GLU B 104 ? 0.6569 0.6604 0.5781 -0.0328 0.0602  0.0380  405 GLU B C   
4193  O O   . GLU B 104 ? 0.5378 0.5395 0.4660 -0.0333 0.0559  0.0357  405 GLU B O   
4194  C CB  . GLU B 104 ? 0.5498 0.6091 0.4795 -0.0392 0.0697  0.0380  405 GLU B CB  
4195  C CG  . GLU B 104 ? 0.5721 0.6570 0.5026 -0.0535 0.0777  0.0402  405 GLU B CG  
4196  C CD  . GLU B 104 ? 0.5775 0.6996 0.5147 -0.0436 0.0804  0.0384  405 GLU B CD  
4197  O OE1 . GLU B 104 ? 0.5777 0.7291 0.5185 -0.0553 0.0868  0.0396  405 GLU B OE1 
4198  O OE2 . GLU B 104 ? 0.5733 0.6952 0.5111 -0.0245 0.0762  0.0356  405 GLU B OE2 
4199  N N   . LEU B 105 ? 0.6151 0.6054 0.5287 -0.0216 0.0584  0.0386  406 LEU B N   
4200  C CA  . LEU B 105 ? 0.5334 0.5063 0.4468 -0.0112 0.0513  0.0365  406 LEU B CA  
4201  C C   . LEU B 105 ? 0.6400 0.5905 0.5503 -0.0174 0.0492  0.0380  406 LEU B C   
4202  O O   . LEU B 105 ? 0.5435 0.4885 0.4592 -0.0143 0.0440  0.0358  406 LEU B O   
4203  C CB  . LEU B 105 ? 0.6031 0.5667 0.5075 -0.0005 0.0498  0.0364  406 LEU B CB  
4204  C CG  . LEU B 105 ? 0.6351 0.5847 0.5393 0.0092  0.0424  0.0335  406 LEU B CG  
4205  C CD1 . LEU B 105 ? 0.6736 0.6345 0.5841 0.0180  0.0392  0.0294  406 LEU B CD1 
4206  C CD2 . LEU B 105 ? 0.4983 0.4348 0.3911 0.0152  0.0412  0.0341  406 LEU B CD2 
4207  N N   . ILE B 106 ? 0.4299 0.3662 0.3300 -0.0255 0.0535  0.0418  407 ILE B N   
4208  C CA  . ILE B 106 ? 0.5938 0.5068 0.4882 -0.0288 0.0518  0.0430  407 ILE B CA  
4209  C C   . ILE B 106 ? 0.6268 0.5445 0.5287 -0.0381 0.0515  0.0407  407 ILE B C   
4210  O O   . ILE B 106 ? 0.6703 0.5790 0.5750 -0.0357 0.0473  0.0389  407 ILE B O   
4211  C CB  . ILE B 106 ? 0.5524 0.4456 0.4305 -0.0336 0.0567  0.0481  407 ILE B CB  
4212  C CG1 . ILE B 106 ? 0.5235 0.4097 0.3936 -0.0220 0.0549  0.0499  407 ILE B CG1 
4213  C CG2 . ILE B 106 ? 0.5303 0.3993 0.4006 -0.0383 0.0563  0.0491  407 ILE B CG2 
4214  C CD1 . ILE B 106 ? 0.5725 0.4504 0.4277 -0.0257 0.0610  0.0553  407 ILE B CD1 
4215  N N   . TYR B 107 ? 0.5738 0.5082 0.4793 -0.0492 0.0562  0.0406  408 TYR B N   
4216  C CA  . TYR B 107 ? 0.6576 0.6010 0.5704 -0.0592 0.0558  0.0377  408 TYR B CA  
4217  C C   . TYR B 107 ? 0.5994 0.5559 0.5249 -0.0503 0.0496  0.0340  408 TYR B C   
4218  O O   . TYR B 107 ? 0.5130 0.4651 0.4415 -0.0535 0.0469  0.0319  408 TYR B O   
4219  C CB  . TYR B 107 ? 0.6659 0.6339 0.5826 -0.0719 0.0614  0.0378  408 TYR B CB  
4220  C CG  . TYR B 107 ? 0.7226 0.7083 0.6491 -0.0815 0.0603  0.0340  408 TYR B CG  
4221  C CD1 . TYR B 107 ? 0.7855 0.7545 0.7051 -0.0955 0.0615  0.0330  408 TYR B CD1 
4222  C CD2 . TYR B 107 ? 0.7384 0.7569 0.6796 -0.0756 0.0577  0.0311  408 TYR B CD2 
4223  C CE1 . TYR B 107 ? 0.7644 0.7509 0.6924 -0.1049 0.0601  0.0288  408 TYR B CE1 
4224  C CE2 . TYR B 107 ? 0.6723 0.7097 0.6223 -0.0836 0.0562  0.0276  408 TYR B CE2 
4225  C CZ  . TYR B 107 ? 0.7657 0.7882 0.7096 -0.0990 0.0573  0.0263  408 TYR B CZ  
4226  O OH  . TYR B 107 ? 0.8202 0.8630 0.7724 -0.1077 0.0554  0.0222  408 TYR B OH  
4227  N N   . GLY B 108 ? 0.5706 0.5414 0.5020 -0.0387 0.0475  0.0333  409 GLY B N   
4228  C CA  . GLY B 108 ? 0.4964 0.4786 0.4374 -0.0301 0.0422  0.0305  409 GLY B CA  
4229  C C   . GLY B 108 ? 0.6167 0.5786 0.5557 -0.0231 0.0368  0.0303  409 GLY B C   
4230  O O   . GLY B 108 ? 0.5757 0.5400 0.5204 -0.0221 0.0331  0.0287  409 GLY B O   
4231  N N   . ALA B 109 ? 0.5525 0.4966 0.4832 -0.0183 0.0363  0.0319  410 ALA B N   
4232  C CA  . ALA B 109 ? 0.5792 0.5079 0.5084 -0.0130 0.0314  0.0316  410 ALA B CA  
4233  C C   . ALA B 109 ? 0.5018 0.4204 0.4298 -0.0197 0.0314  0.0317  410 ALA B C   
4234  O O   . ALA B 109 ? 0.5009 0.4179 0.4330 -0.0177 0.0275  0.0305  410 ALA B O   
4235  C CB  . ALA B 109 ? 0.4936 0.4095 0.4141 -0.0070 0.0307  0.0331  410 ALA B CB  
4236  N N   . LYS B 110 ? 0.4705 0.3807 0.3914 -0.0277 0.0360  0.0331  411 LYS B N   
4237  C CA  . LYS B 110 ? 0.5390 0.4357 0.4556 -0.0333 0.0363  0.0325  411 LYS B CA  
4238  C C   . LYS B 110 ? 0.5866 0.4971 0.5121 -0.0393 0.0351  0.0293  411 LYS B C   
4239  O O   . LYS B 110 ? 0.5368 0.4411 0.4626 -0.0393 0.0327  0.0277  411 LYS B O   
4240  C CB  . LYS B 110 ? 0.5154 0.3959 0.4190 -0.0412 0.0418  0.0347  411 LYS B CB  
4241  C CG  . LYS B 110 ? 0.5818 0.4424 0.4731 -0.0337 0.0421  0.0381  411 LYS B CG  
4242  C CD  . LYS B 110 ? 0.5703 0.4131 0.4463 -0.0417 0.0482  0.0414  411 LYS B CD  
4243  C CE  . LYS B 110 ? 0.5551 0.3790 0.4174 -0.0322 0.0484  0.0455  411 LYS B CE  
4244  N NZ  . LYS B 110 ? 0.5537 0.3528 0.3971 -0.0389 0.0540  0.0493  411 LYS B NZ  
4245  N N   . HIS B 111 ? 0.6214 0.5532 0.5543 -0.0434 0.0365  0.0284  412 HIS B N   
4246  C CA  . HIS B 111 ? 0.5381 0.4859 0.4793 -0.0486 0.0350  0.0255  412 HIS B CA  
4247  C C   . HIS B 111 ? 0.6324 0.5888 0.5816 -0.0385 0.0295  0.0248  412 HIS B C   
4248  O O   . HIS B 111 ? 0.5972 0.5591 0.5504 -0.0406 0.0271  0.0229  412 HIS B O   
4249  C CB  . HIS B 111 ? 0.4174 0.3887 0.3635 -0.0571 0.0384  0.0246  412 HIS B CB  
4250  C CG  . HIS B 111 ? 0.5652 0.5287 0.5037 -0.0729 0.0432  0.0240  412 HIS B CG  
4251  N ND1 . HIS B 111 ? 0.6628 0.6408 0.6050 -0.0854 0.0439  0.0207  412 HIS B ND1 
4252  C CD2 . HIS B 111 ? 0.5996 0.5391 0.5246 -0.0787 0.0474  0.0264  412 HIS B CD2 
4253  C CE1 . HIS B 111 ? 0.6867 0.6487 0.6176 -0.0997 0.0484  0.0206  412 HIS B CE1 
4254  N NE2 . HIS B 111 ? 0.6263 0.5634 0.5460 -0.0953 0.0507  0.0244  412 HIS B NE2 
4255  N N   . ALA B 112 ? 0.5474 0.5031 0.4973 -0.0282 0.0275  0.0263  413 ALA B N   
4256  C CA  . ALA B 112 ? 0.5468 0.5033 0.5004 -0.0198 0.0224  0.0263  413 ALA B CA  
4257  C C   . ALA B 112 ? 0.5669 0.5094 0.5183 -0.0207 0.0202  0.0262  413 ALA B C   
4258  O O   . ALA B 112 ? 0.4552 0.4026 0.4104 -0.0204 0.0174  0.0256  413 ALA B O   
4259  C CB  . ALA B 112 ? 0.5177 0.4699 0.4689 -0.0102 0.0209  0.0273  413 ALA B CB  
4260  N N   . TRP B 113 ? 0.4725 0.3988 0.4169 -0.0210 0.0214  0.0271  414 TRP B N   
4261  C CA  . TRP B 113 ? 0.4579 0.3734 0.3996 -0.0206 0.0198  0.0268  414 TRP B CA  
4262  C C   . TRP B 113 ? 0.5246 0.4411 0.4660 -0.0277 0.0211  0.0245  414 TRP B C   
4263  O O   . TRP B 113 ? 0.5563 0.4737 0.4995 -0.0268 0.0189  0.0235  414 TRP B O   
4264  C CB  . TRP B 113 ? 0.4374 0.3375 0.3704 -0.0178 0.0212  0.0282  414 TRP B CB  
4265  C CG  . TRP B 113 ? 0.4847 0.3764 0.4145 -0.0148 0.0197  0.0279  414 TRP B CG  
4266  C CD1 . TRP B 113 ? 0.4679 0.3654 0.4024 -0.0144 0.0171  0.0267  414 TRP B CD1 
4267  C CD2 . TRP B 113 ? 0.5380 0.4160 0.4584 -0.0104 0.0208  0.0290  414 TRP B CD2 
4268  N NE1 . TRP B 113 ? 0.4871 0.3773 0.4166 -0.0102 0.0168  0.0266  414 TRP B NE1 
4269  C CE2 . TRP B 113 ? 0.5069 0.3851 0.4277 -0.0069 0.0188  0.0280  414 TRP B CE2 
4270  C CE3 . TRP B 113 ? 0.5168 0.3832 0.4278 -0.0082 0.0233  0.0311  414 TRP B CE3 
4271  C CZ2 . TRP B 113 ? 0.5892 0.4578 0.5017 0.0000  0.0192  0.0286  414 TRP B CZ2 
4272  C CZ3 . TRP B 113 ? 0.4561 0.3104 0.3577 -0.0014 0.0234  0.0322  414 TRP B CZ3 
4273  C CH2 . TRP B 113 ? 0.5096 0.3658 0.4123 0.0033  0.0213  0.0308  414 TRP B CH2 
4274  N N   . ARG B 114 ? 0.4814 0.3975 0.4195 -0.0357 0.0250  0.0234  415 ARG B N   
4275  C CA  . ARG B 114 ? 0.5349 0.4505 0.4710 -0.0444 0.0262  0.0203  415 ARG B CA  
4276  C C   . ARG B 114 ? 0.6014 0.5370 0.5470 -0.0450 0.0230  0.0185  415 ARG B C   
4277  O O   . ARG B 114 ? 0.6208 0.5560 0.5653 -0.0484 0.0221  0.0158  415 ARG B O   
4278  C CB  . ARG B 114 ? 0.4845 0.3974 0.4150 -0.0552 0.0309  0.0197  415 ARG B CB  
4279  C CG  . ARG B 114 ? 0.4803 0.3878 0.4052 -0.0664 0.0325  0.0157  415 ARG B CG  
4280  C CD  . ARG B 114 ? 0.5377 0.4499 0.4598 -0.0798 0.0368  0.0152  415 ARG B CD  
4281  N NE  . ARG B 114 ? 0.6262 0.5231 0.5374 -0.0921 0.0389  0.0113  415 ARG B NE  
4282  C CZ  . ARG B 114 ? 0.6362 0.5301 0.5405 -0.1076 0.0432  0.0102  415 ARG B CZ  
4283  N NH1 . ARG B 114 ? 0.4815 0.3570 0.3734 -0.1189 0.0446  0.0059  415 ARG B NH1 
4284  N NH2 . ARG B 114 ? 0.5910 0.4997 0.4996 -0.1121 0.0462  0.0131  415 ARG B NH2 
4285  N N   . ASN B 115 ? 0.5103 0.4627 0.4639 -0.0405 0.0213  0.0200  416 ASN B N   
4286  C CA  . ASN B 115 ? 0.5312 0.5031 0.4923 -0.0391 0.0183  0.0193  416 ASN B CA  
4287  C C   . ASN B 115 ? 0.4780 0.4468 0.4405 -0.0308 0.0142  0.0212  416 ASN B C   
4288  O O   . ASN B 115 ? 0.5130 0.4953 0.4798 -0.0282 0.0115  0.0215  416 ASN B O   
4289  C CB  . ASN B 115 ? 0.4422 0.4333 0.4092 -0.0362 0.0187  0.0201  416 ASN B CB  
4290  C CG  . ASN B 115 ? 0.5123 0.5144 0.4797 -0.0468 0.0229  0.0182  416 ASN B CG  
4291  O OD1 . ASN B 115 ? 0.5333 0.5287 0.4963 -0.0578 0.0250  0.0157  416 ASN B OD1 
4292  N ND2 . ASN B 115 ? 0.4354 0.4541 0.4069 -0.0437 0.0244  0.0192  416 ASN B ND2 
4293  N N   . ALA B 116 ? 0.4808 0.4335 0.4393 -0.0269 0.0137  0.0227  417 ALA B N   
4294  C CA  . ALA B 116 ? 0.5109 0.4615 0.4703 -0.0207 0.0101  0.0251  417 ALA B CA  
4295  C C   . ALA B 116 ? 0.4768 0.4299 0.4362 -0.0231 0.0090  0.0241  417 ALA B C   
4296  O O   . ALA B 116 ? 0.4177 0.3622 0.3735 -0.0239 0.0098  0.0231  417 ALA B O   
4297  C CB  . ALA B 116 ? 0.4694 0.4068 0.4253 -0.0170 0.0098  0.0268  417 ALA B CB  
4298  N N   . SER B 117 ? 0.4485 0.4146 0.4111 -0.0229 0.0070  0.0243  418 SER B N   
4299  C CA  A SER B 117 ? 0.4796 0.4511 0.4417 -0.0258 0.0062  0.0228  418 SER B CA  
4300  C CA  B SER B 117 ? 0.4749 0.4464 0.4370 -0.0257 0.0061  0.0228  418 SER B CA  
4301  C C   . SER B 117 ? 0.4896 0.4534 0.4493 -0.0234 0.0053  0.0245  418 SER B C   
4302  O O   . SER B 117 ? 0.5484 0.5126 0.5057 -0.0256 0.0059  0.0222  418 SER B O   
4303  C CB  A SER B 117 ? 0.4173 0.4052 0.3826 -0.0239 0.0036  0.0238  418 SER B CB  
4304  C CB  B SER B 117 ? 0.4223 0.4100 0.3876 -0.0236 0.0035  0.0240  418 SER B CB  
4305  O OG  A SER B 117 ? 0.4425 0.4279 0.4072 -0.0168 0.0011  0.0287  418 SER B OG  
4306  O OG  B SER B 117 ? 0.4387 0.4403 0.4071 -0.0275 0.0044  0.0211  418 SER B OG  
4307  N N   . ARG B 118 ? 0.4338 0.3915 0.3934 -0.0195 0.0039  0.0282  419 ARG B N   
4308  C CA  . ARG B 118 ? 0.4626 0.4174 0.4208 -0.0188 0.0030  0.0303  419 ARG B CA  
4309  C C   . ARG B 118 ? 0.4702 0.4182 0.4265 -0.0183 0.0048  0.0285  419 ARG B C   
4310  O O   . ARG B 118 ? 0.3678 0.3181 0.3239 -0.0177 0.0043  0.0297  419 ARG B O   
4311  C CB  . ARG B 118 ? 0.3973 0.3482 0.3547 -0.0168 0.0005  0.0347  419 ARG B CB  
4312  C CG  . ARG B 118 ? 0.4536 0.4094 0.4099 -0.0149 -0.0015 0.0374  419 ARG B CG  
4313  C CD  . ARG B 118 ? 0.4804 0.4268 0.4319 -0.0129 -0.0039 0.0421  419 ARG B CD  
4314  N NE  . ARG B 118 ? 0.5514 0.5016 0.4997 -0.0097 -0.0057 0.0453  419 ARG B NE  
4315  C CZ  . ARG B 118 ? 0.6628 0.6022 0.6036 -0.0065 -0.0079 0.0499  419 ARG B CZ  
4316  N NH1 . ARG B 118 ? 0.7463 0.6699 0.6821 -0.0078 -0.0086 0.0513  419 ARG B NH1 
4317  N NH2 . ARG B 118 ? 0.6379 0.5811 0.5745 -0.0020 -0.0094 0.0532  419 ARG B NH2 
4318  N N   . CYS B 119 ? 0.5142 0.4550 0.4685 -0.0183 0.0070  0.0261  420 CYS B N   
4319  C CA  . CYS B 119 ? 0.4221 0.3547 0.3728 -0.0155 0.0083  0.0255  420 CYS B CA  
4320  C C   . CYS B 119 ? 0.3764 0.3045 0.3217 -0.0152 0.0107  0.0219  420 CYS B C   
4321  O O   . CYS B 119 ? 0.4309 0.3529 0.3723 -0.0188 0.0128  0.0191  420 CYS B O   
4322  C CB  . CYS B 119 ? 0.5078 0.4321 0.4566 -0.0147 0.0095  0.0258  420 CYS B CB  
4323  S SG  . CYS B 119 ? 0.4802 0.3939 0.4223 -0.0095 0.0110  0.0255  420 CYS B SG  
4324  N N   . VAL B 120 ? 0.4376 0.3682 0.3813 -0.0109 0.0106  0.0218  421 VAL B N   
4325  C CA  . VAL B 120 ? 0.4725 0.3965 0.4084 -0.0078 0.0129  0.0181  421 VAL B CA  
4326  C C   . VAL B 120 ? 0.5540 0.4614 0.4812 -0.0034 0.0151  0.0172  421 VAL B C   
4327  O O   . VAL B 120 ? 0.4628 0.3574 0.3798 -0.0011 0.0175  0.0138  421 VAL B O   
4328  C CB  . VAL B 120 ? 0.4420 0.3781 0.3791 -0.0030 0.0123  0.0183  421 VAL B CB  
4329  C CG1 . VAL B 120 ? 0.4008 0.3430 0.3407 0.0020  0.0111  0.0212  421 VAL B CG1 
4330  C CG2 . VAL B 120 ? 0.4882 0.4178 0.4161 0.0016  0.0147  0.0136  421 VAL B CG2 
4331  N N   . GLY B 121 ? 0.5137 0.4187 0.4426 -0.0021 0.0145  0.0202  422 GLY B N   
4332  C CA  . GLY B 121 ? 0.4640 0.3545 0.3839 0.0033  0.0162  0.0206  422 GLY B CA  
4333  C C   . GLY B 121 ? 0.5714 0.4450 0.4839 -0.0019 0.0192  0.0200  422 GLY B C   
4334  O O   . GLY B 121 ? 0.5318 0.3904 0.4344 0.0024  0.0211  0.0211  422 GLY B O   
4335  N N   . ARG B 122 ? 0.6256 0.5021 0.5417 -0.0111 0.0198  0.0185  423 ARG B N   
4336  C CA  . ARG B 122 ? 0.5770 0.4449 0.4894 -0.0184 0.0224  0.0185  423 ARG B CA  
4337  C C   . ARG B 122 ? 0.5899 0.4343 0.4867 -0.0208 0.0263  0.0166  423 ARG B C   
4338  O O   . ARG B 122 ? 0.6320 0.4692 0.5247 -0.0289 0.0290  0.0170  423 ARG B O   
4339  C CB  . ARG B 122 ? 0.5171 0.3995 0.4381 -0.0272 0.0217  0.0170  423 ARG B CB  
4340  C CG  . ARG B 122 ? 0.3780 0.2784 0.3110 -0.0251 0.0184  0.0195  423 ARG B CG  
4341  C CD  . ARG B 122 ? 0.6860 0.6013 0.6258 -0.0313 0.0176  0.0181  423 ARG B CD  
4342  N NE  . ARG B 122 ? 0.6166 0.5395 0.5584 -0.0316 0.0157  0.0162  423 ARG B NE  
4343  C CZ  . ARG B 122 ? 0.6785 0.6138 0.6237 -0.0370 0.0149  0.0141  423 ARG B CZ  
4344  N NH1 . ARG B 122 ? 0.3685 0.3118 0.3163 -0.0430 0.0160  0.0132  423 ARG B NH1 
4345  N NH2 . ARG B 122 ? 0.5631 0.5052 0.5089 -0.0365 0.0131  0.0127  423 ARG B NH2 
4346  N N   . ILE B 123 ? 0.5693 0.4006 0.4557 -0.0140 0.0269  0.0146  424 ILE B N   
4347  C CA  . ILE B 123 ? 0.5813 0.3836 0.4486 -0.0149 0.0307  0.0131  424 ILE B CA  
4348  C C   . ILE B 123 ? 0.6676 0.4565 0.5274 -0.0132 0.0329  0.0178  424 ILE B C   
4349  O O   . ILE B 123 ? 0.6472 0.4133 0.4926 -0.0198 0.0367  0.0179  424 ILE B O   
4350  C CB  . ILE B 123 ? 0.5613 0.3523 0.4178 -0.0033 0.0307  0.0105  424 ILE B CB  
4351  C CG1 . ILE B 123 ? 0.6212 0.3767 0.4541 -0.0038 0.0346  0.0081  424 ILE B CG1 
4352  C CG2 . ILE B 123 ? 0.6134 0.4126 0.4725 0.0113  0.0287  0.0141  424 ILE B CG2 
4353  C CD1 . ILE B 123 ? 0.5975 0.3432 0.4246 -0.0191 0.0364  0.0029  424 ILE B CD1 
4354  N N   . GLN B 124 ? 0.6936 0.4964 0.5622 -0.0058 0.0305  0.0217  425 GLN B N   
4355  C CA  . GLN B 124 ? 0.7831 0.5762 0.6446 -0.0022 0.0320  0.0262  425 GLN B CA  
4356  C C   . GLN B 124 ? 0.7406 0.5452 0.6109 -0.0111 0.0326  0.0282  425 GLN B C   
4357  O O   . GLN B 124 ? 0.8042 0.6062 0.6711 -0.0075 0.0333  0.0319  425 GLN B O   
4358  C CB  . GLN B 124 ? 0.8348 0.6380 0.6996 0.0116  0.0286  0.0285  425 GLN B CB  
4359  C CG  . GLN B 124 ? 0.9179 0.7285 0.7846 0.0204  0.0264  0.0261  425 GLN B CG  
4360  C CD  . GLN B 124 ? 1.0447 0.8346 0.8931 0.0328  0.0280  0.0266  425 GLN B CD  
4361  O OE1 . GLN B 124 ? 0.9192 0.6895 0.7538 0.0358  0.0303  0.0298  425 GLN B OE1 
4362  N NE2 . GLN B 124 ? 1.2074 1.0014 1.0543 0.0413  0.0271  0.0236  425 GLN B NE2 
4363  N N   . TRP B 125 ? 0.6219 0.4408 0.5029 -0.0215 0.0325  0.0258  426 TRP B N   
4364  C CA  . TRP B 125 ? 0.5178 0.3546 0.4099 -0.0261 0.0321  0.0272  426 TRP B CA  
4365  C C   . TRP B 125 ? 0.6571 0.4840 0.5404 -0.0292 0.0361  0.0306  426 TRP B C   
4366  O O   . TRP B 125 ? 0.7323 0.5701 0.6210 -0.0262 0.0353  0.0328  426 TRP B O   
4367  C CB  . TRP B 125 ? 0.6017 0.4541 0.5033 -0.0362 0.0320  0.0241  426 TRP B CB  
4368  C CG  . TRP B 125 ? 0.5761 0.4175 0.4686 -0.0487 0.0362  0.0222  426 TRP B CG  
4369  C CD1 . TRP B 125 ? 0.6415 0.4681 0.5247 -0.0534 0.0372  0.0186  426 TRP B CD1 
4370  C CD2 . TRP B 125 ? 0.5798 0.4246 0.4708 -0.0594 0.0401  0.0234  426 TRP B CD2 
4371  N NE1 . TRP B 125 ? 0.6987 0.5170 0.5738 -0.0677 0.0413  0.0173  426 TRP B NE1 
4372  C CE2 . TRP B 125 ? 0.6756 0.5066 0.5561 -0.0720 0.0433  0.0205  426 TRP B CE2 
4373  C CE3 . TRP B 125 ? 0.6709 0.5297 0.5677 -0.0597 0.0414  0.0264  426 TRP B CE3 
4374  C CZ2 . TRP B 125 ? 0.5697 0.4022 0.4463 -0.0868 0.0478  0.0209  426 TRP B CZ2 
4375  C CZ3 . TRP B 125 ? 0.7168 0.5789 0.6102 -0.0725 0.0461  0.0269  426 TRP B CZ3 
4376  C CH2 . TRP B 125 ? 0.6134 0.4631 0.4972 -0.0868 0.0493  0.0244  426 TRP B CH2 
4377  N N   . SER B 126 ? 0.5964 0.4012 0.4645 -0.0355 0.0404  0.0310  427 SER B N   
4378  C CA  . SER B 126 ? 0.6021 0.3973 0.4605 -0.0413 0.0450  0.0348  427 SER B CA  
4379  C C   . SER B 126 ? 0.7023 0.4808 0.5480 -0.0298 0.0454  0.0394  427 SER B C   
4380  O O   . SER B 126 ? 0.6777 0.4467 0.5134 -0.0334 0.0494  0.0435  427 SER B O   
4381  C CB  . SER B 126 ? 0.6608 0.4374 0.5062 -0.0556 0.0498  0.0335  427 SER B CB  
4382  O OG  . SER B 126 ? 0.7495 0.4930 0.5745 -0.0500 0.0514  0.0347  427 SER B OG  
4383  N N   . LYS B 127 ? 0.6858 0.4628 0.5317 -0.0164 0.0415  0.0391  428 LYS B N   
4384  C CA  . LYS B 127 ? 0.8030 0.5693 0.6381 -0.0037 0.0408  0.0432  428 LYS B CA  
4385  C C   . LYS B 127 ? 0.9050 0.6952 0.7541 0.0040  0.0361  0.0434  428 LYS B C   
4386  O O   . LYS B 127 ? 1.1683 0.9636 1.0190 0.0149  0.0321  0.0430  428 LYS B O   
4387  C CB  . LYS B 127 ? 0.8864 0.6349 0.7097 0.0067  0.0399  0.0424  428 LYS B CB  
4388  C CG  . LYS B 127 ? 1.1092 0.8350 0.9122 0.0174  0.0416  0.0473  428 LYS B CG  
4389  C CD  . LYS B 127 ? 1.2151 0.9495 1.0191 0.0351  0.0370  0.0475  428 LYS B CD  
4390  C CE  . LYS B 127 ? 1.2610 0.9811 1.0477 0.0468  0.0378  0.0533  428 LYS B CE  
4391  N NZ  . LYS B 127 ? 1.3003 1.0195 1.0798 0.0655  0.0348  0.0535  428 LYS B NZ  
4392  N N   . LEU B 128 ? 0.6775 0.4831 0.5358 -0.0017 0.0363  0.0435  429 LEU B N   
4393  C CA  . LEU B 128 ? 0.6194 0.4454 0.4901 0.0034  0.0317  0.0425  429 LEU B CA  
4394  C C   . LEU B 128 ? 0.6266 0.4524 0.4909 0.0066  0.0329  0.0456  429 LEU B C   
4395  O O   . LEU B 128 ? 0.6346 0.4565 0.4936 -0.0001 0.0377  0.0476  429 LEU B O   
4396  C CB  . LEU B 128 ? 0.4293 0.2735 0.3153 -0.0035 0.0305  0.0392  429 LEU B CB  
4397  C CG  . LEU B 128 ? 0.4856 0.3460 0.3814 0.0004  0.0264  0.0379  429 LEU B CG  
4398  C CD1 . LEU B 128 ? 0.4194 0.2850 0.3202 0.0064  0.0211  0.0365  429 LEU B CD1 
4399  C CD2 . LEU B 128 ? 0.4805 0.3547 0.3866 -0.0054 0.0268  0.0358  429 LEU B CD2 
4400  N N   . GLN B 129 ? 0.6069 0.4385 0.4712 0.0160  0.0287  0.0459  430 GLN B N   
4401  C CA  . GLN B 129 ? 0.6485 0.4818 0.5066 0.0196  0.0292  0.0481  430 GLN B CA  
4402  C C   . GLN B 129 ? 0.5756 0.4260 0.4453 0.0167  0.0273  0.0449  430 GLN B C   
4403  O O   . GLN B 129 ? 0.6837 0.5447 0.5640 0.0174  0.0227  0.0414  430 GLN B O   
4404  C CB  . GLN B 129 ? 0.7057 0.5386 0.5571 0.0310  0.0252  0.0494  430 GLN B CB  
4405  C CG  . GLN B 129 ? 0.8189 0.6513 0.6603 0.0355  0.0258  0.0522  430 GLN B CG  
4406  C CD  . GLN B 129 ? 0.8438 0.6589 0.6707 0.0321  0.0327  0.0574  430 GLN B CD  
4407  O OE1 . GLN B 129 ? 0.8360 0.6327 0.6532 0.0310  0.0360  0.0601  430 GLN B OE1 
4408  N NE2 . GLN B 129 ? 0.9629 0.7828 0.7868 0.0298  0.0352  0.0586  430 GLN B NE2 
4409  N N   . VAL B 130 ? 0.6067 0.4591 0.4730 0.0134  0.0313  0.0461  431 VAL B N   
4410  C CA  . VAL B 130 ? 0.5384 0.4057 0.4133 0.0123  0.0305  0.0430  431 VAL B CA  
4411  C C   . VAL B 130 ? 0.5911 0.4605 0.4582 0.0186  0.0298  0.0434  431 VAL B C   
4412  O O   . VAL B 130 ? 0.6135 0.4776 0.4698 0.0184  0.0343  0.0472  431 VAL B O   
4413  C CB  . VAL B 130 ? 0.5491 0.4231 0.4279 0.0039  0.0358  0.0432  431 VAL B CB  
4414  C CG1 . VAL B 130 ? 0.4238 0.3140 0.3100 0.0063  0.0348  0.0399  431 VAL B CG1 
4415  C CG2 . VAL B 130 ? 0.6630 0.5355 0.5485 -0.0030 0.0361  0.0422  431 VAL B CG2 
4416  N N   . PHE B 131 ? 0.6320 0.5082 0.5032 0.0233  0.0244  0.0394  432 PHE B N   
4417  C CA  . PHE B 131 ? 0.5185 0.3974 0.3821 0.0290  0.0229  0.0382  432 PHE B CA  
4418  C C   . PHE B 131 ? 0.6193 0.5068 0.4868 0.0291  0.0238  0.0345  432 PHE B C   
4419  O O   . PHE B 131 ? 0.6684 0.5585 0.5431 0.0293  0.0200  0.0304  432 PHE B O   
4420  C CB  . PHE B 131 ? 0.5327 0.4122 0.3958 0.0334  0.0158  0.0355  432 PHE B CB  
4421  C CG  . PHE B 131 ? 0.5467 0.4214 0.4051 0.0363  0.0148  0.0390  432 PHE B CG  
4422  C CD1 . PHE B 131 ? 0.4563 0.3238 0.3019 0.0402  0.0183  0.0440  432 PHE B CD1 
4423  C CD2 . PHE B 131 ? 0.5554 0.4328 0.4208 0.0360  0.0105  0.0377  432 PHE B CD2 
4424  C CE1 . PHE B 131 ? 0.5221 0.3832 0.3610 0.0455  0.0174  0.0476  432 PHE B CE1 
4425  C CE2 . PHE B 131 ? 0.5706 0.4453 0.4310 0.0411  0.0097  0.0408  432 PHE B CE2 
4426  C CZ  . PHE B 131 ? 0.5339 0.3996 0.3807 0.0467  0.0130  0.0457  432 PHE B CZ  
4427  N N   . ASP B 132 ? 0.6156 0.5073 0.4770 0.0296  0.0292  0.0363  433 ASP B N   
4428  C CA  . ASP B 132 ? 0.5944 0.4965 0.4572 0.0327  0.0306  0.0327  433 ASP B CA  
4429  C C   . ASP B 132 ? 0.5590 0.4586 0.4146 0.0402  0.0257  0.0280  433 ASP B C   
4430  O O   . ASP B 132 ? 0.5957 0.4932 0.4408 0.0434  0.0258  0.0292  433 ASP B O   
4431  C CB  . ASP B 132 ? 0.4751 0.3857 0.3335 0.0303  0.0384  0.0363  433 ASP B CB  
4432  C CG  . ASP B 132 ? 0.5603 0.4867 0.4225 0.0339  0.0408  0.0327  433 ASP B CG  
4433  O OD1 . ASP B 132 ? 0.5684 0.4943 0.4321 0.0409  0.0360  0.0272  433 ASP B OD1 
4434  O OD2 . ASP B 132 ? 0.6202 0.5595 0.4829 0.0300  0.0475  0.0354  433 ASP B OD2 
4435  N N   . ALA B 133 ? 0.6286 0.5268 0.4881 0.0426  0.0211  0.0227  434 ALA B N   
4436  C CA  . ALA B 133 ? 0.6322 0.5254 0.4830 0.0484  0.0164  0.0170  434 ALA B CA  
4437  C C   . ALA B 133 ? 0.5585 0.4550 0.4074 0.0548  0.0179  0.0127  434 ALA B C   
4438  O O   . ALA B 133 ? 0.4899 0.3772 0.3328 0.0589  0.0132  0.0069  434 ALA B O   
4439  C CB  . ALA B 133 ? 0.4517 0.3359 0.3048 0.0453  0.0090  0.0141  434 ALA B CB  
4440  N N   . ARG B 134 ? 0.4574 0.3671 0.3103 0.0556  0.0244  0.0152  435 ARG B N   
4441  C CA  . ARG B 134 ? 0.6009 0.5176 0.4529 0.0637  0.0261  0.0113  435 ARG B CA  
4442  C C   . ARG B 134 ? 0.6819 0.5987 0.5203 0.0729  0.0267  0.0069  435 ARG B C   
4443  O O   . ARG B 134 ? 0.7574 0.6786 0.5924 0.0823  0.0278  0.0027  435 ARG B O   
4444  C CB  . ARG B 134 ? 0.5790 0.5155 0.4408 0.0610  0.0328  0.0152  435 ARG B CB  
4445  C CG  . ARG B 134 ? 0.6154 0.5530 0.4897 0.0553  0.0314  0.0169  435 ARG B CG  
4446  C CD  . ARG B 134 ? 0.5397 0.4994 0.4230 0.0508  0.0379  0.0202  435 ARG B CD  
4447  N NE  . ARG B 134 ? 0.5084 0.4715 0.3890 0.0423  0.0432  0.0251  435 ARG B NE  
4448  C CZ  . ARG B 134 ? 0.4572 0.4390 0.3420 0.0359  0.0500  0.0283  435 ARG B CZ  
4449  N NH1 . ARG B 134 ? 0.4733 0.4768 0.3669 0.0381  0.0520  0.0266  435 ARG B NH1 
4450  N NH2 . ARG B 134 ? 0.4567 0.4359 0.3358 0.0273  0.0548  0.0334  435 ARG B NH2 
4451  N N   . ASP B 135 ? 0.6964 0.6087 0.5259 0.0716  0.0259  0.0076  436 ASP B N   
4452  C CA  . ASP B 135 ? 0.6706 0.5814 0.4855 0.0799  0.0255  0.0027  436 ASP B CA  
4453  C C   . ASP B 135 ? 0.6922 0.5841 0.4981 0.0818  0.0173  -0.0045 436 ASP B C   
4454  O O   . ASP B 135 ? 0.6127 0.5004 0.4047 0.0884  0.0158  -0.0101 436 ASP B O   
4455  C CB  . ASP B 135 ? 0.6322 0.5494 0.4403 0.0778  0.0291  0.0075  436 ASP B CB  
4456  C CG  . ASP B 135 ? 0.7394 0.6463 0.5465 0.0717  0.0240  0.0099  436 ASP B CG  
4457  O OD1 . ASP B 135 ? 0.7205 0.6190 0.5354 0.0671  0.0189  0.0090  436 ASP B OD1 
4458  O OD2 . ASP B 135 ? 0.7023 0.6109 0.5004 0.0723  0.0252  0.0130  436 ASP B OD2 
4459  N N   . CYS B 136 ? 0.6416 0.5227 0.4545 0.0752  0.0120  -0.0045 437 CYS B N   
4460  C CA  . CYS B 136 ? 0.6562 0.5198 0.4610 0.0733  0.0041  -0.0107 437 CYS B CA  
4461  C C   . CYS B 136 ? 0.6890 0.5394 0.4817 0.0822  0.0026  -0.0184 437 CYS B C   
4462  O O   . CYS B 136 ? 0.7020 0.5552 0.4978 0.0889  0.0061  -0.0182 437 CYS B O   
4463  C CB  . CYS B 136 ? 0.6250 0.4827 0.4408 0.0639  0.0001  -0.0082 437 CYS B CB  
4464  S SG  . CYS B 136 ? 0.6375 0.4811 0.4465 0.0558  -0.0091 -0.0134 437 CYS B SG  
4465  N N   . THR B 137 ? 0.6200 0.4557 0.3975 0.0828  -0.0028 -0.0258 438 THR B N   
4466  C CA  . THR B 137 ? 0.6464 0.4629 0.4084 0.0912  -0.0048 -0.0339 438 THR B CA  
4467  C C   . THR B 137 ? 0.5934 0.3838 0.3453 0.0835  -0.0129 -0.0400 438 THR B C   
4468  O O   . THR B 137 ? 0.7137 0.4825 0.4535 0.0894  -0.0144 -0.0452 438 THR B O   
4469  C CB  . THR B 137 ? 0.6587 0.4785 0.4052 0.1021  -0.0025 -0.0394 438 THR B CB  
4470  O OG1 . THR B 137 ? 0.6700 0.4823 0.4047 0.0965  -0.0081 -0.0445 438 THR B OG1 
4471  C CG2 . THR B 137 ? 0.6112 0.4586 0.3664 0.1064  0.0057  -0.0328 438 THR B CG2 
4472  N N   . THR B 138 ? 0.6622 0.4536 0.4170 0.0709  -0.0180 -0.0396 439 THR B N   
4473  C CA  . THR B 138 ? 0.6069 0.3760 0.3511 0.0611  -0.0255 -0.0458 439 THR B CA  
4474  C C   . THR B 138 ? 0.5890 0.3651 0.3484 0.0468  -0.0286 -0.0405 439 THR B C   
4475  O O   . THR B 138 ? 0.6873 0.4851 0.4629 0.0451  -0.0258 -0.0331 439 THR B O   
4476  C CB  . THR B 138 ? 0.6840 0.4490 0.4121 0.0586  -0.0303 -0.0539 439 THR B CB  
4477  O OG1 . THR B 138 ? 0.7092 0.4977 0.4480 0.0516  -0.0317 -0.0496 439 THR B OG1 
4478  C CG2 . THR B 138 ? 0.7038 0.4679 0.4176 0.0735  -0.0266 -0.0588 439 THR B CG2 
4479  N N   . ALA B 139 ? 0.7932 0.5496 0.5453 0.0362  -0.0344 -0.0446 440 ALA B N   
4480  C CA  . ALA B 139 ? 0.6527 0.4172 0.4180 0.0218  -0.0375 -0.0402 440 ALA B CA  
4481  C C   . ALA B 139 ? 0.7062 0.4954 0.4787 0.0159  -0.0400 -0.0392 440 ALA B C   
4482  O O   . ALA B 139 ? 0.6636 0.4709 0.4522 0.0104  -0.0397 -0.0329 440 ALA B O   
4483  C CB  . ALA B 139 ? 0.6148 0.3530 0.3681 0.0099  -0.0430 -0.0451 440 ALA B CB  
4484  N N   . HIS B 140 ? 0.7283 0.5191 0.4881 0.0184  -0.0425 -0.0454 441 HIS B N   
4485  C CA  . HIS B 140 ? 0.6854 0.5018 0.4508 0.0166  -0.0445 -0.0437 441 HIS B CA  
4486  C C   . HIS B 140 ? 0.6191 0.4548 0.3980 0.0260  -0.0379 -0.0344 441 HIS B C   
4487  O O   . HIS B 140 ? 0.6197 0.4741 0.4106 0.0229  -0.0384 -0.0288 441 HIS B O   
4488  C CB  . HIS B 140 ? 0.7083 0.5224 0.4558 0.0195  -0.0478 -0.0520 441 HIS B CB  
4489  C CG  . HIS B 140 ? 0.7072 0.5126 0.4434 0.0055  -0.0562 -0.0608 441 HIS B CG  
4490  N ND1 . HIS B 140 ? 0.7192 0.4933 0.4376 0.0013  -0.0588 -0.0692 441 HIS B ND1 
4491  C CD2 . HIS B 140 ? 0.7290 0.5531 0.4678 -0.0055 -0.0625 -0.0628 441 HIS B CD2 
4492  C CE1 . HIS B 140 ? 0.7468 0.5192 0.4572 -0.0140 -0.0663 -0.0762 441 HIS B CE1 
4493  N NE2 . HIS B 140 ? 0.7239 0.5292 0.4475 -0.0184 -0.0688 -0.0726 441 HIS B NE2 
4494  N N   . GLY B 141 ? 0.6155 0.4470 0.3915 0.0375  -0.0316 -0.0329 442 GLY B N   
4495  C CA  . GLY B 141 ? 0.5360 0.3824 0.3241 0.0436  -0.0249 -0.0239 442 GLY B CA  
4496  C C   . GLY B 141 ? 0.6982 0.5486 0.5029 0.0378  -0.0237 -0.0175 442 GLY B C   
4497  O O   . GLY B 141 ? 0.6674 0.5318 0.4817 0.0378  -0.0215 -0.0109 442 GLY B O   
4498  N N   . MET B 142 ? 0.5199 0.3563 0.3264 0.0332  -0.0252 -0.0194 443 MET B N   
4499  C CA  . MET B 142 ? 0.5554 0.3958 0.3769 0.0278  -0.0240 -0.0136 443 MET B CA  
4500  C C   . MET B 142 ? 0.5699 0.4232 0.3988 0.0190  -0.0282 -0.0119 443 MET B C   
4501  O O   . MET B 142 ? 0.5919 0.4569 0.4332 0.0183  -0.0259 -0.0058 443 MET B O   
4502  C CB  . MET B 142 ? 0.5116 0.3332 0.3306 0.0248  -0.0253 -0.0158 443 MET B CB  
4503  C CG  . MET B 142 ? 0.6180 0.4306 0.4331 0.0352  -0.0207 -0.0161 443 MET B CG  
4504  S SD  . MET B 142 ? 0.6974 0.4842 0.5053 0.0324  -0.0236 -0.0185 443 MET B SD  
4505  C CE  . MET B 142 ? 0.6732 0.4724 0.5008 0.0272  -0.0212 -0.0100 443 MET B CE  
4506  N N   . PHE B 143 ? 0.5981 0.4506 0.4189 0.0123  -0.0345 -0.0177 444 PHE B N   
4507  C CA  . PHE B 143 ? 0.5440 0.4146 0.3716 0.0047  -0.0389 -0.0167 444 PHE B CA  
4508  C C   . PHE B 143 ? 0.6305 0.5202 0.4620 0.0130  -0.0368 -0.0118 444 PHE B C   
4509  O O   . PHE B 143 ? 0.5931 0.4978 0.4353 0.0123  -0.0366 -0.0069 444 PHE B O   
4510  C CB  . PHE B 143 ? 0.5528 0.4202 0.3693 -0.0049 -0.0462 -0.0249 444 PHE B CB  
4511  C CG  . PHE B 143 ? 0.6061 0.4986 0.4288 -0.0118 -0.0512 -0.0248 444 PHE B CG  
4512  C CD1 . PHE B 143 ? 0.5872 0.4919 0.4228 -0.0203 -0.0523 -0.0214 444 PHE B CD1 
4513  C CD2 . PHE B 143 ? 0.5241 0.4305 0.3395 -0.0091 -0.0550 -0.0283 444 PHE B CD2 
4514  C CE1 . PHE B 143 ? 0.5982 0.5302 0.4399 -0.0256 -0.0569 -0.0216 444 PHE B CE1 
4515  C CE2 . PHE B 143 ? 0.5202 0.4537 0.3415 -0.0140 -0.0600 -0.0283 444 PHE B CE2 
4516  C CZ  . PHE B 143 ? 0.6028 0.5501 0.4378 -0.0221 -0.0609 -0.0250 444 PHE B CZ  
4517  N N   . ASN B 144 ? 0.6792 0.5676 0.5006 0.0216  -0.0350 -0.0129 445 ASN B N   
4518  C CA  . ASN B 144 ? 0.6490 0.5514 0.4707 0.0301  -0.0324 -0.0073 445 ASN B CA  
4519  C C   . ASN B 144 ? 0.6430 0.5458 0.4754 0.0337  -0.0259 0.0008  445 ASN B C   
4520  O O   . ASN B 144 ? 0.5708 0.4847 0.4083 0.0360  -0.0257 0.0059  445 ASN B O   
4521  C CB  . ASN B 144 ? 0.6558 0.5544 0.4636 0.0382  -0.0304 -0.0094 445 ASN B CB  
4522  C CG  . ASN B 144 ? 0.7408 0.6514 0.5453 0.0468  -0.0279 -0.0030 445 ASN B CG  
4523  O OD1 . ASN B 144 ? 0.6945 0.6011 0.4935 0.0538  -0.0217 0.0008  445 ASN B OD1 
4524  N ND2 . ASN B 144 ? 0.7576 0.6836 0.5646 0.0464  -0.0325 -0.0016 445 ASN B ND2 
4525  N N   . TYR B 145 ? 0.5960 0.4869 0.4308 0.0344  -0.0209 0.0018  446 TYR B N   
4526  C CA  . TYR B 145 ? 0.6335 0.5247 0.4775 0.0361  -0.0149 0.0087  446 TYR B CA  
4527  C C   . TYR B 145 ? 0.5657 0.4624 0.4212 0.0305  -0.0171 0.0108  446 TYR B C   
4528  O O   . TYR B 145 ? 0.5397 0.4412 0.3998 0.0330  -0.0144 0.0161  446 TYR B O   
4529  C CB  . TYR B 145 ? 0.6566 0.5385 0.5020 0.0371  -0.0102 0.0083  446 TYR B CB  
4530  C CG  . TYR B 145 ? 0.5841 0.4666 0.4226 0.0438  -0.0043 0.0103  446 TYR B CG  
4531  C CD1 . TYR B 145 ? 0.4974 0.3838 0.3374 0.0455  0.0012  0.0172  446 TYR B CD1 
4532  C CD2 . TYR B 145 ? 0.6128 0.4911 0.4419 0.0482  -0.0038 0.0054  446 TYR B CD2 
4533  C CE1 . TYR B 145 ? 0.4964 0.3843 0.3298 0.0495  0.0072  0.0197  446 TYR B CE1 
4534  C CE2 . TYR B 145 ? 0.4814 0.3637 0.3047 0.0540  0.0022  0.0075  446 TYR B CE2 
4535  C CZ  . TYR B 145 ? 0.5457 0.4337 0.3717 0.0537  0.0078  0.0150  446 TYR B CZ  
4536  O OH  . TYR B 145 ? 0.6687 0.5616 0.4884 0.0574  0.0144  0.0179  446 TYR B OH  
4537  N N   . ILE B 146 ? 0.5063 0.4013 0.3647 0.0228  -0.0219 0.0065  447 ILE B N   
4538  C CA  . ILE B 146 ? 0.6150 0.5168 0.4843 0.0167  -0.0235 0.0084  447 ILE B CA  
4539  C C   . ILE B 146 ? 0.6360 0.5558 0.5074 0.0182  -0.0266 0.0099  447 ILE B C   
4540  O O   . ILE B 146 ? 0.6025 0.5304 0.4818 0.0195  -0.0251 0.0140  447 ILE B O   
4541  C CB  . ILE B 146 ? 0.6114 0.5049 0.4806 0.0071  -0.0274 0.0039  447 ILE B CB  
4542  C CG1 . ILE B 146 ? 0.5665 0.4436 0.4350 0.0089  -0.0236 0.0042  447 ILE B CG1 
4543  C CG2 . ILE B 146 ? 0.5146 0.4198 0.3932 -0.0010 -0.0302 0.0052  447 ILE B CG2 
4544  C CD1 . ILE B 146 ? 0.5247 0.3873 0.3891 0.0014  -0.0268 0.0005  447 ILE B CD1 
4545  N N   . CYS B 147 ? 0.4801 0.4074 0.3435 0.0194  -0.0308 0.0066  448 CYS B N   
4546  C CA  . CYS B 147 ? 0.4595 0.4074 0.3241 0.0229  -0.0342 0.0080  448 CYS B CA  
4547  C C   . CYS B 147 ? 0.5690 0.5171 0.4320 0.0348  -0.0292 0.0149  448 CYS B C   
4548  O O   . CYS B 147 ? 0.5423 0.5027 0.4102 0.0389  -0.0296 0.0182  448 CYS B O   
4549  C CB  . CYS B 147 ? 0.5923 0.5487 0.4472 0.0224  -0.0398 0.0028  448 CYS B CB  
4550  S SG  . CYS B 147 ? 0.5798 0.5407 0.4353 0.0061  -0.0473 -0.0055 448 CYS B SG  
4551  N N   . ASN B 148 ? 0.5555 0.4898 0.4102 0.0405  -0.0244 0.0171  449 ASN B N   
4552  C CA  . ASN B 148 ? 0.5387 0.4680 0.3891 0.0497  -0.0190 0.0241  449 ASN B CA  
4553  C C   . ASN B 148 ? 0.5324 0.4558 0.3920 0.0477  -0.0151 0.0275  449 ASN B C   
4554  O O   . ASN B 148 ? 0.5028 0.4277 0.3615 0.0540  -0.0135 0.0318  449 ASN B O   
4555  C CB  . ASN B 148 ? 0.4610 0.3775 0.3011 0.0532  -0.0139 0.0259  449 ASN B CB  
4556  C CG  . ASN B 148 ? 0.6700 0.5920 0.4989 0.0561  -0.0176 0.0222  449 ASN B CG  
4557  O OD1 . ASN B 148 ? 0.4770 0.4131 0.3037 0.0579  -0.0237 0.0200  449 ASN B OD1 
4558  N ND2 . ASN B 148 ? 0.5251 0.4381 0.3471 0.0566  -0.0141 0.0210  449 ASN B ND2 
4559  N N   . HIS B 149 ? 0.5354 0.4517 0.4025 0.0398  -0.0136 0.0252  450 HIS B N   
4560  C CA  . HIS B 149 ? 0.5497 0.4623 0.4257 0.0369  -0.0105 0.0275  450 HIS B CA  
4561  C C   . HIS B 149 ? 0.4481 0.3746 0.3303 0.0377  -0.0140 0.0278  450 HIS B C   
4562  O O   . HIS B 149 ? 0.4502 0.3757 0.3320 0.0434  -0.0114 0.0315  450 HIS B O   
4563  C CB  . HIS B 149 ? 0.5319 0.4384 0.4147 0.0289  -0.0101 0.0246  450 HIS B CB  
4564  C CG  . HIS B 149 ? 0.5508 0.4549 0.4423 0.0257  -0.0073 0.0266  450 HIS B CG  
4565  N ND1 . HIS B 149 ? 0.6019 0.4977 0.4961 0.0231  -0.0032 0.0271  450 HIS B ND1 
4566  C CD2 . HIS B 149 ? 0.5331 0.4440 0.4309 0.0250  -0.0080 0.0279  450 HIS B CD2 
4567  C CE1 . HIS B 149 ? 0.5959 0.4925 0.4973 0.0203  -0.0019 0.0285  450 HIS B CE1 
4568  N NE2 . HIS B 149 ? 0.5782 0.4829 0.4815 0.0217  -0.0045 0.0290  450 HIS B NE2 
4569  N N   . VAL B 150 ? 0.4830 0.4229 0.3698 0.0320  -0.0198 0.0237  451 VAL B N   
4570  C CA  . VAL B 150 ? 0.4138 0.3722 0.3078 0.0314  -0.0230 0.0237  451 VAL B CA  
4571  C C   . VAL B 150 ? 0.5909 0.5594 0.4796 0.0440  -0.0231 0.0269  451 VAL B C   
4572  O O   . VAL B 150 ? 0.4791 0.4548 0.3715 0.0491  -0.0221 0.0292  451 VAL B O   
4573  C CB  . VAL B 150 ? 0.4143 0.3861 0.3120 0.0210  -0.0292 0.0186  451 VAL B CB  
4574  C CG1 . VAL B 150 ? 0.4110 0.4092 0.3160 0.0205  -0.0328 0.0184  451 VAL B CG1 
4575  C CG2 . VAL B 150 ? 0.4110 0.3689 0.3125 0.0100  -0.0284 0.0165  451 VAL B CG2 
4576  N N   . LYS B 151 ? 0.5992 0.5671 0.4774 0.0505  -0.0243 0.0274  452 LYS B N   
4577  C CA  . LYS B 151 ? 0.5225 0.4995 0.3931 0.0642  -0.0250 0.0310  452 LYS B CA  
4578  C C   . LYS B 151 ? 0.5356 0.4924 0.3991 0.0730  -0.0184 0.0368  452 LYS B C   
4579  O O   . LYS B 151 ? 0.5486 0.5104 0.4100 0.0831  -0.0181 0.0396  452 LYS B O   
4580  C CB  . LYS B 151 ? 0.5849 0.5656 0.4445 0.0688  -0.0279 0.0303  452 LYS B CB  
4581  C CG  . LYS B 151 ? 0.4630 0.4565 0.3138 0.0841  -0.0299 0.0341  452 LYS B CG  
4582  C CD  . LYS B 151 ? 0.5440 0.5466 0.3850 0.0870  -0.0342 0.0322  452 LYS B CD  
4583  C CE  . LYS B 151 ? 0.4855 0.5063 0.3182 0.1031  -0.0376 0.0356  452 LYS B CE  
4584  N NZ  . LYS B 151 ? 0.6395 0.6757 0.4646 0.1041  -0.0433 0.0325  452 LYS B NZ  
4585  N N   . TYR B 152 ? 0.5032 0.4373 0.3616 0.0695  -0.0131 0.0386  453 TYR B N   
4586  C CA  . TYR B 152 ? 0.5357 0.4487 0.3870 0.0738  -0.0066 0.0436  453 TYR B CA  
4587  C C   . TYR B 152 ? 0.5336 0.4471 0.3940 0.0716  -0.0055 0.0428  453 TYR B C   
4588  O O   . TYR B 152 ? 0.5208 0.4273 0.3746 0.0806  -0.0033 0.0458  453 TYR B O   
4589  C CB  . TYR B 152 ? 0.5651 0.4599 0.4127 0.0668  -0.0013 0.0445  453 TYR B CB  
4590  C CG  . TYR B 152 ? 0.6093 0.4826 0.4503 0.0670  0.0054  0.0489  453 TYR B CG  
4591  C CD1 . TYR B 152 ? 0.6171 0.4861 0.4675 0.0595  0.0076  0.0472  453 TYR B CD1 
4592  C CD2 . TYR B 152 ? 0.5581 0.4147 0.3819 0.0742  0.0093  0.0546  453 TYR B CD2 
4593  C CE1 . TYR B 152 ? 0.6291 0.4783 0.4722 0.0582  0.0134  0.0503  453 TYR B CE1 
4594  C CE2 . TYR B 152 ? 0.6083 0.4423 0.4236 0.0723  0.0155  0.0582  453 TYR B CE2 
4595  C CZ  . TYR B 152 ? 0.6788 0.5097 0.5043 0.0639  0.0174  0.0556  453 TYR B CZ  
4596  O OH  . TYR B 152 ? 0.8015 0.6097 0.6175 0.0605  0.0232  0.0584  453 TYR B OH  
4597  N N   . ALA B 153 ? 0.4327 0.3532 0.3065 0.0604  -0.0068 0.0389  454 ALA B N   
4598  C CA  . ALA B 153 ? 0.5591 0.4798 0.4415 0.0569  -0.0053 0.0382  454 ALA B CA  
4599  C C   . ALA B 153 ? 0.5109 0.4493 0.3958 0.0650  -0.0082 0.0381  454 ALA B C   
4600  O O   . ALA B 153 ? 0.5588 0.4909 0.4413 0.0706  -0.0053 0.0395  454 ALA B O   
4601  C CB  . ALA B 153 ? 0.4099 0.3358 0.3045 0.0441  -0.0069 0.0345  454 ALA B CB  
4602  N N   . THR B 154 ? 0.5238 0.4859 0.4130 0.0654  -0.0138 0.0360  455 THR B N   
4603  C CA  . THR B 154 ? 0.4906 0.4772 0.3839 0.0729  -0.0169 0.0355  455 THR B CA  
4604  C C   . THR B 154 ? 0.5533 0.5342 0.4333 0.0910  -0.0152 0.0394  455 THR B C   
4605  O O   . THR B 154 ? 0.4758 0.4615 0.3555 0.0998  -0.0140 0.0401  455 THR B O   
4606  C CB  . THR B 154 ? 0.5073 0.5214 0.4069 0.0676  -0.0235 0.0322  455 THR B CB  
4607  O OG1 . THR B 154 ? 0.4071 0.4207 0.3158 0.0508  -0.0249 0.0288  455 THR B OG1 
4608  C CG2 . THR B 154 ? 0.4173 0.4640 0.3227 0.0747  -0.0270 0.0316  455 THR B CG2 
4609  N N   . ASN B 155 ? 0.6706 0.6403 0.5377 0.0979  -0.0150 0.0422  456 ASN B N   
4610  C CA  . ASN B 155 ? 0.6140 0.5700 0.4640 0.1156  -0.0126 0.0471  456 ASN B CA  
4611  C C   . ASN B 155 ? 0.6002 0.5814 0.4514 0.1301  -0.0158 0.0469  456 ASN B C   
4612  O O   . ASN B 155 ? 0.5110 0.4798 0.3524 0.1432  -0.0127 0.0493  456 ASN B O   
4613  C CB  . ASN B 155 ? 0.5902 0.5108 0.4308 0.1149  -0.0055 0.0498  456 ASN B CB  
4614  C CG  . ASN B 155 ? 0.7027 0.5988 0.5206 0.1303  -0.0022 0.0556  456 ASN B CG  
4615  O OD1 . ASN B 155 ? 0.6272 0.5247 0.4347 0.1382  -0.0039 0.0587  456 ASN B OD1 
4616  N ND2 . ASN B 155 ? 0.6115 0.4832 0.4197 0.1347  0.0026  0.0571  456 ASN B ND2 
4617  N N   . LYS B 156 ? 0.5790 0.5966 0.4419 0.1273  -0.0220 0.0436  457 LYS B N   
4618  C CA  . LYS B 156 ? 0.6001 0.6512 0.4666 0.1402  -0.0258 0.0429  457 LYS B CA  
4619  C C   . LYS B 156 ? 0.5754 0.6281 0.4474 0.1432  -0.0226 0.0421  457 LYS B C   
4620  O O   . LYS B 156 ? 0.6034 0.6662 0.4693 0.1615  -0.0225 0.0434  457 LYS B O   
4621  C CB  . LYS B 156 ? 0.4922 0.5420 0.3410 0.1624  -0.0268 0.0474  457 LYS B CB  
4622  C CG  . LYS B 156 ? 0.4943 0.5579 0.3400 0.1613  -0.0319 0.0473  457 LYS B CG  
4623  C CD  . LYS B 156 ? 0.5476 0.6029 0.3720 0.1847  -0.0320 0.0532  457 LYS B CD  
4624  C CE  . LYS B 156 ? 0.7668 0.8395 0.5872 0.1854  -0.0375 0.0530  457 LYS B CE  
4625  N NZ  . LYS B 156 ? 0.8821 0.9433 0.6795 0.2095  -0.0370 0.0600  457 LYS B NZ  
4626  N N   . GLY B 157 ? 0.6161 0.6594 0.4987 0.1264  -0.0201 0.0397  458 GLY B N   
4627  C CA  . GLY B 157 ? 0.4642 0.5111 0.3530 0.1267  -0.0174 0.0382  458 GLY B CA  
4628  C C   . GLY B 157 ? 0.5574 0.5647 0.4342 0.1305  -0.0110 0.0400  458 GLY B C   
4629  O O   . GLY B 157 ? 0.6167 0.6218 0.4996 0.1251  -0.0085 0.0380  458 GLY B O   
4630  N N   . ASN B 158 ? 0.5940 0.5704 0.4530 0.1387  -0.0084 0.0437  459 ASN B N   
4631  C CA  . ASN B 158 ? 0.6122 0.5485 0.4587 0.1380  -0.0022 0.0451  459 ASN B CA  
4632  C C   . ASN B 158 ? 0.6706 0.5916 0.5238 0.1179  -0.0003 0.0444  459 ASN B C   
4633  O O   . ASN B 158 ? 0.6692 0.5678 0.5123 0.1152  0.0019  0.0472  459 ASN B O   
4634  C CB  . ASN B 158 ? 0.6361 0.5447 0.4584 0.1547  0.0002  0.0499  459 ASN B CB  
4635  C CG  . ASN B 158 ? 0.7862 0.6515 0.5932 0.1524  0.0067  0.0512  459 ASN B CG  
4636  O OD1 . ASN B 158 ? 0.8873 0.7479 0.7010 0.1438  0.0089  0.0477  459 ASN B OD1 
4637  N ND2 . ASN B 158 ? 0.8513 0.6850 0.6368 0.1589  0.0097  0.0561  459 ASN B ND2 
4638  N N   . LEU B 159 ? 0.5206 0.4544 0.3902 0.1042  -0.0009 0.0408  460 LEU B N   
4639  C CA  . LEU B 159 ? 0.5256 0.4539 0.4039 0.0868  -0.0007 0.0398  460 LEU B CA  
4640  C C   . LEU B 159 ? 0.6509 0.5458 0.5188 0.0823  0.0047  0.0415  460 LEU B C   
4641  O O   . LEU B 159 ? 0.6294 0.5043 0.4867 0.0873  0.0086  0.0422  460 LEU B O   
4642  C CB  . LEU B 159 ? 0.4384 0.3832 0.3332 0.0747  -0.0020 0.0364  460 LEU B CB  
4643  C CG  . LEU B 159 ? 0.6213 0.6009 0.5270 0.0759  -0.0066 0.0347  460 LEU B CG  
4644  C CD1 . LEU B 159 ? 0.6525 0.6449 0.5725 0.0615  -0.0076 0.0324  460 LEU B CD1 
4645  C CD2 . LEU B 159 ? 0.5802 0.5752 0.4859 0.0772  -0.0112 0.0349  460 LEU B CD2 
4646  N N   . ARG B 160 ? 0.4451 0.3350 0.3157 0.0722  0.0049  0.0418  461 ARG B N   
4647  C CA  . ARG B 160 ? 0.4931 0.3581 0.3564 0.0654  0.0099  0.0434  461 ARG B CA  
4648  C C   . ARG B 160 ? 0.4620 0.3337 0.3385 0.0514  0.0095  0.0409  461 ARG B C   
4649  O O   . ARG B 160 ? 0.5343 0.4229 0.4201 0.0481  0.0054  0.0391  461 ARG B O   
4650  C CB  . ARG B 160 ? 0.5050 0.3561 0.3537 0.0704  0.0116  0.0475  461 ARG B CB  
4651  C CG  . ARG B 160 ? 0.6729 0.5123 0.5044 0.0858  0.0124  0.0511  461 ARG B CG  
4652  C CD  . ARG B 160 ? 0.6635 0.4902 0.4800 0.0901  0.0139  0.0559  461 ARG B CD  
4653  N NE  . ARG B 160 ? 0.5887 0.4391 0.4110 0.0934  0.0086  0.0552  461 ARG B NE  
4654  C CZ  . ARG B 160 ? 0.6682 0.5149 0.4772 0.1020  0.0081  0.0591  461 ARG B CZ  
4655  N NH1 . ARG B 160 ? 0.5401 0.3588 0.3288 0.1077  0.0131  0.0648  461 ARG B NH1 
4656  N NH2 . ARG B 160 ? 0.6006 0.4704 0.4148 0.1042  0.0027  0.0575  461 ARG B NH2 
4657  N N   . SER B 161 ? 0.5889 0.4470 0.4650 0.0433  0.0136  0.0406  462 SER B N   
4658  C CA  . SER B 161 ? 0.6313 0.4975 0.5197 0.0324  0.0131  0.0383  462 SER B CA  
4659  C C   . SER B 161 ? 0.6000 0.4645 0.4867 0.0292  0.0138  0.0393  462 SER B C   
4660  O O   . SER B 161 ? 0.5372 0.3887 0.4130 0.0303  0.0176  0.0421  462 SER B O   
4661  C CB  . SER B 161 ? 0.5849 0.4426 0.4749 0.0253  0.0165  0.0371  462 SER B CB  
4662  O OG  . SER B 161 ? 0.6463 0.5065 0.5374 0.0290  0.0157  0.0356  462 SER B OG  
4663  N N   . ALA B 162 ? 0.5200 0.3966 0.4160 0.0251  0.0107  0.0370  463 ALA B N   
4664  C CA  . ALA B 162 ? 0.4740 0.3495 0.3672 0.0238  0.0115  0.0372  463 ALA B CA  
4665  C C   . ALA B 162 ? 0.4785 0.3612 0.3807 0.0184  0.0097  0.0343  463 ALA B C   
4666  O O   . ALA B 162 ? 0.4477 0.3372 0.3577 0.0159  0.0064  0.0324  463 ALA B O   
4667  C CB  . ALA B 162 ? 0.4720 0.3512 0.3586 0.0305  0.0084  0.0377  463 ALA B CB  
4668  N N   . ILE B 163 ? 0.5298 0.4109 0.4297 0.0172  0.0121  0.0342  464 ILE B N   
4669  C CA  . ILE B 163 ? 0.5184 0.4043 0.4231 0.0155  0.0105  0.0315  464 ILE B CA  
4670  C C   . ILE B 163 ? 0.5964 0.4817 0.4936 0.0193  0.0111  0.0309  464 ILE B C   
4671  O O   . ILE B 163 ? 0.5363 0.4186 0.4266 0.0206  0.0151  0.0335  464 ILE B O   
4672  C CB  . ILE B 163 ? 0.4407 0.3295 0.3517 0.0112  0.0135  0.0314  464 ILE B CB  
4673  C CG1 . ILE B 163 ? 0.4341 0.3269 0.3485 0.0122  0.0113  0.0288  464 ILE B CG1 
4674  C CG2 . ILE B 163 ? 0.4473 0.3351 0.3542 0.0091  0.0195  0.0335  464 ILE B CG2 
4675  C CD1 . ILE B 163 ? 0.3819 0.2815 0.3033 0.0095  0.0134  0.0287  464 ILE B CD1 
4676  N N   . THR B 164 ? 0.5539 0.4403 0.4507 0.0207  0.0072  0.0274  465 THR B N   
4677  C CA  . THR B 164 ? 0.5280 0.4136 0.4170 0.0248  0.0073  0.0255  465 THR B CA  
4678  C C   . THR B 164 ? 0.5221 0.4082 0.4131 0.0259  0.0079  0.0228  465 THR B C   
4679  O O   . THR B 164 ? 0.5730 0.4555 0.4667 0.0246  0.0041  0.0205  465 THR B O   
4680  C CB  . THR B 164 ? 0.5089 0.3933 0.3923 0.0264  0.0017  0.0226  465 THR B CB  
4681  O OG1 . THR B 164 ? 0.5710 0.4580 0.4513 0.0282  0.0014  0.0254  465 THR B OG1 
4682  C CG2 . THR B 164 ? 0.5061 0.3881 0.3803 0.0307  0.0013  0.0191  465 THR B CG2 
4683  N N   . ILE B 165 ? 0.4799 0.3706 0.3685 0.0288  0.0126  0.0233  466 ILE B N   
4684  C CA  . ILE B 165 ? 0.4916 0.3867 0.3826 0.0319  0.0139  0.0212  466 ILE B CA  
4685  C C   . ILE B 165 ? 0.6026 0.4955 0.4838 0.0394  0.0133  0.0173  466 ILE B C   
4686  O O   . ILE B 165 ? 0.6242 0.5220 0.4996 0.0419  0.0168  0.0180  466 ILE B O   
4687  C CB  . ILE B 165 ? 0.5658 0.4731 0.4631 0.0291  0.0198  0.0241  466 ILE B CB  
4688  C CG1 . ILE B 165 ? 0.4684 0.3748 0.3728 0.0214  0.0202  0.0270  466 ILE B CG1 
4689  C CG2 . ILE B 165 ? 0.6144 0.5305 0.5155 0.0338  0.0204  0.0219  466 ILE B CG2 
4690  C CD1 . ILE B 165 ? 0.4291 0.3461 0.3384 0.0158  0.0258  0.0293  466 ILE B CD1 
4691  N N   . PHE B 166 ? 0.6636 0.5474 0.5411 0.0429  0.0090  0.0133  467 PHE B N   
4692  C CA  . PHE B 166 ? 0.5087 0.3857 0.3745 0.0507  0.0076  0.0083  467 PHE B CA  
4693  C C   . PHE B 166 ? 0.5690 0.4540 0.4349 0.0593  0.0113  0.0071  467 PHE B C   
4694  O O   . PHE B 166 ? 0.6663 0.5625 0.5422 0.0581  0.0139  0.0101  467 PHE B O   
4695  C CB  . PHE B 166 ? 0.5590 0.4180 0.4181 0.0488  0.0009  0.0044  467 PHE B CB  
4696  C CG  . PHE B 166 ? 0.5807 0.4370 0.4387 0.0416  -0.0029 0.0043  467 PHE B CG  
4697  C CD1 . PHE B 166 ? 0.6110 0.4675 0.4596 0.0437  -0.0038 0.0017  467 PHE B CD1 
4698  C CD2 . PHE B 166 ? 0.4810 0.3375 0.3470 0.0334  -0.0056 0.0068  467 PHE B CD2 
4699  C CE1 . PHE B 166 ? 0.5948 0.4528 0.4426 0.0381  -0.0077 0.0017  467 PHE B CE1 
4700  C CE2 . PHE B 166 ? 0.5352 0.3938 0.4008 0.0279  -0.0092 0.0067  467 PHE B CE2 
4701  C CZ  . PHE B 166 ? 0.5644 0.4245 0.4213 0.0304  -0.0104 0.0042  467 PHE B CZ  
4702  N N   . PRO B 167 ? 0.5614 0.4428 0.4158 0.0689  0.0115  0.0025  468 PRO B N   
4703  C CA  . PRO B 167 ? 0.5364 0.4317 0.3912 0.0791  0.0160  0.0017  468 PRO B CA  
4704  C C   . PRO B 167 ? 0.5290 0.4234 0.3885 0.0830  0.0146  0.0021  468 PRO B C   
4705  O O   . PRO B 167 ? 0.5588 0.4330 0.4133 0.0827  0.0094  0.0005  468 PRO B O   
4706  C CB  . PRO B 167 ? 0.5289 0.4144 0.3672 0.0898  0.0151  -0.0046 468 PRO B CB  
4707  C CG  . PRO B 167 ? 0.5715 0.4472 0.4036 0.0828  0.0123  -0.0054 468 PRO B CG  
4708  C CD  . PRO B 167 ? 0.5709 0.4378 0.4108 0.0716  0.0079  -0.0026 468 PRO B CD  
4709  N N   . GLN B 168 ? 0.5608 0.4787 0.4294 0.0866  0.0193  0.0042  469 GLN B N   
4710  C CA  . GLN B 168 ? 0.6031 0.5266 0.4776 0.0910  0.0184  0.0053  469 GLN B CA  
4711  C C   . GLN B 168 ? 0.7164 0.6236 0.5769 0.1064  0.0153  0.0009  469 GLN B C   
4712  O O   . GLN B 168 ? 0.7462 0.6437 0.5931 0.1153  0.0153  -0.0038 469 GLN B O   
4713  C CB  . GLN B 168 ? 0.4504 0.4072 0.3369 0.0915  0.0243  0.0078  469 GLN B CB  
4714  C CG  . GLN B 168 ? 0.4805 0.4539 0.3614 0.1035  0.0287  0.0049  469 GLN B CG  
4715  C CD  . GLN B 168 ? 0.4887 0.4958 0.3814 0.0967  0.0355  0.0081  469 GLN B CD  
4716  O OE1 . GLN B 168 ? 0.5051 0.5139 0.4037 0.0819  0.0377  0.0118  469 GLN B OE1 
4717  N NE2 . GLN B 168 ? 0.4881 0.5225 0.3838 0.1074  0.0390  0.0068  469 GLN B NE2 
4718  N N   . ARG B 169 ? 0.6847 0.5875 0.5470 0.1100  0.0127  0.0024  470 ARG B N   
4719  C CA  . ARG B 169 ? 0.6520 0.5364 0.4990 0.1258  0.0098  -0.0008 470 ARG B CA  
4720  C C   . ARG B 169 ? 0.6206 0.5282 0.4659 0.1429  0.0142  -0.0032 470 ARG B C   
4721  O O   . ARG B 169 ? 0.6195 0.5622 0.4797 0.1421  0.0185  -0.0005 470 ARG B O   
4722  C CB  . ARG B 169 ? 0.7795 0.6555 0.6289 0.1251  0.0064  0.0028  470 ARG B CB  
4723  C CG  . ARG B 169 ? 0.8881 0.7439 0.7203 0.1428  0.0037  0.0008  470 ARG B CG  
4724  C CD  . ARG B 169 ? 0.8201 0.6670 0.6538 0.1407  0.0005  0.0054  470 ARG B CD  
4725  N NE  . ARG B 169 ? 0.7943 0.6106 0.6219 0.1263  -0.0037 0.0065  470 ARG B NE  
4726  C CZ  . ARG B 169 ? 0.9140 0.7303 0.7501 0.1152  -0.0055 0.0114  470 ARG B CZ  
4727  N NH1 . ARG B 169 ? 0.8600 0.7038 0.7105 0.1166  -0.0037 0.0152  470 ARG B NH1 
4728  N NH2 . ARG B 169 ? 1.0268 0.8184 0.8573 0.1020  -0.0089 0.0122  470 ARG B NH2 
4729  N N   . THR B 170 ? 0.5937 0.4829 0.4200 0.1580  0.0132  -0.0086 471 THR B N   
4730  C CA  . THR B 170 ? 0.6648 0.5779 0.4884 0.1764  0.0176  -0.0114 471 THR B CA  
4731  C C   . THR B 170 ? 0.8366 0.7383 0.6481 0.1963  0.0150  -0.0126 471 THR B C   
4732  O O   . THR B 170 ? 0.9464 0.8765 0.7688 0.2036  0.0167  -0.0095 471 THR B O   
4733  C CB  . THR B 170 ? 0.7379 0.6435 0.5477 0.1823  0.0194  -0.0173 471 THR B CB  
4734  O OG1 . THR B 170 ? 0.8579 0.7184 0.6458 0.1850  0.0138  -0.0222 471 THR B OG1 
4735  C CG2 . THR B 170 ? 0.6462 0.5668 0.4671 0.1649  0.0225  -0.0152 471 THR B CG2 
4736  N N   . ASP B 171 ? 0.9009 0.7607 0.6887 0.2053  0.0109  -0.0170 472 ASP B N   
4737  C CA  . ASP B 171 ? 0.9775 0.8183 0.7484 0.2260  0.0084  -0.0181 472 ASP B CA  
4738  C C   . ASP B 171 ? 0.9640 0.7657 0.7255 0.2184  0.0025  -0.0149 472 ASP B C   
4739  O O   . ASP B 171 ? 1.0909 0.8762 0.8389 0.2343  0.0003  -0.0138 472 ASP B O   
4740  C CB  . ASP B 171 ? 1.0818 0.9007 0.8273 0.2458  0.0086  -0.0261 472 ASP B CB  
4741  C CG  . ASP B 171 ? 1.1297 0.8969 0.8533 0.2371  0.0037  -0.0307 472 ASP B CG  
4742  O OD1 . ASP B 171 ? 1.1600 0.9204 0.8925 0.2140  0.0017  -0.0287 472 ASP B OD1 
4743  O OD2 . ASP B 171 ? 1.1689 0.9025 0.8653 0.2537  0.0019  -0.0368 472 ASP B OD2 
4744  N N   . GLY B 172 ? 0.8829 0.6706 0.6505 0.1952  0.0000  -0.0130 473 GLY B N   
4745  C CA  . GLY B 172 ? 0.8640 0.6180 0.6239 0.1852  -0.0050 -0.0097 473 GLY B CA  
4746  C C   . GLY B 172 ? 0.9506 0.6563 0.6859 0.1805  -0.0092 -0.0147 473 GLY B C   
4747  O O   . GLY B 172 ? 0.9699 0.6518 0.7022 0.1645  -0.0129 -0.0121 473 GLY B O   
4748  N N   . LYS B 173 ? 0.9964 0.6879 0.7133 0.1935  -0.0086 -0.0221 474 LYS B N   
4749  C CA  . LYS B 173 ? 1.1293 0.7760 0.8218 0.1877  -0.0127 -0.0283 474 LYS B CA  
4750  C C   . LYS B 173 ? 1.1756 0.8333 0.8758 0.1722  -0.0123 -0.0323 474 LYS B C   
4751  O O   . LYS B 173 ? 1.1890 0.8161 0.8692 0.1687  -0.0154 -0.0391 474 LYS B O   
4752  C CB  . LYS B 173 ? 1.2426 0.8609 0.9056 0.2122  -0.0128 -0.0350 474 LYS B CB  
4753  C CG  . LYS B 173 ? 1.3354 0.9350 0.9847 0.2300  -0.0139 -0.0312 474 LYS B CG  
4754  C CD  . LYS B 173 ? 1.4606 1.0224 1.0753 0.2543  -0.0147 -0.0385 474 LYS B CD  
4755  C CE  . LYS B 173 ? 1.4855 1.0831 1.1044 0.2774  -0.0096 -0.0431 474 LYS B CE  
4756  N NZ  . LYS B 173 ? 1.4591 1.0894 1.0886 0.2981  -0.0069 -0.0376 474 LYS B NZ  
4757  N N   . HIS B 174 ? 1.0957 0.7954 0.8228 0.1630  -0.0089 -0.0282 475 HIS B N   
4758  C CA  . HIS B 174 ? 1.0391 0.7522 0.7737 0.1504  -0.0081 -0.0307 475 HIS B CA  
4759  C C   . HIS B 174 ? 0.9629 0.6992 0.7221 0.1311  -0.0078 -0.0239 475 HIS B C   
4760  O O   . HIS B 174 ? 0.9572 0.7190 0.7295 0.1249  -0.0049 -0.0231 475 HIS B O   
4761  C CB  . HIS B 174 ? 1.0711 0.8119 0.8081 0.1639  -0.0028 -0.0339 475 HIS B CB  
4762  C CG  . HIS B 174 ? 1.1404 0.8606 0.8524 0.1848  -0.0027 -0.0415 475 HIS B CG  
4763  N ND1 . HIS B 174 ? 1.1779 0.9107 0.8872 0.2067  0.0007  -0.0414 475 HIS B ND1 
4764  C CD2 . HIS B 174 ? 1.1833 0.8713 0.8707 0.1878  -0.0057 -0.0500 475 HIS B CD2 
4765  C CE1 . HIS B 174 ? 1.2119 0.9197 0.8953 0.2238  0.0000  -0.0493 475 HIS B CE1 
4766  N NE2 . HIS B 174 ? 1.2306 0.9094 0.8998 0.2121  -0.0039 -0.0549 475 HIS B NE2 
4767  N N   . ASP B 175 ? 0.8062 0.5332 0.5704 0.1225  -0.0104 -0.0189 476 ASP B N   
4768  C CA  . ASP B 175 ? 0.7641 0.5126 0.5504 0.1061  -0.0099 -0.0128 476 ASP B CA  
4769  C C   . ASP B 175 ? 0.6924 0.4376 0.4799 0.0903  -0.0123 -0.0148 476 ASP B C   
4770  O O   . ASP B 175 ? 0.7678 0.4860 0.5387 0.0857  -0.0166 -0.0197 476 ASP B O   
4771  C CB  . ASP B 175 ? 0.7550 0.4918 0.5436 0.0999  -0.0125 -0.0075 476 ASP B CB  
4772  C CG  . ASP B 175 ? 0.7526 0.5004 0.5447 0.1141  -0.0103 -0.0039 476 ASP B CG  
4773  O OD1 . ASP B 175 ? 0.8045 0.5698 0.5971 0.1292  -0.0068 -0.0057 476 ASP B OD1 
4774  O OD2 . ASP B 175 ? 0.8087 0.5491 0.6024 0.1100  -0.0122 0.0009  476 ASP B OD2 
4775  N N   . PHE B 176 ? 0.6249 0.3975 0.4311 0.0818  -0.0098 -0.0110 477 PHE B N   
4776  C CA  . PHE B 176 ? 0.7006 0.4742 0.5115 0.0666  -0.0125 -0.0108 477 PHE B CA  
4777  C C   . PHE B 176 ? 0.6865 0.4582 0.5066 0.0549  -0.0147 -0.0058 477 PHE B C   
4778  O O   . PHE B 176 ? 0.7019 0.4872 0.5342 0.0564  -0.0122 -0.0008 477 PHE B O   
4779  C CB  . PHE B 176 ? 0.6518 0.4524 0.4750 0.0651  -0.0085 -0.0089 477 PHE B CB  
4780  C CG  . PHE B 176 ? 0.7019 0.5039 0.5144 0.0737  -0.0068 -0.0138 477 PHE B CG  
4781  C CD1 . PHE B 176 ? 0.7393 0.5457 0.5465 0.0884  -0.0031 -0.0157 477 PHE B CD1 
4782  C CD2 . PHE B 176 ? 0.7178 0.5186 0.5248 0.0681  -0.0091 -0.0167 477 PHE B CD2 
4783  C CE1 . PHE B 176 ? 0.7261 0.5349 0.5224 0.0971  -0.0011 -0.0205 477 PHE B CE1 
4784  C CE2 . PHE B 176 ? 0.6970 0.4990 0.4927 0.0765  -0.0075 -0.0214 477 PHE B CE2 
4785  C CZ  . PHE B 176 ? 0.6311 0.4367 0.4213 0.0908  -0.0033 -0.0233 477 PHE B CZ  
4786  N N   . ARG B 177 ? 0.6768 0.4330 0.4906 0.0429  -0.0195 -0.0075 478 ARG B N   
4787  C CA  . ARG B 177 ? 0.7340 0.4904 0.5560 0.0309  -0.0214 -0.0029 478 ARG B CA  
4788  C C   . ARG B 177 ? 0.7390 0.5009 0.5643 0.0166  -0.0248 -0.0040 478 ARG B C   
4789  O O   . ARG B 177 ? 0.7973 0.5464 0.6099 0.0125  -0.0283 -0.0096 478 ARG B O   
4790  C CB  . ARG B 177 ? 0.6796 0.4073 0.4873 0.0307  -0.0241 -0.0027 478 ARG B CB  
4791  C CG  . ARG B 177 ? 0.7147 0.4389 0.5195 0.0460  -0.0213 -0.0005 478 ARG B CG  
4792  C CD  . ARG B 177 ? 0.7357 0.4866 0.5605 0.0463  -0.0181 0.0058  478 ARG B CD  
4793  N NE  . ARG B 177 ? 0.6559 0.4073 0.4877 0.0333  -0.0198 0.0104  478 ARG B NE  
4794  C CZ  . ARG B 177 ? 0.7384 0.4759 0.5645 0.0332  -0.0210 0.0142  478 ARG B CZ  
4795  N NH1 . ARG B 177 ? 0.7463 0.4663 0.5586 0.0465  -0.0210 0.0140  478 ARG B NH1 
4796  N NH2 . ARG B 177 ? 0.6250 0.3666 0.4582 0.0207  -0.0220 0.0184  478 ARG B NH2 
4797  N N   . VAL B 178 ? 0.6253 0.4073 0.4669 0.0095  -0.0238 0.0008  479 VAL B N   
4798  C CA  . VAL B 178 ? 0.6131 0.4002 0.4580 -0.0046 -0.0274 0.0009  479 VAL B CA  
4799  C C   . VAL B 178 ? 0.6866 0.4563 0.5257 -0.0129 -0.0296 0.0028  479 VAL B C   
4800  O O   . VAL B 178 ? 0.6989 0.4686 0.5430 -0.0096 -0.0273 0.0075  479 VAL B O   
4801  C CB  . VAL B 178 ? 0.5640 0.3784 0.4266 -0.0067 -0.0253 0.0052  479 VAL B CB  
4802  C CG1 . VAL B 178 ? 0.5160 0.3395 0.3820 -0.0196 -0.0290 0.0051  479 VAL B CG1 
4803  C CG2 . VAL B 178 ? 0.6106 0.4381 0.4762 0.0016  -0.0226 0.0045  479 VAL B CG2 
4804  N N   . TRP B 179 ? 0.7865 0.5404 0.6134 -0.0241 -0.0340 -0.0008 480 TRP B N   
4805  C CA  . TRP B 179 ? 0.7297 0.4642 0.5485 -0.0335 -0.0357 0.0018  480 TRP B CA  
4806  C C   . TRP B 179 ? 0.6953 0.4514 0.5288 -0.0459 -0.0358 0.0066  480 TRP B C   
4807  O O   . TRP B 179 ? 0.6672 0.4154 0.4997 -0.0507 -0.0352 0.0113  480 TRP B O   
4808  C CB  . TRP B 179 ? 0.7418 0.4459 0.5385 -0.0425 -0.0401 -0.0040 480 TRP B CB  
4809  C CG  . TRP B 179 ? 0.7420 0.4160 0.5199 -0.0284 -0.0396 -0.0075 480 TRP B CG  
4810  C CD1 . TRP B 179 ? 0.6722 0.3533 0.4527 -0.0102 -0.0364 -0.0088 480 TRP B CD1 
4811  C CD2 . TRP B 179 ? 0.7638 0.3961 0.5163 -0.0304 -0.0419 -0.0099 480 TRP B CD2 
4812  N NE1 . TRP B 179 ? 0.6704 0.3199 0.4298 0.0006  -0.0366 -0.0122 480 TRP B NE1 
4813  C CE2 . TRP B 179 ? 0.6955 0.3123 0.4364 -0.0107 -0.0401 -0.0130 480 TRP B CE2 
4814  C CE3 . TRP B 179 ? 0.8591 0.4648 0.5962 -0.0472 -0.0451 -0.0096 480 TRP B CE3 
4815  C CZ2 . TRP B 179 ? 0.7596 0.3337 0.4732 -0.0050 -0.0416 -0.0160 480 TRP B CZ2 
4816  C CZ3 . TRP B 179 ? 0.8584 0.4182 0.5670 -0.0435 -0.0466 -0.0123 480 TRP B CZ3 
4817  C CH2 . TRP B 179 ? 0.8416 0.3852 0.5383 -0.0214 -0.0449 -0.0156 480 TRP B CH2 
4818  N N   . ASN B 180 ? 0.6383 0.4221 0.4845 -0.0499 -0.0364 0.0057  481 ASN B N   
4819  C CA  . ASN B 180 ? 0.5926 0.4011 0.4538 -0.0580 -0.0357 0.0101  481 ASN B CA  
4820  C C   . ASN B 180 ? 0.6777 0.4942 0.5498 -0.0486 -0.0312 0.0156  481 ASN B C   
4821  O O   . ASN B 180 ? 0.6372 0.4527 0.5111 -0.0356 -0.0284 0.0156  481 ASN B O   
4822  C CB  . ASN B 180 ? 0.5771 0.4142 0.4487 -0.0590 -0.0369 0.0081  481 ASN B CB  
4823  C CG  . ASN B 180 ? 0.6186 0.4519 0.4799 -0.0675 -0.0418 0.0017  481 ASN B CG  
4824  O OD1 . ASN B 180 ? 0.5391 0.3533 0.3876 -0.0624 -0.0429 -0.0029 481 ASN B OD1 
4825  N ND2 . ASN B 180 ? 0.6628 0.5167 0.5294 -0.0806 -0.0448 0.0011  481 ASN B ND2 
4826  N N   . SER B 181 ? 0.5896 0.4157 0.4688 -0.0561 -0.0305 0.0202  482 SER B N   
4827  C CA  . SER B 181 ? 0.4862 0.3222 0.3758 -0.0480 -0.0266 0.0247  482 SER B CA  
4828  C C   . SER B 181 ? 0.4804 0.3431 0.3844 -0.0430 -0.0245 0.0248  482 SER B C   
4829  O O   . SER B 181 ? 0.5113 0.3786 0.4211 -0.0333 -0.0212 0.0261  482 SER B O   
4830  C CB  . SER B 181 ? 0.5507 0.3848 0.4402 -0.0564 -0.0262 0.0296  482 SER B CB  
4831  O OG  . SER B 181 ? 0.5443 0.3914 0.4364 -0.0706 -0.0282 0.0299  482 SER B OG  
4832  N N   . GLN B 182 ? 0.4843 0.3643 0.3927 -0.0493 -0.0265 0.0233  483 GLN B N   
4833  C CA  . GLN B 182 ? 0.5330 0.4332 0.4501 -0.0420 -0.0252 0.0226  483 GLN B CA  
4834  C C   . GLN B 182 ? 0.6028 0.5070 0.5151 -0.0438 -0.0287 0.0183  483 GLN B C   
4835  O O   . GLN B 182 ? 0.7365 0.6355 0.6421 -0.0545 -0.0325 0.0158  483 GLN B O   
4836  C CB  . GLN B 182 ? 0.4678 0.3914 0.3957 -0.0441 -0.0241 0.0252  483 GLN B CB  
4837  C CG  . GLN B 182 ? 0.6100 0.5331 0.5429 -0.0415 -0.0205 0.0289  483 GLN B CG  
4838  C CD  . GLN B 182 ? 0.6538 0.5978 0.5942 -0.0473 -0.0202 0.0311  483 GLN B CD  
4839  O OE1 . GLN B 182 ? 0.6029 0.5676 0.5494 -0.0441 -0.0201 0.0303  483 GLN B OE1 
4840  N NE2 . GLN B 182 ? 0.6834 0.6226 0.6223 -0.0553 -0.0200 0.0340  483 GLN B NE2 
4841  N N   . LEU B 183 ? 0.4787 0.3915 0.3933 -0.0339 -0.0275 0.0175  484 LEU B N   
4842  C CA  . LEU B 183 ? 0.5333 0.4513 0.4426 -0.0339 -0.0309 0.0136  484 LEU B CA  
4843  C C   . LEU B 183 ? 0.5756 0.5144 0.4885 -0.0442 -0.0351 0.0122  484 LEU B C   
4844  O O   . LEU B 183 ? 0.5388 0.4770 0.4448 -0.0519 -0.0395 0.0080  484 LEU B O   
4845  C CB  . LEU B 183 ? 0.4369 0.3621 0.3476 -0.0212 -0.0285 0.0145  484 LEU B CB  
4846  C CG  . LEU B 183 ? 0.4740 0.3823 0.3815 -0.0128 -0.0241 0.0157  484 LEU B CG  
4847  C CD1 . LEU B 183 ? 0.5038 0.4172 0.4106 -0.0026 -0.0212 0.0173  484 LEU B CD1 
4848  C CD2 . LEU B 183 ? 0.4227 0.3117 0.3198 -0.0143 -0.0255 0.0121  484 LEU B CD2 
4849  N N   . ILE B 184 ? 0.4771 0.4357 0.4002 -0.0450 -0.0338 0.0154  485 ILE B N   
4850  C CA  . ILE B 184 ? 0.5294 0.5149 0.4581 -0.0540 -0.0371 0.0146  485 ILE B CA  
4851  C C   . ILE B 184 ? 0.5651 0.5532 0.4985 -0.0647 -0.0358 0.0176  485 ILE B C   
4852  O O   . ILE B 184 ? 0.5141 0.5048 0.4537 -0.0585 -0.0318 0.0212  485 ILE B O   
4853  C CB  . ILE B 184 ? 0.5528 0.5653 0.4888 -0.0424 -0.0366 0.0156  485 ILE B CB  
4854  C CG1 . ILE B 184 ? 0.5532 0.5644 0.4823 -0.0341 -0.0387 0.0129  485 ILE B CG1 
4855  C CG2 . ILE B 184 ? 0.4360 0.4821 0.3802 -0.0498 -0.0390 0.0155  485 ILE B CG2 
4856  C CD1 . ILE B 184 ? 0.4773 0.4980 0.4082 -0.0175 -0.0362 0.0156  485 ILE B CD1 
4857  N N   . ARG B 185 ? 0.6016 0.5867 0.5301 -0.0814 -0.0390 0.0159  486 ARG B N   
4858  C CA  . ARG B 185 ? 0.5431 0.5337 0.4744 -0.0947 -0.0382 0.0191  486 ARG B CA  
4859  C C   . ARG B 185 ? 0.6055 0.6119 0.5349 -0.1132 -0.0427 0.0162  486 ARG B C   
4860  O O   . ARG B 185 ? 0.5737 0.5784 0.4968 -0.1168 -0.0469 0.0111  486 ARG B O   
4861  C CB  . ARG B 185 ? 0.5097 0.4657 0.4316 -0.0982 -0.0363 0.0216  486 ARG B CB  
4862  C CG  . ARG B 185 ? 0.5596 0.5032 0.4840 -0.0825 -0.0320 0.0245  486 ARG B CG  
4863  C CD  . ARG B 185 ? 0.6991 0.6204 0.6176 -0.0861 -0.0299 0.0285  486 ARG B CD  
4864  N NE  . ARG B 185 ? 0.7789 0.7181 0.7044 -0.0932 -0.0281 0.0327  486 ARG B NE  
4865  C CZ  . ARG B 185 ? 0.7367 0.6630 0.6584 -0.0964 -0.0261 0.0372  486 ARG B CZ  
4866  N NH1 . ARG B 185 ? 0.6020 0.4975 0.5129 -0.0922 -0.0259 0.0382  486 ARG B NH1 
4867  N NH2 . ARG B 185 ? 0.8609 0.8067 0.7890 -0.1029 -0.0243 0.0409  486 ARG B NH2 
4868  N N   . TYR B 186 ? 0.4851 0.5082 0.4196 -0.1261 -0.0419 0.0192  487 TYR B N   
4869  C CA  . TYR B 186 ? 0.5585 0.5994 0.4918 -0.1470 -0.0457 0.0169  487 TYR B CA  
4870  C C   . TYR B 186 ? 0.6180 0.6233 0.5355 -0.1652 -0.0465 0.0176  487 TYR B C   
4871  O O   . TYR B 186 ? 0.6285 0.6056 0.5398 -0.1623 -0.0432 0.0219  487 TYR B O   
4872  C CB  . TYR B 186 ? 0.5118 0.5967 0.4594 -0.1519 -0.0441 0.0198  487 TYR B CB  
4873  C CG  . TYR B 186 ? 0.5978 0.7178 0.5585 -0.1332 -0.0436 0.0190  487 TYR B CG  
4874  C CD1 . TYR B 186 ? 0.5431 0.6814 0.5049 -0.1287 -0.0480 0.0142  487 TYR B CD1 
4875  C CD2 . TYR B 186 ? 0.5662 0.6996 0.5361 -0.1194 -0.0389 0.0229  487 TYR B CD2 
4876  C CE1 . TYR B 186 ? 0.5746 0.7421 0.5456 -0.1100 -0.0475 0.0141  487 TYR B CE1 
4877  C CE2 . TYR B 186 ? 0.5818 0.7424 0.5602 -0.1010 -0.0384 0.0222  487 TYR B CE2 
4878  C CZ  . TYR B 186 ? 0.5833 0.7603 0.5620 -0.0959 -0.0426 0.0182  487 TYR B CZ  
4879  O OH  . TYR B 186 ? 0.5625 0.7639 0.5472 -0.0760 -0.0421 0.0181  487 TYR B OH  
4880  N N   . ALA B 187 ? 0.6946 0.7009 0.6042 -0.1841 -0.0510 0.0132  488 ALA B N   
4881  C CA  . ALA B 187 ? 0.6992 0.6673 0.5898 -0.2029 -0.0522 0.0131  488 ALA B CA  
4882  C C   . ALA B 187 ? 0.7392 0.7128 0.6307 -0.2187 -0.0491 0.0197  488 ALA B C   
4883  O O   . ALA B 187 ? 0.7618 0.7773 0.6696 -0.2204 -0.0471 0.0227  488 ALA B O   
4884  C CB  . ALA B 187 ? 0.5699 0.5384 0.4506 -0.2209 -0.0582 0.0057  488 ALA B CB  
4885  N N   . GLY B 188 ? 0.7449 0.6745 0.6172 -0.2295 -0.0486 0.0222  489 GLY B N   
4886  C CA  . GLY B 188 ? 0.7952 0.7236 0.6630 -0.2490 -0.0461 0.0285  489 GLY B CA  
4887  C C   . GLY B 188 ? 0.8039 0.6967 0.6480 -0.2738 -0.0492 0.0264  489 GLY B C   
4888  O O   . GLY B 188 ? 0.8687 0.7141 0.6931 -0.2693 -0.0510 0.0234  489 GLY B O   
4889  N N   . TYR B 189 ? 0.7537 0.6685 0.5984 -0.3004 -0.0496 0.0277  490 TYR B N   
4890  C CA  . TYR B 189 ? 0.8385 0.7226 0.6602 -0.3284 -0.0529 0.0248  490 TYR B CA  
4891  C C   . TYR B 189 ? 0.9748 0.8445 0.7854 -0.3490 -0.0490 0.0336  490 TYR B C   
4892  O O   . TYR B 189 ? 0.9162 0.8289 0.7438 -0.3548 -0.0455 0.0391  490 TYR B O   
4893  C CB  . TYR B 189 ? 0.8232 0.7485 0.6534 -0.3467 -0.0578 0.0171  490 TYR B CB  
4894  C CG  . TYR B 189 ? 0.8506 0.8014 0.6946 -0.3261 -0.0614 0.0094  490 TYR B CG  
4895  C CD1 . TYR B 189 ? 0.8904 0.8036 0.7189 -0.3173 -0.0652 0.0022  490 TYR B CD1 
4896  C CD2 . TYR B 189 ? 0.8478 0.8598 0.7187 -0.3152 -0.0609 0.0094  490 TYR B CD2 
4897  C CE1 . TYR B 189 ? 0.9110 0.8477 0.7508 -0.2992 -0.0682 -0.0041 490 TYR B CE1 
4898  C CE2 . TYR B 189 ? 0.8615 0.8945 0.7427 -0.2962 -0.0641 0.0033  490 TYR B CE2 
4899  C CZ  . TYR B 189 ? 0.8649 0.8608 0.7307 -0.2891 -0.0677 -0.0032 490 TYR B CZ  
4900  O OH  . TYR B 189 ? 0.8271 0.8441 0.7020 -0.2705 -0.0706 -0.0084 490 TYR B OH  
4901  N N   . LYS B 190 ? 1.0837 0.8922 0.8643 -0.3593 -0.0495 0.0351  491 LYS B N   
4902  C CA  . LYS B 190 ? 1.1305 0.9160 0.8949 -0.3799 -0.0458 0.0442  491 LYS B CA  
4903  C C   . LYS B 190 ? 1.1552 0.9566 0.9135 -0.4171 -0.0479 0.0417  491 LYS B C   
4904  O O   . LYS B 190 ? 1.2468 1.0192 0.9860 -0.4258 -0.0518 0.0343  491 LYS B O   
4905  C CB  . LYS B 190 ? 1.2072 0.9177 0.9394 -0.3726 -0.0454 0.0472  491 LYS B CB  
4906  C CG  . LYS B 190 ? 1.3172 1.0072 1.0390 -0.3747 -0.0400 0.0596  491 LYS B CG  
4907  C CD  . LYS B 190 ? 1.3052 1.0391 1.0550 -0.3520 -0.0358 0.0651  491 LYS B CD  
4908  C CE  . LYS B 190 ? 1.3374 1.0555 1.0770 -0.3556 -0.0306 0.0774  491 LYS B CE  
4909  N NZ  . LYS B 190 ? 1.3494 1.0751 1.0801 -0.3866 -0.0288 0.0814  491 LYS B NZ  
4910  N N   . GLN B 191 ? 1.1668 1.0207 0.9432 -0.4292 -0.0445 0.0466  492 GLN B N   
4911  C CA  . GLN B 191 ? 1.2518 1.1349 1.0278 -0.4538 -0.0453 0.0436  492 GLN B CA  
4912  C C   . GLN B 191 ? 1.2876 1.1201 1.0321 -0.4685 -0.0433 0.0476  492 GLN B C   
4913  O O   . GLN B 191 ? 1.2974 1.0870 1.0264 -0.4594 -0.0398 0.0553  492 GLN B O   
4914  C CB  . GLN B 191 ? 1.2030 1.1599 1.0076 -0.4595 -0.0419 0.0477  492 GLN B CB  
4915  C CG  . GLN B 191 ? 1.1509 1.1657 0.9874 -0.4456 -0.0441 0.0434  492 GLN B CG  
4916  C CD  . GLN B 191 ? 1.1796 1.2251 1.0237 -0.4525 -0.0505 0.0322  492 GLN B CD  
4917  O OE1 . GLN B 191 ? 1.2003 1.2062 1.0242 -0.4591 -0.0548 0.0256  492 GLN B OE1 
4918  N NE2 . GLN B 191 ? 1.1623 1.2799 1.0351 -0.4490 -0.0512 0.0300  492 GLN B NE2 
4919  N N   . PRO B 192 ? 1.2767 1.1139 1.0109 -0.4913 -0.0454 0.0425  493 PRO B N   
4920  C CA  . PRO B 192 ? 1.3268 1.1138 1.0291 -0.5067 -0.0437 0.0461  493 PRO B CA  
4921  C C   . PRO B 192 ? 1.3613 1.1576 1.0635 -0.5133 -0.0375 0.0575  493 PRO B C   
4922  O O   . PRO B 192 ? 1.3169 1.0598 0.9926 -0.5144 -0.0352 0.0634  493 PRO B O   
4923  C CB  . PRO B 192 ? 1.2561 1.0605 0.9531 -0.5313 -0.0473 0.0377  493 PRO B CB  
4924  C CG  . PRO B 192 ? 1.1473 1.0280 0.8787 -0.5307 -0.0493 0.0329  493 PRO B CG  
4925  C CD  . PRO B 192 ? 1.1804 1.0654 0.9292 -0.5031 -0.0500 0.0330  493 PRO B CD  
4926  N N   . ASP B 193 ? 1.3731 1.2360 1.1035 -0.5163 -0.0348 0.0607  494 ASP B N   
4927  C CA  . ASP B 193 ? 1.3478 1.2262 1.0805 -0.5213 -0.0288 0.0712  494 ASP B CA  
4928  C C   . ASP B 193 ? 1.3116 1.1692 1.0467 -0.4976 -0.0253 0.0793  494 ASP B C   
4929  O O   . ASP B 193 ? 1.3739 1.2482 1.1135 -0.4985 -0.0202 0.0882  494 ASP B O   
4930  C CB  . ASP B 193 ? 1.3437 1.3045 1.1059 -0.5307 -0.0272 0.0709  494 ASP B CB  
4931  C CG  . ASP B 193 ? 1.2924 1.3018 1.0848 -0.5143 -0.0299 0.0647  494 ASP B CG  
4932  O OD1 . ASP B 193 ? 1.1874 1.2141 0.9972 -0.4945 -0.0272 0.0691  494 ASP B OD1 
4933  O OD2 . ASP B 193 ? 1.2867 1.3165 1.0845 -0.5210 -0.0348 0.0554  494 ASP B OD2 
4934  N N   . GLY B 194 ? 1.1512 0.9743 0.8831 -0.4763 -0.0278 0.0766  495 GLY B N   
4935  C CA  . GLY B 194 ? 0.9390 0.7384 0.6702 -0.4537 -0.0248 0.0841  495 GLY B CA  
4936  C C   . GLY B 194 ? 0.9072 0.7552 0.6697 -0.4370 -0.0234 0.0849  495 GLY B C   
4937  O O   . GLY B 194 ? 0.9567 0.7826 0.7187 -0.4162 -0.0220 0.0893  495 GLY B O   
4938  N N   . SER B 195 ? 0.9959 0.9103 0.7850 -0.4447 -0.0237 0.0810  496 SER B N   
4939  C CA  . SER B 195 ? 1.0531 1.0153 0.8719 -0.4282 -0.0228 0.0807  496 SER B CA  
4940  C C   . SER B 195 ? 1.0830 1.0280 0.9050 -0.4086 -0.0280 0.0721  496 SER B C   
4941  O O   . SER B 195 ? 1.0742 0.9685 0.8745 -0.4124 -0.0319 0.0678  496 SER B O   
4942  C CB  . SER B 195 ? 1.0790 1.1182 0.9238 -0.4384 -0.0219 0.0781  496 SER B CB  
4943  O OG  . SER B 195 ? 1.1310 1.1812 0.9727 -0.4551 -0.0267 0.0696  496 SER B OG  
4944  N N   . THR B 196 ? 1.0616 1.0489 0.9099 -0.3824 -0.0278 0.0686  497 THR B N   
4945  C CA  . THR B 196 ? 1.0536 1.0281 0.9063 -0.3568 -0.0318 0.0607  497 THR B CA  
4946  C C   . THR B 196 ? 0.9463 0.9826 0.8266 -0.3462 -0.0336 0.0542  497 THR B C   
4947  O O   . THR B 196 ? 0.9622 1.0435 0.8622 -0.3361 -0.0300 0.0572  497 THR B O   
4948  C CB  . THR B 196 ? 1.1287 1.0732 0.9792 -0.3277 -0.0291 0.0647  497 THR B CB  
4949  O OG1 . THR B 196 ? 1.1177 1.0047 0.9411 -0.3352 -0.0277 0.0712  497 THR B OG1 
4950  C CG2 . THR B 196 ? 1.1593 1.0914 1.0138 -0.3033 -0.0328 0.0569  497 THR B CG2 
4951  N N   . LEU B 197 ? 0.9140 0.9512 0.7939 -0.3470 -0.0392 0.0453  498 LEU B N   
4952  C CA  . LEU B 197 ? 0.8653 0.9567 0.7680 -0.3354 -0.0418 0.0389  498 LEU B CA  
4953  C C   . LEU B 197 ? 0.8345 0.9097 0.7413 -0.3031 -0.0430 0.0352  498 LEU B C   
4954  O O   . LEU B 197 ? 0.7909 0.8156 0.6808 -0.2973 -0.0449 0.0330  498 LEU B O   
4955  C CB  . LEU B 197 ? 0.8321 0.9415 0.7322 -0.3587 -0.0476 0.0314  498 LEU B CB  
4956  C CG  . LEU B 197 ? 0.7249 0.8782 0.6425 -0.3444 -0.0521 0.0234  498 LEU B CG  
4957  C CD1 . LEU B 197 ? 0.6523 0.8734 0.5961 -0.3331 -0.0494 0.0255  498 LEU B CD1 
4958  C CD2 . LEU B 197 ? 0.7673 0.9278 0.6771 -0.3688 -0.0586 0.0154  498 LEU B CD2 
4959  N N   . GLY B 198 ? 0.8763 0.9946 0.8044 -0.2820 -0.0417 0.0345  499 GLY B N   
4960  C CA  . GLY B 198 ? 0.8310 0.9371 0.7636 -0.2520 -0.0418 0.0320  499 GLY B CA  
4961  C C   . GLY B 198 ? 0.7948 0.8768 0.7265 -0.2343 -0.0368 0.0380  499 GLY B C   
4962  O O   . GLY B 198 ? 0.8171 0.9187 0.7560 -0.2355 -0.0324 0.0435  499 GLY B O   
4963  N N   . ASP B 199 ? 0.7312 0.7726 0.6540 -0.2181 -0.0373 0.0366  500 ASP B N   
4964  C CA  . ASP B 199 ? 0.6152 0.6357 0.5375 -0.2008 -0.0331 0.0414  500 ASP B CA  
4965  C C   . ASP B 199 ? 0.6950 0.6655 0.5967 -0.2093 -0.0326 0.0452  500 ASP B C   
4966  O O   . ASP B 199 ? 0.6116 0.5458 0.4990 -0.2079 -0.0355 0.0416  500 ASP B O   
4967  C CB  . ASP B 199 ? 0.6100 0.6244 0.5373 -0.1758 -0.0335 0.0376  500 ASP B CB  
4968  C CG  . ASP B 199 ? 0.6967 0.6997 0.6269 -0.1582 -0.0292 0.0417  500 ASP B CG  
4969  O OD1 . ASP B 199 ? 0.7915 0.7787 0.7151 -0.1638 -0.0266 0.0473  500 ASP B OD1 
4970  O OD2 . ASP B 199 ? 0.5330 0.5426 0.4711 -0.1391 -0.0284 0.0395  500 ASP B OD2 
4971  N N   . PRO B 200 ? 0.5999 0.5658 0.4977 -0.2166 -0.0290 0.0525  501 PRO B N   
4972  C CA  . PRO B 200 ? 0.6035 0.5197 0.4788 -0.2242 -0.0287 0.0570  501 PRO B CA  
4973  C C   . PRO B 200 ? 0.6315 0.5097 0.4980 -0.2033 -0.0291 0.0559  501 PRO B C   
4974  O O   . PRO B 200 ? 0.7248 0.5587 0.5702 -0.2072 -0.0308 0.0561  501 PRO B O   
4975  C CB  . PRO B 200 ? 0.6097 0.5374 0.4865 -0.2308 -0.0240 0.0655  501 PRO B CB  
4976  C CG  . PRO B 200 ? 0.5475 0.5306 0.4431 -0.2396 -0.0230 0.0645  501 PRO B CG  
4977  C CD  . PRO B 200 ? 0.5673 0.5747 0.4790 -0.2213 -0.0252 0.0569  501 PRO B CD  
4978  N N   . ALA B 201 ? 0.5548 0.4489 0.4358 -0.1813 -0.0276 0.0544  502 ALA B N   
4979  C CA  . ALA B 201 ? 0.5592 0.4233 0.4337 -0.1621 -0.0276 0.0535  502 ALA B CA  
4980  C C   . ALA B 201 ? 0.7759 0.6129 0.6381 -0.1613 -0.0314 0.0473  502 ALA B C   
4981  O O   . ALA B 201 ? 0.7944 0.5952 0.6422 -0.1521 -0.0319 0.0474  502 ALA B O   
4982  C CB  . ALA B 201 ? 0.5363 0.4261 0.4290 -0.1423 -0.0254 0.0520  502 ALA B CB  
4983  N N   . ASN B 202 ? 0.7050 0.5599 0.5718 -0.1702 -0.0344 0.0416  503 ASN B N   
4984  C CA  . ASN B 202 ? 0.7865 0.6208 0.6433 -0.1674 -0.0381 0.0347  503 ASN B CA  
4985  C C   . ASN B 202 ? 0.8862 0.6939 0.7230 -0.1887 -0.0414 0.0325  503 ASN B C   
4986  O O   . ASN B 202 ? 0.8530 0.6477 0.6810 -0.1900 -0.0450 0.0256  503 ASN B O   
4987  C CB  . ASN B 202 ? 0.6164 0.4862 0.4896 -0.1605 -0.0396 0.0291  503 ASN B CB  
4988  C CG  . ASN B 202 ? 0.5615 0.4512 0.4508 -0.1400 -0.0362 0.0310  503 ASN B CG  
4989  O OD1 . ASN B 202 ? 0.6493 0.5185 0.5351 -0.1262 -0.0340 0.0328  503 ASN B OD1 
4990  N ND2 . ASN B 202 ? 0.5866 0.5164 0.4926 -0.1379 -0.0356 0.0304  503 ASN B ND2 
4991  N N   . VAL B 203 ? 0.9281 0.7260 0.7559 -0.2060 -0.0401 0.0384  504 VAL B N   
4992  C CA  . VAL B 203 ? 0.8895 0.6581 0.6954 -0.2292 -0.0430 0.0367  504 VAL B CA  
4993  C C   . VAL B 203 ? 0.9052 0.6220 0.6875 -0.2205 -0.0453 0.0324  504 VAL B C   
4994  O O   . VAL B 203 ? 0.9035 0.6035 0.6721 -0.2320 -0.0494 0.0254  504 VAL B O   
4995  C CB  . VAL B 203 ? 0.8963 0.6548 0.6928 -0.2466 -0.0401 0.0455  504 VAL B CB  
4996  C CG1 . VAL B 203 ? 0.7318 0.4440 0.4986 -0.2684 -0.0426 0.0447  504 VAL B CG1 
4997  C CG2 . VAL B 203 ? 0.7337 0.5468 0.5516 -0.2602 -0.0383 0.0481  504 VAL B CG2 
4998  N N   . GLN B 204 ? 0.8131 0.5065 0.5904 -0.1992 -0.0430 0.0358  505 GLN B N   
4999  C CA  . GLN B 204 ? 0.8859 0.5295 0.6388 -0.1891 -0.0447 0.0325  505 GLN B CA  
5000  C C   . GLN B 204 ? 0.9767 0.6276 0.7350 -0.1754 -0.0470 0.0234  505 GLN B C   
5001  O O   . GLN B 204 ? 1.0353 0.6536 0.7733 -0.1772 -0.0501 0.0170  505 GLN B O   
5002  C CB  . GLN B 204 ? 0.8997 0.5210 0.6462 -0.1700 -0.0415 0.0393  505 GLN B CB  
5003  C CG  . GLN B 204 ? 1.0490 0.6180 0.7679 -0.1579 -0.0429 0.0366  505 GLN B CG  
5004  C CD  . GLN B 204 ? 1.1564 0.7180 0.8762 -0.1319 -0.0402 0.0411  505 GLN B CD  
5005  O OE1 . GLN B 204 ? 1.1990 0.7968 0.9421 -0.1219 -0.0376 0.0444  505 GLN B OE1 
5006  N NE2 . GLN B 204 ? 1.2135 0.7284 0.9067 -0.1205 -0.0410 0.0409  505 GLN B NE2 
5007  N N   . PHE B 205 ? 0.9422 0.6335 0.7257 -0.1614 -0.0454 0.0228  506 PHE B N   
5008  C CA  . PHE B 205 ? 0.8130 0.5147 0.6019 -0.1501 -0.0473 0.0151  506 PHE B CA  
5009  C C   . PHE B 205 ? 0.8522 0.5683 0.6404 -0.1685 -0.0517 0.0085  506 PHE B C   
5010  O O   . PHE B 205 ? 0.7969 0.4994 0.5745 -0.1662 -0.0549 0.0008  506 PHE B O   
5011  C CB  . PHE B 205 ? 0.6886 0.4279 0.5024 -0.1326 -0.0443 0.0169  506 PHE B CB  
5012  C CG  . PHE B 205 ? 0.7595 0.5081 0.5777 -0.1197 -0.0455 0.0104  506 PHE B CG  
5013  C CD1 . PHE B 205 ? 0.7752 0.4972 0.5815 -0.1038 -0.0450 0.0075  506 PHE B CD1 
5014  C CD2 . PHE B 205 ? 0.7442 0.5291 0.5775 -0.1225 -0.0470 0.0074  506 PHE B CD2 
5015  C CE1 . PHE B 205 ? 0.7862 0.5175 0.5957 -0.0924 -0.0455 0.0020  506 PHE B CE1 
5016  C CE2 . PHE B 205 ? 0.8153 0.6074 0.6507 -0.1104 -0.0479 0.0022  506 PHE B CE2 
5017  C CZ  . PHE B 205 ? 0.7959 0.5610 0.6194 -0.0961 -0.0470 -0.0004 506 PHE B CZ  
5018  N N   . THR B 206 ? 0.7053 0.4516 0.5048 -0.1867 -0.0520 0.0111  507 THR B N   
5019  C CA  . THR B 206 ? 0.7307 0.4937 0.5292 -0.2066 -0.0565 0.0049  507 THR B CA  
5020  C C   . THR B 206 ? 0.9153 0.6312 0.6843 -0.2222 -0.0600 0.0000  507 THR B C   
5021  O O   . THR B 206 ? 0.9191 0.6332 0.6804 -0.2288 -0.0645 -0.0086 507 THR B O   
5022  C CB  . THR B 206 ? 0.7401 0.5436 0.5544 -0.2242 -0.0557 0.0093  507 THR B CB  
5023  O OG1 . THR B 206 ? 0.7715 0.6157 0.6108 -0.2076 -0.0525 0.0129  507 THR B OG1 
5024  C CG2 . THR B 206 ? 0.7014 0.5285 0.5161 -0.2452 -0.0606 0.0026  507 THR B CG2 
5025  N N   . GLU B 207 ? 0.9954 0.6703 0.7453 -0.2274 -0.0581 0.0053  508 GLU B N   
5026  C CA  . GLU B 207 ? 1.0486 0.6706 0.7660 -0.2408 -0.0611 0.0008  508 GLU B CA  
5027  C C   . GLU B 207 ? 0.9709 0.5644 0.6743 -0.2221 -0.0631 -0.0073 508 GLU B C   
5028  O O   . GLU B 207 ? 0.8961 0.4681 0.5809 -0.2335 -0.0675 -0.0159 508 GLU B O   
5029  C CB  . GLU B 207 ? 1.0991 0.6794 0.7969 -0.2453 -0.0581 0.0093  508 GLU B CB  
5030  C CG  . GLU B 207 ? 1.3114 0.9021 1.0085 -0.2749 -0.0575 0.0148  508 GLU B CG  
5031  C CD  . GLU B 207 ? 1.4941 1.0528 1.1769 -0.2752 -0.0534 0.0256  508 GLU B CD  
5032  O OE1 . GLU B 207 ? 1.5713 1.0873 1.2363 -0.2557 -0.0524 0.0273  508 GLU B OE1 
5033  O OE2 . GLU B 207 ? 1.5037 1.0822 1.1929 -0.2940 -0.0512 0.0325  508 GLU B OE2 
5034  N N   . ILE B 208 ? 0.9191 0.5134 0.6307 -0.1940 -0.0600 -0.0049 509 ILE B N   
5035  C CA  . ILE B 208 ? 0.9344 0.5056 0.6337 -0.1748 -0.0611 -0.0121 509 ILE B CA  
5036  C C   . ILE B 208 ? 0.9387 0.5383 0.6468 -0.1782 -0.0649 -0.0210 509 ILE B C   
5037  O O   . ILE B 208 ? 0.9823 0.5562 0.6706 -0.1790 -0.0683 -0.0299 509 ILE B O   
5038  C CB  . ILE B 208 ? 0.9343 0.5125 0.6456 -0.1459 -0.0567 -0.0074 509 ILE B CB  
5039  C CG1 . ILE B 208 ? 0.9384 0.4905 0.6404 -0.1413 -0.0535 0.0014  509 ILE B CG1 
5040  C CG2 . ILE B 208 ? 1.0017 0.5600 0.7008 -0.1263 -0.0573 -0.0147 509 ILE B CG2 
5041  C CD1 . ILE B 208 ? 0.8447 0.4097 0.5604 -0.1148 -0.0494 0.0060  509 ILE B CD1 
5042  N N   . CYS B 209 ? 0.9090 0.5616 0.6453 -0.1795 -0.0644 -0.0189 510 CYS B N   
5043  C CA  . CYS B 209 ? 0.8484 0.5322 0.5937 -0.1822 -0.0681 -0.0262 510 CYS B CA  
5044  C C   . CYS B 209 ? 0.9068 0.5792 0.6352 -0.2086 -0.0738 -0.0336 510 CYS B C   
5045  O O   . CYS B 209 ? 0.9099 0.5735 0.6262 -0.2086 -0.0778 -0.0429 510 CYS B O   
5046  C CB  . CYS B 209 ? 0.8100 0.5503 0.5861 -0.1796 -0.0665 -0.0215 510 CYS B CB  
5047  S SG  . CYS B 209 ? 0.8639 0.6181 0.6589 -0.1500 -0.0602 -0.0143 510 CYS B SG  
5048  N N   . ILE B 210 ? 0.9759 0.6491 0.7025 -0.2324 -0.0741 -0.0298 511 ILE B N   
5049  C CA  . ILE B 210 ? 1.0370 0.6983 0.7461 -0.2613 -0.0794 -0.0367 511 ILE B CA  
5050  C C   . ILE B 210 ? 1.1201 0.7175 0.7937 -0.2612 -0.0814 -0.0434 511 ILE B C   
5051  O O   . ILE B 210 ? 1.1090 0.6959 0.7675 -0.2715 -0.0866 -0.0538 511 ILE B O   
5052  C CB  . ILE B 210 ? 1.0015 0.6724 0.7134 -0.2874 -0.0783 -0.0301 511 ILE B CB  
5053  C CG1 . ILE B 210 ? 0.9951 0.7280 0.7411 -0.2837 -0.0755 -0.0232 511 ILE B CG1 
5054  C CG2 . ILE B 210 ? 0.9965 0.6677 0.6953 -0.3196 -0.0838 -0.0376 511 ILE B CG2 
5055  C CD1 . ILE B 210 ? 0.9447 0.6881 0.6939 -0.3064 -0.0732 -0.0156 511 ILE B CD1 
5056  N N   . GLN B 211 ? 1.1511 0.7056 0.8102 -0.2477 -0.0775 -0.0379 512 GLN B N   
5057  C CA  . GLN B 211 ? 1.3059 0.7968 0.9304 -0.2404 -0.0784 -0.0430 512 GLN B CA  
5058  C C   . GLN B 211 ? 1.2958 0.7849 0.9177 -0.2168 -0.0795 -0.0513 512 GLN B C   
5059  O O   . GLN B 211 ? 1.3753 0.8146 0.9678 -0.2093 -0.0806 -0.0574 512 GLN B O   
5060  C CB  . GLN B 211 ? 1.4607 0.9179 1.0759 -0.2271 -0.0734 -0.0332 512 GLN B CB  
5061  C CG  . GLN B 211 ? 1.6500 1.0367 1.2258 -0.2218 -0.0739 -0.0362 512 GLN B CG  
5062  C CD  . GLN B 211 ? 1.7561 1.1173 1.3253 -0.2093 -0.0693 -0.0251 512 GLN B CD  
5063  O OE1 . GLN B 211 ? 1.7065 1.0776 1.2829 -0.2244 -0.0673 -0.0162 512 GLN B OE1 
5064  N NE2 . GLN B 211 ? 1.8520 1.1843 1.4085 -0.1806 -0.0673 -0.0255 512 GLN B NE2 
5065  N N   . GLN B 212 ? 1.1739 0.7144 0.8240 -0.2044 -0.0790 -0.0516 513 GLN B N   
5066  C CA  . GLN B 212 ? 1.0948 0.6379 0.7427 -0.1846 -0.0800 -0.0592 513 GLN B CA  
5067  C C   . GLN B 212 ? 1.0890 0.6627 0.7417 -0.1977 -0.0856 -0.0680 513 GLN B C   
5068  O O   . GLN B 212 ? 1.1504 0.7333 0.8034 -0.1824 -0.0865 -0.0739 513 GLN B O   
5069  C CB  . GLN B 212 ? 1.1122 0.6858 0.7850 -0.1575 -0.0748 -0.0525 513 GLN B CB  
5070  C CG  . GLN B 212 ? 1.1298 0.6708 0.7935 -0.1379 -0.0700 -0.0470 513 GLN B CG  
5071  C CD  . GLN B 212 ? 1.2320 0.7222 0.8632 -0.1284 -0.0714 -0.0550 513 GLN B CD  
5072  O OE1 . GLN B 212 ? 1.3394 0.7847 0.9483 -0.1266 -0.0704 -0.0530 513 GLN B OE1 
5073  N NE2 . GLN B 212 ? 1.1899 0.6860 0.8164 -0.1213 -0.0736 -0.0641 513 GLN B NE2 
5074  N N   . GLY B 213 ? 1.0710 0.6623 0.7270 -0.2258 -0.0892 -0.0689 514 GLY B N   
5075  C CA  . GLY B 213 ? 0.9735 0.5975 0.6339 -0.2402 -0.0952 -0.0774 514 GLY B CA  
5076  C C   . GLY B 213 ? 0.9678 0.6585 0.6622 -0.2428 -0.0952 -0.0722 514 GLY B C   
5077  O O   . GLY B 213 ? 0.9842 0.7085 0.6841 -0.2535 -0.1005 -0.0787 514 GLY B O   
5078  N N   . TRP B 214 ? 0.8676 0.5792 0.5837 -0.2321 -0.0897 -0.0612 515 TRP B N   
5079  C CA  . TRP B 214 ? 0.8860 0.6587 0.6321 -0.2335 -0.0896 -0.0565 515 TRP B CA  
5080  C C   . TRP B 214 ? 0.9439 0.7372 0.6915 -0.2653 -0.0933 -0.0577 515 TRP B C   
5081  O O   . TRP B 214 ? 0.8948 0.6585 0.6290 -0.2835 -0.0923 -0.0552 515 TRP B O   
5082  C CB  . TRP B 214 ? 0.8059 0.5913 0.5719 -0.2158 -0.0828 -0.0452 515 TRP B CB  
5083  C CG  . TRP B 214 ? 0.8760 0.7208 0.6710 -0.2114 -0.0820 -0.0406 515 TRP B CG  
5084  C CD1 . TRP B 214 ? 0.8932 0.7733 0.7005 -0.1982 -0.0837 -0.0431 515 TRP B CD1 
5085  C CD2 . TRP B 214 ? 0.8566 0.7306 0.6697 -0.2183 -0.0790 -0.0326 515 TRP B CD2 
5086  N NE1 . TRP B 214 ? 0.8760 0.8036 0.7070 -0.1957 -0.0823 -0.0374 515 TRP B NE1 
5087  C CE2 . TRP B 214 ? 0.8289 0.7548 0.6644 -0.2079 -0.0793 -0.0313 515 TRP B CE2 
5088  C CE3 . TRP B 214 ? 0.9171 0.7778 0.7282 -0.2315 -0.0760 -0.0263 515 TRP B CE3 
5089  C CZ2 . TRP B 214 ? 0.8373 0.8022 0.6932 -0.2094 -0.0767 -0.0246 515 TRP B CZ2 
5090  C CZ3 . TRP B 214 ? 0.9140 0.8157 0.7465 -0.2343 -0.0733 -0.0195 515 TRP B CZ3 
5091  C CH2 . TRP B 214 ? 0.8593 0.8127 0.7139 -0.2230 -0.0736 -0.0191 515 TRP B CH2 
5092  N N   . LYS B 215 ? 0.8856 0.7305 0.6485 -0.2720 -0.0976 -0.0614 516 LYS B N   
5093  C CA  . LYS B 215 ? 0.9746 0.8522 0.7438 -0.3013 -0.1009 -0.0624 516 LYS B CA  
5094  C C   . LYS B 215 ? 1.0364 0.9618 0.8342 -0.2957 -0.0966 -0.0524 516 LYS B C   
5095  O O   . LYS B 215 ? 1.1430 1.1146 0.9616 -0.2793 -0.0969 -0.0511 516 LYS B O   
5096  C CB  . LYS B 215 ? 1.0172 0.9286 0.7866 -0.3122 -0.1086 -0.0725 516 LYS B CB  
5097  C CG  . LYS B 215 ? 1.1610 1.0290 0.9027 -0.3127 -0.1129 -0.0834 516 LYS B CG  
5098  C CD  . LYS B 215 ? 1.2333 1.0381 0.9455 -0.3322 -0.1125 -0.0857 516 LYS B CD  
5099  C CE  . LYS B 215 ? 1.1958 0.9574 0.8779 -0.3344 -0.1174 -0.0980 516 LYS B CE  
5100  N NZ  . LYS B 215 ? 1.2114 0.9116 0.8619 -0.3566 -0.1178 -0.1010 516 LYS B NZ  
5101  N N   . PRO B 216 ? 0.9699 0.8841 0.7679 -0.3077 -0.0925 -0.0451 517 PRO B N   
5102  C CA  . PRO B 216 ? 0.9301 0.8877 0.7536 -0.3017 -0.0881 -0.0360 517 PRO B CA  
5103  C C   . PRO B 216 ? 0.8637 0.8835 0.7037 -0.3192 -0.0919 -0.0383 517 PRO B C   
5104  O O   . PRO B 216 ? 0.8199 0.8410 0.6494 -0.3488 -0.0961 -0.0435 517 PRO B O   
5105  C CB  . PRO B 216 ? 1.0112 0.9332 0.8246 -0.3134 -0.0833 -0.0286 517 PRO B CB  
5106  C CG  . PRO B 216 ? 1.0262 0.9039 0.8107 -0.3392 -0.0872 -0.0350 517 PRO B CG  
5107  C CD  . PRO B 216 ? 1.0068 0.8666 0.7791 -0.3283 -0.0920 -0.0451 517 PRO B CD  
5108  N N   . PRO B 217 ? 0.8660 0.9387 0.7308 -0.3016 -0.0906 -0.0350 518 PRO B N   
5109  C CA  . PRO B 217 ? 0.8665 1.0036 0.7492 -0.3166 -0.0930 -0.0353 518 PRO B CA  
5110  C C   . PRO B 217 ? 0.8558 1.0028 0.7442 -0.3353 -0.0885 -0.0280 518 PRO B C   
5111  O O   . PRO B 217 ? 0.8303 1.0292 0.7312 -0.3531 -0.0902 -0.0285 518 PRO B O   
5112  C CB  . PRO B 217 ? 0.8532 1.0344 0.7574 -0.2863 -0.0920 -0.0328 518 PRO B CB  
5113  C CG  . PRO B 217 ? 0.8306 0.9697 0.7255 -0.2601 -0.0905 -0.0332 518 PRO B CG  
5114  C CD  . PRO B 217 ? 0.8296 0.9059 0.7055 -0.2673 -0.0873 -0.0314 518 PRO B CD  
5115  N N   . ARG B 218 ? 0.8664 0.9679 0.7458 -0.3311 -0.0828 -0.0213 519 ARG B N   
5116  C CA  . ARG B 218 ? 0.9436 1.0441 0.8235 -0.3489 -0.0781 -0.0137 519 ARG B CA  
5117  C C   . ARG B 218 ? 0.9777 1.1454 0.8845 -0.3448 -0.0752 -0.0088 519 ARG B C   
5118  O O   . ARG B 218 ? 1.0021 1.2078 0.9153 -0.3693 -0.0758 -0.0083 519 ARG B O   
5119  C CB  . ARG B 218 ? 0.9681 1.0467 0.8280 -0.3866 -0.0811 -0.0171 519 ARG B CB  
5120  C CG  . ARG B 218 ? 0.9962 0.9999 0.8251 -0.3895 -0.0830 -0.0215 519 ARG B CG  
5121  C CD  . ARG B 218 ? 1.0769 1.0410 0.8816 -0.4233 -0.0827 -0.0201 519 ARG B CD  
5122  N NE  . ARG B 218 ? 1.1573 1.0737 0.9500 -0.4164 -0.0765 -0.0107 519 ARG B NE  
5123  C CZ  . ARG B 218 ? 1.1486 0.9941 0.9128 -0.4132 -0.0762 -0.0112 519 ARG B CZ  
5124  N NH1 . ARG B 218 ? 1.0618 0.8706 0.8167 -0.4052 -0.0707 -0.0019 519 ARG B NH1 
5125  N NH2 . ARG B 218 ? 1.1768 0.9888 0.9207 -0.4168 -0.0816 -0.0211 519 ARG B NH2 
5126  N N   . GLY B 219 ? 0.9383 1.1191 0.8597 -0.3131 -0.0719 -0.0052 520 GLY B N   
5127  C CA  . GLY B 219 ? 0.8281 1.0646 0.7725 -0.3023 -0.0685 -0.0004 520 GLY B CA  
5128  C C   . GLY B 219 ? 0.8201 1.0381 0.7683 -0.2838 -0.0613 0.0078  520 GLY B C   
5129  O O   . GLY B 219 ? 0.7569 0.9204 0.6903 -0.2818 -0.0590 0.0105  520 GLY B O   
5130  N N   . ARG B 220 ? 0.8008 1.0645 0.7681 -0.2692 -0.0580 0.0113  521 ARG B N   
5131  C CA  . ARG B 220 ? 0.7208 0.9709 0.6918 -0.2530 -0.0514 0.0184  521 ARG B CA  
5132  C C   . ARG B 220 ? 0.7935 1.0211 0.7651 -0.2215 -0.0503 0.0179  521 ARG B C   
5133  O O   . ARG B 220 ? 0.7855 0.9819 0.7534 -0.2105 -0.0459 0.0225  521 ARG B O   
5134  C CB  . ARG B 220 ? 0.6881 0.9953 0.6771 -0.2521 -0.0478 0.0221  521 ARG B CB  
5135  C CG  . ARG B 220 ? 0.6475 0.9432 0.6388 -0.2401 -0.0410 0.0290  521 ARG B CG  
5136  C CD  . ARG B 220 ? 0.8216 1.1366 0.8142 -0.2638 -0.0373 0.0343  521 ARG B CD  
5137  N NE  . ARG B 220 ? 0.8767 1.1890 0.8727 -0.2512 -0.0309 0.0407  521 ARG B NE  
5138  C CZ  . ARG B 220 ? 0.8982 1.2574 0.9096 -0.2379 -0.0274 0.0420  521 ARG B CZ  
5139  N NH1 . ARG B 220 ? 0.8994 1.3134 0.9246 -0.2343 -0.0297 0.0379  521 ARG B NH1 
5140  N NH2 . ARG B 220 ? 0.9283 1.2801 0.9404 -0.2273 -0.0218 0.0471  521 ARG B NH2 
5141  N N   . PHE B 221 ? 0.8456 1.0885 0.8210 -0.2076 -0.0543 0.0127  522 PHE B N   
5142  C CA  . PHE B 221 ? 0.7724 0.9948 0.7470 -0.1795 -0.0533 0.0123  522 PHE B CA  
5143  C C   . PHE B 221 ? 0.8444 1.0488 0.8088 -0.1792 -0.0589 0.0060  522 PHE B C   
5144  O O   . PHE B 221 ? 0.8893 1.1202 0.8590 -0.1669 -0.0620 0.0027  522 PHE B O   
5145  C CB  . PHE B 221 ? 0.7197 0.9834 0.7092 -0.1570 -0.0514 0.0137  522 PHE B CB  
5146  C CG  . PHE B 221 ? 0.7767 1.0591 0.7752 -0.1556 -0.0458 0.0190  522 PHE B CG  
5147  C CD1 . PHE B 221 ? 0.8339 1.0801 0.8267 -0.1558 -0.0411 0.0236  522 PHE B CD1 
5148  C CD2 . PHE B 221 ? 0.7374 1.0756 0.7497 -0.1533 -0.0454 0.0193  522 PHE B CD2 
5149  C CE1 . PHE B 221 ? 0.8160 1.0796 0.8159 -0.1547 -0.0361 0.0282  522 PHE B CE1 
5150  C CE2 . PHE B 221 ? 0.7994 1.1554 0.8190 -0.1515 -0.0400 0.0238  522 PHE B CE2 
5151  C CZ  . PHE B 221 ? 0.7728 1.0906 0.7859 -0.1527 -0.0354 0.0282  522 PHE B CZ  
5152  N N   . ASP B 222 ? 0.7492 0.9076 0.6974 -0.1918 -0.0600 0.0044  523 ASP B N   
5153  C CA  . ASP B 222 ? 0.6523 0.7866 0.5879 -0.1911 -0.0647 -0.0019 523 ASP B CA  
5154  C C   . ASP B 222 ? 0.6391 0.7344 0.5685 -0.1688 -0.0616 -0.0004 523 ASP B C   
5155  O O   . ASP B 222 ? 0.6234 0.6795 0.5437 -0.1701 -0.0585 0.0025  523 ASP B O   
5156  C CB  . ASP B 222 ? 0.6864 0.7920 0.6052 -0.2180 -0.0679 -0.0055 523 ASP B CB  
5157  C CG  . ASP B 222 ? 0.7635 0.9095 0.6868 -0.2431 -0.0722 -0.0089 523 ASP B CG  
5158  O OD1 . ASP B 222 ? 0.7754 0.9740 0.7144 -0.2371 -0.0740 -0.0101 523 ASP B OD1 
5159  O OD2 . ASP B 222 ? 0.7401 0.8653 0.6502 -0.2692 -0.0737 -0.0104 523 ASP B OD2 
5160  N N   . VAL B 223 ? 0.6979 0.8045 0.6314 -0.1486 -0.0623 -0.0020 524 VAL B N   
5161  C CA  . VAL B 223 ? 0.5501 0.6220 0.4769 -0.1297 -0.0595 -0.0010 524 VAL B CA  
5162  C C   . VAL B 223 ? 0.5234 0.5522 0.4322 -0.1386 -0.0614 -0.0050 524 VAL B C   
5163  O O   . VAL B 223 ? 0.5860 0.6149 0.4861 -0.1505 -0.0666 -0.0112 524 VAL B O   
5164  C CB  . VAL B 223 ? 0.6189 0.7088 0.5496 -0.1098 -0.0605 -0.0024 524 VAL B CB  
5165  C CG1 . VAL B 223 ? 0.4458 0.5008 0.3694 -0.0925 -0.0568 -0.0008 524 VAL B CG1 
5166  C CG2 . VAL B 223 ? 0.4619 0.5936 0.4077 -0.0990 -0.0589 0.0012  524 VAL B CG2 
5167  N N   . LEU B 224 ? 0.5808 0.5731 0.4830 -0.1326 -0.0574 -0.0019 525 LEU B N   
5168  C CA  . LEU B 224 ? 0.6281 0.5774 0.5116 -0.1382 -0.0587 -0.0054 525 LEU B CA  
5169  C C   . LEU B 224 ? 0.5780 0.5163 0.4544 -0.1238 -0.0601 -0.0100 525 LEU B C   
5170  O O   . LEU B 224 ? 0.6149 0.5689 0.5003 -0.1067 -0.0580 -0.0081 525 LEU B O   
5171  C CB  . LEU B 224 ? 0.6644 0.5820 0.5433 -0.1341 -0.0541 -0.0002 525 LEU B CB  
5172  C CG  . LEU B 224 ? 0.6943 0.6099 0.5729 -0.1509 -0.0529 0.0043  525 LEU B CG  
5173  C CD1 . LEU B 224 ? 0.5242 0.4265 0.4063 -0.1397 -0.0476 0.0109  525 LEU B CD1 
5174  C CD2 . LEU B 224 ? 0.8081 0.6901 0.6660 -0.1696 -0.0562 0.0008  525 LEU B CD2 
5175  N N   . PRO B 225 ? 0.6317 0.5417 0.4904 -0.1306 -0.0634 -0.0162 526 PRO B N   
5176  C CA  . PRO B 225 ? 0.5587 0.4559 0.4090 -0.1161 -0.0639 -0.0204 526 PRO B CA  
5177  C C   . PRO B 225 ? 0.6468 0.5193 0.4956 -0.0991 -0.0582 -0.0164 526 PRO B C   
5178  O O   . PRO B 225 ? 0.7587 0.6137 0.6066 -0.1009 -0.0553 -0.0121 526 PRO B O   
5179  C CB  . PRO B 225 ? 0.6248 0.4957 0.4545 -0.1302 -0.0688 -0.0285 526 PRO B CB  
5180  C CG  . PRO B 225 ? 0.7011 0.5492 0.5239 -0.1460 -0.0681 -0.0260 526 PRO B CG  
5181  C CD  . PRO B 225 ? 0.6226 0.5062 0.4654 -0.1514 -0.0662 -0.0193 526 PRO B CD  
5182  N N   . LEU B 226 ? 0.6095 0.4826 0.4576 -0.0827 -0.0567 -0.0175 527 LEU B N   
5183  C CA  . LEU B 226 ? 0.6817 0.5304 0.5252 -0.0684 -0.0520 -0.0154 527 LEU B CA  
5184  C C   . LEU B 226 ? 0.6088 0.4200 0.4317 -0.0721 -0.0537 -0.0206 527 LEU B C   
5185  O O   . LEU B 226 ? 0.6724 0.4755 0.4825 -0.0821 -0.0586 -0.0275 527 LEU B O   
5186  C CB  . LEU B 226 ? 0.5915 0.4507 0.4380 -0.0518 -0.0495 -0.0152 527 LEU B CB  
5187  C CG  . LEU B 226 ? 0.6276 0.5158 0.4911 -0.0451 -0.0468 -0.0092 527 LEU B CG  
5188  C CD1 . LEU B 226 ? 0.5221 0.4178 0.3851 -0.0308 -0.0446 -0.0087 527 LEU B CD1 
5189  C CD2 . LEU B 226 ? 0.4696 0.3544 0.3429 -0.0426 -0.0419 -0.0028 527 LEU B CD2 
5190  N N   . LEU B 227 ? 0.6615 0.4497 0.4803 -0.0639 -0.0499 -0.0176 528 LEU B N   
5191  C CA  . LEU B 227 ? 0.6140 0.3637 0.4117 -0.0624 -0.0507 -0.0218 528 LEU B CA  
5192  C C   . LEU B 227 ? 0.6757 0.4202 0.4744 -0.0422 -0.0457 -0.0199 528 LEU B C   
5193  O O   . LEU B 227 ? 0.6816 0.4251 0.4876 -0.0361 -0.0419 -0.0140 528 LEU B O   
5194  C CB  . LEU B 227 ? 0.6747 0.4012 0.4645 -0.0740 -0.0513 -0.0190 528 LEU B CB  
5195  C CG  . LEU B 227 ? 0.7805 0.4683 0.5446 -0.0858 -0.0553 -0.0248 528 LEU B CG  
5196  C CD1 . LEU B 227 ? 0.6859 0.3390 0.4371 -0.0825 -0.0532 -0.0207 528 LEU B CD1 
5197  C CD2 . LEU B 227 ? 0.7531 0.4248 0.5000 -0.0802 -0.0580 -0.0342 528 LEU B CD2 
5198  N N   . LEU B 228 ? 0.7704 0.5143 0.5621 -0.0323 -0.0456 -0.0249 529 LEU B N   
5199  C CA  . LEU B 228 ? 0.7161 0.4664 0.5124 -0.0144 -0.0404 -0.0229 529 LEU B CA  
5200  C C   . LEU B 228 ? 0.7739 0.4957 0.5509 -0.0035 -0.0397 -0.0279 529 LEU B C   
5201  O O   . LEU B 228 ? 0.7186 0.4217 0.4775 -0.0065 -0.0435 -0.0355 529 LEU B O   
5202  C CB  . LEU B 228 ? 0.6710 0.4471 0.4748 -0.0099 -0.0397 -0.0235 529 LEU B CB  
5203  C CG  . LEU B 228 ? 0.6719 0.4758 0.4924 -0.0181 -0.0407 -0.0191 529 LEU B CG  
5204  C CD1 . LEU B 228 ? 0.5181 0.3432 0.3430 -0.0105 -0.0396 -0.0187 529 LEU B CD1 
5205  C CD2 . LEU B 228 ? 0.5099 0.3220 0.3457 -0.0175 -0.0369 -0.0115 529 LEU B CD2 
5206  N N   . GLN B 229 ? 0.6884 0.4082 0.4687 0.0098  -0.0350 -0.0241 530 GLN B N   
5207  C CA  . GLN B 229 ? 0.7133 0.4098 0.4765 0.0236  -0.0337 -0.0280 530 GLN B CA  
5208  C C   . GLN B 229 ? 0.6846 0.4015 0.4552 0.0394  -0.0282 -0.0271 530 GLN B C   
5209  O O   . GLN B 229 ? 0.6478 0.3852 0.4351 0.0435  -0.0240 -0.0206 530 GLN B O   
5210  C CB  . GLN B 229 ? 0.7540 0.4301 0.5122 0.0263  -0.0331 -0.0243 530 GLN B CB  
5211  C CG  . GLN B 229 ? 0.8442 0.5016 0.5871 0.0450  -0.0309 -0.0270 530 GLN B CG  
5212  C CD  . GLN B 229 ? 0.9500 0.5955 0.6917 0.0506  -0.0297 -0.0214 530 GLN B CD  
5213  O OE1 . GLN B 229 ? 0.8745 0.5107 0.6173 0.0382  -0.0319 -0.0174 530 GLN B OE1 
5214  N NE2 . GLN B 229 ? 1.0652 0.7139 0.8049 0.0698  -0.0262 -0.0209 530 GLN B NE2 
5215  N N   . ALA B 230 ? 0.7222 0.4336 0.4794 0.0473  -0.0283 -0.0337 531 ALA B N   
5216  C CA  . ALA B 230 ? 0.6043 0.3339 0.3648 0.0620  -0.0229 -0.0335 531 ALA B CA  
5217  C C   . ALA B 230 ? 0.7064 0.4172 0.4502 0.0784  -0.0212 -0.0379 531 ALA B C   
5218  O O   . ALA B 230 ? 0.7430 0.4229 0.4651 0.0795  -0.0251 -0.0448 531 ALA B O   
5219  C CB  . ALA B 230 ? 0.6022 0.3436 0.3593 0.0606  -0.0236 -0.0375 531 ALA B CB  
5220  N N   . ASN B 231 ? 0.7477 0.4777 0.5011 0.0912  -0.0155 -0.0341 532 ASN B N   
5221  C CA  . ASN B 231 ? 0.8296 0.5522 0.5700 0.1104  -0.0127 -0.0378 532 ASN B CA  
5222  C C   . ASN B 231 ? 0.8763 0.5593 0.5950 0.1154  -0.0168 -0.0418 532 ASN B C   
5223  O O   . ASN B 231 ? 0.8218 0.4836 0.5186 0.1281  -0.0173 -0.0490 532 ASN B O   
5224  C CB  . ASN B 231 ? 0.8500 0.5796 0.5804 0.1191  -0.0106 -0.0438 532 ASN B CB  
5225  C CG  . ASN B 231 ? 0.9929 0.7337 0.7194 0.1396  -0.0052 -0.0451 532 ASN B CG  
5226  O OD1 . ASN B 231 ? 1.0401 0.8052 0.7828 0.1441  -0.0009 -0.0390 532 ASN B OD1 
5227  N ND2 . ASN B 231 ? 0.9707 0.6950 0.6751 0.1525  -0.0056 -0.0535 532 ASN B ND2 
5228  N N   . GLY B 232 ? 0.8780 0.5493 0.6011 0.1056  -0.0194 -0.0369 533 GLY B N   
5229  C CA  . GLY B 232 ? 0.8391 0.4712 0.5411 0.1097  -0.0227 -0.0387 533 GLY B CA  
5230  C C   . GLY B 232 ? 0.9595 0.5530 0.6375 0.0994  -0.0283 -0.0460 533 GLY B C   
5231  O O   . GLY B 232 ? 1.0574 0.6135 0.7162 0.0990  -0.0313 -0.0468 533 GLY B O   
5232  N N   . ASN B 233 ? 0.9644 0.5648 0.6416 0.0904  -0.0301 -0.0514 534 ASN B N   
5233  C CA  . ASN B 233 ? 0.9903 0.5568 0.6448 0.0786  -0.0360 -0.0593 534 ASN B CA  
5234  C C   . ASN B 233 ? 0.9151 0.4731 0.5749 0.0555  -0.0401 -0.0552 534 ASN B C   
5235  O O   . ASN B 233 ? 0.9452 0.5260 0.6271 0.0493  -0.0384 -0.0466 534 ASN B O   
5236  C CB  . ASN B 233 ? 1.0216 0.6036 0.6752 0.0757  -0.0369 -0.0659 534 ASN B CB  
5237  C CG  . ASN B 233 ? 1.0108 0.6069 0.6612 0.0976  -0.0319 -0.0691 534 ASN B CG  
5238  O OD1 . ASN B 233 ? 1.1128 0.6846 0.7421 0.1141  -0.0310 -0.0744 534 ASN B OD1 
5239  N ND2 . ASN B 233 ? 0.9708 0.6062 0.6411 0.0982  -0.0283 -0.0656 534 ASN B ND2 
5240  N N   . ASP B 234 ? 0.9436 0.4689 0.5817 0.0420  -0.0455 -0.0619 535 ASP B N   
5241  C CA  . ASP B 234 ? 0.9719 0.4906 0.6133 0.0180  -0.0495 -0.0589 535 ASP B CA  
5242  C C   . ASP B 234 ? 0.9693 0.5340 0.6400 0.0054  -0.0495 -0.0545 535 ASP B C   
5243  O O   . ASP B 234 ? 0.9964 0.5877 0.6763 0.0104  -0.0485 -0.0569 535 ASP B O   
5244  C CB  . ASP B 234 ? 1.1142 0.5940 0.7271 0.0034  -0.0554 -0.0682 535 ASP B CB  
5245  C CG  . ASP B 234 ? 1.1812 0.6062 0.7611 0.0124  -0.0560 -0.0715 535 ASP B CG  
5246  O OD1 . ASP B 234 ? 1.1553 0.5745 0.7354 0.0308  -0.0521 -0.0658 535 ASP B OD1 
5247  O OD2 . ASP B 234 ? 1.2240 0.6110 0.7764 0.0012  -0.0606 -0.0799 535 ASP B OD2 
5248  N N   . PRO B 235 ? 0.9164 0.4914 0.6012 -0.0098 -0.0502 -0.0476 536 PRO B N   
5249  C CA  . PRO B 235 ? 0.8247 0.4418 0.5352 -0.0204 -0.0504 -0.0438 536 PRO B CA  
5250  C C   . PRO B 235 ? 0.8247 0.4460 0.5294 -0.0371 -0.0560 -0.0508 536 PRO B C   
5251  O O   . PRO B 235 ? 0.9366 0.5266 0.6187 -0.0477 -0.0603 -0.0576 536 PRO B O   
5252  C CB  . PRO B 235 ? 0.8004 0.4232 0.5240 -0.0302 -0.0494 -0.0350 536 PRO B CB  
5253  C CG  . PRO B 235 ? 0.7762 0.3552 0.4766 -0.0325 -0.0507 -0.0355 536 PRO B CG  
5254  C CD  . PRO B 235 ? 0.8359 0.3884 0.5157 -0.0132 -0.0497 -0.0414 536 PRO B CD  
5255  N N   . GLU B 236 ? 0.7763 0.4370 0.5009 -0.0395 -0.0560 -0.0490 537 GLU B N   
5256  C CA  . GLU B 236 ? 0.8158 0.4906 0.5384 -0.0529 -0.0613 -0.0551 537 GLU B CA  
5257  C C   . GLU B 236 ? 0.7730 0.4848 0.5187 -0.0650 -0.0622 -0.0492 537 GLU B C   
5258  O O   . GLU B 236 ? 0.7695 0.5067 0.5352 -0.0559 -0.0580 -0.0418 537 GLU B O   
5259  C CB  . GLU B 236 ? 0.7810 0.4687 0.5009 -0.0393 -0.0607 -0.0600 537 GLU B CB  
5260  C CG  . GLU B 236 ? 0.8880 0.5447 0.5866 -0.0235 -0.0587 -0.0656 537 GLU B CG  
5261  C CD  . GLU B 236 ? 0.9484 0.6187 0.6428 -0.0110 -0.0579 -0.0706 537 GLU B CD  
5262  O OE1 . GLU B 236 ? 0.8898 0.5833 0.5888 -0.0184 -0.0614 -0.0729 537 GLU B OE1 
5263  O OE2 . GLU B 236 ? 0.9286 0.5880 0.6146 0.0068  -0.0536 -0.0719 537 GLU B OE2 
5264  N N   . LEU B 237 ? 0.7033 0.4188 0.4455 -0.0855 -0.0678 -0.0529 538 LEU B N   
5265  C CA  . LEU B 237 ? 0.7495 0.5038 0.5125 -0.0965 -0.0691 -0.0483 538 LEU B CA  
5266  C C   . LEU B 237 ? 0.7686 0.5594 0.5427 -0.0890 -0.0703 -0.0495 538 LEU B C   
5267  O O   . LEU B 237 ? 0.7477 0.5347 0.5092 -0.0863 -0.0733 -0.0568 538 LEU B O   
5268  C CB  . LEU B 237 ? 0.6706 0.4201 0.4259 -0.1222 -0.0745 -0.0519 538 LEU B CB  
5269  C CG  . LEU B 237 ? 0.8091 0.5270 0.5558 -0.1321 -0.0729 -0.0481 538 LEU B CG  
5270  C CD1 . LEU B 237 ? 0.8479 0.5525 0.5804 -0.1593 -0.0781 -0.0530 538 LEU B CD1 
5271  C CD2 . LEU B 237 ? 0.7262 0.4660 0.4950 -0.1284 -0.0681 -0.0374 538 LEU B CD2 
5272  N N   . PHE B 238 ? 0.6997 0.5245 0.4956 -0.0847 -0.0678 -0.0421 539 PHE B N   
5273  C CA  . PHE B 238 ? 0.7040 0.5650 0.5106 -0.0783 -0.0692 -0.0415 539 PHE B CA  
5274  C C   . PHE B 238 ? 0.7722 0.6671 0.5976 -0.0857 -0.0697 -0.0362 539 PHE B C   
5275  O O   . PHE B 238 ? 0.7301 0.6240 0.5657 -0.0853 -0.0657 -0.0297 539 PHE B O   
5276  C CB  . PHE B 238 ? 0.6351 0.4996 0.4467 -0.0568 -0.0635 -0.0369 539 PHE B CB  
5277  C CG  . PHE B 238 ? 0.7270 0.5637 0.5222 -0.0468 -0.0617 -0.0414 539 PHE B CG  
5278  C CD1 . PHE B 238 ? 0.7269 0.5352 0.5168 -0.0418 -0.0576 -0.0399 539 PHE B CD1 
5279  C CD2 . PHE B 238 ? 0.6549 0.4960 0.4396 -0.0412 -0.0641 -0.0470 539 PHE B CD2 
5280  C CE1 . PHE B 238 ? 0.7540 0.5397 0.5287 -0.0307 -0.0558 -0.0442 539 PHE B CE1 
5281  C CE2 . PHE B 238 ? 0.7055 0.5229 0.4745 -0.0310 -0.0620 -0.0514 539 PHE B CE2 
5282  C CZ  . PHE B 238 ? 0.7532 0.5436 0.5174 -0.0253 -0.0578 -0.0502 539 PHE B CZ  
5283  N N   . GLN B 239 ? 0.8725 0.7997 0.7025 -0.0911 -0.0746 -0.0389 540 GLN B N   
5284  C CA  . GLN B 239 ? 0.7953 0.7602 0.6434 -0.0947 -0.0751 -0.0340 540 GLN B CA  
5285  C C   . GLN B 239 ? 0.6462 0.6321 0.5049 -0.0740 -0.0716 -0.0281 540 GLN B C   
5286  O O   . GLN B 239 ? 0.5430 0.5376 0.3964 -0.0643 -0.0734 -0.0303 540 GLN B O   
5287  C CB  . GLN B 239 ? 0.8080 0.8011 0.6558 -0.1115 -0.0825 -0.0400 540 GLN B CB  
5288  C CG  . GLN B 239 ? 0.9077 0.9480 0.7742 -0.1106 -0.0833 -0.0356 540 GLN B CG  
5289  C CD  . GLN B 239 ? 1.0835 1.1600 0.9508 -0.1067 -0.0891 -0.0395 540 GLN B CD  
5290  O OE1 . GLN B 239 ? 1.1144 1.1852 0.9738 -0.0923 -0.0894 -0.0409 540 GLN B OE1 
5291  N NE2 . GLN B 239 ? 1.0522 1.1687 0.9292 -0.1194 -0.0936 -0.0411 540 GLN B NE2 
5292  N N   . ILE B 240 ? 0.4916 0.4831 0.3631 -0.0674 -0.0665 -0.0206 541 ILE B N   
5293  C CA  . ILE B 240 ? 0.4924 0.5000 0.3717 -0.0486 -0.0629 -0.0149 541 ILE B CA  
5294  C C   . ILE B 240 ? 0.5344 0.5815 0.4191 -0.0473 -0.0677 -0.0159 541 ILE B C   
5295  O O   . ILE B 240 ? 0.5414 0.6127 0.4337 -0.0601 -0.0713 -0.0173 541 ILE B O   
5296  C CB  . ILE B 240 ? 0.5794 0.5849 0.4700 -0.0434 -0.0570 -0.0078 541 ILE B CB  
5297  C CG1 . ILE B 240 ? 0.5756 0.5464 0.4616 -0.0457 -0.0530 -0.0070 541 ILE B CG1 
5298  C CG2 . ILE B 240 ? 0.4787 0.4928 0.3731 -0.0247 -0.0531 -0.0024 541 ILE B CG2 
5299  C CD1 . ILE B 240 ? 0.5534 0.5234 0.4497 -0.0416 -0.0478 -0.0008 541 ILE B CD1 
5300  N N   . PRO B 241 ? 0.5436 0.6002 0.4241 -0.0325 -0.0683 -0.0151 542 PRO B N   
5301  C CA  . PRO B 241 ? 0.6015 0.6974 0.4865 -0.0286 -0.0731 -0.0154 542 PRO B CA  
5302  C C   . PRO B 241 ? 0.5741 0.6943 0.4738 -0.0251 -0.0710 -0.0101 542 PRO B C   
5303  O O   . PRO B 241 ? 0.5057 0.6134 0.4089 -0.0134 -0.0648 -0.0040 542 PRO B O   
5304  C CB  . PRO B 241 ? 0.6546 0.7473 0.5305 -0.0093 -0.0717 -0.0129 542 PRO B CB  
5305  C CG  . PRO B 241 ? 0.5994 0.6553 0.4635 -0.0102 -0.0690 -0.0152 542 PRO B CG  
5306  C CD  . PRO B 241 ? 0.6273 0.6599 0.4968 -0.0195 -0.0648 -0.0141 542 PRO B CD  
5307  N N   . PRO B 242 ? 0.5874 0.7430 0.4953 -0.0360 -0.0759 -0.0128 543 PRO B N   
5308  C CA  . PRO B 242 ? 0.5403 0.7206 0.4624 -0.0348 -0.0738 -0.0086 543 PRO B CA  
5309  C C   . PRO B 242 ? 0.7157 0.9070 0.6401 -0.0105 -0.0704 -0.0024 543 PRO B C   
5310  O O   . PRO B 242 ? 0.5958 0.7877 0.5279 -0.0047 -0.0657 0.0022  543 PRO B O   
5311  C CB  . PRO B 242 ? 0.4861 0.7086 0.4147 -0.0502 -0.0806 -0.0136 543 PRO B CB  
5312  C CG  . PRO B 242 ? 0.5303 0.7372 0.4471 -0.0660 -0.0857 -0.0210 543 PRO B CG  
5313  C CD  . PRO B 242 ? 0.5305 0.7082 0.4348 -0.0499 -0.0838 -0.0203 543 PRO B CD  
5314  N N   . GLU B 243 ? 0.4401 0.6373 0.3560 0.0042  -0.0727 -0.0022 544 GLU B N   
5315  C CA  . GLU B 243 ? 0.5095 0.7126 0.4234 0.0282  -0.0697 0.0040  544 GLU B CA  
5316  C C   . GLU B 243 ? 0.5084 0.6709 0.4175 0.0373  -0.0617 0.0094  544 GLU B C   
5317  O O   . GLU B 243 ? 0.5235 0.6840 0.4296 0.0554  -0.0581 0.0149  544 GLU B O   
5318  C CB  . GLU B 243 ? 0.4680 0.6833 0.3709 0.0410  -0.0741 0.0035  544 GLU B CB  
5319  C CG  . GLU B 243 ? 0.5234 0.7049 0.4125 0.0399  -0.0732 0.0021  544 GLU B CG  
5320  C CD  . GLU B 243 ? 0.6149 0.8024 0.5014 0.0212  -0.0796 -0.0064 544 GLU B CD  
5321  O OE1 . GLU B 243 ? 0.6220 0.8321 0.5182 0.0047  -0.0835 -0.0108 544 GLU B OE1 
5322  O OE2 . GLU B 243 ? 0.7877 0.9577 0.6613 0.0225  -0.0806 -0.0089 544 GLU B OE2 
5323  N N   . LEU B 244 ? 0.5654 0.6956 0.4722 0.0253  -0.0590 0.0078  545 LEU B N   
5324  C CA  . LEU B 244 ? 0.4275 0.5238 0.3321 0.0304  -0.0517 0.0122  545 LEU B CA  
5325  C C   . LEU B 244 ? 0.5246 0.6192 0.4402 0.0222  -0.0486 0.0133  545 LEU B C   
5326  O O   . LEU B 244 ? 0.5396 0.6110 0.4545 0.0271  -0.0428 0.0169  545 LEU B O   
5327  C CB  . LEU B 244 ? 0.4681 0.5326 0.3638 0.0244  -0.0502 0.0102  545 LEU B CB  
5328  C CG  . LEU B 244 ? 0.5291 0.5883 0.4117 0.0324  -0.0518 0.0093  545 LEU B CG  
5329  C CD1 . LEU B 244 ? 0.5115 0.5416 0.3871 0.0252  -0.0498 0.0065  545 LEU B CD1 
5330  C CD2 . LEU B 244 ? 0.5062 0.5604 0.3816 0.0514  -0.0477 0.0160  545 LEU B CD2 
5331  N N   . VAL B 245 ? 0.4493 0.5685 0.3744 0.0090  -0.0523 0.0103  546 VAL B N   
5332  C CA  . VAL B 245 ? 0.5513 0.6693 0.4859 -0.0008 -0.0494 0.0115  546 VAL B CA  
5333  C C   . VAL B 245 ? 0.3996 0.5503 0.3429 0.0084  -0.0490 0.0138  546 VAL B C   
5334  O O   . VAL B 245 ? 0.4313 0.6180 0.3819 0.0018  -0.0532 0.0116  546 VAL B O   
5335  C CB  . VAL B 245 ? 0.5244 0.6437 0.4614 -0.0232 -0.0529 0.0072  546 VAL B CB  
5336  C CG1 . VAL B 245 ? 0.4741 0.5938 0.4197 -0.0325 -0.0497 0.0095  546 VAL B CG1 
5337  C CG2 . VAL B 245 ? 0.6118 0.6964 0.5379 -0.0293 -0.0532 0.0044  546 VAL B CG2 
5338  N N   . LEU B 246 ? 0.4232 0.5618 0.3649 0.0237  -0.0438 0.0181  547 LEU B N   
5339  C CA  . LEU B 246 ? 0.4694 0.6345 0.4167 0.0357  -0.0426 0.0201  547 LEU B CA  
5340  C C   . LEU B 246 ? 0.5147 0.6945 0.4737 0.0225  -0.0414 0.0196  547 LEU B C   
5341  O O   . LEU B 246 ? 0.5468 0.7017 0.5065 0.0123  -0.0384 0.0202  547 LEU B O   
5342  C CB  . LEU B 246 ? 0.4534 0.5940 0.3922 0.0545  -0.0371 0.0243  547 LEU B CB  
5343  C CG  . LEU B 246 ? 0.5271 0.6873 0.4675 0.0708  -0.0352 0.0262  547 LEU B CG  
5344  C CD1 . LEU B 246 ? 0.6005 0.8012 0.5426 0.0801  -0.0405 0.0252  547 LEU B CD1 
5345  C CD2 . LEU B 246 ? 0.5534 0.6806 0.4806 0.0875  -0.0301 0.0297  547 LEU B CD2 
5346  N N   . GLU B 247 ? 0.5152 0.7374 0.4830 0.0227  -0.0439 0.0187  548 GLU B N   
5347  C CA  . GLU B 247 ? 0.4681 0.7102 0.4468 0.0102  -0.0426 0.0187  548 GLU B CA  
5348  C C   . GLU B 247 ? 0.5051 0.7800 0.4892 0.0268  -0.0408 0.0201  548 GLU B C   
5349  O O   . GLU B 247 ? 0.6253 0.9215 0.6069 0.0439  -0.0430 0.0200  548 GLU B O   
5350  C CB  . GLU B 247 ? 0.4848 0.7518 0.4700 -0.0126 -0.0476 0.0153  548 GLU B CB  
5351  C CG  . GLU B 247 ? 0.5387 0.7712 0.5171 -0.0305 -0.0492 0.0134  548 GLU B CG  
5352  C CD  . GLU B 247 ? 0.5746 0.8289 0.5561 -0.0535 -0.0545 0.0095  548 GLU B CD  
5353  O OE1 . GLU B 247 ? 0.6533 0.9440 0.6381 -0.0524 -0.0593 0.0067  548 GLU B OE1 
5354  O OE2 . GLU B 247 ? 0.6318 0.8672 0.6116 -0.0729 -0.0539 0.0092  548 GLU B OE2 
5355  N N   . VAL B 248 ? 0.5064 0.7854 0.4967 0.0227  -0.0368 0.0214  549 VAL B N   
5356  C CA  . VAL B 248 ? 0.4964 0.8037 0.4907 0.0388  -0.0341 0.0223  549 VAL B CA  
5357  C C   . VAL B 248 ? 0.6076 0.9578 0.6154 0.0225  -0.0349 0.0214  549 VAL B C   
5358  O O   . VAL B 248 ? 0.7297 1.0681 0.7408 0.0036  -0.0330 0.0222  549 VAL B O   
5359  C CB  . VAL B 248 ? 0.5677 0.8418 0.5556 0.0500  -0.0279 0.0243  549 VAL B CB  
5360  C CG1 . VAL B 248 ? 0.4999 0.8025 0.4903 0.0672  -0.0250 0.0244  549 VAL B CG1 
5361  C CG2 . VAL B 248 ? 0.5328 0.7643 0.5066 0.0633  -0.0267 0.0254  549 VAL B CG2 
5362  N N   . PRO B 249 ? 0.5407 0.9424 0.5561 0.0286  -0.0377 0.0201  550 PRO B N   
5363  C CA  . PRO B 249 ? 0.4353 0.8817 0.4639 0.0130  -0.0374 0.0197  550 PRO B CA  
5364  C C   . PRO B 249 ? 0.5589 1.0123 0.5896 0.0252  -0.0313 0.0214  550 PRO B C   
5365  O O   . PRO B 249 ? 0.6680 1.1222 0.6933 0.0518  -0.0293 0.0216  550 PRO B O   
5366  C CB  . PRO B 249 ? 0.4321 0.9338 0.4676 0.0181  -0.0428 0.0173  550 PRO B CB  
5367  C CG  . PRO B 249 ? 0.5247 1.0134 0.5495 0.0481  -0.0436 0.0176  550 PRO B CG  
5368  C CD  . PRO B 249 ? 0.5523 0.9757 0.5642 0.0487  -0.0415 0.0191  550 PRO B CD  
5369  N N   . ILE B 250 ? 0.4585 0.9146 0.4951 0.0061  -0.0283 0.0228  551 ILE B N   
5370  C CA  . ILE B 250 ? 0.4604 0.9169 0.4975 0.0155  -0.0222 0.0243  551 ILE B CA  
5371  C C   . ILE B 250 ? 0.4575 0.9770 0.5054 0.0222  -0.0214 0.0235  551 ILE B C   
5372  O O   . ILE B 250 ? 0.4633 1.0225 0.5220 0.0016  -0.0231 0.0236  551 ILE B O   
5373  C CB  . ILE B 250 ? 0.4677 0.8972 0.5045 -0.0063 -0.0191 0.0268  551 ILE B CB  
5374  C CG1 . ILE B 250 ? 0.4094 0.7837 0.4371 -0.0155 -0.0207 0.0273  551 ILE B CG1 
5375  C CG2 . ILE B 250 ? 0.3458 0.7692 0.3804 0.0066  -0.0129 0.0278  551 ILE B CG2 
5376  C CD1 . ILE B 250 ? 0.3500 0.6860 0.3670 0.0060  -0.0196 0.0267  551 ILE B CD1 
5377  N N   . ARG B 251 ? 0.4774 1.0057 0.5212 0.0507  -0.0185 0.0227  552 ARG B N   
5378  C CA  . ARG B 251 ? 0.4971 1.0829 0.5495 0.0618  -0.0163 0.0218  552 ARG B CA  
5379  C C   . ARG B 251 ? 0.4336 1.0023 0.4788 0.0792  -0.0099 0.0218  552 ARG B C   
5380  O O   . ARG B 251 ? 0.4043 0.9181 0.4373 0.0854  -0.0077 0.0220  552 ARG B O   
5381  C CB  . ARG B 251 ? 0.5320 1.1560 0.5853 0.0844  -0.0203 0.0198  552 ARG B CB  
5382  C CG  . ARG B 251 ? 0.5533 1.1363 0.5901 0.1128  -0.0205 0.0194  552 ARG B CG  
5383  C CD  . ARG B 251 ? 0.5437 1.0926 0.5748 0.1038  -0.0255 0.0199  552 ARG B CD  
5384  N NE  . ARG B 251 ? 0.6048 1.1250 0.6200 0.1322  -0.0261 0.0202  552 ARG B NE  
5385  C CZ  . ARG B 251 ? 0.5703 1.0474 0.5753 0.1309  -0.0284 0.0212  552 ARG B CZ  
5386  N NH1 . ARG B 251 ? 0.6087 1.0611 0.5979 0.1569  -0.0282 0.0222  552 ARG B NH1 
5387  N NH2 . ARG B 251 ? 0.5124 0.9698 0.5214 0.1043  -0.0306 0.0213  552 ARG B NH2 
5388  N N   . HIS B 252 ? 0.4116 1.0303 0.4643 0.0871  -0.0067 0.0210  553 HIS B N   
5389  C CA  . HIS B 252 ? 0.4272 1.0343 0.4731 0.1016  -0.0004 0.0203  553 HIS B CA  
5390  C C   . HIS B 252 ? 0.4878 1.1201 0.5277 0.1373  0.0011  0.0173  553 HIS B C   
5391  O O   . HIS B 252 ? 0.5574 1.2461 0.6065 0.1454  -0.0013 0.0164  553 HIS B O   
5392  C CB  . HIS B 252 ? 0.3667 1.0061 0.4236 0.0812  0.0036  0.0220  553 HIS B CB  
5393  C CG  . HIS B 252 ? 0.5381 1.1539 0.5865 0.0898  0.0097  0.0215  553 HIS B CG  
5394  N ND1 . HIS B 252 ? 0.5804 1.2241 0.6259 0.1145  0.0140  0.0186  553 HIS B ND1 
5395  C CD2 . HIS B 252 ? 0.5289 1.0972 0.5704 0.0776  0.0121  0.0230  553 HIS B CD2 
5396  C CE1 . HIS B 252 ? 0.5598 1.1728 0.5965 0.1160  0.0186  0.0181  553 HIS B CE1 
5397  N NE2 . HIS B 252 ? 0.5656 1.1338 0.6003 0.0937  0.0174  0.0209  553 HIS B NE2 
5398  N N   . PRO B 253 ? 0.4265 1.0181 0.4501 0.1594  0.0048  0.0154  554 PRO B N   
5399  C CA  . PRO B 253 ? 0.4458 1.0511 0.4587 0.1962  0.0061  0.0124  554 PRO B CA  
5400  C C   . PRO B 253 ? 0.5078 1.1777 0.5297 0.2072  0.0094  0.0105  554 PRO B C   
5401  O O   . PRO B 253 ? 0.5379 1.2315 0.5532 0.2385  0.0096  0.0082  554 PRO B O   
5402  C CB  . PRO B 253 ? 0.5141 1.0525 0.5056 0.2105  0.0097  0.0106  554 PRO B CB  
5403  C CG  . PRO B 253 ? 0.5714 1.0766 0.5665 0.1814  0.0112  0.0123  554 PRO B CG  
5404  C CD  . PRO B 253 ? 0.4082 0.9329 0.4198 0.1521  0.0069  0.0158  554 PRO B CD  
5405  N N   . LYS B 254 ? 0.5791 1.2783 0.6147 0.1838  0.0124  0.0118  555 LYS B N   
5406  C CA  . LYS B 254 ? 0.5872 1.3528 0.6328 0.1912  0.0162  0.0105  555 LYS B CA  
5407  C C   . LYS B 254 ? 0.5439 1.3695 0.6118 0.1611  0.0145  0.0135  555 LYS B C   
5408  O O   . LYS B 254 ? 0.5377 1.4322 0.6170 0.1695  0.0145  0.0125  555 LYS B O   
5409  C CB  . LYS B 254 ? 0.7079 1.4554 0.7457 0.1941  0.0230  0.0089  555 LYS B CB  
5410  C CG  . LYS B 254 ? 0.8348 1.5584 0.8521 0.2326  0.0263  0.0039  555 LYS B CG  
5411  C CD  . LYS B 254 ? 0.9181 1.6870 0.9347 0.2643  0.0244  0.0016  555 LYS B CD  
5412  C CE  . LYS B 254 ? 0.9234 1.7173 0.9304 0.2959  0.0301  -0.0032 555 LYS B CE  
5413  N NZ  . LYS B 254 ? 0.9439 1.6686 0.9259 0.3117  0.0337  -0.0070 555 LYS B NZ  
5414  N N   . PHE B 255 ? 0.5778 1.3786 0.6512 0.1263  0.0132  0.0171  556 PHE B N   
5415  C CA  . PHE B 255 ? 0.5326 1.3800 0.6238 0.0932  0.0118  0.0202  556 PHE B CA  
5416  C C   . PHE B 255 ? 0.5127 1.3769 0.6103 0.0878  0.0044  0.0198  556 PHE B C   
5417  O O   . PHE B 255 ? 0.4715 1.2892 0.5644 0.0737  0.0002  0.0209  556 PHE B O   
5418  C CB  . PHE B 255 ? 0.5580 1.3644 0.6481 0.0603  0.0133  0.0243  556 PHE B CB  
5419  C CG  . PHE B 255 ? 0.4839 1.2744 0.5674 0.0637  0.0202  0.0249  556 PHE B CG  
5420  C CD1 . PHE B 255 ? 0.4498 1.2858 0.5353 0.0832  0.0253  0.0227  556 PHE B CD1 
5421  C CD2 . PHE B 255 ? 0.5119 1.2436 0.5868 0.0481  0.0213  0.0275  556 PHE B CD2 
5422  C CE1 . PHE B 255 ? 0.4434 1.2651 0.5217 0.0862  0.0315  0.0227  556 PHE B CE1 
5423  C CE2 . PHE B 255 ? 0.3921 1.1108 0.4605 0.0509  0.0271  0.0279  556 PHE B CE2 
5424  C CZ  . PHE B 255 ? 0.4380 1.2011 0.5078 0.0696  0.0322  0.0254  556 PHE B CZ  
5425  N N   . GLU B 256 ? 0.5686 1.5019 0.6768 0.0997  0.0028  0.0179  557 GLU B N   
5426  C CA  . GLU B 256 ? 0.6043 1.5627 0.7195 0.0943  -0.0046 0.0171  557 GLU B CA  
5427  C C   . GLU B 256 ? 0.6313 1.5926 0.7564 0.0507  -0.0078 0.0194  557 GLU B C   
5428  O O   . GLU B 256 ? 0.7259 1.6812 0.8518 0.0412  -0.0144 0.0186  557 GLU B O   
5429  C CB  . GLU B 256 ? 0.6546 1.6777 0.7720 0.1125  -0.0051 0.0144  557 GLU B CB  
5430  C CG  . GLU B 256 ? 0.7861 1.7988 0.8875 0.1571  -0.0028 0.0117  557 GLU B CG  
5431  C CD  . GLU B 256 ? 0.9466 1.9913 1.0396 0.1772  -0.0062 0.0091  557 GLU B CD  
5432  O OE1 . GLU B 256 ? 1.0038 2.0890 1.1050 0.1556  -0.0092 0.0089  557 GLU B OE1 
5433  O OE2 . GLU B 256 ? 1.0273 2.0546 1.1038 0.2142  -0.0057 0.0073  557 GLU B OE2 
5434  N N   . TRP B 257 ? 0.5203 1.4882 0.6509 0.0242  -0.0031 0.0224  558 TRP B N   
5435  C CA  . TRP B 257 ? 0.4622 1.4263 0.5985 -0.0179 -0.0055 0.0251  558 TRP B CA  
5436  C C   . TRP B 257 ? 0.4727 1.3544 0.5956 -0.0306 -0.0075 0.0267  558 TRP B C   
5437  O O   . TRP B 257 ? 0.5535 1.4225 0.6775 -0.0626 -0.0106 0.0282  558 TRP B O   
5438  C CB  . TRP B 257 ? 0.5256 1.5228 0.6697 -0.0412 0.0007  0.0287  558 TRP B CB  
5439  C CG  . TRP B 257 ? 0.5165 1.4809 0.6515 -0.0282 0.0079  0.0306  558 TRP B CG  
5440  C CD1 . TRP B 257 ? 0.5746 1.5727 0.7109 -0.0027 0.0135  0.0292  558 TRP B CD1 
5441  C CD2 . TRP B 257 ? 0.4650 1.3585 0.5876 -0.0395 0.0099  0.0338  558 TRP B CD2 
5442  N NE1 . TRP B 257 ? 0.5711 1.5223 0.6962 0.0013  0.0188  0.0310  558 TRP B NE1 
5443  C CE2 . TRP B 257 ? 0.5107 1.3990 0.6278 -0.0212 0.0166  0.0340  558 TRP B CE2 
5444  C CE3 . TRP B 257 ? 0.4590 1.2940 0.5738 -0.0626 0.0066  0.0362  558 TRP B CE3 
5445  C CZ2 . TRP B 257 ? 0.5515 1.3806 0.6568 -0.0260 0.0197  0.0366  558 TRP B CZ2 
5446  C CZ3 . TRP B 257 ? 0.4788 1.2554 0.5819 -0.0656 0.0099  0.0391  558 TRP B CZ3 
5447  C CH2 . TRP B 257 ? 0.5294 1.3045 0.6283 -0.0481 0.0162  0.0394  558 TRP B CH2 
5448  N N   . PHE B 258 ? 0.4042 1.2301 0.5139 -0.0071 -0.0056 0.0263  559 PHE B N   
5449  C CA  . PHE B 258 ? 0.4652 1.2173 0.5632 -0.0189 -0.0070 0.0279  559 PHE B CA  
5450  C C   . PHE B 258 ? 0.4611 1.1987 0.5577 -0.0273 -0.0144 0.0261  559 PHE B C   
5451  O O   . PHE B 258 ? 0.4564 1.1597 0.5494 -0.0530 -0.0166 0.0276  559 PHE B O   
5452  C CB  . PHE B 258 ? 0.4623 1.1626 0.5467 0.0080  -0.0039 0.0271  559 PHE B CB  
5453  C CG  . PHE B 258 ? 0.5129 1.1490 0.5877 -0.0071 -0.0026 0.0298  559 PHE B CG  
5454  C CD1 . PHE B 258 ? 0.4365 1.0280 0.5052 -0.0177 -0.0072 0.0300  559 PHE B CD1 
5455  C CD2 . PHE B 258 ? 0.5466 1.1699 0.6183 -0.0106 0.0032  0.0321  559 PHE B CD2 
5456  C CE1 . PHE B 258 ? 0.4649 1.0011 0.5251 -0.0304 -0.0060 0.0324  559 PHE B CE1 
5457  C CE2 . PHE B 258 ? 0.6050 1.1729 0.6680 -0.0234 0.0040  0.0348  559 PHE B CE2 
5458  C CZ  . PHE B 258 ? 0.5421 1.0669 0.5996 -0.0329 -0.0005 0.0349  559 PHE B CZ  
5459  N N   . LYS B 259 ? 0.4735 1.2360 0.5714 -0.0048 -0.0183 0.0229  560 LYS B N   
5460  C CA  . LYS B 259 ? 0.5691 1.3190 0.6647 -0.0114 -0.0254 0.0210  560 LYS B CA  
5461  C C   . LYS B 259 ? 0.5932 1.3673 0.6972 -0.0490 -0.0289 0.0210  560 LYS B C   
5462  O O   . LYS B 259 ? 0.3531 1.0914 0.4510 -0.0657 -0.0332 0.0202  560 LYS B O   
5463  C CB  . LYS B 259 ? 0.6066 1.3926 0.7035 0.0179  -0.0291 0.0180  560 LYS B CB  
5464  C CG  . LYS B 259 ? 0.6280 1.4976 0.7398 0.0219  -0.0291 0.0167  560 LYS B CG  
5465  C CD  . LYS B 259 ? 0.6063 1.5096 0.7177 0.0530  -0.0335 0.0141  560 LYS B CD  
5466  C CE  . LYS B 259 ? 0.6087 1.6016 0.7363 0.0557  -0.0342 0.0125  560 LYS B CE  
5467  N NZ  . LYS B 259 ? 0.5229 1.5341 0.6498 0.0720  -0.0260 0.0132  560 LYS B NZ  
5468  N N   . ASP B 260 ? 0.4891 1.3205 0.6056 -0.0638 -0.0265 0.0219  561 ASP B N   
5469  C CA  . ASP B 260 ? 0.4810 1.3399 0.6047 -0.1015 -0.0294 0.0218  561 ASP B CA  
5470  C C   . ASP B 260 ? 0.4431 1.2457 0.5574 -0.1315 -0.0277 0.0252  561 ASP B C   
5471  O O   . ASP B 260 ? 0.5313 1.3414 0.6466 -0.1643 -0.0306 0.0250  561 ASP B O   
5472  C CB  . ASP B 260 ? 0.6516 1.5898 0.7910 -0.1087 -0.0265 0.0223  561 ASP B CB  
5473  C CG  . ASP B 260 ? 0.7655 1.7584 0.9118 -0.0749 -0.0276 0.0191  561 ASP B CG  
5474  O OD1 . ASP B 260 ? 0.7615 1.7453 0.9043 -0.0552 -0.0332 0.0161  561 ASP B OD1 
5475  O OD2 . ASP B 260 ? 0.8239 1.8537 0.9706 -0.0662 -0.0217 0.0196  561 ASP B OD2 
5476  N N   . LEU B 261 ? 0.4356 1.1820 0.5395 -0.1212 -0.0232 0.0282  562 LEU B N   
5477  C CA  . LEU B 261 ? 0.5334 1.2216 0.6262 -0.1454 -0.0223 0.0314  562 LEU B CA  
5478  C C   . LEU B 261 ? 0.5550 1.1994 0.6384 -0.1521 -0.0286 0.0286  562 LEU B C   
5479  O O   . LEU B 261 ? 0.5851 1.1854 0.6584 -0.1745 -0.0291 0.0304  562 LEU B O   
5480  C CB  . LEU B 261 ? 0.3616 1.0047 0.4463 -0.1305 -0.0165 0.0349  562 LEU B CB  
5481  C CG  . LEU B 261 ? 0.4937 1.1686 0.5841 -0.1244 -0.0095 0.0379  562 LEU B CG  
5482  C CD1 . LEU B 261 ? 0.4516 1.0801 0.5326 -0.1037 -0.0050 0.0394  562 LEU B CD1 
5483  C CD2 . LEU B 261 ? 0.5238 1.2162 0.6165 -0.1583 -0.0067 0.0426  562 LEU B CD2 
5484  N N   . GLY B 262 ? 0.5095 1.1646 0.5943 -0.1320 -0.0333 0.0243  563 GLY B N   
5485  C CA  . GLY B 262 ? 0.6107 1.2313 0.6868 -0.1369 -0.0394 0.0210  563 GLY B CA  
5486  C C   . GLY B 262 ? 0.6358 1.1824 0.6975 -0.1324 -0.0379 0.0227  563 GLY B C   
5487  O O   . GLY B 262 ? 0.7045 1.2143 0.7569 -0.1504 -0.0410 0.0216  563 GLY B O   
5488  N N   . LEU B 263 ? 0.5838 1.1087 0.6429 -0.1089 -0.0331 0.0249  564 LEU B N   
5489  C CA  . LEU B 263 ? 0.5500 1.0105 0.5971 -0.1033 -0.0312 0.0266  564 LEU B CA  
5490  C C   . LEU B 263 ? 0.4789 0.9180 0.5202 -0.0781 -0.0334 0.0241  564 LEU B C   
5491  O O   . LEU B 263 ? 0.4489 0.9164 0.4942 -0.0555 -0.0334 0.0228  564 LEU B O   
5492  C CB  . LEU B 263 ? 0.5576 1.0056 0.6041 -0.0963 -0.0245 0.0305  564 LEU B CB  
5493  C CG  . LEU B 263 ? 0.6240 1.0826 0.6727 -0.1213 -0.0215 0.0344  564 LEU B CG  
5494  C CD1 . LEU B 263 ? 0.6167 1.0675 0.6647 -0.1100 -0.0151 0.0378  564 LEU B CD1 
5495  C CD2 . LEU B 263 ? 0.6613 1.0769 0.6996 -0.1458 -0.0237 0.0359  564 LEU B CD2 
5496  N N   . LYS B 264 ? 0.4961 0.8843 0.5267 -0.0813 -0.0349 0.0237  565 LYS B N   
5497  C CA  . LYS B 264 ? 0.4990 0.8580 0.5221 -0.0590 -0.0355 0.0225  565 LYS B CA  
5498  C C   . LYS B 264 ? 0.5562 0.8581 0.5693 -0.0621 -0.0331 0.0243  565 LYS B C   
5499  O O   . LYS B 264 ? 0.6802 0.9642 0.6908 -0.0818 -0.0326 0.0258  565 LYS B O   
5500  C CB  . LYS B 264 ? 0.4004 0.7696 0.4215 -0.0579 -0.0417 0.0188  565 LYS B CB  
5501  C CG  . LYS B 264 ? 0.5675 0.9202 0.5837 -0.0832 -0.0459 0.0165  565 LYS B CG  
5502  C CD  . LYS B 264 ? 0.6669 1.0303 0.6799 -0.0801 -0.0522 0.0122  565 LYS B CD  
5503  C CE  . LYS B 264 ? 0.7526 1.1166 0.7627 -0.1085 -0.0572 0.0085  565 LYS B CE  
5504  N NZ  . LYS B 264 ? 0.8310 1.2240 0.8414 -0.1079 -0.0639 0.0036  565 LYS B NZ  
5505  N N   . TRP B 265 ? 0.4081 0.6820 0.4147 -0.0421 -0.0315 0.0243  566 TRP B N   
5506  C CA  . TRP B 265 ? 0.3682 0.5920 0.3656 -0.0436 -0.0301 0.0252  566 TRP B CA  
5507  C C   . TRP B 265 ? 0.5026 0.7085 0.4926 -0.0288 -0.0319 0.0236  566 TRP B C   
5508  O O   . TRP B 265 ? 0.5536 0.7831 0.5448 -0.0153 -0.0337 0.0224  566 TRP B O   
5509  C CB  . TRP B 265 ? 0.3563 0.5610 0.3527 -0.0369 -0.0245 0.0280  566 TRP B CB  
5510  C CG  . TRP B 265 ? 0.4020 0.5649 0.3915 -0.0464 -0.0235 0.0294  566 TRP B CG  
5511  C CD1 . TRP B 265 ? 0.4484 0.5766 0.4311 -0.0366 -0.0215 0.0297  566 TRP B CD1 
5512  C CD2 . TRP B 265 ? 0.4373 0.5896 0.4249 -0.0670 -0.0244 0.0309  566 TRP B CD2 
5513  N NE1 . TRP B 265 ? 0.4766 0.5768 0.4546 -0.0482 -0.0213 0.0310  566 TRP B NE1 
5514  C CE2 . TRP B 265 ? 0.4450 0.5567 0.4247 -0.0662 -0.0230 0.0320  566 TRP B CE2 
5515  C CE3 . TRP B 265 ? 0.4112 0.5840 0.4018 -0.0864 -0.0260 0.0317  566 TRP B CE3 
5516  C CZ2 . TRP B 265 ? 0.3809 0.4703 0.3546 -0.0814 -0.0235 0.0338  566 TRP B CZ2 
5517  C CZ3 . TRP B 265 ? 0.4787 0.6257 0.4621 -0.1036 -0.0263 0.0337  566 TRP B CZ3 
5518  C CH2 . TRP B 265 ? 0.4772 0.5820 0.4516 -0.0997 -0.0251 0.0348  566 TRP B CH2 
5519  N N   . TYR B 266 ? 0.4405 0.6059 0.4224 -0.0309 -0.0313 0.0237  567 TYR B N   
5520  C CA  . TYR B 266 ? 0.5209 0.6673 0.4949 -0.0182 -0.0322 0.0227  567 TYR B CA  
5521  C C   . TYR B 266 ? 0.5848 0.7109 0.5546 -0.0011 -0.0273 0.0248  567 TYR B C   
5522  O O   . TYR B 266 ? 0.4953 0.6140 0.4672 -0.0014 -0.0235 0.0265  567 TYR B O   
5523  C CB  . TYR B 266 ? 0.4859 0.6021 0.4525 -0.0292 -0.0342 0.0211  567 TYR B CB  
5524  C CG  . TYR B 266 ? 0.5094 0.5991 0.4744 -0.0396 -0.0316 0.0228  567 TYR B CG  
5525  C CD1 . TYR B 266 ? 0.4904 0.5842 0.4571 -0.0580 -0.0330 0.0229  567 TYR B CD1 
5526  C CD2 . TYR B 266 ? 0.6142 0.6754 0.5751 -0.0311 -0.0276 0.0245  567 TYR B CD2 
5527  C CE1 . TYR B 266 ? 0.5868 0.6549 0.5498 -0.0657 -0.0307 0.0251  567 TYR B CE1 
5528  C CE2 . TYR B 266 ? 0.6515 0.6916 0.6108 -0.0388 -0.0256 0.0262  567 TYR B CE2 
5529  C CZ  . TYR B 266 ? 0.6434 0.6861 0.6032 -0.0550 -0.0272 0.0267  567 TYR B CZ  
5530  O OH  . TYR B 266 ? 0.6560 0.6761 0.6123 -0.0607 -0.0252 0.0290  567 TYR B OH  
5531  N N   . GLY B 267 ? 0.5464 0.6628 0.5089 0.0131  -0.0275 0.0248  568 GLY B N   
5532  C CA  . GLY B 267 ? 0.4005 0.4974 0.3566 0.0287  -0.0229 0.0268  568 GLY B CA  
5533  C C   . GLY B 267 ? 0.4232 0.4825 0.3732 0.0260  -0.0197 0.0277  568 GLY B C   
5534  O O   . GLY B 267 ? 0.4029 0.4456 0.3490 0.0335  -0.0154 0.0289  568 GLY B O   
5535  N N   . LEU B 268 ? 0.4513 0.4974 0.3998 0.0154  -0.0217 0.0266  569 LEU B N   
5536  C CA  . LEU B 268 ? 0.4577 0.4725 0.3997 0.0158  -0.0189 0.0273  569 LEU B CA  
5537  C C   . LEU B 268 ? 0.4654 0.4677 0.4107 0.0030  -0.0183 0.0271  569 LEU B C   
5538  O O   . LEU B 268 ? 0.4010 0.4025 0.3462 -0.0073 -0.0215 0.0255  569 LEU B O   
5539  C CB  . LEU B 268 ? 0.5015 0.5085 0.4360 0.0185  -0.0210 0.0264  569 LEU B CB  
5540  C CG  . LEU B 268 ? 0.5431 0.5219 0.4707 0.0198  -0.0175 0.0273  569 LEU B CG  
5541  C CD1 . LEU B 268 ? 0.6151 0.5821 0.5380 0.0301  -0.0126 0.0300  569 LEU B CD1 
5542  C CD2 . LEU B 268 ? 0.6151 0.5886 0.5354 0.0211  -0.0196 0.0261  569 LEU B CD2 
5543  N N   . PRO B 269 ? 0.4518 0.4428 0.3984 0.0036  -0.0144 0.0285  570 PRO B N   
5544  C CA  . PRO B 269 ? 0.4405 0.4186 0.3886 -0.0062 -0.0139 0.0288  570 PRO B CA  
5545  C C   . PRO B 269 ? 0.3800 0.3363 0.3222 -0.0044 -0.0127 0.0285  570 PRO B C   
5546  O O   . PRO B 269 ? 0.3956 0.3422 0.3349 0.0024  -0.0092 0.0293  570 PRO B O   
5547  C CB  . PRO B 269 ? 0.3572 0.3372 0.3091 -0.0049 -0.0106 0.0302  570 PRO B CB  
5548  C CG  . PRO B 269 ? 0.5000 0.4785 0.4482 0.0075  -0.0079 0.0302  570 PRO B CG  
5549  C CD  . PRO B 269 ? 0.5166 0.5049 0.4617 0.0136  -0.0104 0.0296  570 PRO B CD  
5550  N N   . ALA B 270 ? 0.4405 0.3886 0.3796 -0.0107 -0.0152 0.0272  571 ALA B N   
5551  C CA  . ALA B 270 ? 0.4492 0.3804 0.3823 -0.0075 -0.0140 0.0264  571 ALA B CA  
5552  C C   . ALA B 270 ? 0.4903 0.4083 0.4214 -0.0133 -0.0147 0.0260  571 ALA B C   
5553  O O   . ALA B 270 ? 0.5902 0.5036 0.5168 -0.0193 -0.0181 0.0242  571 ALA B O   
5554  C CB  . ALA B 270 ? 0.4093 0.3423 0.3366 -0.0048 -0.0165 0.0243  571 ALA B CB  
5555  N N   . VAL B 271 ? 0.5116 0.4228 0.4445 -0.0113 -0.0116 0.0275  572 VAL B N   
5556  C CA  . VAL B 271 ? 0.4457 0.3456 0.3761 -0.0147 -0.0123 0.0279  572 VAL B CA  
5557  C C   . VAL B 271 ? 0.4967 0.3837 0.4194 -0.0107 -0.0126 0.0258  572 VAL B C   
5558  O O   . VAL B 271 ? 0.5183 0.4055 0.4407 -0.0044 -0.0098 0.0254  572 VAL B O   
5559  C CB  . VAL B 271 ? 0.4019 0.3031 0.3370 -0.0131 -0.0093 0.0301  572 VAL B CB  
5560  C CG1 . VAL B 271 ? 0.4022 0.2918 0.3330 -0.0131 -0.0100 0.0308  572 VAL B CG1 
5561  C CG2 . VAL B 271 ? 0.4185 0.3315 0.3594 -0.0172 -0.0092 0.0319  572 VAL B CG2 
5562  N N   . SER B 272 ? 0.5246 0.3994 0.4398 -0.0144 -0.0157 0.0243  573 SER B N   
5563  C CA  . SER B 272 ? 0.5263 0.3886 0.4321 -0.0099 -0.0165 0.0211  573 SER B CA  
5564  C C   . SER B 272 ? 0.5540 0.3980 0.4510 -0.0079 -0.0173 0.0208  573 SER B C   
5565  O O   . SER B 272 ? 0.5960 0.4272 0.4827 -0.0037 -0.0183 0.0174  573 SER B O   
5566  C CB  . SER B 272 ? 0.4570 0.3193 0.3572 -0.0145 -0.0202 0.0177  573 SER B CB  
5567  O OG  . SER B 272 ? 0.4611 0.3175 0.3571 -0.0250 -0.0240 0.0171  573 SER B OG  
5568  N N   . ASN B 273 ? 0.6651 0.5068 0.5641 -0.0094 -0.0168 0.0241  574 ASN B N   
5569  C CA  . ASN B 273 ? 0.6388 0.4617 0.5274 -0.0053 -0.0176 0.0244  574 ASN B CA  
5570  C C   . ASN B 273 ? 0.4909 0.3204 0.3842 0.0042  -0.0145 0.0265  574 ASN B C   
5571  O O   . ASN B 273 ? 0.5378 0.3549 0.4232 0.0097  -0.0152 0.0277  574 ASN B O   
5572  C CB  . ASN B 273 ? 0.6845 0.4956 0.5673 -0.0147 -0.0202 0.0271  574 ASN B CB  
5573  C CG  . ASN B 273 ? 0.6400 0.4680 0.5344 -0.0201 -0.0189 0.0313  574 ASN B CG  
5574  O OD1 . ASN B 273 ? 0.6654 0.5114 0.5713 -0.0162 -0.0161 0.0319  574 ASN B OD1 
5575  N ND2 . ASN B 273 ? 0.5970 0.4183 0.4871 -0.0297 -0.0206 0.0341  574 ASN B ND2 
5576  N N   . MET B 274 ? 0.5178 0.3663 0.4226 0.0064  -0.0113 0.0269  575 MET B N   
5577  C CA  . MET B 274 ? 0.5385 0.3970 0.4488 0.0126  -0.0086 0.0286  575 MET B CA  
5578  C C   . MET B 274 ? 0.6061 0.4684 0.5145 0.0218  -0.0062 0.0261  575 MET B C   
5579  O O   . MET B 274 ? 0.5806 0.4396 0.4850 0.0228  -0.0060 0.0234  575 MET B O   
5580  C CB  . MET B 274 ? 0.4679 0.3436 0.3902 0.0077  -0.0063 0.0303  575 MET B CB  
5581  C CG  . MET B 274 ? 0.5144 0.3900 0.4386 0.0016  -0.0080 0.0333  575 MET B CG  
5582  S SD  . MET B 274 ? 0.6216 0.5155 0.5573 -0.0023 -0.0053 0.0344  575 MET B SD  
5583  C CE  . MET B 274 ? 0.4754 0.3769 0.4131 0.0030  -0.0043 0.0356  575 MET B CE  
5584  N N   . LEU B 275 ? 0.4898 0.3612 0.4009 0.0286  -0.0045 0.0271  576 LEU B N   
5585  C CA  . LEU B 275 ? 0.4544 0.3351 0.3650 0.0377  -0.0018 0.0251  576 LEU B CA  
5586  C C   . LEU B 275 ? 0.4857 0.3893 0.4085 0.0340  0.0023  0.0259  576 LEU B C   
5587  O O   . LEU B 275 ? 0.5762 0.4888 0.5062 0.0293  0.0024  0.0278  576 LEU B O   
5588  C CB  . LEU B 275 ? 0.5505 0.4273 0.4541 0.0493  -0.0030 0.0255  576 LEU B CB  
5589  C CG  . LEU B 275 ? 0.6055 0.4949 0.5078 0.0616  -0.0003 0.0233  576 LEU B CG  
5590  C CD1 . LEU B 275 ? 0.6087 0.4828 0.4972 0.0754  -0.0028 0.0229  576 LEU B CD1 
5591  C CD2 . LEU B 275 ? 0.5198 0.4396 0.4357 0.0608  0.0030  0.0245  576 LEU B CD2 
5592  N N   . LEU B 276 ? 0.4634 0.3752 0.3870 0.0352  0.0056  0.0242  577 LEU B N   
5593  C CA  . LEU B 276 ? 0.4340 0.3646 0.3665 0.0300  0.0100  0.0249  577 LEU B CA  
5594  C C   . LEU B 276 ? 0.4705 0.4195 0.4047 0.0375  0.0128  0.0239  577 LEU B C   
5595  O O   . LEU B 276 ? 0.5907 0.5383 0.5185 0.0454  0.0137  0.0221  577 LEU B O   
5596  C CB  . LEU B 276 ? 0.4777 0.4043 0.4087 0.0242  0.0123  0.0249  577 LEU B CB  
5597  C CG  . LEU B 276 ? 0.4882 0.4292 0.4232 0.0194  0.0177  0.0256  577 LEU B CG  
5598  C CD1 . LEU B 276 ? 0.4888 0.4375 0.4311 0.0107  0.0190  0.0268  577 LEU B CD1 
5599  C CD2 . LEU B 276 ? 0.3926 0.3250 0.3216 0.0170  0.0197  0.0262  577 LEU B CD2 
5600  N N   . GLU B 277 ? 0.5111 0.4794 0.4538 0.0351  0.0141  0.0247  578 GLU B N   
5601  C CA  . GLU B 277 ? 0.5099 0.5023 0.4562 0.0422  0.0164  0.0238  578 GLU B CA  
5602  C C   . GLU B 277 ? 0.5574 0.5710 0.5117 0.0314  0.0215  0.0239  578 GLU B C   
5603  O O   . GLU B 277 ? 0.4038 0.4201 0.3636 0.0202  0.0219  0.0246  578 GLU B O   
5604  C CB  . GLU B 277 ? 0.6139 0.6143 0.5625 0.0486  0.0132  0.0247  578 GLU B CB  
5605  C CG  . GLU B 277 ? 0.6881 0.7168 0.6403 0.0588  0.0147  0.0237  578 GLU B CG  
5606  C CD  . GLU B 277 ? 0.8212 0.8802 0.7858 0.0486  0.0172  0.0237  578 GLU B CD  
5607  O OE1 . GLU B 277 ? 0.8795 0.9329 0.8479 0.0360  0.0166  0.0244  578 GLU B OE1 
5608  O OE2 . GLU B 277 ? 0.8088 0.8980 0.7788 0.0529  0.0198  0.0225  578 GLU B OE2 
5609  N N   . ILE B 278 ? 0.5034 0.5306 0.4570 0.0342  0.0257  0.0230  579 ILE B N   
5610  C CA  . ILE B 278 ? 0.4750 0.5229 0.4345 0.0227  0.0312  0.0234  579 ILE B CA  
5611  C C   . ILE B 278 ? 0.5314 0.6110 0.4948 0.0306  0.0342  0.0221  579 ILE B C   
5612  O O   . ILE B 278 ? 0.5219 0.6004 0.4791 0.0430  0.0348  0.0210  579 ILE B O   
5613  C CB  . ILE B 278 ? 0.4947 0.5266 0.4477 0.0151  0.0346  0.0247  579 ILE B CB  
5614  C CG1 . ILE B 278 ? 0.4835 0.4871 0.4325 0.0102  0.0313  0.0258  579 ILE B CG1 
5615  C CG2 . ILE B 278 ? 0.4131 0.4626 0.3697 0.0017  0.0406  0.0258  579 ILE B CG2 
5616  C CD1 . ILE B 278 ? 0.4825 0.4685 0.4231 0.0075  0.0332  0.0272  579 ILE B CD1 
5617  N N   . GLY B 279 ? 0.5156 0.6246 0.4888 0.0238  0.0360  0.0218  580 GLY B N   
5618  C CA  . GLY B 279 ? 0.4658 0.6127 0.4450 0.0306  0.0388  0.0205  580 GLY B CA  
5619  C C   . GLY B 279 ? 0.4990 0.6484 0.4732 0.0533  0.0363  0.0191  580 GLY B C   
5620  O O   . GLY B 279 ? 0.5249 0.6923 0.4976 0.0617  0.0400  0.0179  580 GLY B O   
5621  N N   . GLY B 280 ? 0.4856 0.6157 0.4553 0.0636  0.0304  0.0192  581 GLY B N   
5622  C CA  . GLY B 280 ? 0.6012 0.7250 0.5619 0.0856  0.0276  0.0180  581 GLY B CA  
5623  C C   . GLY B 280 ? 0.6052 0.6933 0.5517 0.0921  0.0266  0.0170  581 GLY B C   
5624  O O   . GLY B 280 ? 0.5606 0.6320 0.4959 0.1088  0.0232  0.0158  581 GLY B O   
5625  N N   . LEU B 281 ? 0.5080 0.5829 0.4532 0.0797  0.0291  0.0173  582 LEU B N   
5626  C CA  . LEU B 281 ? 0.5604 0.6035 0.4925 0.0841  0.0276  0.0160  582 LEU B CA  
5627  C C   . LEU B 281 ? 0.6123 0.6225 0.5398 0.0793  0.0221  0.0171  582 LEU B C   
5628  O O   . LEU B 281 ? 0.6044 0.6144 0.5395 0.0675  0.0211  0.0194  582 LEU B O   
5629  C CB  . LEU B 281 ? 0.4698 0.5144 0.4016 0.0738  0.0324  0.0164  582 LEU B CB  
5630  C CG  . LEU B 281 ? 0.4652 0.5445 0.4018 0.0746  0.0390  0.0161  582 LEU B CG  
5631  C CD1 . LEU B 281 ? 0.4808 0.5550 0.4134 0.0647  0.0436  0.0174  582 LEU B CD1 
5632  C CD2 . LEU B 281 ? 0.4315 0.5226 0.3622 0.0955  0.0390  0.0128  582 LEU B CD2 
5633  N N   . GLU B 282 ? 0.5681 0.5508 0.4823 0.0881  0.0187  0.0152  583 GLU B N   
5634  C CA  . GLU B 282 ? 0.5925 0.5451 0.5008 0.0840  0.0134  0.0161  583 GLU B CA  
5635  C C   . GLU B 282 ? 0.7005 0.6307 0.6004 0.0789  0.0124  0.0144  583 GLU B C   
5636  O O   . GLU B 282 ? 0.7310 0.6483 0.6185 0.0881  0.0116  0.0110  583 GLU B O   
5637  C CB  . GLU B 282 ? 0.6071 0.5444 0.5046 0.0979  0.0094  0.0155  583 GLU B CB  
5638  C CG  . GLU B 282 ? 0.7645 0.7247 0.6687 0.1057  0.0096  0.0173  583 GLU B CG  
5639  C CD  . GLU B 282 ? 0.8627 0.8010 0.7536 0.1185  0.0051  0.0181  583 GLU B CD  
5640  O OE1 . GLU B 282 ? 0.9239 0.8636 0.8186 0.1160  0.0028  0.0216  583 GLU B OE1 
5641  O OE2 . GLU B 282 ? 0.8421 0.7594 0.7169 0.1308  0.0040  0.0152  583 GLU B OE2 
5642  N N   . PHE B 283 ? 0.6367 0.5627 0.5424 0.0651  0.0122  0.0165  584 PHE B N   
5643  C CA  . PHE B 283 ? 0.5139 0.4223 0.4129 0.0598  0.0106  0.0153  584 PHE B CA  
5644  C C   . PHE B 283 ? 0.6156 0.5014 0.5097 0.0561  0.0050  0.0154  584 PHE B C   
5645  O O   . PHE B 283 ? 0.6240 0.5098 0.5252 0.0467  0.0038  0.0181  584 PHE B O   
5646  C CB  . PHE B 283 ? 0.5166 0.4348 0.4231 0.0491  0.0139  0.0176  584 PHE B CB  
5647  C CG  . PHE B 283 ? 0.6149 0.5541 0.5246 0.0502  0.0199  0.0181  584 PHE B CG  
5648  C CD1 . PHE B 283 ? 0.5117 0.4506 0.4134 0.0545  0.0222  0.0164  584 PHE B CD1 
5649  C CD2 . PHE B 283 ? 0.5755 0.5357 0.4956 0.0456  0.0234  0.0202  584 PHE B CD2 
5650  C CE1 . PHE B 283 ? 0.4446 0.4042 0.3487 0.0542  0.0284  0.0175  584 PHE B CE1 
5651  C CE2 . PHE B 283 ? 0.5369 0.5180 0.4600 0.0440  0.0293  0.0208  584 PHE B CE2 
5652  C CZ  . PHE B 283 ? 0.5410 0.5221 0.4560 0.0483  0.0321  0.0198  584 PHE B CZ  
5653  N N   . SER B 284 ? 0.5430 0.4092 0.4235 0.0635  0.0018  0.0124  585 SER B N   
5654  C CA  . SER B 284 ? 0.4881 0.3308 0.3610 0.0593  -0.0032 0.0124  585 SER B CA  
5655  C C   . SER B 284 ? 0.5357 0.3709 0.4087 0.0472  -0.0056 0.0120  585 SER B C   
5656  O O   . SER B 284 ? 0.5872 0.4083 0.4569 0.0402  -0.0094 0.0128  585 SER B O   
5657  C CB  . SER B 284 ? 0.5908 0.4108 0.4457 0.0702  -0.0056 0.0088  585 SER B CB  
5658  O OG  . SER B 284 ? 0.7404 0.5592 0.5872 0.0762  -0.0043 0.0041  585 SER B OG  
5659  N N   . ALA B 285 ? 0.6271 0.4724 0.5033 0.0448  -0.0036 0.0111  586 ALA B N   
5660  C CA  . ALA B 285 ? 0.5702 0.4125 0.4468 0.0353  -0.0061 0.0108  586 ALA B CA  
5661  C C   . ALA B 285 ? 0.5223 0.3826 0.4093 0.0322  -0.0023 0.0137  586 ALA B C   
5662  O O   . ALA B 285 ? 0.5350 0.4027 0.4202 0.0364  0.0011  0.0132  586 ALA B O   
5663  C CB  . ALA B 285 ? 0.7033 0.5325 0.5663 0.0371  -0.0088 0.0057  586 ALA B CB  
5664  N N   . CYS B 286 ? 0.5289 0.3947 0.4249 0.0249  -0.0026 0.0169  587 CYS B N   
5665  C CA  . CYS B 286 ? 0.4761 0.3542 0.3799 0.0221  0.0010  0.0199  587 CYS B CA  
5666  C C   . CYS B 286 ? 0.5552 0.4343 0.4638 0.0153  -0.0012 0.0216  587 CYS B C   
5667  O O   . CYS B 286 ? 0.5985 0.4834 0.5145 0.0123  0.0004  0.0241  587 CYS B O   
5668  C CB  . CYS B 286 ? 0.5571 0.4453 0.4682 0.0230  0.0049  0.0219  587 CYS B CB  
5669  S SG  . CYS B 286 ? 0.4984 0.3846 0.4145 0.0209  0.0020  0.0232  587 CYS B SG  
5670  N N   . PRO B 287 ? 0.6234 0.4990 0.5277 0.0130  -0.0050 0.0201  588 PRO B N   
5671  C CA  . PRO B 287 ? 0.5393 0.4204 0.4488 0.0075  -0.0071 0.0216  588 PRO B CA  
5672  C C   . PRO B 287 ? 0.5570 0.4458 0.4711 0.0089  -0.0035 0.0245  588 PRO B C   
5673  O O   . PRO B 287 ? 0.4833 0.3721 0.3933 0.0127  -0.0007 0.0252  588 PRO B O   
5674  C CB  . PRO B 287 ? 0.5677 0.4480 0.4711 0.0057  -0.0114 0.0188  588 PRO B CB  
5675  C CG  . PRO B 287 ? 0.5576 0.4319 0.4521 0.0113  -0.0106 0.0163  588 PRO B CG  
5676  C CD  . PRO B 287 ? 0.6263 0.4954 0.5206 0.0154  -0.0074 0.0164  588 PRO B CD  
5677  N N   . PHE B 288 ? 0.4453 0.3387 0.3660 0.0057  -0.0032 0.0262  589 PHE B N   
5678  C CA  . PHE B 288 ? 0.3976 0.2943 0.3204 0.0070  0.0001  0.0284  589 PHE B CA  
5679  C C   . PHE B 288 ? 0.4207 0.3248 0.3470 0.0057  -0.0022 0.0289  589 PHE B C   
5680  O O   . PHE B 288 ? 0.4558 0.3643 0.3858 0.0013  -0.0052 0.0283  589 PHE B O   
5681  C CB  . PHE B 288 ? 0.4290 0.3251 0.3557 0.0053  0.0038  0.0293  589 PHE B CB  
5682  C CG  . PHE B 288 ? 0.5080 0.4069 0.4405 0.0018  0.0020  0.0291  589 PHE B CG  
5683  C CD1 . PHE B 288 ? 0.5477 0.4513 0.4844 -0.0008 0.0015  0.0299  589 PHE B CD1 
5684  C CD2 . PHE B 288 ? 0.4729 0.3695 0.4051 0.0024  0.0012  0.0285  589 PHE B CD2 
5685  C CE1 . PHE B 288 ? 0.4305 0.3367 0.3713 -0.0040 0.0002  0.0304  589 PHE B CE1 
5686  C CE2 . PHE B 288 ? 0.5527 0.4501 0.4878 0.0003  -0.0005 0.0292  589 PHE B CE2 
5687  C CZ  . PHE B 288 ? 0.4567 0.3591 0.3963 -0.0035 -0.0009 0.0304  589 PHE B CZ  
5688  N N   . SER B 289 ? 0.4285 0.3337 0.3526 0.0099  -0.0003 0.0302  590 SER B N   
5689  C CA  . SER B 289 ? 0.4064 0.3217 0.3327 0.0115  -0.0024 0.0304  590 SER B CA  
5690  C C   . SER B 289 ? 0.4143 0.3255 0.3376 0.0166  0.0012  0.0318  590 SER B C   
5691  O O   . SER B 289 ? 0.3839 0.2830 0.3007 0.0187  0.0049  0.0329  590 SER B O   
5692  C CB  . SER B 289 ? 0.4929 0.4159 0.4158 0.0146  -0.0060 0.0297  590 SER B CB  
5693  O OG  . SER B 289 ? 0.5236 0.4400 0.4380 0.0218  -0.0040 0.0311  590 SER B OG  
5694  N N   . GLY B 290 ? 0.5244 0.4451 0.4513 0.0179  0.0004  0.0315  591 GLY B N   
5695  C CA  . GLY B 290 ? 0.4665 0.3817 0.3879 0.0245  0.0034  0.0321  591 GLY B CA  
5696  C C   . GLY B 290 ? 0.6052 0.5367 0.5282 0.0311  0.0011  0.0319  591 GLY B C   
5697  O O   . GLY B 290 ? 0.6369 0.5781 0.5586 0.0352  -0.0018 0.0322  591 GLY B O   
5698  N N   . TRP B 291 ? 0.5331 0.4704 0.4587 0.0322  0.0021  0.0310  592 TRP B N   
5699  C CA  . TRP B 291 ? 0.5159 0.4748 0.4451 0.0378  0.0001  0.0305  592 TRP B CA  
5700  C C   . TRP B 291 ? 0.5292 0.4993 0.4664 0.0315  0.0004  0.0295  592 TRP B C   
5701  O O   . TRP B 291 ? 0.4755 0.4341 0.4133 0.0258  0.0024  0.0291  592 TRP B O   
5702  C CB  . TRP B 291 ? 0.5219 0.4758 0.4403 0.0527  0.0019  0.0309  592 TRP B CB  
5703  C CG  . TRP B 291 ? 0.5969 0.5275 0.5063 0.0551  0.0063  0.0302  592 TRP B CG  
5704  C CD1 . TRP B 291 ? 0.5380 0.4693 0.4481 0.0552  0.0082  0.0281  592 TRP B CD1 
5705  C CD2 . TRP B 291 ? 0.6126 0.5152 0.5095 0.0563  0.0095  0.0314  592 TRP B CD2 
5706  N NE1 . TRP B 291 ? 0.5691 0.4736 0.4676 0.0560  0.0120  0.0272  592 TRP B NE1 
5707  C CE2 . TRP B 291 ? 0.6439 0.5304 0.5342 0.0559  0.0131  0.0294  592 TRP B CE2 
5708  C CE3 . TRP B 291 ? 0.7119 0.6019 0.6017 0.0568  0.0099  0.0338  592 TRP B CE3 
5709  C CZ2 . TRP B 291 ? 0.7559 0.6135 0.6327 0.0545  0.0170  0.0298  592 TRP B CZ2 
5710  C CZ3 . TRP B 291 ? 0.7447 0.6070 0.6215 0.0560  0.0143  0.0350  592 TRP B CZ3 
5711  C CH2 . TRP B 291 ? 0.8216 0.6677 0.6920 0.0541  0.0177  0.0330  592 TRP B CH2 
5712  N N   . TYR B 292 ? 0.3679 0.3631 0.3116 0.0319  -0.0018 0.0293  593 TYR B N   
5713  C CA  . TYR B 292 ? 0.4970 0.5064 0.4485 0.0244  -0.0017 0.0292  593 TYR B CA  
5714  C C   . TYR B 292 ? 0.5380 0.5456 0.4859 0.0318  0.0018  0.0277  593 TYR B C   
5715  O O   . TYR B 292 ? 0.5372 0.5431 0.4778 0.0449  0.0033  0.0266  593 TYR B O   
5716  C CB  . TYR B 292 ? 0.4171 0.4569 0.3762 0.0212  -0.0047 0.0295  593 TYR B CB  
5717  C CG  . TYR B 292 ? 0.4943 0.5367 0.4580 0.0071  -0.0081 0.0304  593 TYR B CG  
5718  C CD1 . TYR B 292 ? 0.5473 0.5781 0.5126 -0.0041 -0.0077 0.0316  593 TYR B CD1 
5719  C CD2 . TYR B 292 ? 0.4708 0.5268 0.4359 0.0053  -0.0119 0.0299  593 TYR B CD2 
5720  C CE1 . TYR B 292 ? 0.4460 0.4744 0.4123 -0.0163 -0.0107 0.0324  593 TYR B CE1 
5721  C CE2 . TYR B 292 ? 0.4720 0.5271 0.4389 -0.0086 -0.0150 0.0299  593 TYR B CE2 
5722  C CZ  . TYR B 292 ? 0.5022 0.5416 0.4689 -0.0191 -0.0143 0.0312  593 TYR B CZ  
5723  O OH  . TYR B 292 ? 0.5759 0.6094 0.5411 -0.0321 -0.0173 0.0312  593 TYR B OH  
5724  N N   . MET B 293 ? 0.5606 0.5674 0.5120 0.0239  0.0029  0.0277  594 MET B N   
5725  C CA  . MET B 293 ? 0.4191 0.4360 0.3701 0.0284  0.0053  0.0261  594 MET B CA  
5726  C C   . MET B 293 ? 0.3733 0.4224 0.3332 0.0250  0.0037  0.0274  594 MET B C   
5727  O O   . MET B 293 ? 0.3969 0.4534 0.3632 0.0127  0.0013  0.0297  594 MET B O   
5728  C CB  . MET B 293 ? 0.4025 0.4069 0.3530 0.0211  0.0070  0.0256  594 MET B CB  
5729  C CG  . MET B 293 ? 0.4571 0.4671 0.4040 0.0268  0.0097  0.0229  594 MET B CG  
5730  S SD  . MET B 293 ? 0.5078 0.4979 0.4506 0.0203  0.0114  0.0210  594 MET B SD  
5731  C CE  . MET B 293 ? 0.4772 0.4794 0.4299 0.0065  0.0090  0.0253  594 MET B CE  
5732  N N   . GLY B 294 ? 0.4393 0.5074 0.3983 0.0358  0.0051  0.0258  595 GLY B N   
5733  C CA  . GLY B 294 ? 0.4269 0.5312 0.3948 0.0329  0.0038  0.0270  595 GLY B CA  
5734  C C   . GLY B 294 ? 0.4392 0.5540 0.4145 0.0161  0.0035  0.0296  595 GLY B C   
5735  O O   . GLY B 294 ? 0.3838 0.5200 0.3662 0.0059  0.0014  0.0317  595 GLY B O   
5736  N N   . THR B 295 ? 0.4020 0.5011 0.3744 0.0124  0.0056  0.0297  596 THR B N   
5737  C CA  . THR B 295 ? 0.4247 0.5325 0.4015 -0.0016 0.0058  0.0330  596 THR B CA  
5738  C C   . THR B 295 ? 0.4667 0.5635 0.4455 -0.0159 0.0026  0.0363  596 THR B C   
5739  O O   . THR B 295 ? 0.4149 0.5232 0.3967 -0.0285 0.0021  0.0398  596 THR B O   
5740  C CB  . THR B 295 ? 0.4472 0.5400 0.4192 -0.0008 0.0082  0.0322  596 THR B CB  
5741  O OG1 . THR B 295 ? 0.3792 0.4421 0.3457 0.0019  0.0077  0.0305  596 THR B OG1 
5742  C CG2 . THR B 295 ? 0.4347 0.5416 0.4036 0.0110  0.0115  0.0288  596 THR B CG2 
5743  N N   . GLU B 296 ? 0.5153 0.5886 0.4907 -0.0142 0.0009  0.0354  597 GLU B N   
5744  C CA  . GLU B 296 ? 0.5125 0.5735 0.4878 -0.0257 -0.0021 0.0377  597 GLU B CA  
5745  C C   . GLU B 296 ? 0.5702 0.6530 0.5499 -0.0347 -0.0045 0.0389  597 GLU B C   
5746  O O   . GLU B 296 ? 0.5771 0.6578 0.5561 -0.0488 -0.0059 0.0418  597 GLU B O   
5747  C CB  . GLU B 296 ? 0.5349 0.5730 0.5060 -0.0202 -0.0033 0.0358  597 GLU B CB  
5748  C CG  . GLU B 296 ? 0.5674 0.5842 0.5342 -0.0145 -0.0011 0.0347  597 GLU B CG  
5749  C CD  . GLU B 296 ? 0.5726 0.5705 0.5353 -0.0100 -0.0016 0.0332  597 GLU B CD  
5750  O OE1 . GLU B 296 ? 0.5208 0.5066 0.4825 -0.0158 -0.0034 0.0343  597 GLU B OE1 
5751  O OE2 . GLU B 296 ? 0.3937 0.3879 0.3530 -0.0004 0.0000  0.0312  597 GLU B OE2 
5752  N N   . ILE B 297 ? 0.4290 0.5329 0.4120 -0.0269 -0.0051 0.0366  598 ILE B N   
5753  C CA  . ILE B 297 ? 0.3738 0.5058 0.3623 -0.0355 -0.0075 0.0370  598 ILE B CA  
5754  C C   . ILE B 297 ? 0.5000 0.6609 0.4939 -0.0423 -0.0053 0.0392  598 ILE B C   
5755  O O   . ILE B 297 ? 0.5597 0.7298 0.5552 -0.0593 -0.0064 0.0419  598 ILE B O   
5756  C CB  . ILE B 297 ? 0.3782 0.5272 0.3684 -0.0226 -0.0090 0.0341  598 ILE B CB  
5757  C CG1 . ILE B 297 ? 0.4462 0.5673 0.4300 -0.0164 -0.0108 0.0326  598 ILE B CG1 
5758  C CG2 . ILE B 297 ? 0.3467 0.5312 0.3439 -0.0320 -0.0118 0.0341  598 ILE B CG2 
5759  C CD1 . ILE B 297 ? 0.5096 0.6410 0.4917 0.0005  -0.0114 0.0305  598 ILE B CD1 
5760  N N   . GLY B 298 ? 0.4259 0.6012 0.4211 -0.0291 -0.0020 0.0378  599 GLY B N   
5761  C CA  . GLY B 298 ? 0.5449 0.7561 0.5458 -0.0322 0.0004  0.0391  599 GLY B CA  
5762  C C   . GLY B 298 ? 0.4162 0.6224 0.4154 -0.0434 0.0030  0.0428  599 GLY B C   
5763  O O   . GLY B 298 ? 0.4341 0.6670 0.4376 -0.0551 0.0042  0.0457  599 GLY B O   
5764  N N   . VAL B 299 ? 0.3948 0.5686 0.3875 -0.0406 0.0040  0.0432  600 VAL B N   
5765  C CA  . VAL B 299 ? 0.5058 0.6718 0.4952 -0.0509 0.0057  0.0473  600 VAL B CA  
5766  C C   . VAL B 299 ? 0.5689 0.7140 0.5544 -0.0676 0.0030  0.0515  600 VAL B C   
5767  O O   . VAL B 299 ? 0.6046 0.7597 0.5895 -0.0828 0.0033  0.0560  600 VAL B O   
5768  C CB  . VAL B 299 ? 0.5100 0.6545 0.4938 -0.0401 0.0077  0.0454  600 VAL B CB  
5769  C CG1 . VAL B 299 ? 0.5446 0.6838 0.5244 -0.0496 0.0091  0.0500  600 VAL B CG1 
5770  C CG2 . VAL B 299 ? 0.4658 0.6266 0.4500 -0.0237 0.0105  0.0407  600 VAL B CG2 
5771  N N   . ARG B 300 ? 0.5092 0.6240 0.4905 -0.0648 0.0004  0.0501  601 ARG B N   
5772  C CA  . ARG B 300 ? 0.5628 0.6508 0.5371 -0.0767 -0.0019 0.0535  601 ARG B CA  
5773  C C   . ARG B 300 ? 0.5634 0.6552 0.5377 -0.0893 -0.0051 0.0536  601 ARG B C   
5774  O O   . ARG B 300 ? 0.5250 0.6109 0.4938 -0.1052 -0.0058 0.0577  601 ARG B O   
5775  C CB  . ARG B 300 ? 0.4352 0.4920 0.4048 -0.0675 -0.0031 0.0515  601 ARG B CB  
5776  C CG  . ARG B 300 ? 0.5020 0.5526 0.4706 -0.0574 -0.0006 0.0507  601 ARG B CG  
5777  C CD  . ARG B 300 ? 0.5424 0.5940 0.5070 -0.0643 0.0010  0.0557  601 ARG B CD  
5778  N NE  . ARG B 300 ? 0.5930 0.6236 0.5498 -0.0748 -0.0011 0.0604  601 ARG B NE  
5779  C CZ  . ARG B 300 ? 0.5398 0.5443 0.4903 -0.0712 -0.0026 0.0611  601 ARG B CZ  
5780  N NH1 . ARG B 300 ? 0.5713 0.5700 0.5240 -0.0596 -0.0022 0.0573  601 ARG B NH1 
5781  N NH2 . ARG B 300 ? 0.5819 0.5661 0.5229 -0.0793 -0.0043 0.0654  601 ARG B NH2 
5782  N N   . ASP B 301 ? 0.5264 0.6251 0.5047 -0.0828 -0.0073 0.0492  602 ASP B N   
5783  C CA  . ASP B 301 ? 0.6021 0.7034 0.5794 -0.0947 -0.0109 0.0483  602 ASP B CA  
5784  C C   . ASP B 301 ? 0.4804 0.6160 0.4630 -0.1089 -0.0106 0.0501  602 ASP B C   
5785  O O   . ASP B 301 ? 0.5286 0.6593 0.5061 -0.1274 -0.0125 0.0520  602 ASP B O   
5786  C CB  . ASP B 301 ? 0.5957 0.7002 0.5759 -0.0834 -0.0133 0.0433  602 ASP B CB  
5787  C CG  . ASP B 301 ? 0.6443 0.7145 0.6182 -0.0737 -0.0139 0.0418  602 ASP B CG  
5788  O OD1 . ASP B 301 ? 0.6705 0.7129 0.6365 -0.0803 -0.0147 0.0435  602 ASP B OD1 
5789  O OD2 . ASP B 301 ? 0.6420 0.7133 0.6179 -0.0592 -0.0134 0.0389  602 ASP B OD2 
5790  N N   . TYR B 302 ? 0.5651 0.7355 0.5566 -0.1009 -0.0080 0.0494  603 TYR B N   
5791  C CA  . TYR B 302 ? 0.5440 0.7540 0.5420 -0.1136 -0.0074 0.0508  603 TYR B CA  
5792  C C   . TYR B 302 ? 0.5275 0.7404 0.5226 -0.1267 -0.0038 0.0567  603 TYR B C   
5793  O O   . TYR B 302 ? 0.4884 0.7208 0.4843 -0.1460 -0.0038 0.0595  603 TYR B O   
5794  C CB  . TYR B 302 ? 0.6293 0.8789 0.6375 -0.0974 -0.0060 0.0474  603 TYR B CB  
5795  C CG  . TYR B 302 ? 0.6794 0.9411 0.6913 -0.0907 -0.0101 0.0428  603 TYR B CG  
5796  C CD1 . TYR B 302 ? 0.6646 0.9117 0.6726 -0.1039 -0.0146 0.0418  603 TYR B CD1 
5797  C CD2 . TYR B 302 ? 0.6601 0.9472 0.6776 -0.0705 -0.0095 0.0396  603 TYR B CD2 
5798  C CE1 . TYR B 302 ? 0.6854 0.9452 0.6960 -0.0977 -0.0185 0.0377  603 TYR B CE1 
5799  C CE2 . TYR B 302 ? 0.6252 0.9240 0.6447 -0.0632 -0.0134 0.0361  603 TYR B CE2 
5800  C CZ  . TYR B 302 ? 0.6707 0.9574 0.6875 -0.0772 -0.0179 0.0352  603 TYR B CZ  
5801  O OH  . TYR B 302 ? 0.7479 1.0479 0.7662 -0.0696 -0.0220 0.0317  603 TYR B OH  
5802  N N   . CYS B 303 ? 0.5009 0.6959 0.4918 -0.1178 -0.0008 0.0588  604 CYS B N   
5803  C CA  . CYS B 303 ? 0.6191 0.8248 0.6079 -0.1270 0.0031  0.0642  604 CYS B CA  
5804  C C   . CYS B 303 ? 0.6370 0.8042 0.6128 -0.1364 0.0032  0.0699  604 CYS B C   
5805  O O   . CYS B 303 ? 0.6196 0.7943 0.5915 -0.1474 0.0061  0.0756  604 CYS B O   
5806  C CB  . CYS B 303 ? 0.6483 0.8743 0.6421 -0.1096 0.0071  0.0624  604 CYS B CB  
5807  S SG  . CYS B 303 ? 0.6240 0.9042 0.6309 -0.1003 0.0082  0.0579  604 CYS B SG  
5808  N N   . ASP B 304 ? 0.6212 0.7490 0.5894 -0.1318 0.0003  0.0688  605 ASP B N   
5809  C CA  . ASP B 304 ? 0.6762 0.7683 0.6305 -0.1402 0.0000  0.0745  605 ASP B CA  
5810  C C   . ASP B 304 ? 0.7768 0.8681 0.7235 -0.1640 -0.0004 0.0795  605 ASP B C   
5811  O O   . ASP B 304 ? 0.8018 0.9080 0.7525 -0.1746 -0.0024 0.0768  605 ASP B O   
5812  C CB  . ASP B 304 ? 0.7337 0.7877 0.6813 -0.1318 -0.0034 0.0719  605 ASP B CB  
5813  C CG  . ASP B 304 ? 0.7318 0.7744 0.6802 -0.1138 -0.0022 0.0704  605 ASP B CG  
5814  O OD1 . ASP B 304 ? 0.7965 0.8609 0.7515 -0.1058 0.0007  0.0696  605 ASP B OD1 
5815  O OD2 . ASP B 304 ? 0.6847 0.6972 0.6264 -0.1079 -0.0043 0.0697  605 ASP B OD2 
5816  N N   . ASN B 305 ? 0.7422 0.8162 0.6768 -0.1731 0.0016  0.0869  606 ASN B N   
5817  C CA  . ASN B 305 ? 0.7368 0.8047 0.6607 -0.1976 0.0018  0.0926  606 ASN B CA  
5818  C C   . ASN B 305 ? 0.8213 0.8539 0.7339 -0.2061 -0.0028 0.0905  606 ASN B C   
5819  O O   . ASN B 305 ? 0.8551 0.8936 0.7647 -0.2262 -0.0040 0.0905  606 ASN B O   
5820  C CB  . ASN B 305 ? 0.6184 0.6690 0.5283 -0.2036 0.0049  0.1018  606 ASN B CB  
5821  C CG  . ASN B 305 ? 0.6902 0.7826 0.6078 -0.2096 0.0099  0.1055  606 ASN B CG  
5822  O OD1 . ASN B 305 ? 0.8076 0.9222 0.7259 -0.2297 0.0115  0.1083  606 ASN B OD1 
5823  N ND2 . ASN B 305 ? 0.5355 0.6405 0.4586 -0.1927 0.0124  0.1052  606 ASN B ND2 
5824  N N   . SER B 306 ? 0.8339 0.8310 0.7397 -0.1916 -0.0053 0.0883  607 SER B N   
5825  C CA  . SER B 306 ? 0.7807 0.7426 0.6747 -0.1959 -0.0094 0.0854  607 SER B CA  
5826  C C   . SER B 306 ? 0.7309 0.7104 0.6372 -0.1908 -0.0125 0.0766  607 SER B C   
5827  O O   . SER B 306 ? 0.8194 0.7720 0.7172 -0.1909 -0.0161 0.0728  607 SER B O   
5828  C CB  . SER B 306 ? 0.7641 0.6845 0.6457 -0.1807 -0.0105 0.0867  607 SER B CB  
5829  O OG  . SER B 306 ? 0.9278 0.8334 0.7976 -0.1825 -0.0080 0.0951  607 SER B OG  
5830  N N   . ARG B 307 ? 0.6732 0.6965 0.5979 -0.1850 -0.0112 0.0734  608 ARG B N   
5831  C CA  . ARG B 307 ? 0.6838 0.7251 0.6192 -0.1782 -0.0140 0.0659  608 ARG B CA  
5832  C C   . ARG B 307 ? 0.7230 0.8073 0.6683 -0.1927 -0.0143 0.0646  608 ARG B C   
5833  O O   . ARG B 307 ? 0.7902 0.8730 0.7277 -0.2154 -0.0148 0.0673  608 ARG B O   
5834  C CB  . ARG B 307 ? 0.5965 0.6480 0.5432 -0.1538 -0.0127 0.0625  608 ARG B CB  
5835  C CG  . ARG B 307 ? 0.5848 0.5984 0.5232 -0.1403 -0.0130 0.0628  608 ARG B CG  
5836  C CD  . ARG B 307 ? 0.6699 0.6522 0.5985 -0.1411 -0.0169 0.0594  608 ARG B CD  
5837  N NE  . ARG B 307 ? 0.6255 0.6231 0.5624 -0.1348 -0.0192 0.0529  608 ARG B NE  
5838  C CZ  . ARG B 307 ? 0.6241 0.6289 0.5693 -0.1168 -0.0185 0.0496  608 ARG B CZ  
5839  N NH1 . ARG B 307 ? 0.6067 0.6062 0.5539 -0.1043 -0.0156 0.0513  608 ARG B NH1 
5840  N NH2 . ARG B 307 ? 0.4618 0.4790 0.4122 -0.1117 -0.0207 0.0446  608 ARG B NH2 
5841  N N   . TYR B 308 ? 0.7130 0.8360 0.6743 -0.1803 -0.0139 0.0604  609 TYR B N   
5842  C CA  . TYR B 308 ? 0.6109 0.7781 0.5818 -0.1926 -0.0148 0.0585  609 TYR B CA  
5843  C C   . TYR B 308 ? 0.6578 0.8579 0.6337 -0.2037 -0.0104 0.0638  609 TYR B C   
5844  O O   . TYR B 308 ? 0.7270 0.9595 0.7073 -0.2218 -0.0109 0.0638  609 TYR B O   
5845  C CB  . TYR B 308 ? 0.5918 0.7890 0.5761 -0.1741 -0.0163 0.0524  609 TYR B CB  
5846  C CG  . TYR B 308 ? 0.7142 0.8962 0.6944 -0.1751 -0.0217 0.0471  609 TYR B CG  
5847  C CD1 . TYR B 308 ? 0.6426 0.7863 0.6159 -0.1607 -0.0231 0.0449  609 TYR B CD1 
5848  C CD2 . TYR B 308 ? 0.8241 1.0307 0.8066 -0.1917 -0.0254 0.0441  609 TYR B CD2 
5849  C CE1 . TYR B 308 ? 0.6875 0.8173 0.6559 -0.1612 -0.0277 0.0401  609 TYR B CE1 
5850  C CE2 . TYR B 308 ? 0.7924 0.9846 0.7698 -0.1927 -0.0306 0.0387  609 TYR B CE2 
5851  C CZ  . TYR B 308 ? 0.7090 0.8621 0.6790 -0.1768 -0.0315 0.0369  609 TYR B CZ  
5852  O OH  . TYR B 308 ? 0.6058 0.7446 0.5698 -0.1768 -0.0362 0.0316  609 TYR B OH  
5853  N N   . ASN B 309 ? 0.5187 0.7135 0.4937 -0.1940 -0.0060 0.0680  610 ASN B N   
5854  C CA  . ASN B 309 ? 0.5336 0.7491 0.5082 -0.2073 -0.0014 0.0744  610 ASN B CA  
5855  C C   . ASN B 309 ? 0.4984 0.7749 0.4883 -0.2112 0.0003  0.0727  610 ASN B C   
5856  O O   . ASN B 309 ? 0.5452 0.8450 0.5349 -0.2334 0.0021  0.0767  610 ASN B O   
5857  C CB  . ASN B 309 ? 0.5626 0.7473 0.5205 -0.2331 -0.0019 0.0803  610 ASN B CB  
5858  C CG  . ASN B 309 ? 0.6183 0.8099 0.5707 -0.2444 0.0033  0.0888  610 ASN B CG  
5859  O OD1 . ASN B 309 ? 0.5819 0.7931 0.5412 -0.2303 0.0071  0.0900  610 ASN B OD1 
5860  N ND2 . ASN B 309 ? 0.6442 0.8175 0.5822 -0.2701 0.0035  0.0945  610 ASN B ND2 
5861  N N   . ILE B 310 ? 0.5155 0.8190 0.5180 -0.1895 -0.0001 0.0669  611 ILE B N   
5862  C CA  . ILE B 310 ? 0.5813 0.9440 0.5980 -0.1904 0.0005  0.0643  611 ILE B CA  
5863  C C   . ILE B 310 ? 0.6077 1.0068 0.6313 -0.1828 0.0064  0.0668  611 ILE B C   
5864  O O   . ILE B 310 ? 0.5993 1.0516 0.6351 -0.1788 0.0077  0.0645  611 ILE B O   
5865  C CB  . ILE B 310 ? 0.6166 0.9919 0.6415 -0.1701 -0.0033 0.0570  611 ILE B CB  
5866  C CG1 . ILE B 310 ? 0.5816 0.9521 0.6086 -0.1403 -0.0008 0.0546  611 ILE B CG1 
5867  C CG2 . ILE B 310 ? 0.6722 1.0062 0.6886 -0.1739 -0.0087 0.0543  611 ILE B CG2 
5868  C CD1 . ILE B 310 ? 0.3643 0.7487 0.3973 -0.1197 -0.0038 0.0485  611 ILE B CD1 
5869  N N   . LEU B 311 ? 0.5456 0.9185 0.5607 -0.1801 0.0101  0.0714  612 LEU B N   
5870  C CA  . LEU B 311 ? 0.4973 0.9007 0.5172 -0.1690 0.0157  0.0727  612 LEU B CA  
5871  C C   . LEU B 311 ? 0.4758 0.9327 0.5032 -0.1869 0.0191  0.0760  612 LEU B C   
5872  O O   . LEU B 311 ? 0.5831 1.0887 0.6217 -0.1743 0.0217  0.0730  612 LEU B O   
5873  C CB  . LEU B 311 ? 0.3972 0.7630 0.4053 -0.1663 0.0184  0.0773  612 LEU B CB  
5874  C CG  . LEU B 311 ? 0.3857 0.7177 0.3903 -0.1418 0.0173  0.0730  612 LEU B CG  
5875  C CD1 . LEU B 311 ? 0.4254 0.7223 0.4182 -0.1427 0.0191  0.0779  612 LEU B CD1 
5876  C CD2 . LEU B 311 ? 0.3712 0.7324 0.3844 -0.1175 0.0193  0.0667  612 LEU B CD2 
5877  N N   . GLU B 312 ? 0.5304 0.9793 0.5506 -0.2162 0.0193  0.0822  613 GLU B N   
5878  C CA  . GLU B 312 ? 0.6464 1.1468 0.6729 -0.2365 0.0232  0.0862  613 GLU B CA  
5879  C C   . GLU B 312 ? 0.6981 1.2550 0.7411 -0.2341 0.0212  0.0801  613 GLU B C   
5880  O O   . GLU B 312 ? 0.6251 1.2396 0.6795 -0.2303 0.0252  0.0798  613 GLU B O   
5881  C CB  . GLU B 312 ? 0.7790 1.2553 0.7924 -0.2709 0.0232  0.0936  613 GLU B CB  
5882  C CG  . GLU B 312 ? 0.9061 1.3176 0.9003 -0.2727 0.0233  0.0992  613 GLU B CG  
5883  C CD  . GLU B 312 ? 0.9843 1.3425 0.9693 -0.2715 0.0168  0.0959  613 GLU B CD  
5884  O OE1 . GLU B 312 ? 1.0192 1.3492 0.9911 -0.2957 0.0149  0.0994  613 GLU B OE1 
5885  O OE2 . GLU B 312 ? 0.9445 1.2884 0.9341 -0.2466 0.0140  0.0896  613 GLU B OE2 
5886  N N   . GLU B 313 ? 0.7629 1.3058 0.8070 -0.2348 0.0148  0.0750  614 GLU B N   
5887  C CA  . GLU B 313 ? 0.7718 1.3683 0.8305 -0.2334 0.0119  0.0694  614 GLU B CA  
5888  C C   . GLU B 313 ? 0.7516 1.3838 0.8217 -0.1996 0.0136  0.0643  614 GLU B C   
5889  O O   . GLU B 313 ? 0.7968 1.4923 0.8801 -0.1968 0.0150  0.0624  614 GLU B O   
5890  C CB  . GLU B 313 ? 0.8759 1.4446 0.9311 -0.2387 0.0045  0.0649  614 GLU B CB  
5891  C CG  . GLU B 313 ? 1.0783 1.6690 1.1344 -0.2723 0.0017  0.0653  614 GLU B CG  
5892  C CD  . GLU B 313 ? 1.1521 1.7817 1.2199 -0.2669 -0.0041 0.0578  614 GLU B CD  
5893  O OE1 . GLU B 313 ? 1.1396 1.7857 1.2158 -0.2358 -0.0050 0.0532  614 GLU B OE1 
5894  O OE2 . GLU B 313 ? 1.1729 1.8158 1.2404 -0.2938 -0.0079 0.0564  614 GLU B OE2 
5895  N N   . VAL B 314 ? 0.6866 1.2793 0.7508 -0.1735 0.0134  0.0620  615 VAL B N   
5896  C CA  . VAL B 314 ? 0.5903 1.2094 0.6611 -0.1413 0.0155  0.0573  615 VAL B CA  
5897  C C   . VAL B 314 ? 0.5315 1.1855 0.6052 -0.1389 0.0226  0.0602  615 VAL B C   
5898  O O   . VAL B 314 ? 0.5045 1.2102 0.5876 -0.1226 0.0250  0.0571  615 VAL B O   
5899  C CB  . VAL B 314 ? 0.5274 1.0923 0.5891 -0.1171 0.0138  0.0540  615 VAL B CB  
5900  C CG1 . VAL B 314 ? 0.4672 1.0520 0.5315 -0.0848 0.0167  0.0494  615 VAL B CG1 
5901  C CG2 . VAL B 314 ? 0.4473 0.9865 0.5073 -0.1173 0.0071  0.0507  615 VAL B CG2 
5902  N N   . ALA B 315 ? 0.5498 1.1777 0.6144 -0.1545 0.0261  0.0665  616 ALA B N   
5903  C CA  . ALA B 315 ? 0.5607 1.2200 0.6264 -0.1524 0.0331  0.0696  616 ALA B CA  
5904  C C   . ALA B 315 ? 0.3800 1.1087 0.4579 -0.1691 0.0359  0.0715  616 ALA B C   
5905  O O   . ALA B 315 ? 0.3747 1.1541 0.4607 -0.1538 0.0403  0.0694  616 ALA B O   
5906  C CB  . ALA B 315 ? 0.5771 1.1930 0.6292 -0.1664 0.0359  0.0767  616 ALA B CB  
5907  N N   . LYS B 316 ? 0.5630 1.2961 0.6419 -0.2004 0.0333  0.0750  617 LYS B N   
5908  C CA  . LYS B 316 ? 0.5400 1.3419 0.6313 -0.2196 0.0353  0.0764  617 LYS B CA  
5909  C C   . LYS B 316 ? 0.5024 1.3610 0.6092 -0.1956 0.0335  0.0687  617 LYS B C   
5910  O O   . LYS B 316 ? 0.4299 1.3348 0.5395 -0.1868 0.0353  0.0670  617 LYS B O   
5911  C CB  . LYS B 316 ? 0.6483 1.4330 0.7340 -0.2549 0.0306  0.0790  617 LYS B CB  
5912  C CG  . LYS B 316 ? 0.7851 1.5203 0.8530 -0.2814 0.0326  0.0875  617 LYS B CG  
5913  C CD  . LYS B 316 ? 0.8400 1.5458 0.8975 -0.3115 0.0268  0.0882  617 LYS B CD  
5914  C CE  . LYS B 316 ? 0.9152 1.6040 0.9786 -0.3057 0.0209  0.0825  617 LYS B CE  
5915  N NZ  . LYS B 316 ? 0.9549 1.5984 1.0040 -0.3326 0.0155  0.0830  617 LYS B NZ  
5916  N N   . LYS B 317 ? 0.5489 1.3846 0.6560 -0.1793 0.0270  0.0627  618 LYS B N   
5917  C CA  . LYS B 317 ? 0.5750 1.4600 0.6942 -0.1538 0.0249  0.0560  618 LYS B CA  
5918  C C   . LYS B 317 ? 0.6185 1.5238 0.7384 -0.1201 0.0302  0.0534  618 LYS B C   
5919  O O   . LYS B 317 ? 0.6269 1.5879 0.7558 -0.1015 0.0306  0.0493  618 LYS B O   
5920  C CB  . LYS B 317 ? 0.6368 1.4841 0.7525 -0.1405 0.0173  0.0509  618 LYS B CB  
5921  C CG  . LYS B 317 ? 0.6855 1.5414 0.8051 -0.1671 0.0110  0.0502  618 LYS B CG  
5922  C CD  . LYS B 317 ? 0.7677 1.7007 0.9012 -0.1663 0.0094  0.0468  618 LYS B CD  
5923  C CE  . LYS B 317 ? 0.9033 1.8432 1.0305 -0.2032 0.0071  0.0486  618 LYS B CE  
5924  N NZ  . LYS B 317 ? 0.9830 1.8840 1.1060 -0.2249 0.0009  0.0478  618 LYS B NZ  
5925  N N   . MET B 318 ? 0.5765 1.4352 0.6845 -0.1113 0.0339  0.0553  619 MET B N   
5926  C CA  . MET B 318 ? 0.5729 1.4424 0.6783 -0.0797 0.0388  0.0519  619 MET B CA  
5927  C C   . MET B 318 ? 0.5644 1.4820 0.6738 -0.0873 0.0465  0.0556  619 MET B C   
5928  O O   . MET B 318 ? 0.5034 1.4368 0.6105 -0.0610 0.0510  0.0522  619 MET B O   
5929  C CB  . MET B 318 ? 0.5838 1.3801 0.6736 -0.0654 0.0385  0.0510  619 MET B CB  
5930  C CG  . MET B 318 ? 0.5398 1.2937 0.6248 -0.0474 0.0324  0.0460  619 MET B CG  
5931  S SD  . MET B 318 ? 0.5965 1.2675 0.6642 -0.0363 0.0321  0.0452  619 MET B SD  
5932  C CE  . MET B 318 ? 0.5563 1.2436 0.6183 -0.0096 0.0390  0.0417  619 MET B CE  
5933  N N   . ASN B 319 ? 0.5779 1.5086 0.6880 -0.1214 0.0467  0.0618  620 ASN B N   
5934  C CA  . ASN B 319 ? 0.7131 1.6685 0.8182 -0.1305 0.0503  0.0653  620 ASN B CA  
5935  C C   . ASN B 319 ? 0.7052 1.6315 0.8014 -0.1231 0.0570  0.0683  620 ASN B C   
5936  O O   . ASN B 319 ? 0.6610 1.6068 0.7549 -0.1000 0.0609  0.0652  620 ASN B O   
5937  C CB  . ASN B 319 ? 0.8195 1.8333 0.9293 -0.1095 0.0495  0.0597  620 ASN B CB  
5938  C CG  . ASN B 319 ? 0.9192 1.9640 1.0358 -0.1159 0.0430  0.0567  620 ASN B CG  
5939  O OD1 . ASN B 319 ? 1.0343 2.0891 1.1502 -0.1467 0.0406  0.0602  620 ASN B OD1 
5940  N ND2 . ASN B 319 ? 0.8929 1.9511 1.0140 -0.0864 0.0402  0.0500  620 ASN B ND2 
5941  N N   . LEU B 320 ? 0.6903 1.5677 0.7794 -0.1431 0.0580  0.0745  621 LEU B N   
5942  C CA  . LEU B 320 ? 0.6305 1.4648 0.7064 -0.1360 0.0617  0.0770  621 LEU B CA  
5943  C C   . LEU B 320 ? 0.7242 1.5530 0.7923 -0.1661 0.0654  0.0869  621 LEU B C   
5944  O O   . LEU B 320 ? 0.7679 1.5874 0.8340 -0.1949 0.0618  0.0917  621 LEU B O   
5945  C CB  . LEU B 320 ? 0.6082 1.3685 0.6739 -0.1279 0.0556  0.0746  621 LEU B CB  
5946  C CG  . LEU B 320 ? 0.5441 1.2943 0.6115 -0.0946 0.0520  0.0651  621 LEU B CG  
5947  C CD1 . LEU B 320 ? 0.4429 1.1236 0.5012 -0.0929 0.0461  0.0639  621 LEU B CD1 
5948  C CD2 . LEU B 320 ? 0.3678 1.1302 0.4308 -0.0659 0.0570  0.0602  621 LEU B CD2 
5949  N N   . ASP B 321 ? 0.7173 1.5431 0.7770 -0.1571 0.0707  0.0888  622 ASP B N   
5950  C CA  . ASP B 321 ? 0.7726 1.5811 0.8203 -0.1798 0.0729  0.0978  622 ASP B CA  
5951  C C   . ASP B 321 ? 0.6732 1.4215 0.7097 -0.1983 0.0717  0.1048  622 ASP B C   
5952  O O   . ASP B 321 ? 0.7500 1.4522 0.7753 -0.1842 0.0708  0.1041  622 ASP B O   
5953  C CB  . ASP B 321 ? 0.9794 1.7975 1.0206 -0.1610 0.0786  0.0969  622 ASP B CB  
5954  C CG  . ASP B 321 ? 1.1193 1.9244 1.1482 -0.1819 0.0810  0.1062  622 ASP B CG  
5955  O OD1 . ASP B 321 ? 1.1700 1.9510 1.1932 -0.2103 0.0785  0.1137  622 ASP B OD1 
5956  O OD2 . ASP B 321 ? 1.1409 1.9581 1.1645 -0.1692 0.0852  0.1058  622 ASP B OD2 
5957  N N   . MET B 322 ? 0.5725 1.3053 0.6074 -0.2253 0.0671  0.1089  623 MET B N   
5958  C CA  . MET B 322 ? 0.6283 1.2984 0.6507 -0.2402 0.0640  0.1142  623 MET B CA  
5959  C C   . MET B 322 ? 0.6934 1.3337 0.6983 -0.2641 0.0658  0.1248  623 MET B C   
5960  O O   . MET B 322 ? 0.7584 1.3501 0.7513 -0.2818 0.0626  0.1300  623 MET B O   
5961  C CB  . MET B 322 ? 0.5319 1.1948 0.5603 -0.2531 0.0576  0.1112  623 MET B CB  
5962  C CG  . MET B 322 ? 0.5480 1.2272 0.5900 -0.2270 0.0532  0.1001  623 MET B CG  
5963  S SD  . MET B 322 ? 0.7433 1.4219 0.7922 -0.2440 0.0458  0.0967  623 MET B SD  
5964  C CE  . MET B 322 ? 0.7038 1.2952 0.7327 -0.2577 0.0410  0.1012  623 MET B CE  
5965  N N   . ARG B 323 ? 0.6866 1.3503 0.6881 -0.2627 0.0700  0.1277  624 ARG B N   
5966  C CA  . ARG B 323 ? 0.7043 1.3380 0.6881 -0.2837 0.0712  0.1376  624 ARG B CA  
5967  C C   . ARG B 323 ? 0.6527 1.2444 0.6213 -0.2742 0.0740  0.1432  624 ARG B C   
5968  O O   . ARG B 323 ? 0.8108 1.3642 0.7619 -0.2903 0.0739  0.1522  624 ARG B O   
5969  C CB  . ARG B 323 ? 0.8885 1.5680 0.8747 -0.2914 0.0741  0.1391  624 ARG B CB  
5970  C CG  . ARG B 323 ? 0.9831 1.7012 0.9756 -0.2666 0.0790  0.1353  624 ARG B CG  
5971  C CD  . ARG B 323 ? 1.0377 1.8011 1.0319 -0.2751 0.0816  0.1373  624 ARG B CD  
5972  N NE  . ARG B 323 ? 1.1245 1.8662 1.1027 -0.2822 0.0855  0.1460  624 ARG B NE  
5973  C CZ  . ARG B 323 ? 1.1905 1.8992 1.1537 -0.3084 0.0851  0.1554  624 ARG B CZ  
5974  N NH1 . ARG B 323 ? 1.2398 1.9334 1.2019 -0.3302 0.0808  0.1565  624 ARG B NH1 
5975  N NH2 . ARG B 323 ? 1.1667 1.8566 1.1149 -0.3121 0.0888  0.1636  624 ARG B NH2 
5976  N N   . LYS B 324 ? 0.6437 1.2405 0.6168 -0.2482 0.0762  0.1382  625 LYS B N   
5977  C CA  . LYS B 324 ? 0.7389 1.2889 0.6966 -0.2367 0.0758  0.1411  625 LYS B CA  
5978  C C   . LYS B 324 ? 0.7190 1.2416 0.6821 -0.2088 0.0697  0.1298  625 LYS B C   
5979  O O   . LYS B 324 ? 0.7751 1.3236 0.7530 -0.1944 0.0682  0.1202  625 LYS B O   
5980  C CB  . LYS B 324 ? 0.7458 1.3219 0.6973 -0.2299 0.0827  0.1446  625 LYS B CB  
5981  C CG  . LYS B 324 ? 0.9166 1.4489 0.8462 -0.2380 0.0833  0.1552  625 LYS B CG  
5982  C CD  . LYS B 324 ? 1.0045 1.4897 0.9270 -0.2146 0.0780  0.1499  625 LYS B CD  
5983  C CE  . LYS B 324 ? 1.0486 1.4902 0.9490 -0.2213 0.0777  0.1607  625 LYS B CE  
5984  N NZ  . LYS B 324 ? 0.9818 1.4457 0.8737 -0.2148 0.0834  0.1643  625 LYS B NZ  
5985  N N   . THR B 325 ? 0.6597 1.1296 0.6098 -0.2016 0.0663  0.1313  626 THR B N   
5986  C CA  . THR B 325 ? 0.5673 1.0095 0.5208 -0.1771 0.0610  0.1213  626 THR B CA  
5987  C C   . THR B 325 ? 0.5158 0.9883 0.4763 -0.1518 0.0636  0.1119  626 THR B C   
5988  O O   . THR B 325 ? 0.4528 0.9233 0.4216 -0.1334 0.0605  0.1018  626 THR B O   
5989  C CB  . THR B 325 ? 0.6198 1.0070 0.5577 -0.1746 0.0575  0.1253  626 THR B CB  
5990  O OG1 . THR B 325 ? 0.8142 1.2065 0.7400 -0.1768 0.0620  0.1324  626 THR B OG1 
5991  C CG2 . THR B 325 ? 0.5610 0.9094 0.4904 -0.1938 0.0538  0.1322  626 THR B CG2 
5992  N N   . SER B 326 ? 0.5782 1.0759 0.5331 -0.1501 0.0694  0.1150  627 SER B N   
5993  C CA  . SER B 326 ? 0.4357 0.9491 0.3912 -0.1249 0.0715  0.1059  627 SER B CA  
5994  C C   . SER B 326 ? 0.5047 1.0605 0.4744 -0.1100 0.0731  0.0964  627 SER B C   
5995  O O   . SER B 326 ? 0.5155 1.0763 0.4844 -0.0863 0.0738  0.0870  627 SER B O   
5996  C CB  . SER B 326 ? 0.4904 1.0236 0.4355 -0.1273 0.0776  0.1115  627 SER B CB  
5997  O OG  . SER B 326 ? 0.6456 1.1867 0.5853 -0.1538 0.0808  0.1245  627 SER B OG  
5998  N N   . SER B 327 ? 0.4224 1.0097 0.4036 -0.1230 0.0738  0.0985  628 SER B N   
5999  C CA  . SER B 327 ? 0.4678 1.0905 0.4627 -0.1066 0.0737  0.0893  628 SER B CA  
6000  C C   . SER B 327 ? 0.3994 0.9849 0.3964 -0.0901 0.0670  0.0809  628 SER B C   
6001  O O   . SER B 327 ? 0.4936 1.1003 0.4983 -0.0712 0.0666  0.0725  628 SER B O   
6002  C CB  . SER B 327 ? 0.4988 1.1644 0.5058 -0.1263 0.0750  0.0937  628 SER B CB  
6003  O OG  . SER B 327 ? 0.4825 1.1142 0.4900 -0.1436 0.0693  0.0971  628 SER B OG  
6004  N N   . LEU B 328 ? 0.4208 0.9525 0.4103 -0.0961 0.0621  0.0832  629 LEU B N   
6005  C CA  . LEU B 328 ? 0.4061 0.9010 0.3967 -0.0823 0.0562  0.0760  629 LEU B CA  
6006  C C   . LEU B 328 ? 0.4498 0.9632 0.4527 -0.0832 0.0534  0.0731  629 LEU B C   
6007  O O   . LEU B 328 ? 0.3857 0.8895 0.3916 -0.0646 0.0505  0.0652  629 LEU B O   
6008  C CB  . LEU B 328 ? 0.3869 0.8724 0.3724 -0.0551 0.0567  0.0663  629 LEU B CB  
6009  C CG  . LEU B 328 ? 0.4179 0.8846 0.3906 -0.0516 0.0586  0.0670  629 LEU B CG  
6010  C CD1 . LEU B 328 ? 0.3912 0.8309 0.3574 -0.0289 0.0566  0.0567  629 LEU B CD1 
6011  C CD2 . LEU B 328 ? 0.3994 0.8325 0.3646 -0.0708 0.0563  0.0764  629 LEU B CD2 
6012  N N   . TRP B 329 ? 0.3907 0.9307 0.4000 -0.1056 0.0542  0.0795  630 TRP B N   
6013  C CA  . TRP B 329 ? 0.4579 1.0194 0.4790 -0.1082 0.0511  0.0767  630 TRP B CA  
6014  C C   . TRP B 329 ? 0.4847 0.9979 0.5036 -0.1069 0.0443  0.0742  630 TRP B C   
6015  O O   . TRP B 329 ? 0.4348 0.9540 0.4606 -0.0940 0.0411  0.0679  630 TRP B O   
6016  C CB  . TRP B 329 ? 0.5071 1.1040 0.5338 -0.1366 0.0531  0.0841  630 TRP B CB  
6017  C CG  . TRP B 329 ? 0.5459 1.1055 0.5619 -0.1638 0.0520  0.0934  630 TRP B CG  
6018  C CD1 . TRP B 329 ? 0.5463 1.0966 0.5513 -0.1766 0.0560  0.1017  630 TRP B CD1 
6019  C CD2 . TRP B 329 ? 0.6182 1.1434 0.6314 -0.1805 0.0464  0.0954  630 TRP B CD2 
6020  N NE1 . TRP B 329 ? 0.5862 1.0965 0.5807 -0.1995 0.0534  0.1091  630 TRP B NE1 
6021  C CE2 . TRP B 329 ? 0.6421 1.1359 0.6413 -0.2022 0.0475  0.1050  630 TRP B CE2 
6022  C CE3 . TRP B 329 ? 0.5827 1.0999 0.6024 -0.1783 0.0407  0.0900  630 TRP B CE3 
6023  C CZ2 . TRP B 329 ? 0.5971 1.0499 0.5878 -0.2209 0.0431  0.1087  630 TRP B CZ2 
6024  C CZ3 . TRP B 329 ? 0.5428 1.0220 0.5552 -0.1978 0.0363  0.0934  630 TRP B CZ3 
6025  C CH2 . TRP B 329 ? 0.5049 0.9515 0.5026 -0.2185 0.0376  0.1024  630 TRP B CH2 
6026  N N   . LYS B 330 ? 0.4289 0.8946 0.4374 -0.1187 0.0421  0.0792  631 LYS B N   
6027  C CA  . LYS B 330 ? 0.4021 0.8221 0.4076 -0.1162 0.0362  0.0768  631 LYS B CA  
6028  C C   . LYS B 330 ? 0.5474 0.9526 0.5531 -0.0890 0.0347  0.0680  631 LYS B C   
6029  O O   . LYS B 330 ? 0.3642 0.7601 0.3740 -0.0813 0.0308  0.0633  631 LYS B O   
6030  C CB  . LYS B 330 ? 0.3920 0.7657 0.3846 -0.1292 0.0349  0.0834  631 LYS B CB  
6031  C CG  . LYS B 330 ? 0.5011 0.8730 0.4896 -0.1575 0.0348  0.0918  631 LYS B CG  
6032  C CD  . LYS B 330 ? 0.5236 0.8442 0.4968 -0.1658 0.0329  0.0980  631 LYS B CD  
6033  C CE  . LYS B 330 ? 0.5791 0.8878 0.5447 -0.1931 0.0321  0.1056  631 LYS B CE  
6034  N NZ  . LYS B 330 ? 0.7514 1.0075 0.7000 -0.1971 0.0302  0.1114  631 LYS B NZ  
6035  N N   . ASP B 331 ? 0.5038 0.9056 0.5037 -0.0750 0.0378  0.0658  632 ASP B N   
6036  C CA  . ASP B 331 ? 0.4242 0.8073 0.4211 -0.0511 0.0367  0.0574  632 ASP B CA  
6037  C C   . ASP B 331 ? 0.4775 0.8912 0.4819 -0.0345 0.0371  0.0510  632 ASP B C   
6038  O O   . ASP B 331 ? 0.4882 0.8813 0.4911 -0.0192 0.0344  0.0452  632 ASP B O   
6039  C CB  . ASP B 331 ? 0.3684 0.7469 0.3566 -0.0412 0.0403  0.0556  632 ASP B CB  
6040  C CG  . ASP B 331 ? 0.3798 0.7375 0.3602 -0.0568 0.0405  0.0631  632 ASP B CG  
6041  O OD1 . ASP B 331 ? 0.3808 0.7601 0.3621 -0.0733 0.0430  0.0705  632 ASP B OD1 
6042  O OD2 . ASP B 331 ? 0.3746 0.6956 0.3474 -0.0526 0.0382  0.0618  632 ASP B OD2 
6043  N N   . GLN B 332 ? 0.4275 0.8915 0.4393 -0.0369 0.0406  0.0522  633 GLN B N   
6044  C CA  . GLN B 332 ? 0.5191 1.0190 0.5376 -0.0187 0.0412  0.0464  633 GLN B CA  
6045  C C   . GLN B 332 ? 0.4811 0.9824 0.5073 -0.0230 0.0363  0.0460  633 GLN B C   
6046  O O   . GLN B 332 ? 0.4047 0.9022 0.4307 -0.0034 0.0341  0.0403  633 GLN B O   
6047  C CB  . GLN B 332 ? 0.5715 1.1300 0.5967 -0.0215 0.0465  0.0483  633 GLN B CB  
6048  C CG  . GLN B 332 ? 0.6376 1.2166 0.6587 0.0055  0.0506  0.0414  633 GLN B CG  
6049  C CD  . GLN B 332 ? 0.6670 1.3065 0.6947 0.0027  0.0564  0.0435  633 GLN B CD  
6050  O OE1 . GLN B 332 ? 0.6677 1.3245 0.6992 -0.0218 0.0585  0.0511  633 GLN B OE1 
6051  N NE2 . GLN B 332 ? 0.7245 1.3966 0.7526 0.0279  0.0592  0.0369  633 GLN B NE2 
6052  N N   . ALA B 333 ? 0.5000 1.0070 0.5314 -0.0487 0.0344  0.0521  634 ALA B N   
6053  C CA  . ALA B 333 ? 0.4491 0.9539 0.4862 -0.0552 0.0292  0.0515  634 ALA B CA  
6054  C C   . ALA B 333 ? 0.4483 0.8991 0.4779 -0.0458 0.0250  0.0485  634 ALA B C   
6055  O O   . ALA B 333 ? 0.4177 0.8669 0.4496 -0.0344 0.0216  0.0445  634 ALA B O   
6056  C CB  . ALA B 333 ? 0.4122 0.9232 0.4523 -0.0867 0.0280  0.0583  634 ALA B CB  
6057  N N   . LEU B 334 ? 0.4586 0.8671 0.4789 -0.0498 0.0254  0.0507  635 LEU B N   
6058  C CA  . LEU B 334 ? 0.5029 0.8624 0.5164 -0.0430 0.0218  0.0483  635 LEU B CA  
6059  C C   . LEU B 334 ? 0.5225 0.8775 0.5336 -0.0170 0.0218  0.0412  635 LEU B C   
6060  O O   . LEU B 334 ? 0.5409 0.8744 0.5507 -0.0108 0.0182  0.0388  635 LEU B O   
6061  C CB  . LEU B 334 ? 0.4995 0.8231 0.5039 -0.0486 0.0228  0.0512  635 LEU B CB  
6062  C CG  . LEU B 334 ? 0.5087 0.7854 0.5066 -0.0419 0.0196  0.0487  635 LEU B CG  
6063  C CD1 . LEU B 334 ? 0.4460 0.7050 0.4451 -0.0558 0.0153  0.0514  635 LEU B CD1 
6064  C CD2 . LEU B 334 ? 0.4595 0.7100 0.4490 -0.0421 0.0210  0.0501  635 LEU B CD2 
6065  N N   . VAL B 335 ? 0.4945 0.8690 0.5035 -0.0015 0.0258  0.0380  636 VAL B N   
6066  C CA  . VAL B 335 ? 0.4527 0.8185 0.4557 0.0241  0.0262  0.0313  636 VAL B CA  
6067  C C   . VAL B 335 ? 0.4696 0.8618 0.4789 0.0334  0.0239  0.0295  636 VAL B C   
6068  O O   . VAL B 335 ? 0.5279 0.8969 0.5319 0.0467  0.0214  0.0264  636 VAL B O   
6069  C CB  . VAL B 335 ? 0.3679 0.7478 0.3649 0.0389  0.0312  0.0276  636 VAL B CB  
6070  C CG1 . VAL B 335 ? 0.3998 0.7743 0.3888 0.0660  0.0317  0.0207  636 VAL B CG1 
6071  C CG2 . VAL B 335 ? 0.3636 0.7102 0.3518 0.0332  0.0324  0.0280  636 VAL B CG2 
6072  N N   . GLU B 336 ? 0.3869 0.8290 0.4071 0.0260  0.0246  0.0317  637 GLU B N   
6073  C CA  . GLU B 336 ? 0.4595 0.9338 0.4867 0.0350  0.0220  0.0298  637 GLU B CA  
6074  C C   . GLU B 336 ? 0.4786 0.9284 0.5069 0.0255  0.0163  0.0310  637 GLU B C   
6075  O O   . GLU B 336 ? 0.4484 0.8991 0.4755 0.0408  0.0136  0.0281  637 GLU B O   
6076  C CB  . GLU B 336 ? 0.3783 0.9142 0.4183 0.0242  0.0237  0.0323  637 GLU B CB  
6077  C CG  . GLU B 336 ? 0.4187 0.9878 0.4580 0.0375  0.0296  0.0305  637 GLU B CG  
6078  C CD  . GLU B 336 ? 0.5078 1.0769 0.5386 0.0721  0.0309  0.0238  637 GLU B CD  
6079  O OE1 . GLU B 336 ? 0.5356 1.0949 0.5639 0.0865  0.0273  0.0213  637 GLU B OE1 
6080  O OE2 . GLU B 336 ? 0.5269 1.1049 0.5518 0.0855  0.0358  0.0212  637 GLU B OE2 
6081  N N   . ILE B 337 ? 0.4433 0.8702 0.4724 0.0014  0.0146  0.0351  638 ILE B N   
6082  C CA  . ILE B 337 ? 0.4268 0.8289 0.4557 -0.0079 0.0094  0.0358  638 ILE B CA  
6083  C C   . ILE B 337 ? 0.4481 0.8062 0.4668 0.0096  0.0082  0.0326  638 ILE B C   
6084  O O   . ILE B 337 ? 0.4563 0.8074 0.4741 0.0158  0.0046  0.0310  638 ILE B O   
6085  C CB  . ILE B 337 ? 0.4043 0.7859 0.4326 -0.0351 0.0084  0.0407  638 ILE B CB  
6086  C CG1 . ILE B 337 ? 0.4126 0.8383 0.4498 -0.0551 0.0092  0.0441  638 ILE B CG1 
6087  C CG2 . ILE B 337 ? 0.4302 0.7777 0.4551 -0.0423 0.0035  0.0405  638 ILE B CG2 
6088  C CD1 . ILE B 337 ? 0.4633 0.8686 0.4963 -0.0797 0.0101  0.0498  638 ILE B CD1 
6089  N N   . ASN B 338 ? 0.4492 0.7782 0.4595 0.0173  0.0113  0.0316  639 ASN B N   
6090  C CA  . ASN B 338 ? 0.4922 0.7787 0.4921 0.0308  0.0106  0.0288  639 ASN B CA  
6091  C C   . ASN B 338 ? 0.4942 0.7884 0.4884 0.0563  0.0115  0.0246  639 ASN B C   
6092  O O   . ASN B 338 ? 0.4958 0.7626 0.4825 0.0662  0.0097  0.0231  639 ASN B O   
6093  C CB  . ASN B 338 ? 0.5134 0.7681 0.5059 0.0282  0.0133  0.0287  639 ASN B CB  
6094  C CG  . ASN B 338 ? 0.5284 0.7612 0.5224 0.0073  0.0114  0.0329  639 ASN B CG  
6095  O OD1 . ASN B 338 ? 0.4800 0.6797 0.4698 0.0057  0.0092  0.0328  639 ASN B OD1 
6096  N ND2 . ASN B 338 ? 0.5011 0.7528 0.5001 -0.0085 0.0123  0.0369  639 ASN B ND2 
6097  N N   . ILE B 339 ? 0.4098 0.7402 0.4060 0.0678  0.0144  0.0228  640 ILE B N   
6098  C CA  . ILE B 339 ? 0.4349 0.7792 0.4257 0.0935  0.0147  0.0193  640 ILE B CA  
6099  C C   . ILE B 339 ? 0.5627 0.9245 0.5596 0.0936  0.0100  0.0205  640 ILE B C   
6100  O O   . ILE B 339 ? 0.6386 0.9867 0.6268 0.1120  0.0085  0.0188  640 ILE B O   
6101  C CB  . ILE B 339 ? 0.3774 0.7658 0.3713 0.1050  0.0185  0.0174  640 ILE B CB  
6102  C CG1 . ILE B 339 ? 0.3845 0.7511 0.3681 0.1104  0.0231  0.0147  640 ILE B CG1 
6103  C CG2 . ILE B 339 ? 0.3890 0.8008 0.3790 0.1317  0.0180  0.0144  640 ILE B CG2 
6104  C CD1 . ILE B 339 ? 0.3920 0.7986 0.3756 0.1262  0.0272  0.0118  640 ILE B CD1 
6105  N N   . ALA B 340 ? 0.5320 0.9230 0.5424 0.0724  0.0075  0.0235  641 ALA B N   
6106  C CA  . ALA B 340 ? 0.4494 0.8652 0.4665 0.0709  0.0027  0.0239  641 ALA B CA  
6107  C C   . ALA B 340 ? 0.4708 0.8438 0.4814 0.0669  -0.0011 0.0245  641 ALA B C   
6108  O O   . ALA B 340 ? 0.4987 0.8739 0.5059 0.0802  -0.0041 0.0235  641 ALA B O   
6109  C CB  . ALA B 340 ? 0.3904 0.8490 0.4222 0.0466  0.0014  0.0264  641 ALA B CB  
6110  N N   . VAL B 341 ? 0.4532 0.7888 0.4616 0.0497  -0.0009 0.0263  642 VAL B N   
6111  C CA  . VAL B 341 ? 0.4833 0.7795 0.4855 0.0458  -0.0039 0.0267  642 VAL B CA  
6112  C C   . VAL B 341 ? 0.5561 0.8235 0.5452 0.0691  -0.0028 0.0248  642 VAL B C   
6113  O O   . VAL B 341 ? 0.4552 0.7160 0.4400 0.0770  -0.0057 0.0246  642 VAL B O   
6114  C CB  . VAL B 341 ? 0.4317 0.6943 0.4328 0.0266  -0.0032 0.0288  642 VAL B CB  
6115  C CG1 . VAL B 341 ? 0.3795 0.5975 0.3717 0.0288  -0.0045 0.0285  642 VAL B CG1 
6116  C CG2 . VAL B 341 ? 0.4104 0.6918 0.4203 0.0022  -0.0056 0.0312  642 VAL B CG2 
6117  N N   . LEU B 342 ? 0.4482 0.6981 0.4293 0.0801  0.0016  0.0233  643 LEU B N   
6118  C CA  . LEU B 342 ? 0.4505 0.6695 0.4162 0.1011  0.0032  0.0213  643 LEU B CA  
6119  C C   . LEU B 342 ? 0.5504 0.7928 0.5124 0.1225  0.0017  0.0205  643 LEU B C   
6120  O O   . LEU B 342 ? 0.6040 0.8251 0.5563 0.1326  0.0000  0.0212  643 LEU B O   
6121  C CB  . LEU B 342 ? 0.4696 0.6730 0.4270 0.1088  0.0080  0.0188  643 LEU B CB  
6122  C CG  . LEU B 342 ? 0.5124 0.6841 0.4688 0.0924  0.0096  0.0192  643 LEU B CG  
6123  C CD1 . LEU B 342 ? 0.3939 0.5590 0.3433 0.0989  0.0139  0.0160  643 LEU B CD1 
6124  C CD2 . LEU B 342 ? 0.3906 0.5192 0.3381 0.0905  0.0086  0.0197  643 LEU B CD2 
6125  N N   . TYR B 343 ? 0.5489 0.8366 0.5178 0.1308  0.0024  0.0194  644 TYR B N   
6126  C CA  . TYR B 343 ? 0.6056 0.9211 0.5711 0.1539  0.0009  0.0186  644 TYR B CA  
6127  C C   . TYR B 343 ? 0.6461 0.9734 0.6164 0.1494  -0.0046 0.0205  644 TYR B C   
6128  O O   . TYR B 343 ? 0.6280 0.9555 0.5889 0.1700  -0.0064 0.0206  644 TYR B O   
6129  C CB  . TYR B 343 ? 0.4044 0.7752 0.3803 0.1592  0.0025  0.0171  644 TYR B CB  
6130  C CG  . TYR B 343 ? 0.4167 0.8335 0.3953 0.1787  -0.0001 0.0166  644 TYR B CG  
6131  C CD1 . TYR B 343 ? 0.4794 0.8894 0.4420 0.2110  0.0014  0.0148  644 TYR B CD1 
6132  C CD2 . TYR B 343 ? 0.4494 0.9174 0.4454 0.1650  -0.0042 0.0177  644 TYR B CD2 
6133  C CE1 . TYR B 343 ? 0.5532 1.0077 0.5178 0.2311  -0.0012 0.0145  644 TYR B CE1 
6134  C CE2 . TYR B 343 ? 0.5089 1.0244 0.5083 0.1828  -0.0069 0.0170  644 TYR B CE2 
6135  C CZ  . TYR B 343 ? 0.5751 1.0848 0.5591 0.2169  -0.0055 0.0156  644 TYR B CZ  
6136  O OH  . TYR B 343 ? 0.5534 1.1123 0.5402 0.2373  -0.0085 0.0151  644 TYR B OH  
6137  N N   . SER B 344 ? 0.5965 0.9303 0.5791 0.1233  -0.0075 0.0220  645 SER B N   
6138  C CA  . SER B 344 ? 0.4637 0.8118 0.4507 0.1174  -0.0131 0.0228  645 SER B CA  
6139  C C   . SER B 344 ? 0.5197 0.8192 0.4935 0.1212  -0.0142 0.0240  645 SER B C   
6140  O O   . SER B 344 ? 0.5959 0.8990 0.5633 0.1351  -0.0172 0.0245  645 SER B O   
6141  C CB  . SER B 344 ? 0.3909 0.7607 0.3930 0.0878  -0.0156 0.0234  645 SER B CB  
6142  O OG  . SER B 344 ? 0.5176 0.9388 0.5317 0.0843  -0.0147 0.0229  645 SER B OG  
6143  N N   . PHE B 345 ? 0.4717 0.7278 0.4412 0.1091  -0.0118 0.0246  646 PHE B N   
6144  C CA  . PHE B 345 ? 0.5112 0.7215 0.4676 0.1129  -0.0117 0.0258  646 PHE B CA  
6145  C C   . PHE B 345 ? 0.6075 0.8003 0.5468 0.1397  -0.0096 0.0260  646 PHE B C   
6146  O O   . PHE B 345 ? 0.6588 0.8349 0.5879 0.1484  -0.0113 0.0277  646 PHE B O   
6147  C CB  . PHE B 345 ? 0.4267 0.5985 0.3816 0.0977  -0.0087 0.0261  646 PHE B CB  
6148  C CG  . PHE B 345 ? 0.4490 0.6203 0.4134 0.0741  -0.0115 0.0268  646 PHE B CG  
6149  C CD1 . PHE B 345 ? 0.4332 0.6384 0.4107 0.0590  -0.0135 0.0265  646 PHE B CD1 
6150  C CD2 . PHE B 345 ? 0.4260 0.5624 0.3846 0.0671  -0.0119 0.0276  646 PHE B CD2 
6151  C CE1 . PHE B 345 ? 0.3735 0.5729 0.3563 0.0376  -0.0161 0.0270  646 PHE B CE1 
6152  C CE2 . PHE B 345 ? 0.4147 0.5483 0.3797 0.0476  -0.0145 0.0278  646 PHE B CE2 
6153  C CZ  . PHE B 345 ? 0.3841 0.5468 0.3601 0.0331  -0.0167 0.0275  646 PHE B CZ  
6154  N N   . GLN B 346 ? 0.5472 0.7421 0.4813 0.1536  -0.0058 0.0244  647 GLN B N   
6155  C CA  . GLN B 346 ? 0.5874 0.7587 0.5014 0.1797  -0.0035 0.0244  647 GLN B CA  
6156  C C   . GLN B 346 ? 0.6926 0.8967 0.6043 0.2001  -0.0069 0.0253  647 GLN B C   
6157  O O   . GLN B 346 ? 0.7336 0.9136 0.6276 0.2183  -0.0070 0.0273  647 GLN B O   
6158  C CB  . GLN B 346 ? 0.5539 0.7168 0.4610 0.1895  0.0014  0.0215  647 GLN B CB  
6159  C CG  . GLN B 346 ? 0.6065 0.7324 0.5119 0.1726  0.0047  0.0204  647 GLN B CG  
6160  C CD  . GLN B 346 ? 0.6299 0.7550 0.5310 0.1791  0.0089  0.0167  647 GLN B CD  
6161  O OE1 . GLN B 346 ? 0.6250 0.7804 0.5260 0.1955  0.0097  0.0149  647 GLN B OE1 
6162  N NE2 . GLN B 346 ? 0.6207 0.7132 0.5180 0.1666  0.0116  0.0153  647 GLN B NE2 
6163  N N   . SER B 347 ? 0.6518 0.9119 0.5806 0.1973  -0.0097 0.0242  648 SER B N   
6164  C CA  . SER B 347 ? 0.5704 0.8698 0.4992 0.2160  -0.0136 0.0248  648 SER B CA  
6165  C C   . SER B 347 ? 0.5769 0.8683 0.5032 0.2116  -0.0184 0.0273  648 SER B C   
6166  O O   . SER B 347 ? 0.5794 0.8782 0.4951 0.2331  -0.0208 0.0289  648 SER B O   
6167  C CB  . SER B 347 ? 0.4965 0.8616 0.4463 0.2087  -0.0156 0.0229  648 SER B CB  
6168  O OG  . SER B 347 ? 0.6993 1.0764 0.6497 0.2172  -0.0110 0.0207  648 SER B OG  
6169  N N   . ASP B 348 ? 0.5722 0.8494 0.5071 0.1852  -0.0198 0.0275  649 ASP B N   
6170  C CA  . ASP B 348 ? 0.5675 0.8361 0.4998 0.1792  -0.0241 0.0292  649 ASP B CA  
6171  C C   . ASP B 348 ? 0.6316 0.8408 0.5456 0.1827  -0.0212 0.0318  649 ASP B C   
6172  O O   . ASP B 348 ? 0.5418 0.7372 0.4535 0.1742  -0.0237 0.0331  649 ASP B O   
6173  C CB  . ASP B 348 ? 0.4178 0.7041 0.3674 0.1495  -0.0275 0.0275  649 ASP B CB  
6174  C CG  . ASP B 348 ? 0.5421 0.8904 0.5082 0.1441  -0.0315 0.0254  649 ASP B CG  
6175  O OD1 . ASP B 348 ? 0.4716 0.8533 0.4369 0.1652  -0.0319 0.0252  649 ASP B OD1 
6176  O OD2 . ASP B 348 ? 0.5394 0.9033 0.5183 0.1188  -0.0341 0.0238  649 ASP B OD2 
6177  N N   . LYS B 349 ? 0.7275 0.9024 0.6278 0.1945  -0.0158 0.0322  650 LYS B N   
6178  C CA  . LYS B 349 ? 0.7868 0.9049 0.6686 0.1965  -0.0121 0.0346  650 LYS B CA  
6179  C C   . LYS B 349 ? 0.8135 0.9117 0.7023 0.1714  -0.0126 0.0349  650 LYS B C   
6180  O O   . LYS B 349 ? 0.9126 0.9843 0.7910 0.1710  -0.0127 0.0376  650 LYS B O   
6181  C CB  . LYS B 349 ? 0.7781 0.8816 0.6393 0.2201  -0.0129 0.0382  650 LYS B CB  
6182  C CG  . LYS B 349 ? 0.9139 1.0344 0.7654 0.2483  -0.0123 0.0378  650 LYS B CG  
6183  C CD  . LYS B 349 ? 1.0104 1.1126 0.8380 0.2743  -0.0131 0.0423  650 LYS B CD  
6184  C CE  . LYS B 349 ? 1.1547 1.1923 0.9552 0.2826  -0.0071 0.0446  650 LYS B CE  
6185  N NZ  . LYS B 349 ? 1.2318 1.2569 1.0231 0.2953  -0.0028 0.0414  650 LYS B NZ  
6186  N N   . VAL B 350 ? 0.6121 0.7232 0.5176 0.1512  -0.0126 0.0324  651 VAL B N   
6187  C CA  . VAL B 350 ? 0.5513 0.6415 0.4626 0.1290  -0.0123 0.0324  651 VAL B CA  
6188  C C   . VAL B 350 ? 0.5770 0.6377 0.4854 0.1232  -0.0072 0.0315  651 VAL B C   
6189  O O   . VAL B 350 ? 0.5331 0.6076 0.4471 0.1238  -0.0055 0.0296  651 VAL B O   
6190  C CB  . VAL B 350 ? 0.4777 0.6011 0.4075 0.1100  -0.0165 0.0305  651 VAL B CB  
6191  C CG1 . VAL B 350 ? 0.4868 0.5855 0.4197 0.0900  -0.0161 0.0304  651 VAL B CG1 
6192  C CG2 . VAL B 350 ? 0.5563 0.7117 0.4886 0.1146  -0.0221 0.0304  651 VAL B CG2 
6193  N N   . THR B 351 ? 0.4465 0.4692 0.3462 0.1173  -0.0046 0.0328  652 THR B N   
6194  C CA  . THR B 351 ? 0.4670 0.4618 0.3629 0.1113  -0.0001 0.0318  652 THR B CA  
6195  C C   . THR B 351 ? 0.5375 0.5506 0.4493 0.0965  -0.0004 0.0296  652 THR B C   
6196  O O   . THR B 351 ? 0.5543 0.5823 0.4782 0.0824  -0.0034 0.0297  652 THR B O   
6197  C CB  . THR B 351 ? 0.5196 0.4805 0.4083 0.1023  0.0019  0.0334  652 THR B CB  
6198  O OG1 . THR B 351 ? 0.6697 0.6167 0.5442 0.1137  0.0018  0.0364  652 THR B OG1 
6199  C CG2 . THR B 351 ? 0.4782 0.4100 0.3591 0.0994  0.0068  0.0321  652 THR B CG2 
6200  N N   . ILE B 352 ? 0.5393 0.5492 0.4489 0.1003  0.0027  0.0276  653 ILE B N   
6201  C CA  . ILE B 352 ? 0.5153 0.5378 0.4369 0.0872  0.0032  0.0260  653 ILE B CA  
6202  C C   . ILE B 352 ? 0.5422 0.5449 0.4542 0.0930  0.0075  0.0236  653 ILE B C   
6203  O O   . ILE B 352 ? 0.5487 0.5373 0.4461 0.1092  0.0095  0.0226  653 ILE B O   
6204  C CB  . ILE B 352 ? 0.4713 0.5372 0.4060 0.0863  0.0006  0.0257  653 ILE B CB  
6205  C CG1 . ILE B 352 ? 0.4793 0.5561 0.4262 0.0685  0.0006  0.0256  653 ILE B CG1 
6206  C CG2 . ILE B 352 ? 0.4080 0.4893 0.3373 0.1048  0.0025  0.0239  653 ILE B CG2 
6207  C CD1 . ILE B 352 ? 0.4506 0.5693 0.4103 0.0626  -0.0018 0.0261  653 ILE B CD1 
6208  N N   . VAL B 353 ? 0.5623 0.5616 0.4803 0.0801  0.0087  0.0224  654 VAL B N   
6209  C CA  . VAL B 353 ? 0.6441 0.6269 0.5536 0.0832  0.0123  0.0192  654 VAL B CA  
6210  C C   . VAL B 353 ? 0.5440 0.5517 0.4647 0.0760  0.0124  0.0182  654 VAL B C   
6211  O O   . VAL B 353 ? 0.5456 0.5661 0.4787 0.0616  0.0104  0.0203  654 VAL B O   
6212  C CB  . VAL B 353 ? 0.6252 0.5734 0.5274 0.0741  0.0142  0.0187  654 VAL B CB  
6213  C CG1 . VAL B 353 ? 0.5006 0.4535 0.4156 0.0570  0.0122  0.0209  654 VAL B CG1 
6214  C CG2 . VAL B 353 ? 0.7286 0.6623 0.6223 0.0749  0.0173  0.0146  654 VAL B CG2 
6215  N N   . ASP B 354 ? 0.5705 0.5840 0.4852 0.0867  0.0148  0.0149  655 ASP B N   
6216  C CA  . ASP B 354 ? 0.4662 0.5023 0.3895 0.0802  0.0156  0.0140  655 ASP B CA  
6217  C C   . ASP B 354 ? 0.5328 0.5482 0.4545 0.0680  0.0168  0.0127  655 ASP B C   
6218  O O   . ASP B 354 ? 0.5686 0.5534 0.4818 0.0656  0.0175  0.0116  655 ASP B O   
6219  C CB  . ASP B 354 ? 0.5099 0.5619 0.4269 0.0968  0.0180  0.0105  655 ASP B CB  
6220  C CG  . ASP B 354 ? 0.6184 0.6375 0.5167 0.1071  0.0212  0.0055  655 ASP B CG  
6221  O OD1 . ASP B 354 ? 0.6833 0.6904 0.5794 0.0984  0.0226  0.0031  655 ASP B OD1 
6222  O OD2 . ASP B 354 ? 0.7309 0.7353 0.6150 0.1240  0.0222  0.0040  655 ASP B OD2 
6223  N N   . HIS B 355 ? 0.4681 0.5024 0.3979 0.0597  0.0170  0.0131  656 HIS B N   
6224  C CA  . HIS B 355 ? 0.4334 0.4523 0.3625 0.0483  0.0174  0.0124  656 HIS B CA  
6225  C C   . HIS B 355 ? 0.5307 0.5286 0.4456 0.0551  0.0202  0.0065  656 HIS B C   
6226  O O   . HIS B 355 ? 0.6430 0.6209 0.5542 0.0468  0.0203  0.0049  656 HIS B O   
6227  C CB  . HIS B 355 ? 0.4884 0.5313 0.4283 0.0375  0.0167  0.0154  656 HIS B CB  
6228  C CG  . HIS B 355 ? 0.5126 0.5850 0.4546 0.0443  0.0185  0.0148  656 HIS B CG  
6229  N ND1 . HIS B 355 ? 0.5200 0.6186 0.4687 0.0485  0.0177  0.0168  656 HIS B ND1 
6230  C CD2 . HIS B 355 ? 0.4342 0.5172 0.3727 0.0476  0.0210  0.0121  656 HIS B CD2 
6231  C CE1 . HIS B 355 ? 0.4992 0.6247 0.4490 0.0541  0.0200  0.0157  656 HIS B CE1 
6232  N NE2 . HIS B 355 ? 0.5192 0.6348 0.4624 0.0540  0.0221  0.0128  656 HIS B NE2 
6233  N N   . HIS B 356 ? 0.4527 0.4542 0.3582 0.0703  0.0224  0.0027  657 HIS B N   
6234  C CA  . HIS B 356 ? 0.5744 0.5504 0.4628 0.0768  0.0250  -0.0038 657 HIS B CA  
6235  C C   . HIS B 356 ? 0.5271 0.4657 0.4028 0.0776  0.0254  -0.0049 657 HIS B C   
6236  O O   . HIS B 356 ? 0.4946 0.4088 0.3623 0.0692  0.0262  -0.0081 657 HIS B O   
6237  C CB  . HIS B 356 ? 0.5444 0.5314 0.4234 0.0953  0.0275  -0.0079 657 HIS B CB  
6238  C CG  . HIS B 356 ? 0.5677 0.5965 0.4595 0.0954  0.0277  -0.0061 657 HIS B CG  
6239  N ND1 . HIS B 356 ? 0.4942 0.5349 0.3895 0.0869  0.0285  -0.0072 657 HIS B ND1 
6240  C CD2 . HIS B 356 ? 0.5202 0.5834 0.4220 0.1019  0.0273  -0.0029 657 HIS B CD2 
6241  C CE1 . HIS B 356 ? 0.5245 0.6034 0.4308 0.0875  0.0290  -0.0042 657 HIS B CE1 
6242  N NE2 . HIS B 356 ? 0.5328 0.6271 0.4437 0.0960  0.0283  -0.0018 657 HIS B NE2 
6243  N N   . SER B 357 ? 0.6425 0.5774 0.5155 0.0870  0.0250  -0.0023 658 SER B N   
6244  C CA  . SER B 357 ? 0.7186 0.6181 0.5786 0.0873  0.0257  -0.0021 658 SER B CA  
6245  C C   . SER B 357 ? 0.5282 0.4197 0.3969 0.0686  0.0243  0.0005  658 SER B C   
6246  O O   . SER B 357 ? 0.5134 0.3764 0.3713 0.0620  0.0258  -0.0017 658 SER B O   
6247  C CB  . SER B 357 ? 0.7597 0.6622 0.6171 0.1008  0.0248  0.0015  658 SER B CB  
6248  O OG  . SER B 357 ? 0.8912 0.7555 0.7292 0.1059  0.0266  0.0012  658 SER B OG  
6249  N N   . ALA B 358 ? 0.4989 0.4156 0.3860 0.0596  0.0216  0.0049  659 ALA B N   
6250  C CA  . ALA B 358 ? 0.5317 0.4415 0.4260 0.0451  0.0203  0.0075  659 ALA B CA  
6251  C C   . ALA B 358 ? 0.6041 0.5082 0.4984 0.0339  0.0209  0.0044  659 ALA B C   
6252  O O   . ALA B 358 ? 0.5555 0.4429 0.4469 0.0251  0.0214  0.0039  659 ALA B O   
6253  C CB  . ALA B 358 ? 0.4288 0.3634 0.3398 0.0396  0.0172  0.0125  659 ALA B CB  
6254  N N   . THR B 359 ? 0.5833 0.5036 0.4808 0.0339  0.0209  0.0023  660 THR B N   
6255  C CA  . THR B 359 ? 0.5097 0.4270 0.4066 0.0240  0.0209  -0.0008 660 THR B CA  
6256  C C   . THR B 359 ? 0.5278 0.4172 0.4072 0.0248  0.0234  -0.0072 660 THR B C   
6257  O O   . THR B 359 ? 0.5942 0.4731 0.4715 0.0136  0.0234  -0.0094 660 THR B O   
6258  C CB  . THR B 359 ? 0.5294 0.4711 0.4327 0.0239  0.0204  -0.0009 660 THR B CB  
6259  O OG1 . THR B 359 ? 0.6074 0.5541 0.5031 0.0368  0.0223  -0.0040 660 THR B OG1 
6260  C CG2 . THR B 359 ? 0.4176 0.3818 0.3363 0.0186  0.0179  0.0058  660 THR B CG2 
6261  N N   . GLU B 360 ? 0.4694 0.3459 0.3346 0.0379  0.0256  -0.0105 661 GLU B N   
6262  C CA  . GLU B 360 ? 0.5109 0.3535 0.3552 0.0388  0.0281  -0.0165 661 GLU B CA  
6263  C C   . GLU B 360 ? 0.6697 0.4890 0.5096 0.0296  0.0287  -0.0145 661 GLU B C   
6264  O O   . GLU B 360 ? 0.6977 0.4980 0.5287 0.0183  0.0298  -0.0185 661 GLU B O   
6265  C CB  . GLU B 360 ? 0.5843 0.4151 0.4128 0.0576  0.0302  -0.0191 661 GLU B CB  
6266  C CG  . GLU B 360 ? 0.8530 0.6423 0.6556 0.0601  0.0330  -0.0251 661 GLU B CG  
6267  C CD  . GLU B 360 ? 1.1364 0.9126 0.9210 0.0822  0.0351  -0.0275 661 GLU B CD  
6268  O OE1 . GLU B 360 ? 1.1710 0.9675 0.9637 0.0953  0.0343  -0.0228 661 GLU B OE1 
6269  O OE2 . GLU B 360 ? 1.2437 0.9895 1.0052 0.0868  0.0374  -0.0345 661 GLU B OE2 
6270  N N   . SER B 361 ? 0.5674 0.3896 0.4132 0.0336  0.0281  -0.0084 662 SER B N   
6271  C CA  A SER B 361 ? 0.5797 0.3831 0.4220 0.0252  0.0290  -0.0057 662 SER B CA  
6272  C CA  B SER B 361 ? 0.5798 0.3832 0.4221 0.0252  0.0290  -0.0057 662 SER B CA  
6273  C C   . SER B 361 ? 0.5404 0.3543 0.3947 0.0078  0.0279  -0.0056 662 SER B C   
6274  O O   . SER B 361 ? 0.5953 0.3911 0.4419 -0.0029 0.0296  -0.0072 662 SER B O   
6275  C CB  A SER B 361 ? 0.6012 0.4120 0.4498 0.0326  0.0280  0.0008  662 SER B CB  
6276  C CB  B SER B 361 ? 0.6008 0.4121 0.4499 0.0323  0.0279  0.0008  662 SER B CB  
6277  O OG  A SER B 361 ? 0.5091 0.3123 0.3461 0.0501  0.0288  0.0009  662 SER B OG  
6278  O OG  B SER B 361 ? 0.5402 0.3775 0.4095 0.0243  0.0251  0.0047  662 SER B OG  
6279  N N   . PHE B 362 ? 0.4917 0.3352 0.3639 0.0050  0.0250  -0.0036 663 PHE B N   
6280  C CA  . PHE B 362 ? 0.5275 0.3830 0.4108 -0.0085 0.0236  -0.0030 663 PHE B CA  
6281  C C   . PHE B 362 ? 0.6187 0.4667 0.4942 -0.0179 0.0244  -0.0094 663 PHE B C   
6282  O O   . PHE B 362 ? 0.6994 0.5453 0.5759 -0.0300 0.0247  -0.0103 663 PHE B O   
6283  C CB  . PHE B 362 ? 0.4698 0.3541 0.3702 -0.0081 0.0204  0.0009  663 PHE B CB  
6284  C CG  . PHE B 362 ? 0.5634 0.4596 0.4736 -0.0187 0.0187  0.0020  663 PHE B CG  
6285  C CD1 . PHE B 362 ? 0.5677 0.4628 0.4828 -0.0228 0.0186  0.0054  663 PHE B CD1 
6286  C CD2 . PHE B 362 ? 0.6102 0.5190 0.5232 -0.0237 0.0173  -0.0006 663 PHE B CD2 
6287  C CE1 . PHE B 362 ? 0.4642 0.3722 0.3878 -0.0305 0.0172  0.0061  663 PHE B CE1 
6288  C CE2 . PHE B 362 ? 0.6520 0.5735 0.5733 -0.0315 0.0155  0.0005  663 PHE B CE2 
6289  C CZ  . PHE B 362 ? 0.5632 0.4849 0.4899 -0.0344 0.0155  0.0038  663 PHE B CZ  
6290  N N   . ILE B 363 ? 0.6392 0.4853 0.5066 -0.0130 0.0247  -0.0144 664 ILE B N   
6291  C CA  . ILE B 363 ? 0.6261 0.4622 0.4831 -0.0221 0.0253  -0.0217 664 ILE B CA  
6292  C C   . ILE B 363 ? 0.6798 0.4846 0.5210 -0.0301 0.0282  -0.0244 664 ILE B C   
6293  O O   . ILE B 363 ? 0.5931 0.3968 0.4335 -0.0451 0.0282  -0.0274 664 ILE B O   
6294  C CB  . ILE B 363 ? 0.5536 0.3871 0.4002 -0.0129 0.0259  -0.0272 664 ILE B CB  
6295  C CG1 . ILE B 363 ? 0.6937 0.5603 0.5554 -0.0082 0.0235  -0.0244 664 ILE B CG1 
6296  C CG2 . ILE B 363 ? 0.5251 0.3409 0.3561 -0.0225 0.0268  -0.0360 664 ILE B CG2 
6297  C CD1 . ILE B 363 ? 0.6794 0.5664 0.5507 -0.0196 0.0208  -0.0251 664 ILE B CD1 
6298  N N   . LYS B 364 ? 0.5848 0.3647 0.4126 -0.0203 0.0307  -0.0229 665 LYS B N   
6299  C CA  . LYS B 364 ? 0.7037 0.4503 0.5142 -0.0276 0.0339  -0.0238 665 LYS B CA  
6300  C C   . LYS B 364 ? 0.7142 0.4710 0.5367 -0.0407 0.0339  -0.0190 665 LYS B C   
6301  O O   . LYS B 364 ? 0.7627 0.5070 0.5776 -0.0562 0.0357  -0.0217 665 LYS B O   
6302  C CB  . LYS B 364 ? 0.7408 0.4617 0.5355 -0.0116 0.0361  -0.0213 665 LYS B CB  
6303  C CG  . LYS B 364 ? 0.9043 0.5923 0.6827 -0.0177 0.0395  -0.0189 665 LYS B CG  
6304  C CD  . LYS B 364 ? 1.1423 0.7856 0.8895 -0.0149 0.0427  -0.0245 665 LYS B CD  
6305  C CE  . LYS B 364 ? 1.2772 0.9105 1.0158 -0.0326 0.0432  -0.0329 665 LYS B CE  
6306  N NZ  . LYS B 364 ? 1.2778 0.9138 1.0216 -0.0557 0.0441  -0.0319 665 LYS B NZ  
6307  N N   . HIS B 365 ? 0.6573 0.4371 0.4975 -0.0351 0.0320  -0.0124 666 HIS B N   
6308  C CA  . HIS B 365 ? 0.6101 0.4028 0.4621 -0.0456 0.0320  -0.0084 666 HIS B CA  
6309  C C   . HIS B 365 ? 0.7166 0.5279 0.5770 -0.0602 0.0306  -0.0122 666 HIS B C   
6310  O O   . HIS B 365 ? 0.6595 0.4689 0.5183 -0.0739 0.0324  -0.0129 666 HIS B O   
6311  C CB  . HIS B 365 ? 0.5448 0.3598 0.4137 -0.0365 0.0295  -0.0019 666 HIS B CB  
6312  C CG  . HIS B 365 ? 0.5175 0.3479 0.3985 -0.0445 0.0292  0.0017  666 HIS B CG  
6313  N ND1 . HIS B 365 ? 0.5747 0.3917 0.4488 -0.0518 0.0324  0.0035  666 HIS B ND1 
6314  C CD2 . HIS B 365 ? 0.5259 0.3835 0.4241 -0.0454 0.0263  0.0040  666 HIS B CD2 
6315  C CE1 . HIS B 365 ? 0.5122 0.3505 0.4000 -0.0563 0.0316  0.0063  666 HIS B CE1 
6316  N NE2 . HIS B 365 ? 0.5380 0.3996 0.4399 -0.0518 0.0278  0.0065  666 HIS B NE2 
6317  N N   . MET B 366 ? 0.7104 0.5415 0.5791 -0.0574 0.0275  -0.0147 667 MET B N   
6318  C CA  . MET B 366 ? 0.6623 0.5130 0.5378 -0.0693 0.0256  -0.0186 667 MET B CA  
6319  C C   . MET B 366 ? 0.5760 0.4072 0.4359 -0.0839 0.0280  -0.0255 667 MET B C   
6320  O O   . MET B 366 ? 0.6224 0.4652 0.4869 -0.0982 0.0282  -0.0265 667 MET B O   
6321  C CB  . MET B 366 ? 0.6525 0.5208 0.5336 -0.0627 0.0225  -0.0205 667 MET B CB  
6322  C CG  . MET B 366 ? 0.6914 0.5884 0.5910 -0.0574 0.0194  -0.0144 667 MET B CG  
6323  S SD  . MET B 366 ? 0.6995 0.6194 0.6043 -0.0542 0.0159  -0.0163 667 MET B SD  
6324  C CE  . MET B 366 ? 0.7074 0.6407 0.6125 -0.0690 0.0144  -0.0221 667 MET B CE  
6325  N N   . GLU B 367 ? 0.5835 0.3855 0.4238 -0.0809 0.0298  -0.0305 668 GLU B N   
6326  C CA  A GLU B 367 ? 0.7123 0.4887 0.5336 -0.0957 0.0322  -0.0375 668 GLU B CA  
6327  C CA  B GLU B 367 ? 0.7093 0.4865 0.5310 -0.0961 0.0322  -0.0375 668 GLU B CA  
6328  C C   . GLU B 367 ? 0.7431 0.5083 0.5610 -0.1081 0.0355  -0.0341 668 GLU B C   
6329  O O   . GLU B 367 ? 0.6942 0.4640 0.5108 -0.1270 0.0362  -0.0376 668 GLU B O   
6330  C CB  A GLU B 367 ? 0.8090 0.5485 0.6065 -0.0858 0.0343  -0.0420 668 GLU B CB  
6331  C CB  B GLU B 367 ? 0.8088 0.5482 0.6057 -0.0881 0.0343  -0.0427 668 GLU B CB  
6332  C CG  A GLU B 367 ? 0.8676 0.5677 0.6386 -0.0992 0.0375  -0.0487 668 GLU B CG  
6333  C CG  B GLU B 367 ? 0.8459 0.5906 0.6448 -0.0674 0.0329  -0.0418 668 GLU B CG  
6334  C CD  A GLU B 367 ? 0.8920 0.5506 0.6373 -0.0843 0.0401  -0.0511 668 GLU B CD  
6335  C CD  B GLU B 367 ? 0.8170 0.5690 0.6117 -0.0667 0.0310  -0.0497 668 GLU B CD  
6336  O OE1 A GLU B 367 ? 0.8470 0.5135 0.5969 -0.0639 0.0390  -0.0486 668 GLU B OE1 
6337  O OE1 B GLU B 367 ? 0.7168 0.5037 0.5293 -0.0693 0.0276  -0.0492 668 GLU B OE1 
6338  O OE2 A GLU B 367 ? 0.9805 0.5982 0.6996 -0.0930 0.0432  -0.0555 668 GLU B OE2 
6339  O OE2 B GLU B 367 ? 0.6243 0.3458 0.3962 -0.0626 0.0329  -0.0563 668 GLU B OE2 
6340  N N   . ASN B 368 ? 0.8196 0.5726 0.6363 -0.0979 0.0375  -0.0270 669 ASN B N   
6341  C CA  . ASN B 368 ? 0.7411 0.4837 0.5538 -0.1084 0.0411  -0.0228 669 ASN B CA  
6342  C C   . ASN B 368 ? 0.6842 0.4649 0.5178 -0.1204 0.0398  -0.0211 669 ASN B C   
6343  O O   . ASN B 368 ? 0.6783 0.4589 0.5080 -0.1390 0.0421  -0.0231 669 ASN B O   
6344  C CB  . ASN B 368 ? 0.7551 0.4848 0.5655 -0.0930 0.0425  -0.0152 669 ASN B CB  
6345  C CG  . ASN B 368 ? 0.7977 0.4876 0.5841 -0.0811 0.0445  -0.0164 669 ASN B CG  
6346  O OD1 . ASN B 368 ? 0.9267 0.5871 0.6921 -0.0885 0.0465  -0.0224 669 ASN B OD1 
6347  N ND2 . ASN B 368 ? 0.7672 0.4561 0.5555 -0.0623 0.0439  -0.0111 669 ASN B ND2 
6348  N N   . GLU B 369 ? 0.6321 0.4459 0.4871 -0.1101 0.0361  -0.0177 670 GLU B N   
6349  C CA  . GLU B 369 ? 0.6338 0.4829 0.5075 -0.1169 0.0349  -0.0153 670 GLU B CA  
6350  C C   . GLU B 369 ? 0.7296 0.5979 0.6062 -0.1335 0.0337  -0.0217 670 GLU B C   
6351  O O   . GLU B 369 ? 0.7205 0.6053 0.6023 -0.1470 0.0352  -0.0215 670 GLU B O   
6352  C CB  . GLU B 369 ? 0.4703 0.3450 0.3622 -0.1014 0.0309  -0.0108 670 GLU B CB  
6353  C CG  . GLU B 369 ? 0.5667 0.4302 0.4587 -0.0881 0.0318  -0.0044 670 GLU B CG  
6354  C CD  . GLU B 369 ? 0.6193 0.4883 0.5152 -0.0926 0.0344  0.0001  670 GLU B CD  
6355  O OE1 . GLU B 369 ? 0.6085 0.4973 0.5177 -0.0847 0.0326  0.0041  670 GLU B OE1 
6356  O OE2 . GLU B 369 ? 0.5826 0.4352 0.4667 -0.1043 0.0386  -0.0007 670 GLU B OE2 
6357  N N   . TYR B 370 ? 0.7017 0.5712 0.5751 -0.1328 0.0308  -0.0276 671 TYR B N   
6358  C CA  . TYR B 370 ? 0.5714 0.4595 0.4461 -0.1491 0.0292  -0.0345 671 TYR B CA  
6359  C C   . TYR B 370 ? 0.6884 0.5529 0.5460 -0.1695 0.0334  -0.0388 671 TYR B C   
6360  O O   . TYR B 370 ? 0.8300 0.7167 0.6931 -0.1869 0.0337  -0.0412 671 TYR B O   
6361  C CB  . TYR B 370 ? 0.5503 0.4399 0.4214 -0.1441 0.0256  -0.0404 671 TYR B CB  
6362  C CG  . TYR B 370 ? 0.5794 0.5056 0.4699 -0.1324 0.0209  -0.0370 671 TYR B CG  
6363  C CD1 . TYR B 370 ? 0.5657 0.4910 0.4627 -0.1140 0.0199  -0.0306 671 TYR B CD1 
6364  C CD2 . TYR B 370 ? 0.5903 0.5519 0.4918 -0.1401 0.0174  -0.0397 671 TYR B CD2 
6365  C CE1 . TYR B 370 ? 0.5146 0.4685 0.4263 -0.1045 0.0160  -0.0269 671 TYR B CE1 
6366  C CE2 . TYR B 370 ? 0.4983 0.4898 0.4147 -0.1282 0.0133  -0.0357 671 TYR B CE2 
6367  C CZ  . TYR B 370 ? 0.5652 0.5504 0.4858 -0.1109 0.0128  -0.0291 671 TYR B CZ  
6368  O OH  . TYR B 370 ? 0.6359 0.6462 0.5685 -0.1002 0.0089  -0.0246 671 TYR B OH  
6369  N N   . ARG B 371 ? 0.6765 0.4959 0.5122 -0.1675 0.0368  -0.0394 672 ARG B N   
6370  C CA  . ARG B 371 ? 0.7849 0.5723 0.5986 -0.1870 0.0411  -0.0436 672 ARG B CA  
6371  C C   . ARG B 371 ? 0.8102 0.6086 0.6291 -0.2014 0.0448  -0.0387 672 ARG B C   
6372  O O   . ARG B 371 ? 0.8694 0.6652 0.6798 -0.2246 0.0471  -0.0429 672 ARG B O   
6373  C CB  . ARG B 371 ? 0.9568 0.6921 0.7453 -0.1764 0.0440  -0.0433 672 ARG B CB  
6374  C CG  . ARG B 371 ? 1.1291 0.8191 0.8891 -0.1928 0.0491  -0.0460 672 ARG B CG  
6375  C CD  . ARG B 371 ? 1.3359 0.9779 1.0711 -0.1762 0.0505  -0.0470 672 ARG B CD  
6376  N NE  . ARG B 371 ? 1.4885 1.1321 1.2205 -0.1696 0.0469  -0.0555 672 ARG B NE  
6377  C CZ  . ARG B 371 ? 1.5189 1.1457 1.2427 -0.1475 0.0460  -0.0562 672 ARG B CZ  
6378  N NH1 . ARG B 371 ? 1.5420 1.1500 1.2603 -0.1292 0.0480  -0.0491 672 ARG B NH1 
6379  N NH2 . ARG B 371 ? 1.4657 1.0976 1.1869 -0.1435 0.0430  -0.0643 672 ARG B NH2 
6380  N N   . CYS B 372 ? 0.7181 0.5303 0.5506 -0.1888 0.0455  -0.0301 673 CYS B N   
6381  C CA  . CYS B 372 ? 0.8999 0.7200 0.7351 -0.2005 0.0498  -0.0251 673 CYS B CA  
6382  C C   . CYS B 372 ? 0.8729 0.7448 0.7352 -0.1974 0.0477  -0.0215 673 CYS B C   
6383  O O   . CYS B 372 ? 0.9026 0.7916 0.7691 -0.2111 0.0510  -0.0195 673 CYS B O   
6384  C CB  . CYS B 372 ? 0.9249 0.7100 0.7468 -0.1899 0.0538  -0.0178 673 CYS B CB  
6385  S SG  . CYS B 372 ? 1.0778 0.8820 0.9188 -0.1623 0.0506  -0.0103 673 CYS B SG  
6386  N N   . ARG B 373 ? 0.7906 0.6868 0.6697 -0.1799 0.0426  -0.0206 674 ARG B N   
6387  C CA  . ARG B 373 ? 0.6438 0.5842 0.5455 -0.1736 0.0404  -0.0170 674 ARG B CA  
6388  C C   . ARG B 373 ? 0.6646 0.6421 0.5795 -0.1765 0.0355  -0.0221 674 ARG B C   
6389  O O   . ARG B 373 ? 0.5765 0.5930 0.5086 -0.1727 0.0337  -0.0199 674 ARG B O   
6390  C CB  . ARG B 373 ? 0.6386 0.5766 0.5480 -0.1501 0.0385  -0.0107 674 ARG B CB  
6391  C CG  . ARG B 373 ? 0.5688 0.5384 0.4949 -0.1423 0.0380  -0.0056 674 ARG B CG  
6392  C CD  . ARG B 373 ? 0.5985 0.5600 0.5288 -0.1211 0.0358  -0.0005 674 ARG B CD  
6393  N NE  . ARG B 373 ? 0.5652 0.5514 0.5081 -0.1131 0.0356  0.0038  674 ARG B NE  
6394  C CZ  . ARG B 373 ? 0.6068 0.5968 0.5566 -0.0962 0.0325  0.0073  674 ARG B CZ  
6395  N NH1 . ARG B 373 ? 0.5473 0.5215 0.4945 -0.0863 0.0294  0.0076  674 ARG B NH1 
6396  N NH2 . ARG B 373 ? 0.5821 0.5922 0.5406 -0.0895 0.0327  0.0103  674 ARG B NH2 
6397  N N   . GLY B 374 ? 0.7062 0.6726 0.6122 -0.1819 0.0332  -0.0287 675 GLY B N   
6398  C CA  . GLY B 374 ? 0.7254 0.7261 0.6422 -0.1835 0.0281  -0.0335 675 GLY B CA  
6399  C C   . GLY B 374 ? 0.6883 0.7016 0.6157 -0.1620 0.0233  -0.0304 675 GLY B C   
6400  O O   . GLY B 374 ? 0.6191 0.6684 0.5591 -0.1594 0.0191  -0.0313 675 GLY B O   
6401  N N   . GLY B 375 ? 0.6128 0.5983 0.5348 -0.1468 0.0238  -0.0264 676 GLY B N   
6402  C CA  . GLY B 375 ? 0.5952 0.5914 0.5267 -0.1280 0.0198  -0.0224 676 GLY B CA  
6403  C C   . GLY B 375 ? 0.6904 0.6689 0.6225 -0.1131 0.0211  -0.0155 676 GLY B C   
6404  O O   . GLY B 375 ? 0.7130 0.6750 0.6403 -0.1151 0.0249  -0.0129 676 GLY B O   
6405  N N   . CYS B 376 ? 0.6554 0.6379 0.5928 -0.0985 0.0179  -0.0124 677 CYS B N   
6406  C CA  . CYS B 376 ? 0.5211 0.4902 0.4596 -0.0848 0.0182  -0.0064 677 CYS B CA  
6407  C C   . CYS B 376 ? 0.5080 0.4941 0.4559 -0.0731 0.0140  -0.0028 677 CYS B C   
6408  O O   . CYS B 376 ? 0.5794 0.5666 0.5250 -0.0707 0.0119  -0.0047 677 CYS B O   
6409  C CB  . CYS B 376 ? 0.4606 0.3980 0.3858 -0.0817 0.0203  -0.0078 677 CYS B CB  
6410  S SG  . CYS B 376 ? 0.5185 0.4463 0.4462 -0.0653 0.0196  -0.0013 677 CYS B SG  
6411  N N   . PRO B 377 ? 0.4025 0.4005 0.3592 -0.0655 0.0129  0.0024  678 PRO B N   
6412  C CA  . PRO B 377 ? 0.3799 0.3894 0.3423 -0.0549 0.0091  0.0063  678 PRO B CA  
6413  C C   . PRO B 377 ? 0.4610 0.4525 0.4195 -0.0474 0.0088  0.0090  678 PRO B C   
6414  O O   . PRO B 377 ? 0.3755 0.3501 0.3308 -0.0453 0.0108  0.0105  678 PRO B O   
6415  C CB  . PRO B 377 ? 0.5067 0.5281 0.4761 -0.0491 0.0086  0.0103  678 PRO B CB  
6416  C CG  . PRO B 377 ? 0.4247 0.4320 0.3913 -0.0531 0.0126  0.0103  678 PRO B CG  
6417  C CD  . PRO B 377 ? 0.5021 0.5011 0.4618 -0.0658 0.0153  0.0050  678 PRO B CD  
6418  N N   . ALA B 378 ? 0.5195 0.5169 0.4779 -0.0437 0.0062  0.0099  679 ALA B N   
6419  C CA  . ALA B 378 ? 0.4635 0.4483 0.4184 -0.0384 0.0063  0.0120  679 ALA B CA  
6420  C C   . ALA B 378 ? 0.4995 0.4951 0.4563 -0.0336 0.0033  0.0157  679 ALA B C   
6421  O O   . ALA B 378 ? 0.4558 0.4651 0.4126 -0.0354 0.0015  0.0141  679 ALA B O   
6422  C CB  . ALA B 378 ? 0.3660 0.3379 0.3126 -0.0419 0.0087  0.0067  679 ALA B CB  
6423  N N   . ASP B 379 ? 0.4665 0.4555 0.4236 -0.0283 0.0027  0.0207  680 ASP B N   
6424  C CA  . ASP B 379 ? 0.4852 0.4800 0.4423 -0.0245 0.0003  0.0259  680 ASP B CA  
6425  C C   . ASP B 379 ? 0.5039 0.4973 0.4576 -0.0249 0.0013  0.0256  680 ASP B C   
6426  O O   . ASP B 379 ? 0.4239 0.4097 0.3774 -0.0237 0.0024  0.0270  680 ASP B O   
6427  C CB  . ASP B 379 ? 0.4572 0.4445 0.4153 -0.0204 -0.0009 0.0312  680 ASP B CB  
6428  C CG  . ASP B 379 ? 0.5914 0.5795 0.5463 -0.0174 -0.0033 0.0373  680 ASP B CG  
6429  O OD1 . ASP B 379 ? 0.6536 0.6461 0.6060 -0.0189 -0.0033 0.0386  680 ASP B OD1 
6430  O OD2 . ASP B 379 ? 0.6141 0.5966 0.5674 -0.0132 -0.0049 0.0410  680 ASP B OD2 
6431  N N   . TRP B 380 ? 0.4790 0.4826 0.4301 -0.0262 0.0008  0.0237  681 TRP B N   
6432  C CA  . TRP B 380 ? 0.4381 0.4434 0.3855 -0.0258 0.0022  0.0226  681 TRP B CA  
6433  C C   . TRP B 380 ? 0.4183 0.4232 0.3664 -0.0240 0.0021  0.0291  681 TRP B C   
6434  O O   . TRP B 380 ? 0.3852 0.3891 0.3327 -0.0230 0.0040  0.0283  681 TRP B O   
6435  C CB  . TRP B 380 ? 0.4173 0.4354 0.3610 -0.0270 0.0011  0.0204  681 TRP B CB  
6436  C CG  . TRP B 380 ? 0.4955 0.5161 0.4338 -0.0264 0.0031  0.0165  681 TRP B CG  
6437  C CD1 . TRP B 380 ? 0.4809 0.4974 0.4135 -0.0277 0.0047  0.0083  681 TRP B CD1 
6438  C CD2 . TRP B 380 ? 0.4995 0.5275 0.4361 -0.0241 0.0040  0.0206  681 TRP B CD2 
6439  N NE1 . TRP B 380 ? 0.4952 0.5161 0.4226 -0.0245 0.0064  0.0066  681 TRP B NE1 
6440  C CE2 . TRP B 380 ? 0.5214 0.5516 0.4521 -0.0225 0.0062  0.0143  681 TRP B CE2 
6441  C CE3 . TRP B 380 ? 0.5102 0.5424 0.4485 -0.0239 0.0034  0.0290  681 TRP B CE3 
6442  C CZ2 . TRP B 380 ? 0.5851 0.6259 0.5133 -0.0198 0.0080  0.0161  681 TRP B CZ2 
6443  C CZ3 . TRP B 380 ? 0.4829 0.5250 0.4187 -0.0235 0.0052  0.0313  681 TRP B CZ3 
6444  C CH2 . TRP B 380 ? 0.4996 0.5478 0.4311 -0.0210 0.0076  0.0248  681 TRP B CH2 
6445  N N   . VAL B 381 ? 0.5022 0.5075 0.4505 -0.0235 -0.0001 0.0355  682 VAL B N   
6446  C CA  . VAL B 381 ? 0.4783 0.4815 0.4252 -0.0246 -0.0003 0.0419  682 VAL B CA  
6447  C C   . VAL B 381 ? 0.5113 0.5067 0.4612 -0.0254 0.0008  0.0417  682 VAL B C   
6448  O O   . VAL B 381 ? 0.4873 0.4863 0.4369 -0.0278 0.0016  0.0444  682 VAL B O   
6449  C CB  . VAL B 381 ? 0.3980 0.3964 0.3413 -0.0234 -0.0029 0.0485  682 VAL B CB  
6450  C CG1 . VAL B 381 ? 0.4639 0.4546 0.4037 -0.0268 -0.0029 0.0549  682 VAL B CG1 
6451  C CG2 . VAL B 381 ? 0.4126 0.4220 0.3518 -0.0217 -0.0042 0.0499  682 VAL B CG2 
6452  N N   . TRP B 382 ? 0.4942 0.4810 0.4466 -0.0237 0.0008  0.0385  683 TRP B N   
6453  C CA  . TRP B 382 ? 0.4979 0.4775 0.4523 -0.0236 0.0014  0.0382  683 TRP B CA  
6454  C C   . TRP B 382 ? 0.5266 0.5067 0.4814 -0.0213 0.0038  0.0329  683 TRP B C   
6455  O O   . TRP B 382 ? 0.5377 0.5173 0.4935 -0.0201 0.0043  0.0330  683 TRP B O   
6456  C CB  . TRP B 382 ? 0.3742 0.3430 0.3293 -0.0222 0.0001  0.0387  683 TRP B CB  
6457  C CG  . TRP B 382 ? 0.5383 0.5003 0.4904 -0.0229 -0.0022 0.0441  683 TRP B CG  
6458  C CD1 . TRP B 382 ? 0.6197 0.5819 0.5677 -0.0222 -0.0038 0.0481  683 TRP B CD1 
6459  C CD2 . TRP B 382 ? 0.6011 0.5524 0.5515 -0.0240 -0.0034 0.0459  683 TRP B CD2 
6460  N NE1 . TRP B 382 ? 0.6312 0.5803 0.5736 -0.0226 -0.0056 0.0525  683 TRP B NE1 
6461  C CE2 . TRP B 382 ? 0.6193 0.5616 0.5633 -0.0244 -0.0055 0.0508  683 TRP B CE2 
6462  C CE3 . TRP B 382 ? 0.6081 0.5559 0.5603 -0.0245 -0.0030 0.0437  683 TRP B CE3 
6463  C CZ2 . TRP B 382 ? 0.6672 0.5950 0.6059 -0.0264 -0.0071 0.0529  683 TRP B CZ2 
6464  C CZ3 . TRP B 382 ? 0.6496 0.5868 0.5982 -0.0266 -0.0050 0.0457  683 TRP B CZ3 
6465  C CH2 . TRP B 382 ? 0.6016 0.5279 0.5432 -0.0281 -0.0069 0.0499  683 TRP B CH2 
6466  N N   . ILE B 383 ? 0.4810 0.4613 0.4336 -0.0205 0.0051  0.0281  684 ILE B N   
6467  C CA  . ILE B 383 ? 0.4369 0.4117 0.3861 -0.0175 0.0075  0.0229  684 ILE B CA  
6468  C C   . ILE B 383 ? 0.4884 0.4724 0.4354 -0.0142 0.0089  0.0219  684 ILE B C   
6469  O O   . ILE B 383 ? 0.5192 0.5009 0.4641 -0.0091 0.0104  0.0201  684 ILE B O   
6470  C CB  . ILE B 383 ? 0.3974 0.3661 0.3427 -0.0197 0.0084  0.0177  684 ILE B CB  
6471  C CG1 . ILE B 383 ? 0.4493 0.4119 0.3974 -0.0225 0.0079  0.0184  684 ILE B CG1 
6472  C CG2 . ILE B 383 ? 0.4778 0.4366 0.4153 -0.0166 0.0111  0.0122  684 ILE B CG2 
6473  C CD1 . ILE B 383 ? 0.4927 0.4432 0.4397 -0.0202 0.0092  0.0187  684 ILE B CD1 
6474  N N   . VAL B 384 ? 0.5415 0.5375 0.4882 -0.0160 0.0086  0.0232  685 VAL B N   
6475  C CA  . VAL B 384 ? 0.3968 0.4050 0.3413 -0.0125 0.0104  0.0221  685 VAL B CA  
6476  C C   . VAL B 384 ? 0.4253 0.4428 0.3747 -0.0125 0.0103  0.0267  685 VAL B C   
6477  O O   . VAL B 384 ? 0.4876 0.5070 0.4406 -0.0183 0.0084  0.0325  685 VAL B O   
6478  C CB  . VAL B 384 ? 0.4579 0.4781 0.4004 -0.0151 0.0102  0.0231  685 VAL B CB  
6479  C CG1 . VAL B 384 ? 0.3604 0.3968 0.3016 -0.0119 0.0124  0.0232  685 VAL B CG1 
6480  C CG2 . VAL B 384 ? 0.3638 0.3786 0.3007 -0.0153 0.0102  0.0170  685 VAL B CG2 
6481  N N   . PRO B 385 ? 0.4281 0.4523 0.3768 -0.0062 0.0121  0.0244  686 PRO B N   
6482  C CA  . PRO B 385 ? 0.4284 0.4654 0.3827 -0.0071 0.0116  0.0282  686 PRO B CA  
6483  C C   . PRO B 385 ? 0.5019 0.5572 0.4591 -0.0142 0.0116  0.0334  686 PRO B C   
6484  O O   . PRO B 385 ? 0.5503 0.6109 0.5044 -0.0154 0.0127  0.0335  686 PRO B O   
6485  C CB  . PRO B 385 ? 0.3726 0.4160 0.3241 0.0038  0.0137  0.0238  686 PRO B CB  
6486  C CG  . PRO B 385 ? 0.4125 0.4368 0.3552 0.0098  0.0151  0.0179  686 PRO B CG  
6487  C CD  . PRO B 385 ? 0.3810 0.4006 0.3224 0.0027  0.0145  0.0178  686 PRO B CD  
6488  N N   . PRO B 386 ? 0.5150 0.5797 0.4771 -0.0202 0.0105  0.0378  687 PRO B N   
6489  C CA  . PRO B 386 ? 0.4863 0.5659 0.4496 -0.0298 0.0108  0.0436  687 PRO B CA  
6490  C C   . PRO B 386 ? 0.4988 0.6072 0.4643 -0.0280 0.0137  0.0434  687 PRO B C   
6491  O O   . PRO B 386 ? 0.4757 0.5987 0.4421 -0.0376 0.0145  0.0487  687 PRO B O   
6492  C CB  . PRO B 386 ? 0.5223 0.5957 0.4881 -0.0384 0.0082  0.0475  687 PRO B CB  
6493  C CG  . PRO B 386 ? 0.4545 0.5274 0.4234 -0.0306 0.0076  0.0429  687 PRO B CG  
6494  C CD  . PRO B 386 ? 0.4383 0.4957 0.4033 -0.0207 0.0085  0.0380  687 PRO B CD  
6495  N N   . MET B 387 ? 0.5247 0.6418 0.4900 -0.0158 0.0156  0.0375  688 MET B N   
6496  C CA  . MET B 387 ? 0.4702 0.6143 0.4355 -0.0106 0.0189  0.0361  688 MET B CA  
6497  C C   . MET B 387 ? 0.5116 0.6461 0.4690 0.0027  0.0208  0.0289  688 MET B C   
6498  O O   . MET B 387 ? 0.4934 0.6035 0.4465 0.0083  0.0197  0.0248  688 MET B O   
6499  C CB  . MET B 387 ? 0.4157 0.5874 0.3874 -0.0074 0.0196  0.0360  688 MET B CB  
6500  C CG  . MET B 387 ? 0.4942 0.6591 0.4650 0.0066  0.0189  0.0307  688 MET B CG  
6501  S SD  . MET B 387 ? 0.6047 0.8076 0.5836 0.0115  0.0189  0.0308  688 MET B SD  
6502  C CE  . MET B 387 ? 0.6837 0.9185 0.6605 0.0234  0.0238  0.0277  688 MET B CE  
6503  N N   . SER B 388 ? 0.5133 0.6663 0.4676 0.0064  0.0239  0.0274  689 SER B N   
6504  C CA  . SER B 388 ? 0.3735 0.5202 0.3183 0.0198  0.0261  0.0196  689 SER B CA  
6505  C C   . SER B 388 ? 0.4154 0.5302 0.3530 0.0187  0.0244  0.0159  689 SER B C   
6506  O O   . SER B 388 ? 0.5341 0.6311 0.4630 0.0281  0.0251  0.0089  689 SER B O   
6507  C CB  . SER B 388 ? 0.5625 0.7133 0.5055 0.0347  0.0272  0.0148  689 SER B CB  
6508  O OG  . SER B 388 ? 0.5681 0.7528 0.5198 0.0347  0.0282  0.0183  689 SER B OG  
6509  N N   . GLY B 389 ? 0.3820 0.4898 0.3219 0.0069  0.0222  0.0207  690 GLY B N   
6510  C CA  . GLY B 389 ? 0.4548 0.5370 0.3904 0.0046  0.0201  0.0179  690 GLY B CA  
6511  C C   . GLY B 389 ? 0.4915 0.5645 0.4163 0.0115  0.0216  0.0095  690 GLY B C   
6512  O O   . GLY B 389 ? 0.4923 0.5430 0.4114 0.0145  0.0212  0.0041  690 GLY B O   
6513  N N   . SER B 390 ? 0.4302 0.5192 0.3504 0.0134  0.0235  0.0080  691 SER B N   
6514  C CA  . SER B 390 ? 0.4030 0.4813 0.3114 0.0179  0.0242  -0.0006 691 SER B CA  
6515  C C   . SER B 390 ? 0.4985 0.5672 0.3969 0.0312  0.0269  -0.0087 691 SER B C   
6516  O O   . SER B 390 ? 0.5217 0.5734 0.4076 0.0343  0.0273  -0.0169 691 SER B O   
6517  C CB  . SER B 390 ? 0.4843 0.5818 0.3893 0.0158  0.0252  0.0002  691 SER B CB  
6518  O OG  . SER B 390 ? 0.4651 0.5840 0.3682 0.0241  0.0289  -0.0008 691 SER B OG  
6519  N N   . ILE B 391 ? 0.5584 0.6361 0.4606 0.0393  0.0284  -0.0070 692 ILE B N   
6520  C CA  . ILE B 391 ? 0.6613 0.7247 0.5518 0.0540  0.0305  -0.0144 692 ILE B CA  
6521  C C   . ILE B 391 ? 0.6725 0.7074 0.5614 0.0535  0.0288  -0.0146 692 ILE B C   
6522  O O   . ILE B 391 ? 0.6613 0.6812 0.5402 0.0659  0.0303  -0.0188 692 ILE B O   
6523  C CB  . ILE B 391 ? 0.7029 0.7932 0.5956 0.0669  0.0332  -0.0137 692 ILE B CB  
6524  C CG1 . ILE B 391 ? 0.6619 0.7698 0.5701 0.0621  0.0318  -0.0054 692 ILE B CG1 
6525  C CG2 . ILE B 391 ? 0.6624 0.7809 0.5538 0.0689  0.0359  -0.0146 692 ILE B CG2 
6526  C CD1 . ILE B 391 ? 0.6487 0.7806 0.5587 0.0760  0.0338  -0.0057 692 ILE B CD1 
6527  N N   . THR B 392 ? 0.6805 0.7071 0.5779 0.0403  0.0259  -0.0099 693 THR B N   
6528  C CA  . THR B 392 ? 0.6331 0.6314 0.5266 0.0390  0.0249  -0.0111 693 THR B CA  
6529  C C   . THR B 392 ? 0.5900 0.5677 0.4760 0.0302  0.0240  -0.0159 693 THR B C   
6530  O O   . THR B 392 ? 0.5530 0.5421 0.4419 0.0227  0.0229  -0.0158 693 THR B O   
6531  C CB  . THR B 392 ? 0.6416 0.6437 0.5486 0.0320  0.0225  -0.0035 693 THR B CB  
6532  O OG1 . THR B 392 ? 0.6678 0.6778 0.5838 0.0193  0.0202  0.0010  693 THR B OG1 
6533  C CG2 . THR B 392 ? 0.5019 0.5271 0.4170 0.0382  0.0228  0.0010  693 THR B CG2 
6534  N N   . PRO B 393 ? 0.6221 0.5705 0.4976 0.0302  0.0245  -0.0201 694 PRO B N   
6535  C CA  . PRO B 393 ? 0.5889 0.5204 0.4562 0.0203  0.0239  -0.0258 694 PRO B CA  
6536  C C   . PRO B 393 ? 0.6436 0.5844 0.5237 0.0064  0.0209  -0.0213 694 PRO B C   
6537  O O   . PRO B 393 ? 0.6858 0.6248 0.5623 -0.0020 0.0198  -0.0255 694 PRO B O   
6538  C CB  . PRO B 393 ? 0.6170 0.5140 0.4694 0.0228  0.0256  -0.0300 694 PRO B CB  
6539  C CG  . PRO B 393 ? 0.6091 0.5077 0.4674 0.0313  0.0260  -0.0238 694 PRO B CG  
6540  C CD  . PRO B 393 ? 0.5664 0.4955 0.4338 0.0401  0.0261  -0.0207 694 PRO B CD  
6541  N N   . VAL B 394 ? 0.6689 0.6197 0.5627 0.0043  0.0195  -0.0134 695 VAL B N   
6542  C CA  . VAL B 394 ? 0.5961 0.5532 0.4997 -0.0065 0.0168  -0.0097 695 VAL B CA  
6543  C C   . VAL B 394 ? 0.4510 0.4303 0.3602 -0.0096 0.0150  -0.0072 695 VAL B C   
6544  O O   . VAL B 394 ? 0.4436 0.4282 0.3565 -0.0171 0.0127  -0.0063 695 VAL B O   
6545  C CB  . VAL B 394 ? 0.5423 0.5000 0.4563 -0.0073 0.0157  -0.0026 695 VAL B CB  
6546  C CG1 . VAL B 394 ? 0.5479 0.4832 0.4556 -0.0061 0.0173  -0.0046 695 VAL B CG1 
6547  C CG2 . VAL B 394 ? 0.4623 0.4357 0.3831 -0.0015 0.0157  0.0027  695 VAL B CG2 
6548  N N   . PHE B 395 ? 0.4210 0.4153 0.3307 -0.0037 0.0160  -0.0054 696 PHE B N   
6549  C CA  . PHE B 395 ? 0.5131 0.5272 0.4253 -0.0066 0.0149  -0.0028 696 PHE B CA  
6550  C C   . PHE B 395 ? 0.4375 0.4497 0.3420 -0.0109 0.0138  -0.0093 696 PHE B C   
6551  O O   . PHE B 395 ? 0.3991 0.4226 0.3072 -0.0164 0.0113  -0.0064 696 PHE B O   
6552  C CB  . PHE B 395 ? 0.4785 0.5090 0.3895 0.0003  0.0172  -0.0017 696 PHE B CB  
6553  C CG  . PHE B 395 ? 0.4612 0.5117 0.3729 -0.0028 0.0167  0.0019  696 PHE B CG  
6554  C CD1 . PHE B 395 ? 0.4529 0.5070 0.3554 -0.0019 0.0170  -0.0043 696 PHE B CD1 
6555  C CD2 . PHE B 395 ? 0.4185 0.4827 0.3384 -0.0069 0.0159  0.0114  696 PHE B CD2 
6556  C CE1 . PHE B 395 ? 0.5404 0.6136 0.4423 -0.0043 0.0166  -0.0005 696 PHE B CE1 
6557  C CE2 . PHE B 395 ? 0.5264 0.6066 0.4448 -0.0098 0.0157  0.0157  696 PHE B CE2 
6558  C CZ  . PHE B 395 ? 0.5239 0.6098 0.4336 -0.0080 0.0161  0.0099  696 PHE B CZ  
6559  N N   . HIS B 396 ? 0.4488 0.4457 0.3413 -0.0085 0.0156  -0.0183 697 HIS B N   
6560  C CA  . HIS B 396 ? 0.5004 0.4942 0.3830 -0.0133 0.0147  -0.0264 697 HIS B CA  
6561  C C   . HIS B 396 ? 0.5114 0.4923 0.3936 -0.0236 0.0129  -0.0296 697 HIS B C   
6562  O O   . HIS B 396 ? 0.5805 0.5559 0.4530 -0.0295 0.0122  -0.0377 697 HIS B O   
6563  C CB  . HIS B 396 ? 0.4899 0.4710 0.3567 -0.0054 0.0177  -0.0352 697 HIS B CB  
6564  C CG  . HIS B 396 ? 0.5760 0.5733 0.4438 0.0056  0.0200  -0.0323 697 HIS B CG  
6565  N ND1 . HIS B 396 ? 0.6224 0.6417 0.4894 0.0069  0.0201  -0.0319 697 HIS B ND1 
6566  C CD2 . HIS B 396 ? 0.6016 0.5997 0.4717 0.0154  0.0224  -0.0292 697 HIS B CD2 
6567  C CE1 . HIS B 396 ? 0.6359 0.6692 0.5050 0.0162  0.0228  -0.0287 697 HIS B CE1 
6568  N NE2 . HIS B 396 ? 0.6158 0.6379 0.4873 0.0216  0.0241  -0.0272 697 HIS B NE2 
6569  N N   . GLN B 397 ? 0.5382 0.5163 0.4304 -0.0266 0.0121  -0.0237 698 GLN B N   
6570  C CA  . GLN B 397 ? 0.5213 0.4900 0.4143 -0.0362 0.0111  -0.0260 698 GLN B CA  
6571  C C   . GLN B 397 ? 0.4921 0.4815 0.3978 -0.0412 0.0077  -0.0202 698 GLN B C   
6572  O O   . GLN B 397 ? 0.5623 0.5576 0.4779 -0.0375 0.0071  -0.0121 698 GLN B O   
6573  C CB  . GLN B 397 ? 0.5807 0.5292 0.4732 -0.0343 0.0134  -0.0241 698 GLN B CB  
6574  C CG  . GLN B 397 ? 0.5666 0.5073 0.4607 -0.0447 0.0131  -0.0251 698 GLN B CG  
6575  C CD  . GLN B 397 ? 0.4878 0.4114 0.3673 -0.0532 0.0143  -0.0346 698 GLN B CD  
6576  O OE1 . GLN B 397 ? 0.4789 0.3780 0.3436 -0.0491 0.0171  -0.0392 698 GLN B OE1 
6577  N NE2 . GLN B 397 ? 0.4684 0.4045 0.3504 -0.0650 0.0121  -0.0379 698 GLN B NE2 
6578  N N   . GLU B 398 ? 0.4181 0.4179 0.3223 -0.0491 0.0054  -0.0247 699 GLU B N   
6579  C CA  . GLU B 398 ? 0.4055 0.4248 0.3205 -0.0526 0.0021  -0.0200 699 GLU B CA  
6580  C C   . GLU B 398 ? 0.6091 0.6207 0.5309 -0.0553 0.0030  -0.0170 699 GLU B C   
6581  O O   . GLU B 398 ? 0.4103 0.4035 0.3264 -0.0604 0.0055  -0.0215 699 GLU B O   
6582  C CB  . GLU B 398 ? 0.4719 0.5056 0.3834 -0.0611 -0.0006 -0.0268 699 GLU B CB  
6583  C CG  . GLU B 398 ? 0.5111 0.5574 0.4165 -0.0575 -0.0021 -0.0287 699 GLU B CG  
6584  C CD  . GLU B 398 ? 0.6201 0.6843 0.5224 -0.0658 -0.0056 -0.0353 699 GLU B CD  
6585  O OE1 . GLU B 398 ? 0.5149 0.5944 0.4133 -0.0626 -0.0077 -0.0356 699 GLU B OE1 
6586  O OE2 . GLU B 398 ? 0.6394 0.7041 0.5430 -0.0762 -0.0063 -0.0402 699 GLU B OE2 
6587  N N   . MET B 399 ? 0.4903 0.5144 0.4225 -0.0516 0.0011  -0.0093 700 MET B N   
6588  C CA  . MET B 399 ? 0.4974 0.5168 0.4360 -0.0528 0.0019  -0.0064 700 MET B CA  
6589  C C   . MET B 399 ? 0.5624 0.6038 0.5094 -0.0526 -0.0012 -0.0030 700 MET B C   
6590  O O   . MET B 399 ? 0.7244 0.7801 0.6733 -0.0470 -0.0041 0.0012  700 MET B O   
6591  C CB  . MET B 399 ? 0.4561 0.4626 0.3971 -0.0450 0.0034  -0.0001 700 MET B CB  
6592  C CG  . MET B 399 ? 0.4646 0.4505 0.3980 -0.0435 0.0067  -0.0031 700 MET B CG  
6593  S SD  . MET B 399 ? 0.4522 0.4338 0.3891 -0.0339 0.0073  0.0041  700 MET B SD  
6594  C CE  . MET B 399 ? 0.3844 0.3533 0.3105 -0.0300 0.0102  -0.0013 700 MET B CE  
6595  N N   . LEU B 400 ? 0.4339 0.4786 0.3849 -0.0582 -0.0005 -0.0045 701 LEU B N   
6596  C CA  . LEU B 400 ? 0.4389 0.5057 0.3984 -0.0559 -0.0029 -0.0013 701 LEU B CA  
6597  C C   . LEU B 400 ? 0.5125 0.5706 0.4766 -0.0489 -0.0018 0.0049  701 LEU B C   
6598  O O   . LEU B 400 ? 0.4819 0.5235 0.4447 -0.0521 0.0015  0.0039  701 LEU B O   
6599  C CB  . LEU B 400 ? 0.4134 0.4957 0.3751 -0.0676 -0.0028 -0.0075 701 LEU B CB  
6600  C CG  . LEU B 400 ? 0.5072 0.6039 0.4648 -0.0762 -0.0049 -0.0146 701 LEU B CG  
6601  C CD1 . LEU B 400 ? 0.5510 0.6644 0.5116 -0.0901 -0.0045 -0.0205 701 LEU B CD1 
6602  C CD2 . LEU B 400 ? 0.4750 0.5933 0.4350 -0.0670 -0.0094 -0.0109 701 LEU B CD2 
6603  N N   . ASN B 401 ? 0.5537 0.6207 0.5212 -0.0389 -0.0044 0.0111  702 ASN B N   
6604  C CA  . ASN B 401 ? 0.5058 0.5635 0.4758 -0.0317 -0.0037 0.0164  702 ASN B CA  
6605  C C   . ASN B 401 ? 0.5403 0.6183 0.5161 -0.0282 -0.0049 0.0171  702 ASN B C   
6606  O O   . ASN B 401 ? 0.4292 0.5283 0.4065 -0.0242 -0.0080 0.0178  702 ASN B O   
6607  C CB  . ASN B 401 ? 0.5266 0.5734 0.4931 -0.0227 -0.0053 0.0231  702 ASN B CB  
6608  C CG  . ASN B 401 ? 0.5142 0.5433 0.4806 -0.0187 -0.0039 0.0265  702 ASN B CG  
6609  O OD1 . ASN B 401 ? 0.5172 0.5407 0.4855 -0.0224 -0.0014 0.0238  702 ASN B OD1 
6610  N ND2 . ASN B 401 ? 0.4780 0.4976 0.4408 -0.0121 -0.0055 0.0323  702 ASN B ND2 
6611  N N   . TYR B 402 ? 0.5523 0.6255 0.5308 -0.0286 -0.0023 0.0171  703 TYR B N   
6612  C CA  . TYR B 402 ? 0.3431 0.4364 0.3271 -0.0239 -0.0027 0.0178  703 TYR B CA  
6613  C C   . TYR B 402 ? 0.4258 0.5048 0.4099 -0.0215 0.0003  0.0193  703 TYR B C   
6614  O O   . TYR B 402 ? 0.3966 0.4539 0.3773 -0.0266 0.0028  0.0187  703 TYR B O   
6615  C CB  . TYR B 402 ? 0.3444 0.4649 0.3338 -0.0344 -0.0023 0.0121  703 TYR B CB  
6616  C CG  . TYR B 402 ? 0.5456 0.6550 0.5323 -0.0506 0.0012  0.0064  703 TYR B CG  
6617  C CD1 . TYR B 402 ? 0.4762 0.5801 0.4579 -0.0584 0.0004  0.0023  703 TYR B CD1 
6618  C CD2 . TYR B 402 ? 0.4258 0.5288 0.4130 -0.0578 0.0055  0.0051  703 TYR B CD2 
6619  C CE1 . TYR B 402 ? 0.4521 0.5412 0.4280 -0.0721 0.0036  -0.0032 703 TYR B CE1 
6620  C CE2 . TYR B 402 ? 0.4037 0.4918 0.3851 -0.0722 0.0088  0.0006  703 TYR B CE2 
6621  C CZ  . TYR B 402 ? 0.5040 0.5840 0.4793 -0.0791 0.0077  -0.0038 703 TYR B CZ  
6622  O OH  . TYR B 402 ? 0.5133 0.5739 0.4796 -0.0925 0.0111  -0.0086 703 TYR B OH  
6623  N N   . ARG B 403 ? 0.4613 0.5534 0.4483 -0.0124 -0.0002 0.0213  704 ARG B N   
6624  C CA  . ARG B 403 ? 0.5362 0.6142 0.5214 -0.0063 0.0018  0.0235  704 ARG B CA  
6625  C C   . ARG B 403 ? 0.5613 0.6553 0.5517 -0.0124 0.0055  0.0205  704 ARG B C   
6626  O O   . ARG B 403 ? 0.5566 0.6788 0.5524 -0.0085 0.0052  0.0197  704 ARG B O   
6627  C CB  . ARG B 403 ? 0.5637 0.6400 0.5450 0.0100  -0.0012 0.0278  704 ARG B CB  
6628  C CG  . ARG B 403 ? 0.5585 0.6188 0.5332 0.0143  -0.0046 0.0317  704 ARG B CG  
6629  C CD  . ARG B 403 ? 0.6840 0.7179 0.6505 0.0223  -0.0053 0.0354  704 ARG B CD  
6630  N NE  . ARG B 403 ? 0.7414 0.7782 0.7024 0.0375  -0.0076 0.0384  704 ARG B NE  
6631  C CZ  . ARG B 403 ? 0.7143 0.7376 0.6696 0.0463  -0.0072 0.0392  704 ARG B CZ  
6632  N NH1 . ARG B 403 ? 0.6576 0.6664 0.6130 0.0405  -0.0047 0.0373  704 ARG B NH1 
6633  N NH2 . ARG B 403 ? 0.8036 0.8274 0.7515 0.0618  -0.0093 0.0417  704 ARG B NH2 
6634  N N   . LEU B 404 ? 0.5347 0.6118 0.5228 -0.0216 0.0092  0.0191  705 LEU B N   
6635  C CA  . LEU B 404 ? 0.4959 0.5827 0.4864 -0.0291 0.0136  0.0173  705 LEU B CA  
6636  C C   . LEU B 404 ? 0.5405 0.6153 0.5280 -0.0203 0.0153  0.0198  705 LEU B C   
6637  O O   . LEU B 404 ? 0.6161 0.6677 0.5983 -0.0130 0.0136  0.0222  705 LEU B O   
6638  C CB  . LEU B 404 ? 0.3545 0.4272 0.3411 -0.0451 0.0169  0.0145  705 LEU B CB  
6639  C CG  . LEU B 404 ? 0.4635 0.5460 0.4508 -0.0567 0.0159  0.0104  705 LEU B CG  
6640  C CD1 . LEU B 404 ? 0.4204 0.4805 0.3995 -0.0709 0.0196  0.0077  705 LEU B CD1 
6641  C CD2 . LEU B 404 ? 0.3640 0.4849 0.3597 -0.0609 0.0154  0.0079  705 LEU B CD2 
6642  N N   . THR B 405 ? 0.5963 0.6886 0.5870 -0.0221 0.0188  0.0191  706 THR B N   
6643  C CA  . THR B 405 ? 0.4773 0.5617 0.4647 -0.0141 0.0209  0.0208  706 THR B CA  
6644  C C   . THR B 405 ? 0.5613 0.6414 0.5465 -0.0267 0.0265  0.0202  706 THR B C   
6645  O O   . THR B 405 ? 0.5286 0.6237 0.5169 -0.0405 0.0292  0.0183  706 THR B O   
6646  C CB  . THR B 405 ? 0.5459 0.6567 0.5373 -0.0011 0.0204  0.0209  706 THR B CB  
6647  O OG1 . THR B 405 ? 0.6242 0.7191 0.6092 0.0114  0.0204  0.0224  706 THR B OG1 
6648  C CG2 . THR B 405 ? 0.5097 0.6536 0.5083 -0.0095 0.0247  0.0190  706 THR B CG2 
6649  N N   . PRO B 406 ? 0.5227 0.5808 0.5009 -0.0232 0.0281  0.0220  707 PRO B N   
6650  C CA  . PRO B 406 ? 0.5172 0.5549 0.4899 -0.0102 0.0253  0.0237  707 PRO B CA  
6651  C C   . PRO B 406 ? 0.4936 0.5104 0.4636 -0.0085 0.0209  0.0244  707 PRO B C   
6652  O O   . PRO B 406 ? 0.6238 0.6354 0.5942 -0.0175 0.0209  0.0237  707 PRO B O   
6653  C CB  . PRO B 406 ? 0.5294 0.5519 0.4954 -0.0134 0.0291  0.0248  707 PRO B CB  
6654  C CG  . PRO B 406 ? 0.5450 0.5854 0.5133 -0.0248 0.0345  0.0243  707 PRO B CG  
6655  C CD  . PRO B 406 ? 0.4857 0.5392 0.4598 -0.0346 0.0337  0.0224  707 PRO B CD  
6656  N N   . SER B 407 ? 0.4123 0.4165 0.3783 0.0025  0.0174  0.0256  708 SER B N   
6657  C CA  . SER B 407 ? 0.5095 0.4972 0.4732 0.0030  0.0136  0.0267  708 SER B CA  
6658  C C   . SER B 407 ? 0.5326 0.5000 0.4893 0.0097  0.0113  0.0277  708 SER B C   
6659  O O   . SER B 407 ? 0.5592 0.5252 0.5120 0.0168  0.0118  0.0272  708 SER B O   
6660  C CB  . SER B 407 ? 0.6041 0.6027 0.5708 0.0075  0.0102  0.0273  708 SER B CB  
6661  O OG  . SER B 407 ? 0.7143 0.7164 0.6781 0.0201  0.0086  0.0281  708 SER B OG  
6662  N N   . PHE B 408 ? 0.6274 0.5803 0.5819 0.0069  0.0089  0.0287  709 PHE B N   
6663  C CA  . PHE B 408 ? 0.5301 0.4662 0.4783 0.0115  0.0056  0.0297  709 PHE B CA  
6664  C C   . PHE B 408 ? 0.5632 0.4983 0.5096 0.0162  0.0023  0.0315  709 PHE B C   
6665  O O   . PHE B 408 ? 0.5617 0.5057 0.5123 0.0133  0.0018  0.0324  709 PHE B O   
6666  C CB  . PHE B 408 ? 0.4625 0.3876 0.4096 0.0054  0.0049  0.0301  709 PHE B CB  
6667  C CG  . PHE B 408 ? 0.5288 0.4512 0.4745 0.0030  0.0077  0.0291  709 PHE B CG  
6668  C CD1 . PHE B 408 ? 0.4615 0.3766 0.4017 0.0069  0.0074  0.0284  709 PHE B CD1 
6669  C CD2 . PHE B 408 ? 0.4860 0.4113 0.4339 -0.0028 0.0105  0.0289  709 PHE B CD2 
6670  C CE1 . PHE B 408 ? 0.5006 0.4133 0.4381 0.0055  0.0100  0.0283  709 PHE B CE1 
6671  C CE2 . PHE B 408 ? 0.4618 0.3812 0.4055 -0.0042 0.0133  0.0289  709 PHE B CE2 
6672  C CZ  . PHE B 408 ? 0.4685 0.3827 0.4074 0.0002  0.0130  0.0290  709 PHE B CZ  
6673  N N   . GLU B 409 ? 0.4947 0.4171 0.4328 0.0237  0.0000  0.0319  710 GLU B N   
6674  C CA  . GLU B 409 ? 0.4645 0.3801 0.3965 0.0300  -0.0030 0.0343  710 GLU B CA  
6675  C C   . GLU B 409 ? 0.5355 0.4264 0.4571 0.0285  -0.0060 0.0353  710 GLU B C   
6676  O O   . GLU B 409 ? 0.6713 0.5524 0.5896 0.0258  -0.0060 0.0333  710 GLU B O   
6677  C CB  . GLU B 409 ? 0.4655 0.3877 0.3938 0.0430  -0.0028 0.0336  710 GLU B CB  
6678  C CG  . GLU B 409 ? 0.5544 0.5060 0.4932 0.0441  0.0000  0.0324  710 GLU B CG  
6679  C CD  . GLU B 409 ? 0.7008 0.6674 0.6464 0.0399  -0.0009 0.0341  710 GLU B CD  
6680  O OE1 . GLU B 409 ? 0.6786 0.6339 0.6191 0.0406  -0.0039 0.0371  710 GLU B OE1 
6681  O OE2 . GLU B 409 ? 0.6397 0.6293 0.5947 0.0350  0.0015  0.0323  710 GLU B OE2 
6682  N N   . TYR B 410 ? 0.5124 0.3932 0.4277 0.0295  -0.0085 0.0386  711 TYR B N   
6683  C CA  . TYR B 410 ? 0.5336 0.3886 0.4359 0.0276  -0.0113 0.0398  711 TYR B CA  
6684  C C   . TYR B 410 ? 0.5715 0.4104 0.4606 0.0396  -0.0123 0.0383  711 TYR B C   
6685  O O   . TYR B 410 ? 0.6540 0.5042 0.5441 0.0512  -0.0111 0.0376  711 TYR B O   
6686  C CB  . TYR B 410 ? 0.6343 0.4812 0.5317 0.0236  -0.0132 0.0447  711 TYR B CB  
6687  C CG  . TYR B 410 ? 0.7495 0.6131 0.6584 0.0138  -0.0121 0.0460  711 TYR B CG  
6688  C CD1 . TYR B 410 ? 0.8495 0.7131 0.7622 0.0031  -0.0120 0.0451  711 TYR B CD1 
6689  C CD2 . TYR B 410 ? 0.9097 0.7906 0.8252 0.0161  -0.0113 0.0477  711 TYR B CD2 
6690  C CE1 . TYR B 410 ? 0.9602 0.8392 0.8822 -0.0037 -0.0107 0.0459  711 TYR B CE1 
6691  C CE2 . TYR B 410 ? 0.9751 0.8697 0.8993 0.0079  -0.0103 0.0481  711 TYR B CE2 
6692  C CZ  . TYR B 410 ? 1.0224 0.9152 0.9494 -0.0013 -0.0098 0.0472  711 TYR B CZ  
6693  O OH  . TYR B 410 ? 1.0287 0.9351 0.9631 -0.0074 -0.0085 0.0472  711 TYR B OH  
6694  N N   . GLN B 411 ? 0.5474 0.3605 0.4233 0.0366  -0.0145 0.0374  712 GLN B N   
6695  C CA  . GLN B 411 ? 0.5339 0.3250 0.3932 0.0477  -0.0158 0.0352  712 GLN B CA  
6696  C C   . GLN B 411 ? 0.5838 0.3419 0.4258 0.0405  -0.0190 0.0366  712 GLN B C   
6697  O O   . GLN B 411 ? 0.5743 0.3322 0.4203 0.0255  -0.0198 0.0380  712 GLN B O   
6698  C CB  . GLN B 411 ? 0.5529 0.3490 0.4136 0.0514  -0.0142 0.0296  712 GLN B CB  
6699  C CG  . GLN B 411 ? 0.5282 0.3212 0.3913 0.0384  -0.0149 0.0270  712 GLN B CG  
6700  C CD  . GLN B 411 ? 0.5903 0.3917 0.4553 0.0426  -0.0130 0.0221  712 GLN B CD  
6701  O OE1 . GLN B 411 ? 0.6965 0.4974 0.5556 0.0552  -0.0117 0.0197  712 GLN B OE1 
6702  N NE2 . GLN B 411 ? 0.5463 0.3565 0.4190 0.0327  -0.0127 0.0210  712 GLN B NE2 
6703  N N   . PRO B 412 ? 0.7412 0.4713 0.5631 0.0506  -0.0207 0.0365  713 PRO B N   
6704  C CA  . PRO B 412 ? 0.8530 0.5472 0.6554 0.0417  -0.0236 0.0378  713 PRO B CA  
6705  C C   . PRO B 412 ? 0.7966 0.4833 0.5974 0.0288  -0.0248 0.0326  713 PRO B C   
6706  O O   . PRO B 412 ? 0.7792 0.4762 0.5848 0.0334  -0.0239 0.0271  713 PRO B O   
6707  C CB  . PRO B 412 ? 0.9388 0.6031 0.7179 0.0591  -0.0248 0.0376  713 PRO B CB  
6708  C CG  . PRO B 412 ? 0.8108 0.5027 0.6004 0.0775  -0.0225 0.0376  713 PRO B CG  
6709  C CD  . PRO B 412 ? 0.7489 0.4781 0.5632 0.0709  -0.0199 0.0348  713 PRO B CD  
6710  N N   . ASP B 413 ? 0.8156 0.4869 0.6097 0.0121  -0.0269 0.0344  714 ASP B N   
6711  C CA  . ASP B 413 ? 0.9015 0.5629 0.6904 -0.0009 -0.0290 0.0292  714 ASP B CA  
6712  C C   . ASP B 413 ? 0.9510 0.5836 0.7192 0.0094  -0.0305 0.0232  714 ASP B C   
6713  O O   . ASP B 413 ? 0.9362 0.5376 0.6836 0.0188  -0.0313 0.0246  714 ASP B O   
6714  C CB  . ASP B 413 ? 0.9721 0.6172 0.7522 -0.0204 -0.0311 0.0324  714 ASP B CB  
6715  C CG  . ASP B 413 ? 0.9948 0.6711 0.7953 -0.0314 -0.0296 0.0373  714 ASP B CG  
6716  O OD1 . ASP B 413 ? 0.9545 0.6637 0.7755 -0.0295 -0.0279 0.0356  714 ASP B OD1 
6717  O OD2 . ASP B 413 ? 1.0633 0.7297 0.8573 -0.0417 -0.0299 0.0428  714 ASP B OD2 
6718  N N   . PRO B 414 ? 0.9691 0.6096 0.7404 0.0088  -0.0309 0.0165  715 PRO B N   
6719  C CA  . PRO B 414 ? 0.8899 0.5060 0.6418 0.0212  -0.0318 0.0101  715 PRO B CA  
6720  C C   . PRO B 414 ? 0.9727 0.5417 0.6953 0.0148  -0.0352 0.0080  715 PRO B C   
6721  O O   . PRO B 414 ? 1.1287 0.6695 0.8301 0.0291  -0.0357 0.0041  715 PRO B O   
6722  C CB  . PRO B 414 ? 0.8690 0.5063 0.6314 0.0178  -0.0317 0.0040  715 PRO B CB  
6723  C CG  . PRO B 414 ? 0.9076 0.5667 0.6864 -0.0006 -0.0325 0.0064  715 PRO B CG  
6724  C CD  . PRO B 414 ? 0.9254 0.5952 0.7151 -0.0028 -0.0308 0.0144  715 PRO B CD  
6725  N N   . TRP B 415 ? 0.9232 0.4817 0.6422 -0.0060 -0.0374 0.0106  716 TRP B N   
6726  C CA  . TRP B 415 ? 1.0482 0.5588 0.7368 -0.0147 -0.0406 0.0083  716 TRP B CA  
6727  C C   . TRP B 415 ? 1.1142 0.5908 0.7826 -0.0056 -0.0402 0.0146  716 TRP B C   
6728  O O   . TRP B 415 ? 1.1055 0.5351 0.7440 -0.0103 -0.0425 0.0130  716 TRP B O   
6729  C CB  . TRP B 415 ? 1.0595 0.5717 0.7499 -0.0426 -0.0432 0.0083  716 TRP B CB  
6730  C CG  . TRP B 415 ? 1.0369 0.5745 0.7457 -0.0534 -0.0415 0.0167  716 TRP B CG  
6731  C CD1 . TRP B 415 ? 1.0521 0.5703 0.7505 -0.0595 -0.0410 0.0245  716 TRP B CD1 
6732  C CD2 . TRP B 415 ? 0.9786 0.5648 0.7178 -0.0588 -0.0400 0.0184  716 TRP B CD2 
6733  N NE1 . TRP B 415 ? 0.9993 0.5533 0.7207 -0.0686 -0.0391 0.0304  716 TRP B NE1 
6734  C CE2 . TRP B 415 ? 0.9551 0.5504 0.7016 -0.0679 -0.0385 0.0266  716 TRP B CE2 
6735  C CE3 . TRP B 415 ? 0.8232 0.4444 0.5824 -0.0560 -0.0395 0.0140  716 TRP B CE3 
6736  C CZ2 . TRP B 415 ? 0.8774 0.5154 0.6501 -0.0736 -0.0367 0.0296  716 TRP B CZ2 
6737  C CZ3 . TRP B 415 ? 0.8326 0.4936 0.6168 -0.0614 -0.0378 0.0175  716 TRP B CZ3 
6738  C CH2 . TRP B 415 ? 0.8355 0.5046 0.6263 -0.0698 -0.0365 0.0249  716 TRP B CH2 
6739  N N   . ASN B 416 ? 1.1486 0.6463 0.8309 0.0067  -0.0374 0.0216  717 ASN B N   
6740  C CA  . ASN B 416 ? 1.1762 0.6439 0.8382 0.0215  -0.0371 0.0272  717 ASN B CA  
6741  C C   . ASN B 416 ? 1.2318 0.6877 0.8812 0.0484  -0.0365 0.0225  717 ASN B C   
6742  O O   . ASN B 416 ? 1.2355 0.6565 0.8600 0.0632  -0.0370 0.0251  717 ASN B O   
6743  C CB  . ASN B 416 ? 1.0410 0.5381 0.7220 0.0248  -0.0348 0.0362  717 ASN B CB  
6744  C CG  . ASN B 416 ? 1.0050 0.5173 0.6989 0.0003  -0.0348 0.0410  717 ASN B CG  
6745  O OD1 . ASN B 416 ? 1.0729 0.5599 0.7523 -0.0190 -0.0367 0.0408  717 ASN B OD1 
6746  N ND2 . ASN B 416 ? 0.8947 0.4491 0.6154 0.0005  -0.0326 0.0449  717 ASN B ND2 
6747  N N   . THR B 417 ? 1.2234 0.7075 0.8881 0.0554  -0.0353 0.0157  718 THR B N   
6748  C CA  . THR B 417 ? 1.2827 0.7703 0.9426 0.0815  -0.0337 0.0117  718 THR B CA  
6749  C C   . THR B 417 ? 1.3029 0.7711 0.9467 0.0854  -0.0348 0.0015  718 THR B C   
6750  O O   . THR B 417 ? 1.3368 0.7914 0.9650 0.1081  -0.0340 -0.0022 718 THR B O   
6751  C CB  . THR B 417 ? 1.2844 0.8278 0.9772 0.0891  -0.0301 0.0134  718 THR B CB  
6752  O OG1 . THR B 417 ? 1.2099 0.7800 0.9257 0.0702  -0.0297 0.0186  718 THR B OG1 
6753  C CG2 . THR B 417 ? 1.3035 0.8560 0.9954 0.1128  -0.0283 0.0175  718 THR B CG2 
6754  N N   . HIS B 418 ? 1.3322 0.7990 0.9780 0.0648  -0.0369 -0.0034 719 HIS B N   
6755  C CA  . HIS B 418 ? 1.3902 0.8513 1.0272 0.0683  -0.0377 -0.0134 719 HIS B CA  
6756  C C   . HIS B 418 ? 1.5023 0.9050 1.1001 0.0710  -0.0408 -0.0194 719 HIS B C   
6757  O O   . HIS B 418 ? 1.5432 0.9115 1.1239 0.0534  -0.0437 -0.0179 719 HIS B O   
6758  C CB  . HIS B 418 ? 1.3381 0.8247 0.9931 0.0463  -0.0391 -0.0164 719 HIS B CB  
6759  C CG  . HIS B 418 ? 1.2796 0.7612 0.9248 0.0482  -0.0404 -0.0266 719 HIS B CG  
6760  N ND1 . HIS B 418 ? 1.2834 0.7390 0.9114 0.0307  -0.0448 -0.0331 719 HIS B ND1 
6761  C CD2 . HIS B 418 ? 1.2430 0.7429 0.8922 0.0653  -0.0379 -0.0315 719 HIS B CD2 
6762  C CE1 . HIS B 418 ? 1.2919 0.7495 0.9134 0.0377  -0.0452 -0.0419 719 HIS B CE1 
6763  N NE2 . HIS B 418 ? 1.2757 0.7597 0.9096 0.0590  -0.0409 -0.0408 719 HIS B NE2 
6764  N N   . VAL B 419 ? 1.5641 0.9554 1.1466 0.0927  -0.0399 -0.0264 720 VAL B N   
6765  C CA  . VAL B 419 ? 1.6366 0.9713 1.1796 0.0978  -0.0427 -0.0341 720 VAL B CA  
6766  C C   . VAL B 419 ? 1.6113 0.9464 1.1516 0.0833  -0.0452 -0.0443 720 VAL B C   
6767  O O   . VAL B 419 ? 1.6478 1.0136 1.2006 0.0933  -0.0432 -0.0493 720 VAL B O   
6768  C CB  . VAL B 419 ? 1.6517 0.9740 1.1776 0.1317  -0.0403 -0.0366 720 VAL B CB  
6769  C CG1 . VAL B 419 ? 1.6360 0.9266 1.1435 0.1440  -0.0404 -0.0288 720 VAL B CG1 
6770  C CG2 . VAL B 419 ? 1.5858 0.9681 1.1432 0.1477  -0.0358 -0.0356 720 VAL B CG2 
6771  N N   . TRP B 420 ? 1.5621 0.8643 1.0854 0.0590  -0.0495 -0.0471 721 TRP B N   
6772  C CA  . TRP B 420 ? 1.5340 0.8400 1.0559 0.0416  -0.0527 -0.0565 721 TRP B CA  
6773  C C   . TRP B 420 ? 1.6072 0.8771 1.0970 0.0565  -0.0540 -0.0685 721 TRP B C   
6774  O O   . TRP B 420 ? 1.6021 0.8350 1.0658 0.0780  -0.0529 -0.0697 721 TRP B O   
6775  C CB  . TRP B 420 ? 1.5088 0.7952 1.0235 0.0089  -0.0570 -0.0558 721 TRP B CB  
6776  C CG  . TRP B 420 ? 1.5031 0.8317 1.0511 -0.0079 -0.0559 -0.0459 721 TRP B CG  
6777  C CD1 . TRP B 420 ? 1.5030 0.8396 1.0625 -0.0041 -0.0531 -0.0348 721 TRP B CD1 
6778  C CD2 . TRP B 420 ? 1.4065 0.7750 0.9790 -0.0301 -0.0577 -0.0466 721 TRP B CD2 
6779  N NE1 . TRP B 420 ? 1.4307 0.8086 1.0199 -0.0225 -0.0528 -0.0289 721 TRP B NE1 
6780  C CE2 . TRP B 420 ? 1.3719 0.7702 0.9696 -0.0380 -0.0555 -0.0358 721 TRP B CE2 
6781  C CE3 . TRP B 420 ? 1.3095 0.6927 0.8844 -0.0427 -0.0610 -0.0553 721 TRP B CE3 
6782  C CZ2 . TRP B 420 ? 1.2930 0.7337 0.9173 -0.0568 -0.0564 -0.0337 721 TRP B CZ2 
6783  C CZ3 . TRP B 420 ? 1.2736 0.7003 0.8754 -0.0614 -0.0622 -0.0527 721 TRP B CZ3 
6784  C CH2 . TRP B 420 ? 1.2902 0.7450 0.9163 -0.0677 -0.0597 -0.0420 721 TRP B CH2 
6785  N N   . LYS B 421 ? 1.6630 0.9445 1.1540 0.0457  -0.0565 -0.0776 722 LYS B N   
6786  C CA  . LYS B 421 ? 1.6792 0.9302 1.1404 0.0578  -0.0580 -0.0902 722 LYS B CA  
6787  C C   . LYS B 421 ? 1.6633 0.9142 1.1192 0.0340  -0.0631 -0.0999 722 LYS B C   
6788  O O   . LYS B 421 ? 1.6620 0.8919 1.1088 0.0070  -0.0675 -0.1006 722 LYS B O   
6789  C CB  . LYS B 421 ? 1.6343 0.9185 1.1076 0.0873  -0.0531 -0.0917 722 LYS B CB  
6790  C CG  . LYS B 421 ? 1.5677 0.9177 1.0849 0.0873  -0.0491 -0.0829 722 LYS B CG  
6791  C CD  . LYS B 421 ? 1.5440 0.9199 1.0705 0.1176  -0.0432 -0.0809 722 LYS B CD  
6792  C CE  . LYS B 421 ? 1.4740 0.8934 1.0349 0.1190  -0.0393 -0.0686 722 LYS B CE  
6793  N NZ  . LYS B 421 ? 1.4263 0.8678 0.9935 0.1475  -0.0338 -0.0664 722 LYS B NZ  
6794  N N   . ARG C 3   ? 1.2837 1.7155 1.3090 0.2088  0.0440  -0.0618 304 ARG C N   
6795  C CA  . ARG C 3   ? 1.3362 1.7462 1.3646 0.2085  0.0361  -0.0570 304 ARG C CA  
6796  C C   . ARG C 3   ? 1.2736 1.6168 1.2837 0.2071  0.0309  -0.0564 304 ARG C C   
6797  O O   . ARG C 3   ? 1.3572 1.6711 1.3594 0.2211  0.0245  -0.0575 304 ARG C O   
6798  C CB  . ARG C 3   ? 1.4336 1.8674 1.4663 0.2363  0.0329  -0.0620 304 ARG C CB  
6799  C CG  . ARG C 3   ? 1.4490 1.8825 1.4907 0.2341  0.0255  -0.0560 304 ARG C CG  
6800  C CD  . ARG C 3   ? 1.5107 2.0116 1.5724 0.2408  0.0265  -0.0563 304 ARG C CD  
6801  N NE  . ARG C 3   ? 1.5792 2.0800 1.6438 0.2555  0.0185  -0.0547 304 ARG C NE  
6802  C CZ  . ARG C 3   ? 1.6285 2.1541 1.6938 0.2862  0.0163  -0.0602 304 ARG C CZ  
6803  N NH1 . ARG C 3   ? 1.6605 2.2125 1.7239 0.3052  0.0219  -0.0682 304 ARG C NH1 
6804  N NH2 . ARG C 3   ? 1.5987 2.1221 1.6655 0.2983  0.0084  -0.0575 304 ARG C NH2 
6805  N N   . PHE C 4   ? 1.1022 1.4228 1.1050 0.1897  0.0335  -0.0541 305 PHE C N   
6806  C CA  . PHE C 4   ? 1.0078 1.2706 0.9929 0.1881  0.0293  -0.0545 305 PHE C CA  
6807  C C   . PHE C 4   ? 0.8816 1.1332 0.8643 0.1652  0.0323  -0.0498 305 PHE C C   
6808  O O   . PHE C 4   ? 0.8877 1.1715 0.8773 0.1553  0.0383  -0.0482 305 PHE C O   
6809  C CB  . PHE C 4   ? 1.1359 1.3745 1.1015 0.2124  0.0287  -0.0650 305 PHE C CB  
6810  C CG  . PHE C 4   ? 1.2748 1.5257 1.2329 0.2146  0.0353  -0.0714 305 PHE C CG  
6811  C CD1 . PHE C 4   ? 1.3039 1.6089 1.2743 0.2171  0.0422  -0.0732 305 PHE C CD1 
6812  C CD2 . PHE C 4   ? 1.2883 1.4982 1.2262 0.2133  0.0347  -0.0758 305 PHE C CD2 
6813  C CE1 . PHE C 4   ? 1.2806 1.5976 1.2430 0.2188  0.0486  -0.0791 305 PHE C CE1 
6814  C CE2 . PHE C 4   ? 1.2951 1.5163 1.2247 0.2149  0.0405  -0.0820 305 PHE C CE2 
6815  C CZ  . PHE C 4   ? 1.2928 1.5671 1.2344 0.2181  0.0476  -0.0835 305 PHE C CZ  
6816  N N   . LEU C 5   ? 0.7472 0.9534 0.7193 0.1573  0.0279  -0.0473 306 LEU C N   
6817  C CA  . LEU C 5   ? 0.6381 0.8293 0.6066 0.1377  0.0293  -0.0425 306 LEU C CA  
6818  C C   . LEU C 5   ? 0.6468 0.7899 0.5984 0.1394  0.0245  -0.0450 306 LEU C C   
6819  O O   . LEU C 5   ? 0.8053 0.9231 0.7556 0.1385  0.0192  -0.0424 306 LEU C O   
6820  C CB  . LEU C 5   ? 0.5611 0.7590 0.5426 0.1171  0.0289  -0.0320 306 LEU C CB  
6821  C CG  . LEU C 5   ? 0.5526 0.7937 0.5484 0.1062  0.0340  -0.0274 306 LEU C CG  
6822  C CD1 . LEU C 5   ? 0.5266 0.7611 0.5302 0.0871  0.0322  -0.0180 306 LEU C CD1 
6823  C CD2 . LEU C 5   ? 0.4348 0.6918 0.4260 0.1005  0.0402  -0.0280 306 LEU C CD2 
6824  N N   . LYS C 6   ? 0.5969 0.7285 0.5350 0.1403  0.0264  -0.0501 307 LYS C N   
6825  C CA  . LYS C 6   ? 0.5903 0.6784 0.5105 0.1410  0.0220  -0.0538 307 LYS C CA  
6826  C C   . LYS C 6   ? 0.6302 0.7044 0.5510 0.1207  0.0205  -0.0466 307 LYS C C   
6827  O O   . LYS C 6   ? 0.6362 0.7317 0.5653 0.1089  0.0239  -0.0411 307 LYS C O   
6828  C CB  . LYS C 6   ? 0.7008 0.7816 0.6031 0.1535  0.0242  -0.0646 307 LYS C CB  
6829  C CG  . LYS C 6   ? 0.8064 0.8949 0.7039 0.1779  0.0253  -0.0732 307 LYS C CG  
6830  C CD  . LYS C 6   ? 0.9380 1.0247 0.8181 0.1895  0.0291  -0.0842 307 LYS C CD  
6831  C CE  . LYS C 6   ? 0.9509 1.0387 0.8222 0.2171  0.0298  -0.0939 307 LYS C CE  
6832  N NZ  . LYS C 6   ? 0.9572 0.9991 0.8135 0.2266  0.0230  -0.0958 307 LYS C NZ  
6833  N N   . VAL C 7   ? 0.5639 0.6025 0.4752 0.1169  0.0152  -0.0464 308 VAL C N   
6834  C CA  . VAL C 7   ? 0.5523 0.5767 0.4614 0.1004  0.0133  -0.0415 308 VAL C CA  
6835  C C   . VAL C 7   ? 0.5962 0.5900 0.4844 0.1021  0.0104  -0.0491 308 VAL C C   
6836  O O   . VAL C 7   ? 0.6161 0.5885 0.4910 0.1143  0.0084  -0.0562 308 VAL C O   
6837  C CB  . VAL C 7   ? 0.6591 0.6732 0.5778 0.0905  0.0098  -0.0332 308 VAL C CB  
6838  C CG1 . VAL C 7   ? 0.6317 0.6724 0.5682 0.0894  0.0121  -0.0271 308 VAL C CG1 
6839  C CG2 . VAL C 7   ? 0.6619 0.6439 0.5699 0.0959  0.0048  -0.0363 308 VAL C CG2 
6840  N N   . LYS C 8   ? 0.5381 0.5293 0.4217 0.0898  0.0100  -0.0476 309 LYS C N   
6841  C CA  . LYS C 8   ? 0.5561 0.5221 0.4190 0.0883  0.0075  -0.0552 309 LYS C CA  
6842  C C   . LYS C 8   ? 0.4770 0.4308 0.3398 0.0718  0.0034  -0.0498 309 LYS C C   
6843  O O   . LYS C 8   ? 0.6325 0.6047 0.5092 0.0625  0.0042  -0.0411 309 LYS C O   
6844  C CB  . LYS C 8   ? 0.5931 0.5744 0.4478 0.0907  0.0113  -0.0610 309 LYS C CB  
6845  C CG  . LYS C 8   ? 0.6920 0.6491 0.5244 0.0861  0.0084  -0.0690 309 LYS C CG  
6846  C CD  . LYS C 8   ? 0.7637 0.7366 0.5865 0.0906  0.0126  -0.0758 309 LYS C CD  
6847  C CE  . LYS C 8   ? 0.8338 0.7834 0.6333 0.0837  0.0094  -0.0839 309 LYS C CE  
6848  N NZ  . LYS C 8   ? 0.7716 0.7401 0.5627 0.0849  0.0132  -0.0891 309 LYS C NZ  
6849  N N   . ASN C 9   ? 0.6244 0.5472 0.4700 0.0683  -0.0008 -0.0550 310 ASN C N   
6850  C CA  . ASN C 9   ? 0.6946 0.6085 0.5373 0.0519  -0.0047 -0.0518 310 ASN C CA  
6851  C C   . ASN C 9   ? 0.7043 0.6159 0.5307 0.0467  -0.0053 -0.0587 310 ASN C C   
6852  O O   . ASN C 9   ? 0.7753 0.6655 0.5817 0.0530  -0.0056 -0.0688 310 ASN C O   
6853  C CB  . ASN C 9   ? 0.6489 0.5313 0.4825 0.0481  -0.0090 -0.0525 310 ASN C CB  
6854  C CG  . ASN C 9   ? 0.7473 0.6247 0.5786 0.0302  -0.0128 -0.0493 310 ASN C CG  
6855  O OD1 . ASN C 9   ? 0.8287 0.7048 0.6485 0.0218  -0.0143 -0.0536 310 ASN C OD1 
6856  N ND2 . ASN C 9   ? 0.6807 0.5578 0.5230 0.0241  -0.0143 -0.0420 310 ASN C ND2 
6857  N N   . TRP C 10  ? 0.7022 0.6348 0.5358 0.0361  -0.0056 -0.0535 311 TRP C N   
6858  C CA  . TRP C 10  ? 0.7030 0.6406 0.5229 0.0319  -0.0058 -0.0593 311 TRP C CA  
6859  C C   . TRP C 10  ? 0.7718 0.6888 0.5746 0.0185  -0.0111 -0.0643 311 TRP C C   
6860  O O   . TRP C 10  ? 0.8912 0.8076 0.6786 0.0144  -0.0120 -0.0712 311 TRP C O   
6861  C CB  . TRP C 10  ? 0.5098 0.4809 0.3430 0.0280  -0.0038 -0.0511 311 TRP C CB  
6862  C CG  . TRP C 10  ? 0.5225 0.5136 0.3667 0.0387  0.0020  -0.0481 311 TRP C CG  
6863  C CD1 . TRP C 10  ? 0.5438 0.5448 0.4058 0.0422  0.0043  -0.0402 311 TRP C CD1 
6864  C CD2 . TRP C 10  ? 0.5947 0.5994 0.4318 0.0461  0.0064  -0.0534 311 TRP C CD2 
6865  N NE1 . TRP C 10  ? 0.5765 0.5977 0.4435 0.0500  0.0097  -0.0399 311 TRP C NE1 
6866  C CE2 . TRP C 10  ? 0.5932 0.6181 0.4456 0.0529  0.0114  -0.0477 311 TRP C CE2 
6867  C CE3 . TRP C 10  ? 0.6768 0.6799 0.4956 0.0469  0.0068  -0.0626 311 TRP C CE3 
6868  C CZ2 . TRP C 10  ? 0.6340 0.6794 0.4848 0.0602  0.0170  -0.0506 311 TRP C CZ2 
6869  C CZ3 . TRP C 10  ? 0.6588 0.6810 0.4755 0.0556  0.0125  -0.0657 311 TRP C CZ3 
6870  C CH2 . TRP C 10  ? 0.6458 0.6902 0.4789 0.0619  0.0177  -0.0595 311 TRP C CH2 
6871  N N   . GLU C 11  ? 0.7706 0.6717 0.5748 0.0104  -0.0147 -0.0613 312 GLU C N   
6872  C CA  . GLU C 11  ? 0.6844 0.5609 0.4692 -0.0031 -0.0195 -0.0672 312 GLU C CA  
6873  C C   . GLU C 11  ? 0.7283 0.5658 0.4882 0.0041  -0.0197 -0.0783 312 GLU C C   
6874  O O   . GLU C 11  ? 0.8841 0.7022 0.6204 -0.0028 -0.0220 -0.0875 312 GLU C O   
6875  C CB  . GLU C 11  ? 0.8025 0.6759 0.5965 -0.0143 -0.0224 -0.0600 312 GLU C CB  
6876  C CG  . GLU C 11  ? 0.9499 0.8534 0.7584 -0.0266 -0.0244 -0.0522 312 GLU C CG  
6877  C CD  . GLU C 11  ? 1.0382 0.9360 0.8514 -0.0383 -0.0272 -0.0474 312 GLU C CD  
6878  O OE1 . GLU C 11  ? 0.9689 0.8666 0.7958 -0.0323 -0.0254 -0.0412 312 GLU C OE1 
6879  O OE2 . GLU C 11  ? 1.0980 0.9926 0.9004 -0.0545 -0.0311 -0.0502 312 GLU C OE2 
6880  N N   . THR C 12  ? 0.7265 0.5508 0.4897 0.0181  -0.0178 -0.0775 313 THR C N   
6881  C CA  . THR C 12  ? 0.7390 0.5217 0.4779 0.0263  -0.0189 -0.0863 313 THR C CA  
6882  C C   . THR C 12  ? 0.8377 0.6206 0.5710 0.0478  -0.0146 -0.0934 313 THR C C   
6883  O O   . THR C 12  ? 0.8947 0.6421 0.6037 0.0573  -0.0153 -0.1025 313 THR C O   
6884  C CB  . THR C 12  ? 0.8678 0.6324 0.6111 0.0276  -0.0206 -0.0803 313 THR C CB  
6885  O OG1 . THR C 12  ? 0.7949 0.5778 0.5571 0.0450  -0.0171 -0.0758 313 THR C OG1 
6886  C CG2 . THR C 12  ? 0.8388 0.6178 0.5968 0.0090  -0.0231 -0.0710 313 THR C CG2 
6887  N N   . GLU C 13  ? 0.8322 0.6536 0.5862 0.0559  -0.0102 -0.0894 314 GLU C N   
6888  C CA  . GLU C 13  ? 0.8258 0.6587 0.5805 0.0762  -0.0052 -0.0945 314 GLU C CA  
6889  C C   . GLU C 13  ? 0.7918 0.6131 0.5495 0.0930  -0.0047 -0.0939 314 GLU C C   
6890  O O   . GLU C 13  ? 0.6731 0.5006 0.4281 0.1120  -0.0010 -0.0996 314 GLU C O   
6891  C CB  . GLU C 13  ? 0.8855 0.7017 0.6135 0.0814  -0.0043 -0.1077 314 GLU C CB  
6892  C CG  . GLU C 13  ? 0.9979 0.8323 0.7241 0.0663  -0.0046 -0.1082 314 GLU C CG  
6893  C CD  . GLU C 13  ? 1.0832 0.9033 0.7827 0.0714  -0.0033 -0.1219 314 GLU C CD  
6894  O OE1 . GLU C 13  ? 1.1229 0.9574 0.8224 0.0887  0.0020  -0.1269 314 GLU C OE1 
6895  O OE2 . GLU C 13  ? 1.0810 0.8761 0.7587 0.0576  -0.0075 -0.1280 314 GLU C OE2 
6896  N N   . VAL C 14  ? 0.6882 0.4959 0.4520 0.0873  -0.0081 -0.0869 315 VAL C N   
6897  C CA  . VAL C 14  ? 0.7497 0.5530 0.5195 0.1031  -0.0079 -0.0846 315 VAL C CA  
6898  C C   . VAL C 14  ? 0.7999 0.6489 0.5968 0.1111  -0.0031 -0.0791 315 VAL C C   
6899  O O   . VAL C 14  ? 0.8609 0.7380 0.6768 0.0989  -0.0017 -0.0713 315 VAL C O   
6900  C CB  . VAL C 14  ? 0.8526 0.6355 0.6240 0.0929  -0.0124 -0.0773 315 VAL C CB  
6901  C CG1 . VAL C 14  ? 0.8430 0.6357 0.6294 0.1061  -0.0120 -0.0716 315 VAL C CG1 
6902  C CG2 . VAL C 14  ? 0.8678 0.6004 0.6076 0.0887  -0.0167 -0.0839 315 VAL C CG2 
6903  N N   . VAL C 15  ? 0.7661 0.6228 0.5631 0.1316  -0.0005 -0.0834 316 VAL C N   
6904  C CA  . VAL C 15  ? 0.7600 0.6601 0.5819 0.1386  0.0038  -0.0783 316 VAL C CA  
6905  C C   . VAL C 15  ? 0.8694 0.7664 0.6989 0.1491  0.0016  -0.0743 316 VAL C C   
6906  O O   . VAL C 15  ? 0.9607 0.8304 0.7733 0.1643  -0.0007 -0.0800 316 VAL C O   
6907  C CB  . VAL C 15  ? 0.6638 0.5873 0.4831 0.1533  0.0094  -0.0861 316 VAL C CB  
6908  C CG1 . VAL C 15  ? 0.5392 0.5097 0.3842 0.1579  0.0138  -0.0803 316 VAL C CG1 
6909  C CG2 . VAL C 15  ? 0.5530 0.4804 0.3635 0.1425  0.0114  -0.0899 316 VAL C CG2 
6910  N N   . LEU C 16  ? 0.7821 0.7054 0.6351 0.1412  0.0021  -0.0646 317 LEU C N   
6911  C CA  . LEU C 16  ? 0.7227 0.6512 0.5857 0.1502  0.0003  -0.0604 317 LEU C CA  
6912  C C   . LEU C 16  ? 0.6969 0.6722 0.5802 0.1576  0.0049  -0.0588 317 LEU C C   
6913  O O   . LEU C 16  ? 0.7115 0.7149 0.6054 0.1489  0.0093  -0.0569 317 LEU C O   
6914  C CB  . LEU C 16  ? 0.6445 0.5641 0.5164 0.1344  -0.0032 -0.0511 317 LEU C CB  
6915  C CG  . LEU C 16  ? 0.6018 0.4821 0.4565 0.1224  -0.0072 -0.0514 317 LEU C CG  
6916  C CD1 . LEU C 16  ? 0.5412 0.4230 0.4084 0.1058  -0.0091 -0.0421 317 LEU C CD1 
6917  C CD2 . LEU C 16  ? 0.6059 0.4462 0.4365 0.1349  -0.0111 -0.0571 317 LEU C CD2 
6918  N N   . THR C 17  ? 0.6209 0.6050 0.5085 0.1733  0.0037  -0.0591 318 THR C N   
6919  C CA  . THR C 17  ? 0.5907 0.6213 0.4956 0.1826  0.0079  -0.0592 318 THR C CA  
6920  C C   . THR C 17  ? 0.6113 0.6592 0.5342 0.1774  0.0056  -0.0508 318 THR C C   
6921  O O   . THR C 17  ? 0.6917 0.7229 0.6099 0.1870  0.0008  -0.0501 318 THR C O   
6922  C CB  . THR C 17  ? 0.6973 0.7295 0.5910 0.2092  0.0086  -0.0685 318 THR C CB  
6923  O OG1 . THR C 17  ? 0.7298 0.7232 0.5980 0.2142  0.0079  -0.0766 318 THR C OG1 
6924  C CG2 . THR C 17  ? 0.7016 0.7861 0.6101 0.2159  0.0151  -0.0710 318 THR C CG2 
6925  N N   . ASP C 18  ? 0.5211 0.6014 0.4626 0.1622  0.0089  -0.0447 319 ASP C N   
6926  C CA  . ASP C 18  ? 0.5018 0.5948 0.4587 0.1520  0.0069  -0.0367 319 ASP C CA  
6927  C C   . ASP C 18  ? 0.5554 0.6933 0.5274 0.1606  0.0089  -0.0370 319 ASP C C   
6928  O O   . ASP C 18  ? 0.4848 0.6572 0.4651 0.1584  0.0145  -0.0383 319 ASP C O   
6929  C CB  . ASP C 18  ? 0.5284 0.6240 0.4933 0.1289  0.0091  -0.0297 319 ASP C CB  
6930  C CG  . ASP C 18  ? 0.5062 0.6033 0.4820 0.1173  0.0065  -0.0222 319 ASP C CG  
6931  O OD1 . ASP C 18  ? 0.5096 0.6349 0.4971 0.1199  0.0066  -0.0208 319 ASP C OD1 
6932  O OD2 . ASP C 18  ? 0.5253 0.5974 0.4977 0.1054  0.0045  -0.0180 319 ASP C OD2 
6933  N N   . THR C 19  ? 0.5036 0.6426 0.4787 0.1698  0.0043  -0.0356 320 THR C N   
6934  C CA  . THR C 19  ? 0.5157 0.6998 0.5079 0.1732  0.0049  -0.0339 320 THR C CA  
6935  C C   . THR C 19  ? 0.5468 0.7329 0.5492 0.1583  0.0014  -0.0263 320 THR C C   
6936  O O   . THR C 19  ? 0.4791 0.7049 0.4968 0.1534  0.0025  -0.0240 320 THR C O   
6937  C CB  . THR C 19  ? 0.5620 0.7550 0.5496 0.2010  0.0022  -0.0397 320 THR C CB  
6938  O OG1 . THR C 19  ? 0.5968 0.7442 0.5683 0.2101  -0.0044 -0.0393 320 THR C OG1 
6939  C CG2 . THR C 19  ? 0.4470 0.6488 0.4266 0.2174  0.0068  -0.0483 320 THR C CG2 
6940  N N   . LEU C 20  ? 0.5934 0.7393 0.5871 0.1500  -0.0024 -0.0227 321 LEU C N   
6941  C CA  . LEU C 20  ? 0.5943 0.7401 0.5959 0.1362  -0.0054 -0.0161 321 LEU C CA  
6942  C C   . LEU C 20  ? 0.5783 0.7516 0.5937 0.1157  -0.0009 -0.0119 321 LEU C C   
6943  O O   . LEU C 20  ? 0.4116 0.6036 0.4368 0.1073  -0.0024 -0.0083 321 LEU C O   
6944  C CB  . LEU C 20  ? 0.5189 0.6185 0.5083 0.1289  -0.0087 -0.0132 321 LEU C CB  
6945  C CG  . LEU C 20  ? 0.4975 0.5914 0.4922 0.1143  -0.0112 -0.0070 321 LEU C CG  
6946  C CD1 . LEU C 20  ? 0.4173 0.5263 0.4160 0.1238  -0.0161 -0.0060 321 LEU C CD1 
6947  C CD2 . LEU C 20  ? 0.4352 0.4868 0.4176 0.1074  -0.0132 -0.0049 321 LEU C CD2 
6948  N N   . HIS C 21  ? 0.5305 0.7061 0.5452 0.1075  0.0043  -0.0123 322 HIS C N   
6949  C CA  . HIS C 21  ? 0.5284 0.7242 0.5523 0.0877  0.0087  -0.0076 322 HIS C CA  
6950  C C   . HIS C 21  ? 0.4817 0.7247 0.5192 0.0859  0.0105  -0.0077 322 HIS C C   
6951  O O   . HIS C 21  ? 0.5324 0.7898 0.5763 0.0672  0.0129  -0.0031 322 HIS C O   
6952  C CB  . HIS C 21  ? 0.5427 0.7362 0.5617 0.0827  0.0139  -0.0083 322 HIS C CB  
6953  C CG  . HIS C 21  ? 0.4111 0.6376 0.4329 0.0934  0.0181  -0.0135 322 HIS C CG  
6954  N ND1 . HIS C 21  ? 0.4480 0.6662 0.4608 0.1126  0.0177  -0.0206 322 HIS C ND1 
6955  C CD2 . HIS C 21  ? 0.3990 0.6681 0.4311 0.0880  0.0227  -0.0131 322 HIS C CD2 
6956  C CE1 . HIS C 21  ? 0.5245 0.7795 0.5422 0.1200  0.0223  -0.0247 322 HIS C CE1 
6957  N NE2 . HIS C 21  ? 0.5166 0.8050 0.5469 0.1048  0.0255  -0.0200 322 HIS C NE2 
6958  N N   . LEU C 22  ? 0.4233 0.6913 0.4641 0.1047  0.0095  -0.0128 323 LEU C N   
6959  C CA  . LEU C 22  ? 0.4838 0.8021 0.5390 0.1025  0.0108  -0.0127 323 LEU C CA  
6960  C C   . LEU C 22  ? 0.4994 0.8217 0.5610 0.0925  0.0060  -0.0085 323 LEU C C   
6961  O O   . LEU C 22  ? 0.5274 0.8900 0.6006 0.0828  0.0071  -0.0073 323 LEU C O   
6962  C CB  . LEU C 22  ? 0.5344 0.8805 0.5918 0.1282  0.0105  -0.0195 323 LEU C CB  
6963  C CG  . LEU C 22  ? 0.5725 0.9214 0.6239 0.1364  0.0163  -0.0245 323 LEU C CG  
6964  C CD1 . LEU C 22  ? 0.5370 0.8978 0.5846 0.1662  0.0155  -0.0323 323 LEU C CD1 
6965  C CD2 . LEU C 22  ? 0.5877 0.9765 0.6490 0.1191  0.0234  -0.0226 323 LEU C CD2 
6966  N N   . LYS C 23  ? 0.5100 0.7923 0.5633 0.0925  0.0011  -0.0063 324 LYS C N   
6967  C CA  . LYS C 23  ? 0.5169 0.7976 0.5737 0.0813  -0.0031 -0.0024 324 LYS C CA  
6968  C C   . LYS C 23  ? 0.6223 0.8854 0.6773 0.0565  -0.0005 0.0025  324 LYS C C   
6969  O O   . LYS C 23  ? 0.6714 0.9270 0.7266 0.0461  -0.0036 0.0053  324 LYS C O   
6970  C CB  . LYS C 23  ? 0.4074 0.6540 0.4546 0.0943  -0.0097 -0.0022 324 LYS C CB  
6971  C CG  . LYS C 23  ? 0.5192 0.7763 0.5646 0.1201  -0.0136 -0.0062 324 LYS C CG  
6972  C CD  . LYS C 23  ? 0.6840 0.9627 0.7355 0.1239  -0.0195 -0.0045 324 LYS C CD  
6973  C CE  . LYS C 23  ? 0.7438 1.0812 0.8118 0.1201  -0.0177 -0.0056 324 LYS C CE  
6974  N NZ  . LYS C 23  ? 0.7453 1.1071 0.8184 0.1296  -0.0246 -0.0048 324 LYS C NZ  
6975  N N   . SER C 24  ? 0.6092 0.8635 0.6608 0.0479  0.0049  0.0036  325 SER C N   
6976  C CA  . SER C 24  ? 0.6592 0.8936 0.7068 0.0268  0.0074  0.0085  325 SER C CA  
6977  C C   . SER C 24  ? 0.6433 0.9035 0.6975 0.0087  0.0081  0.0109  325 SER C C   
6978  O O   . SER C 24  ? 0.6161 0.9182 0.6794 0.0072  0.0097  0.0094  325 SER C O   
6979  C CB  . SER C 24  ? 0.6884 0.9167 0.7313 0.0223  0.0131  0.0095  325 SER C CB  
6980  O OG  . SER C 24  ? 0.7186 0.9325 0.7571 0.0026  0.0158  0.0148  325 SER C OG  
6981  N N   . THR C 25  ? 0.7094 0.9453 0.7583 -0.0056 0.0068  0.0143  326 THR C N   
6982  C CA  . THR C 25  ? 0.8245 1.0800 0.8767 -0.0239 0.0067  0.0158  326 THR C CA  
6983  C C   . THR C 25  ? 0.8467 1.0911 0.8917 -0.0458 0.0119  0.0200  326 THR C C   
6984  O O   . THR C 25  ? 0.9625 1.2368 1.0111 -0.0602 0.0147  0.0207  326 THR C O   
6985  C CB  . THR C 25  ? 0.8205 1.0604 0.8704 -0.0247 0.0010  0.0157  326 THR C CB  
6986  O OG1 . THR C 25  ? 0.8324 1.0336 0.8747 -0.0130 -0.0011 0.0159  326 THR C OG1 
6987  C CG2 . THR C 25  ? 0.7774 1.0536 0.8372 -0.0145 -0.0039 0.0128  326 THR C CG2 
6988  N N   . LEU C 26  ? 0.7422 0.9453 0.7762 -0.0486 0.0133  0.0229  327 LEU C N   
6989  C CA  . LEU C 26  ? 0.7615 0.9483 0.7854 -0.0681 0.0175  0.0275  327 LEU C CA  
6990  C C   . LEU C 26  ? 0.7388 0.9109 0.7565 -0.0649 0.0218  0.0304  327 LEU C C   
6991  O O   . LEU C 26  ? 0.5780 0.7446 0.5977 -0.0483 0.0211  0.0286  327 LEU C O   
6992  C CB  . LEU C 26  ? 0.8356 0.9862 0.8490 -0.0768 0.0157  0.0291  327 LEU C CB  
6993  C CG  . LEU C 26  ? 0.8859 1.0123 0.8977 -0.0662 0.0111  0.0272  327 LEU C CG  
6994  C CD1 . LEU C 26  ? 0.7852 0.8875 0.7860 -0.0813 0.0109  0.0284  327 LEU C CD1 
6995  C CD2 . LEU C 26  ? 0.9116 1.0605 0.9338 -0.0539 0.0059  0.0232  327 LEU C CD2 
6996  N N   . GLU C 27  ? 0.7101 0.8748 0.7184 -0.0821 0.0261  0.0351  328 GLU C N   
6997  C CA  . GLU C 27  ? 0.6425 0.7984 0.6439 -0.0816 0.0303  0.0389  328 GLU C CA  
6998  C C   . GLU C 27  ? 0.6169 0.7356 0.6113 -0.0697 0.0288  0.0403  328 GLU C C   
6999  O O   . GLU C 27  ? 0.6638 0.7559 0.6540 -0.0684 0.0261  0.0404  328 GLU C O   
7000  C CB  . GLU C 27  ? 0.5987 0.7492 0.5882 -0.1040 0.0347  0.0447  328 GLU C CB  
7001  C CG  . GLU C 27  ? 0.6143 0.8093 0.6109 -0.1171 0.0376  0.0439  328 GLU C CG  
7002  C CD  . GLU C 27  ? 0.7510 0.9377 0.7332 -0.1431 0.0417  0.0499  328 GLU C CD  
7003  O OE1 . GLU C 27  ? 0.8472 0.9902 0.8122 -0.1490 0.0424  0.0549  328 GLU C OE1 
7004  O OE2 . GLU C 27  ? 0.7617 0.9855 0.7486 -0.1577 0.0443  0.0496  328 GLU C OE2 
7005  N N   . THR C 28  ? 0.5867 0.7070 0.5802 -0.0608 0.0307  0.0410  329 THR C N   
7006  C CA  . THR C 28  ? 0.4932 0.5834 0.4796 -0.0515 0.0296  0.0429  329 THR C CA  
7007  C C   . THR C 28  ? 0.4597 0.5256 0.4317 -0.0618 0.0324  0.0502  329 THR C C   
7008  O O   . THR C 28  ? 0.5686 0.6068 0.5339 -0.0558 0.0310  0.0526  329 THR C O   
7009  C CB  . THR C 28  ? 0.5161 0.6181 0.5063 -0.0377 0.0298  0.0400  329 THR C CB  
7010  O OG1 . THR C 28  ? 0.4942 0.6187 0.4830 -0.0437 0.0343  0.0417  329 THR C OG1 
7011  C CG2 . THR C 28  ? 0.4947 0.6109 0.4952 -0.0241 0.0264  0.0328  329 THR C CG2 
7012  N N   . GLY C 29  ? 0.5038 0.5795 0.4699 -0.0769 0.0364  0.0542  330 GLY C N   
7013  C CA  . GLY C 29  ? 0.5962 0.6491 0.5458 -0.0860 0.0394  0.0620  330 GLY C CA  
7014  C C   . GLY C 29  ? 0.6656 0.7349 0.6126 -0.0856 0.0428  0.0648  330 GLY C C   
7015  O O   . GLY C 29  ? 0.6580 0.7183 0.5912 -0.0982 0.0463  0.0718  330 GLY C O   
7016  N N   . CYS C 30  ? 0.6363 0.7285 0.5945 -0.0720 0.0421  0.0594  331 CYS C N   
7017  C CA  . CYS C 30  ? 0.5248 0.6350 0.4805 -0.0705 0.0455  0.0607  331 CYS C CA  
7018  C C   . CYS C 30  ? 0.5857 0.7314 0.5454 -0.0829 0.0500  0.0602  331 CYS C C   
7019  O O   . CYS C 30  ? 0.5875 0.7503 0.5557 -0.0893 0.0497  0.0570  331 CYS C O   
7020  C CB  . CYS C 30  ? 0.3883 0.5086 0.3525 -0.0519 0.0431  0.0539  331 CYS C CB  
7021  S SG  . CYS C 30  ? 0.4695 0.5559 0.4311 -0.0387 0.0377  0.0536  331 CYS C SG  
7022  N N   . THR C 31  ? 0.5425 0.7015 0.4954 -0.0871 0.0544  0.0636  332 THR C N   
7023  C CA  . THR C 31  ? 0.4947 0.6959 0.4536 -0.0948 0.0593  0.0616  332 THR C CA  
7024  C C   . THR C 31  ? 0.5378 0.7568 0.4968 -0.0830 0.0615  0.0588  332 THR C C   
7025  O O   . THR C 31  ? 0.6460 0.8434 0.5993 -0.0715 0.0591  0.0591  332 THR C O   
7026  C CB  . THR C 31  ? 0.5665 0.7680 0.5128 -0.1194 0.0639  0.0700  332 THR C CB  
7027  O OG1 . THR C 31  ? 0.5152 0.6949 0.4437 -0.1230 0.0661  0.0782  332 THR C OG1 
7028  C CG2 . THR C 31  ? 0.5746 0.7506 0.5160 -0.1325 0.0616  0.0728  332 THR C CG2 
7029  N N   . GLU C 32  ? 0.5266 0.7874 0.4915 -0.0865 0.0665  0.0559  333 GLU C N   
7030  C CA  . GLU C 32  ? 0.5186 0.7980 0.4807 -0.0780 0.0699  0.0535  333 GLU C CA  
7031  C C   . GLU C 32  ? 0.5744 0.8267 0.5178 -0.0840 0.0710  0.0624  333 GLU C C   
7032  O O   . GLU C 32  ? 0.5050 0.7568 0.4440 -0.0725 0.0709  0.0602  333 GLU C O   
7033  C CB  . GLU C 32  ? 0.6400 0.9695 0.6085 -0.0857 0.0764  0.0512  333 GLU C CB  
7034  C CG  . GLU C 32  ? 0.8303 1.1954 0.8173 -0.0707 0.0756  0.0402  333 GLU C CG  
7035  C CD  . GLU C 32  ? 1.0112 1.3871 1.0095 -0.0791 0.0733  0.0397  333 GLU C CD  
7036  O OE1 . GLU C 32  ? 1.1021 1.5231 1.1138 -0.0762 0.0754  0.0341  333 GLU C OE1 
7037  O OE2 . GLU C 32  ? 0.9669 1.3085 0.9604 -0.0879 0.0694  0.0446  333 GLU C OE2 
7038  N N   . TYR C 33  ? 0.5269 0.7545 0.4575 -0.1013 0.0715  0.0725  334 TYR C N   
7039  C CA  . TYR C 33  ? 0.6507 0.8544 0.5615 -0.1072 0.0728  0.0823  334 TYR C CA  
7040  C C   . TYR C 33  ? 0.6990 0.8560 0.6006 -0.1007 0.0672  0.0872  334 TYR C C   
7041  O O   . TYR C 33  ? 0.7902 0.9264 0.6751 -0.1022 0.0672  0.0955  334 TYR C O   
7042  C CB  . TYR C 33  ? 0.6322 0.8397 0.5294 -0.1317 0.0784  0.0917  334 TYR C CB  
7043  C CG  . TYR C 33  ? 0.6997 0.9576 0.6042 -0.1396 0.0849  0.0882  334 TYR C CG  
7044  C CD1 . TYR C 33  ? 0.8428 1.1183 0.7379 -0.1411 0.0897  0.0909  334 TYR C CD1 
7045  C CD2 . TYR C 33  ? 0.6777 0.9685 0.5984 -0.1449 0.0863  0.0819  334 TYR C CD2 
7046  C CE1 . TYR C 33  ? 0.8599 1.1851 0.7619 -0.1477 0.0964  0.0872  334 TYR C CE1 
7047  C CE2 . TYR C 33  ? 0.7154 1.0573 0.6440 -0.1508 0.0924  0.0784  334 TYR C CE2 
7048  C CZ  . TYR C 33  ? 0.8424 1.2016 0.7618 -0.1522 0.0978  0.0809  334 TYR C CZ  
7049  O OH  . TYR C 33  ? 0.9590 1.3720 0.8865 -0.1575 0.1045  0.0769  334 TYR C OH  
7050  N N   . ILE C 34  ? 0.5983 0.7398 0.5097 -0.0929 0.0623  0.0827  335 ILE C N   
7051  C CA  . ILE C 34  ? 0.6307 0.7319 0.5340 -0.0860 0.0575  0.0869  335 ILE C CA  
7052  C C   . ILE C 34  ? 0.5931 0.6906 0.5117 -0.0717 0.0524  0.0783  335 ILE C C   
7053  O O   . ILE C 34  ? 0.6050 0.7156 0.5356 -0.0736 0.0521  0.0726  335 ILE C O   
7054  C CB  . ILE C 34  ? 0.7516 0.8218 0.6391 -0.1015 0.0584  0.0963  335 ILE C CB  
7055  C CG1 . ILE C 34  ? 0.7791 0.8091 0.6560 -0.0917 0.0540  0.1013  335 ILE C CG1 
7056  C CG2 . ILE C 34  ? 0.8560 0.9307 0.7523 -0.1112 0.0584  0.0922  335 ILE C CG2 
7057  C CD1 . ILE C 34  ? 0.8608 0.8565 0.7148 -0.1042 0.0556  0.1123  335 ILE C CD1 
7058  N N   . CYS C 35  ? 0.4536 0.5351 0.3713 -0.0579 0.0483  0.0775  336 CYS C N   
7059  C CA  . CYS C 35  ? 0.4593 0.5333 0.3884 -0.0457 0.0434  0.0706  336 CYS C CA  
7060  C C   . CYS C 35  ? 0.5180 0.5582 0.4401 -0.0453 0.0405  0.0760  336 CYS C C   
7061  O O   . CYS C 35  ? 0.5815 0.6035 0.4905 -0.0447 0.0402  0.0836  336 CYS C O   
7062  C CB  . CYS C 35  ? 0.3916 0.4737 0.3245 -0.0317 0.0409  0.0648  336 CYS C CB  
7063  S SG  . CYS C 35  ? 0.4553 0.5237 0.3984 -0.0191 0.0348  0.0579  336 CYS C SG  
7064  N N   . MET C 36  ? 0.3970 0.4296 0.3270 -0.0447 0.0384  0.0721  337 MET C N   
7065  C CA  . MET C 36  ? 0.4759 0.4782 0.4003 -0.0429 0.0360  0.0755  337 MET C CA  
7066  C C   . MET C 36  ? 0.4967 0.4963 0.4315 -0.0300 0.0316  0.0694  337 MET C C   
7067  O O   . MET C 36  ? 0.5891 0.5710 0.5240 -0.0285 0.0298  0.0693  337 MET C O   
7068  C CB  . MET C 36  ? 0.5099 0.5020 0.4309 -0.0558 0.0377  0.0768  337 MET C CB  
7069  C CG  . MET C 36  ? 0.6662 0.6542 0.5724 -0.0714 0.0420  0.0843  337 MET C CG  
7070  S SD  . MET C 36  ? 0.8565 0.8214 0.7528 -0.0878 0.0432  0.0864  337 MET C SD  
7071  C CE  . MET C 36  ? 0.8995 0.8627 0.7772 -0.1074 0.0485  0.0954  337 MET C CE  
7072  N N   . GLY C 37  ? 0.4988 0.5146 0.4404 -0.0214 0.0300  0.0644  338 GLY C N   
7073  C CA  . GLY C 37  ? 0.5163 0.5305 0.4663 -0.0116 0.0260  0.0584  338 GLY C CA  
7074  C C   . GLY C 37  ? 0.4800 0.4752 0.4264 -0.0059 0.0233  0.0617  338 GLY C C   
7075  O O   . GLY C 37  ? 0.4764 0.4691 0.4293 -0.0003 0.0204  0.0572  338 GLY C O   
7076  N N   . SER C 38  ? 0.4683 0.4508 0.4036 -0.0064 0.0242  0.0695  339 SER C N   
7077  C CA  . SER C 38  ? 0.4666 0.4334 0.3985 0.0009  0.0218  0.0728  339 SER C CA  
7078  C C   . SER C 38  ? 0.5533 0.4960 0.4762 -0.0022 0.0234  0.0777  339 SER C C   
7079  O O   . SER C 38  ? 0.6157 0.5436 0.5326 0.0053  0.0222  0.0816  339 SER C O   
7080  C CB  . SER C 38  ? 0.5679 0.5381 0.4927 0.0068  0.0204  0.0778  339 SER C CB  
7081  O OG  . SER C 38  ? 0.4968 0.4561 0.4075 0.0026  0.0229  0.0862  339 SER C OG  
7082  N N   . ILE C 39  ? 0.5393 0.4781 0.4601 -0.0129 0.0261  0.0774  340 ILE C N   
7083  C CA  . ILE C 39  ? 0.6314 0.5452 0.5428 -0.0177 0.0275  0.0801  340 ILE C CA  
7084  C C   . ILE C 39  ? 0.5519 0.4646 0.4734 -0.0146 0.0256  0.0734  340 ILE C C   
7085  O O   . ILE C 39  ? 0.5546 0.4857 0.4887 -0.0162 0.0246  0.0671  340 ILE C O   
7086  C CB  . ILE C 39  ? 0.6426 0.5546 0.5466 -0.0333 0.0310  0.0823  340 ILE C CB  
7087  C CG1 . ILE C 39  ? 0.6466 0.5616 0.5400 -0.0372 0.0331  0.0892  340 ILE C CG1 
7088  C CG2 . ILE C 39  ? 0.6544 0.5365 0.5454 -0.0398 0.0322  0.0846  340 ILE C CG2 
7089  C CD1 . ILE C 39  ? 0.6727 0.5587 0.5476 -0.0321 0.0330  0.0980  340 ILE C CD1 
7090  N N   . MET C 40  ? 0.6126 0.5033 0.5273 -0.0095 0.0253  0.0748  341 MET C N   
7091  C CA  . MET C 40  ? 0.6363 0.5278 0.5600 -0.0063 0.0237  0.0686  341 MET C CA  
7092  C C   . MET C 40  ? 0.6434 0.5337 0.5683 -0.0179 0.0247  0.0648  341 MET C C   
7093  O O   . MET C 40  ? 0.5953 0.4997 0.5320 -0.0179 0.0229  0.0590  341 MET C O   
7094  C CB  . MET C 40  ? 0.7396 0.6118 0.6563 0.0035  0.0235  0.0702  341 MET C CB  
7095  C CG  . MET C 40  ? 0.9004 0.7772 0.8268 0.0062  0.0222  0.0638  341 MET C CG  
7096  S SD  . MET C 40  ? 1.0425 0.9136 0.9682 0.0210  0.0216  0.0639  341 MET C SD  
7097  C CE  . MET C 40  ? 0.8814 0.7681 0.8092 0.0297  0.0198  0.0689  341 MET C CE  
7098  N N   . HIS C 41  ? 0.7046 0.5785 0.6165 -0.0285 0.0272  0.0681  342 HIS C N   
7099  C CA  . HIS C 41  ? 0.6695 0.5448 0.5813 -0.0422 0.0279  0.0648  342 HIS C CA  
7100  C C   . HIS C 41  ? 0.5635 0.4493 0.4715 -0.0553 0.0303  0.0681  342 HIS C C   
7101  O O   . HIS C 41  ? 0.5643 0.4305 0.4564 -0.0673 0.0327  0.0719  342 HIS C O   
7102  C CB  . HIS C 41  ? 0.6968 0.5408 0.5937 -0.0461 0.0290  0.0648  342 HIS C CB  
7103  C CG  . HIS C 41  ? 0.9153 0.7443 0.8104 -0.0314 0.0281  0.0640  342 HIS C CG  
7104  N ND1 . HIS C 41  ? 0.9553 0.7994 0.8646 -0.0231 0.0258  0.0588  342 HIS C ND1 
7105  C CD2 . HIS C 41  ? 1.0198 0.8210 0.8997 -0.0232 0.0293  0.0677  342 HIS C CD2 
7106  C CE1 . HIS C 41  ? 1.0012 0.8310 0.9057 -0.0115 0.0260  0.0592  342 HIS C CE1 
7107  N NE2 . HIS C 41  ? 1.0313 0.8355 0.9184 -0.0100 0.0280  0.0644  342 HIS C NE2 
7108  N N   . PRO C 42  ? 0.6230 0.5390 0.5439 -0.0543 0.0299  0.0662  343 PRO C N   
7109  C CA  . PRO C 42  ? 0.7289 0.6580 0.6458 -0.0660 0.0329  0.0697  343 PRO C CA  
7110  C C   . PRO C 42  ? 0.7380 0.6743 0.6535 -0.0834 0.0344  0.0681  343 PRO C C   
7111  O O   . PRO C 42  ? 0.6810 0.6119 0.5842 -0.0977 0.0375  0.0730  343 PRO C O   
7112  C CB  . PRO C 42  ? 0.7142 0.6749 0.6458 -0.0577 0.0321  0.0665  343 PRO C CB  
7113  C CG  . PRO C 42  ? 0.7008 0.6655 0.6448 -0.0448 0.0282  0.0603  343 PRO C CG  
7114  C CD  . PRO C 42  ? 0.6118 0.5511 0.5501 -0.0445 0.0271  0.0601  343 PRO C CD  
7115  N N   . SER C 43  ? 0.7855 0.7334 0.7119 -0.0838 0.0320  0.0618  344 SER C N   
7116  C CA  . SER C 43  ? 0.7592 0.7242 0.6878 -0.0999 0.0327  0.0594  344 SER C CA  
7117  C C   . SER C 43  ? 0.8164 0.7588 0.7367 -0.1072 0.0313  0.0572  344 SER C C   
7118  O O   . SER C 43  ? 0.6809 0.6070 0.6020 -0.0961 0.0290  0.0547  344 SER C O   
7119  C CB  . SER C 43  ? 0.6891 0.6946 0.6380 -0.0942 0.0307  0.0535  344 SER C CB  
7120  O OG  . SER C 43  ? 0.6796 0.7109 0.6316 -0.1098 0.0319  0.0525  344 SER C OG  
7121  N N   . GLN C 44  ? 0.8990 0.8417 0.8106 -0.1273 0.0329  0.0579  345 GLN C N   
7122  C CA  . GLN C 44  ? 0.9986 0.9274 0.9033 -0.1377 0.0314  0.0543  345 GLN C CA  
7123  C C   . GLN C 44  ? 0.9381 0.9063 0.8572 -0.1470 0.0293  0.0492  345 GLN C C   
7124  O O   . GLN C 44  ? 0.8153 0.7776 0.7287 -0.1589 0.0277  0.0460  345 GLN C O   
7125  C CB  . GLN C 44  ? 1.0677 0.9602 0.9466 -0.1554 0.0344  0.0586  345 GLN C CB  
7126  C CG  . GLN C 44  ? 1.1015 0.9546 0.9634 -0.1459 0.0364  0.0646  345 GLN C CG  
7127  C CD  . GLN C 44  ? 1.1669 0.9829 1.0005 -0.1643 0.0394  0.0695  345 GLN C CD  
7128  O OE1 . GLN C 44  ? 1.2190 1.0335 1.0432 -0.1734 0.0423  0.0761  345 GLN C OE1 
7129  N NE2 . GLN C 44  ? 1.1510 0.9353 0.9690 -0.1708 0.0388  0.0663  345 GLN C NE2 
7130  N N   . HIS C 45  ? 0.9151 0.9240 0.8520 -0.1413 0.0290  0.0482  346 HIS C N   
7131  C CA  . HIS C 45  ? 0.9262 0.9779 0.8788 -0.1457 0.0267  0.0435  346 HIS C CA  
7132  C C   . HIS C 45  ? 0.9028 0.9538 0.8626 -0.1359 0.0216  0.0382  346 HIS C C   
7133  O O   . HIS C 45  ? 0.7641 0.8162 0.7333 -0.1163 0.0194  0.0364  346 HIS C O   
7134  C CB  . HIS C 45  ? 0.8543 0.9451 0.8234 -0.1348 0.0275  0.0429  346 HIS C CB  
7135  C CG  . HIS C 45  ? 0.8673 1.0067 0.8508 -0.1409 0.0263  0.0393  346 HIS C CG  
7136  N ND1 . HIS C 45  ? 0.8641 1.0412 0.8642 -0.1263 0.0258  0.0365  346 HIS C ND1 
7137  C CD2 . HIS C 45  ? 0.8673 1.0252 0.8505 -0.1596 0.0254  0.0377  346 HIS C CD2 
7138  C CE1 . HIS C 45  ? 0.8485 1.0674 0.8591 -0.1341 0.0247  0.0337  346 HIS C CE1 
7139  N NE2 . HIS C 45  ? 0.8351 1.0449 0.8364 -0.1552 0.0242  0.0345  346 HIS C NE2 
7140  N N   . ALA C 46  ? 1.0205 1.0693 0.9745 -0.1504 0.0198  0.0357  347 ALA C N   
7141  C CA  . ALA C 46  ? 0.9438 0.9938 0.9029 -0.1436 0.0150  0.0309  347 ALA C CA  
7142  C C   . ALA C 46  ? 0.9422 1.0394 0.9157 -0.1487 0.0116  0.0274  347 ALA C C   
7143  O O   . ALA C 46  ? 0.9055 1.0301 0.8812 -0.1642 0.0133  0.0282  347 ALA C O   
7144  C CB  . ALA C 46  ? 0.9220 0.9333 0.8621 -0.1547 0.0149  0.0297  347 ALA C CB  
7145  N N   . ARG C 47  ? 0.9889 1.0972 0.9720 -0.1352 0.0066  0.0240  348 ARG C N   
7146  C CA  . ARG C 47  ? 0.9894 1.1445 0.9871 -0.1351 0.0025  0.0211  348 ARG C CA  
7147  C C   . ARG C 47  ? 1.0307 1.1952 1.0224 -0.1564 0.0001  0.0186  348 ARG C C   
7148  O O   . ARG C 47  ? 0.9781 1.1875 0.9807 -0.1633 -0.0021 0.0170  348 ARG C O   
7149  C CB  . ARG C 47  ? 0.9086 1.0700 0.9166 -0.1114 -0.0022 0.0191  348 ARG C CB  
7150  C CG  . ARG C 47  ? 0.8434 1.0197 0.8623 -0.0927 -0.0010 0.0200  348 ARG C CG  
7151  C CD  . ARG C 47  ? 0.8808 1.0388 0.9010 -0.0710 -0.0041 0.0193  348 ARG C CD  
7152  N NE  . ARG C 47  ? 1.0223 1.1919 1.0459 -0.0649 -0.0102 0.0171  348 ARG C NE  
7153  C CZ  . ARG C 47  ? 1.0323 1.2387 1.0670 -0.0551 -0.0140 0.0154  348 ARG C CZ  
7154  N NH1 . ARG C 47  ? 0.9984 1.2349 1.0426 -0.0504 -0.0118 0.0151  348 ARG C NH1 
7155  N NH2 . ARG C 47  ? 0.9224 1.1362 0.9581 -0.0492 -0.0201 0.0142  348 ARG C NH2 
7156  N N   . ARG C 48  ? 1.0585 1.1833 1.0327 -0.1671 0.0005  0.0178  349 ARG C N   
7157  C CA  . ARG C 48  ? 1.0339 1.1621 0.9983 -0.1903 -0.0014 0.0149  349 ARG C CA  
7158  C C   . ARG C 48  ? 1.0798 1.1604 1.0200 -0.2078 0.0032  0.0161  349 ARG C C   
7159  O O   . ARG C 48  ? 1.0857 1.1243 1.0158 -0.1968 0.0058  0.0177  349 ARG C O   
7160  C CB  . ARG C 48  ? 0.9231 1.0528 0.8884 -0.1842 -0.0074 0.0108  349 ARG C CB  
7161  C CG  . ARG C 48  ? 0.8049 0.9067 0.7703 -0.1607 -0.0082 0.0111  349 ARG C CG  
7162  C CD  . ARG C 48  ? 0.8670 0.9243 0.8131 -0.1663 -0.0074 0.0089  349 ARG C CD  
7163  N NE  . ARG C 48  ? 0.8563 0.9243 0.7980 -0.1770 -0.0123 0.0044  349 ARG C NE  
7164  C CZ  . ARG C 48  ? 1.0600 1.1263 0.9891 -0.2015 -0.0123 0.0016  349 ARG C CZ  
7165  N NH1 . ARG C 48  ? 1.1538 1.2059 1.0724 -0.2179 -0.0074 0.0034  349 ARG C NH1 
7166  N NH2 . ARG C 48  ? 1.1368 1.2146 1.0619 -0.2104 -0.0173 -0.0028 349 ARG C NH2 
7167  N N   . PRO C 49  ? 1.2069 1.2932 1.1364 -0.2350 0.0042  0.0154  350 PRO C N   
7168  C CA  . PRO C 49  ? 1.3575 1.3944 1.2602 -0.2526 0.0087  0.0170  350 PRO C CA  
7169  C C   . PRO C 49  ? 1.5236 1.5089 1.4065 -0.2492 0.0083  0.0138  350 PRO C C   
7170  O O   . PRO C 49  ? 1.5328 1.5174 1.4230 -0.2315 0.0051  0.0110  350 PRO C O   
7171  C CB  . PRO C 49  ? 1.3490 1.4095 1.2452 -0.2845 0.0085  0.0157  350 PRO C CB  
7172  C CG  . PRO C 49  ? 1.3094 1.4329 1.2302 -0.2816 0.0030  0.0125  350 PRO C CG  
7173  C CD  . PRO C 49  ? 1.2509 1.3924 1.1932 -0.2501 0.0021  0.0143  350 PRO C CD  
7174  N N   . GLU C 50  ? 1.6508 1.5917 1.5066 -0.2666 0.0119  0.0144  351 GLU C N   
7175  C CA  . GLU C 50  ? 1.6958 1.5796 1.5286 -0.2612 0.0134  0.0122  351 GLU C CA  
7176  C C   . GLU C 50  ? 1.6375 1.5212 1.4702 -0.2567 0.0091  0.0051  351 GLU C C   
7177  O O   . GLU C 50  ? 1.5765 1.4486 1.4144 -0.2340 0.0086  0.0042  351 GLU C O   
7178  C CB  . GLU C 50  ? 1.7869 1.6267 1.5875 -0.2857 0.0171  0.0128  351 GLU C CB  
7179  C CG  . GLU C 50  ? 1.8215 1.6556 1.6167 -0.2933 0.0217  0.0205  351 GLU C CG  
7180  C CD  . GLU C 50  ? 1.8698 1.6371 1.6321 -0.2952 0.0261  0.0235  351 GLU C CD  
7181  O OE1 . GLU C 50  ? 1.8914 1.6169 1.6313 -0.2976 0.0259  0.0185  351 GLU C OE1 
7182  O OE2 . GLU C 50  ? 1.8715 1.6276 1.6291 -0.2931 0.0298  0.0310  351 GLU C OE2 
7183  N N   . ASP C 51  ? 1.6290 1.5266 1.4550 -0.2793 0.0059  0.0003  352 ASP C N   
7184  C CA  . ASP C 51  ? 1.6447 1.5337 1.4627 -0.2806 0.0022  -0.0068 352 ASP C CA  
7185  C C   . ASP C 51  ? 1.6182 1.5660 1.4607 -0.2785 -0.0044 -0.0090 352 ASP C C   
7186  O O   . ASP C 51  ? 1.5859 1.5730 1.4536 -0.2641 -0.0057 -0.0049 352 ASP C O   
7187  C CB  . ASP C 51  ? 1.6864 1.5383 1.4725 -0.3084 0.0035  -0.0114 352 ASP C CB  
7188  C CG  . ASP C 51  ? 1.7070 1.4932 1.4657 -0.2997 0.0076  -0.0135 352 ASP C CG  
7189  O OD1 . ASP C 51  ? 1.6431 1.4163 1.4093 -0.2726 0.0096  -0.0110 352 ASP C OD1 
7190  O OD2 . ASP C 51  ? 1.7878 1.5355 1.5165 -0.3200 0.0089  -0.0179 352 ASP C OD2 
7191  N N   . VAL C 52  ? 1.6117 1.5643 1.4454 -0.2919 -0.0087 -0.0153 353 VAL C N   
7192  C CA  . VAL C 52  ? 1.5305 1.5363 1.3845 -0.2887 -0.0158 -0.0173 353 VAL C CA  
7193  C C   . VAL C 52  ? 1.4463 1.5068 1.3184 -0.3011 -0.0176 -0.0144 353 VAL C C   
7194  O O   . VAL C 52  ? 1.5057 1.5709 1.3666 -0.3293 -0.0167 -0.0157 353 VAL C O   
7195  C CB  . VAL C 52  ? 1.4986 1.4958 1.3359 -0.3031 -0.0200 -0.0248 353 VAL C CB  
7196  C CG1 . VAL C 52  ? 1.5679 1.5341 1.3768 -0.3348 -0.0174 -0.0287 353 VAL C CG1 
7197  C CG2 . VAL C 52  ? 1.4274 1.4844 1.2840 -0.3042 -0.0280 -0.0262 353 VAL C CG2 
7198  N N   . ALA C 53  ? 1.2430 1.3451 1.1420 -0.2801 -0.0198 -0.0107 354 ALA C N   
7199  C CA  . ALA C 53  ? 1.0091 1.1637 0.9273 -0.2856 -0.0203 -0.0076 354 ALA C CA  
7200  C C   . ALA C 53  ? 0.9005 1.1095 0.8282 -0.2997 -0.0271 -0.0111 354 ALA C C   
7201  O O   . ALA C 53  ? 0.8116 1.0263 0.7384 -0.2954 -0.0330 -0.0147 354 ALA C O   
7202  C CB  . ALA C 53  ? 0.9064 1.0811 0.8474 -0.2557 -0.0198 -0.0030 354 ALA C CB  
7203  N N   . THR C 54  ? 0.8398 1.0915 0.7766 -0.3169 -0.0264 -0.0098 355 THR C N   
7204  C CA  . THR C 54  ? 0.8363 1.1509 0.7865 -0.3284 -0.0331 -0.0125 355 THR C CA  
7205  C C   . THR C 54  ? 0.7455 1.1045 0.7220 -0.2970 -0.0384 -0.0107 355 THR C C   
7206  O O   . THR C 54  ? 0.7156 1.0570 0.6996 -0.2692 -0.0363 -0.0075 355 THR C O   
7207  C CB  . THR C 54  ? 0.8185 1.1707 0.7724 -0.3548 -0.0301 -0.0112 355 THR C CB  
7208  O OG1 . THR C 54  ? 0.8048 1.1653 0.7721 -0.3396 -0.0245 -0.0058 355 THR C OG1 
7209  C CG2 . THR C 54  ? 0.7758 1.0830 0.6997 -0.3891 -0.0261 -0.0131 355 THR C CG2 
7210  N N   . LYS C 55  ? 0.6231 1.0406 0.6126 -0.3017 -0.0455 -0.0129 356 LYS C N   
7211  C CA  . LYS C 55  ? 0.6075 1.0679 0.6199 -0.2712 -0.0511 -0.0110 356 LYS C CA  
7212  C C   . LYS C 55  ? 0.5958 1.0813 0.6269 -0.2536 -0.0467 -0.0069 356 LYS C C   
7213  O O   . LYS C 55  ? 0.4001 0.8770 0.4400 -0.2226 -0.0470 -0.0044 356 LYS C O   
7214  C CB  . LYS C 55  ? 0.6883 1.2115 0.7110 -0.2798 -0.0598 -0.0138 356 LYS C CB  
7215  C CG  . LYS C 55  ? 0.6782 1.2322 0.7177 -0.2461 -0.0671 -0.0119 356 LYS C CG  
7216  C CD  . LYS C 55  ? 0.6459 1.2154 0.6796 -0.2521 -0.0761 -0.0149 356 LYS C CD  
7217  C CE  . LYS C 55  ? 0.6648 1.3142 0.7151 -0.2617 -0.0827 -0.0162 356 LYS C CE  
7218  N NZ  . LYS C 55  ? 0.6432 1.3344 0.7117 -0.2275 -0.0903 -0.0132 356 LYS C NZ  
7219  N N   . ASP C 56  ? 0.5004 1.0173 0.5364 -0.2739 -0.0425 -0.0064 357 ASP C N   
7220  C CA  . ASP C 56  ? 0.6096 1.1552 0.6630 -0.2582 -0.0380 -0.0032 357 ASP C CA  
7221  C C   . ASP C 56  ? 0.5475 1.0360 0.5925 -0.2447 -0.0309 0.0001  357 ASP C C   
7222  O O   . ASP C 56  ? 0.5504 1.0553 0.6085 -0.2259 -0.0277 0.0024  357 ASP C O   
7223  C CB  . ASP C 56  ? 0.7166 1.3105 0.7758 -0.2857 -0.0345 -0.0032 357 ASP C CB  
7224  C CG  . ASP C 56  ? 0.8576 1.4063 0.8934 -0.3188 -0.0279 -0.0025 357 ASP C CG  
7225  O OD1 . ASP C 56  ? 0.9835 1.4816 0.9978 -0.3319 -0.0289 -0.0046 357 ASP C OD1 
7226  O OD2 . ASP C 56  ? 0.9470 1.5089 0.9840 -0.3308 -0.0213 0.0001  357 ASP C OD2 
7227  N N   . GLN C 57  ? 0.5236 0.9473 0.5467 -0.2529 -0.0286 -0.0001 358 GLN C N   
7228  C CA  . GLN C 57  ? 0.5645 0.9351 0.5801 -0.2373 -0.0230 0.0029  358 GLN C CA  
7229  C C   . GLN C 57  ? 0.6409 0.9933 0.6613 -0.2060 -0.0268 0.0031  358 GLN C C   
7230  O O   . GLN C 57  ? 0.6938 1.0421 0.7228 -0.1829 -0.0246 0.0056  358 GLN C O   
7231  C CB  . GLN C 57  ? 0.6718 0.9827 0.6612 -0.2586 -0.0186 0.0028  358 GLN C CB  
7232  C CG  . GLN C 57  ? 0.7998 1.1100 0.7809 -0.2836 -0.0121 0.0052  358 GLN C CG  
7233  C CD  . GLN C 57  ? 0.8992 1.1580 0.8515 -0.3101 -0.0097 0.0039  358 GLN C CD  
7234  O OE1 . GLN C 57  ? 0.9055 1.1190 0.8433 -0.3047 -0.0111 0.0016  358 GLN C OE1 
7235  N NE2 . GLN C 57  ? 0.9078 1.1726 0.8501 -0.3393 -0.0059 0.0053  358 GLN C NE2 
7236  N N   . LEU C 58  ? 0.7253 1.0658 0.7385 -0.2057 -0.0323 0.0005  359 LEU C N   
7237  C CA  . LEU C 58  ? 0.6777 0.9929 0.6910 -0.1793 -0.0352 0.0012  359 LEU C CA  
7238  C C   . LEU C 58  ? 0.5963 0.9552 0.6282 -0.1551 -0.0411 0.0021  359 LEU C C   
7239  O O   . LEU C 58  ? 0.5283 0.8707 0.5636 -0.1301 -0.0412 0.0042  359 LEU C O   
7240  C CB  . LEU C 58  ? 0.6225 0.9054 0.6190 -0.1877 -0.0382 -0.0017 359 LEU C CB  
7241  C CG  . LEU C 58  ? 0.5553 0.8118 0.5506 -0.1625 -0.0405 -0.0005 359 LEU C CG  
7242  C CD1 . LEU C 58  ? 0.4073 0.6239 0.3995 -0.1505 -0.0339 0.0024  359 LEU C CD1 
7243  C CD2 . LEU C 58  ? 0.4946 0.7267 0.4742 -0.1690 -0.0441 -0.0036 359 LEU C CD2 
7244  N N   . PHE C 59  ? 0.5769 0.9907 0.6195 -0.1617 -0.0463 0.0005  360 PHE C N   
7245  C CA  . PHE C 59  ? 0.5078 0.9605 0.5657 -0.1358 -0.0527 0.0015  360 PHE C CA  
7246  C C   . PHE C 59  ? 0.4837 0.9472 0.5540 -0.1128 -0.0493 0.0037  360 PHE C C   
7247  O O   . PHE C 59  ? 0.4716 0.9277 0.5446 -0.0853 -0.0526 0.0052  360 PHE C O   
7248  C CB  . PHE C 59  ? 0.3679 0.8842 0.4366 -0.1460 -0.0590 -0.0004 360 PHE C CB  
7249  C CG  . PHE C 59  ? 0.5277 1.0816 0.6096 -0.1169 -0.0665 0.0009  360 PHE C CG  
7250  C CD1 . PHE C 59  ? 0.5260 1.0653 0.6006 -0.1045 -0.0738 0.0017  360 PHE C CD1 
7251  C CD2 . PHE C 59  ? 0.4791 1.0799 0.5789 -0.1003 -0.0659 0.0016  360 PHE C CD2 
7252  C CE1 . PHE C 59  ? 0.5285 1.0977 0.6122 -0.0766 -0.0810 0.0037  360 PHE C CE1 
7253  C CE2 . PHE C 59  ? 0.5250 1.1562 0.6345 -0.0708 -0.0729 0.0029  360 PHE C CE2 
7254  C CZ  . PHE C 59  ? 0.5719 1.1859 0.6727 -0.0589 -0.0806 0.0043  360 PHE C CZ  
7255  N N   . PRO C 60  ? 0.4877 0.9688 0.5644 -0.1223 -0.0429 0.0039  361 PRO C N   
7256  C CA  . PRO C 60  ? 0.3540 0.8451 0.4413 -0.0991 -0.0395 0.0052  361 PRO C CA  
7257  C C   . PRO C 60  ? 0.4303 0.8661 0.5087 -0.0800 -0.0375 0.0070  361 PRO C C   
7258  O O   . PRO C 60  ? 0.4676 0.9073 0.5519 -0.0535 -0.0388 0.0075  361 PRO C O   
7259  C CB  . PRO C 60  ? 0.4656 0.9727 0.5554 -0.1199 -0.0320 0.0054  361 PRO C CB  
7260  C CG  . PRO C 60  ? 0.4785 1.0167 0.5677 -0.1488 -0.0342 0.0037  361 PRO C CG  
7261  C CD  . PRO C 60  ? 0.4754 0.9751 0.5501 -0.1546 -0.0390 0.0028  361 PRO C CD  
7262  N N   . LEU C 61  ? 0.4289 0.8130 0.4919 -0.0928 -0.0345 0.0077  362 LEU C N   
7263  C CA  . LEU C 61  ? 0.3376 0.6717 0.3921 -0.0768 -0.0330 0.0093  362 LEU C CA  
7264  C C   . LEU C 61  ? 0.4213 0.7472 0.4735 -0.0584 -0.0400 0.0096  362 LEU C C   
7265  O O   . LEU C 61  ? 0.3341 0.6423 0.3859 -0.0367 -0.0406 0.0109  362 LEU C O   
7266  C CB  . LEU C 61  ? 0.3494 0.6357 0.3884 -0.0947 -0.0282 0.0099  362 LEU C CB  
7267  C CG  . LEU C 61  ? 0.4701 0.7577 0.5071 -0.1139 -0.0213 0.0106  362 LEU C CG  
7268  C CD1 . LEU C 61  ? 0.4151 0.6556 0.4341 -0.1312 -0.0176 0.0111  362 LEU C CD1 
7269  C CD2 . LEU C 61  ? 0.4311 0.7204 0.4750 -0.0990 -0.0169 0.0124  362 LEU C CD2 
7270  N N   . ALA C 62  ? 0.4574 0.7948 0.5065 -0.0677 -0.0456 0.0085  363 ALA C N   
7271  C CA  . ALA C 62  ? 0.4737 0.8053 0.5193 -0.0509 -0.0526 0.0095  363 ALA C CA  
7272  C C   . ALA C 62  ? 0.4713 0.8358 0.5282 -0.0254 -0.0569 0.0106  363 ALA C C   
7273  O O   . ALA C 62  ? 0.3836 0.7249 0.4359 -0.0038 -0.0589 0.0126  363 ALA C O   
7274  C CB  . ALA C 62  ? 0.4962 0.8413 0.5367 -0.0667 -0.0580 0.0079  363 ALA C CB  
7275  N N   . LYS C 63  ? 0.4729 0.8914 0.5437 -0.0276 -0.0581 0.0092  364 LYS C N   
7276  C CA  . LYS C 63  ? 0.5095 0.9631 0.5913 -0.0015 -0.0618 0.0096  364 LYS C CA  
7277  C C   . LYS C 63  ? 0.5661 0.9921 0.6462 0.0179  -0.0571 0.0102  364 LYS C C   
7278  O O   . LYS C 63  ? 0.5590 0.9801 0.6374 0.0441  -0.0608 0.0112  364 LYS C O   
7279  C CB  . LYS C 63  ? 0.5674 1.0858 0.6655 -0.0097 -0.0616 0.0075  364 LYS C CB  
7280  C CG  . LYS C 63  ? 0.6125 1.1747 0.7225 0.0189  -0.0661 0.0073  364 LYS C CG  
7281  C CD  . LYS C 63  ? 0.6269 1.2510 0.7540 0.0122  -0.0629 0.0049  364 LYS C CD  
7282  C CE  . LYS C 63  ? 0.5433 1.2150 0.6822 0.0431  -0.0678 0.0043  364 LYS C CE  
7283  N NZ  . LYS C 63  ? 0.4553 1.0884 0.5862 0.0746  -0.0675 0.0051  364 LYS C NZ  
7284  N N   . GLU C 64  ? 0.5564 0.9621 0.6351 0.0051  -0.0491 0.0096  365 GLU C N   
7285  C CA  . GLU C 64  ? 0.6171 0.9964 0.6932 0.0209  -0.0445 0.0097  365 GLU C CA  
7286  C C   . GLU C 64  ? 0.4753 0.8044 0.5378 0.0348  -0.0472 0.0117  365 GLU C C   
7287  O O   . GLU C 64  ? 0.3789 0.6980 0.4386 0.0578  -0.0487 0.0118  365 GLU C O   
7288  C CB  . GLU C 64  ? 0.6736 1.0384 0.7488 0.0021  -0.0361 0.0095  365 GLU C CB  
7289  C CG  . GLU C 64  ? 0.8527 1.1871 0.9236 0.0144  -0.0312 0.0096  365 GLU C CG  
7290  C CD  . GLU C 64  ? 1.0443 1.3629 1.1123 -0.0054 -0.0237 0.0104  365 GLU C CD  
7291  O OE1 . GLU C 64  ? 1.0708 1.4073 1.1445 -0.0042 -0.0188 0.0096  365 GLU C OE1 
7292  O OE2 . GLU C 64  ? 1.1012 1.3898 1.1601 -0.0217 -0.0227 0.0119  365 GLU C OE2 
7293  N N   . PHE C 65  ? 0.5030 0.7997 0.5553 0.0208  -0.0476 0.0130  366 PHE C N   
7294  C CA  . PHE C 65  ? 0.5162 0.7669 0.5553 0.0309  -0.0491 0.0151  366 PHE C CA  
7295  C C   . PHE C 65  ? 0.5222 0.7783 0.5574 0.0503  -0.0572 0.0169  366 PHE C C   
7296  O O   . PHE C 65  ? 0.4787 0.7085 0.5054 0.0682  -0.0586 0.0183  366 PHE C O   
7297  C CB  . PHE C 65  ? 0.5334 0.7526 0.5630 0.0119  -0.0471 0.0157  366 PHE C CB  
7298  C CG  . PHE C 65  ? 0.6274 0.8066 0.6441 0.0201  -0.0489 0.0180  366 PHE C CG  
7299  C CD1 . PHE C 65  ? 0.5647 0.7136 0.5764 0.0295  -0.0457 0.0188  366 PHE C CD1 
7300  C CD2 . PHE C 65  ? 0.5544 0.7282 0.5634 0.0180  -0.0541 0.0193  366 PHE C CD2 
7301  C CE1 . PHE C 65  ? 0.5960 0.7104 0.5955 0.0351  -0.0472 0.0210  366 PHE C CE1 
7302  C CE2 . PHE C 65  ? 0.5749 0.7135 0.5713 0.0244  -0.0555 0.0217  366 PHE C CE2 
7303  C CZ  . PHE C 65  ? 0.5999 0.7092 0.5916 0.0324  -0.0520 0.0227  366 PHE C CZ  
7304  N N   . ILE C 66  ? 0.5074 0.7963 0.5469 0.0466  -0.0628 0.0170  367 ILE C N   
7305  C CA  . ILE C 66  ? 0.5595 0.8549 0.5940 0.0653  -0.0713 0.0195  367 ILE C CA  
7306  C C   . ILE C 66  ? 0.5623 0.8747 0.6013 0.0920  -0.0731 0.0192  367 ILE C C   
7307  O O   . ILE C 66  ? 0.4401 0.7301 0.4678 0.1129  -0.0775 0.0218  367 ILE C O   
7308  C CB  . ILE C 66  ? 0.5577 0.8916 0.5972 0.0545  -0.0771 0.0193  367 ILE C CB  
7309  C CG1 . ILE C 66  ? 0.4888 0.8012 0.5208 0.0284  -0.0749 0.0185  367 ILE C CG1 
7310  C CG2 . ILE C 66  ? 0.5858 0.9305 0.6201 0.0756  -0.0865 0.0226  367 ILE C CG2 
7311  C CD1 . ILE C 66  ? 0.5416 0.8073 0.5567 0.0311  -0.0765 0.0213  367 ILE C CD1 
7312  N N   . ASP C 67  ? 0.5914 0.9425 0.6451 0.0917  -0.0694 0.0160  368 ASP C N   
7313  C CA  . ASP C 67  ? 0.6106 0.9786 0.6686 0.1175  -0.0697 0.0146  368 ASP C CA  
7314  C C   . ASP C 67  ? 0.5894 0.9060 0.6340 0.1297  -0.0663 0.0147  368 ASP C C   
7315  O O   . ASP C 67  ? 0.4844 0.7854 0.5192 0.1543  -0.0703 0.0156  368 ASP C O   
7316  C CB  . ASP C 67  ? 0.6060 1.0224 0.6815 0.1104  -0.0644 0.0108  368 ASP C CB  
7317  C CG  . ASP C 67  ? 0.6510 1.1287 0.7406 0.1041  -0.0688 0.0103  368 ASP C CG  
7318  O OD1 . ASP C 67  ? 0.7122 1.1986 0.7985 0.1105  -0.0769 0.0126  368 ASP C OD1 
7319  O OD2 . ASP C 67  ? 0.6868 1.2059 0.7903 0.0919  -0.0643 0.0077  368 ASP C OD2 
7320  N N   . GLN C 68  ? 0.3492 0.6384 0.3920 0.1123  -0.0593 0.0139  369 GLN C N   
7321  C CA  . GLN C 68  ? 0.4430 0.6835 0.4729 0.1192  -0.0563 0.0140  369 GLN C CA  
7322  C C   . GLN C 68  ? 0.5592 0.7598 0.5717 0.1281  -0.0618 0.0176  369 GLN C C   
7323  O O   . GLN C 68  ? 0.5360 0.7130 0.5367 0.1480  -0.0640 0.0179  369 GLN C O   
7324  C CB  . GLN C 68  ? 0.5464 0.7674 0.5774 0.0965  -0.0489 0.0135  369 GLN C CB  
7325  C CG  . GLN C 68  ? 0.6330 0.8070 0.6519 0.0992  -0.0455 0.0136  369 GLN C CG  
7326  C CD  . GLN C 68  ? 0.7467 0.9057 0.7672 0.0777  -0.0390 0.0137  369 GLN C CD  
7327  O OE1 . GLN C 68  ? 0.8202 1.0042 0.8510 0.0642  -0.0352 0.0128  369 GLN C OE1 
7328  N NE2 . GLN C 68  ? 0.7692 0.8875 0.7786 0.0744  -0.0377 0.0152  369 GLN C NE2 
7329  N N   . TYR C 69  ? 0.5745 0.7661 0.5833 0.1133  -0.0642 0.0205  370 TYR C N   
7330  C CA  . TYR C 69  ? 0.5938 0.7472 0.5850 0.1188  -0.0687 0.0245  370 TYR C CA  
7331  C C   . TYR C 69  ? 0.5214 0.6815 0.5052 0.1437  -0.0766 0.0268  370 TYR C C   
7332  O O   . TYR C 69  ? 0.5485 0.6708 0.5148 0.1572  -0.0790 0.0292  370 TYR C O   
7333  C CB  . TYR C 69  ? 0.5800 0.7294 0.5690 0.0993  -0.0699 0.0266  370 TYR C CB  
7334  C CG  . TYR C 69  ? 0.5123 0.6330 0.4837 0.1066  -0.0757 0.0313  370 TYR C CG  
7335  C CD1 . TYR C 69  ? 0.5587 0.6332 0.5150 0.1064  -0.0737 0.0333  370 TYR C CD1 
7336  C CD2 . TYR C 69  ? 0.5177 0.6591 0.4869 0.1138  -0.0835 0.0340  370 TYR C CD2 
7337  C CE1 . TYR C 69  ? 0.6044 0.6521 0.5429 0.1116  -0.0787 0.0382  370 TYR C CE1 
7338  C CE2 . TYR C 69  ? 0.6398 0.7537 0.5910 0.1204  -0.0889 0.0391  370 TYR C CE2 
7339  C CZ  . TYR C 69  ? 0.6607 0.7269 0.5961 0.1188  -0.0863 0.0413  370 TYR C CZ  
7340  O OH  . TYR C 69  ? 0.6672 0.7057 0.5830 0.1238  -0.0913 0.0469  370 TYR C OH  
7341  N N   . TYR C 70  ? 0.4150 0.6225 0.4106 0.1498  -0.0809 0.0263  371 TYR C N   
7342  C CA  . TYR C 70  ? 0.5047 0.7207 0.4930 0.1762  -0.0888 0.0287  371 TYR C CA  
7343  C C   . TYR C 70  ? 0.6006 0.8099 0.5855 0.2000  -0.0872 0.0260  371 TYR C C   
7344  O O   . TYR C 70  ? 0.4630 0.6481 0.4312 0.2228  -0.0924 0.0286  371 TYR C O   
7345  C CB  . TYR C 70  ? 0.5546 0.8278 0.5571 0.1769  -0.0942 0.0289  371 TYR C CB  
7346  C CG  . TYR C 70  ? 0.5767 0.8429 0.5706 0.1672  -0.1003 0.0334  371 TYR C CG  
7347  C CD1 . TYR C 70  ? 0.5145 0.7671 0.4926 0.1871  -0.1088 0.0387  371 TYR C CD1 
7348  C CD2 . TYR C 70  ? 0.5950 0.8639 0.5937 0.1385  -0.0974 0.0324  371 TYR C CD2 
7349  C CE1 . TYR C 70  ? 0.5315 0.7771 0.5002 0.1780  -0.1142 0.0430  371 TYR C CE1 
7350  C CE2 . TYR C 70  ? 0.6275 0.8891 0.6165 0.1298  -0.1027 0.0358  371 TYR C CE2 
7351  C CZ  . TYR C 70  ? 0.5739 0.8251 0.5485 0.1493  -0.1110 0.0413  371 TYR C CZ  
7352  O OH  . TYR C 70  ? 0.6294 0.8739 0.5933 0.1409  -0.1162 0.0449  371 TYR C OH  
7353  N N   . SER C 71  ? 0.6161 0.8426 0.6140 0.1952  -0.0800 0.0209  372 SER C N   
7354  C CA  . SER C 71  ? 0.6320 0.8445 0.6236 0.2159  -0.0775 0.0174  372 SER C CA  
7355  C C   . SER C 71  ? 0.5923 0.7397 0.5612 0.2168  -0.0766 0.0190  372 SER C C   
7356  O O   . SER C 71  ? 0.6838 0.8039 0.6355 0.2394  -0.0797 0.0191  372 SER C O   
7357  C CB  . SER C 71  ? 0.7454 0.9873 0.7541 0.2071  -0.0694 0.0119  372 SER C CB  
7358  O OG  . SER C 71  ? 0.8321 1.1369 0.8604 0.2088  -0.0703 0.0102  372 SER C OG  
7359  N N   . SER C 72  ? 0.4856 0.6075 0.4528 0.1923  -0.0727 0.0204  373 SER C N   
7360  C CA  . SER C 72  ? 0.5103 0.5755 0.4575 0.1894  -0.0715 0.0219  373 SER C CA  
7361  C C   . SER C 72  ? 0.6386 0.6697 0.5629 0.2047  -0.0788 0.0268  373 SER C C   
7362  O O   . SER C 72  ? 0.6874 0.6729 0.5916 0.2107  -0.0787 0.0271  373 SER C O   
7363  C CB  . SER C 72  ? 0.5236 0.5750 0.4741 0.1616  -0.0671 0.0234  373 SER C CB  
7364  O OG  . SER C 72  ? 0.7127 0.7427 0.6512 0.1562  -0.0716 0.0287  373 SER C OG  
7365  N N   . ILE C 73  ? 0.5469 0.5979 0.4720 0.2103  -0.0855 0.0309  374 ILE C N   
7366  C CA  . ILE C 73  ? 0.6014 0.6184 0.5028 0.2232  -0.0928 0.0369  374 ILE C CA  
7367  C C   . ILE C 73  ? 0.5985 0.6313 0.4946 0.2548  -0.0994 0.0374  374 ILE C C   
7368  O O   . ILE C 73  ? 0.7232 0.7425 0.6035 0.2672  -0.1070 0.0434  374 ILE C O   
7369  C CB  . ILE C 73  ? 0.5727 0.5909 0.4727 0.2065  -0.0960 0.0424  374 ILE C CB  
7370  C CG1 . ILE C 73  ? 0.5738 0.6493 0.4937 0.2056  -0.0995 0.0421  374 ILE C CG1 
7371  C CG2 . ILE C 73  ? 0.5322 0.5315 0.4349 0.1786  -0.0893 0.0417  374 ILE C CG2 
7372  C CD1 . ILE C 73  ? 0.5806 0.6581 0.4964 0.1917  -0.1038 0.0470  374 ILE C CD1 
7373  N N   . LYS C 74  ? 0.6502 0.7111 0.5582 0.2692  -0.0967 0.0315  375 LYS C N   
7374  C CA  . LYS C 74  ? 0.7854 0.8611 0.6879 0.3027  -0.1020 0.0308  375 LYS C CA  
7375  C C   . LYS C 74  ? 0.8095 0.9311 0.7220 0.3113  -0.1097 0.0349  375 LYS C C   
7376  O O   . LYS C 74  ? 0.7637 0.8844 0.6635 0.3394  -0.1171 0.0379  375 LYS C O   
7377  C CB  . LYS C 74  ? 0.9113 0.9239 0.7801 0.3223  -0.1057 0.0333  375 LYS C CB  
7378  C CG  . LYS C 74  ? 0.9947 0.9577 0.8503 0.3102  -0.0990 0.0299  375 LYS C CG  
7379  C CD  . LYS C 74  ? 1.0601 1.0105 0.9058 0.3347  -0.0970 0.0233  375 LYS C CD  
7380  C CE  . LYS C 74  ? 1.0083 0.9197 0.8453 0.3194  -0.0899 0.0185  375 LYS C CE  
7381  N NZ  . LYS C 74  ? 0.8984 0.8438 0.7627 0.2927  -0.0824 0.0152  375 LYS C NZ  
7382  N N   . ARG C 75  ? 0.7985 0.9591 0.7318 0.2873  -0.1084 0.0351  376 ARG C N   
7383  C CA  . ARG C 75  ? 0.8237 1.0390 0.7708 0.2923  -0.1150 0.0372  376 ARG C CA  
7384  C C   . ARG C 75  ? 0.9846 1.2636 0.9597 0.2908  -0.1106 0.0308  376 ARG C C   
7385  O O   . ARG C 75  ? 1.0905 1.3828 1.0679 0.3134  -0.1090 0.0267  376 ARG C O   
7386  C CB  . ARG C 75  ? 0.7978 1.0117 0.7456 0.2663  -0.1172 0.0416  376 ARG C CB  
7387  C CG  . ARG C 75  ? 0.7739 0.9300 0.6929 0.2697  -0.1220 0.0487  376 ARG C CG  
7388  C CD  . ARG C 75  ? 1.0570 1.2165 0.9617 0.3020  -0.1321 0.0538  376 ARG C CD  
7389  N NE  . ARG C 75  ? 1.2094 1.3047 1.0814 0.3117  -0.1361 0.0605  376 ARG C NE  
7390  C CZ  . ARG C 75  ? 1.2291 1.2769 1.0811 0.3275  -0.1343 0.0597  376 ARG C CZ  
7391  N NH1 . ARG C 75  ? 1.1676 1.1564 0.9896 0.3293  -0.1364 0.0653  376 ARG C NH1 
7392  N NH2 . ARG C 75  ? 1.2783 1.3363 1.1405 0.3358  -0.1282 0.0520  376 ARG C NH2 
7393  N N   . PHE C 76  ? 0.9577 1.2741 0.9523 0.2636  -0.1082 0.0296  377 PHE C N   
7394  C CA  . PHE C 76  ? 0.9361 1.3138 0.9566 0.2563  -0.1037 0.0242  377 PHE C CA  
7395  C C   . PHE C 76  ? 0.8692 1.3074 0.9009 0.2795  -0.1105 0.0241  377 PHE C C   
7396  O O   . PHE C 76  ? 0.7370 1.1689 0.7597 0.3089  -0.1117 0.0232  377 PHE C O   
7397  C CB  . PHE C 76  ? 0.9782 1.3465 1.0027 0.2580  -0.0945 0.0185  377 PHE C CB  
7398  C CG  . PHE C 76  ? 0.9649 1.3973 1.0145 0.2503  -0.0896 0.0135  377 PHE C CG  
7399  C CD1 . PHE C 76  ? 0.9191 1.3663 0.9818 0.2170  -0.0837 0.0121  377 PHE C CD1 
7400  C CD2 . PHE C 76  ? 0.9733 1.4516 1.0321 0.2765  -0.0909 0.0103  377 PHE C CD2 
7401  C CE1 . PHE C 76  ? 0.8485 1.3535 0.9322 0.2075  -0.0792 0.0082  377 PHE C CE1 
7402  C CE2 . PHE C 76  ? 0.9388 1.4797 1.0207 0.2678  -0.0861 0.0060  377 PHE C CE2 
7403  C CZ  . PHE C 76  ? 0.8883 1.4420 0.9823 0.2321  -0.0802 0.0052  377 PHE C CZ  
7404  N N   . GLY C 77  ? 0.7870 1.2803 0.8368 0.2623  -0.1127 0.0240  378 GLY C N   
7405  C CA  . GLY C 77  ? 0.6931 1.2350 0.7502 0.2752  -0.1173 0.0241  378 GLY C CA  
7406  C C   . GLY C 77  ? 0.6452 1.1636 0.6846 0.2859  -0.1261 0.0303  378 GLY C C   
7407  O O   . GLY C 77  ? 0.6949 1.2516 0.7396 0.2905  -0.1295 0.0307  378 GLY C O   
7408  N N   . SER C 78  ? 0.6096 1.0666 0.6274 0.2892  -0.1295 0.0353  379 SER C N   
7409  C CA  . SER C 78  ? 0.6452 1.0739 0.6432 0.2979  -0.1375 0.0421  379 SER C CA  
7410  C C   . SER C 78  ? 0.6692 1.1362 0.6767 0.2767  -0.1431 0.0443  379 SER C C   
7411  O O   . SER C 78  ? 0.6412 1.1438 0.6666 0.2516  -0.1409 0.0410  379 SER C O   
7412  C CB  . SER C 78  ? 0.5272 0.8828 0.4995 0.2993  -0.1389 0.0470  379 SER C CB  
7413  O OG  . SER C 78  ? 0.5038 0.8415 0.4786 0.2651  -0.1339 0.0464  379 SER C OG  
7414  N N   . LYS C 79  ? 0.6684 1.1266 0.6621 0.2862  -0.1503 0.0497  380 LYS C N   
7415  C CA  . LYS C 79  ? 0.7176 1.2050 0.7158 0.2664  -0.1563 0.0520  380 LYS C CA  
7416  C C   . LYS C 79  ? 0.6883 1.1615 0.6868 0.2366  -0.1551 0.0517  380 LYS C C   
7417  O O   . LYS C 79  ? 0.7086 1.2202 0.7236 0.2101  -0.1529 0.0474  380 LYS C O   
7418  C CB  . LYS C 79  ? 0.7336 1.1945 0.7101 0.2812  -0.1643 0.0594  380 LYS C CB  
7419  C CG  . LYS C 79  ? 0.8680 1.3770 0.8525 0.2724  -0.1704 0.0604  380 LYS C CG  
7420  C CD  . LYS C 79  ? 0.9478 1.4596 0.9226 0.3001  -0.1753 0.0642  380 LYS C CD  
7421  C CE  . LYS C 79  ? 0.9691 1.5278 0.9617 0.3162  -0.1708 0.0583  380 LYS C CE  
7422  N NZ  . LYS C 79  ? 0.8923 1.5235 0.9090 0.2986  -0.1706 0.0539  380 LYS C NZ  
7423  N N   . ALA C 80  ? 0.6498 1.0541 0.6292 0.2330  -0.1504 0.0538  381 ALA C N   
7424  C CA  . ALA C 80  ? 0.6084 0.9822 0.5847 0.1998  -0.1440 0.0520  381 ALA C CA  
7425  C C   . ALA C 80  ? 0.5867 0.9791 0.5830 0.1778  -0.1341 0.0445  381 ALA C C   
7426  O O   . ALA C 80  ? 0.5142 0.9102 0.5153 0.1487  -0.1305 0.0416  381 ALA C O   
7427  C CB  . ALA C 80  ? 0.5982 0.8992 0.5506 0.2023  -0.1411 0.0559  381 ALA C CB  
7428  N N   . HIS C 81  ? 0.5900 0.9926 0.5962 0.1917  -0.1295 0.0412  382 HIS C N   
7429  C CA  . HIS C 81  ? 0.6217 1.0424 0.6456 0.1717  -0.1202 0.0348  382 HIS C CA  
7430  C C   . HIS C 81  ? 0.6436 1.1298 0.6870 0.1547  -0.1221 0.0317  382 HIS C C   
7431  O O   . HIS C 81  ? 0.6262 1.1150 0.6754 0.1246  -0.1169 0.0284  382 HIS C O   
7432  C CB  . HIS C 81  ? 0.6450 1.0651 0.6736 0.1924  -0.1155 0.0321  382 HIS C CB  
7433  C CG  . HIS C 81  ? 0.7736 1.2082 0.8178 0.1735  -0.1058 0.0265  382 HIS C CG  
7434  N ND1 . HIS C 81  ? 0.8050 1.2498 0.8566 0.1882  -0.1007 0.0229  382 HIS C ND1 
7435  C CD2 . HIS C 81  ? 0.7958 1.2339 0.8475 0.1416  -0.1000 0.0239  382 HIS C CD2 
7436  C CE1 . HIS C 81  ? 0.7849 1.2406 0.8483 0.1655  -0.0925 0.0190  382 HIS C CE1 
7437  N NE2 . HIS C 81  ? 0.7720 1.2223 0.8352 0.1373  -0.0920 0.0197  382 HIS C NE2 
7438  N N   . MET C 82  ? 0.5845 1.1242 0.6371 0.1737  -0.1296 0.0326  383 MET C N   
7439  C CA  . MET C 82  ? 0.5244 1.1322 0.5957 0.1571  -0.1321 0.0296  383 MET C CA  
7440  C C   . MET C 82  ? 0.5418 1.1460 0.6061 0.1312  -0.1361 0.0306  383 MET C C   
7441  O O   . MET C 82  ? 0.5114 1.1485 0.5866 0.1030  -0.1341 0.0265  383 MET C O   
7442  C CB  . MET C 82  ? 0.4729 1.1306 0.5526 0.1829  -0.1374 0.0302  383 MET C CB  
7443  C CG  . MET C 82  ? 0.5131 1.1766 0.5993 0.2053  -0.1307 0.0272  383 MET C CG  
7444  S SD  . MET C 82  ? 0.6284 1.3013 0.7300 0.1821  -0.1212 0.0219  383 MET C SD  
7445  C CE  . MET C 82  ? 0.8385 1.5260 0.9463 0.2102  -0.1135 0.0177  383 MET C CE  
7446  N N   . GLU C 83  ? 0.5958 1.1596 0.6404 0.1398  -0.1416 0.0357  384 GLU C N   
7447  C CA  . GLU C 83  ? 0.5501 1.1027 0.5848 0.1159  -0.1446 0.0363  384 GLU C CA  
7448  C C   . GLU C 83  ? 0.5168 1.0301 0.5481 0.0860  -0.1345 0.0322  384 GLU C C   
7449  O O   . GLU C 83  ? 0.5349 1.0644 0.5697 0.0576  -0.1332 0.0282  384 GLU C O   
7450  C CB  . GLU C 83  ? 0.6208 1.1342 0.6331 0.1331  -0.1517 0.0433  384 GLU C CB  
7451  C CG  . GLU C 83  ? 0.7367 1.2873 0.7459 0.1372  -0.1633 0.0468  384 GLU C CG  
7452  C CD  . GLU C 83  ? 0.8904 1.4248 0.8842 0.1721  -0.1718 0.0548  384 GLU C CD  
7453  O OE1 . GLU C 83  ? 0.9292 1.4032 0.9057 0.1829  -0.1687 0.0584  384 GLU C OE1 
7454  O OE2 . GLU C 83  ? 0.9592 1.5284 0.9573 0.1846  -0.1771 0.0562  384 GLU C OE2 
7455  N N   . ARG C 84  ? 0.5252 0.9860 0.5485 0.0925  -0.1275 0.0330  385 ARG C N   
7456  C CA  . ARG C 84  ? 0.5027 0.9251 0.5225 0.0680  -0.1180 0.0296  385 ARG C CA  
7457  C C   . ARG C 84  ? 0.5523 1.0086 0.5888 0.0465  -0.1121 0.0238  385 ARG C C   
7458  O O   . ARG C 84  ? 0.5837 1.0270 0.6171 0.0194  -0.1075 0.0205  385 ARG C O   
7459  C CB  . ARG C 84  ? 0.4767 0.8468 0.4877 0.0816  -0.1122 0.0314  385 ARG C CB  
7460  C CG  . ARG C 84  ? 0.5470 0.8737 0.5517 0.0606  -0.1035 0.0292  385 ARG C CG  
7461  C CD  . ARG C 84  ? 0.5441 0.8409 0.5322 0.0495  -0.1056 0.0310  385 ARG C CD  
7462  N NE  . ARG C 84  ? 0.6224 0.8801 0.6053 0.0320  -0.0967 0.0285  385 ARG C NE  
7463  C CZ  . ARG C 84  ? 0.6320 0.8883 0.6136 0.0077  -0.0933 0.0245  385 ARG C CZ  
7464  N NH1 . ARG C 84  ? 0.6939 0.9847 0.6781 -0.0047 -0.0982 0.0222  385 ARG C NH1 
7465  N NH2 . ARG C 84  ? 0.5183 0.7378 0.4945 -0.0038 -0.0853 0.0225  385 ARG C NH2 
7466  N N   . LEU C 85  ? 0.5787 1.0784 0.6315 0.0584  -0.1120 0.0226  386 LEU C N   
7467  C CA  . LEU C 85  ? 0.4741 1.0121 0.5424 0.0371  -0.1068 0.0178  386 LEU C CA  
7468  C C   . LEU C 85  ? 0.4953 1.0679 0.5655 0.0119  -0.1114 0.0156  386 LEU C C   
7469  O O   . LEU C 85  ? 0.5046 1.0679 0.5726 -0.0176 -0.1061 0.0120  386 LEU C O   
7470  C CB  . LEU C 85  ? 0.4786 1.0645 0.5640 0.0568  -0.1068 0.0171  386 LEU C CB  
7471  C CG  . LEU C 85  ? 0.4811 1.0532 0.5725 0.0581  -0.0969 0.0149  386 LEU C CG  
7472  C CD1 . LEU C 85  ? 0.4605 0.9619 0.5365 0.0530  -0.0909 0.0159  386 LEU C CD1 
7473  C CD2 . LEU C 85  ? 0.4989 1.0944 0.5981 0.0913  -0.0982 0.0154  386 LEU C CD2 
7474  N N   . GLU C 86  ? 0.4246 1.0358 0.4968 0.0232  -0.1215 0.0176  387 GLU C N   
7475  C CA  . GLU C 86  ? 0.5345 1.1811 0.6074 -0.0009 -0.1268 0.0151  387 GLU C CA  
7476  C C   . GLU C 86  ? 0.5195 1.1155 0.5732 -0.0229 -0.1252 0.0139  387 GLU C C   
7477  O O   . GLU C 86  ? 0.4482 1.0554 0.4997 -0.0529 -0.1244 0.0095  387 GLU C O   
7478  C CB  . GLU C 86  ? 0.6472 1.3421 0.7242 0.0188  -0.1389 0.0184  387 GLU C CB  
7479  C CG  . GLU C 86  ? 0.8704 1.6239 0.9673 0.0387  -0.1398 0.0184  387 GLU C CG  
7480  C CD  . GLU C 86  ? 1.0308 1.8326 1.1410 0.0122  -0.1344 0.0132  387 GLU C CD  
7481  O OE1 . GLU C 86  ? 1.0969 1.9241 1.2207 0.0155  -0.1273 0.0112  387 GLU C OE1 
7482  O OE2 . GLU C 86  ? 1.0696 1.8823 1.1747 -0.0125 -0.1369 0.0111  387 GLU C OE2 
7483  N N   . GLU C 87  ? 0.5217 1.0614 0.5600 -0.0090 -0.1242 0.0174  388 GLU C N   
7484  C CA  . GLU C 87  ? 0.6203 1.1140 0.6402 -0.0273 -0.1223 0.0161  388 GLU C CA  
7485  C C   . GLU C 87  ? 0.5541 1.0179 0.5722 -0.0515 -0.1117 0.0113  388 GLU C C   
7486  O O   . GLU C 87  ? 0.4536 0.9120 0.4637 -0.0780 -0.1104 0.0068  388 GLU C O   
7487  C CB  . GLU C 87  ? 0.6188 1.0639 0.6234 -0.0064 -0.1236 0.0215  388 GLU C CB  
7488  C CG  . GLU C 87  ? 0.4725 0.8728 0.4580 -0.0223 -0.1214 0.0203  388 GLU C CG  
7489  C CD  . GLU C 87  ? 0.6533 1.0089 0.6239 -0.0032 -0.1221 0.0261  388 GLU C CD  
7490  O OE1 . GLU C 87  ? 0.6961 1.0424 0.6702 0.0193  -0.1216 0.0301  388 GLU C OE1 
7491  O OE2 . GLU C 87  ? 0.7429 1.0724 0.6971 -0.0113 -0.1231 0.0265  388 GLU C OE2 
7492  N N   . VAL C 88  ? 0.5391 0.9822 0.5629 -0.0424 -0.1042 0.0121  389 VAL C N   
7493  C CA  . VAL C 88  ? 0.5497 0.9672 0.5719 -0.0635 -0.0945 0.0084  389 VAL C CA  
7494  C C   . VAL C 88  ? 0.5381 0.9972 0.5683 -0.0891 -0.0941 0.0040  389 VAL C C   
7495  O O   . VAL C 88  ? 0.4643 0.9019 0.4851 -0.1149 -0.0893 0.0002  389 VAL C O   
7496  C CB  . VAL C 88  ? 0.5257 0.9231 0.5543 -0.0481 -0.0877 0.0103  389 VAL C CB  
7497  C CG1 . VAL C 88  ? 0.5082 0.8905 0.5375 -0.0693 -0.0784 0.0072  389 VAL C CG1 
7498  C CG2 . VAL C 88  ? 0.4852 0.8326 0.5016 -0.0305 -0.0869 0.0139  389 VAL C CG2 
7499  N N   . ASN C 89  ? 0.5707 1.0899 0.6169 -0.0828 -0.0994 0.0045  390 ASN C N   
7500  C CA  . ASN C 89  ? 0.5891 1.1539 0.6436 -0.1087 -0.0992 0.0005  390 ASN C CA  
7501  C C   . ASN C 89  ? 0.5969 1.1567 0.6372 -0.1356 -0.1028 -0.0033 390 ASN C C   
7502  O O   . ASN C 89  ? 0.5471 1.0852 0.5778 -0.1635 -0.0971 -0.0073 390 ASN C O   
7503  C CB  . ASN C 89  ? 0.5861 1.2225 0.6606 -0.0946 -0.1054 0.0017  390 ASN C CB  
7504  C CG  . ASN C 89  ? 0.6830 1.3672 0.7701 -0.1186 -0.1020 -0.0016 390 ASN C CG  
7505  O OD1 . ASN C 89  ? 0.6535 1.3612 0.7373 -0.1468 -0.1047 -0.0051 390 ASN C OD1 
7506  N ND2 . ASN C 89  ? 0.8041 1.5027 0.9042 -0.1088 -0.0959 -0.0008 390 ASN C ND2 
7507  N N   . LYS C 90  ? 0.5282 1.1040 0.5644 -0.1272 -0.1122 -0.0022 391 LYS C N   
7508  C CA  . LYS C 90  ? 0.5345 1.1071 0.5560 -0.1524 -0.1160 -0.0065 391 LYS C CA  
7509  C C   . LYS C 90  ? 0.4296 0.9323 0.4298 -0.1655 -0.1089 -0.0092 391 LYS C C   
7510  O O   . LYS C 90  ? 0.7117 1.2027 0.6987 -0.1942 -0.1073 -0.0148 391 LYS C O   
7511  C CB  . LYS C 90  ? 0.6646 1.2613 0.6837 -0.1370 -0.1274 -0.0038 391 LYS C CB  
7512  C CG  . LYS C 90  ? 0.8675 1.5433 0.9039 -0.1370 -0.1359 -0.0037 391 LYS C CG  
7513  C CD  . LYS C 90  ? 0.9670 1.6689 1.0030 -0.1135 -0.1476 0.0009  391 LYS C CD  
7514  C CE  . LYS C 90  ? 1.0269 1.7884 1.0793 -0.1080 -0.1482 0.0014  391 LYS C CE  
7515  N NZ  . LYS C 90  ? 1.0727 1.8513 1.1242 -0.0808 -0.1568 0.0067  391 LYS C NZ  
7516  N N   . GLU C 91  ? 0.5054 0.9614 0.5012 -0.1449 -0.1043 -0.0056 392 GLU C N   
7517  C CA  . GLU C 91  ? 0.6349 1.0279 0.6120 -0.1540 -0.0973 -0.0080 392 GLU C CA  
7518  C C   . GLU C 91  ? 0.6381 1.0131 0.6119 -0.1774 -0.0886 -0.0120 392 GLU C C   
7519  O O   . GLU C 91  ? 0.5810 0.9181 0.5365 -0.1959 -0.0847 -0.0165 392 GLU C O   
7520  C CB  . GLU C 91  ? 0.6398 0.9941 0.6156 -0.1277 -0.0940 -0.0029 392 GLU C CB  
7521  C CG  . GLU C 91  ? 0.6528 0.9617 0.6091 -0.1270 -0.0933 -0.0035 392 GLU C CG  
7522  C CD  . GLU C 91  ? 0.7279 1.0078 0.6835 -0.1013 -0.0919 0.0022  392 GLU C CD  
7523  O OE1 . GLU C 91  ? 0.7830 1.0178 0.7255 -0.1023 -0.0865 0.0016  392 GLU C OE1 
7524  O OE2 . GLU C 91  ? 0.6372 0.9394 0.6043 -0.0804 -0.0960 0.0072  392 GLU C OE2 
7525  N N   . ILE C 92  ? 0.6801 1.0803 0.6697 -0.1761 -0.0854 -0.0104 393 ILE C N   
7526  C CA  . ILE C 92  ? 0.6757 1.0601 0.6607 -0.1994 -0.0776 -0.0132 393 ILE C CA  
7527  C C   . ILE C 92  ? 0.6795 1.0902 0.6579 -0.2315 -0.0805 -0.0185 393 ILE C C   
7528  O O   . ILE C 92  ? 0.7299 1.1042 0.6897 -0.2551 -0.0759 -0.0227 393 ILE C O   
7529  C CB  . ILE C 92  ? 0.7071 1.1116 0.7099 -0.1891 -0.0730 -0.0097 393 ILE C CB  
7530  C CG1 . ILE C 92  ? 0.5565 0.9216 0.5602 -0.1627 -0.0686 -0.0056 393 ILE C CG1 
7531  C CG2 . ILE C 92  ? 0.7567 1.1561 0.7550 -0.2163 -0.0661 -0.0119 393 ILE C CG2 
7532  C CD1 . ILE C 92  ? 0.5519 0.9451 0.5746 -0.1430 -0.0672 -0.0020 393 ILE C CD1 
7533  N N   . ASP C 93  ? 0.6981 1.1712 0.6898 -0.2326 -0.0887 -0.0185 394 ASP C N   
7534  C CA  . ASP C 93  ? 0.6263 1.1316 0.6124 -0.2643 -0.0928 -0.0238 394 ASP C CA  
7535  C C   . ASP C 93  ? 0.7715 1.2370 0.7321 -0.2810 -0.0945 -0.0291 394 ASP C C   
7536  O O   . ASP C 93  ? 0.8889 1.3557 0.8361 -0.3130 -0.0946 -0.0348 394 ASP C O   
7537  C CB  . ASP C 93  ? 0.5289 1.1099 0.5338 -0.2573 -0.1029 -0.0225 394 ASP C CB  
7538  C CG  . ASP C 93  ? 0.6587 1.2881 0.6887 -0.2418 -0.1017 -0.0184 394 ASP C CG  
7539  O OD1 . ASP C 93  ? 0.8031 1.4078 0.8390 -0.2175 -0.0968 -0.0144 394 ASP C OD1 
7540  O OD2 . ASP C 93  ? 0.7312 1.4136 0.7722 -0.2489 -0.1022 -0.0186 394 ASP C OD2 
7541  N N   . THR C 94  ? 0.7267 1.1579 0.6789 -0.2606 -0.0959 -0.0277 395 THR C N   
7542  C CA  . THR C 94  ? 0.8119 1.2133 0.7408 -0.2737 -0.0983 -0.0331 395 THR C CA  
7543  C C   . THR C 94  ? 0.8661 1.1941 0.7742 -0.2741 -0.0895 -0.0354 395 THR C C   
7544  O O   . THR C 94  ? 1.0121 1.3106 0.8976 -0.2899 -0.0895 -0.0415 395 THR C O   
7545  C CB  . THR C 94  ? 0.7545 1.1781 0.6864 -0.2534 -0.1076 -0.0302 395 THR C CB  
7546  O OG1 . THR C 94  ? 0.8323 1.2350 0.7717 -0.2210 -0.1056 -0.0236 395 THR C OG1 
7547  C CG2 . THR C 94  ? 0.6172 1.1156 0.5678 -0.2532 -0.1171 -0.0285 395 THR C CG2 
7548  N N   . THR C 95  ? 0.7035 1.0025 0.6180 -0.2570 -0.0822 -0.0310 396 THR C N   
7549  C CA  . THR C 95  ? 0.6563 0.8902 0.5527 -0.2561 -0.0738 -0.0329 396 THR C CA  
7550  C C   . THR C 95  ? 0.7296 0.9409 0.6292 -0.2578 -0.0650 -0.0308 396 THR C C   
7551  O O   . THR C 95  ? 0.7296 0.8886 0.6150 -0.2552 -0.0580 -0.0318 396 THR C O   
7552  C CB  . THR C 95  ? 0.6231 0.8330 0.5195 -0.2281 -0.0736 -0.0291 396 THR C CB  
7553  O OG1 . THR C 95  ? 0.7026 0.9168 0.6173 -0.2057 -0.0708 -0.0224 396 THR C OG1 
7554  C CG2 . THR C 95  ? 0.4970 0.7358 0.3948 -0.2198 -0.0829 -0.0282 396 THR C CG2 
7555  N N   . SER C 96  ? 0.7137 0.9638 0.6313 -0.2604 -0.0651 -0.0276 397 SER C N   
7556  C CA  . SER C 96  ? 0.7846 1.0180 0.7062 -0.2608 -0.0572 -0.0246 397 SER C CA  
7557  C C   . SER C 96  ? 0.7722 0.9790 0.7011 -0.2318 -0.0530 -0.0196 397 SER C C   
7558  O O   . SER C 96  ? 0.8181 1.0035 0.7475 -0.2305 -0.0461 -0.0172 397 SER C O   
7559  C CB  . SER C 96  ? 0.8246 1.0125 0.7220 -0.2862 -0.0509 -0.0289 397 SER C CB  
7560  O OG  . SER C 96  ? 0.8472 1.0624 0.7395 -0.3166 -0.0535 -0.0327 397 SER C OG  
7561  N N   . THR C 97  ? 0.6818 0.8894 0.6153 -0.2097 -0.0570 -0.0176 398 THR C N   
7562  C CA  . THR C 97  ? 0.6535 0.8415 0.5946 -0.1834 -0.0538 -0.0127 398 THR C CA  
7563  C C   . THR C 97  ? 0.6044 0.8221 0.5576 -0.1620 -0.0612 -0.0092 398 THR C C   
7564  O O   . THR C 97  ? 0.5168 0.7772 0.4766 -0.1657 -0.0684 -0.0098 398 THR C O   
7565  C CB  . THR C 97  ? 0.6453 0.7761 0.5685 -0.1812 -0.0480 -0.0143 398 THR C CB  
7566  O OG1 . THR C 97  ? 0.6639 0.7777 0.5950 -0.1595 -0.0442 -0.0096 398 THR C OG1 
7567  C CG2 . THR C 97  ? 0.6162 0.7357 0.5261 -0.1807 -0.0520 -0.0174 398 THR C CG2 
7568  N N   . TYR C 98  ? 0.5615 0.7575 0.5170 -0.1394 -0.0597 -0.0053 399 TYR C N   
7569  C CA  . TYR C 98  ? 0.5213 0.7336 0.4818 -0.1195 -0.0666 -0.0017 399 TYR C CA  
7570  C C   . TYR C 98  ? 0.5368 0.7086 0.4904 -0.1030 -0.0634 0.0011  399 TYR C C   
7571  O O   . TYR C 98  ? 0.5774 0.7160 0.5269 -0.1041 -0.0560 0.0007  399 TYR C O   
7572  C CB  . TYR C 98  ? 0.4550 0.7115 0.4346 -0.1055 -0.0707 0.0017  399 TYR C CB  
7573  C CG  . TYR C 98  ? 0.4832 0.7282 0.4719 -0.0893 -0.0657 0.0050  399 TYR C CG  
7574  C CD1 . TYR C 98  ? 0.4790 0.7258 0.4739 -0.0986 -0.0593 0.0040  399 TYR C CD1 
7575  C CD2 . TYR C 98  ? 0.4353 0.6672 0.4246 -0.0655 -0.0675 0.0091  399 TYR C CD2 
7576  C CE1 . TYR C 98  ? 0.5594 0.7966 0.5616 -0.0840 -0.0549 0.0066  399 TYR C CE1 
7577  C CE2 . TYR C 98  ? 0.5264 0.7473 0.5224 -0.0519 -0.0632 0.0114  399 TYR C CE2 
7578  C CZ  . TYR C 98  ? 0.5868 0.8116 0.5897 -0.0608 -0.0570 0.0099  399 TYR C CZ  
7579  O OH  . TYR C 98  ? 0.6806 0.8950 0.6891 -0.0474 -0.0529 0.0119  399 TYR C OH  
7580  N N   . GLN C 99  ? 0.5515 0.7274 0.5031 -0.0881 -0.0693 0.0044  400 GLN C N   
7581  C CA  . GLN C 99  ? 0.5316 0.6716 0.4740 -0.0758 -0.0671 0.0072  400 GLN C CA  
7582  C C   . GLN C 99  ? 0.4852 0.6310 0.4358 -0.0530 -0.0699 0.0130  400 GLN C C   
7583  O O   . GLN C 99  ? 0.5156 0.6934 0.4733 -0.0435 -0.0769 0.0153  400 GLN C O   
7584  C CB  . GLN C 99  ? 0.4533 0.5848 0.3803 -0.0800 -0.0710 0.0062  400 GLN C CB  
7585  C CG  . GLN C 99  ? 0.5178 0.6407 0.4330 -0.1022 -0.0686 -0.0006 400 GLN C CG  
7586  C CD  . GLN C 99  ? 0.7017 0.7875 0.6106 -0.1093 -0.0589 -0.0039 400 GLN C CD  
7587  O OE1 . GLN C 99  ? 0.6943 0.7525 0.6000 -0.0991 -0.0543 -0.0018 400 GLN C OE1 
7588  N NE2 . GLN C 99  ? 0.7942 0.8799 0.7004 -0.1273 -0.0561 -0.0088 400 GLN C NE2 
7589  N N   . LEU C 100 ? 0.5567 0.6712 0.5049 -0.0441 -0.0648 0.0152  401 LEU C N   
7590  C CA  . LEU C 100 ? 0.5730 0.6854 0.5256 -0.0240 -0.0667 0.0201  401 LEU C CA  
7591  C C   . LEU C 100 ? 0.5141 0.6123 0.4540 -0.0140 -0.0716 0.0244  401 LEU C C   
7592  O O   . LEU C 100 ? 0.5015 0.5763 0.4293 -0.0211 -0.0693 0.0239  401 LEU C O   
7593  C CB  . LEU C 100 ? 0.5210 0.6073 0.4760 -0.0207 -0.0592 0.0204  401 LEU C CB  
7594  C CG  . LEU C 100 ? 0.5362 0.6312 0.5020 -0.0281 -0.0538 0.0176  401 LEU C CG  
7595  C CD1 . LEU C 100 ? 0.6096 0.6773 0.5756 -0.0232 -0.0473 0.0186  401 LEU C CD1 
7596  C CD2 . LEU C 100 ? 0.3646 0.4963 0.3435 -0.0208 -0.0575 0.0180  401 LEU C CD2 
7597  N N   . LYS C 101 ? 0.4736 0.5853 0.4151 0.0031  -0.0781 0.0286  402 LYS C N   
7598  C CA  . LYS C 101 ? 0.4539 0.5445 0.3814 0.0152  -0.0821 0.0342  402 LYS C CA  
7599  C C   . LYS C 101 ? 0.5156 0.5676 0.4365 0.0164  -0.0756 0.0356  402 LYS C C   
7600  O O   . LYS C 101 ? 0.4936 0.5391 0.4229 0.0144  -0.0695 0.0331  402 LYS C O   
7601  C CB  . LYS C 101 ? 0.4583 0.5649 0.3875 0.0362  -0.0896 0.0386  402 LYS C CB  
7602  C CG  . LYS C 101 ? 0.5278 0.6782 0.4647 0.0385  -0.0970 0.0380  402 LYS C CG  
7603  C CD  . LYS C 101 ? 0.5797 0.7369 0.5070 0.0262  -0.1011 0.0378  402 LYS C CD  
7604  C CE  . LYS C 101 ? 0.6011 0.8059 0.5358 0.0291  -0.1097 0.0377  402 LYS C CE  
7605  N NZ  . LYS C 101 ? 0.7245 0.9429 0.6549 0.0082  -0.1113 0.0338  402 LYS C NZ  
7606  N N   . ASP C 102 ? 0.6045 0.6325 0.5096 0.0193  -0.0773 0.0399  403 ASP C N   
7607  C CA  . ASP C 102 ? 0.5339 0.5283 0.4315 0.0184  -0.0715 0.0415  403 ASP C CA  
7608  C C   . ASP C 102 ? 0.5524 0.5375 0.4542 0.0310  -0.0707 0.0430  403 ASP C C   
7609  O O   . ASP C 102 ? 0.6271 0.5971 0.5324 0.0271  -0.0642 0.0412  403 ASP C O   
7610  C CB  . ASP C 102 ? 0.6754 0.6493 0.5538 0.0191  -0.0742 0.0467  403 ASP C CB  
7611  C CG  . ASP C 102 ? 0.8059 0.7826 0.6778 0.0049  -0.0727 0.0442  403 ASP C CG  
7612  O OD1 . ASP C 102 ? 0.8073 0.7992 0.6884 -0.0054 -0.0698 0.0382  403 ASP C OD1 
7613  O OD2 . ASP C 102 ? 0.8563 0.8184 0.7121 0.0034  -0.0742 0.0482  403 ASP C OD2 
7614  N N   . THR C 103 ? 0.5763 0.5699 0.4766 0.0471  -0.0774 0.0461  404 THR C N   
7615  C CA  . THR C 103 ? 0.6458 0.6316 0.5488 0.0607  -0.0769 0.0465  404 THR C CA  
7616  C C   . THR C 103 ? 0.6212 0.6253 0.5428 0.0563  -0.0714 0.0409  404 THR C C   
7617  O O   . THR C 103 ? 0.5755 0.5634 0.4988 0.0564  -0.0663 0.0396  404 THR C O   
7618  C CB  . THR C 103 ? 0.6442 0.6413 0.5427 0.0806  -0.0854 0.0500  404 THR C CB  
7619  O OG1 . THR C 103 ? 0.6459 0.6847 0.5575 0.0803  -0.0891 0.0477  404 THR C OG1 
7620  C CG2 . THR C 103 ? 0.5807 0.5538 0.4574 0.0856  -0.0909 0.0567  404 THR C CG2 
7621  N N   . GLU C 104 ? 0.6022 0.6402 0.5366 0.0508  -0.0723 0.0377  405 GLU C N   
7622  C CA  . GLU C 104 ? 0.5087 0.5647 0.4590 0.0446  -0.0670 0.0330  405 GLU C CA  
7623  C C   . GLU C 104 ? 0.5824 0.6170 0.5328 0.0302  -0.0590 0.0309  405 GLU C C   
7624  O O   . GLU C 104 ? 0.5439 0.5760 0.5016 0.0300  -0.0540 0.0289  405 GLU C O   
7625  C CB  . GLU C 104 ? 0.4909 0.5856 0.4518 0.0369  -0.0696 0.0304  405 GLU C CB  
7626  C CG  . GLU C 104 ? 0.5334 0.6552 0.4951 0.0513  -0.0782 0.0327  405 GLU C CG  
7627  C CD  . GLU C 104 ? 0.5633 0.7252 0.5342 0.0404  -0.0813 0.0301  405 GLU C CD  
7628  O OE1 . GLU C 104 ? 0.5171 0.7128 0.4940 0.0519  -0.0876 0.0311  405 GLU C OE1 
7629  O OE2 . GLU C 104 ? 0.5814 0.7409 0.5524 0.0203  -0.0775 0.0270  405 GLU C OE2 
7630  N N   . LEU C 105 ? 0.5727 0.5931 0.5145 0.0189  -0.0577 0.0310  406 LEU C N   
7631  C CA  . LEU C 105 ? 0.4920 0.4926 0.4327 0.0078  -0.0502 0.0290  406 LEU C CA  
7632  C C   . LEU C 105 ? 0.5720 0.5485 0.5087 0.0144  -0.0474 0.0311  406 LEU C C   
7633  O O   . LEU C 105 ? 0.5523 0.5226 0.4946 0.0109  -0.0418 0.0293  406 LEU C O   
7634  C CB  . LEU C 105 ? 0.5031 0.4937 0.4336 -0.0029 -0.0495 0.0285  406 LEU C CB  
7635  C CG  . LEU C 105 ? 0.4878 0.4608 0.4166 -0.0129 -0.0418 0.0259  406 LEU C CG  
7636  C CD1 . LEU C 105 ? 0.4784 0.4617 0.4141 -0.0232 -0.0383 0.0213  406 LEU C CD1 
7637  C CD2 . LEU C 105 ? 0.5101 0.4683 0.4257 -0.0183 -0.0408 0.0263  406 LEU C CD2 
7638  N N   . ILE C 106 ? 0.5159 0.4775 0.4411 0.0231  -0.0515 0.0352  407 ILE C N   
7639  C CA  . ILE C 106 ? 0.5561 0.4931 0.4748 0.0267  -0.0492 0.0370  407 ILE C CA  
7640  C C   . ILE C 106 ? 0.6443 0.5861 0.5712 0.0356  -0.0484 0.0353  407 ILE C C   
7641  O O   . ILE C 106 ? 0.6113 0.5413 0.5397 0.0333  -0.0439 0.0341  407 ILE C O   
7642  C CB  . ILE C 106 ? 0.5161 0.4333 0.4173 0.0327  -0.0541 0.0421  407 ILE C CB  
7643  C CG1 . ILE C 106 ? 0.4222 0.3301 0.3139 0.0214  -0.0525 0.0437  407 ILE C CG1 
7644  C CG2 . ILE C 106 ? 0.4759 0.3692 0.3691 0.0390  -0.0535 0.0437  407 ILE C CG2 
7645  C CD1 . ILE C 106 ? 0.4752 0.3714 0.3490 0.0262  -0.0589 0.0495  407 ILE C CD1 
7646  N N   . TYR C 107 ? 0.6165 0.5784 0.5488 0.0461  -0.0528 0.0348  408 TYR C N   
7647  C CA  . TYR C 107 ? 0.5668 0.5373 0.5067 0.0560  -0.0520 0.0326  408 TYR C CA  
7648  C C   . TYR C 107 ? 0.5937 0.5770 0.5472 0.0461  -0.0456 0.0289  408 TYR C C   
7649  O O   . TYR C 107 ? 0.5516 0.5275 0.5073 0.0482  -0.0421 0.0275  408 TYR C O   
7650  C CB  . TYR C 107 ? 0.5269 0.5230 0.4709 0.0693  -0.0579 0.0327  408 TYR C CB  
7651  C CG  . TYR C 107 ? 0.6141 0.6284 0.5684 0.0794  -0.0565 0.0294  408 TYR C CG  
7652  C CD1 . TYR C 107 ? 0.6396 0.6372 0.5856 0.0950  -0.0577 0.0293  408 TYR C CD1 
7653  C CD2 . TYR C 107 ? 0.6151 0.6627 0.5858 0.0726  -0.0537 0.0263  408 TYR C CD2 
7654  C CE1 . TYR C 107 ? 0.7232 0.7387 0.6779 0.1051  -0.0560 0.0256  408 TYR C CE1 
7655  C CE2 . TYR C 107 ? 0.5905 0.6576 0.5704 0.0812  -0.0519 0.0234  408 TYR C CE2 
7656  C CZ  . TYR C 107 ? 0.7219 0.7740 0.6943 0.0982  -0.0529 0.0229  408 TYR C CZ  
7657  O OH  . TYR C 107 ? 0.8145 0.8873 0.7954 0.1076  -0.0507 0.0193  408 TYR C OH  
7658  N N   . GLY C 108 ? 0.5323 0.5330 0.4930 0.0347  -0.0443 0.0276  409 GLY C N   
7659  C CA  . GLY C 108 ? 0.4170 0.4265 0.3876 0.0247  -0.0385 0.0249  409 GLY C CA  
7660  C C   . GLY C 108 ? 0.5791 0.5648 0.5462 0.0185  -0.0330 0.0250  409 GLY C C   
7661  O O   . GLY C 108 ? 0.5680 0.5545 0.5407 0.0176  -0.0289 0.0238  409 GLY C O   
7662  N N   . ALA C 109 ? 0.5579 0.5249 0.5157 0.0143  -0.0327 0.0265  410 ALA C N   
7663  C CA  . ALA C 109 ? 0.5246 0.4739 0.4800 0.0092  -0.0276 0.0266  410 ALA C CA  
7664  C C   . ALA C 109 ? 0.4489 0.3878 0.4028 0.0165  -0.0274 0.0272  410 ALA C C   
7665  O O   . ALA C 109 ? 0.4687 0.4041 0.4262 0.0140  -0.0232 0.0264  410 ALA C O   
7666  C CB  . ALA C 109 ? 0.4217 0.3568 0.3674 0.0038  -0.0273 0.0279  410 ALA C CB  
7667  N N   . LYS C 110 ? 0.4237 0.3561 0.3705 0.0258  -0.0320 0.0287  411 LYS C N   
7668  C CA  . LYS C 110 ? 0.5087 0.4262 0.4502 0.0314  -0.0319 0.0287  411 LYS C CA  
7669  C C   . LYS C 110 ? 0.5676 0.4985 0.5184 0.0368  -0.0302 0.0258  411 LYS C C   
7670  O O   . LYS C 110 ? 0.5212 0.4435 0.4709 0.0371  -0.0278 0.0247  411 LYS C O   
7671  C CB  . LYS C 110 ? 0.5750 0.4763 0.5025 0.0402  -0.0373 0.0310  411 LYS C CB  
7672  C CG  . LYS C 110 ? 0.6035 0.4875 0.5187 0.0333  -0.0384 0.0345  411 LYS C CG  
7673  C CD  . LYS C 110 ? 0.5163 0.3797 0.4143 0.0419  -0.0440 0.0377  411 LYS C CD  
7674  C CE  . LYS C 110 ? 0.6171 0.4609 0.5009 0.0325  -0.0440 0.0417  411 LYS C CE  
7675  N NZ  . LYS C 110 ? 0.6370 0.4537 0.4999 0.0391  -0.0491 0.0456  411 LYS C NZ  
7676  N N   . HIS C 111 ? 0.5497 0.5039 0.5095 0.0398  -0.0312 0.0246  412 HIS C N   
7677  C CA  . HIS C 111 ? 0.5282 0.4988 0.4967 0.0447  -0.0292 0.0220  412 HIS C CA  
7678  C C   . HIS C 111 ? 0.6453 0.6239 0.6224 0.0338  -0.0236 0.0213  412 HIS C C   
7679  O O   . HIS C 111 ? 0.5981 0.5825 0.5793 0.0358  -0.0209 0.0198  412 HIS C O   
7680  C CB  . HIS C 111 ? 0.4323 0.4280 0.4065 0.0532  -0.0328 0.0211  412 HIS C CB  
7681  C CG  . HIS C 111 ? 0.5275 0.5152 0.4929 0.0697  -0.0376 0.0210  412 HIS C CG  
7682  N ND1 . HIS C 111 ? 0.5511 0.5509 0.5192 0.0828  -0.0377 0.0181  412 HIS C ND1 
7683  C CD2 . HIS C 111 ? 0.5597 0.5250 0.5111 0.0759  -0.0421 0.0235  412 HIS C CD2 
7684  C CE1 . HIS C 111 ? 0.6086 0.5924 0.5643 0.0976  -0.0424 0.0185  412 HIS C CE1 
7685  N NE2 . HIS C 111 ? 0.6141 0.5758 0.5590 0.0931  -0.0452 0.0222  412 HIS C NE2 
7686  N N   . ALA C 112 ? 0.6061 0.5833 0.5841 0.0228  -0.0219 0.0224  413 ALA C N   
7687  C CA  . ALA C 112 ? 0.6106 0.5873 0.5925 0.0138  -0.0167 0.0224  413 ALA C CA  
7688  C C   . ALA C 112 ? 0.5603 0.5203 0.5385 0.0146  -0.0142 0.0230  413 ALA C C   
7689  O O   . ALA C 112 ? 0.5273 0.4897 0.5088 0.0126  -0.0108 0.0230  413 ALA C O   
7690  C CB  . ALA C 112 ? 0.5282 0.5020 0.5084 0.0037  -0.0154 0.0229  413 ALA C CB  
7691  N N   . TRP C 113 ? 0.4362 0.3804 0.4067 0.0164  -0.0162 0.0239  414 TRP C N   
7692  C CA  . TRP C 113 ? 0.4477 0.3794 0.4142 0.0164  -0.0147 0.0241  414 TRP C CA  
7693  C C   . TRP C 113 ? 0.5600 0.4926 0.5258 0.0240  -0.0158 0.0222  414 TRP C C   
7694  O O   . TRP C 113 ? 0.5770 0.5089 0.5438 0.0230  -0.0134 0.0215  414 TRP C O   
7695  C CB  . TRP C 113 ? 0.3747 0.2905 0.3318 0.0143  -0.0164 0.0256  414 TRP C CB  
7696  C CG  . TRP C 113 ? 0.4450 0.3510 0.3982 0.0112  -0.0148 0.0258  414 TRP C CG  
7697  C CD1 . TRP C 113 ? 0.4084 0.3193 0.3663 0.0104  -0.0121 0.0250  414 TRP C CD1 
7698  C CD2 . TRP C 113 ? 0.4687 0.3604 0.4119 0.0072  -0.0160 0.0272  414 TRP C CD2 
7699  N NE1 . TRP C 113 ? 0.3790 0.2817 0.3313 0.0063  -0.0118 0.0254  414 TRP C NE1 
7700  C CE2 . TRP C 113 ? 0.4401 0.3310 0.3833 0.0035  -0.0140 0.0266  414 TRP C CE2 
7701  C CE3 . TRP C 113 ? 0.4705 0.3510 0.4038 0.0055  -0.0186 0.0291  414 TRP C CE3 
7702  C CZ2 . TRP C 113 ? 0.4450 0.3256 0.3794 -0.0032 -0.0144 0.0276  414 TRP C CZ2 
7703  C CZ3 . TRP C 113 ? 0.4281 0.2959 0.3515 -0.0011 -0.0187 0.0306  414 TRP C CZ3 
7704  C CH2 . TRP C 113 ? 0.5225 0.3913 0.4468 -0.0060 -0.0165 0.0296  414 TRP C CH2 
7705  N N   . ARG C 114 ? 0.4858 0.4206 0.4489 0.0326  -0.0194 0.0211  415 ARG C N   
7706  C CA  . ARG C 114 ? 0.5061 0.4403 0.4666 0.0417  -0.0202 0.0184  415 ARG C CA  
7707  C C   . ARG C 114 ? 0.6212 0.5750 0.5916 0.0415  -0.0166 0.0168  415 ARG C C   
7708  O O   . ARG C 114 ? 0.6254 0.5777 0.5936 0.0453  -0.0154 0.0145  415 ARG C O   
7709  C CB  . ARG C 114 ? 0.4796 0.4144 0.4352 0.0536  -0.0248 0.0176  415 ARG C CB  
7710  C CG  . ARG C 114 ? 0.4083 0.3309 0.3543 0.0649  -0.0265 0.0145  415 ARG C CG  
7711  C CD  . ARG C 114 ? 0.4046 0.3345 0.3483 0.0797  -0.0306 0.0137  415 ARG C CD  
7712  N NE  . ARG C 114 ? 0.5047 0.4183 0.4357 0.0930  -0.0324 0.0103  415 ARG C NE  
7713  C CZ  . ARG C 114 ? 0.5224 0.4349 0.4466 0.1095  -0.0365 0.0093  415 ARG C CZ  
7714  N NH1 . ARG C 114 ? 0.4590 0.3522 0.3689 0.1225  -0.0377 0.0056  415 ARG C NH1 
7715  N NH2 . ARG C 114 ? 0.4597 0.3900 0.3902 0.1135  -0.0395 0.0120  415 ARG C NH2 
7716  N N   . ASN C 115 ? 0.5362 0.5076 0.5158 0.0360  -0.0148 0.0180  416 ASN C N   
7717  C CA  . ASN C 115 ? 0.5035 0.4943 0.4912 0.0342  -0.0113 0.0172  416 ASN C CA  
7718  C C   . ASN C 115 ? 0.5105 0.4965 0.4993 0.0250  -0.0072 0.0193  416 ASN C C   
7719  O O   . ASN C 115 ? 0.4727 0.4716 0.4658 0.0222  -0.0040 0.0196  416 ASN C O   
7720  C CB  . ASN C 115 ? 0.3945 0.4077 0.3897 0.0315  -0.0117 0.0174  416 ASN C CB  
7721  C CG  . ASN C 115 ? 0.4838 0.5081 0.4792 0.0430  -0.0161 0.0156  416 ASN C CG  
7722  O OD1 . ASN C 115 ? 0.4501 0.4696 0.4409 0.0550  -0.0177 0.0133  416 ASN C OD1 
7723  N ND2 . ASN C 115 ? 0.4556 0.4942 0.4551 0.0398  -0.0184 0.0164  416 ASN C ND2 
7724  N N   . ALA C 116 ? 0.4446 0.4135 0.4289 0.0208  -0.0070 0.0210  417 ALA C N   
7725  C CA  . ALA C 116 ? 0.4845 0.4490 0.4693 0.0144  -0.0035 0.0233  417 ALA C CA  
7726  C C   . ALA C 116 ? 0.5473 0.5123 0.5310 0.0170  -0.0022 0.0228  417 ALA C C   
7727  O O   . ALA C 116 ? 0.5169 0.4719 0.4960 0.0180  -0.0034 0.0222  417 ALA C O   
7728  C CB  . ALA C 116 ? 0.4547 0.4053 0.4357 0.0109  -0.0038 0.0248  417 ALA C CB  
7729  N N   . SER C 117 ? 0.4800 0.4576 0.4669 0.0166  0.0002  0.0231  418 SER C N   
7730  C CA  A SER C 117 ? 0.5044 0.4852 0.4894 0.0199  0.0011  0.0218  418 SER C CA  
7731  C CA  B SER C 117 ? 0.4904 0.4716 0.4756 0.0197  0.0012  0.0219  418 SER C CA  
7732  C C   . SER C 117 ? 0.5181 0.4902 0.5001 0.0172  0.0018  0.0240  418 SER C C   
7733  O O   . SER C 117 ? 0.5523 0.5242 0.5308 0.0196  0.0013  0.0222  418 SER C O   
7734  C CB  A SER C 117 ? 0.4467 0.4447 0.4354 0.0187  0.0041  0.0223  418 SER C CB  
7735  C CB  B SER C 117 ? 0.4467 0.4443 0.4355 0.0176  0.0044  0.0229  418 SER C CB  
7736  O OG  A SER C 117 ? 0.4233 0.4208 0.4124 0.0109  0.0070  0.0268  418 SER C OG  
7737  O OG  B SER C 117 ? 0.4166 0.4285 0.4101 0.0186  0.0041  0.0213  418 SER C OG  
7738  N N   . ARG C 118 ? 0.5190 0.4848 0.5014 0.0130  0.0029  0.0273  419 ARG C N   
7739  C CA  . ARG C 118 ? 0.3654 0.3271 0.3459 0.0121  0.0036  0.0297  419 ARG C CA  
7740  C C   . ARG C 118 ? 0.4959 0.4508 0.4742 0.0120  0.0013  0.0283  419 ARG C C   
7741  O O   . ARG C 118 ? 0.4120 0.3683 0.3896 0.0113  0.0015  0.0299  419 ARG C O   
7742  C CB  . ARG C 118 ? 0.3445 0.3024 0.3249 0.0095  0.0063  0.0339  419 ARG C CB  
7743  C CG  . ARG C 118 ? 0.3592 0.3222 0.3388 0.0074  0.0088  0.0364  419 ARG C CG  
7744  C CD  . ARG C 118 ? 0.4435 0.3965 0.4187 0.0047  0.0114  0.0407  419 ARG C CD  
7745  N NE  . ARG C 118 ? 0.5034 0.4592 0.4750 0.0016  0.0138  0.0441  419 ARG C NE  
7746  C CZ  . ARG C 118 ? 0.6122 0.5569 0.5768 -0.0026 0.0162  0.0482  419 ARG C CZ  
7747  N NH1 . ARG C 118 ? 0.7518 0.6815 0.7124 -0.0032 0.0167  0.0485  419 ARG C NH1 
7748  N NH2 . ARG C 118 ? 0.6129 0.5598 0.5727 -0.0068 0.0184  0.0518  419 ARG C NH2 
7749  N N   . CYS C 119 ? 0.5280 0.4767 0.5045 0.0123  -0.0010 0.0258  420 CYS C N   
7750  C CA  . CYS C 119 ? 0.5190 0.4597 0.4917 0.0097  -0.0027 0.0254  420 CYS C CA  
7751  C C   . CYS C 119 ? 0.4425 0.3777 0.4085 0.0097  -0.0054 0.0223  420 CYS C C   
7752  O O   . CYS C 119 ? 0.4686 0.3981 0.4304 0.0136  -0.0072 0.0195  420 CYS C O   
7753  C CB  . CYS C 119 ? 0.5491 0.4831 0.5208 0.0091  -0.0039 0.0253  420 CYS C CB  
7754  S SG  . CYS C 119 ? 0.4889 0.4124 0.4535 0.0047  -0.0059 0.0252  420 CYS C SG  
7755  N N   . VAL C 120 ? 0.4276 0.3643 0.3916 0.0053  -0.0056 0.0227  421 VAL C N   
7756  C CA  . VAL C 120 ? 0.4473 0.3766 0.4024 0.0024  -0.0082 0.0194  421 VAL C CA  
7757  C C   . VAL C 120 ? 0.5000 0.4132 0.4461 -0.0017 -0.0106 0.0184  421 VAL C C   
7758  O O   . VAL C 120 ? 0.5061 0.4059 0.4408 -0.0037 -0.0131 0.0153  421 VAL C O   
7759  C CB  . VAL C 120 ? 0.4701 0.4107 0.4263 -0.0024 -0.0079 0.0201  421 VAL C CB  
7760  C CG1 . VAL C 120 ? 0.4114 0.3587 0.3710 -0.0078 -0.0071 0.0230  421 VAL C CG1 
7761  C CG2 . VAL C 120 ? 0.4096 0.3432 0.3553 -0.0063 -0.0106 0.0158  421 VAL C CG2 
7762  N N   . GLY C 121 ? 0.5580 0.4698 0.5065 -0.0031 -0.0100 0.0210  422 GLY C N   
7763  C CA  . GLY C 121 ? 0.5211 0.4184 0.4602 -0.0079 -0.0120 0.0213  422 GLY C CA  
7764  C C   . GLY C 121 ? 0.5975 0.4796 0.5296 -0.0018 -0.0146 0.0204  422 GLY C C   
7765  O O   . GLY C 121 ? 0.6431 0.5104 0.5653 -0.0052 -0.0166 0.0215  422 GLY C O   
7766  N N   . ARG C 122 ? 0.5830 0.4691 0.5192 0.0074  -0.0147 0.0188  423 ARG C N   
7767  C CA  . ARG C 122 ? 0.5379 0.4173 0.4709 0.0152  -0.0170 0.0185  423 ARG C CA  
7768  C C   . ARG C 122 ? 0.5536 0.4091 0.4697 0.0184  -0.0210 0.0167  423 ARG C C   
7769  O O   . ARG C 122 ? 0.6195 0.4699 0.5322 0.0272  -0.0234 0.0168  423 ARG C O   
7770  C CB  . ARG C 122 ? 0.4324 0.3268 0.3744 0.0237  -0.0159 0.0167  423 ARG C CB  
7771  C CG  . ARG C 122 ? 0.4095 0.3221 0.3646 0.0212  -0.0127 0.0190  423 ARG C CG  
7772  C CD  . ARG C 122 ? 0.4919 0.4194 0.4538 0.0272  -0.0115 0.0174  423 ARG C CD  
7773  N NE  . ARG C 122 ? 0.4771 0.4094 0.4393 0.0277  -0.0097 0.0157  423 ARG C NE  
7774  C CZ  . ARG C 122 ? 0.5067 0.4520 0.4727 0.0327  -0.0082 0.0138  423 ARG C CZ  
7775  N NH1 . ARG C 122 ? 0.3530 0.3099 0.3237 0.0377  -0.0085 0.0133  423 ARG C NH1 
7776  N NH2 . ARG C 122 ? 0.5361 0.4853 0.5010 0.0324  -0.0065 0.0125  423 ARG C NH2 
7777  N N   . ILE C 123 ? 0.5859 0.4259 0.4900 0.0117  -0.0219 0.0153  424 ILE C N   
7778  C CA  . ILE C 123 ? 0.5791 0.3903 0.4633 0.0146  -0.0257 0.0140  424 ILE C CA  
7779  C C   . ILE C 123 ? 0.6272 0.4257 0.5037 0.0115  -0.0278 0.0184  424 ILE C C   
7780  O O   . ILE C 123 ? 0.5584 0.3329 0.4186 0.0174  -0.0315 0.0187  424 ILE C O   
7781  C CB  . ILE C 123 ? 0.6094 0.4041 0.4795 0.0056  -0.0264 0.0111  424 ILE C CB  
7782  C CG1 . ILE C 123 ? 0.5347 0.2954 0.3815 0.0122  -0.0303 0.0082  424 ILE C CG1 
7783  C CG2 . ILE C 123 ? 0.4403 0.2355 0.3084 -0.0111 -0.0256 0.0141  424 ILE C CG2 
7784  C CD1 . ILE C 123 ? 0.6383 0.3814 0.4696 0.0046  -0.0310 0.0035  424 ILE C CD1 
7785  N N   . GLN C 124 ? 0.6214 0.4352 0.5084 0.0036  -0.0255 0.0219  425 GLN C N   
7786  C CA  . GLN C 124 ? 0.6592 0.4656 0.5403 -0.0005 -0.0266 0.0261  425 GLN C CA  
7787  C C   . GLN C 124 ? 0.6486 0.4660 0.5381 0.0090  -0.0275 0.0276  425 GLN C C   
7788  O O   . GLN C 124 ? 0.6961 0.5096 0.5811 0.0061  -0.0285 0.0310  425 GLN C O   
7789  C CB  . GLN C 124 ? 0.6773 0.4967 0.5648 -0.0139 -0.0231 0.0282  425 GLN C CB  
7790  C CG  . GLN C 124 ? 0.7131 0.5260 0.5922 -0.0261 -0.0225 0.0273  425 GLN C CG  
7791  C CD  . GLN C 124 ? 0.8246 0.6123 0.6828 -0.0358 -0.0249 0.0300  425 GLN C CD  
7792  O OE1 . GLN C 124 ? 0.9437 0.7264 0.7975 -0.0363 -0.0255 0.0337  425 GLN C OE1 
7793  N NE2 . GLN C 124 ? 0.9509 0.7214 0.7945 -0.0444 -0.0263 0.0282  425 GLN C NE2 
7794  N N   . TRP C 125 ? 0.5580 0.3901 0.4585 0.0192  -0.0272 0.0250  426 TRP C N   
7795  C CA  . TRP C 125 ? 0.5202 0.3710 0.4326 0.0243  -0.0271 0.0259  426 TRP C CA  
7796  C C   . TRP C 125 ? 0.6599 0.5012 0.5630 0.0287  -0.0313 0.0288  426 TRP C C   
7797  O O   . TRP C 125 ? 0.7059 0.5592 0.6152 0.0264  -0.0311 0.0306  426 TRP C O   
7798  C CB  . TRP C 125 ? 0.4833 0.3498 0.4054 0.0341  -0.0266 0.0227  426 TRP C CB  
7799  C CG  . TRP C 125 ? 0.4649 0.3210 0.3773 0.0474  -0.0306 0.0209  426 TRP C CG  
7800  C CD1 . TRP C 125 ? 0.5049 0.3451 0.4066 0.0526  -0.0314 0.0178  426 TRP C CD1 
7801  C CD2 . TRP C 125 ? 0.5053 0.3669 0.4168 0.0587  -0.0344 0.0218  426 TRP C CD2 
7802  N NE1 . TRP C 125 ? 0.5707 0.4041 0.4642 0.0677  -0.0352 0.0165  426 TRP C NE1 
7803  C CE2 . TRP C 125 ? 0.5661 0.4142 0.4663 0.0722  -0.0373 0.0193  426 TRP C CE2 
7804  C CE3 . TRP C 125 ? 0.5962 0.4734 0.5147 0.0588  -0.0360 0.0243  426 TRP C CE3 
7805  C CZ2 . TRP C 125 ? 0.5201 0.3717 0.4167 0.0877  -0.0416 0.0195  426 TRP C CZ2 
7806  C CZ3 . TRP C 125 ? 0.5784 0.4609 0.4939 0.0724  -0.0406 0.0247  426 TRP C CZ3 
7807  C CH2 . TRP C 125 ? 0.5787 0.4493 0.4838 0.0875  -0.0434 0.0225  426 TRP C CH2 
7808  N N   . SER C 126 ? 0.6455 0.4642 0.5321 0.0357  -0.0355 0.0293  427 SER C N   
7809  C CA  . SER C 126 ? 0.6685 0.4772 0.5443 0.0420  -0.0402 0.0328  427 SER C CA  
7810  C C   . SER C 126 ? 0.7694 0.5636 0.6340 0.0301  -0.0404 0.0373  427 SER C C   
7811  O O   . SER C 126 ? 0.9109 0.6985 0.7665 0.0337  -0.0442 0.0410  427 SER C O   
7812  C CB  . SER C 126 ? 0.6520 0.4379 0.5112 0.0556  -0.0447 0.0320  427 SER C CB  
7813  O OG  . SER C 126 ? 0.8022 0.5575 0.6431 0.0481  -0.0448 0.0323  427 SER C OG  
7814  N N   . LYS C 127 ? 0.7591 0.5511 0.6240 0.0165  -0.0364 0.0372  428 LYS C N   
7815  C CA  . LYS C 127 ? 0.7551 0.5374 0.6101 0.0038  -0.0356 0.0411  428 LYS C CA  
7816  C C   . LYS C 127 ? 0.8629 0.6706 0.7343 -0.0039 -0.0307 0.0406  428 LYS C C   
7817  O O   . LYS C 127 ? 1.0708 0.8852 0.9466 -0.0139 -0.0265 0.0399  428 LYS C O   
7818  C CB  . LYS C 127 ? 0.7382 0.4998 0.5792 -0.0065 -0.0349 0.0412  428 LYS C CB  
7819  C CG  . LYS C 127 ? 0.9626 0.7111 0.7889 -0.0201 -0.0346 0.0458  428 LYS C CG  
7820  C CD  . LYS C 127 ? 1.0693 0.8261 0.8988 -0.0359 -0.0300 0.0448  428 LYS C CD  
7821  C CE  . LYS C 127 ? 1.1232 0.8743 0.9404 -0.0507 -0.0287 0.0496  428 LYS C CE  
7822  N NZ  . LYS C 127 ? 1.1256 0.8397 0.9147 -0.0536 -0.0334 0.0539  428 LYS C NZ  
7823  N N   . LEU C 128 ? 0.7356 0.5582 0.6156 0.0014  -0.0313 0.0407  429 LEU C N   
7824  C CA  . LEU C 128 ? 0.6105 0.4534 0.5035 -0.0040 -0.0270 0.0394  429 LEU C CA  
7825  C C   . LEU C 128 ? 0.5633 0.4056 0.4492 -0.0063 -0.0286 0.0421  429 LEU C C   
7826  O O   . LEU C 128 ? 0.6400 0.4802 0.5213 0.0011  -0.0334 0.0435  429 LEU C O   
7827  C CB  . LEU C 128 ? 0.4239 0.2855 0.3330 0.0023  -0.0258 0.0360  429 LEU C CB  
7828  C CG  . LEU C 128 ? 0.3861 0.2637 0.3055 -0.0021 -0.0219 0.0344  429 LEU C CG  
7829  C CD1 . LEU C 128 ? 0.3533 0.2354 0.2785 -0.0081 -0.0162 0.0332  429 LEU C CD1 
7830  C CD2 . LEU C 128 ? 0.4693 0.3613 0.3994 0.0031  -0.0226 0.0320  429 LEU C CD2 
7831  N N   . GLN C 129 ? 0.5280 0.3742 0.4128 -0.0157 -0.0246 0.0427  430 GLN C N   
7832  C CA  . GLN C 129 ? 0.5656 0.4129 0.4433 -0.0188 -0.0254 0.0447  430 GLN C CA  
7833  C C   . GLN C 129 ? 0.5275 0.3927 0.4173 -0.0166 -0.0237 0.0410  430 GLN C C   
7834  O O   . GLN C 129 ? 0.6596 0.5348 0.5597 -0.0190 -0.0186 0.0377  430 GLN C O   
7835  C CB  . GLN C 129 ? 0.6330 0.4781 0.5031 -0.0299 -0.0212 0.0465  430 GLN C CB  
7836  C CG  . GLN C 129 ? 0.7319 0.5777 0.5922 -0.0343 -0.0213 0.0486  430 GLN C CG  
7837  C CD  . GLN C 129 ? 0.7444 0.5757 0.5902 -0.0298 -0.0284 0.0531  430 GLN C CD  
7838  O OE1 . GLN C 129 ? 0.7633 0.5759 0.5983 -0.0275 -0.0322 0.0565  430 GLN C OE1 
7839  N NE2 . GLN C 129 ? 0.8483 0.6872 0.6925 -0.0279 -0.0303 0.0530  430 GLN C NE2 
7840  N N   . VAL C 130 ? 0.5788 0.4473 0.4662 -0.0122 -0.0282 0.0415  431 VAL C N   
7841  C CA  . VAL C 130 ? 0.5723 0.4565 0.4688 -0.0123 -0.0274 0.0378  431 VAL C CA  
7842  C C   . VAL C 130 ? 0.6119 0.4973 0.4998 -0.0184 -0.0268 0.0377  431 VAL C C   
7843  O O   . VAL C 130 ? 0.7092 0.5897 0.5856 -0.0177 -0.0314 0.0413  431 VAL C O   
7844  C CB  . VAL C 130 ? 0.5929 0.4863 0.4942 -0.0043 -0.0330 0.0375  431 VAL C CB  
7845  C CG1 . VAL C 130 ? 0.5089 0.4188 0.4180 -0.0081 -0.0321 0.0335  431 VAL C CG1 
7846  C CG2 . VAL C 130 ? 0.6971 0.5901 0.6058 0.0026  -0.0333 0.0369  431 VAL C CG2 
7847  N N   . PHE C 131 ? 0.6091 0.5001 0.5011 -0.0235 -0.0211 0.0337  432 PHE C N   
7848  C CA  . PHE C 131 ? 0.5138 0.4066 0.3975 -0.0290 -0.0196 0.0321  432 PHE C CA  
7849  C C   . PHE C 131 ? 0.5915 0.4932 0.4791 -0.0298 -0.0211 0.0278  432 PHE C C   
7850  O O   . PHE C 131 ? 0.5616 0.4658 0.4570 -0.0308 -0.0173 0.0237  432 PHE C O   
7851  C CB  . PHE C 131 ? 0.4894 0.3815 0.3726 -0.0331 -0.0120 0.0297  432 PHE C CB  
7852  C CG  . PHE C 131 ? 0.5187 0.4057 0.3968 -0.0355 -0.0105 0.0339  432 PHE C CG  
7853  C CD1 . PHE C 131 ? 0.4106 0.2901 0.2753 -0.0384 -0.0143 0.0389  432 PHE C CD1 
7854  C CD2 . PHE C 131 ? 0.5080 0.3976 0.3936 -0.0356 -0.0058 0.0333  432 PHE C CD2 
7855  C CE1 . PHE C 131 ? 0.6765 0.5490 0.5342 -0.0431 -0.0130 0.0431  432 PHE C CE1 
7856  C CE2 . PHE C 131 ? 0.5648 0.4514 0.4452 -0.0403 -0.0047 0.0370  432 PHE C CE2 
7857  C CZ  . PHE C 131 ? 0.5585 0.4356 0.4245 -0.0449 -0.0081 0.0418  432 PHE C CZ  
7858  N N   . ASP C 132 ? 0.5531 0.4595 0.4342 -0.0300 -0.0270 0.0292  433 ASP C N   
7859  C CA  . ASP C 132 ? 0.5917 0.5092 0.4749 -0.0332 -0.0293 0.0251  433 ASP C CA  
7860  C C   . ASP C 132 ? 0.6248 0.5386 0.4994 -0.0409 -0.0247 0.0202  433 ASP C C   
7861  O O   . ASP C 132 ? 0.6862 0.5965 0.5492 -0.0432 -0.0247 0.0214  433 ASP C O   
7862  C CB  . ASP C 132 ? 0.4706 0.3978 0.3498 -0.0297 -0.0379 0.0286  433 ASP C CB  
7863  C CG  . ASP C 132 ? 0.5220 0.4658 0.4045 -0.0343 -0.0412 0.0246  433 ASP C CG  
7864  O OD1 . ASP C 132 ? 0.5088 0.4526 0.3939 -0.0418 -0.0367 0.0190  433 ASP C OD1 
7865  O OD2 . ASP C 132 ? 0.6663 0.6232 0.5476 -0.0304 -0.0486 0.0272  433 ASP C OD2 
7866  N N   . ALA C 133 ? 0.6448 0.5575 0.5234 -0.0447 -0.0205 0.0147  434 ALA C N   
7867  C CA  . ALA C 133 ? 0.5776 0.4828 0.4464 -0.0504 -0.0154 0.0088  434 ALA C CA  
7868  C C   . ALA C 133 ? 0.5166 0.4247 0.3833 -0.0578 -0.0172 0.0036  434 ALA C C   
7869  O O   . ALA C 133 ? 0.4466 0.3436 0.3066 -0.0622 -0.0122 -0.0023 434 ALA C O   
7870  C CB  . ALA C 133 ? 0.5072 0.4021 0.3784 -0.0472 -0.0073 0.0068  434 ALA C CB  
7871  N N   . ARG C 134 ? 0.4739 0.3970 0.3455 -0.0593 -0.0243 0.0056  435 ARG C N   
7872  C CA  . ARG C 134 ? 0.5436 0.4738 0.4143 -0.0687 -0.0264 0.0009  435 ARG C CA  
7873  C C   . ARG C 134 ? 0.5667 0.4956 0.4220 -0.0775 -0.0278 -0.0039 435 ARG C C   
7874  O O   . ARG C 134 ? 0.6617 0.5954 0.5133 -0.0879 -0.0297 -0.0086 435 ARG C O   
7875  C CB  . ARG C 134 ? 0.5892 0.5418 0.4713 -0.0668 -0.0335 0.0045  435 ARG C CB  
7876  C CG  . ARG C 134 ? 0.5738 0.5283 0.4701 -0.0599 -0.0318 0.0075  435 ARG C CG  
7877  C CD  . ARG C 134 ? 0.5215 0.5005 0.4280 -0.0561 -0.0386 0.0105  435 ARG C CD  
7878  N NE  . ARG C 134 ? 0.5047 0.4882 0.4091 -0.0458 -0.0441 0.0157  435 ARG C NE  
7879  C CZ  . ARG C 134 ? 0.4836 0.4886 0.3928 -0.0400 -0.0513 0.0185  435 ARG C CZ  
7880  N NH1 . ARG C 134 ? 0.4740 0.5024 0.3924 -0.0447 -0.0537 0.0162  435 ARG C NH1 
7881  N NH2 . ARG C 134 ? 0.4769 0.4804 0.3808 -0.0295 -0.0563 0.0238  435 ARG C NH2 
7882  N N   . ASP C 135 ? 0.5791 0.5022 0.4242 -0.0749 -0.0268 -0.0031 436 ASP C N   
7883  C CA  . ASP C 135 ? 0.5797 0.4997 0.4083 -0.0832 -0.0270 -0.0086 436 ASP C CA  
7884  C C   . ASP C 135 ? 0.6449 0.5433 0.4632 -0.0851 -0.0182 -0.0156 436 ASP C C   
7885  O O   . ASP C 135 ? 0.6074 0.4992 0.4097 -0.0918 -0.0170 -0.0217 436 ASP C O   
7886  C CB  . ASP C 135 ? 0.5376 0.4641 0.3582 -0.0800 -0.0309 -0.0040 436 ASP C CB  
7887  C CG  . ASP C 135 ? 0.6662 0.5818 0.4857 -0.0726 -0.0252 -0.0003 436 ASP C CG  
7888  O OD1 . ASP C 135 ? 0.6660 0.5730 0.4940 -0.0683 -0.0193 -0.0008 436 ASP C OD1 
7889  O OD2 . ASP C 135 ? 0.6935 0.6105 0.5032 -0.0717 -0.0267 0.0032  436 ASP C OD2 
7890  N N   . CYS C 136 ? 0.6106 0.4981 0.4366 -0.0785 -0.0121 -0.0148 437 CYS C N   
7891  C CA  . CYS C 136 ? 0.6535 0.5211 0.4698 -0.0767 -0.0036 -0.0209 437 CYS C CA  
7892  C C   . CYS C 136 ? 0.7306 0.5839 0.5347 -0.0865 -0.0026 -0.0290 437 CYS C C   
7893  O O   . CYS C 136 ? 0.7558 0.6141 0.5645 -0.0943 -0.0068 -0.0289 437 CYS C O   
7894  C CB  . CYS C 136 ? 0.5237 0.3858 0.3520 -0.0670 0.0015  -0.0176 437 CYS C CB  
7895  S SG  . CYS C 136 ? 0.6165 0.4606 0.4353 -0.0590 0.0118  -0.0230 437 CYS C SG  
7896  N N   . THR C 137 ? 0.6539 0.4893 0.4406 -0.0868 0.0031  -0.0364 438 THR C N   
7897  C CA  . THR C 137 ? 0.5619 0.3769 0.3319 -0.0966 0.0046  -0.0449 438 THR C CA  
7898  C C   . THR C 137 ? 0.6115 0.3978 0.3694 -0.0892 0.0135  -0.0508 438 THR C C   
7899  O O   . THR C 137 ? 0.6648 0.4282 0.4087 -0.0967 0.0149  -0.0569 438 THR C O   
7900  C CB  . THR C 137 ? 0.6947 0.5124 0.4476 -0.1074 0.0011  -0.0509 438 THR C CB  
7901  O OG1 . THR C 137 ? 0.6432 0.4493 0.3812 -0.1011 0.0074  -0.0562 438 THR C OG1 
7902  C CG2 . THR C 137 ? 0.6705 0.5179 0.4336 -0.1104 -0.0075 -0.0444 438 THR C CG2 
7903  N N   . THR C 138 ? 0.6557 0.4420 0.4170 -0.0751 0.0195  -0.0494 439 THR C N   
7904  C CA  . THR C 138 ? 0.6219 0.3834 0.3710 -0.0653 0.0279  -0.0552 439 THR C CA  
7905  C C   . THR C 138 ? 0.6380 0.4069 0.4033 -0.0502 0.0321  -0.0491 439 THR C C   
7906  O O   . THR C 138 ? 0.6687 0.4613 0.4520 -0.0477 0.0294  -0.0415 439 THR C O   
7907  C CB  . THR C 138 ? 0.7116 0.4656 0.4415 -0.0617 0.0331  -0.0633 439 THR C CB  
7908  O OG1 . THR C 138 ? 0.7013 0.4797 0.4419 -0.0539 0.0347  -0.0586 439 THR C OG1 
7909  C CG2 . THR C 138 ? 0.6269 0.3760 0.3392 -0.0772 0.0287  -0.0699 439 THR C CG2 
7910  N N   . ALA C 139 ? 0.7450 0.4919 0.5017 -0.0398 0.0386  -0.0530 440 ALA C N   
7911  C CA  . ALA C 139 ? 0.7094 0.4642 0.4795 -0.0244 0.0429  -0.0482 440 ALA C CA  
7912  C C   . ALA C 139 ? 0.6973 0.4777 0.4751 -0.0176 0.0456  -0.0463 440 ALA C C   
7913  O O   . ALA C 139 ? 0.7864 0.5868 0.5822 -0.0119 0.0455  -0.0393 440 ALA C O   
7914  C CB  . ALA C 139 ? 0.7041 0.4299 0.4597 -0.0126 0.0494  -0.0534 440 ALA C CB  
7915  N N   . HIS C 140 ? 0.7652 0.5454 0.5284 -0.0193 0.0481  -0.0526 441 HIS C N   
7916  C CA  . HIS C 140 ? 0.6939 0.4996 0.4624 -0.0161 0.0506  -0.0505 441 HIS C CA  
7917  C C   . HIS C 140 ? 0.5659 0.3938 0.3500 -0.0252 0.0435  -0.0412 441 HIS C C   
7918  O O   . HIS C 140 ? 0.5646 0.4122 0.3620 -0.0213 0.0445  -0.0351 441 HIS C O   
7919  C CB  . HIS C 140 ? 0.6424 0.4430 0.3900 -0.0186 0.0538  -0.0590 441 HIS C CB  
7920  C CG  . HIS C 140 ? 0.7311 0.5196 0.4653 -0.0040 0.0631  -0.0673 441 HIS C CG  
7921  N ND1 . HIS C 140 ? 0.7943 0.5492 0.5094 -0.0005 0.0657  -0.0759 441 HIS C ND1 
7922  C CD2 . HIS C 140 ? 0.7852 0.5911 0.5220 0.0089  0.0705  -0.0684 441 HIS C CD2 
7923  C CE1 . HIS C 140 ? 0.8521 0.6024 0.5576 0.0159  0.0742  -0.0821 441 HIS C CE1 
7924  N NE2 . HIS C 140 ? 0.7887 0.5724 0.5084 0.0221  0.0774  -0.0777 441 HIS C NE2 
7925  N N   . GLY C 141 ? 0.5465 0.3714 0.3281 -0.0374 0.0362  -0.0404 442 GLY C N   
7926  C CA  . GLY C 141 ? 0.5372 0.3800 0.3325 -0.0435 0.0291  -0.0316 442 GLY C CA  
7927  C C   . GLY C 141 ? 0.6424 0.4908 0.4567 -0.0385 0.0278  -0.0247 442 GLY C C   
7928  O O   . GLY C 141 ? 0.6818 0.5455 0.5072 -0.0382 0.0254  -0.0176 442 GLY C O   
7929  N N   . MET C 142 ? 0.5511 0.3852 0.3673 -0.0352 0.0293  -0.0267 443 MET C N   
7930  C CA  . MET C 142 ? 0.5683 0.4079 0.4014 -0.0299 0.0286  -0.0205 443 MET C CA  
7931  C C   . MET C 142 ? 0.6026 0.4549 0.4430 -0.0202 0.0337  -0.0180 443 MET C C   
7932  O O   . MET C 142 ? 0.6316 0.4970 0.4860 -0.0189 0.0318  -0.0116 443 MET C O   
7933  C CB  . MET C 142 ? 0.5362 0.3566 0.3669 -0.0279 0.0300  -0.0229 443 MET C CB  
7934  C CG  . MET C 142 ? 0.5228 0.3361 0.3509 -0.0394 0.0244  -0.0236 443 MET C CG  
7935  S SD  . MET C 142 ? 0.6764 0.4625 0.4966 -0.0387 0.0274  -0.0263 443 MET C SD  
7936  C CE  . MET C 142 ? 0.5734 0.3720 0.4146 -0.0305 0.0269  -0.0177 443 MET C CE  
7937  N N   . PHE C 143 ? 0.6253 0.4751 0.4555 -0.0135 0.0405  -0.0235 444 PHE C N   
7938  C CA  . PHE C 143 ? 0.5782 0.4455 0.4160 -0.0046 0.0457  -0.0215 444 PHE C CA  
7939  C C   . PHE C 143 ? 0.5839 0.4717 0.4263 -0.0118 0.0437  -0.0164 444 PHE C C   
7940  O O   . PHE C 143 ? 0.5770 0.4811 0.4313 -0.0105 0.0440  -0.0110 444 PHE C O   
7941  C CB  . PHE C 143 ? 0.6195 0.4808 0.4447 0.0060  0.0538  -0.0293 444 PHE C CB  
7942  C CG  . PHE C 143 ? 0.5984 0.4843 0.4304 0.0145  0.0597  -0.0282 444 PHE C CG  
7943  C CD1 . PHE C 143 ? 0.6042 0.5018 0.4500 0.0237  0.0613  -0.0244 444 PHE C CD1 
7944  C CD2 . PHE C 143 ? 0.5192 0.4194 0.3439 0.0125  0.0636  -0.0308 444 PHE C CD2 
7945  C CE1 . PHE C 143 ? 0.6144 0.5393 0.4674 0.0305  0.0666  -0.0236 444 PHE C CE1 
7946  C CE2 . PHE C 143 ? 0.6416 0.5687 0.4731 0.0188  0.0694  -0.0298 444 PHE C CE2 
7947  C CZ  . PHE C 143 ? 0.6472 0.5877 0.4934 0.0276  0.0708  -0.0262 444 PHE C CZ  
7948  N N   . ASN C 144 ? 0.6642 0.5503 0.4955 -0.0203 0.0412  -0.0178 445 ASN C N   
7949  C CA  . ASN C 144 ? 0.6311 0.5322 0.4629 -0.0278 0.0388  -0.0121 445 ASN C CA  
7950  C C   . ASN C 144 ? 0.6300 0.5340 0.4740 -0.0320 0.0319  -0.0039 445 ASN C C   
7951  O O   . ASN C 144 ? 0.5427 0.4585 0.3917 -0.0347 0.0317  0.0019  445 ASN C O   
7952  C CB  . ASN C 144 ? 0.6415 0.5379 0.4575 -0.0355 0.0364  -0.0149 445 ASN C CB  
7953  C CG  . ASN C 144 ? 0.7262 0.6343 0.5391 -0.0434 0.0333  -0.0081 445 ASN C CG  
7954  O OD1 . ASN C 144 ? 0.7990 0.7034 0.6084 -0.0500 0.0259  -0.0043 445 ASN C OD1 
7955  N ND2 . ASN C 144 ? 0.6692 0.5921 0.4825 -0.0429 0.0389  -0.0064 445 ASN C ND2 
7956  N N   . TYR C 145 ? 0.5713 0.4645 0.4191 -0.0332 0.0264  -0.0036 446 TYR C N   
7957  C CA  . TYR C 145 ? 0.6780 0.5734 0.5364 -0.0354 0.0200  0.0032  446 TYR C CA  
7958  C C   . TYR C 145 ? 0.6166 0.5179 0.4880 -0.0299 0.0225  0.0061  446 TYR C C   
7959  O O   . TYR C 145 ? 0.5327 0.4401 0.4097 -0.0323 0.0198  0.0118  446 TYR C O   
7960  C CB  . TYR C 145 ? 0.6253 0.5122 0.4852 -0.0374 0.0146  0.0020  446 TYR C CB  
7961  C CG  . TYR C 145 ? 0.6245 0.5123 0.4768 -0.0441 0.0080  0.0031  446 TYR C CG  
7962  C CD1 . TYR C 145 ? 0.4372 0.3306 0.2912 -0.0455 0.0023  0.0099  446 TYR C CD1 
7963  C CD2 . TYR C 145 ? 0.5303 0.4126 0.3728 -0.0487 0.0069  -0.0026 446 TYR C CD2 
7964  C CE1 . TYR C 145 ? 0.4605 0.3560 0.3076 -0.0494 -0.0044 0.0115  446 TYR C CE1 
7965  C CE2 . TYR C 145 ? 0.4599 0.3469 0.2965 -0.0545 0.0002  -0.0014 446 TYR C CE2 
7966  C CZ  . TYR C 145 ? 0.5469 0.4415 0.3864 -0.0538 -0.0056 0.0060  446 TYR C CZ  
7967  O OH  . TYR C 145 ? 0.6628 0.5633 0.4959 -0.0575 -0.0128 0.0079  446 TYR C OH  
7968  N N   . ILE C 146 ? 0.5988 0.4970 0.4735 -0.0226 0.0273  0.0022  447 ILE C N   
7969  C CA  . ILE C 146 ? 0.5847 0.4904 0.4715 -0.0167 0.0294  0.0048  447 ILE C CA  
7970  C C   . ILE C 146 ? 0.6115 0.5350 0.5004 -0.0172 0.0331  0.0070  447 ILE C C   
7971  O O   . ILE C 146 ? 0.5832 0.5160 0.4810 -0.0187 0.0318  0.0116  447 ILE C O   
7972  C CB  . ILE C 146 ? 0.5624 0.4588 0.4489 -0.0076 0.0336  0.0004  447 ILE C CB  
7973  C CG1 . ILE C 146 ? 0.5175 0.3984 0.4041 -0.0102 0.0293  0.0001  447 ILE C CG1 
7974  C CG2 . ILE C 146 ? 0.4826 0.3907 0.3797 0.0004  0.0367  0.0027  447 ILE C CG2 
7975  C CD1 . ILE C 146 ? 0.4458 0.3093 0.3248 -0.0045 0.0329  -0.0047 447 ILE C CD1 
7976  N N   . CYS C 147 ? 0.5026 0.4319 0.3824 -0.0171 0.0379  0.0036  448 CYS C N   
7977  C CA  . CYS C 147 ? 0.5011 0.4509 0.3822 -0.0198 0.0419  0.0058  448 CYS C CA  
7978  C C   . CYS C 147 ? 0.5617 0.5132 0.4418 -0.0314 0.0367  0.0126  448 CYS C C   
7979  O O   . CYS C 147 ? 0.4905 0.4555 0.3761 -0.0355 0.0375  0.0165  448 CYS C O   
7980  C CB  . CYS C 147 ? 0.5091 0.4649 0.3787 -0.0183 0.0479  0.0006  448 CYS C CB  
7981  S SG  . CYS C 147 ? 0.5614 0.5218 0.4314 -0.0019 0.0563  -0.0070 448 CYS C SG  
7982  N N   . ASN C 148 ? 0.5960 0.5336 0.4675 -0.0370 0.0312  0.0141  449 ASN C N   
7983  C CA  . ASN C 148 ? 0.4764 0.4109 0.3439 -0.0460 0.0258  0.0210  449 ASN C CA  
7984  C C   . ASN C 148 ? 0.5191 0.4488 0.3969 -0.0450 0.0213  0.0247  449 ASN C C   
7985  O O   . ASN C 148 ? 0.5186 0.4490 0.3952 -0.0514 0.0194  0.0298  449 ASN C O   
7986  C CB  . ASN C 148 ? 0.4771 0.3993 0.3327 -0.0497 0.0204  0.0219  449 ASN C CB  
7987  C CG  . ASN C 148 ? 0.5660 0.4929 0.4091 -0.0521 0.0246  0.0182  449 ASN C CG  
7988  O OD1 . ASN C 148 ? 0.4606 0.4010 0.3017 -0.0531 0.0314  0.0168  449 ASN C OD1 
7989  N ND2 . ASN C 148 ? 0.4733 0.3909 0.3077 -0.0529 0.0207  0.0162  449 ASN C ND2 
7990  N N   . HIS C 149 ? 0.4759 0.3995 0.3621 -0.0378 0.0198  0.0220  450 HIS C N   
7991  C CA  . HIS C 149 ? 0.4970 0.4181 0.3931 -0.0358 0.0164  0.0247  450 HIS C CA  
7992  C C   . HIS C 149 ? 0.4781 0.4129 0.3811 -0.0366 0.0202  0.0260  450 HIS C C   
7993  O O   . HIS C 149 ? 0.4569 0.3909 0.3602 -0.0420 0.0174  0.0300  450 HIS C O   
7994  C CB  . HIS C 149 ? 0.5143 0.4294 0.4174 -0.0287 0.0158  0.0213  450 HIS C CB  
7995  C CG  . HIS C 149 ? 0.5575 0.4711 0.4703 -0.0261 0.0127  0.0235  450 HIS C CG  
7996  N ND1 . HIS C 149 ? 0.5620 0.4684 0.4783 -0.0236 0.0089  0.0230  450 HIS C ND1 
7997  C CD2 . HIS C 149 ? 0.5662 0.4861 0.4854 -0.0263 0.0131  0.0259  450 HIS C CD2 
7998  C CE1 . HIS C 149 ? 0.5878 0.4954 0.5119 -0.0215 0.0073  0.0250  450 HIS C CE1 
7999  N NE2 . HIS C 149 ? 0.6076 0.5223 0.5331 -0.0232 0.0096  0.0266  450 HIS C NE2 
8000  N N   . VAL C 150 ? 0.4603 0.4078 0.3677 -0.0310 0.0264  0.0223  451 VAL C N   
8001  C CA  . VAL C 150 ? 0.3679 0.3340 0.2836 -0.0303 0.0299  0.0232  451 VAL C CA  
8002  C C   . VAL C 150 ? 0.5605 0.5373 0.4710 -0.0421 0.0305  0.0268  451 VAL C C   
8003  O O   . VAL C 150 ? 0.4555 0.4418 0.3708 -0.0473 0.0298  0.0295  451 VAL C O   
8004  C CB  . VAL C 150 ? 0.3818 0.3598 0.3011 -0.0195 0.0365  0.0184  451 VAL C CB  
8005  C CG1 . VAL C 150 ? 0.3656 0.3702 0.2930 -0.0187 0.0406  0.0192  451 VAL C CG1 
8006  C CG2 . VAL C 150 ? 0.3659 0.3300 0.2892 -0.0093 0.0355  0.0161  451 VAL C CG2 
8007  N N   . LYS C 151 ? 0.6088 0.5838 0.5079 -0.0479 0.0317  0.0271  452 LYS C N   
8008  C CA  . LYS C 151 ? 0.4660 0.4503 0.3575 -0.0609 0.0328  0.0312  452 LYS C CA  
8009  C C   . LYS C 151 ? 0.4761 0.4412 0.3606 -0.0700 0.0259  0.0368  452 LYS C C   
8010  O O   . LYS C 151 ? 0.5084 0.4788 0.3917 -0.0798 0.0256  0.0402  452 LYS C O   
8011  C CB  . LYS C 151 ? 0.4636 0.4511 0.3431 -0.0643 0.0363  0.0301  452 LYS C CB  
8012  C CG  . LYS C 151 ? 0.4737 0.4750 0.3448 -0.0788 0.0391  0.0343  452 LYS C CG  
8013  C CD  . LYS C 151 ? 0.4742 0.4820 0.3332 -0.0812 0.0437  0.0327  452 LYS C CD  
8014  C CE  . LYS C 151 ? 0.4600 0.4844 0.3101 -0.0969 0.0474  0.0371  452 LYS C CE  
8015  N NZ  . LYS C 151 ? 0.6391 0.6748 0.4782 -0.0988 0.0531  0.0349  452 LYS C NZ  
8016  N N   . TYR C 152 ? 0.5092 0.4519 0.3880 -0.0665 0.0201  0.0377  453 TYR C N   
8017  C CA  . TYR C 152 ? 0.5191 0.4415 0.3902 -0.0715 0.0133  0.0426  453 TYR C CA  
8018  C C   . TYR C 152 ? 0.5147 0.4374 0.3953 -0.0703 0.0118  0.0425  453 TYR C C   
8019  O O   . TYR C 152 ? 0.5858 0.5009 0.4593 -0.0794 0.0095  0.0461  453 TYR C O   
8020  C CB  . TYR C 152 ? 0.5036 0.4080 0.3701 -0.0646 0.0076  0.0428  453 TYR C CB  
8021  C CG  . TYR C 152 ? 0.5476 0.4315 0.4076 -0.0649 0.0005  0.0469  453 TYR C CG  
8022  C CD1 . TYR C 152 ? 0.5421 0.4225 0.4125 -0.0578 -0.0020 0.0452  453 TYR C CD1 
8023  C CD2 . TYR C 152 ? 0.4963 0.3632 0.3382 -0.0717 -0.0033 0.0526  453 TYR C CD2 
8024  C CE1 . TYR C 152 ? 0.5744 0.4361 0.4378 -0.0564 -0.0079 0.0481  453 TYR C CE1 
8025  C CE2 . TYR C 152 ? 0.5448 0.3898 0.3783 -0.0698 -0.0097 0.0561  453 TYR C CE2 
8026  C CZ  . TYR C 152 ? 0.6473 0.4904 0.4921 -0.0616 -0.0118 0.0533  453 TYR C CZ  
8027  O OH  . TYR C 152 ? 0.7565 0.5777 0.5921 -0.0579 -0.0177 0.0559  453 TYR C OH  
8028  N N   . ALA C 153 ? 0.5095 0.4392 0.4043 -0.0598 0.0129  0.0385  454 ALA C N   
8029  C CA  . ALA C 153 ? 0.4982 0.4281 0.4018 -0.0575 0.0110  0.0383  454 ALA C CA  
8030  C C   . ALA C 153 ? 0.5314 0.4806 0.4394 -0.0647 0.0145  0.0387  454 ALA C C   
8031  O O   . ALA C 153 ? 0.4888 0.4343 0.3969 -0.0693 0.0118  0.0399  454 ALA C O   
8032  C CB  . ALA C 153 ? 0.3824 0.3153 0.2983 -0.0452 0.0116  0.0346  454 ALA C CB  
8033  N N   . THR C 154 ? 0.5014 0.4730 0.4133 -0.0651 0.0205  0.0371  455 THR C N   
8034  C CA  . THR C 154 ? 0.5061 0.5030 0.4236 -0.0720 0.0240  0.0375  455 THR C CA  
8035  C C   . THR C 154 ? 0.5787 0.5703 0.4830 -0.0899 0.0222  0.0417  455 THR C C   
8036  O O   . THR C 154 ? 0.5227 0.5200 0.4278 -0.0988 0.0209  0.0428  455 THR C O   
8037  C CB  . THR C 154 ? 0.5381 0.5622 0.4618 -0.0665 0.0311  0.0346  455 THR C CB  
8038  O OG1 . THR C 154 ? 0.4495 0.4733 0.3821 -0.0499 0.0326  0.0308  455 THR C OG1 
8039  C CG2 . THR C 154 ? 0.4292 0.4860 0.3600 -0.0734 0.0347  0.0350  455 THR C CG2 
8040  N N   . ASN C 155 ? 0.6675 0.6472 0.5578 -0.0964 0.0222  0.0442  456 ASN C N   
8041  C CA  . ASN C 155 ? 0.5607 0.5264 0.4333 -0.1138 0.0199  0.0493  456 ASN C CA  
8042  C C   . ASN C 155 ? 0.5886 0.5787 0.4633 -0.1285 0.0231  0.0502  456 ASN C C   
8043  O O   . ASN C 155 ? 0.5756 0.5527 0.4407 -0.1415 0.0197  0.0529  456 ASN C O   
8044  C CB  . ASN C 155 ? 0.5506 0.4803 0.4126 -0.1132 0.0123  0.0517  456 ASN C CB  
8045  C CG  . ASN C 155 ? 0.6615 0.5677 0.5003 -0.1292 0.0094  0.0575  456 ASN C CG  
8046  O OD1 . ASN C 155 ? 0.6931 0.6020 0.5209 -0.1381 0.0119  0.0606  456 ASN C OD1 
8047  N ND2 . ASN C 155 ? 0.6700 0.5509 0.4992 -0.1328 0.0041  0.0589  456 ASN C ND2 
8048  N N   . LYS C 156 ? 0.5422 0.5690 0.4292 -0.1260 0.0298  0.0475  457 LYS C N   
8049  C CA  . LYS C 156 ? 0.6150 0.6751 0.5062 -0.1396 0.0337  0.0481  457 LYS C CA  
8050  C C   . LYS C 156 ? 0.6287 0.6931 0.5272 -0.1429 0.0302  0.0473  457 LYS C C   
8051  O O   . LYS C 156 ? 0.6870 0.7674 0.5825 -0.1605 0.0307  0.0490  457 LYS C O   
8052  C CB  . LYS C 156 ? 0.5951 0.6502 0.4671 -0.1618 0.0346  0.0531  457 LYS C CB  
8053  C CG  . LYS C 156 ? 0.5941 0.6567 0.4601 -0.1604 0.0396  0.0536  457 LYS C CG  
8054  C CD  . LYS C 156 ? 0.7071 0.7606 0.5512 -0.1834 0.0401  0.0598  457 LYS C CD  
8055  C CE  . LYS C 156 ? 0.8684 0.9313 0.7055 -0.1826 0.0453  0.0602  457 LYS C CE  
8056  N NZ  . LYS C 156 ? 0.8807 0.9905 0.7359 -0.1732 0.0536  0.0546  457 LYS C NZ  
8057  N N   . GLY C 157 ? 0.6728 0.7246 0.5804 -0.1272 0.0268  0.0448  458 GLY C N   
8058  C CA  . GLY C 157 ? 0.5646 0.6200 0.4789 -0.1284 0.0235  0.0437  458 GLY C CA  
8059  C C   . GLY C 157 ? 0.5787 0.5940 0.4799 -0.1324 0.0166  0.0450  458 GLY C C   
8060  O O   . GLY C 157 ? 0.6813 0.6941 0.5886 -0.1274 0.0136  0.0430  458 GLY C O   
8061  N N   . ASN C 158 ? 0.5886 0.5724 0.4707 -0.1402 0.0141  0.0482  459 ASN C N   
8062  C CA  . ASN C 158 ? 0.6659 0.6094 0.5348 -0.1391 0.0076  0.0491  459 ASN C CA  
8063  C C   . ASN C 158 ? 0.6776 0.6074 0.5533 -0.1186 0.0059  0.0474  459 ASN C C   
8064  O O   . ASN C 158 ? 0.6840 0.5932 0.5496 -0.1150 0.0042  0.0495  459 ASN C O   
8065  C CB  . ASN C 158 ? 0.6766 0.5905 0.5199 -0.1551 0.0052  0.0538  459 ASN C CB  
8066  C CG  . ASN C 158 ? 0.7997 0.6703 0.6271 -0.1517 -0.0015 0.0544  459 ASN C CG  
8067  O OD1 . ASN C 158 ? 0.8841 0.7512 0.7184 -0.1443 -0.0040 0.0509  459 ASN C OD1 
8068  N ND2 . ASN C 158 ? 0.7275 0.5653 0.5329 -0.1560 -0.0045 0.0589  459 ASN C ND2 
8069  N N   . LEU C 159 ? 0.5567 0.4991 0.4490 -0.1058 0.0061  0.0438  460 LEU C N   
8070  C CA  . LEU C 159 ? 0.4904 0.4288 0.3922 -0.0881 0.0060  0.0419  460 LEU C CA  
8071  C C   . LEU C 159 ? 0.5145 0.4199 0.4054 -0.0828 0.0005  0.0428  460 LEU C C   
8072  O O   . LEU C 159 ? 0.5293 0.4142 0.4092 -0.0875 -0.0036 0.0435  460 LEU C O   
8073  C CB  . LEU C 159 ? 0.5072 0.4625 0.4258 -0.0774 0.0070  0.0387  460 LEU C CB  
8074  C CG  . LEU C 159 ? 0.5544 0.5449 0.4863 -0.0765 0.0119  0.0375  460 LEU C CG  
8075  C CD1 . LEU C 159 ? 0.6078 0.6064 0.5534 -0.0609 0.0127  0.0353  460 LEU C CD1 
8076  C CD2 . LEU C 159 ? 0.5143 0.5197 0.4458 -0.0779 0.0169  0.0379  460 LEU C CD2 
8077  N N   . ARG C 160 ? 0.4365 0.3377 0.3299 -0.0726 0.0005  0.0425  461 ARG C N   
8078  C CA  . ARG C 160 ? 0.4423 0.3189 0.3273 -0.0658 -0.0046 0.0435  461 ARG C CA  
8079  C C   . ARG C 160 ? 0.4895 0.3733 0.3883 -0.0522 -0.0042 0.0405  461 ARG C C   
8080  O O   . ARG C 160 ? 0.5399 0.4402 0.4481 -0.0489 -0.0001 0.0386  461 ARG C O   
8081  C CB  . ARG C 160 ? 0.5379 0.4026 0.4084 -0.0701 -0.0056 0.0471  461 ARG C CB  
8082  C CG  . ARG C 160 ? 0.6856 0.5409 0.5393 -0.0857 -0.0056 0.0511  461 ARG C CG  
8083  C CD  . ARG C 160 ? 0.7496 0.5899 0.5866 -0.0889 -0.0074 0.0556  461 ARG C CD  
8084  N NE  . ARG C 160 ? 0.7451 0.6072 0.5869 -0.0918 -0.0020 0.0551  461 ARG C NE  
8085  C CZ  . ARG C 160 ? 0.6297 0.4867 0.4568 -0.0996 -0.0014 0.0591  461 ARG C CZ  
8086  N NH1 . ARG C 160 ? 0.5901 0.4194 0.3961 -0.1055 -0.0062 0.0646  461 ARG C NH1 
8087  N NH2 . ARG C 160 ? 0.6109 0.4897 0.4430 -0.1010 0.0041  0.0575  461 ARG C NH2 
8088  N N   . SER C 161 ? 0.4987 0.3700 0.3975 -0.0444 -0.0084 0.0397  462 SER C N   
8089  C CA  . SER C 161 ? 0.5885 0.4684 0.4999 -0.0340 -0.0078 0.0370  462 SER C CA  
8090  C C   . SER C 161 ? 0.5748 0.4521 0.4833 -0.0306 -0.0090 0.0375  462 SER C C   
8091  O O   . SER C 161 ? 0.5416 0.4055 0.4382 -0.0316 -0.0128 0.0401  462 SER C O   
8092  C CB  . SER C 161 ? 0.6598 0.5333 0.5740 -0.0272 -0.0110 0.0356  462 SER C CB  
8093  O OG  . SER C 161 ? 0.8533 0.7068 0.7541 -0.0267 -0.0158 0.0372  462 SER C OG  
8094  N N   . ALA C 162 ? 0.5862 0.4751 0.5040 -0.0268 -0.0060 0.0350  463 ALA C N   
8095  C CA  . ALA C 162 ? 0.5210 0.4088 0.4358 -0.0251 -0.0072 0.0346  463 ALA C CA  
8096  C C   . ALA C 162 ? 0.5471 0.4424 0.4718 -0.0201 -0.0056 0.0313  463 ALA C C   
8097  O O   . ALA C 162 ? 0.3964 0.2978 0.3293 -0.0181 -0.0023 0.0298  463 ALA C O   
8098  C CB  . ALA C 162 ? 0.5706 0.4615 0.4786 -0.0309 -0.0040 0.0350  463 ALA C CB  
8099  N N   . ILE C 163 ? 0.5153 0.4098 0.4375 -0.0191 -0.0081 0.0305  464 ILE C N   
8100  C CA  . ILE C 163 ? 0.5375 0.4372 0.4651 -0.0180 -0.0065 0.0273  464 ILE C CA  
8101  C C   . ILE C 163 ? 0.5483 0.4472 0.4679 -0.0215 -0.0072 0.0261  464 ILE C C   
8102  O O   . ILE C 163 ? 0.5206 0.4172 0.4329 -0.0223 -0.0114 0.0284  464 ILE C O   
8103  C CB  . ILE C 163 ? 0.4332 0.3369 0.3677 -0.0142 -0.0097 0.0270  464 ILE C CB  
8104  C CG1 . ILE C 163 ? 0.4110 0.3187 0.3493 -0.0161 -0.0076 0.0240  464 ILE C CG1 
8105  C CG2 . ILE C 163 ? 0.3993 0.3026 0.3292 -0.0117 -0.0160 0.0289  464 ILE C CG2 
8106  C CD1 . ILE C 163 ? 0.3783 0.2934 0.3251 -0.0137 -0.0090 0.0238  464 ILE C CD1 
8107  N N   . THR C 164 ? 0.5669 0.4661 0.4860 -0.0232 -0.0032 0.0224  465 THR C N   
8108  C CA  . THR C 164 ? 0.5525 0.4504 0.4630 -0.0272 -0.0035 0.0199  465 THR C CA  
8109  C C   . THR C 164 ? 0.5268 0.4255 0.4396 -0.0292 -0.0044 0.0166  465 THR C C   
8110  O O   . THR C 164 ? 0.5005 0.3952 0.4165 -0.0284 -0.0005 0.0146  465 THR C O   
8111  C CB  . THR C 164 ? 0.4963 0.3917 0.4004 -0.0282 0.0024  0.0174  465 THR C CB  
8112  O OG1 . THR C 164 ? 0.4927 0.3903 0.3929 -0.0295 0.0026  0.0208  465 THR C OG1 
8113  C CG2 . THR C 164 ? 0.5828 0.4747 0.4772 -0.0322 0.0030  0.0130  465 THR C CG2 
8114  N N   . ILE C 165 ? 0.5023 0.4065 0.4124 -0.0323 -0.0096 0.0164  466 ILE C N   
8115  C CA  . ILE C 165 ? 0.5345 0.4443 0.4479 -0.0362 -0.0115 0.0141  466 ILE C CA  
8116  C C   . ILE C 165 ? 0.6294 0.5363 0.5322 -0.0441 -0.0114 0.0095  466 ILE C C   
8117  O O   . ILE C 165 ? 0.6181 0.5311 0.5149 -0.0464 -0.0157 0.0098  466 ILE C O   
8118  C CB  . ILE C 165 ? 0.5954 0.5192 0.5158 -0.0332 -0.0179 0.0170  466 ILE C CB  
8119  C CG1 . ILE C 165 ? 0.5357 0.4587 0.4640 -0.0255 -0.0175 0.0204  466 ILE C CG1 
8120  C CG2 . ILE C 165 ? 0.5631 0.4978 0.4882 -0.0389 -0.0193 0.0145  466 ILE C CG2 
8121  C CD1 . ILE C 165 ? 0.4286 0.3635 0.3630 -0.0197 -0.0229 0.0227  466 ILE C CD1 
8122  N N   . PHE C 166 ? 0.6212 0.5177 0.5201 -0.0482 -0.0068 0.0054  467 PHE C N   
8123  C CA  . PHE C 166 ? 0.4996 0.3878 0.3856 -0.0564 -0.0057 -0.0002 467 PHE C CA  
8124  C C   . PHE C 166 ? 0.6211 0.5184 0.5079 -0.0661 -0.0099 -0.0020 467 PHE C C   
8125  O O   . PHE C 166 ? 0.6078 0.5170 0.5059 -0.0655 -0.0121 0.0009  467 PHE C O   
8126  C CB  . PHE C 166 ? 0.5652 0.4333 0.4440 -0.0546 0.0016  -0.0038 467 PHE C CB  
8127  C CG  . PHE C 166 ? 0.6279 0.4919 0.5045 -0.0463 0.0060  -0.0033 467 PHE C CG  
8128  C CD1 . PHE C 166 ? 0.6243 0.4873 0.4902 -0.0476 0.0068  -0.0061 467 PHE C CD1 
8129  C CD2 . PHE C 166 ? 0.4629 0.3267 0.3481 -0.0378 0.0093  -0.0002 467 PHE C CD2 
8130  C CE1 . PHE C 166 ? 0.5888 0.4520 0.4531 -0.0410 0.0114  -0.0057 467 PHE C CE1 
8131  C CE2 . PHE C 166 ? 0.5218 0.3868 0.4061 -0.0313 0.0135  0.0002  467 PHE C CE2 
8132  C CZ  . PHE C 166 ? 0.6118 0.4771 0.4858 -0.0330 0.0148  -0.0025 467 PHE C CZ  
8133  N N   . PRO C 167 ? 0.6019 0.4953 0.4763 -0.0761 -0.0109 -0.0071 468 PRO C N   
8134  C CA  . PRO C 167 ? 0.5546 0.4634 0.4302 -0.0873 -0.0161 -0.0086 468 PRO C CA  
8135  C C   . PRO C 167 ? 0.6108 0.5192 0.4924 -0.0926 -0.0144 -0.0082 468 PRO C C   
8136  O O   . PRO C 167 ? 0.5425 0.4290 0.4186 -0.0925 -0.0086 -0.0095 468 PRO C O   
8137  C CB  . PRO C 167 ? 0.6143 0.5117 0.4717 -0.0982 -0.0158 -0.0154 468 PRO C CB  
8138  C CG  . PRO C 167 ? 0.5738 0.4582 0.4229 -0.0902 -0.0122 -0.0163 468 PRO C CG  
8139  C CD  . PRO C 167 ? 0.6071 0.4831 0.4649 -0.0783 -0.0071 -0.0125 468 PRO C CD  
8140  N N   . GLN C 168 ? 0.6405 0.5743 0.5322 -0.0973 -0.0195 -0.0064 469 GLN C N   
8141  C CA  . GLN C 168 ? 0.5909 0.5304 0.4900 -0.1024 -0.0181 -0.0051 469 GLN C CA  
8142  C C   . GLN C 168 ? 0.6748 0.5961 0.5593 -0.1189 -0.0150 -0.0099 469 GLN C C   
8143  O O   . GLN C 168 ? 0.6331 0.5432 0.5025 -0.1282 -0.0154 -0.0152 469 GLN C O   
8144  C CB  . GLN C 168 ? 0.4955 0.4713 0.4086 -0.1034 -0.0242 -0.0027 469 GLN C CB  
8145  C CG  . GLN C 168 ? 0.4801 0.4743 0.3881 -0.1151 -0.0299 -0.0060 469 GLN C CG  
8146  C CD  . GLN C 168 ? 0.5416 0.5722 0.4634 -0.1073 -0.0370 -0.0026 469 GLN C CD  
8147  O OE1 . GLN C 168 ? 0.4848 0.5173 0.4137 -0.0909 -0.0383 0.0017  469 GLN C OE1 
8148  N NE2 . GLN C 168 ? 0.5684 0.6286 0.4935 -0.1189 -0.0417 -0.0044 469 GLN C NE2 
8149  N N   . ARG C 169 ? 0.6257 0.5421 0.5128 -0.1229 -0.0117 -0.0081 470 ARG C N   
8150  C CA  . ARG C 169 ? 0.6448 0.5424 0.5165 -0.1402 -0.0090 -0.0117 470 ARG C CA  
8151  C C   . ARG C 169 ? 0.6113 0.5341 0.4823 -0.1580 -0.0144 -0.0147 470 ARG C C   
8152  O O   . ARG C 169 ? 0.6251 0.5856 0.5125 -0.1558 -0.0195 -0.0122 470 ARG C O   
8153  C CB  . ARG C 169 ? 0.7512 0.6411 0.6261 -0.1407 -0.0048 -0.0076 470 ARG C CB  
8154  C CG  . ARG C 169 ? 0.8483 0.7149 0.7048 -0.1596 -0.0019 -0.0101 470 ARG C CG  
8155  C CD  . ARG C 169 ? 0.8098 0.6684 0.6688 -0.1586 0.0022  -0.0048 470 ARG C CD  
8156  N NE  . ARG C 169 ? 0.7678 0.5953 0.6207 -0.1427 0.0070  -0.0029 470 ARG C NE  
8157  C CZ  . ARG C 169 ? 0.9397 0.7695 0.8026 -0.1315 0.0093  0.0027  470 ARG C CZ  
8158  N NH1 . ARG C 169 ? 0.9116 0.7717 0.7902 -0.1342 0.0076  0.0064  470 ARG C NH1 
8159  N NH2 . ARG C 169 ? 1.0677 0.8721 0.9248 -0.1171 0.0132  0.0042  470 ARG C NH2 
8160  N N   . THR C 170 ? 0.6495 0.5514 0.5001 -0.1752 -0.0134 -0.0204 471 THR C N   
8161  C CA  . THR C 170 ? 0.7452 0.6710 0.5928 -0.1951 -0.0187 -0.0241 471 THR C CA  
8162  C C   . THR C 170 ? 0.8175 0.7317 0.6533 -0.2172 -0.0161 -0.0255 471 THR C C   
8163  O O   . THR C 170 ? 0.8719 0.8179 0.7208 -0.2255 -0.0180 -0.0224 471 THR C O   
8164  C CB  . THR C 170 ? 0.7680 0.6826 0.5996 -0.1996 -0.0211 -0.0305 471 THR C CB  
8165  O OG1 . THR C 170 ? 0.8780 0.7437 0.6855 -0.2029 -0.0150 -0.0353 471 THR C OG1 
8166  C CG2 . THR C 170 ? 0.7210 0.6487 0.5633 -0.1796 -0.0238 -0.0282 471 THR C CG2 
8167  N N   . ASP C 171 ? 0.8729 0.7419 0.6828 -0.2269 -0.0118 -0.0301 472 ASP C N   
8168  C CA  . ASP C 171 ? 0.9565 0.8060 0.7501 -0.2489 -0.0090 -0.0310 472 ASP C CA  
8169  C C   . ASP C 171 ? 0.9850 0.7925 0.7682 -0.2404 -0.0018 -0.0274 472 ASP C C   
8170  O O   . ASP C 171 ? 1.1258 0.9132 0.8941 -0.2574 0.0009  -0.0267 472 ASP C O   
8171  C CB  . ASP C 171 ? 1.0530 0.8790 0.8192 -0.2707 -0.0101 -0.0396 472 ASP C CB  
8172  C CG  . ASP C 171 ? 1.0717 0.8465 0.8146 -0.2602 -0.0057 -0.0448 472 ASP C CG  
8173  O OD1 . ASP C 171 ? 1.1161 0.8820 0.8675 -0.2354 -0.0026 -0.0417 472 ASP C OD1 
8174  O OD2 . ASP C 171 ? 1.0847 0.8287 0.8001 -0.2769 -0.0050 -0.0522 472 ASP C OD2 
8175  N N   . GLY C 172 ? 0.8900 0.6849 0.6798 -0.2153 0.0010  -0.0249 473 GLY C N   
8176  C CA  . GLY C 172 ? 0.8510 0.6092 0.6316 -0.2045 0.0071  -0.0213 473 GLY C CA  
8177  C C   . GLY C 172 ? 0.9273 0.6340 0.6801 -0.2003 0.0114  -0.0267 473 GLY C C   
8178  O O   . GLY C 172 ? 0.9313 0.6118 0.6797 -0.1833 0.0160  -0.0239 473 GLY C O   
8179  N N   . LYS C 173 ? 0.9444 0.6372 0.6781 -0.2144 0.0099  -0.0346 474 LYS C N   
8180  C CA  . LYS C 173 ? 1.1026 0.7470 0.8085 -0.2088 0.0141  -0.0411 474 LYS C CA  
8181  C C   . LYS C 173 ? 1.1851 0.8397 0.8978 -0.1911 0.0136  -0.0448 474 LYS C C   
8182  O O   . LYS C 173 ? 1.2922 0.9123 0.9827 -0.1858 0.0170  -0.0515 474 LYS C O   
8183  C CB  . LYS C 173 ? 1.1413 0.7578 0.8170 -0.2356 0.0134  -0.0485 474 LYS C CB  
8184  C CG  . LYS C 173 ? 1.2347 0.8298 0.8964 -0.2543 0.0153  -0.0448 474 LYS C CG  
8185  C CD  . LYS C 173 ? 1.3391 0.9141 0.9728 -0.2858 0.0135  -0.0521 474 LYS C CD  
8186  C CE  . LYS C 173 ? 1.3485 0.8956 0.9638 -0.3006 0.0166  -0.0475 474 LYS C CE  
8187  N NZ  . LYS C 173 ? 1.3190 0.8535 0.9098 -0.3221 0.0157  -0.0527 474 LYS C NZ  
8188  N N   . HIS C 174 ? 1.0380 0.7377 0.7792 -0.1818 0.0097  -0.0407 475 HIS C N   
8189  C CA  . HIS C 174 ? 1.0452 0.7573 0.7927 -0.1674 0.0088  -0.0432 475 HIS C CA  
8190  C C   . HIS C 174 ? 0.9814 0.7184 0.7550 -0.1468 0.0089  -0.0357 475 HIS C C   
8191  O O   . HIS C 174 ? 0.8948 0.6607 0.6833 -0.1400 0.0054  -0.0344 475 HIS C O   
8192  C CB  . HIS C 174 ? 1.0413 0.7822 0.7912 -0.1809 0.0023  -0.0471 475 HIS C CB  
8193  C CG  . HIS C 174 ? 1.1130 0.8300 0.8354 -0.2019 0.0017  -0.0559 475 HIS C CG  
8194  N ND1 . HIS C 174 ? 1.1459 0.8703 0.8633 -0.2263 -0.0016 -0.0568 475 HIS C ND1 
8195  C CD2 . HIS C 174 ? 1.1285 0.8146 0.8257 -0.2032 0.0042  -0.0646 475 HIS C CD2 
8196  C CE1 . HIS C 174 ? 1.1715 0.8687 0.8609 -0.2428 -0.0014 -0.0657 475 HIS C CE1 
8197  N NE2 . HIS C 174 ? 1.1955 0.8679 0.8717 -0.2285 0.0021  -0.0708 475 HIS C NE2 
8198  N N   . ASP C 175 ? 0.9381 0.6633 0.7161 -0.1374 0.0128  -0.0304 476 ASP C N   
8199  C CA  . ASP C 175 ? 0.7885 0.5366 0.5900 -0.1197 0.0128  -0.0237 476 ASP C CA  
8200  C C   . ASP C 175 ? 0.7303 0.4752 0.5320 -0.1027 0.0153  -0.0254 476 ASP C C   
8201  O O   . ASP C 175 ? 0.7663 0.4820 0.5494 -0.0979 0.0198  -0.0304 476 ASP C O   
8202  C CB  . ASP C 175 ? 0.7878 0.5223 0.5912 -0.1135 0.0164  -0.0181 476 ASP C CB  
8203  C CG  . ASP C 175 ? 0.7778 0.5279 0.5889 -0.1276 0.0140  -0.0140 476 ASP C CG  
8204  O OD1 . ASP C 175 ? 0.8050 0.5765 0.6193 -0.1428 0.0095  -0.0160 476 ASP C OD1 
8205  O OD2 . ASP C 175 ? 0.8352 0.5783 0.6490 -0.1231 0.0165  -0.0087 476 ASP C OD2 
8206  N N   . PHE C 176 ? 0.6160 0.3907 0.4376 -0.0937 0.0125  -0.0213 477 PHE C N   
8207  C CA  . PHE C 176 ? 0.6661 0.4419 0.4925 -0.0769 0.0156  -0.0203 477 PHE C CA  
8208  C C   . PHE C 176 ? 0.6984 0.4727 0.5351 -0.0651 0.0185  -0.0146 477 PHE C C   
8209  O O   . PHE C 176 ? 0.7020 0.4909 0.5519 -0.0676 0.0160  -0.0096 477 PHE C O   
8210  C CB  . PHE C 176 ? 0.6759 0.4809 0.5157 -0.0745 0.0111  -0.0182 477 PHE C CB  
8211  C CG  . PHE C 176 ? 0.7520 0.5590 0.5804 -0.0831 0.0084  -0.0235 477 PHE C CG  
8212  C CD1 . PHE C 176 ? 0.7871 0.5987 0.6100 -0.0990 0.0040  -0.0263 477 PHE C CD1 
8213  C CD2 . PHE C 176 ? 0.7366 0.5432 0.5595 -0.0763 0.0103  -0.0258 477 PHE C CD2 
8214  C CE1 . PHE C 176 ? 0.7097 0.5246 0.5215 -0.1074 0.0010  -0.0313 477 PHE C CE1 
8215  C CE2 . PHE C 176 ? 0.7355 0.5442 0.5467 -0.0844 0.0078  -0.0306 477 PHE C CE2 
8216  C CZ  . PHE C 176 ? 0.6918 0.5042 0.4973 -0.0997 0.0029  -0.0335 477 PHE C CZ  
8217  N N   . ARG C 177 ? 0.6807 0.4393 0.5111 -0.0519 0.0238  -0.0155 478 ARG C N   
8218  C CA  . ARG C 177 ? 0.6495 0.4077 0.4885 -0.0398 0.0264  -0.0102 478 ARG C CA  
8219  C C   . ARG C 177 ? 0.6248 0.3869 0.4662 -0.0240 0.0303  -0.0106 478 ARG C C   
8220  O O   . ARG C 177 ? 0.8117 0.5581 0.6385 -0.0190 0.0342  -0.0161 478 ARG C O   
8221  C CB  . ARG C 177 ? 0.6528 0.3807 0.4767 -0.0409 0.0295  -0.0101 478 ARG C CB  
8222  C CG  . ARG C 177 ? 0.6986 0.4256 0.5221 -0.0567 0.0264  -0.0079 478 ARG C CG  
8223  C CD  . ARG C 177 ? 0.6857 0.4417 0.5317 -0.0558 0.0233  -0.0011 478 ARG C CD  
8224  N NE  . ARG C 177 ? 0.7124 0.4661 0.5640 -0.0424 0.0259  0.0040  478 ARG C NE  
8225  C CZ  . ARG C 177 ? 0.7373 0.4775 0.5837 -0.0437 0.0273  0.0080  478 ARG C CZ  
8226  N NH1 . ARG C 177 ? 0.6859 0.4125 0.5208 -0.0592 0.0269  0.0076  478 ARG C NH1 
8227  N NH2 . ARG C 177 ? 0.6859 0.4272 0.5379 -0.0305 0.0291  0.0127  478 ARG C NH2 
8228  N N   . VAL C 178 ? 0.6503 0.4343 0.5094 -0.0166 0.0295  -0.0053 479 VAL C N   
8229  C CA  . VAL C 178 ? 0.6157 0.4043 0.4781 -0.0016 0.0336  -0.0042 479 VAL C CA  
8230  C C   . VAL C 178 ? 0.6878 0.4585 0.5447 0.0061  0.0362  -0.0019 479 VAL C C   
8231  O O   . VAL C 178 ? 0.7003 0.4735 0.5642 0.0025  0.0338  0.0029  479 VAL C O   
8232  C CB  . VAL C 178 ? 0.5847 0.4023 0.4662 0.0007  0.0312  0.0006  479 VAL C CB  
8233  C CG1 . VAL C 178 ? 0.4304 0.2579 0.3161 0.0141  0.0353  0.0015  479 VAL C CG1 
8234  C CG2 . VAL C 178 ? 0.6102 0.4412 0.4943 -0.0077 0.0278  -0.0006 479 VAL C CG2 
8235  N N   . TRP C 179 ? 0.7460 0.4969 0.5882 0.0170  0.0411  -0.0054 480 TRP C N   
8236  C CA  . TRP C 179 ? 0.7191 0.4491 0.5526 0.0262  0.0434  -0.0026 480 TRP C CA  
8237  C C   . TRP C 179 ? 0.6587 0.4104 0.5077 0.0395  0.0438  0.0030  480 TRP C C   
8238  O O   . TRP C 179 ? 0.6635 0.4055 0.5104 0.0447  0.0438  0.0077  480 TRP C O   
8239  C CB  . TRP C 179 ? 0.7240 0.4211 0.5334 0.0354  0.0483  -0.0084 480 TRP C CB  
8240  C CG  . TRP C 179 ? 0.7583 0.4236 0.5473 0.0207  0.0476  -0.0128 480 TRP C CG  
8241  C CD1 . TRP C 179 ? 0.6899 0.3624 0.4813 0.0016  0.0437  -0.0149 480 TRP C CD1 
8242  C CD2 . TRP C 179 ? 0.7588 0.3801 0.5206 0.0228  0.0505  -0.0154 480 TRP C CD2 
8243  N NE1 . TRP C 179 ? 0.7277 0.3665 0.4963 -0.0099 0.0440  -0.0190 480 TRP C NE1 
8244  C CE2 . TRP C 179 ? 0.7628 0.3671 0.5118 0.0021  0.0482  -0.0195 480 TRP C CE2 
8245  C CE3 . TRP C 179 ? 0.7331 0.3268 0.4788 0.0405  0.0545  -0.0147 480 TRP C CE3 
8246  C CZ2 . TRP C 179 ? 0.7894 0.3480 0.5087 -0.0037 0.0501  -0.0230 480 TRP C CZ2 
8247  C CZ3 . TRP C 179 ? 0.7207 0.2658 0.4358 0.0370  0.0564  -0.0180 480 TRP C CZ3 
8248  C CH2 . TRP C 179 ? 0.8237 0.3506 0.5253 0.0138  0.0543  -0.0222 480 TRP C CH2 
8249  N N   . ASN C 180 ? 0.6040 0.3849 0.4670 0.0439  0.0441  0.0029  481 ASN C N   
8250  C CA  . ASN C 180 ? 0.6474 0.4535 0.5262 0.0527  0.0436  0.0080  481 ASN C CA  
8251  C C   . ASN C 180 ? 0.7597 0.5762 0.6511 0.0430  0.0388  0.0134  481 ASN C C   
8252  O O   . ASN C 180 ? 0.8160 0.6333 0.7100 0.0295  0.0355  0.0129  481 ASN C O   
8253  C CB  . ASN C 180 ? 0.5578 0.3930 0.4475 0.0546  0.0447  0.0065  481 ASN C CB  
8254  C CG  . ASN C 180 ? 0.5908 0.4208 0.4691 0.0639  0.0499  0.0006  481 ASN C CG  
8255  O OD1 . ASN C 180 ? 0.5960 0.4086 0.4615 0.0579  0.0509  -0.0047 481 ASN C OD1 
8256  N ND2 . ASN C 180 ? 0.6491 0.4967 0.5318 0.0788  0.0535  0.0009  481 ASN C ND2 
8257  N N   . SER C 181 ? 0.6311 0.4579 0.5303 0.0507  0.0383  0.0185  482 SER C N   
8258  C CA  . SER C 181 ? 0.5715 0.4105 0.4825 0.0427  0.0341  0.0229  482 SER C CA  
8259  C C   . SER C 181 ? 0.4640 0.3309 0.3900 0.0380  0.0317  0.0231  482 SER C C   
8260  O O   . SER C 181 ? 0.5282 0.4005 0.4603 0.0277  0.0281  0.0239  482 SER C O   
8261  C CB  . SER C 181 ? 0.5693 0.4070 0.4806 0.0516  0.0341  0.0282  482 SER C CB  
8262  O OG  . SER C 181 ? 0.5856 0.4346 0.4984 0.0668  0.0365  0.0288  482 SER C OG  
8263  N N   . GLN C 182 ? 0.4409 0.3249 0.3713 0.0450  0.0338  0.0222  483 GLN C N   
8264  C CA  . GLN C 182 ? 0.4549 0.3602 0.3945 0.0382  0.0323  0.0217  483 GLN C CA  
8265  C C   . GLN C 182 ? 0.5908 0.4995 0.5250 0.0408  0.0361  0.0175  483 GLN C C   
8266  O O   . GLN C 182 ? 0.5921 0.4943 0.5188 0.0519  0.0403  0.0152  483 GLN C O   
8267  C CB  . GLN C 182 ? 0.4930 0.4224 0.4442 0.0404  0.0310  0.0251  483 GLN C CB  
8268  C CG  . GLN C 182 ? 0.5992 0.5283 0.5557 0.0376  0.0273  0.0288  483 GLN C CG  
8269  C CD  . GLN C 182 ? 0.6477 0.5986 0.6125 0.0430  0.0268  0.0317  483 GLN C CD  
8270  O OE1 . GLN C 182 ? 0.6444 0.6158 0.6156 0.0390  0.0264  0.0314  483 GLN C OE1 
8271  N NE2 . GLN C 182 ? 0.5873 0.5344 0.5507 0.0514  0.0269  0.0346  483 GLN C NE2 
8272  N N   . LEU C 183 ? 0.5157 0.4337 0.4523 0.0312  0.0346  0.0166  484 LEU C N   
8273  C CA  . LEU C 183 ? 0.5177 0.4403 0.4484 0.0319  0.0383  0.0128  484 LEU C CA  
8274  C C   . LEU C 183 ? 0.5442 0.4870 0.4786 0.0430  0.0429  0.0123  484 LEU C C   
8275  O O   . LEU C 183 ? 0.5601 0.5007 0.4866 0.0512  0.0478  0.0082  484 LEU C O   
8276  C CB  . LEU C 183 ? 0.3748 0.3058 0.3071 0.0196  0.0356  0.0135  484 LEU C CB  
8277  C CG  . LEU C 183 ? 0.4519 0.3661 0.3806 0.0108  0.0308  0.0137  484 LEU C CG  
8278  C CD1 . LEU C 183 ? 0.3745 0.2941 0.3022 0.0008  0.0277  0.0149  484 LEU C CD1 
8279  C CD2 . LEU C 183 ? 0.3806 0.2748 0.2980 0.0125  0.0325  0.0094  484 LEU C CD2 
8280  N N   . ILE C 184 ? 0.5917 0.5552 0.5374 0.0439  0.0415  0.0162  485 ILE C N   
8281  C CA  . ILE C 184 ? 0.5193 0.5099 0.4712 0.0534  0.0452  0.0163  485 ILE C CA  
8282  C C   . ILE C 184 ? 0.5932 0.5866 0.5502 0.0637  0.0438  0.0197  485 ILE C C   
8283  O O   . ILE C 184 ? 0.5540 0.5516 0.5180 0.0569  0.0395  0.0233  485 ILE C O   
8284  C CB  . ILE C 184 ? 0.4602 0.4787 0.4202 0.0420  0.0445  0.0180  485 ILE C CB  
8285  C CG1 . ILE C 184 ? 0.4984 0.5144 0.4510 0.0334  0.0465  0.0152  485 ILE C CG1 
8286  C CG2 . ILE C 184 ? 0.3970 0.4501 0.3658 0.0502  0.0476  0.0186  485 ILE C CG2 
8287  C CD1 . ILE C 184 ? 0.5046 0.5310 0.4598 0.0169  0.0435  0.0181  485 ILE C CD1 
8288  N N   . ARG C 185 ? 0.6538 0.6424 0.6052 0.0806  0.0474  0.0184  486 ARG C N   
8289  C CA  . ARG C 185 ? 0.6022 0.5966 0.5569 0.0936  0.0466  0.0220  486 ARG C CA  
8290  C C   . ARG C 185 ? 0.5686 0.5773 0.5209 0.1130  0.0518  0.0199  486 ARG C C   
8291  O O   . ARG C 185 ? 0.5731 0.5774 0.5178 0.1171  0.0563  0.0148  486 ARG C O   
8292  C CB  . ARG C 185 ? 0.5360 0.4952 0.4808 0.0960  0.0445  0.0241  486 ARG C CB  
8293  C CG  . ARG C 185 ? 0.5513 0.4996 0.4991 0.0792  0.0397  0.0261  486 ARG C CG  
8294  C CD  . ARG C 185 ? 0.6856 0.6103 0.6269 0.0819  0.0378  0.0295  486 ARG C CD  
8295  N NE  . ARG C 185 ? 0.7952 0.7373 0.7437 0.0894  0.0359  0.0344  486 ARG C NE  
8296  C CZ  . ARG C 185 ? 0.7648 0.6928 0.7089 0.0920  0.0340  0.0386  486 ARG C CZ  
8297  N NH1 . ARG C 185 ? 0.7421 0.6389 0.6750 0.0866  0.0339  0.0387  486 ARG C NH1 
8298  N NH2 . ARG C 185 ? 0.7313 0.6780 0.6818 0.0990  0.0320  0.0430  486 ARG C NH2 
8299  N N   . TYR C 186 ? 0.4835 0.5107 0.4418 0.1260  0.0510  0.0235  487 TYR C N   
8300  C CA  . TYR C 186 ? 0.4811 0.5244 0.4374 0.1479  0.0556  0.0218  487 TYR C CA  
8301  C C   . TYR C 186 ? 0.6053 0.6113 0.5445 0.1662  0.0567  0.0223  487 TYR C C   
8302  O O   . TYR C 186 ? 0.7067 0.6848 0.6396 0.1627  0.0532  0.0262  487 TYR C O   
8303  C CB  . TYR C 186 ? 0.4599 0.5500 0.4322 0.1533  0.0541  0.0255  487 TYR C CB  
8304  C CG  . TYR C 186 ? 0.5226 0.6491 0.5095 0.1339  0.0530  0.0252  487 TYR C CG  
8305  C CD1 . TYR C 186 ? 0.5465 0.6928 0.5351 0.1298  0.0577  0.0208  487 TYR C CD1 
8306  C CD2 . TYR C 186 ? 0.4704 0.6100 0.4672 0.1193  0.0475  0.0293  487 TYR C CD2 
8307  C CE1 . TYR C 186 ? 0.5346 0.7113 0.5337 0.1106  0.0569  0.0212  487 TYR C CE1 
8308  C CE2 . TYR C 186 ? 0.4180 0.5859 0.4245 0.1005  0.0464  0.0290  487 TYR C CE2 
8309  C CZ  . TYR C 186 ? 0.5158 0.7015 0.5231 0.0957  0.0511  0.0254  487 TYR C CZ  
8310  O OH  . TYR C 186 ? 0.4101 0.6209 0.4243 0.0753  0.0502  0.0257  487 TYR C OH  
8311  N N   . ALA C 187 ? 0.7308 0.7365 0.6612 0.1861  0.0620  0.0184  488 ALA C N   
8312  C CA  . ALA C 187 ? 0.7061 0.6719 0.6157 0.2053  0.0639  0.0179  488 ALA C CA  
8313  C C   . ALA C 187 ? 0.7285 0.6987 0.6388 0.2215  0.0608  0.0250  488 ALA C C   
8314  O O   . ALA C 187 ? 0.7741 0.7879 0.7020 0.2243  0.0586  0.0288  488 ALA C O   
8315  C CB  . ALA C 187 ? 0.5970 0.5639 0.4964 0.2243  0.0708  0.0110  488 ALA C CB  
8316  N N   . GLY C 188 ? 0.7584 0.6821 0.6477 0.2316  0.0606  0.0270  489 GLY C N   
8317  C CA  . GLY C 188 ? 0.7456 0.6653 0.6297 0.2501  0.0581  0.0341  489 GLY C CA  
8318  C C   . GLY C 188 ? 0.7389 0.6239 0.5984 0.2770  0.0620  0.0323  489 GLY C C   
8319  O O   . GLY C 188 ? 0.8394 0.6750 0.6767 0.2739  0.0644  0.0283  489 GLY C O   
8320  N N   . TYR C 189 ? 0.7526 0.6626 0.6143 0.3038  0.0626  0.0348  490 TYR C N   
8321  C CA  . TYR C 189 ? 0.8108 0.6917 0.6489 0.3337  0.0668  0.0324  490 TYR C CA  
8322  C C   . TYR C 189 ? 0.9633 0.8246 0.7882 0.3533  0.0630  0.0416  490 TYR C C   
8323  O O   . TYR C 189 ? 0.9262 0.8267 0.7685 0.3560  0.0584  0.0486  490 TYR C O   
8324  C CB  . TYR C 189 ? 0.7983 0.7265 0.6480 0.3534  0.0717  0.0265  490 TYR C CB  
8325  C CG  . TYR C 189 ? 0.8180 0.7669 0.6794 0.3339  0.0757  0.0181  490 TYR C CG  
8326  C CD1 . TYR C 189 ? 0.8812 0.7855 0.7234 0.3253  0.0795  0.0108  490 TYR C CD1 
8327  C CD2 . TYR C 189 ? 0.8440 0.8563 0.7340 0.3228  0.0753  0.0179  490 TYR C CD2 
8328  C CE1 . TYR C 189 ? 0.9582 0.8817 0.8098 0.3079  0.0828  0.0037  490 TYR C CE1 
8329  C CE2 . TYR C 189 ? 0.8951 0.9242 0.7935 0.3046  0.0788  0.0112  490 TYR C CE2 
8330  C CZ  . TYR C 189 ? 0.9282 0.9136 0.8076 0.2981  0.0825  0.0043  490 TYR C CZ  
8331  O OH  . TYR C 189 ? 0.7461 0.7491 0.6330 0.2803  0.0856  -0.0017 490 TYR C OH  
8332  N N   . LYS C 190 ? 1.0868 0.8877 0.8799 0.3627  0.0643  0.0414  491 LYS C N   
8333  C CA  . LYS C 190 ? 1.1387 0.9160 0.9151 0.3720  0.0599  0.0493  491 LYS C CA  
8334  C C   . LYS C 190 ? 1.2059 1.0059 0.9789 0.3989  0.0610  0.0478  491 LYS C C   
8335  O O   . LYS C 190 ? 1.3255 1.0986 1.0788 0.4094  0.0650  0.0412  491 LYS C O   
8336  C CB  . LYS C 190 ? 1.2248 0.9292 0.9688 0.3605  0.0602  0.0494  491 LYS C CB  
8337  C CG  . LYS C 190 ? 1.3458 1.0238 1.0755 0.3594  0.0552  0.0594  491 LYS C CG  
8338  C CD  . LYS C 190 ? 1.3742 1.0435 1.1109 0.3346  0.0519  0.0654  491 LYS C CD  
8339  C CE  . LYS C 190 ? 1.3178 1.0438 1.0844 0.3356  0.0477  0.0721  491 LYS C CE  
8340  N NZ  . LYS C 190 ? 1.2889 1.0365 1.0552 0.3557  0.0442  0.0784  491 LYS C NZ  
8341  N N   . GLN C 191 ? 1.2370 1.0874 1.0286 0.4098  0.0572  0.0538  492 GLN C N   
8342  C CA  . GLN C 191 ? 1.2779 1.1627 1.0714 0.4346  0.0581  0.0524  492 GLN C CA  
8343  C C   . GLN C 191 ? 1.2811 1.1200 1.0430 0.4522  0.0570  0.0556  492 GLN C C   
8344  O O   . GLN C 191 ? 1.2183 1.0067 0.9603 0.4438  0.0546  0.0607  492 GLN C O   
8345  C CB  . GLN C 191 ? 1.2888 1.2439 1.1120 0.4375  0.0538  0.0578  492 GLN C CB  
8346  C CG  . GLN C 191 ? 1.2817 1.2913 1.1366 0.4229  0.0554  0.0538  492 GLN C CG  
8347  C CD  . GLN C 191 ? 1.2686 1.3123 1.1317 0.4321  0.0613  0.0448  492 GLN C CD  
8348  O OE1 . GLN C 191 ? 1.2511 1.2585 1.0948 0.4387  0.0662  0.0380  492 GLN C OE1 
8349  N NE2 . GLN C 191 ? 1.2689 1.3837 1.1600 0.4307  0.0606  0.0445  492 GLN C NE2 
8350  N N   . PRO C 192 ? 1.3401 1.1959 1.0960 0.4768  0.0590  0.0526  493 PRO C N   
8351  C CA  . PRO C 192 ? 1.3907 1.2005 1.1142 0.4956  0.0583  0.0551  493 PRO C CA  
8352  C C   . PRO C 192 ? 1.4325 1.2423 1.1525 0.5007  0.0522  0.0661  493 PRO C C   
8353  O O   . PRO C 192 ? 1.3920 1.1447 1.0843 0.4999  0.0508  0.0705  493 PRO C O   
8354  C CB  . PRO C 192 ? 1.3573 1.1997 1.0816 0.5211  0.0617  0.0493  493 PRO C CB  
8355  C CG  . PRO C 192 ? 1.3277 1.2478 1.0896 0.5167  0.0616  0.0479  493 PRO C CG  
8356  C CD  . PRO C 192 ? 1.3323 1.2476 1.1086 0.4880  0.0623  0.0462  493 PRO C CD  
8357  N N   . ASP C 193 ? 1.4177 1.2917 1.1647 0.5049  0.0487  0.0706  494 ASP C N   
8358  C CA  . ASP C 193 ? 1.3902 1.2685 1.1347 0.5099  0.0427  0.0808  494 ASP C CA  
8359  C C   . ASP C 193 ? 1.3896 1.2285 1.1281 0.4864  0.0398  0.0868  494 ASP C C   
8360  O O   . ASP C 193 ? 1.4790 1.2894 1.2003 0.4896  0.0361  0.0947  494 ASP C O   
8361  C CB  . ASP C 193 ? 1.3559 1.3142 1.1322 0.5148  0.0393  0.0836  494 ASP C CB  
8362  C CG  . ASP C 193 ? 1.3047 1.3052 1.1128 0.4911  0.0390  0.0814  494 ASP C CG  
8363  O OD1 . ASP C 193 ? 1.2888 1.2558 1.0951 0.4707  0.0405  0.0796  494 ASP C OD1 
8364  O OD2 . ASP C 193 ? 1.2624 1.3309 1.0970 0.4924  0.0373  0.0814  494 ASP C OD2 
8365  N N   . GLY C 194 ? 1.2621 1.0988 1.0135 0.4630  0.0414  0.0832  495 GLY C N   
8366  C CA  . GLY C 194 ? 1.1515 0.9525 0.8972 0.4400  0.0389  0.0884  495 GLY C CA  
8367  C C   . GLY C 194 ? 1.0750 0.9176 0.8513 0.4202  0.0369  0.0893  495 GLY C C   
8368  O O   . GLY C 194 ? 1.0856 0.9013 0.8595 0.3991  0.0357  0.0921  495 GLY C O   
8369  N N   . SER C 195 ? 1.1296 1.0382 0.9340 0.4260  0.0365  0.0869  496 SER C N   
8370  C CA  . SER C 195 ? 1.1762 1.1275 1.0099 0.4074  0.0347  0.0872  496 SER C CA  
8371  C C   . SER C 195 ? 1.1559 1.0920 0.9933 0.3933  0.0399  0.0791  496 SER C C   
8372  O O   . SER C 195 ? 1.2102 1.0973 1.0257 0.3946  0.0442  0.0741  496 SER C O   
8373  C CB  . SER C 195 ? 1.1642 1.1919 1.0252 0.4159  0.0325  0.0872  496 SER C CB  
8374  O OG  . SER C 195 ? 1.1652 1.2193 1.0337 0.4255  0.0376  0.0787  496 SER C OG  
8375  N N   . THR C 196 ? 1.0326 1.0108 0.8970 0.3791  0.0394  0.0776  497 THR C N   
8376  C CA  . THR C 196 ? 0.9832 0.9489 0.8521 0.3609  0.0439  0.0701  497 THR C CA  
8377  C C   . THR C 196 ? 0.8546 0.8849 0.7529 0.3524  0.0453  0.0642  497 THR C C   
8378  O O   . THR C 196 ? 0.8402 0.9199 0.7599 0.3447  0.0410  0.0676  497 THR C O   
8379  C CB  . THR C 196 ? 1.0469 0.9846 0.9149 0.3290  0.0408  0.0725  497 THR C CB  
8380  O OG1 . THR C 196 ? 1.1320 1.0095 0.9714 0.3341  0.0399  0.0783  497 THR C OG1 
8381  C CG2 . THR C 196 ? 0.9734 0.9016 0.8463 0.3049  0.0446  0.0637  497 THR C CG2 
8382  N N   . LEU C 197 ? 0.8598 0.8887 0.7573 0.3519  0.0515  0.0552  498 LEU C N   
8383  C CA  . LEU C 197 ? 0.7686 0.8546 0.6908 0.3417  0.0538  0.0494  498 LEU C CA  
8384  C C   . LEU C 197 ? 0.7753 0.8484 0.7031 0.3079  0.0546  0.0447  498 LEU C C   
8385  O O   . LEU C 197 ? 0.8077 0.8294 0.7177 0.3007  0.0568  0.0416  498 LEU C O   
8386  C CB  . LEU C 197 ? 0.7458 0.8471 0.6642 0.3664  0.0606  0.0426  498 LEU C CB  
8387  C CG  . LEU C 197 ? 0.7334 0.8897 0.6743 0.3532  0.0642  0.0361  498 LEU C CG  
8388  C CD1 . LEU C 197 ? 0.7454 0.9707 0.7127 0.3489  0.0600  0.0405  498 LEU C CD1 
8389  C CD2 . LEU C 197 ? 0.7869 0.9496 0.7202 0.3758  0.0721  0.0283  498 LEU C CD2 
8390  N N   . GLY C 198 ? 0.7672 0.8866 0.7185 0.2873  0.0524  0.0444  499 GLY C N   
8391  C CA  . GLY C 198 ? 0.7743 0.8828 0.7307 0.2562  0.0521  0.0411  499 GLY C CA  
8392  C C   . GLY C 198 ? 0.7923 0.8749 0.7469 0.2377  0.0465  0.0463  499 GLY C C   
8393  O O   . GLY C 198 ? 0.8745 0.9760 0.8363 0.2390  0.0416  0.0523  499 GLY C O   
8394  N N   . ASP C 199 ? 0.7030 0.7441 0.6476 0.2209  0.0471  0.0437  500 ASP C N   
8395  C CA  . ASP C 199 ? 0.6195 0.6395 0.5637 0.2014  0.0425  0.0474  500 ASP C CA  
8396  C C   . ASP C 199 ? 0.7344 0.7017 0.6563 0.2088  0.0425  0.0504  500 ASP C C   
8397  O O   . ASP C 199 ? 0.6882 0.6187 0.5954 0.2061  0.0458  0.0461  500 ASP C O   
8398  C CB  . ASP C 199 ? 0.6455 0.6617 0.5956 0.1762  0.0427  0.0428  500 ASP C CB  
8399  C CG  . ASP C 199 ? 0.6900 0.6917 0.6420 0.1570  0.0380  0.0460  500 ASP C CG  
8400  O OD1 . ASP C 199 ? 0.7970 0.7728 0.7388 0.1605  0.0360  0.0506  500 ASP C OD1 
8401  O OD2 . ASP C 199 ? 0.6378 0.6538 0.6006 0.1382  0.0365  0.0438  500 ASP C OD2 
8402  N N   . PRO C 200 ? 0.6739 0.6350 0.5914 0.2157  0.0387  0.0578  501 PRO C N   
8403  C CA  . PRO C 200 ? 0.6801 0.5895 0.5730 0.2239  0.0392  0.0615  501 PRO C CA  
8404  C C   . PRO C 200 ? 0.7054 0.5763 0.5889 0.2018  0.0392  0.0600  501 PRO C C   
8405  O O   . PRO C 200 ? 0.8034 0.6279 0.6641 0.2054  0.0412  0.0603  501 PRO C O   
8406  C CB  . PRO C 200 ? 0.6362 0.5566 0.5295 0.2333  0.0345  0.0705  501 PRO C CB  
8407  C CG  . PRO C 200 ? 0.5970 0.5761 0.5121 0.2409  0.0330  0.0701  501 PRO C CG  
8408  C CD  . PRO C 200 ? 0.5702 0.5726 0.5024 0.2197  0.0343  0.0631  501 PRO C CD  
8409  N N   . ALA C 201 ? 0.6253 0.5135 0.5244 0.1791  0.0371  0.0581  502 ALA C N   
8410  C CA  . ALA C 201 ? 0.6613 0.5186 0.5532 0.1591  0.0370  0.0565  502 ALA C CA  
8411  C C   . ALA C 201 ? 0.7899 0.6213 0.6700 0.1571  0.0412  0.0495  502 ALA C C   
8412  O O   . ALA C 201 ? 0.7308 0.5271 0.5971 0.1458  0.0418  0.0485  502 ALA C O   
8413  C CB  . ALA C 201 ? 0.6699 0.5537 0.5809 0.1386  0.0339  0.0555  502 ALA C CB  
8414  N N   . ASN C 202 ? 0.7839 0.6340 0.6689 0.1671  0.0443  0.0445  503 ASN C N   
8415  C CA  . ASN C 202 ? 0.7070 0.5378 0.5821 0.1646  0.0483  0.0370  503 ASN C CA  
8416  C C   . ASN C 202 ? 0.8140 0.6151 0.6670 0.1863  0.0524  0.0351  503 ASN C C   
8417  O O   . ASN C 202 ? 0.9029 0.6882 0.7456 0.1872  0.0563  0.0280  503 ASN C O   
8418  C CB  . ASN C 202 ? 0.5378 0.4077 0.4310 0.1593  0.0494  0.0321  503 ASN C CB  
8419  C CG  . ASN C 202 ? 0.5784 0.4682 0.4884 0.1374  0.0454  0.0334  503 ASN C CG  
8420  O OD1 . ASN C 202 ? 0.6667 0.5346 0.5724 0.1227  0.0432  0.0342  503 ASN C OD1 
8421  N ND2 . ASN C 202 ? 0.5137 0.4449 0.4419 0.1350  0.0444  0.0335  503 ASN C ND2 
8422  N N   . VAL C 203 ? 0.8768 0.6678 0.7205 0.2041  0.0515  0.0412  504 VAL C N   
8423  C CA  . VAL C 203 ? 0.9075 0.6671 0.7275 0.2280  0.0552  0.0399  504 VAL C CA  
8424  C C   . VAL C 203 ? 0.9474 0.6532 0.7420 0.2189  0.0579  0.0347  504 VAL C C   
8425  O O   . VAL C 203 ? 1.0353 0.7235 0.8152 0.2304  0.0624  0.0277  504 VAL C O   
8426  C CB  . VAL C 203 ? 0.8921 0.6412 0.7024 0.2456  0.0526  0.0490  504 VAL C CB  
8427  C CG1 . VAL C 203 ? 0.8208 0.5204 0.5990 0.2674  0.0560  0.0482  504 VAL C CG1 
8428  C CG2 . VAL C 203 ? 0.8677 0.6729 0.7008 0.2600  0.0506  0.0525  504 VAL C CG2 
8429  N N   . GLN C 204 ? 0.8472 0.5279 0.6357 0.1974  0.0552  0.0376  505 GLN C N   
8430  C CA  . GLN C 204 ? 0.9104 0.5401 0.6732 0.1865  0.0572  0.0332  505 GLN C CA  
8431  C C   . GLN C 204 ? 0.9781 0.6172 0.7466 0.1746  0.0596  0.0235  505 GLN C C   
8432  O O   . GLN C 204 ? 1.0039 0.6106 0.7509 0.1788  0.0633  0.0165  505 GLN C O   
8433  C CB  . GLN C 204 ? 0.8846 0.4924 0.6415 0.1644  0.0539  0.0387  505 GLN C CB  
8434  C CG  . GLN C 204 ? 1.0652 0.6160 0.7907 0.1544  0.0559  0.0353  505 GLN C CG  
8435  C CD  . GLN C 204 ? 1.1677 0.7073 0.8921 0.1263  0.0532  0.0384  505 GLN C CD  
8436  O OE1 . GLN C 204 ? 1.1134 0.6901 0.8627 0.1134  0.0501  0.0410  505 GLN C OE1 
8437  N NE2 . GLN C 204 ? 1.2385 0.7267 0.9328 0.1166  0.0544  0.0377  505 GLN C NE2 
8438  N N   . PHE C 205 ? 0.8778 0.5589 0.6731 0.1599  0.0573  0.0229  506 PHE C N   
8439  C CA  . PHE C 205 ? 0.8105 0.5021 0.6111 0.1484  0.0589  0.0148  506 PHE C CA  
8440  C C   . PHE C 205 ? 0.8470 0.5526 0.6464 0.1679  0.0638  0.0088  506 PHE C C   
8441  O O   . PHE C 205 ? 0.9222 0.6129 0.7097 0.1655  0.0671  0.0008  506 PHE C O   
8442  C CB  . PHE C 205 ? 0.7218 0.4533 0.5494 0.1304  0.0551  0.0167  506 PHE C CB  
8443  C CG  . PHE C 205 ? 0.8094 0.5510 0.6416 0.1174  0.0560  0.0097  506 PHE C CG  
8444  C CD1 . PHE C 205 ? 0.8060 0.5220 0.6268 0.0998  0.0549  0.0063  506 PHE C CD1 
8445  C CD2 . PHE C 205 ? 0.7933 0.5713 0.6404 0.1222  0.0577  0.0070  506 PHE C CD2 
8446  C CE1 . PHE C 205 ? 0.8111 0.5374 0.6354 0.0884  0.0551  0.0004  506 PHE C CE1 
8447  C CE2 . PHE C 205 ? 0.7816 0.5678 0.6311 0.1102  0.0583  0.0014  506 PHE C CE2 
8448  C CZ  . PHE C 205 ? 0.7550 0.5150 0.5930 0.0940  0.0568  -0.0017 506 PHE C CZ  
8449  N N   . THR C 206 ? 0.6839 0.4206 0.4954 0.1871  0.0644  0.0123  507 THR C N   
8450  C CA  . THR C 206 ? 0.7286 0.4818 0.5387 0.2082  0.0695  0.0069  507 THR C CA  
8451  C C   . THR C 206 ? 0.8108 0.5146 0.5889 0.2242  0.0738  0.0016  507 THR C C   
8452  O O   . THR C 206 ? 0.8333 0.5362 0.6035 0.2318  0.0788  -0.0068 507 THR C O   
8453  C CB  . THR C 206 ? 0.7631 0.5569 0.5897 0.2269  0.0687  0.0125  507 THR C CB  
8454  O OG1 . THR C 206 ? 0.7904 0.6277 0.6443 0.2104  0.0647  0.0164  507 THR C OG1 
8455  C CG2 . THR C 206 ? 0.6780 0.4952 0.5047 0.2494  0.0744  0.0066  507 THR C CG2 
8456  N N   . GLU C 207 ? 0.8639 0.5242 0.6213 0.2291  0.0723  0.0063  508 GLU C N   
8457  C CA  . GLU C 207 ? 0.9467 0.5526 0.6692 0.2437  0.0762  0.0014  508 GLU C CA  
8458  C C   . GLU C 207 ? 0.9720 0.5437 0.6777 0.2227  0.0776  -0.0068 508 GLU C C   
8459  O O   . GLU C 207 ? 1.0338 0.5765 0.7165 0.2333  0.0823  -0.0153 508 GLU C O   
8460  C CB  . GLU C 207 ? 1.1054 0.6710 0.8077 0.2528  0.0739  0.0096  508 GLU C CB  
8461  C CG  . GLU C 207 ? 1.3023 0.8840 1.0057 0.2857  0.0744  0.0148  508 GLU C CG  
8462  C CD  . GLU C 207 ? 1.4638 1.0267 1.1592 0.2872  0.0696  0.0261  508 GLU C CD  
8463  O OE1 . GLU C 207 ? 1.4713 0.9971 1.1531 0.2659  0.0673  0.0292  508 GLU C OE1 
8464  O OE2 . GLU C 207 ? 1.4786 1.0692 1.1828 0.3071  0.0677  0.0319  508 GLU C OE2 
8465  N N   . ILE C 208 ? 0.9439 0.5199 0.6603 0.1935  0.0735  -0.0047 509 ILE C N   
8466  C CA  . ILE C 208 ? 1.0048 0.5575 0.7089 0.1721  0.0740  -0.0123 509 ILE C CA  
8467  C C   . ILE C 208 ? 1.0416 0.6206 0.7531 0.1759  0.0778  -0.0213 509 ILE C C   
8468  O O   . ILE C 208 ? 1.1572 0.7072 0.8468 0.1743  0.0810  -0.0303 509 ILE C O   
8469  C CB  . ILE C 208 ? 0.9722 0.5371 0.6919 0.1426  0.0685  -0.0080 509 ILE C CB  
8470  C CG1 . ILE C 208 ? 0.9862 0.5276 0.6983 0.1374  0.0653  0.0009  509 ILE C CG1 
8471  C CG2 . ILE C 208 ? 0.9800 0.5253 0.6875 0.1211  0.0685  -0.0158 509 ILE C CG2 
8472  C CD1 . ILE C 208 ? 0.9003 0.4540 0.6263 0.1092  0.0605  0.0043  509 ILE C CD1 
8473  N N   . CYS C 209 ? 0.9735 0.6075 0.7144 0.1798  0.0774  -0.0189 510 CYS C N   
8474  C CA  . CYS C 209 ? 0.8584 0.5216 0.6071 0.1824  0.0813  -0.0263 510 CYS C CA  
8475  C C   . CYS C 209 ? 0.8963 0.5468 0.6266 0.2099  0.0880  -0.0330 510 CYS C C   
8476  O O   . CYS C 209 ? 0.9727 0.6129 0.6893 0.2103  0.0922  -0.0424 510 CYS C O   
8477  C CB  . CYS C 209 ? 0.8037 0.5267 0.5859 0.1795  0.0795  -0.0213 510 CYS C CB  
8478  S SG  . CYS C 209 ? 0.8601 0.5997 0.6631 0.1490  0.0722  -0.0150 510 CYS C SG  
8479  N N   . ILE C 210 ? 0.9727 0.6259 0.7023 0.2344  0.0889  -0.0283 511 ILE C N   
8480  C CA  . ILE C 210 ? 1.0322 0.6729 0.7432 0.2648  0.0952  -0.0344 511 ILE C CA  
8481  C C   . ILE C 210 ? 1.0892 0.6623 0.7611 0.2653  0.0977  -0.0419 511 ILE C C   
8482  O O   . ILE C 210 ? 1.0960 0.6565 0.7505 0.2775  0.1035  -0.0521 511 ILE C O   
8483  C CB  . ILE C 210 ? 0.9629 0.6161 0.6788 0.2912  0.0945  -0.0268 511 ILE C CB  
8484  C CG1 . ILE C 210 ? 1.0039 0.7265 0.7574 0.2893  0.0922  -0.0205 511 ILE C CG1 
8485  C CG2 . ILE C 210 ? 0.9347 0.5761 0.6309 0.3251  0.1009  -0.0332 511 ILE C CG2 
8486  C CD1 . ILE C 210 ? 1.0904 0.8273 0.8513 0.3085  0.0892  -0.0112 511 ILE C CD1 
8487  N N   . GLN C 211 ? 1.0891 0.6182 0.7458 0.2504  0.0934  -0.0373 512 GLN C N   
8488  C CA  . GLN C 211 ? 1.2274 0.6902 0.8461 0.2437  0.0948  -0.0438 512 GLN C CA  
8489  C C   . GLN C 211 ? 1.2311 0.6926 0.8467 0.2204  0.0956  -0.0532 512 GLN C C   
8490  O O   . GLN C 211 ? 1.3384 0.7518 0.9224 0.2160  0.0975  -0.0612 512 GLN C O   
8491  C CB  . GLN C 211 ? 1.3901 0.8191 0.9996 0.2277  0.0891  -0.0347 512 GLN C CB  
8492  C CG  . GLN C 211 ? 1.5629 0.9375 1.1406 0.2103  0.0877  -0.0382 512 GLN C CG  
8493  C CD  . GLN C 211 ? 1.6704 1.0332 1.2487 0.1768  0.0845  -0.0385 512 GLN C CD  
8494  O OE1 . GLN C 211 ? 1.6793 1.0621 1.2775 0.1648  0.0807  -0.0302 512 GLN C OE1 
8495  N NE2 . GLN C 211 ? 1.7315 1.0687 1.2906 0.1600  0.0853  -0.0477 512 GLN C NE2 
8496  N N   . GLN C 212 ? 1.1251 0.6390 0.7717 0.2049  0.0936  -0.0521 513 GLN C N   
8497  C CA  . GLN C 212 ? 1.1093 0.6276 0.7538 0.1859  0.0943  -0.0605 513 GLN C CA  
8498  C C   . GLN C 212 ? 1.0993 0.6457 0.7465 0.2024  0.1007  -0.0688 513 GLN C C   
8499  O O   . GLN C 212 ? 1.0392 0.5948 0.6857 0.1883  0.1016  -0.0755 513 GLN C O   
8500  C CB  . GLN C 212 ? 1.2207 0.7757 0.8940 0.1586  0.0882  -0.0545 513 GLN C CB  
8501  C CG  . GLN C 212 ? 1.2132 0.7383 0.8791 0.1358  0.0826  -0.0501 513 GLN C CG  
8502  C CD  . GLN C 212 ? 1.3135 0.7849 0.9442 0.1258  0.0839  -0.0588 513 GLN C CD  
8503  O OE1 . GLN C 212 ? 1.4047 0.8291 1.0114 0.1255  0.0835  -0.0575 513 GLN C OE1 
8504  N NE2 . GLN C 212 ? 1.3329 0.8096 0.9584 0.1168  0.0854  -0.0678 513 GLN C NE2 
8505  N N   . GLY C 213 ? 1.1491 0.7112 0.7990 0.2320  0.1051  -0.0682 514 GLY C N   
8506  C CA  . GLY C 213 ? 1.0208 0.6158 0.6750 0.2489  0.1117  -0.0756 514 GLY C CA  
8507  C C   . GLY C 213 ? 0.9749 0.6405 0.6666 0.2495  0.1115  -0.0698 514 GLY C C   
8508  O O   . GLY C 213 ? 0.8946 0.5939 0.5922 0.2580  0.1170  -0.0757 514 GLY C O   
8509  N N   . TRP C 214 ? 0.9482 0.6372 0.6641 0.2395  0.1055  -0.0588 515 TRP C N   
8510  C CA  . TRP C 214 ? 0.9709 0.7240 0.7195 0.2412  0.1053  -0.0533 515 TRP C CA  
8511  C C   . TRP C 214 ? 1.0510 0.8252 0.8015 0.2742  0.1099  -0.0532 515 TRP C C   
8512  O O   . TRP C 214 ? 1.0097 0.7541 0.7465 0.2924  0.1092  -0.0504 515 TRP C O   
8513  C CB  . TRP C 214 ? 0.9262 0.6952 0.6974 0.2223  0.0976  -0.0424 515 TRP C CB  
8514  C CG  . TRP C 214 ? 0.9665 0.7975 0.7690 0.2174  0.0967  -0.0375 515 TRP C CG  
8515  C CD1 . TRP C 214 ? 0.8985 0.7637 0.7130 0.2045  0.0985  -0.0402 515 TRP C CD1 
8516  C CD2 . TRP C 214 ? 0.9622 0.8267 0.7861 0.2235  0.0936  -0.0287 515 TRP C CD2 
8517  N NE1 . TRP C 214 ? 0.8925 0.8085 0.7334 0.2013  0.0968  -0.0338 515 TRP C NE1 
8518  C CE2 . TRP C 214 ? 0.9372 0.8548 0.7848 0.2127  0.0937  -0.0271 515 TRP C CE2 
8519  C CE3 . TRP C 214 ? 1.0143 0.8684 0.8379 0.2362  0.0905  -0.0220 515 TRP C CE3 
8520  C CZ2 . TRP C 214 ? 0.8831 0.8434 0.7540 0.2133  0.0909  -0.0198 515 TRP C CZ2 
8521  C CZ3 . TRP C 214 ? 0.9838 0.8827 0.8318 0.2381  0.0875  -0.0145 515 TRP C CZ3 
8522  C CH2 . TRP C 214 ? 0.9077 0.8591 0.7789 0.2263  0.0877  -0.0139 515 TRP C CH2 
8523  N N   . LYS C 215 ? 1.0763 0.9020 0.8423 0.2821  0.1148  -0.0563 516 LYS C N   
8524  C CA  . LYS C 215 ? 1.0970 0.9574 0.8703 0.3124  0.1191  -0.0560 516 LYS C CA  
8525  C C   . LYS C 215 ? 1.0566 0.9663 0.8614 0.3069  0.1141  -0.0452 516 LYS C C   
8526  O O   . LYS C 215 ? 1.0576 1.0148 0.8855 0.2897  0.1136  -0.0432 516 LYS C O   
8527  C CB  . LYS C 215 ? 1.1692 1.0650 0.9436 0.3227  0.1275  -0.0650 516 LYS C CB  
8528  C CG  . LYS C 215 ? 1.3167 1.1650 1.0578 0.3320  0.1332  -0.0769 516 LYS C CG  
8529  C CD  . LYS C 215 ? 1.4064 1.2245 1.1271 0.3637  0.1349  -0.0790 516 LYS C CD  
8530  C CE  . LYS C 215 ? 1.4058 1.1778 1.0954 0.3665  0.1380  -0.0896 516 LYS C CE  
8531  N NZ  . LYS C 215 ? 1.3605 1.0676 1.0260 0.3463  0.1348  -0.0916 516 LYS C NZ  
8532  N N   . PRO C 216 ? 1.0090 0.9072 0.8137 0.3198  0.1100  -0.0380 517 PRO C N   
8533  C CA  . PRO C 216 ? 1.0248 0.9691 0.8576 0.3144  0.1049  -0.0283 517 PRO C CA  
8534  C C   . PRO C 216 ? 1.0120 1.0208 0.8633 0.3329  0.1093  -0.0292 517 PRO C C   
8535  O O   . PRO C 216 ? 1.0044 1.0144 0.8448 0.3644  0.1141  -0.0329 517 PRO C O   
8536  C CB  . PRO C 216 ? 1.0889 0.9961 0.9102 0.3267  0.1002  -0.0213 517 PRO C CB  
8537  C CG  . PRO C 216 ? 1.1409 0.9999 0.9300 0.3524  0.1052  -0.0280 517 PRO C CG  
8538  C CD  . PRO C 216 ? 1.0385 0.8781 0.8144 0.3397  0.1099  -0.0384 517 PRO C CD  
8539  N N   . PRO C 217 ? 0.9327 0.9966 0.8107 0.3143  0.1080  -0.0261 518 PRO C N   
8540  C CA  . PRO C 217 ? 0.8376 0.9689 0.7362 0.3293  0.1106  -0.0247 518 PRO C CA  
8541  C C   . PRO C 217 ? 0.7678 0.9113 0.6737 0.3477  0.1058  -0.0168 518 PRO C C   
8542  O O   . PRO C 217 ? 0.7688 0.9655 0.6885 0.3667  0.1079  -0.0161 518 PRO C O   
8543  C CB  . PRO C 217 ? 0.7731 0.9493 0.6950 0.2980  0.1090  -0.0223 518 PRO C CB  
8544  C CG  . PRO C 217 ? 0.6941 0.8258 0.6103 0.2696  0.1032  -0.0196 518 PRO C CG  
8545  C CD  . PRO C 217 ? 0.7998 0.8662 0.6881 0.2789  0.1045  -0.0244 518 PRO C CD  
8546  N N   . ARG C 218 ? 0.7734 0.8716 0.6702 0.3422  0.0994  -0.0109 519 ARG C N   
8547  C CA  . ARG C 218 ? 0.9114 1.0108 0.8098 0.3600  0.0945  -0.0028 519 ARG C CA  
8548  C C   . ARG C 218 ? 0.9230 1.0917 0.8513 0.3546  0.0908  0.0032  519 ARG C C   
8549  O O   . ARG C 218 ? 0.8866 1.0922 0.8222 0.3795  0.0910  0.0057  519 ARG C O   
8550  C CB  . ARG C 218 ? 0.9339 1.0117 0.8114 0.3955  0.0974  -0.0052 519 ARG C CB  
8551  C CG  . ARG C 218 ? 1.0156 1.0139 0.8597 0.3966  0.0986  -0.0092 519 ARG C CG  
8552  C CD  . ARG C 218 ? 1.0850 1.0462 0.9054 0.4176  0.0956  -0.0065 519 ARG C CD  
8553  N NE  . ARG C 218 ? 1.1940 1.0782 0.9825 0.4125  0.0959  -0.0093 519 ARG C NE  
8554  C CZ  . ARG C 218 ? 1.2669 1.1045 1.0419 0.4044  0.0910  -0.0027 519 ARG C CZ  
8555  N NH1 . ARG C 218 ? 1.3624 1.1334 1.1081 0.3968  0.0916  -0.0060 519 ARG C NH1 
8556  N NH2 . ARG C 218 ? 1.1544 1.0128 0.9445 0.4025  0.0853  0.0072  519 ARG C NH2 
8557  N N   . GLY C 219 ? 0.9073 1.0918 0.8516 0.3216  0.0871  0.0057  520 GLY C N   
8558  C CA  . GLY C 219 ? 0.8366 1.0780 0.8063 0.3096  0.0827  0.0114  520 GLY C CA  
8559  C C   . GLY C 219 ? 0.8218 1.0416 0.7948 0.2892  0.0746  0.0185  520 GLY C C   
8560  O O   . GLY C 219 ? 0.8436 1.0065 0.7999 0.2855  0.0725  0.0197  520 GLY C O   
8561  N N   . ARG C 220 ? 0.8068 1.0730 0.8005 0.2750  0.0702  0.0230  521 ARG C N   
8562  C CA  . ARG C 220 ? 0.6948 0.9463 0.6921 0.2573  0.0627  0.0293  521 ARG C CA  
8563  C C   . ARG C 220 ? 0.7156 0.9458 0.7137 0.2248  0.0612  0.0278  521 ARG C C   
8564  O O   . ARG C 220 ? 0.7350 0.9342 0.7292 0.2124  0.0562  0.0315  521 ARG C O   
8565  C CB  . ARG C 220 ? 0.7079 1.0175 0.7250 0.2564  0.0583  0.0341  521 ARG C CB  
8566  C CG  . ARG C 220 ? 0.7471 1.0447 0.7663 0.2443  0.0505  0.0407  521 ARG C CG  
8567  C CD  . ARG C 220 ? 0.8129 1.1555 0.8428 0.2603  0.0465  0.0459  521 ARG C CD  
8568  N NE  . ARG C 220 ? 0.8766 1.1981 0.9026 0.2558  0.0396  0.0525  521 ARG C NE  
8569  C CZ  . ARG C 220 ? 0.8992 1.2549 0.9384 0.2416  0.0337  0.0559  521 ARG C CZ  
8570  N NH1 . ARG C 220 ? 0.8613 1.2737 0.9182 0.2294  0.0338  0.0537  521 ARG C NH1 
8571  N NH2 . ARG C 220 ? 0.8975 1.2306 0.9310 0.2388  0.0280  0.0615  521 ARG C NH2 
8572  N N   . PHE C 221 ? 0.6096 0.8567 0.6121 0.2115  0.0655  0.0226  522 PHE C N   
8573  C CA  . PHE C 221 ? 0.6432 0.8726 0.6457 0.1822  0.0640  0.0215  522 PHE C CA  
8574  C C   . PHE C 221 ? 0.7705 0.9802 0.7617 0.1815  0.0701  0.0149  522 PHE C C   
8575  O O   . PHE C 221 ? 0.8269 1.0616 0.8237 0.1684  0.0732  0.0120  522 PHE C O   
8576  C CB  . PHE C 221 ? 0.6498 0.9247 0.6695 0.1605  0.0614  0.0235  522 PHE C CB  
8577  C CG  . PHE C 221 ? 0.6614 0.9564 0.6912 0.1593  0.0551  0.0292  522 PHE C CG  
8578  C CD1 . PHE C 221 ? 0.7156 0.9814 0.7428 0.1448  0.0491  0.0326  522 PHE C CD1 
8579  C CD2 . PHE C 221 ? 0.6090 0.9541 0.6504 0.1733  0.0551  0.0309  522 PHE C CD2 
8580  C CE1 . PHE C 221 ? 0.6018 0.8855 0.6366 0.1436  0.0434  0.0373  522 PHE C CE1 
8581  C CE2 . PHE C 221 ? 0.6262 0.9904 0.6758 0.1718  0.0488  0.0361  522 PHE C CE2 
8582  C CZ  . PHE C 221 ? 0.5180 0.8504 0.5638 0.1566  0.0430  0.0391  522 PHE C CZ  
8583  N N   . ASP C 222 ? 0.7553 0.9185 0.7285 0.1954  0.0719  0.0125  523 ASP C N   
8584  C CA  . ASP C 222 ? 0.6456 0.7827 0.6045 0.1951  0.0772  0.0057  523 ASP C CA  
8585  C C   . ASP C 222 ? 0.6360 0.7333 0.5880 0.1721  0.0734  0.0061  523 ASP C C   
8586  O O   . ASP C 222 ? 0.6833 0.7414 0.6257 0.1726  0.0699  0.0083  523 ASP C O   
8587  C CB  . ASP C 222 ? 0.7713 0.8772 0.7116 0.2225  0.0811  0.0021  523 ASP C CB  
8588  C CG  . ASP C 222 ? 0.8378 0.9830 0.7832 0.2496  0.0855  0.0009  523 ASP C CG  
8589  O OD1 . ASP C 222 ? 0.8526 1.0540 0.8169 0.2453  0.0863  0.0018  523 ASP C OD1 
8590  O OD2 . ASP C 222 ? 0.8060 0.9255 0.7353 0.2754  0.0881  -0.0012 523 ASP C OD2 
8591  N N   . VAL C 223 ? 0.6526 0.7605 0.6085 0.1519  0.0740  0.0042  524 VAL C N   
8592  C CA  . VAL C 223 ? 0.5745 0.6474 0.5235 0.1321  0.0703  0.0044  524 VAL C CA  
8593  C C   . VAL C 223 ? 0.5802 0.6075 0.5093 0.1404  0.0725  -0.0003 524 VAL C C   
8594  O O   . VAL C 223 ? 0.6168 0.6421 0.5357 0.1514  0.0783  -0.0063 524 VAL C O   
8595  C CB  . VAL C 223 ? 0.5781 0.6696 0.5320 0.1117  0.0708  0.0034  524 VAL C CB  
8596  C CG1 . VAL C 223 ? 0.5807 0.6362 0.5259 0.0948  0.0671  0.0033  524 VAL C CG1 
8597  C CG2 . VAL C 223 ? 0.4126 0.5432 0.3834 0.1001  0.0680  0.0083  524 VAL C CG2 
8598  N N   . LEU C 224 ? 0.5713 0.5622 0.4934 0.1347  0.0680  0.0021  525 LEU C N   
8599  C CA  . LEU C 224 ? 0.6346 0.5806 0.5361 0.1398  0.0696  -0.0021 525 LEU C CA  
8600  C C   . LEU C 224 ? 0.6373 0.5727 0.5311 0.1256  0.0710  -0.0075 525 LEU C C   
8601  O O   . LEU C 224 ? 0.6053 0.5585 0.5091 0.1085  0.0685  -0.0058 525 LEU C O   
8602  C CB  . LEU C 224 ? 0.7099 0.6236 0.6064 0.1343  0.0645  0.0022  525 LEU C CB  
8603  C CG  . LEU C 224 ? 0.7963 0.7085 0.6934 0.1503  0.0634  0.0074  525 LEU C CG  
8604  C CD1 . LEU C 224 ? 0.6558 0.5514 0.5550 0.1380  0.0576  0.0131  525 LEU C CD1 
8605  C CD2 . LEU C 224 ? 0.9355 0.8162 0.8113 0.1711  0.0676  0.0039  525 LEU C CD2 
8606  N N   . PRO C 225 ? 0.6717 0.5771 0.5458 0.1326  0.0747  -0.0140 526 PRO C N   
8607  C CA  . PRO C 225 ? 0.6059 0.4981 0.4708 0.1178  0.0749  -0.0190 526 PRO C CA  
8608  C C   . PRO C 225 ? 0.6145 0.4812 0.4773 0.1001  0.0686  -0.0161 526 PRO C C   
8609  O O   . PRO C 225 ? 0.7364 0.5865 0.5991 0.1013  0.0655  -0.0120 526 PRO C O   
8610  C CB  . PRO C 225 ? 0.5928 0.4580 0.4352 0.1324  0.0808  -0.0273 526 PRO C CB  
8611  C CG  . PRO C 225 ? 0.7074 0.5501 0.5422 0.1493  0.0808  -0.0251 526 PRO C CG  
8612  C CD  . PRO C 225 ? 0.6109 0.4899 0.4678 0.1543  0.0785  -0.0173 526 PRO C CD  
8613  N N   . LEU C 226 ? 0.6571 0.5232 0.5183 0.0837  0.0667  -0.0180 527 LEU C N   
8614  C CA  . LEU C 226 ? 0.7304 0.5732 0.5875 0.0682  0.0611  -0.0168 527 LEU C CA  
8615  C C   . LEU C 226 ? 0.7985 0.6017 0.6329 0.0707  0.0629  -0.0227 527 LEU C C   
8616  O O   . LEU C 226 ? 0.7890 0.5827 0.6087 0.0787  0.0680  -0.0297 527 LEU C O   
8617  C CB  . LEU C 226 ? 0.6651 0.5209 0.5266 0.0515  0.0580  -0.0165 527 LEU C CB  
8618  C CG  . LEU C 226 ? 0.6356 0.5239 0.5158 0.0455  0.0554  -0.0104 527 LEU C CG  
8619  C CD1 . LEU C 226 ? 0.6316 0.5289 0.5105 0.0322  0.0536  -0.0108 527 LEU C CD1 
8620  C CD2 . LEU C 226 ? 0.5532 0.4417 0.4454 0.0406  0.0498  -0.0039 527 LEU C CD2 
8621  N N   . LEU C 227 ? 0.8389 0.6185 0.6691 0.0638  0.0591  -0.0201 528 LEU C N   
8622  C CA  . LEU C 227 ? 0.7710 0.5106 0.5784 0.0604  0.0597  -0.0252 528 LEU C CA  
8623  C C   . LEU C 227 ? 0.8355 0.5727 0.6450 0.0388  0.0539  -0.0243 528 LEU C C   
8624  O O   . LEU C 227 ? 0.7447 0.4842 0.5639 0.0313  0.0497  -0.0185 528 LEU C O   
8625  C CB  . LEU C 227 ? 0.6641 0.3773 0.4620 0.0705  0.0607  -0.0224 528 LEU C CB  
8626  C CG  . LEU C 227 ? 0.8006 0.4738 0.5710 0.0833  0.0655  -0.0283 528 LEU C CG  
8627  C CD1 . LEU C 227 ? 0.7494 0.3868 0.5062 0.0803  0.0637  -0.0245 528 LEU C CD1 
8628  C CD2 . LEU C 227 ? 0.7192 0.3736 0.4696 0.0781  0.0682  -0.0384 528 LEU C CD2 
8629  N N   . LEU C 228 ? 0.8333 0.5688 0.6342 0.0295  0.0537  -0.0300 529 LEU C N   
8630  C CA  . LEU C 228 ? 0.7511 0.4943 0.5570 0.0108  0.0477  -0.0289 529 LEU C CA  
8631  C C   . LEU C 228 ? 0.7813 0.4943 0.5663 -0.0010 0.0466  -0.0348 529 LEU C C   
8632  O O   . LEU C 228 ? 0.7771 0.4691 0.5418 0.0024  0.0507  -0.0425 529 LEU C O   
8633  C CB  . LEU C 228 ? 0.6547 0.4243 0.4681 0.0074  0.0469  -0.0296 529 LEU C CB  
8634  C CG  . LEU C 228 ? 0.6643 0.4632 0.4955 0.0166  0.0484  -0.0244 529 LEU C CG  
8635  C CD1 . LEU C 228 ? 0.4867 0.3084 0.3229 0.0098  0.0470  -0.0238 529 LEU C CD1 
8636  C CD2 . LEU C 228 ? 0.4777 0.2872 0.3262 0.0160  0.0446  -0.0166 529 LEU C CD2 
8637  N N   . GLN C 229 ? 0.7877 0.4997 0.5770 -0.0154 0.0414  -0.0316 530 GLN C N   
8638  C CA  . GLN C 229 ? 0.7799 0.4682 0.5511 -0.0307 0.0394  -0.0364 530 GLN C CA  
8639  C C   . GLN C 229 ? 0.6886 0.4004 0.4693 -0.0469 0.0329  -0.0356 530 GLN C C   
8640  O O   . GLN C 229 ? 0.6326 0.3685 0.4331 -0.0498 0.0286  -0.0289 530 GLN C O   
8641  C CB  . GLN C 229 ? 0.7995 0.4652 0.5646 -0.0346 0.0393  -0.0333 530 GLN C CB  
8642  C CG  . GLN C 229 ? 0.8536 0.5033 0.6044 -0.0554 0.0361  -0.0369 530 GLN C CG  
8643  C CD  . GLN C 229 ? 0.8903 0.5230 0.6369 -0.0628 0.0355  -0.0324 530 GLN C CD  
8644  O OE1 . GLN C 229 ? 0.8093 0.4523 0.5703 -0.0546 0.0357  -0.0251 530 GLN C OE1 
8645  N NE2 . GLN C 229 ? 1.0271 0.6331 0.7523 -0.0796 0.0349  -0.0368 530 GLN C NE2 
8646  N N   . ALA C 230 ? 0.7801 0.4847 0.5457 -0.0564 0.0320  -0.0426 531 ALA C N   
8647  C CA  . ALA C 230 ? 0.7748 0.5015 0.5462 -0.0708 0.0255  -0.0425 531 ALA C CA  
8648  C C   . ALA C 230 ? 0.7724 0.4804 0.5256 -0.0889 0.0231  -0.0482 531 ALA C C   
8649  O O   . ALA C 230 ? 0.7007 0.3764 0.4299 -0.0901 0.0272  -0.0556 531 ALA C O   
8650  C CB  . ALA C 230 ? 0.9020 0.6431 0.6720 -0.0673 0.0256  -0.0452 531 ALA C CB  
8651  N N   . ASN C 231 ? 0.7884 0.5172 0.5523 -0.1027 0.0167  -0.0449 532 ASN C N   
8652  C CA  . ASN C 231 ? 0.8442 0.5645 0.5939 -0.1233 0.0133  -0.0498 532 ASN C CA  
8653  C C   . ASN C 231 ? 0.8763 0.5546 0.6033 -0.1288 0.0179  -0.0538 532 ASN C C   
8654  O O   . ASN C 231 ? 0.9574 0.6113 0.6602 -0.1417 0.0183  -0.0617 532 ASN C O   
8655  C CB  . ASN C 231 ? 0.9218 0.6468 0.6590 -0.1311 0.0107  -0.0566 532 ASN C CB  
8656  C CG  . ASN C 231 ? 1.0517 0.7889 0.7847 -0.1533 0.0042  -0.0591 532 ASN C CG  
8657  O OD1 . ASN C 231 ? 1.0561 0.8169 0.8057 -0.1601 -0.0002 -0.0534 532 ASN C OD1 
8658  N ND2 . ASN C 231 ? 1.1176 0.8403 0.8280 -0.1650 0.0036  -0.0680 532 ASN C ND2 
8659  N N   . GLY C 232 ? 0.8953 0.5630 0.6283 -0.1195 0.0212  -0.0482 533 GLY C N   
8660  C CA  . GLY C 232 ? 0.8890 0.5161 0.6004 -0.1246 0.0249  -0.0499 533 GLY C CA  
8661  C C   . GLY C 232 ? 1.0310 0.6152 0.7153 -0.1140 0.0312  -0.0570 533 GLY C C   
8662  O O   . GLY C 232 ? 1.0393 0.5834 0.7015 -0.1170 0.0344  -0.0584 533 GLY C O   
8663  N N   . ASN C 233 ? 1.0099 0.6002 0.6936 -0.1011 0.0334  -0.0614 534 ASN C N   
8664  C CA  . ASN C 233 ? 1.0130 0.5652 0.6703 -0.0896 0.0398  -0.0693 534 ASN C CA  
8665  C C   . ASN C 233 ? 0.9184 0.4582 0.5788 -0.0658 0.0453  -0.0649 534 ASN C C   
8666  O O   . ASN C 233 ? 0.8950 0.4578 0.5788 -0.0588 0.0441  -0.0559 534 ASN C O   
8667  C CB  . ASN C 233 ? 1.0473 0.6147 0.7028 -0.0854 0.0404  -0.0759 534 ASN C CB  
8668  C CG  . ASN C 233 ? 1.0416 0.6178 0.6894 -0.1084 0.0347  -0.0811 534 ASN C CG  
8669  O OD1 . ASN C 233 ? 1.1703 0.7142 0.7912 -0.1229 0.0348  -0.0886 534 ASN C OD1 
8670  N ND2 . ASN C 233 ? 0.9093 0.5282 0.5791 -0.1121 0.0294  -0.0771 534 ASN C ND2 
8671  N N   . ASP C 234 ? 0.9236 0.4262 0.5586 -0.0528 0.0513  -0.0717 535 ASP C N   
8672  C CA  . ASP C 234 ? 0.9306 0.4247 0.5677 -0.0273 0.0566  -0.0683 535 ASP C CA  
8673  C C   . ASP C 234 ? 0.9387 0.4805 0.6063 -0.0127 0.0569  -0.0636 535 ASP C C   
8674  O O   . ASP C 234 ? 0.9461 0.5126 0.6206 -0.0159 0.0561  -0.0670 535 ASP C O   
8675  C CB  . ASP C 234 ? 1.0887 0.5386 0.6927 -0.0133 0.0631  -0.0778 535 ASP C CB  
8676  C CG  . ASP C 234 ? 1.1618 0.5552 0.7316 -0.0245 0.0635  -0.0812 535 ASP C CG  
8677  O OD1 . ASP C 234 ? 1.1376 0.5279 0.7110 -0.0418 0.0594  -0.0749 535 ASP C OD1 
8678  O OD2 . ASP C 234 ? 1.2024 0.5537 0.7402 -0.0161 0.0683  -0.0905 535 ASP C OD2 
8679  N N   . PRO C 235 ? 0.9817 0.5375 0.6668 0.0018  0.0579  -0.0554 536 PRO C N   
8680  C CA  . PRO C 235 ? 0.8988 0.4988 0.6113 0.0134  0.0581  -0.0509 536 PRO C CA  
8681  C C   . PRO C 235 ? 0.8569 0.4600 0.5623 0.0316  0.0643  -0.0573 536 PRO C C   
8682  O O   . PRO C 235 ? 0.8959 0.4652 0.5765 0.0426  0.0693  -0.0641 536 PRO C O   
8683  C CB  . PRO C 235 ? 0.7618 0.3693 0.4894 0.0233  0.0576  -0.0416 536 PRO C CB  
8684  C CG  . PRO C 235 ? 0.8674 0.4285 0.5700 0.0250  0.0595  -0.0423 536 PRO C CG  
8685  C CD  . PRO C 235 ? 0.8704 0.4058 0.5525 0.0037  0.0574  -0.0487 536 PRO C CD  
8686  N N   . GLU C 236 ? 0.7888 0.4332 0.5157 0.0350  0.0642  -0.0548 537 GLU C N   
8687  C CA  . GLU C 236 ? 0.7722 0.4300 0.4962 0.0493  0.0700  -0.0603 537 GLU C CA  
8688  C C   . GLU C 236 ? 0.7370 0.4334 0.4859 0.0626  0.0715  -0.0534 537 GLU C C   
8689  O O   . GLU C 236 ? 0.6771 0.4001 0.4481 0.0539  0.0667  -0.0457 537 GLU C O   
8690  C CB  . GLU C 236 ? 0.7030 0.3734 0.4237 0.0355  0.0686  -0.0653 537 GLU C CB  
8691  C CG  . GLU C 236 ? 0.7782 0.4157 0.4763 0.0185  0.0657  -0.0716 537 GLU C CG  
8692  C CD  . GLU C 236 ? 0.9252 0.5735 0.6164 0.0060  0.0642  -0.0775 537 GLU C CD  
8693  O OE1 . GLU C 236 ? 0.9404 0.6128 0.6367 0.0135  0.0676  -0.0790 537 GLU C OE1 
8694  O OE2 . GLU C 236 ? 0.9447 0.5783 0.6246 -0.0122 0.0595  -0.0805 537 GLU C OE2 
8695  N N   . LEU C 237 ? 0.6926 0.3925 0.4370 0.0837  0.0781  -0.0567 538 LEU C N   
8696  C CA  . LEU C 237 ? 0.6859 0.4255 0.4528 0.0959  0.0799  -0.0510 538 LEU C CA  
8697  C C   . LEU C 237 ? 0.7226 0.5000 0.5013 0.0896  0.0810  -0.0517 538 LEU C C   
8698  O O   . LEU C 237 ? 0.7953 0.5678 0.5601 0.0863  0.0838  -0.0590 538 LEU C O   
8699  C CB  . LEU C 237 ? 0.6488 0.3820 0.4071 0.1223  0.0864  -0.0539 538 LEU C CB  
8700  C CG  . LEU C 237 ? 0.8842 0.5867 0.6343 0.1327  0.0852  -0.0501 538 LEU C CG  
8701  C CD1 . LEU C 237 ? 0.9490 0.6377 0.6835 0.1608  0.0919  -0.0547 538 LEU C CD1 
8702  C CD2 . LEU C 237 ? 0.8307 0.5587 0.6058 0.1294  0.0803  -0.0392 538 LEU C CD2 
8703  N N   . PHE C 238 ? 0.7249 0.5388 0.5277 0.0871  0.0789  -0.0439 539 PHE C N   
8704  C CA  . PHE C 238 ? 0.6800 0.5311 0.4947 0.0805  0.0799  -0.0425 539 PHE C CA  
8705  C C   . PHE C 238 ? 0.7718 0.6588 0.6073 0.0884  0.0809  -0.0362 539 PHE C C   
8706  O O   . PHE C 238 ? 0.8586 0.7468 0.7063 0.0868  0.0764  -0.0296 539 PHE C O   
8707  C CB  . PHE C 238 ? 0.6765 0.5303 0.4969 0.0586  0.0729  -0.0385 539 PHE C CB  
8708  C CG  . PHE C 238 ? 0.7266 0.5518 0.5286 0.0483  0.0709  -0.0441 539 PHE C CG  
8709  C CD1 . PHE C 238 ? 0.7189 0.5147 0.5144 0.0424  0.0665  -0.0439 539 PHE C CD1 
8710  C CD2 . PHE C 238 ? 0.6795 0.5090 0.4700 0.0432  0.0732  -0.0497 539 PHE C CD2 
8711  C CE1 . PHE C 238 ? 0.7693 0.5415 0.5477 0.0310  0.0643  -0.0494 539 PHE C CE1 
8712  C CE2 . PHE C 238 ? 0.6813 0.4862 0.4541 0.0327  0.0708  -0.0553 539 PHE C CE2 
8713  C CZ  . PHE C 238 ? 0.7221 0.4990 0.4891 0.0261  0.0662  -0.0553 539 PHE C CZ  
8714  N N   . GLN C 239 ? 0.8063 0.7249 0.6460 0.0953  0.0866  -0.0382 540 GLN C N   
8715  C CA  . GLN C 239 ? 0.7493 0.7078 0.6092 0.0993  0.0874  -0.0324 540 GLN C CA  
8716  C C   . GLN C 239 ? 0.5743 0.5553 0.4462 0.0785  0.0833  -0.0265 540 GLN C C   
8717  O O   . GLN C 239 ? 0.6311 0.6201 0.4969 0.0691  0.0852  -0.0287 540 GLN C O   
8718  C CB  . GLN C 239 ? 0.8625 0.8486 0.7217 0.1170  0.0959  -0.0373 540 GLN C CB  
8719  C CG  . GLN C 239 ? 0.9916 1.0218 0.8718 0.1217  0.0965  -0.0316 540 GLN C CG  
8720  C CD  . GLN C 239 ? 1.0990 1.1732 0.9840 0.1244  0.1036  -0.0343 540 GLN C CD  
8721  O OE1 . GLN C 239 ? 1.1346 1.2057 1.0063 0.1260  0.1089  -0.0410 540 GLN C OE1 
8722  N NE2 . GLN C 239 ? 1.1546 1.2715 1.0583 0.1236  0.1038  -0.0292 540 GLN C NE2 
8723  N N   . ILE C 240 ? 0.5078 0.4962 0.3943 0.0712  0.0777  -0.0191 541 ILE C N   
8724  C CA  . ILE C 240 ? 0.5306 0.5381 0.4267 0.0529  0.0739  -0.0132 541 ILE C CA  
8725  C C   . ILE C 240 ? 0.5589 0.6062 0.4608 0.0530  0.0796  -0.0134 541 ILE C C   
8726  O O   . ILE C 240 ? 0.5449 0.6157 0.4542 0.0671  0.0839  -0.0144 541 ILE C O   
8727  C CB  . ILE C 240 ? 0.5822 0.5906 0.4918 0.0477  0.0676  -0.0063 541 ILE C CB  
8728  C CG1 . ILE C 240 ? 0.5455 0.5188 0.4501 0.0489  0.0630  -0.0062 541 ILE C CG1 
8729  C CG2 . ILE C 240 ? 0.5080 0.5276 0.4231 0.0290  0.0632  -0.0008 541 ILE C CG2 
8730  C CD1 . ILE C 240 ? 0.6025 0.5779 0.5193 0.0469  0.0579  -0.0003 541 ILE C CD1 
8731  N N   . PRO C 241 ? 0.4898 0.5476 0.3879 0.0381  0.0799  -0.0122 542 PRO C N   
8732  C CA  . PRO C 241 ? 0.5129 0.6110 0.4164 0.0353  0.0855  -0.0116 542 PRO C CA  
8733  C C   . PRO C 241 ? 0.4847 0.6093 0.4051 0.0314  0.0833  -0.0056 542 PRO C C   
8734  O O   . PRO C 241 ? 0.5511 0.6653 0.4757 0.0181  0.0765  0.0002  542 PRO C O   
8735  C CB  . PRO C 241 ? 0.5557 0.6509 0.4495 0.0163  0.0843  -0.0096 542 PRO C CB  
8736  C CG  . PRO C 241 ? 0.4564 0.5126 0.3369 0.0159  0.0805  -0.0125 542 PRO C CG  
8737  C CD  . PRO C 241 ? 0.5150 0.5489 0.4016 0.0242  0.0757  -0.0118 542 PRO C CD  
8738  N N   . PRO C 242 ? 0.5147 0.6743 0.4445 0.0436  0.0887  -0.0073 543 PRO C N   
8739  C CA  . PRO C 242 ? 0.5511 0.7392 0.4972 0.0405  0.0864  -0.0021 543 PRO C CA  
8740  C C   . PRO C 242 ? 0.6121 0.8106 0.5610 0.0154  0.0825  0.0042  543 PRO C C   
8741  O O   . PRO C 242 ? 0.5765 0.7774 0.5342 0.0082  0.0772  0.0089  543 PRO C O   
8742  C CB  . PRO C 242 ? 0.5634 0.7955 0.5167 0.0555  0.0942  -0.0057 543 PRO C CB  
8743  C CG  . PRO C 242 ? 0.4942 0.7072 0.4348 0.0748  0.0995  -0.0133 543 PRO C CG  
8744  C CD  . PRO C 242 ? 0.5516 0.7265 0.4767 0.0623  0.0972  -0.0145 543 PRO C CD  
8745  N N   . GLU C 243 ? 0.4712 0.6728 0.4103 0.0015  0.0850  0.0043  544 GLU C N   
8746  C CA  . GLU C 243 ? 0.4781 0.6859 0.4157 -0.0228 0.0817  0.0106  544 GLU C CA  
8747  C C   . GLU C 243 ? 0.4725 0.6404 0.4055 -0.0321 0.0728  0.0150  544 GLU C C   
8748  O O   . GLU C 243 ? 0.4859 0.6533 0.4176 -0.0500 0.0688  0.0205  544 GLU C O   
8749  C CB  . GLU C 243 ? 0.5528 0.7696 0.4780 -0.0348 0.0865  0.0104  544 GLU C CB  
8750  C CG  . GLU C 243 ? 0.5756 0.7568 0.4852 -0.0320 0.0856  0.0075  544 GLU C CG  
8751  C CD  . GLU C 243 ? 0.6297 0.8183 0.5355 -0.0132 0.0931  -0.0008 544 GLU C CD  
8752  O OE1 . GLU C 243 ? 0.5729 0.7863 0.4894 0.0028  0.0977  -0.0043 544 GLU C OE1 
8753  O OE2 . GLU C 243 ? 0.7361 0.9059 0.6270 -0.0137 0.0944  -0.0040 544 GLU C OE2 
8754  N N   . LEU C 244 ? 0.4877 0.6224 0.4170 -0.0207 0.0698  0.0124  545 LEU C N   
8755  C CA  . LEU C 244 ? 0.4578 0.5599 0.3855 -0.0261 0.0616  0.0159  545 LEU C CA  
8756  C C   . LEU C 244 ? 0.5311 0.6348 0.4715 -0.0188 0.0583  0.0172  545 LEU C C   
8757  O O   . LEU C 244 ? 0.5161 0.5986 0.4565 -0.0247 0.0518  0.0204  545 LEU C O   
8758  C CB  . LEU C 244 ? 0.4945 0.5631 0.4121 -0.0199 0.0597  0.0128  545 LEU C CB  
8759  C CG  . LEU C 244 ? 0.5042 0.5663 0.4071 -0.0258 0.0620  0.0111  545 LEU C CG  
8760  C CD1 . LEU C 244 ? 0.4593 0.4889 0.3535 -0.0214 0.0583  0.0083  545 LEU C CD1 
8761  C CD2 . LEU C 244 ? 0.4527 0.5169 0.3486 -0.0449 0.0594  0.0172  545 LEU C CD2 
8762  N N   . VAL C 245 ? 0.5513 0.6795 0.5016 -0.0051 0.0624  0.0148  546 VAL C N   
8763  C CA  . VAL C 245 ? 0.5107 0.6390 0.4714 0.0039  0.0592  0.0161  546 VAL C CA  
8764  C C   . VAL C 245 ? 0.4165 0.5784 0.3874 -0.0060 0.0584  0.0195  546 VAL C C   
8765  O O   . VAL C 245 ? 0.4101 0.6091 0.3893 0.0005  0.0630  0.0183  546 VAL C O   
8766  C CB  . VAL C 245 ? 0.4991 0.6291 0.4621 0.0267  0.0631  0.0120  546 VAL C CB  
8767  C CG1 . VAL C 245 ? 0.3748 0.5027 0.3464 0.0347  0.0592  0.0145  546 VAL C CG1 
8768  C CG2 . VAL C 245 ? 0.4908 0.5859 0.4408 0.0337  0.0641  0.0079  546 VAL C CG2 
8769  N N   . LEU C 246 ? 0.4609 0.6103 0.4304 -0.0217 0.0525  0.0235  547 LEU C N   
8770  C CA  . LEU C 246 ? 0.4395 0.6158 0.4158 -0.0346 0.0510  0.0265  547 LEU C CA  
8771  C C   . LEU C 246 ? 0.4742 0.6654 0.4629 -0.0224 0.0493  0.0265  547 LEU C C   
8772  O O   . LEU C 246 ? 0.4168 0.5824 0.4055 -0.0136 0.0456  0.0266  547 LEU C O   
8773  C CB  . LEU C 246 ? 0.4160 0.5671 0.3832 -0.0538 0.0450  0.0301  547 LEU C CB  
8774  C CG  . LEU C 246 ? 0.4509 0.6215 0.4207 -0.0705 0.0425  0.0328  547 LEU C CG  
8775  C CD1 . LEU C 246 ? 0.3712 0.5837 0.3439 -0.0800 0.0482  0.0329  547 LEU C CD1 
8776  C CD2 . LEU C 246 ? 0.4723 0.6092 0.4282 -0.0874 0.0369  0.0358  547 LEU C CD2 
8777  N N   . GLU C 247 ? 0.5158 0.7505 0.5146 -0.0219 0.0520  0.0265  548 GLU C N   
8778  C CA  . GLU C 247 ? 0.4552 0.7107 0.4659 -0.0093 0.0505  0.0269  548 GLU C CA  
8779  C C   . GLU C 247 ? 0.4985 0.7894 0.5163 -0.0258 0.0484  0.0291  548 GLU C C   
8780  O O   . GLU C 247 ? 0.4221 0.7363 0.4385 -0.0422 0.0510  0.0295  548 GLU C O   
8781  C CB  . GLU C 247 ? 0.4174 0.6961 0.4343 0.0144  0.0562  0.0241  548 GLU C CB  
8782  C CG  . GLU C 247 ? 0.4441 0.6854 0.4528 0.0325  0.0577  0.0215  548 GLU C CG  
8783  C CD  . GLU C 247 ? 0.5165 0.7769 0.5283 0.0575  0.0632  0.0185  548 GLU C CD  
8784  O OE1 . GLU C 247 ? 0.5341 0.8260 0.5481 0.0597  0.0691  0.0159  548 GLU C OE1 
8785  O OE2 . GLU C 247 ? 0.5961 0.8401 0.6071 0.0754  0.0618  0.0187  548 GLU C OE2 
8786  N N   . VAL C 248 ? 0.4318 0.7275 0.4562 -0.0222 0.0436  0.0305  549 VAL C N   
8787  C CA  . VAL C 248 ? 0.4369 0.7623 0.4667 -0.0391 0.0403  0.0322  549 VAL C CA  
8788  C C   . VAL C 248 ? 0.5116 0.8809 0.5560 -0.0233 0.0408  0.0323  549 VAL C C   
8789  O O   . VAL C 248 ? 0.5942 0.9510 0.6413 -0.0058 0.0382  0.0330  549 VAL C O   
8790  C CB  . VAL C 248 ? 0.5258 0.8166 0.5479 -0.0515 0.0333  0.0336  549 VAL C CB  
8791  C CG1 . VAL C 248 ? 0.5023 0.8200 0.5263 -0.0724 0.0299  0.0345  549 VAL C CG1 
8792  C CG2 . VAL C 248 ? 0.6233 0.8680 0.6306 -0.0616 0.0324  0.0337  549 VAL C CG2 
8793  N N   . PRO C 249 ? 0.5072 0.9293 0.5607 -0.0284 0.0439  0.0320  550 PRO C N   
8794  C CA  . PRO C 249 ? 0.4452 0.9137 0.5132 -0.0137 0.0432  0.0326  550 PRO C CA  
8795  C C   . PRO C 249 ? 0.5759 1.0493 0.6458 -0.0274 0.0359  0.0345  550 PRO C C   
8796  O O   . PRO C 249 ? 0.6184 1.0898 0.6823 -0.0546 0.0333  0.0347  550 PRO C O   
8797  C CB  . PRO C 249 ? 0.4907 1.0164 0.5673 -0.0194 0.0489  0.0314  550 PRO C CB  
8798  C CG  . PRO C 249 ? 0.5417 1.0524 0.6072 -0.0494 0.0499  0.0315  550 PRO C CG  
8799  C CD  . PRO C 249 ? 0.5420 0.9861 0.5927 -0.0480 0.0484  0.0315  550 PRO C CD  
8800  N N   . ILE C 250 ? 0.5631 1.0396 0.6387 -0.0084 0.0324  0.0359  551 ILE C N   
8801  C CA  . ILE C 250 ? 0.4522 0.9263 0.5275 -0.0185 0.0252  0.0374  551 ILE C CA  
8802  C C   . ILE C 250 ? 0.4678 1.0057 0.5556 -0.0256 0.0234  0.0379  551 ILE C C   
8803  O O   . ILE C 250 ? 0.4194 0.9967 0.5190 -0.0041 0.0247  0.0389  551 ILE C O   
8804  C CB  . ILE C 250 ? 0.4699 0.9145 0.5435 0.0036  0.0221  0.0392  551 ILE C CB  
8805  C CG1 . ILE C 250 ? 0.3538 0.7431 0.4168 0.0130  0.0248  0.0385  551 ILE C CG1 
8806  C CG2 . ILE C 250 ? 0.3401 0.7749 0.4102 -0.0098 0.0149  0.0401  551 ILE C CG2 
8807  C CD1 . ILE C 250 ? 0.3145 0.6613 0.3657 -0.0077 0.0223  0.0375  551 ILE C CD1 
8808  N N   . ARG C 251 ? 0.5666 1.1143 0.6507 -0.0555 0.0203  0.0372  552 ARG C N   
8809  C CA  . ARG C 251 ? 0.5290 1.1348 0.6231 -0.0676 0.0172  0.0374  552 ARG C CA  
8810  C C   . ARG C 251 ? 0.4875 1.0741 0.5733 -0.0852 0.0094  0.0371  552 ARG C C   
8811  O O   . ARG C 251 ? 0.3910 0.9210 0.4627 -0.0916 0.0073  0.0364  552 ARG C O   
8812  C CB  . ARG C 251 ? 0.5639 1.2080 0.6600 -0.0913 0.0212  0.0362  552 ARG C CB  
8813  C CG  . ARG C 251 ? 0.6153 1.2145 0.6936 -0.1186 0.0218  0.0353  552 ARG C CG  
8814  C CD  . ARG C 251 ? 0.5943 1.1665 0.6677 -0.1089 0.0286  0.0351  552 ARG C CD  
8815  N NE  . ARG C 251 ? 0.6114 1.1513 0.6678 -0.1371 0.0292  0.0351  552 ARG C NE  
8816  C CZ  . ARG C 251 ? 0.5968 1.0912 0.6416 -0.1349 0.0321  0.0353  552 ARG C CZ  
8817  N NH1 . ARG C 251 ? 0.6886 1.1552 0.7166 -0.1609 0.0318  0.0360  552 ARG C NH1 
8818  N NH2 . ARG C 251 ? 0.5099 0.9851 0.5582 -0.1073 0.0350  0.0348  552 ARG C NH2 
8819  N N   . HIS C 252 ? 0.4606 1.0975 0.5551 -0.0927 0.0052  0.0373  553 HIS C N   
8820  C CA  . HIS C 252 ? 0.4664 1.0919 0.5531 -0.1089 -0.0023 0.0363  553 HIS C CA  
8821  C C   . HIS C 252 ? 0.4869 1.1395 0.5689 -0.1454 -0.0043 0.0340  553 HIS C C   
8822  O O   . HIS C 252 ? 0.5194 1.2298 0.6128 -0.1526 -0.0017 0.0342  553 HIS C O   
8823  C CB  . HIS C 252 ? 0.4123 1.0709 0.5102 -0.0887 -0.0071 0.0385  553 HIS C CB  
8824  C CG  . HIS C 252 ? 0.5428 1.1779 0.6306 -0.0987 -0.0143 0.0375  553 HIS C CG  
8825  N ND1 . HIS C 252 ? 0.5838 1.2458 0.6683 -0.1258 -0.0197 0.0350  553 HIS C ND1 
8826  C CD2 . HIS C 252 ? 0.5390 1.1280 0.6185 -0.0855 -0.0170 0.0383  553 HIS C CD2 
8827  C CE1 . HIS C 252 ? 0.5504 1.1821 0.6245 -0.1278 -0.0252 0.0339  553 HIS C CE1 
8828  N NE2 . HIS C 252 ? 0.5652 1.1538 0.6368 -0.1034 -0.0235 0.0361  553 HIS C NE2 
8829  N N   . PRO C 253 ? 0.4080 1.0200 0.4721 -0.1691 -0.0087 0.0316  554 PRO C N   
8830  C CA  . PRO C 253 ? 0.4039 1.0336 0.4588 -0.2067 -0.0106 0.0292  554 PRO C CA  
8831  C C   . PRO C 253 ? 0.5090 1.2069 0.5758 -0.2164 -0.0149 0.0286  554 PRO C C   
8832  O O   . PRO C 253 ? 0.5641 1.2927 0.6273 -0.2453 -0.0148 0.0272  554 PRO C O   
8833  C CB  . PRO C 253 ? 0.3896 0.9523 0.4205 -0.2229 -0.0148 0.0263  554 PRO C CB  
8834  C CG  . PRO C 253 ? 0.4417 0.9740 0.4750 -0.1939 -0.0170 0.0271  554 PRO C CG  
8835  C CD  . PRO C 253 ? 0.3551 0.8998 0.4044 -0.1633 -0.0113 0.0306  554 PRO C CD  
8836  N N   . LYS C 254 ? 0.4776 1.1985 0.5563 -0.1934 -0.0188 0.0300  555 LYS C N   
8837  C CA  . LYS C 254 ? 0.5031 1.2876 0.5918 -0.1996 -0.0240 0.0297  555 LYS C CA  
8838  C C   . LYS C 254 ? 0.4878 1.3232 0.5950 -0.1671 -0.0212 0.0333  555 LYS C C   
8839  O O   . LYS C 254 ? 0.4546 1.3337 0.5618 -0.1713 -0.0204 0.0330  555 LYS C O   
8840  C CB  . LYS C 254 ? 0.5837 1.3469 0.6639 -0.2006 -0.0320 0.0281  555 LYS C CB  
8841  C CG  . LYS C 254 ? 0.7174 1.4526 0.7754 -0.2385 -0.0363 0.0230  555 LYS C CG  
8842  C CD  . LYS C 254 ? 0.8599 1.6350 0.9105 -0.2554 -0.0370 0.0215  555 LYS C CD  
8843  C CE  . LYS C 254 ? 0.9165 1.6606 0.9405 -0.2943 -0.0369 0.0172  555 LYS C CE  
8844  N NZ  . LYS C 254 ? 0.8810 1.5720 0.8851 -0.3097 -0.0425 0.0127  555 LYS C NZ  
8845  N N   . PHE C 255 ? 0.5662 1.3921 0.6857 -0.1339 -0.0195 0.0366  556 PHE C N   
8846  C CA  . PHE C 255 ? 0.6096 1.4758 0.7437 -0.0992 -0.0174 0.0400  556 PHE C CA  
8847  C C   . PHE C 255 ? 0.5861 1.4660 0.7251 -0.0925 -0.0089 0.0398  556 PHE C C   
8848  O O   . PHE C 255 ? 0.4914 1.3415 0.6332 -0.0795 -0.0037 0.0406  556 PHE C O   
8849  C CB  . PHE C 255 ? 0.6191 1.4525 0.7551 -0.0660 -0.0189 0.0436  556 PHE C CB  
8850  C CG  . PHE C 255 ? 0.5760 1.3870 0.7027 -0.0701 -0.0267 0.0438  556 PHE C CG  
8851  C CD1 . PHE C 255 ? 0.4938 1.3522 0.6239 -0.0820 -0.0334 0.0434  556 PHE C CD1 
8852  C CD2 . PHE C 255 ? 0.5981 1.3396 0.7108 -0.0619 -0.0271 0.0441  556 PHE C CD2 
8853  C CE1 . PHE C 255 ? 0.4970 1.3385 0.6189 -0.0858 -0.0408 0.0433  556 PHE C CE1 
8854  C CE2 . PHE C 255 ? 0.5284 1.2513 0.6321 -0.0651 -0.0337 0.0441  556 PHE C CE2 
8855  C CZ  . PHE C 255 ? 0.4657 1.2374 0.5734 -0.0769 -0.0404 0.0436  556 PHE C CZ  
8856  N N   . GLU C 256 ? 0.6880 1.6111 0.8258 -0.1007 -0.0072 0.0385  557 GLU C N   
8857  C CA  . GLU C 256 ? 0.7276 1.6677 0.8693 -0.0930 0.0003  0.0379  557 GLU C CA  
8858  C C   . GLU C 256 ? 0.6625 1.6026 0.8152 -0.0506 0.0041  0.0404  557 GLU C C   
8859  O O   . GLU C 256 ? 0.7380 1.6677 0.8929 -0.0411 0.0111  0.0396  557 GLU C O   
8860  C CB  . GLU C 256 ? 0.8106 1.8040 0.9499 -0.1048 0.0003  0.0365  557 GLU C CB  
8861  C CG  . GLU C 256 ? 0.9334 1.9249 1.0579 -0.1478 -0.0023 0.0338  557 GLU C CG  
8862  C CD  . GLU C 256 ? 1.0797 2.0545 1.1957 -0.1703 0.0030  0.0321  557 GLU C CD  
8863  O OE1 . GLU C 256 ? 1.1537 2.1338 1.2554 -0.2034 0.0017  0.0302  557 GLU C OE1 
8864  O OE2 . GLU C 256 ? 1.1123 2.0674 1.2339 -0.1550 0.0086  0.0327  557 GLU C OE2 
8865  N N   . TRP C 257 ? 0.5509 1.4983 0.7078 -0.0249 -0.0002 0.0433  558 TRP C N   
8866  C CA  . TRP C 257 ? 0.4865 1.4305 0.6490 0.0163  0.0030  0.0458  558 TRP C CA  
8867  C C   . TRP C 257 ? 0.5079 1.3995 0.6709 0.0298  0.0058  0.0471  558 TRP C C   
8868  O O   . TRP C 257 ? 0.6079 1.4869 0.7720 0.0630  0.0093  0.0487  558 TRP C O   
8869  C CB  . TRP C 257 ? 0.5728 1.5367 0.7357 0.0383  -0.0027 0.0494  558 TRP C CB  
8870  C CG  . TRP C 257 ? 0.5255 1.4711 0.6850 0.0253  -0.0103 0.0509  558 TRP C CG  
8871  C CD1 . TRP C 257 ? 0.6184 1.5880 0.7740 0.0010  -0.0159 0.0499  558 TRP C CD1 
8872  C CD2 . TRP C 257 ? 0.4670 1.3662 0.6251 0.0354  -0.0130 0.0536  558 TRP C CD2 
8873  N NE1 . TRP C 257 ? 0.5434 1.4838 0.6950 -0.0041 -0.0222 0.0512  558 TRP C NE1 
8874  C CE2 . TRP C 257 ? 0.4858 1.3841 0.6392 0.0168  -0.0208 0.0537  558 TRP C CE2 
8875  C CE3 . TRP C 257 ? 0.4118 1.2700 0.5706 0.0583  -0.0097 0.0556  558 TRP C CE3 
8876  C CZ2 . TRP C 257 ? 0.4748 1.3343 0.6248 0.0205  -0.0258 0.0560  558 TRP C CZ2 
8877  C CZ3 . TRP C 257 ? 0.4653 1.2666 0.6118 0.0601  -0.0135 0.0575  558 TRP C CZ3 
8878  C CH2 . TRP C 257 ? 0.5475 1.3496 0.6894 0.0419  -0.0212 0.0577  558 TRP C CH2 
8879  N N   . PHE C 258 ? 0.4887 1.3428 0.6466 0.0051  0.0041  0.0461  559 PHE C N   
8880  C CA  . PHE C 258 ? 0.4962 1.2733 0.6397 0.0168  0.0059  0.0465  559 PHE C CA  
8881  C C   . PHE C 258 ? 0.4604 1.2189 0.6019 0.0263  0.0146  0.0446  559 PHE C C   
8882  O O   . PHE C 258 ? 0.4461 1.1681 0.5826 0.0528  0.0175  0.0456  559 PHE C O   
8883  C CB  . PHE C 258 ? 0.5178 1.2443 0.6466 -0.0120 0.0019  0.0448  559 PHE C CB  
8884  C CG  . PHE C 258 ? 0.5710 1.2295 0.6873 0.0019  0.0009  0.0461  559 PHE C CG  
8885  C CD1 . PHE C 258 ? 0.4846 1.0957 0.5933 0.0110  0.0066  0.0453  559 PHE C CD1 
8886  C CD2 . PHE C 258 ? 0.5417 1.1860 0.6536 0.0054  -0.0057 0.0482  559 PHE C CD2 
8887  C CE1 . PHE C 258 ? 0.4743 1.0272 0.5721 0.0224  0.0056  0.0465  559 PHE C CE1 
8888  C CE2 . PHE C 258 ? 0.5001 1.0856 0.6008 0.0171  -0.0062 0.0496  559 PHE C CE2 
8889  C CZ  . PHE C 258 ? 0.4550 0.9954 0.5490 0.0252  -0.0006 0.0488  559 PHE C CZ  
8890  N N   . LYS C 259 ? 0.3898 1.1709 0.5334 0.0035  0.0189  0.0418  560 LYS C N   
8891  C CA  . LYS C 259 ? 0.4203 1.1871 0.5613 0.0115  0.0273  0.0397  560 LYS C CA  
8892  C C   . LYS C 259 ? 0.4534 1.2466 0.6035 0.0500  0.0317  0.0403  560 LYS C C   
8893  O O   . LYS C 259 ? 0.3692 1.1264 0.5122 0.0682  0.0371  0.0390  560 LYS C O   
8894  C CB  . LYS C 259 ? 0.4324 1.2339 0.5758 -0.0184 0.0313  0.0374  560 LYS C CB  
8895  C CG  . LYS C 259 ? 0.4561 1.3311 0.6110 -0.0238 0.0297  0.0372  560 LYS C CG  
8896  C CD  . LYS C 259 ? 0.5171 1.4072 0.6646 -0.0573 0.0318  0.0349  560 LYS C CD  
8897  C CE  . LYS C 259 ? 0.5595 1.5063 0.7089 -0.0591 0.0294  0.0339  560 LYS C CE  
8898  N NZ  . LYS C 259 ? 0.5575 1.5235 0.7046 -0.0763 0.0211  0.0346  560 LYS C NZ  
8899  N N   . ASP C 260 ? 0.5141 1.3647 0.6770 0.0637  0.0286  0.0421  561 ASP C N   
8900  C CA  . ASP C 260 ? 0.5379 1.4000 0.7001 0.1005  0.0308  0.0424  561 ASP C CA  
8901  C C   . ASP C 260 ? 0.4767 1.2949 0.6343 0.1325  0.0307  0.0452  561 ASP C C   
8902  O O   . ASP C 260 ? 0.5496 1.3630 0.7021 0.1637  0.0336  0.0451  561 ASP C O   
8903  C CB  . ASP C 260 ? 0.6889 1.6007 0.8534 0.1034  0.0252  0.0436  561 ASP C CB  
8904  C CG  . ASP C 260 ? 0.7451 1.6992 0.9117 0.0699  0.0247  0.0410  561 ASP C CG  
8905  O OD1 . ASP C 260 ? 0.7528 1.6990 0.9180 0.0500  0.0299  0.0381  561 ASP C OD1 
8906  O OD2 . ASP C 260 ? 0.7258 1.7191 0.8934 0.0631  0.0194  0.0420  561 ASP C OD2 
8907  N N   . LEU C 261 ? 0.4339 1.1996 0.5820 0.1225  0.0260  0.0472  562 LEU C N   
8908  C CA  . LEU C 261 ? 0.5098 1.2154 0.6446 0.1471  0.0256  0.0495  562 LEU C CA  
8909  C C   . LEU C 261 ? 0.6295 1.2907 0.7538 0.1557  0.0333  0.0460  562 LEU C C   
8910  O O   . LEU C 261 ? 0.6343 1.2496 0.7468 0.1785  0.0342  0.0473  562 LEU C O   
8911  C CB  . LEU C 261 ? 0.4707 1.1288 0.5956 0.1306  0.0191  0.0518  562 LEU C CB  
8912  C CG  . LEU C 261 ? 0.5350 1.2260 0.6662 0.1262  0.0108  0.0554  562 LEU C CG  
8913  C CD1 . LEU C 261 ? 0.5155 1.1679 0.6377 0.0992  0.0056  0.0553  562 LEU C CD1 
8914  C CD2 . LEU C 261 ? 0.6176 1.3077 0.7467 0.1613  0.0083  0.0607  562 LEU C CD2 
8915  N N   . GLY C 262 ? 0.5546 1.2276 0.6811 0.1369  0.0386  0.0417  563 GLY C N   
8916  C CA  . GLY C 262 ? 0.5920 1.2285 0.7085 0.1438  0.0458  0.0379  563 GLY C CA  
8917  C C   . GLY C 262 ? 0.6135 1.1746 0.7137 0.1371  0.0444  0.0381  563 GLY C C   
8918  O O   . GLY C 262 ? 0.6394 1.1607 0.7285 0.1555  0.0482  0.0365  563 GLY C O   
8919  N N   . LEU C 263 ? 0.5659 1.1071 0.6637 0.1113  0.0389  0.0396  564 LEU C N   
8920  C CA  . LEU C 263 ? 0.4872 0.9626 0.5711 0.1047  0.0368  0.0400  564 LEU C CA  
8921  C C   . LEU C 263 ? 0.4291 0.8829 0.5071 0.0787  0.0390  0.0370  564 LEU C C   
8922  O O   . LEU C 263 ? 0.4299 0.9151 0.5135 0.0567  0.0391  0.0361  564 LEU C O   
8923  C CB  . LEU C 263 ? 0.4334 0.8979 0.5167 0.0968  0.0290  0.0436  564 LEU C CB  
8924  C CG  . LEU C 263 ? 0.4508 0.9273 0.5365 0.1209  0.0253  0.0480  564 LEU C CG  
8925  C CD1 . LEU C 263 ? 0.4383 0.9164 0.5249 0.1061  0.0177  0.0507  564 LEU C CD1 
8926  C CD2 . LEU C 263 ? 0.4329 0.8604 0.5059 0.1446  0.0273  0.0494  564 LEU C CD2 
8927  N N   . LYS C 264 ? 0.4276 0.8271 0.4932 0.0806  0.0403  0.0358  565 LYS C N   
8928  C CA  . LYS C 264 ? 0.4729 0.8445 0.5307 0.0581  0.0412  0.0338  565 LYS C CA  
8929  C C   . LYS C 264 ? 0.4488 0.7617 0.4948 0.0606  0.0390  0.0343  565 LYS C C   
8930  O O   . LYS C 264 ? 0.5931 0.8869 0.6358 0.0799  0.0383  0.0356  565 LYS C O   
8931  C CB  . LYS C 264 ? 0.3956 0.7793 0.4520 0.0583  0.0484  0.0304  565 LYS C CB  
8932  C CG  . LYS C 264 ? 0.5937 0.9592 0.6443 0.0849  0.0534  0.0280  565 LYS C CG  
8933  C CD  . LYS C 264 ? 0.6361 1.0182 0.6849 0.0854  0.0609  0.0238  565 LYS C CD  
8934  C CE  . LYS C 264 ? 0.7637 1.1453 0.8090 0.1161  0.0664  0.0207  565 LYS C CE  
8935  N NZ  . LYS C 264 ? 0.7799 1.2096 0.8314 0.1228  0.0737  0.0171  565 LYS C NZ  
8936  N N   . TRP C 265 ? 0.3587 0.6435 0.3974 0.0406  0.0375  0.0335  566 TRP C N   
8937  C CA  . TRP C 265 ? 0.3133 0.5470 0.3415 0.0418  0.0360  0.0333  566 TRP C CA  
8938  C C   . TRP C 265 ? 0.5104 0.7259 0.5310 0.0268  0.0380  0.0312  566 TRP C C   
8939  O O   . TRP C 265 ? 0.5342 0.7729 0.5565 0.0124  0.0395  0.0307  566 TRP C O   
8940  C CB  . TRP C 265 ? 0.3918 0.6066 0.4187 0.0348  0.0297  0.0357  566 TRP C CB  
8941  C CG  . TRP C 265 ? 0.3786 0.5508 0.3974 0.0442  0.0289  0.0361  566 TRP C CG  
8942  C CD1 . TRP C 265 ? 0.4092 0.5463 0.4204 0.0343  0.0269  0.0355  566 TRP C CD1 
8943  C CD2 . TRP C 265 ? 0.4420 0.6030 0.4584 0.0652  0.0301  0.0375  566 TRP C CD2 
8944  N NE1 . TRP C 265 ? 0.4677 0.5760 0.4733 0.0458  0.0270  0.0361  566 TRP C NE1 
8945  C CE2 . TRP C 265 ? 0.4136 0.5332 0.4210 0.0641  0.0290  0.0375  566 TRP C CE2 
8946  C CE3 . TRP C 265 ? 0.3260 0.5076 0.3457 0.0851  0.0321  0.0389  566 TRP C CE3 
8947  C CZ2 . TRP C 265 ? 0.3570 0.4535 0.3575 0.0793  0.0298  0.0390  566 TRP C CZ2 
8948  C CZ3 . TRP C 265 ? 0.3926 0.5477 0.4042 0.1024  0.0327  0.0405  566 TRP C CZ3 
8949  C CH2 . TRP C 265 ? 0.4659 0.5778 0.4674 0.0982  0.0317  0.0406  566 TRP C CH2 
8950  N N   . TYR C 266 ? 0.4620 0.6369 0.4733 0.0298  0.0379  0.0302  567 TYR C N   
8951  C CA  . TYR C 266 ? 0.4932 0.6487 0.4960 0.0173  0.0390  0.0287  567 TYR C CA  
8952  C C   . TYR C 266 ? 0.5599 0.6955 0.5583 -0.0005 0.0335  0.0304  567 TYR C C   
8953  O O   . TYR C 266 ? 0.5442 0.6718 0.5444 -0.0010 0.0291  0.0319  567 TYR C O   
8954  C CB  . TYR C 266 ? 0.4618 0.5861 0.4562 0.0286  0.0413  0.0264  567 TYR C CB  
8955  C CG  . TYR C 266 ? 0.4521 0.5495 0.4442 0.0388  0.0386  0.0274  567 TYR C CG  
8956  C CD1 . TYR C 266 ? 0.5038 0.6054 0.4975 0.0573  0.0403  0.0277  567 TYR C CD1 
8957  C CD2 . TYR C 266 ? 0.5007 0.5686 0.4879 0.0303  0.0344  0.0282  567 TYR C CD2 
8958  C CE1 . TYR C 266 ? 0.4807 0.5555 0.4699 0.0650  0.0381  0.0294  567 TYR C CE1 
8959  C CE2 . TYR C 266 ? 0.4699 0.5157 0.4546 0.0378  0.0324  0.0293  567 TYR C CE2 
8960  C CZ  . TYR C 266 ? 0.5281 0.5764 0.5133 0.0540  0.0343  0.0301  567 TYR C CZ  
8961  O OH  . TYR C 266 ? 0.5861 0.6107 0.5669 0.0595  0.0324  0.0319  567 TYR C OH  
8962  N N   . GLY C 267 ? 0.4972 0.6238 0.4882 -0.0143 0.0338  0.0301  568 GLY C N   
8963  C CA  . GLY C 267 ? 0.3422 0.4507 0.3266 -0.0308 0.0289  0.0317  568 GLY C CA  
8964  C C   . GLY C 267 ? 0.3885 0.4588 0.3655 -0.0289 0.0255  0.0317  568 GLY C C   
8965  O O   . GLY C 267 ? 0.4739 0.5282 0.4461 -0.0379 0.0209  0.0328  568 GLY C O   
8966  N N   . LEU C 268 ? 0.4340 0.4902 0.4094 -0.0174 0.0276  0.0301  569 LEU C N   
8967  C CA  . LEU C 268 ? 0.4275 0.4521 0.3955 -0.0179 0.0247  0.0299  569 LEU C CA  
8968  C C   . LEU C 268 ? 0.4815 0.4934 0.4526 -0.0055 0.0241  0.0292  569 LEU C C   
8969  O O   . LEU C 268 ? 0.4452 0.4567 0.4163 0.0052  0.0278  0.0275  569 LEU C O   
8970  C CB  . LEU C 268 ? 0.4290 0.4463 0.3891 -0.0198 0.0273  0.0285  569 LEU C CB  
8971  C CG  . LEU C 268 ? 0.4466 0.4357 0.3992 -0.0210 0.0238  0.0284  569 LEU C CG  
8972  C CD1 . LEU C 268 ? 0.4787 0.4561 0.4261 -0.0318 0.0185  0.0311  569 LEU C CD1 
8973  C CD2 . LEU C 268 ? 0.4910 0.4735 0.4357 -0.0207 0.0263  0.0265  569 LEU C CD2 
8974  N N   . PRO C 269 ? 0.4706 0.4706 0.4428 -0.0066 0.0198  0.0303  570 PRO C N   
8975  C CA  . PRO C 269 ? 0.4250 0.4118 0.3982 0.0030  0.0196  0.0301  570 PRO C CA  
8976  C C   . PRO C 269 ? 0.4059 0.3712 0.3727 0.0010  0.0183  0.0289  570 PRO C C   
8977  O O   . PRO C 269 ? 0.5080 0.4645 0.4717 -0.0061 0.0147  0.0294  570 PRO C O   
8978  C CB  . PRO C 269 ? 0.3422 0.3307 0.3194 0.0015  0.0160  0.0317  570 PRO C CB  
8979  C CG  . PRO C 269 ? 0.3938 0.3817 0.3675 -0.0106 0.0129  0.0319  570 PRO C CG  
8980  C CD  . PRO C 269 ? 0.4469 0.4441 0.4176 -0.0166 0.0155  0.0316  570 PRO C CD  
8981  N N   . ALA C 270 ? 0.4487 0.4050 0.4124 0.0074  0.0210  0.0273  571 ALA C N   
8982  C CA  . ALA C 270 ? 0.4297 0.3697 0.3867 0.0040  0.0199  0.0256  571 ALA C CA  
8983  C C   . ALA C 270 ? 0.3918 0.3180 0.3466 0.0092  0.0206  0.0247  571 ALA C C   
8984  O O   . ALA C 270 ? 0.4365 0.3571 0.3864 0.0152  0.0243  0.0229  571 ALA C O   
8985  C CB  . ALA C 270 ? 0.3485 0.2910 0.2996 0.0023  0.0228  0.0235  571 ALA C CB  
8986  N N   . VAL C 271 ? 0.5437 0.4638 0.5007 0.0069  0.0173  0.0260  572 VAL C N   
8987  C CA  . VAL C 271 ? 0.4690 0.3773 0.4233 0.0096  0.0182  0.0260  572 VAL C CA  
8988  C C   . VAL C 271 ? 0.5554 0.4509 0.5018 0.0055  0.0185  0.0231  572 VAL C C   
8989  O O   . VAL C 271 ? 0.5451 0.4417 0.4914 -0.0007 0.0153  0.0224  572 VAL C O   
8990  C CB  . VAL C 271 ? 0.4132 0.3228 0.3724 0.0075  0.0152  0.0281  572 VAL C CB  
8991  C CG1 . VAL C 271 ? 0.5029 0.4000 0.4573 0.0064  0.0160  0.0281  572 VAL C CG1 
8992  C CG2 . VAL C 271 ? 0.4100 0.3300 0.3747 0.0121  0.0153  0.0306  572 VAL C CG2 
8993  N N   . SER C 272 ? 0.5815 0.4637 0.5196 0.0090  0.0219  0.0214  573 SER C N   
8994  C CA  . SER C 272 ? 0.5747 0.4441 0.5030 0.0041  0.0224  0.0176  573 SER C CA  
8995  C C   . SER C 272 ? 0.6383 0.4892 0.5578 0.0010  0.0232  0.0168  573 SER C C   
8996  O O   . SER C 272 ? 0.6530 0.4917 0.5623 -0.0044 0.0236  0.0130  573 SER C O   
8997  C CB  . SER C 272 ? 0.3880 0.2556 0.3094 0.0092  0.0264  0.0143  573 SER C CB  
8998  O OG  . SER C 272 ? 0.4243 0.2864 0.3423 0.0200  0.0305  0.0145  573 SER C OG  
8999  N N   . ASN C 273 ? 0.6256 0.4734 0.5471 0.0027  0.0232  0.0202  574 ASN C N   
9000  C CA  . ASN C 273 ? 0.5769 0.4051 0.4876 -0.0022 0.0243  0.0201  574 ASN C CA  
9001  C C   . ASN C 273 ? 0.5867 0.4225 0.5029 -0.0124 0.0210  0.0219  574 ASN C C   
9002  O O   . ASN C 273 ? 0.6151 0.4374 0.5230 -0.0186 0.0219  0.0227  574 ASN C O   
9003  C CB  . ASN C 273 ? 0.5874 0.4019 0.4914 0.0073  0.0275  0.0230  574 ASN C CB  
9004  C CG  . ASN C 273 ? 0.5919 0.4230 0.5078 0.0129  0.0262  0.0280  574 ASN C CG  
9005  O OD1 . ASN C 273 ? 0.5426 0.3932 0.4709 0.0094  0.0232  0.0289  574 ASN C OD1 
9006  N ND2 . ASN C 273 ? 0.6466 0.4684 0.5569 0.0222  0.0283  0.0313  574 ASN C ND2 
9007  N N   . MET C 274 ? 0.5444 0.4006 0.4728 -0.0145 0.0174  0.0224  575 MET C N   
9008  C CA  . MET C 274 ? 0.5624 0.4297 0.4969 -0.0216 0.0147  0.0237  575 MET C CA  
9009  C C   . MET C 274 ? 0.6239 0.4963 0.5571 -0.0309 0.0118  0.0206  575 MET C C   
9010  O O   . MET C 274 ? 0.4905 0.3581 0.4183 -0.0317 0.0116  0.0175  575 MET C O   
9011  C CB  . MET C 274 ? 0.5450 0.4305 0.4922 -0.0164 0.0124  0.0261  575 MET C CB  
9012  C CG  . MET C 274 ? 0.4730 0.3571 0.4217 -0.0099 0.0144  0.0295  575 MET C CG  
9013  S SD  . MET C 274 ? 0.5770 0.4800 0.5376 -0.0057 0.0117  0.0312  575 MET C SD  
9014  C CE  . MET C 274 ? 0.4827 0.3936 0.4456 -0.0120 0.0111  0.0323  575 MET C CE  
9015  N N   . LEU C 275 ? 0.5428 0.4273 0.4807 -0.0379 0.0098  0.0213  576 LEU C N   
9016  C CA  . LEU C 275 ? 0.5190 0.4135 0.4565 -0.0473 0.0066  0.0187  576 LEU C CA  
9017  C C   . LEU C 275 ? 0.5362 0.4555 0.4867 -0.0434 0.0023  0.0196  576 LEU C C   
9018  O O   . LEU C 275 ? 0.5683 0.4974 0.5264 -0.0393 0.0025  0.0219  576 LEU C O   
9019  C CB  . LEU C 275 ? 0.6425 0.5323 0.5730 -0.0601 0.0080  0.0184  576 LEU C CB  
9020  C CG  . LEU C 275 ? 0.6127 0.5146 0.5415 -0.0734 0.0050  0.0155  576 LEU C CG  
9021  C CD1 . LEU C 275 ? 0.6577 0.5408 0.5717 -0.0876 0.0078  0.0146  576 LEU C CD1 
9022  C CD2 . LEU C 275 ? 0.4998 0.4340 0.4430 -0.0741 0.0016  0.0168  576 LEU C CD2 
9023  N N   . LEU C 276 ? 0.4948 0.4228 0.4461 -0.0438 -0.0015 0.0178  577 LEU C N   
9024  C CA  . LEU C 276 ? 0.4156 0.3642 0.3763 -0.0383 -0.0061 0.0186  577 LEU C CA  
9025  C C   . LEU C 276 ? 0.4694 0.4384 0.4333 -0.0463 -0.0090 0.0173  577 LEU C C   
9026  O O   . LEU C 276 ? 0.5689 0.5370 0.5264 -0.0554 -0.0102 0.0149  577 LEU C O   
9027  C CB  . LEU C 276 ? 0.4141 0.3591 0.3720 -0.0324 -0.0090 0.0184  577 LEU C CB  
9028  C CG  . LEU C 276 ? 0.4606 0.4211 0.4235 -0.0258 -0.0145 0.0195  577 LEU C CG  
9029  C CD1 . LEU C 276 ? 0.5598 0.5241 0.5293 -0.0166 -0.0146 0.0213  577 LEU C CD1 
9030  C CD2 . LEU C 276 ? 0.4765 0.4284 0.4322 -0.0230 -0.0169 0.0199  577 LEU C CD2 
9031  N N   . GLU C 277 ? 0.4482 0.4374 0.4217 -0.0432 -0.0102 0.0184  578 GLU C N   
9032  C CA  . GLU C 277 ? 0.4613 0.4764 0.4400 -0.0509 -0.0124 0.0173  578 GLU C CA  
9033  C C   . GLU C 277 ? 0.5048 0.5437 0.4922 -0.0396 -0.0177 0.0174  578 GLU C C   
9034  O O   . GLU C 277 ? 0.4996 0.5409 0.4921 -0.0276 -0.0177 0.0187  578 GLU C O   
9035  C CB  . GLU C 277 ? 0.5923 0.6142 0.5740 -0.0576 -0.0084 0.0184  578 GLU C CB  
9036  C CG  . GLU C 277 ? 0.6461 0.6939 0.6310 -0.0708 -0.0094 0.0172  578 GLU C CG  
9037  C CD  . GLU C 277 ? 0.8219 0.9055 0.8203 -0.0628 -0.0119 0.0173  578 GLU C CD  
9038  O OE1 . GLU C 277 ? 0.8496 0.9594 0.8532 -0.0638 -0.0165 0.0157  578 GLU C OE1 
9039  O OE2 . GLU C 277 ? 0.9481 1.0346 0.9516 -0.0547 -0.0094 0.0187  578 GLU C OE2 
9040  N N   . ILE C 278 ? 0.4340 0.4894 0.4215 -0.0430 -0.0224 0.0161  579 ILE C N   
9041  C CA  . ILE C 278 ? 0.5050 0.5830 0.4987 -0.0310 -0.0283 0.0165  579 ILE C CA  
9042  C C   . ILE C 278 ? 0.5542 0.6657 0.5531 -0.0400 -0.0317 0.0149  579 ILE C C   
9043  O O   . ILE C 278 ? 0.3924 0.5015 0.3849 -0.0539 -0.0324 0.0131  579 ILE C O   
9044  C CB  . ILE C 278 ? 0.4523 0.5136 0.4382 -0.0226 -0.0321 0.0177  579 ILE C CB  
9045  C CG1 . ILE C 278 ? 0.4138 0.4458 0.3948 -0.0154 -0.0288 0.0193  579 ILE C CG1 
9046  C CG2 . ILE C 278 ? 0.3313 0.4139 0.3211 -0.0095 -0.0387 0.0188  579 ILE C CG2 
9047  C CD1 . ILE C 278 ? 0.4519 0.4639 0.4226 -0.0133 -0.0307 0.0204  579 ILE C CD1 
9048  N N   . GLY C 279 ? 0.5629 0.7067 0.5729 -0.0323 -0.0337 0.0149  580 GLY C N   
9049  C CA  . GLY C 279 ? 0.5322 0.7161 0.5498 -0.0402 -0.0369 0.0134  580 GLY C CA  
9050  C C   . GLY C 279 ? 0.5455 0.7317 0.5589 -0.0646 -0.0344 0.0115  580 GLY C C   
9051  O O   . GLY C 279 ? 0.5822 0.7893 0.5952 -0.0746 -0.0386 0.0098  580 GLY C O   
9052  N N   . GLY C 280 ? 0.4613 0.6252 0.4699 -0.0746 -0.0278 0.0118  581 GLY C N   
9053  C CA  . GLY C 280 ? 0.5497 0.7070 0.5498 -0.0981 -0.0250 0.0102  581 GLY C CA  
9054  C C   . GLY C 280 ? 0.5387 0.6596 0.5231 -0.1058 -0.0247 0.0085  581 GLY C C   
9055  O O   . GLY C 280 ? 0.5298 0.6351 0.5030 -0.1243 -0.0217 0.0069  581 GLY C O   
9056  N N   . LEU C 281 ? 0.4490 0.5543 0.4303 -0.0923 -0.0274 0.0089  582 LEU C N   
9057  C CA  . LEU C 281 ? 0.5015 0.5732 0.4680 -0.0969 -0.0264 0.0071  582 LEU C CA  
9058  C C   . LEU C 281 ? 0.5196 0.5556 0.4803 -0.0909 -0.0204 0.0086  582 LEU C C   
9059  O O   . LEU C 281 ? 0.6096 0.6453 0.5780 -0.0780 -0.0189 0.0114  582 LEU C O   
9060  C CB  . LEU C 281 ? 0.4495 0.5244 0.4148 -0.0862 -0.0320 0.0072  582 LEU C CB  
9061  C CG  . LEU C 281 ? 0.5223 0.6354 0.4939 -0.0879 -0.0392 0.0065  582 LEU C CG  
9062  C CD1 . LEU C 281 ? 0.5482 0.6583 0.5158 -0.0757 -0.0446 0.0078  582 LEU C CD1 
9063  C CD2 . LEU C 281 ? 0.4430 0.5651 0.4078 -0.1105 -0.0398 0.0025  582 LEU C CD2 
9064  N N   . GLU C 282 ? 0.5328 0.5388 0.4789 -0.0997 -0.0171 0.0064  583 GLU C N   
9065  C CA  . GLU C 282 ? 0.4972 0.4709 0.4364 -0.0955 -0.0111 0.0076  583 GLU C CA  
9066  C C   . GLU C 282 ? 0.5896 0.5385 0.5182 -0.0902 -0.0102 0.0057  583 GLU C C   
9067  O O   . GLU C 282 ? 0.5634 0.4972 0.4783 -0.1001 -0.0095 0.0018  583 GLU C O   
9068  C CB  . GLU C 282 ? 0.5719 0.5303 0.5009 -0.1106 -0.0068 0.0069  583 GLU C CB  
9069  C CG  . GLU C 282 ? 0.6972 0.6806 0.6351 -0.1184 -0.0067 0.0090  583 GLU C CG  
9070  C CD  . GLU C 282 ? 0.8051 0.7667 0.7296 -0.1333 -0.0019 0.0095  583 GLU C CD  
9071  O OE1 . GLU C 282 ? 0.7824 0.7222 0.6901 -0.1463 -0.0012 0.0061  583 GLU C OE1 
9072  O OE2 . GLU C 282 ? 0.9209 0.8845 0.8495 -0.1318 0.0012  0.0132  583 GLU C OE2 
9073  N N   . PHE C 283 ? 0.5650 0.5093 0.4987 -0.0754 -0.0097 0.0081  584 PHE C N   
9074  C CA  . PHE C 283 ? 0.4750 0.3987 0.3999 -0.0698 -0.0078 0.0069  584 PHE C CA  
9075  C C   . PHE C 283 ? 0.5428 0.4426 0.4625 -0.0661 -0.0017 0.0075  584 PHE C C   
9076  O O   . PHE C 283 ? 0.5461 0.4469 0.4736 -0.0565 -0.0002 0.0109  584 PHE C O   
9077  C CB  . PHE C 283 ? 0.5272 0.4607 0.4589 -0.0581 -0.0111 0.0094  584 PHE C CB  
9078  C CG  . PHE C 283 ? 0.5514 0.5081 0.4874 -0.0591 -0.0177 0.0096  584 PHE C CG  
9079  C CD1 . PHE C 283 ? 0.4597 0.4393 0.4075 -0.0553 -0.0209 0.0117  584 PHE C CD1 
9080  C CD2 . PHE C 283 ? 0.5062 0.4632 0.4335 -0.0631 -0.0208 0.0074  584 PHE C CD2 
9081  C CE1 . PHE C 283 ? 0.4955 0.4987 0.4472 -0.0539 -0.0273 0.0121  584 PHE C CE1 
9082  C CE2 . PHE C 283 ? 0.5646 0.5446 0.4954 -0.0627 -0.0275 0.0082  584 PHE C CE2 
9083  C CZ  . PHE C 283 ? 0.5397 0.5433 0.4829 -0.0575 -0.0310 0.0106  584 PHE C CZ  
9084  N N   . SER C 284 ? 0.5304 0.4083 0.4355 -0.0734 0.0017  0.0042  585 SER C N   
9085  C CA  . SER C 284 ? 0.5209 0.3740 0.4180 -0.0689 0.0073  0.0047  585 SER C CA  
9086  C C   . SER C 284 ? 0.5522 0.3964 0.4481 -0.0560 0.0099  0.0046  585 SER C C   
9087  O O   . SER C 284 ? 0.5748 0.4033 0.4665 -0.0488 0.0142  0.0056  585 SER C O   
9088  C CB  . SER C 284 ? 0.6418 0.4705 0.5202 -0.0806 0.0097  0.0008  585 SER C CB  
9089  O OG  . SER C 284 ? 0.8627 0.6902 0.7320 -0.0881 0.0077  -0.0044 585 SER C OG  
9090  N N   . ALA C 285 ? 0.5706 0.4254 0.4691 -0.0531 0.0075  0.0035  586 ALA C N   
9091  C CA  . ALA C 285 ? 0.5616 0.4125 0.4592 -0.0430 0.0102  0.0035  586 ALA C CA  
9092  C C   . ALA C 285 ? 0.4995 0.3702 0.4087 -0.0390 0.0062  0.0068  586 ALA C C   
9093  O O   . ALA C 285 ? 0.5551 0.4346 0.4630 -0.0429 0.0021  0.0061  586 ALA C O   
9094  C CB  . ALA C 285 ? 0.6324 0.4698 0.5150 -0.0451 0.0124  -0.0020 586 ALA C CB  
9095  N N   . CYS C 286 ? 0.4739 0.3500 0.3925 -0.0313 0.0070  0.0106  587 CYS C N   
9096  C CA  . CYS C 286 ? 0.4588 0.3488 0.3861 -0.0279 0.0032  0.0139  587 CYS C CA  
9097  C C   . CYS C 286 ? 0.5198 0.4103 0.4517 -0.0206 0.0058  0.0164  587 CYS C C   
9098  O O   . CYS C 286 ? 0.5852 0.4823 0.5252 -0.0176 0.0043  0.0192  587 CYS C O   
9099  C CB  . CYS C 286 ? 0.5154 0.4169 0.4510 -0.0294 -0.0007 0.0158  587 CYS C CB  
9100  S SG  . CYS C 286 ? 0.5281 0.4267 0.4689 -0.0283 0.0026  0.0173  587 CYS C SG  
9101  N N   . PRO C 287 ? 0.4951 0.3810 0.4220 -0.0177 0.0098  0.0152  588 PRO C N   
9102  C CA  . PRO C 287 ? 0.4206 0.3116 0.3529 -0.0119 0.0122  0.0174  588 PRO C CA  
9103  C C   . PRO C 287 ? 0.5306 0.4303 0.4678 -0.0128 0.0084  0.0206  588 PRO C C   
9104  O O   . PRO C 287 ? 0.5484 0.4487 0.4811 -0.0162 0.0057  0.0210  588 PRO C O   
9105  C CB  . PRO C 287 ? 0.5015 0.3904 0.4269 -0.0093 0.0168  0.0149  588 PRO C CB  
9106  C CG  . PRO C 287 ? 0.4428 0.3264 0.3587 -0.0151 0.0155  0.0118  588 PRO C CG  
9107  C CD  . PRO C 287 ? 0.4545 0.3333 0.3706 -0.0199 0.0120  0.0113  588 PRO C CD  
9108  N N   . PHE C 288 ? 0.4048 0.3092 0.3492 -0.0099 0.0081  0.0229  589 PHE C N   
9109  C CA  . PHE C 288 ? 0.3904 0.2988 0.3370 -0.0109 0.0048  0.0254  589 PHE C CA  
9110  C C   . PHE C 288 ? 0.4417 0.3568 0.3916 -0.0095 0.0073  0.0266  589 PHE C C   
9111  O O   . PHE C 288 ? 0.4655 0.3844 0.4193 -0.0054 0.0105  0.0263  589 PHE C O   
9112  C CB  . PHE C 288 ? 0.3624 0.2713 0.3135 -0.0094 0.0010  0.0262  589 PHE C CB  
9113  C CG  . PHE C 288 ? 0.4259 0.3371 0.3830 -0.0067 0.0030  0.0261  589 PHE C CG  
9114  C CD1 . PHE C 288 ? 0.4986 0.4139 0.4600 -0.0040 0.0037  0.0274  589 PHE C CD1 
9115  C CD2 . PHE C 288 ? 0.4414 0.3503 0.3982 -0.0079 0.0038  0.0249  589 PHE C CD2 
9116  C CE1 . PHE C 288 ? 0.4293 0.3465 0.3947 -0.0015 0.0053  0.0280  589 PHE C CE1 
9117  C CE2 . PHE C 288 ? 0.5638 0.4728 0.5237 -0.0066 0.0057  0.0256  589 PHE C CE2 
9118  C CZ  . PHE C 288 ? 0.4465 0.3598 0.4108 -0.0027 0.0064  0.0275  589 PHE C CZ  
9119  N N   . SER C 289 ? 0.4884 0.4049 0.4357 -0.0134 0.0055  0.0282  590 SER C N   
9120  C CA  . SER C 289 ? 0.3884 0.3145 0.3383 -0.0148 0.0076  0.0292  590 SER C CA  
9121  C C   . SER C 289 ? 0.3998 0.3220 0.3467 -0.0195 0.0037  0.0309  590 SER C C   
9122  O O   . SER C 289 ? 0.3710 0.2815 0.3112 -0.0212 -0.0001 0.0317  590 SER C O   
9123  C CB  . SER C 289 ? 0.4138 0.3482 0.3606 -0.0173 0.0115  0.0288  590 SER C CB  
9124  O OG  . SER C 289 ? 0.5079 0.4368 0.4459 -0.0245 0.0096  0.0302  590 SER C OG  
9125  N N   . GLY C 290 ? 0.4458 0.3767 0.3965 -0.0210 0.0044  0.0313  591 GLY C N   
9126  C CA  . GLY C 290 ? 0.3494 0.2745 0.2943 -0.0274 0.0012  0.0322  591 GLY C CA  
9127  C C   . GLY C 290 ? 0.5238 0.4642 0.4701 -0.0342 0.0034  0.0328  591 GLY C C   
9128  O O   . GLY C 290 ? 0.5537 0.5030 0.4985 -0.0383 0.0063  0.0334  591 GLY C O   
9129  N N   . TRP C 291 ? 0.5284 0.4747 0.4775 -0.0358 0.0023  0.0323  592 TRP C N   
9130  C CA  . TRP C 291 ? 0.5337 0.5013 0.4867 -0.0416 0.0042  0.0327  592 TRP C CA  
9131  C C   . TRP C 291 ? 0.4614 0.4399 0.4227 -0.0358 0.0038  0.0319  592 TRP C C   
9132  O O   . TRP C 291 ? 0.5399 0.5071 0.5017 -0.0297 0.0018  0.0312  592 TRP C O   
9133  C CB  . TRP C 291 ? 0.4985 0.4609 0.4404 -0.0565 0.0022  0.0334  592 TRP C CB  
9134  C CG  . TRP C 291 ? 0.5746 0.5136 0.5067 -0.0587 -0.0024 0.0325  592 TRP C CG  
9135  C CD1 . TRP C 291 ? 0.5416 0.4814 0.4747 -0.0586 -0.0045 0.0307  592 TRP C CD1 
9136  C CD2 . TRP C 291 ? 0.5785 0.4894 0.4970 -0.0599 -0.0056 0.0332  592 TRP C CD2 
9137  N NE1 . TRP C 291 ? 0.6468 0.5599 0.5676 -0.0591 -0.0084 0.0295  592 TRP C NE1 
9138  C CE2 . TRP C 291 ? 0.6001 0.4950 0.5117 -0.0592 -0.0093 0.0312  592 TRP C CE2 
9139  C CE3 . TRP C 291 ? 0.5344 0.4324 0.4450 -0.0604 -0.0059 0.0353  592 TRP C CE3 
9140  C CZ2 . TRP C 291 ? 0.6144 0.4802 0.5114 -0.0575 -0.0131 0.0312  592 TRP C CZ2 
9141  C CZ3 . TRP C 291 ? 0.5942 0.4643 0.4906 -0.0593 -0.0102 0.0360  592 TRP C CZ3 
9142  C CH2 . TRP C 291 ? 0.7473 0.6011 0.6369 -0.0571 -0.0137 0.0339  592 TRP C CH2 
9143  N N   . TYR C 292 ? 0.4245 0.4278 0.3924 -0.0371 0.0057  0.0323  593 TYR C N   
9144  C CA  . TYR C 292 ? 0.4366 0.4542 0.4127 -0.0297 0.0055  0.0325  593 TYR C CA  
9145  C C   . TYR C 292 ? 0.4554 0.4710 0.4275 -0.0372 0.0015  0.0314  593 TYR C C   
9146  O O   . TYR C 292 ? 0.5453 0.5580 0.5095 -0.0503 -0.0004 0.0305  593 TYR C O   
9147  C CB  . TYR C 292 ? 0.3844 0.4328 0.3691 -0.0267 0.0086  0.0335  593 TYR C CB  
9148  C CG  . TYR C 292 ? 0.4547 0.5061 0.4445 -0.0122 0.0124  0.0341  593 TYR C CG  
9149  C CD1 . TYR C 292 ? 0.4451 0.4853 0.4363 -0.0010 0.0122  0.0349  593 TYR C CD1 
9150  C CD2 . TYR C 292 ? 0.4416 0.5063 0.4331 -0.0100 0.0165  0.0338  593 TYR C CD2 
9151  C CE1 . TYR C 292 ? 0.3878 0.4257 0.3802 0.0115  0.0156  0.0354  593 TYR C CE1 
9152  C CE2 . TYR C 292 ? 0.4462 0.5100 0.4396 0.0040  0.0201  0.0336  593 TYR C CE2 
9153  C CZ  . TYR C 292 ? 0.4901 0.5384 0.4831 0.0146  0.0195  0.0345  593 TYR C CZ  
9154  O OH  . TYR C 292 ? 0.6218 0.6639 0.6133 0.0279  0.0229  0.0343  593 TYR C OH  
9155  N N   . MET C 293 ? 0.5201 0.5361 0.4960 -0.0293 0.0004  0.0313  594 MET C N   
9156  C CA  . MET C 293 ? 0.4866 0.5117 0.4614 -0.0342 -0.0024 0.0302  594 MET C CA  
9157  C C   . MET C 293 ? 0.4381 0.4954 0.4227 -0.0305 -0.0011 0.0322  594 MET C C   
9158  O O   . MET C 293 ? 0.4591 0.5232 0.4505 -0.0177 0.0015  0.0344  594 MET C O   
9159  C CB  . MET C 293 ? 0.4846 0.4957 0.4577 -0.0273 -0.0041 0.0293  594 MET C CB  
9160  C CG  . MET C 293 ? 0.5137 0.5289 0.4821 -0.0336 -0.0074 0.0271  594 MET C CG  
9161  S SD  . MET C 293 ? 0.5487 0.5427 0.5110 -0.0277 -0.0091 0.0245  594 MET C SD  
9162  C CE  . MET C 293 ? 0.3081 0.3145 0.2807 -0.0140 -0.0066 0.0285  594 MET C CE  
9163  N N   . GLY C 294 ? 0.4875 0.5643 0.4715 -0.0417 -0.0030 0.0313  595 GLY C N   
9164  C CA  . GLY C 294 ? 0.5068 0.6202 0.5008 -0.0383 -0.0020 0.0332  595 GLY C CA  
9165  C C   . GLY C 294 ? 0.4467 0.5691 0.4477 -0.0217 -0.0018 0.0358  595 GLY C C   
9166  O O   . GLY C 294 ? 0.4205 0.5660 0.4296 -0.0113 0.0003  0.0383  595 GLY C O   
9167  N N   . THR C 295 ? 0.3742 0.4782 0.3709 -0.0182 -0.0038 0.0355  596 THR C N   
9168  C CA  . THR C 295 ? 0.3823 0.4939 0.3830 -0.0043 -0.0040 0.0388  596 THR C CA  
9169  C C   . THR C 295 ? 0.4356 0.5370 0.4387 0.0104  -0.0001 0.0417  596 THR C C   
9170  O O   . THR C 295 ? 0.4722 0.5847 0.4784 0.0232  0.0005  0.0453  596 THR C O   
9171  C CB  . THR C 295 ? 0.4200 0.5150 0.4143 -0.0053 -0.0065 0.0377  596 THR C CB  
9172  O OG1 . THR C 295 ? 0.4230 0.4882 0.4116 -0.0077 -0.0055 0.0354  596 THR C OG1 
9173  C CG2 . THR C 295 ? 0.3824 0.4898 0.3727 -0.0179 -0.0106 0.0347  596 THR C CG2 
9174  N N   . GLU C 296 ? 0.4051 0.4841 0.4052 0.0089  0.0022  0.0402  597 GLU C N   
9175  C CA  . GLU C 296 ? 0.4977 0.5643 0.4977 0.0209  0.0058  0.0421  597 GLU C CA  
9176  C C   . GLU C 296 ? 0.4818 0.5705 0.4870 0.0305  0.0084  0.0438  597 GLU C C   
9177  O O   . GLU C 296 ? 0.5065 0.5914 0.5107 0.0446  0.0102  0.0465  597 GLU C O   
9178  C CB  . GLU C 296 ? 0.5492 0.5931 0.5451 0.0158  0.0073  0.0396  597 GLU C CB  
9179  C CG  . GLU C 296 ? 0.4772 0.5013 0.4681 0.0086  0.0049  0.0377  597 GLU C CG  
9180  C CD  . GLU C 296 ? 0.4940 0.4993 0.4810 0.0045  0.0058  0.0357  597 GLU C CD  
9181  O OE1 . GLU C 296 ? 0.4609 0.4546 0.4470 0.0106  0.0080  0.0364  597 GLU C OE1 
9182  O OE2 . GLU C 296 ? 0.3854 0.3869 0.3688 -0.0049 0.0040  0.0338  597 GLU C OE2 
9183  N N   . ILE C 297 ? 0.4269 0.5389 0.4365 0.0230  0.0085  0.0421  598 ILE C N   
9184  C CA  . ILE C 297 ? 0.4087 0.5491 0.4247 0.0323  0.0111  0.0432  598 ILE C CA  
9185  C C   . ILE C 297 ? 0.4755 0.6452 0.4970 0.0383  0.0083  0.0460  598 ILE C C   
9186  O O   . ILE C 297 ? 0.5275 0.7080 0.5511 0.0554  0.0096  0.0489  598 ILE C O   
9187  C CB  . ILE C 297 ? 0.4303 0.5883 0.4489 0.0201  0.0127  0.0407  598 ILE C CB  
9188  C CG1 . ILE C 297 ? 0.5014 0.6303 0.5130 0.0125  0.0145  0.0384  598 ILE C CG1 
9189  C CG2 . ILE C 297 ? 0.2993 0.4896 0.3252 0.0315  0.0162  0.0413  598 ILE C CG2 
9190  C CD1 . ILE C 297 ? 0.4772 0.6167 0.4876 -0.0044 0.0147  0.0366  598 ILE C CD1 
9191  N N   . GLY C 298 ? 0.4716 0.6552 0.4943 0.0241  0.0043  0.0449  599 GLY C N   
9192  C CA  . GLY C 298 ? 0.5365 0.7558 0.5652 0.0266  0.0012  0.0468  599 GLY C CA  
9193  C C   . GLY C 298 ? 0.4857 0.6981 0.5117 0.0390  -0.0013 0.0506  599 GLY C C   
9194  O O   . GLY C 298 ? 0.4429 0.6821 0.4735 0.0510  -0.0027 0.0541  599 GLY C O   
9195  N N   . VAL C 299 ? 0.4018 0.5801 0.4199 0.0366  -0.0019 0.0504  600 VAL C N   
9196  C CA  . VAL C 299 ? 0.3959 0.5654 0.4098 0.0472  -0.0036 0.0545  600 VAL C CA  
9197  C C   . VAL C 299 ? 0.5108 0.6581 0.5204 0.0639  0.0000  0.0581  600 VAL C C   
9198  O O   . VAL C 299 ? 0.4959 0.6537 0.5052 0.0798  0.0000  0.0627  600 VAL C O   
9199  C CB  . VAL C 299 ? 0.3501 0.4977 0.3572 0.0363  -0.0058 0.0524  600 VAL C CB  
9200  C CG1 . VAL C 299 ? 0.4529 0.5945 0.4550 0.0465  -0.0071 0.0571  600 VAL C CG1 
9201  C CG2 . VAL C 299 ? 0.3468 0.5110 0.3543 0.0196  -0.0096 0.0482  600 VAL C CG2 
9202  N N   . ARG C 300 ? 0.5541 0.6698 0.5589 0.0603  0.0029  0.0559  601 ARG C N   
9203  C CA  . ARG C 300 ? 0.5120 0.6003 0.5093 0.0722  0.0060  0.0588  601 ARG C CA  
9204  C C   . ARG C 300 ? 0.6189 0.7114 0.6169 0.0850  0.0096  0.0590  601 ARG C C   
9205  O O   . ARG C 300 ? 0.6020 0.6882 0.5942 0.1013  0.0107  0.0632  601 ARG C O   
9206  C CB  . ARG C 300 ? 0.3942 0.4514 0.3864 0.0627  0.0075  0.0560  601 ARG C CB  
9207  C CG  . ARG C 300 ? 0.3858 0.4376 0.3766 0.0520  0.0046  0.0550  601 ARG C CG  
9208  C CD  . ARG C 300 ? 0.4929 0.5450 0.4788 0.0585  0.0030  0.0600  601 ARG C CD  
9209  N NE  . ARG C 300 ? 0.6075 0.6384 0.5853 0.0693  0.0057  0.0645  601 ARG C NE  
9210  C CZ  . ARG C 300 ? 0.5515 0.5555 0.5227 0.0657  0.0079  0.0643  601 ARG C CZ  
9211  N NH1 . ARG C 300 ? 0.5295 0.5274 0.5030 0.0537  0.0077  0.0600  601 ARG C NH1 
9212  N NH2 . ARG C 300 ? 0.5229 0.5063 0.4844 0.0741  0.0103  0.0685  601 ARG C NH2 
9213  N N   . ASP C 301 ? 0.5508 0.6517 0.5538 0.0785  0.0117  0.0546  602 ASP C N   
9214  C CA  . ASP C 301 ? 0.5795 0.6843 0.5823 0.0906  0.0159  0.0538  602 ASP C CA  
9215  C C   . ASP C 301 ? 0.5855 0.7243 0.5939 0.1056  0.0154  0.0567  602 ASP C C   
9216  O O   . ASP C 301 ? 0.5326 0.6660 0.5358 0.1244  0.0180  0.0586  602 ASP C O   
9217  C CB  . ASP C 301 ? 0.6243 0.7353 0.6312 0.0789  0.0181  0.0488  602 ASP C CB  
9218  C CG  . ASP C 301 ? 0.6795 0.7559 0.6795 0.0692  0.0192  0.0462  602 ASP C CG  
9219  O OD1 . ASP C 301 ? 0.6853 0.7332 0.6769 0.0754  0.0202  0.0475  602 ASP C OD1 
9220  O OD2 . ASP C 301 ? 0.6492 0.7275 0.6513 0.0550  0.0187  0.0432  602 ASP C OD2 
9221  N N   . TYR C 302 ? 0.5826 0.7561 0.6002 0.0980  0.0118  0.0570  603 TYR C N   
9222  C CA  . TYR C 302 ? 0.4651 0.6790 0.4901 0.1109  0.0109  0.0593  603 TYR C CA  
9223  C C   . TYR C 302 ? 0.5348 0.7516 0.5562 0.1244  0.0071  0.0654  603 TYR C C   
9224  O O   . TYR C 302 ? 0.5290 0.7651 0.5514 0.1443  0.0074  0.0686  603 TYR C O   
9225  C CB  . TYR C 302 ? 0.5611 0.8153 0.5974 0.0942  0.0087  0.0566  603 TYR C CB  
9226  C CG  . TYR C 302 ? 0.6306 0.8990 0.6720 0.0878  0.0129  0.0523  603 TYR C CG  
9227  C CD1 . TYR C 302 ? 0.6022 0.8577 0.6400 0.1018  0.0183  0.0511  603 TYR C CD1 
9228  C CD2 . TYR C 302 ? 0.6786 0.9723 0.7262 0.0669  0.0117  0.0494  603 TYR C CD2 
9229  C CE1 . TYR C 302 ? 0.6042 0.8744 0.6458 0.0957  0.0225  0.0473  603 TYR C CE1 
9230  C CE2 . TYR C 302 ? 0.5552 0.8628 0.6062 0.0598  0.0157  0.0462  603 TYR C CE2 
9231  C CZ  . TYR C 302 ? 0.6153 0.9124 0.6639 0.0745  0.0212  0.0452  603 TYR C CZ  
9232  O OH  . TYR C 302 ? 0.6892 1.0012 0.7403 0.0670  0.0256  0.0420  603 TYR C OH  
9233  N N   . CYS C 303 ? 0.4873 0.6859 0.5034 0.1152  0.0037  0.0672  604 CYS C N   
9234  C CA  . CYS C 303 ? 0.5790 0.7874 0.5922 0.1246  -0.0006 0.0730  604 CYS C CA  
9235  C C   . CYS C 303 ? 0.5159 0.6840 0.5146 0.1335  -0.0002 0.0780  604 CYS C C   
9236  O O   . CYS C 303 ? 0.5576 0.7322 0.5515 0.1452  -0.0033 0.0841  604 CYS C O   
9237  C CB  . CYS C 303 ? 0.5920 0.8221 0.6104 0.1068  -0.0056 0.0714  604 CYS C CB  
9238  S SG  . CYS C 303 ? 0.5774 0.8614 0.6107 0.0949  -0.0074 0.0671  604 CYS C SG  
9239  N N   . ASP C 304 ? 0.4485 0.5767 0.4394 0.1275  0.0032  0.0760  605 ASP C N   
9240  C CA  . ASP C 304 ? 0.5062 0.5965 0.4818 0.1360  0.0044  0.0810  605 ASP C CA  
9241  C C   . ASP C 304 ? 0.6391 0.7288 0.6072 0.1604  0.0052  0.0864  605 ASP C C   
9242  O O   . ASP C 304 ? 0.8177 0.9258 0.7913 0.1712  0.0071  0.0842  605 ASP C O   
9243  C CB  . ASP C 304 ? 0.4610 0.5135 0.4299 0.1276  0.0086  0.0774  605 ASP C CB  
9244  C CG  . ASP C 304 ? 0.6501 0.6909 0.6198 0.1084  0.0075  0.0749  605 ASP C CG  
9245  O OD1 . ASP C 304 ? 0.6551 0.7169 0.6312 0.0997  0.0039  0.0743  605 ASP C OD1 
9246  O OD2 . ASP C 304 ? 0.7196 0.7308 0.6829 0.1022  0.0102  0.0732  605 ASP C OD2 
9247  N N   . ASN C 305 ? 0.6860 0.7538 0.6398 0.1699  0.0039  0.0936  606 ASN C N   
9248  C CA  . ASN C 305 ? 0.7158 0.7802 0.6595 0.1952  0.0039  0.0996  606 ASN C CA  
9249  C C   . ASN C 305 ? 0.7443 0.7765 0.6773 0.2055  0.0093  0.0971  606 ASN C C   
9250  O O   . ASN C 305 ? 0.7907 0.8332 0.7223 0.2263  0.0106  0.0976  606 ASN C O   
9251  C CB  . ASN C 305 ? 0.7537 0.7975 0.6812 0.2018  0.0011  0.1087  606 ASN C CB  
9252  C CG  . ASN C 305 ? 0.8135 0.8977 0.7491 0.2044  -0.0048 0.1128  606 ASN C CG  
9253  O OD1 . ASN C 305 ? 0.8764 0.9621 0.8115 0.1906  -0.0075 0.1143  606 ASN C OD1 
9254  N ND2 . ASN C 305 ? 0.8045 0.9241 0.7473 0.2220  -0.0068 0.1143  606 ASN C ND2 
9255  N N   . SER C 306 ? 0.7267 0.7210 0.6516 0.1918  0.0125  0.0940  607 SER C N   
9256  C CA  . SER C 306 ? 0.8387 0.7992 0.7511 0.1989  0.0175  0.0909  607 SER C CA  
9257  C C   . SER C 306 ? 0.8172 0.7931 0.7431 0.1895  0.0205  0.0819  607 SER C C   
9258  O O   . SER C 306 ? 0.8777 0.8244 0.7943 0.1883  0.0246  0.0776  607 SER C O   
9259  C CB  . SER C 306 ? 0.8051 0.7152 0.6982 0.1895  0.0191  0.0933  607 SER C CB  
9260  O OG  . SER C 306 ? 0.8562 0.7706 0.7566 0.1680  0.0172  0.0930  607 SER C OG  
9261  N N   . ARG C 307 ? 0.7011 0.7212 0.6468 0.1821  0.0184  0.0790  608 ARG C N   
9262  C CA  . ARG C 307 ? 0.6793 0.7194 0.6374 0.1744  0.0211  0.0716  608 ARG C CA  
9263  C C   . ARG C 307 ? 0.6563 0.7400 0.6250 0.1899  0.0211  0.0715  608 ARG C C   
9264  O O   . ARG C 307 ? 0.7499 0.8300 0.7098 0.2131  0.0219  0.0749  608 ARG C O   
9265  C CB  . ARG C 307 ? 0.5881 0.6374 0.5573 0.1494  0.0190  0.0682  608 ARG C CB  
9266  C CG  . ARG C 307 ? 0.5752 0.5851 0.5347 0.1365  0.0197  0.0676  608 ARG C CG  
9267  C CD  . ARG C 307 ? 0.6910 0.6710 0.6408 0.1379  0.0244  0.0634  608 ARG C CD  
9268  N NE  . ARG C 307 ? 0.6144 0.6131 0.5740 0.1323  0.0265  0.0572  608 ARG C NE  
9269  C CZ  . ARG C 307 ? 0.6604 0.6685 0.6293 0.1140  0.0253  0.0536  608 ARG C CZ  
9270  N NH1 . ARG C 307 ? 0.5514 0.5529 0.5218 0.1008  0.0221  0.0549  608 ARG C NH1 
9271  N NH2 . ARG C 307 ? 0.5559 0.5796 0.5312 0.1095  0.0274  0.0489  608 ARG C NH2 
9272  N N   . TYR C 308 ? 0.5736 0.6985 0.5596 0.1785  0.0202  0.0678  609 TYR C N   
9273  C CA  . TYR C 308 ? 0.4980 0.6671 0.4942 0.1927  0.0211  0.0671  609 TYR C CA  
9274  C C   . TYR C 308 ? 0.5515 0.7519 0.5521 0.2050  0.0162  0.0732  609 TYR C C   
9275  O O   . TYR C 308 ? 0.5965 0.8251 0.6002 0.2259  0.0169  0.0746  609 TYR C O   
9276  C CB  . TYR C 308 ? 0.5072 0.7104 0.5186 0.1750  0.0224  0.0613  609 TYR C CB  
9277  C CG  . TYR C 308 ? 0.7265 0.9138 0.7338 0.1754  0.0285  0.0555  609 TYR C CG  
9278  C CD1 . TYR C 308 ? 0.6882 0.8374 0.6883 0.1597  0.0299  0.0524  609 TYR C CD1 
9279  C CD2 . TYR C 308 ? 0.7751 0.9863 0.7849 0.1928  0.0328  0.0532  609 TYR C CD2 
9280  C CE1 . TYR C 308 ? 0.6732 0.8081 0.6683 0.1599  0.0351  0.0472  609 TYR C CE1 
9281  C CE2 . TYR C 308 ? 0.7868 0.9832 0.7914 0.1933  0.0386  0.0475  609 TYR C CE2 
9282  C CZ  . TYR C 308 ? 0.7519 0.9095 0.7488 0.1764  0.0395  0.0447  609 TYR C CZ  
9283  O OH  . TYR C 308 ? 0.7277 0.8714 0.7183 0.1767  0.0449  0.0390  609 TYR C OH  
9284  N N   . ASN C 309 ? 0.4530 0.6509 0.4535 0.1933  0.0112  0.0769  610 ASN C N   
9285  C CA  . ASN C 309 ? 0.5288 0.7484 0.5293 0.2056  0.0060  0.0837  610 ASN C CA  
9286  C C   . ASN C 309 ? 0.5375 0.8197 0.5547 0.2106  0.0037  0.0831  610 ASN C C   
9287  O O   . ASN C 309 ? 0.5718 0.8768 0.5888 0.2339  0.0021  0.0877  610 ASN C O   
9288  C CB  . ASN C 309 ? 0.5143 0.7012 0.4966 0.2314  0.0068  0.0900  610 ASN C CB  
9289  C CG  . ASN C 309 ? 0.5967 0.7905 0.5735 0.2405  0.0010  0.0985  610 ASN C CG  
9290  O OD1 . ASN C 309 ? 0.6239 0.8190 0.6025 0.2235  -0.0027 0.0998  610 ASN C OD1 
9291  N ND2 . ASN C 309 ? 0.5658 0.7632 0.5342 0.2685  0.0002  0.1042  610 ASN C ND2 
9292  N N   . ILE C 310 ? 0.5508 0.8616 0.5818 0.1882  0.0034  0.0776  611 ILE C N   
9293  C CA  . ILE C 310 ? 0.6129 0.9848 0.6599 0.1889  0.0023  0.0761  611 ILE C CA  
9294  C C   . ILE C 310 ? 0.6153 1.0235 0.6693 0.1805  -0.0049 0.0790  611 ILE C C   
9295  O O   . ILE C 310 ? 0.5670 1.0304 0.6347 0.1775  -0.0069 0.0779  611 ILE C O   
9296  C CB  . ILE C 310 ? 0.6341 1.0193 0.6904 0.1682  0.0061  0.0688  611 ILE C CB  
9297  C CG1 . ILE C 310 ? 0.5995 0.9789 0.6574 0.1376  0.0027  0.0661  611 ILE C CG1 
9298  C CG2 . ILE C 310 ? 0.6632 1.0066 0.7104 0.1730  0.0127  0.0655  611 ILE C CG2 
9299  C CD1 . ILE C 310 ? 0.5188 0.9116 0.5836 0.1161  0.0056  0.0601  611 ILE C CD1 
9300  N N   . LEU C 311 ? 0.5929 0.9727 0.6371 0.1760  -0.0088 0.0827  612 LEU C N   
9301  C CA  . LEU C 311 ? 0.5996 1.0100 0.6483 0.1653  -0.0156 0.0845  612 LEU C CA  
9302  C C   . LEU C 311 ? 0.5505 1.0127 0.6066 0.1850  -0.0196 0.0893  612 LEU C C   
9303  O O   . LEU C 311 ? 0.5737 1.0871 0.6421 0.1736  -0.0235 0.0875  612 LEU C O   
9304  C CB  . LEU C 311 ? 0.5416 0.9117 0.5766 0.1614  -0.0184 0.0882  612 LEU C CB  
9305  C CG  . LEU C 311 ? 0.4380 0.7759 0.4694 0.1355  -0.0172 0.0827  612 LEU C CG  
9306  C CD1 . LEU C 311 ? 0.3502 0.6507 0.3681 0.1347  -0.0189 0.0864  612 LEU C CD1 
9307  C CD2 . LEU C 311 ? 0.3613 0.7329 0.4022 0.1118  -0.0205 0.0771  612 LEU C CD2 
9308  N N   . GLU C 312 ? 0.5900 1.0400 0.6378 0.2149  -0.0188 0.0955  613 GLU C N   
9309  C CA  . GLU C 312 ? 0.6686 1.1674 0.7223 0.2376  -0.0230 0.1009  613 GLU C CA  
9310  C C   . GLU C 312 ? 0.6890 1.2492 0.7620 0.2358  -0.0216 0.0960  613 GLU C C   
9311  O O   . GLU C 312 ? 0.6370 1.2552 0.7219 0.2332  -0.0269 0.0971  613 GLU C O   
9312  C CB  . GLU C 312 ? 0.7803 1.2488 0.8192 0.2719  -0.0211 0.1076  613 GLU C CB  
9313  C CG  . GLU C 312 ? 0.9655 1.3988 0.9869 0.2791  -0.0254 0.1158  613 GLU C CG  
9314  C CD  . GLU C 312 ? 1.1653 1.5696 1.1691 0.3116  -0.0237 0.1223  613 GLU C CD  
9315  O OE1 . GLU C 312 ? 1.2848 1.6299 1.2706 0.3172  -0.0208 0.1253  613 GLU C OE1 
9316  O OE2 . GLU C 312 ? 1.2106 1.6445 1.2154 0.3265  -0.0237 0.1224  613 GLU C OE2 
9317  N N   . GLU C 313 ? 0.7548 1.3049 0.8305 0.2358  -0.0143 0.0906  614 GLU C N   
9318  C CA  . GLU C 313 ? 0.7359 1.3442 0.8287 0.2365  -0.0118 0.0864  614 GLU C CA  
9319  C C   . GLU C 313 ? 0.6993 1.3453 0.8051 0.2016  -0.0143 0.0813  614 GLU C C   
9320  O O   . GLU C 313 ? 0.7201 1.4314 0.8411 0.1992  -0.0162 0.0803  614 GLU C O   
9321  C CB  . GLU C 313 ? 0.7609 1.3437 0.8506 0.2444  -0.0031 0.0817  614 GLU C CB  
9322  C CG  . GLU C 313 ? 0.8504 1.4871 0.9567 0.2375  0.0011  0.0760  614 GLU C CG  
9323  C CD  . GLU C 313 ? 0.9925 1.6137 1.0944 0.2587  0.0093  0.0730  614 GLU C CD  
9324  O OE1 . GLU C 313 ? 1.0323 1.6959 1.1416 0.2631  0.0128  0.0694  614 GLU C OE1 
9325  O OE2 . GLU C 313 ? 1.0481 1.6053 1.1331 0.2665  0.0123  0.0731  614 GLU C OE2 
9326  N N   . VAL C 314 ? 0.6637 1.2692 0.7627 0.1744  -0.0143 0.0780  615 VAL C N   
9327  C CA  . VAL C 314 ? 0.6214 1.2535 0.7278 0.1409  -0.0174 0.0735  615 VAL C CA  
9328  C C   . VAL C 314 ? 0.5798 1.2481 0.6891 0.1379  -0.0259 0.0769  615 VAL C C   
9329  O O   . VAL C 314 ? 0.5206 1.2410 0.6407 0.1200  -0.0292 0.0743  615 VAL C O   
9330  C CB  . VAL C 314 ? 0.5566 1.1316 0.6522 0.1168  -0.0156 0.0694  615 VAL C CB  
9331  C CG1 . VAL C 314 ? 0.4899 1.0834 0.5883 0.0833  -0.0194 0.0649  615 VAL C CG1 
9332  C CG2 . VAL C 314 ? 0.5190 1.0669 0.6130 0.1178  -0.0077 0.0657  615 VAL C CG2 
9333  N N   . ALA C 315 ? 0.6171 1.2598 0.7160 0.1547  -0.0295 0.0829  616 ALA C N   
9334  C CA  . ALA C 315 ? 0.5963 1.2717 0.6963 0.1526  -0.0378 0.0865  616 ALA C CA  
9335  C C   . ALA C 315 ? 0.5233 1.2669 0.6359 0.1677  -0.0402 0.0888  616 ALA C C   
9336  O O   . ALA C 315 ? 0.4862 1.2705 0.6035 0.1489  -0.0438 0.0860  616 ALA C O   
9337  C CB  . ALA C 315 ? 0.6140 1.2447 0.6979 0.1684  -0.0404 0.0932  616 ALA C CB  
9338  N N   . LYS C 316 ? 0.5954 1.3331 0.7046 0.1967  -0.0348 0.0912  617 LYS C N   
9339  C CA  . LYS C 316 ? 0.6410 1.4246 0.7537 0.2081  -0.0331 0.0906  617 LYS C CA  
9340  C C   . LYS C 316 ? 0.5950 1.4291 0.7210 0.1807  -0.0321 0.0838  617 LYS C C   
9341  O O   . LYS C 316 ? 0.5460 1.4234 0.6750 0.1693  -0.0356 0.0830  617 LYS C O   
9342  C CB  . LYS C 316 ? 0.6741 1.4401 0.7810 0.2393  -0.0264 0.0917  617 LYS C CB  
9343  C CG  . LYS C 316 ? 0.7576 1.4761 0.8471 0.2684  -0.0269 0.0987  617 LYS C CG  
9344  C CD  . LYS C 316 ? 0.8470 1.5320 0.9282 0.2925  -0.0196 0.0979  617 LYS C CD  
9345  C CE  . LYS C 316 ? 0.9555 1.6819 1.0403 0.3074  -0.0157 0.0949  617 LYS C CE  
9346  N NZ  . LYS C 316 ? 0.9861 1.7042 1.0562 0.3382  -0.0164 0.1002  617 LYS C NZ  
9347  N N   . LYS C 317 ? 0.5172 1.3445 0.6499 0.1683  -0.0271 0.0790  618 LYS C N   
9348  C CA  . LYS C 317 ? 0.5638 1.4333 0.7061 0.1406  -0.0253 0.0729  618 LYS C CA  
9349  C C   . LYS C 317 ? 0.5979 1.4843 0.7409 0.1073  -0.0318 0.0707  618 LYS C C   
9350  O O   . LYS C 317 ? 0.5932 1.5225 0.7397 0.0873  -0.0320 0.0672  618 LYS C O   
9351  C CB  . LYS C 317 ? 0.5595 1.4094 0.7066 0.1309  -0.0191 0.0687  618 LYS C CB  
9352  C CG  . LYS C 317 ? 0.6411 1.4910 0.7882 0.1562  -0.0113 0.0680  618 LYS C CG  
9353  C CD  . LYS C 317 ? 0.7166 1.6219 0.8692 0.1490  -0.0087 0.0645  618 LYS C CD  
9354  C CE  . LYS C 317 ? 0.8048 1.7107 0.9561 0.1747  -0.0014 0.0631  618 LYS C CE  
9355  N NZ  . LYS C 317 ? 0.8444 1.7276 0.9859 0.2127  -0.0018 0.0678  618 LYS C NZ  
9356  N N   . MET C 318 ? 0.5808 1.4329 0.7183 0.1005  -0.0372 0.0725  619 MET C N   
9357  C CA  . MET C 318 ? 0.5301 1.3919 0.6650 0.0688  -0.0435 0.0694  619 MET C CA  
9358  C C   . MET C 318 ? 0.5341 1.4234 0.6646 0.0737  -0.0487 0.0722  619 MET C C   
9359  O O   . MET C 318 ? 0.4568 1.3587 0.5839 0.0470  -0.0534 0.0688  619 MET C O   
9360  C CB  . MET C 318 ? 0.5161 1.3243 0.6425 0.0576  -0.0465 0.0689  619 MET C CB  
9361  C CG  . MET C 318 ? 0.4645 1.2288 0.5859 0.0404  -0.0394 0.0634  619 MET C CG  
9362  S SD  . MET C 318 ? 0.5262 1.2069 0.6273 0.0277  -0.0392 0.0612  619 MET C SD  
9363  C CE  . MET C 318 ? 0.5942 1.2941 0.6892 -0.0009 -0.0478 0.0576  619 MET C CE  
9364  N N   . ASN C 319 ? 0.5933 1.4894 0.7222 0.1064  -0.0478 0.0779  620 ASN C N   
9365  C CA  . ASN C 319 ? 0.6323 1.5552 0.7571 0.1145  -0.0523 0.0814  620 ASN C CA  
9366  C C   . ASN C 319 ? 0.6189 1.5141 0.7344 0.1066  -0.0592 0.0834  620 ASN C C   
9367  O O   . ASN C 319 ? 0.6035 1.5198 0.7168 0.0848  -0.0639 0.0808  620 ASN C O   
9368  C CB  . ASN C 319 ? 0.6528 1.6337 0.7831 0.0938  -0.0525 0.0770  620 ASN C CB  
9369  C CG  . ASN C 319 ? 0.7745 1.7883 0.9118 0.1063  -0.0461 0.0760  620 ASN C CG  
9370  O OD1 . ASN C 319 ? 0.9193 1.9478 1.0559 0.1362  -0.0447 0.0802  620 ASN C OD1 
9371  N ND2 . ASN C 319 ? 0.7002 1.7246 0.8427 0.0834  -0.0423 0.0703  620 ASN C ND2 
9372  N N   . LEU C 320 ? 0.5941 1.4405 0.7024 0.1247  -0.0595 0.0882  621 LEU C N   
9373  C CA  . LEU C 320 ? 0.5339 1.3485 0.6311 0.1197  -0.0654 0.0908  621 LEU C CA  
9374  C C   . LEU C 320 ? 0.6556 1.4584 0.7431 0.1496  -0.0669 0.0993  621 LEU C C   
9375  O O   . LEU C 320 ? 0.6590 1.4552 0.7456 0.1775  -0.0625 0.1036  621 LEU C O   
9376  C CB  . LEU C 320 ? 0.4453 1.2102 0.5386 0.1144  -0.0649 0.0902  621 LEU C CB  
9377  C CG  . LEU C 320 ? 0.4414 1.1999 0.5399 0.0857  -0.0614 0.0815  621 LEU C CG  
9378  C CD1 . LEU C 320 ? 0.3807 1.0647 0.4669 0.0839  -0.0550 0.0798  621 LEU C CD1 
9379  C CD2 . LEU C 320 ? 0.3302 1.1115 0.4273 0.0514  -0.0669 0.0751  621 LEU C CD2 
9380  N N   . ASP C 321 ? 0.7356 1.5338 0.8138 0.1431  -0.0729 0.1015  622 ASP C N   
9381  C CA  . ASP C 321 ? 0.7997 1.5819 0.8663 0.1687  -0.0747 0.1101  622 ASP C CA  
9382  C C   . ASP C 321 ? 0.6847 1.4071 0.7402 0.1851  -0.0723 0.1155  622 ASP C C   
9383  O O   . ASP C 321 ? 0.7645 1.4540 0.8109 0.1738  -0.0750 0.1160  622 ASP C O   
9384  C CB  . ASP C 321 ? 0.9046 1.6970 0.9635 0.1551  -0.0815 0.1106  622 ASP C CB  
9385  C CG  . ASP C 321 ? 1.0404 1.8137 1.0857 0.1801  -0.0834 0.1201  622 ASP C CG  
9386  O OD1 . ASP C 321 ? 1.0365 1.8088 1.0808 0.2077  -0.0802 0.1255  622 ASP C OD1 
9387  O OD2 . ASP C 321 ? 1.1084 1.8654 1.1423 0.1721  -0.0881 0.1221  622 ASP C OD2 
9388  N N   . MET C 322 ? 0.6323 1.3390 0.6865 0.2112  -0.0669 0.1192  623 MET C N   
9389  C CA  . MET C 322 ? 0.6266 1.2738 0.6681 0.2267  -0.0638 0.1243  623 MET C CA  
9390  C C   . MET C 322 ? 0.7199 1.3379 0.7431 0.2483  -0.0653 0.1335  623 MET C C   
9391  O O   . MET C 322 ? 0.7985 1.3665 0.8085 0.2647  -0.0617 0.1384  623 MET C O   
9392  C CB  . MET C 322 ? 0.4892 1.1271 0.5360 0.2412  -0.0566 0.1222  623 MET C CB  
9393  C CG  . MET C 322 ? 0.6107 1.2749 0.6746 0.2192  -0.0546 0.1136  623 MET C CG  
9394  S SD  . MET C 322 ? 0.7338 1.3979 0.8046 0.2363  -0.0458 0.1103  623 MET C SD  
9395  C CE  . MET C 322 ? 0.7200 1.3074 0.7735 0.2542  -0.0420 0.1155  623 MET C CE  
9396  N N   . ARG C 323 ? 0.7514 1.3979 0.7724 0.2474  -0.0704 0.1360  624 ARG C N   
9397  C CA  . ARG C 323 ? 0.7772 1.3980 0.7803 0.2672  -0.0722 0.1452  624 ARG C CA  
9398  C C   . ARG C 323 ? 0.7251 1.2913 0.7116 0.2617  -0.0730 0.1498  624 ARG C C   
9399  O O   . ARG C 323 ? 0.7695 1.2874 0.7399 0.2792  -0.0699 0.1563  624 ARG C O   
9400  C CB  . ARG C 323 ? 0.8448 1.5105 0.8498 0.2641  -0.0781 0.1464  624 ARG C CB  
9401  C CG  . ARG C 323 ? 1.0292 1.7137 1.0313 0.2913  -0.0775 0.1514  624 ARG C CG  
9402  C CD  . ARG C 323 ? 1.1408 1.8374 1.1329 0.2962  -0.0836 0.1578  624 ARG C CD  
9403  N NE  . ARG C 323 ? 1.2094 1.9169 1.2019 0.2696  -0.0890 0.1553  624 ARG C NE  
9404  C CZ  . ARG C 323 ? 1.2618 2.0193 1.2683 0.2473  -0.0919 0.1479  624 ARG C CZ  
9405  N NH1 . ARG C 323 ? 1.2972 2.1011 1.3195 0.2473  -0.0898 0.1429  624 ARG C NH1 
9406  N NH2 . ARG C 323 ? 1.2628 2.0227 1.2659 0.2240  -0.0966 0.1452  624 ARG C NH2 
9407  N N   . LYS C 324 ? 0.7200 1.2921 0.7082 0.2366  -0.0768 0.1461  625 LYS C N   
9408  C CA  . LYS C 324 ? 0.8273 1.3548 0.7990 0.2289  -0.0777 0.1501  625 LYS C CA  
9409  C C   . LYS C 324 ? 0.7931 1.3088 0.7706 0.2079  -0.0764 0.1435  625 LYS C C   
9410  O O   . LYS C 324 ? 0.8480 1.3919 0.8423 0.1941  -0.0755 0.1347  625 LYS C O   
9411  C CB  . LYS C 324 ? 0.8419 1.3853 0.8056 0.2194  -0.0838 0.1521  625 LYS C CB  
9412  C CG  . LYS C 324 ? 0.8998 1.4966 0.8783 0.1972  -0.0883 0.1431  625 LYS C CG  
9413  C CD  . LYS C 324 ? 1.0059 1.6352 0.9813 0.1991  -0.0935 0.1457  625 LYS C CD  
9414  C CE  . LYS C 324 ? 1.0096 1.6948 1.0009 0.1787  -0.0966 0.1363  625 LYS C CE  
9415  N NZ  . LYS C 324 ? 0.9582 1.6393 0.9520 0.1494  -0.0976 0.1270  625 LYS C NZ  
9416  N N   . THR C 325 ? 0.6758 1.1385 0.6387 0.1996  -0.0724 0.1441  626 THR C N   
9417  C CA  . THR C 325 ? 0.6646 1.1006 0.6320 0.1748  -0.0666 0.1332  626 THR C CA  
9418  C C   . THR C 325 ? 0.5789 1.0413 0.5517 0.1480  -0.0703 0.1241  626 THR C C   
9419  O O   . THR C 325 ? 0.4989 0.9616 0.4813 0.1289  -0.0675 0.1140  626 THR C O   
9420  C CB  . THR C 325 ? 0.6876 1.0631 0.6387 0.1737  -0.0609 0.1360  626 THR C CB  
9421  O OG1 . THR C 325 ? 0.7203 1.0913 0.6576 0.1683  -0.0645 0.1400  626 THR C OG1 
9422  C CG2 . THR C 325 ? 0.7020 1.0475 0.6434 0.1990  -0.0578 0.1453  626 THR C CG2 
9423  N N   . SER C 326 ? 0.5611 1.0437 0.5257 0.1460  -0.0768 0.1275  627 SER C N   
9424  C CA  . SER C 326 ? 0.4972 0.9948 0.4613 0.1199  -0.0800 0.1184  627 SER C CA  
9425  C C   . SER C 326 ? 0.5090 1.0510 0.4892 0.1042  -0.0829 0.1094  627 SER C C   
9426  O O   . SER C 326 ? 0.4802 1.0242 0.4589 0.0795  -0.0840 0.0998  627 SER C O   
9427  C CB  . SER C 326 ? 0.4521 0.9661 0.4031 0.1228  -0.0869 0.1243  627 SER C CB  
9428  O OG  . SER C 326 ? 0.5908 1.1495 0.5460 0.1415  -0.0937 0.1327  627 SER C OG  
9429  N N   . SER C 327 ? 0.4183 0.9954 0.4127 0.1171  -0.0839 0.1121  628 SER C N   
9430  C CA  . SER C 327 ? 0.3848 1.0000 0.3947 0.0996  -0.0848 0.1033  628 SER C CA  
9431  C C   . SER C 327 ? 0.3719 0.9510 0.3845 0.0821  -0.0775 0.0943  628 SER C C   
9432  O O   . SER C 327 ? 0.4588 1.0612 0.4806 0.0627  -0.0778 0.0864  628 SER C O   
9433  C CB  . SER C 327 ? 0.3922 1.0531 0.4172 0.1192  -0.0862 0.1083  628 SER C CB  
9434  O OG  . SER C 327 ? 0.4604 1.0886 0.4875 0.1359  -0.0787 0.1108  628 SER C OG  
9435  N N   . LEU C 328 ? 0.3952 0.9192 0.3993 0.0881  -0.0712 0.0957  629 LEU C N   
9436  C CA  . LEU C 328 ? 0.4919 0.9798 0.4976 0.0742  -0.0644 0.0881  629 LEU C CA  
9437  C C   . LEU C 328 ? 0.5388 1.0465 0.5596 0.0763  -0.0613 0.0860  629 LEU C C   
9438  O O   . LEU C 328 ? 0.5271 1.0256 0.5518 0.0578  -0.0581 0.0781  629 LEU C O   
9439  C CB  . LEU C 328 ? 0.4064 0.8854 0.4060 0.0460  -0.0658 0.0780  629 LEU C CB  
9440  C CG  . LEU C 328 ? 0.3760 0.8302 0.3596 0.0434  -0.0673 0.0786  629 LEU C CG  
9441  C CD1 . LEU C 328 ? 0.3701 0.7959 0.3463 0.0205  -0.0652 0.0679  629 LEU C CD1 
9442  C CD2 . LEU C 328 ? 0.3719 0.7898 0.3479 0.0633  -0.0632 0.0871  629 LEU C CD2 
9443  N N   . TRP C 329 ? 0.4793 1.0133 0.5073 0.0999  -0.0620 0.0932  630 TRP C N   
9444  C CA  . TRP C 329 ? 0.4052 0.9653 0.4478 0.1036  -0.0589 0.0912  630 TRP C CA  
9445  C C   . TRP C 329 ? 0.4540 0.9681 0.4956 0.1028  -0.0507 0.0880  630 TRP C C   
9446  O O   . TRP C 329 ? 0.4434 0.9672 0.4938 0.0897  -0.0476 0.0819  630 TRP C O   
9447  C CB  . TRP C 329 ? 0.3844 0.9811 0.4332 0.1330  -0.0612 0.0997  630 TRP C CB  
9448  C CG  . TRP C 329 ? 0.4499 1.0068 0.4871 0.1609  -0.0585 0.1083  630 TRP C CG  
9449  C CD1 . TRP C 329 ? 0.5543 1.0973 0.5780 0.1750  -0.0623 0.1167  630 TRP C CD1 
9450  C CD2 . TRP C 329 ? 0.5304 1.0547 0.5663 0.1769  -0.0514 0.1095  630 TRP C CD2 
9451  N NE1 . TRP C 329 ? 0.5456 1.0471 0.5587 0.1980  -0.0580 0.1233  630 TRP C NE1 
9452  C CE2 . TRP C 329 ? 0.5667 1.0559 0.5870 0.1996  -0.0513 0.1186  630 TRP C CE2 
9453  C CE3 . TRP C 329 ? 0.5237 1.0444 0.5686 0.1737  -0.0451 0.1037  630 TRP C CE3 
9454  C CZ2 . TRP C 329 ? 0.5439 0.9929 0.5564 0.2180  -0.0453 0.1214  630 TRP C CZ2 
9455  C CZ3 . TRP C 329 ? 0.4936 0.9765 0.5318 0.1929  -0.0391 0.1063  630 TRP C CZ3 
9456  C CH2 . TRP C 329 ? 0.4615 0.9083 0.4833 0.2145  -0.0393 0.1147  630 TRP C CH2 
9457  N N   . LYS C 330 ? 0.4327 0.8968 0.4625 0.1148  -0.0472 0.0921  631 LYS C N   
9458  C CA  . LYS C 330 ? 0.3558 0.7758 0.3835 0.1114  -0.0400 0.0885  631 LYS C CA  
9459  C C   . LYS C 330 ? 0.4711 0.8770 0.4988 0.0832  -0.0390 0.0794  631 LYS C C   
9460  O O   . LYS C 330 ? 0.3684 0.7662 0.4013 0.0748  -0.0347 0.0745  631 LYS C O   
9461  C CB  . LYS C 330 ? 0.4124 0.7826 0.4260 0.1249  -0.0371 0.0941  631 LYS C CB  
9462  C CG  . LYS C 330 ? 0.5376 0.9076 0.5471 0.1542  -0.0367 0.1030  631 LYS C CG  
9463  C CD  . LYS C 330 ? 0.5162 0.8320 0.5092 0.1634  -0.0334 0.1081  631 LYS C CD  
9464  C CE  . LYS C 330 ? 0.4828 0.7891 0.4690 0.1918  -0.0319 0.1157  631 LYS C CE  
9465  N NZ  . LYS C 330 ? 0.6629 0.9155 0.6299 0.1978  -0.0292 0.1214  631 LYS C NZ  
9466  N N   . ASP C 331 ? 0.4261 0.8272 0.4462 0.0690  -0.0428 0.0771  632 ASP C N   
9467  C CA  . ASP C 331 ? 0.4220 0.8040 0.4385 0.0444  -0.0419 0.0684  632 ASP C CA  
9468  C C   . ASP C 331 ? 0.3659 0.7800 0.3917 0.0274  -0.0429 0.0626  632 ASP C C   
9469  O O   . ASP C 331 ? 0.3929 0.7868 0.4179 0.0127  -0.0397 0.0567  632 ASP C O   
9470  C CB  . ASP C 331 ? 0.3346 0.7100 0.3400 0.0341  -0.0461 0.0665  632 ASP C CB  
9471  C CG  . ASP C 331 ? 0.3583 0.7090 0.3542 0.0500  -0.0454 0.0734  632 ASP C CG  
9472  O OD1 . ASP C 331 ? 0.4271 0.7988 0.4233 0.0665  -0.0483 0.0812  632 ASP C OD1 
9473  O OD2 . ASP C 331 ? 0.3469 0.6584 0.3344 0.0463  -0.0420 0.0715  632 ASP C OD2 
9474  N N   . GLN C 332 ? 0.3797 0.8448 0.4135 0.0290  -0.0475 0.0645  633 GLN C N   
9475  C CA  . GLN C 332 ? 0.4587 0.9612 0.5007 0.0101  -0.0491 0.0593  633 GLN C CA  
9476  C C   . GLN C 332 ? 0.4689 0.9742 0.5206 0.0139  -0.0432 0.0588  633 GLN C C   
9477  O O   . GLN C 332 ? 0.3148 0.8135 0.3662 -0.0063 -0.0410 0.0530  633 GLN C O   
9478  C CB  . GLN C 332 ? 0.5680 1.1297 0.6174 0.0135  -0.0555 0.0623  633 GLN C CB  
9479  C CG  . GLN C 332 ? 0.6751 1.2714 0.7262 -0.0147 -0.0597 0.0557  633 GLN C CG  
9480  C CD  . GLN C 332 ? 0.7231 1.3650 0.7750 -0.0153 -0.0677 0.0577  633 GLN C CD  
9481  O OE1 . GLN C 332 ? 0.6608 1.3262 0.7179 0.0091  -0.0700 0.0654  633 GLN C OE1 
9482  N NE2 . GLN C 332 ? 0.8171 1.4699 0.8620 -0.0430 -0.0722 0.0508  633 GLN C NE2 
9483  N N   . ALA C 333 ? 0.3508 0.8646 0.4092 0.0401  -0.0406 0.0650  634 ALA C N   
9484  C CA  . ALA C 333 ? 0.4338 0.9485 0.4999 0.0463  -0.0345 0.0643  634 ALA C CA  
9485  C C   . ALA C 333 ? 0.4479 0.9068 0.5057 0.0384  -0.0292 0.0607  634 ALA C C   
9486  O O   . ALA C 333 ? 0.4737 0.9310 0.5346 0.0267  -0.0255 0.0567  634 ALA C O   
9487  C CB  . ALA C 333 ? 0.3188 0.8452 0.3897 0.0785  -0.0326 0.0711  634 ALA C CB  
9488  N N   . LEU C 334 ? 0.4461 0.8610 0.4928 0.0437  -0.0292 0.0623  635 LEU C N   
9489  C CA  . LEU C 334 ? 0.5436 0.9084 0.5829 0.0373  -0.0247 0.0592  635 LEU C CA  
9490  C C   . LEU C 334 ? 0.5805 0.9395 0.6171 0.0105  -0.0250 0.0521  635 LEU C C   
9491  O O   . LEU C 334 ? 0.5788 0.9141 0.6140 0.0044  -0.0209 0.0492  635 LEU C O   
9492  C CB  . LEU C 334 ? 0.4151 0.7418 0.4433 0.0438  -0.0252 0.0616  635 LEU C CB  
9493  C CG  . LEU C 334 ? 0.4491 0.7287 0.4701 0.0357  -0.0213 0.0579  635 LEU C CG  
9494  C CD1 . LEU C 334 ? 0.4560 0.7184 0.4794 0.0475  -0.0157 0.0593  635 LEU C CD1 
9495  C CD2 . LEU C 334 ? 0.4179 0.6675 0.4286 0.0368  -0.0222 0.0589  635 LEU C CD2 
9496  N N   . VAL C 335 ? 0.5278 0.9075 0.5621 -0.0058 -0.0302 0.0492  636 VAL C N   
9497  C CA  . VAL C 335 ? 0.4356 0.8056 0.4635 -0.0319 -0.0309 0.0424  636 VAL C CA  
9498  C C   . VAL C 335 ? 0.4057 0.8031 0.4418 -0.0418 -0.0286 0.0410  636 VAL C C   
9499  O O   . VAL C 335 ? 0.4325 0.8066 0.4631 -0.0560 -0.0259 0.0375  636 VAL C O   
9500  C CB  . VAL C 335 ? 0.4854 0.8689 0.5060 -0.0473 -0.0372 0.0392  636 VAL C CB  
9501  C CG1 . VAL C 335 ? 0.4350 0.8112 0.4470 -0.0752 -0.0382 0.0322  636 VAL C CG1 
9502  C CG2 . VAL C 335 ? 0.5759 0.9261 0.5861 -0.0400 -0.0384 0.0394  636 VAL C CG2 
9503  N N   . GLU C 336 ? 0.3609 0.8088 0.4097 -0.0337 -0.0294 0.0442  637 GLU C N   
9504  C CA  . GLU C 336 ? 0.3970 0.8778 0.4545 -0.0433 -0.0267 0.0428  637 GLU C CA  
9505  C C   . GLU C 336 ? 0.4625 0.9202 0.5222 -0.0321 -0.0197 0.0437  637 GLU C C   
9506  O O   . GLU C 336 ? 0.4826 0.9403 0.5416 -0.0472 -0.0166 0.0410  637 GLU C O   
9507  C CB  . GLU C 336 ? 0.3567 0.9016 0.4284 -0.0343 -0.0291 0.0459  637 GLU C CB  
9508  C CG  . GLU C 336 ? 0.5105 1.0842 0.5805 -0.0461 -0.0366 0.0450  637 GLU C CG  
9509  C CD  . GLU C 336 ? 0.5871 1.1710 0.6505 -0.0812 -0.0392 0.0389  637 GLU C CD  
9510  O OE1 . GLU C 336 ? 0.5625 1.1291 0.6217 -0.0975 -0.0353 0.0358  637 GLU C OE1 
9511  O OE2 . GLU C 336 ? 0.6151 1.2239 0.6760 -0.0932 -0.0454 0.0373  637 GLU C OE2 
9512  N N   . ILE C 337 ? 0.4450 0.8817 0.5054 -0.0068 -0.0173 0.0475  638 ILE C N   
9513  C CA  . ILE C 337 ? 0.4530 0.8648 0.5134 0.0036  -0.0110 0.0477  638 ILE C CA  
9514  C C   . ILE C 337 ? 0.5123 0.8794 0.5618 -0.0142 -0.0094 0.0438  638 ILE C C   
9515  O O   . ILE C 337 ? 0.5011 0.8628 0.5506 -0.0205 -0.0053 0.0421  638 ILE C O   
9516  C CB  . ILE C 337 ? 0.4301 0.8208 0.4892 0.0314  -0.0093 0.0523  638 ILE C CB  
9517  C CG1 . ILE C 337 ? 0.4291 0.8646 0.4979 0.0518  -0.0104 0.0565  638 ILE C CG1 
9518  C CG2 . ILE C 337 ? 0.3983 0.7551 0.4540 0.0393  -0.0032 0.0514  638 ILE C CG2 
9519  C CD1 . ILE C 337 ? 0.4486 0.8652 0.5121 0.0756  -0.0117 0.0620  638 ILE C CD1 
9520  N N   . ASN C 338 ? 0.4686 0.8044 0.5080 -0.0220 -0.0128 0.0424  639 ASN C N   
9521  C CA  . ASN C 338 ? 0.5203 0.8133 0.5485 -0.0358 -0.0118 0.0388  639 ASN C CA  
9522  C C   . ASN C 338 ? 0.5800 0.8819 0.6031 -0.0619 -0.0131 0.0350  639 ASN C C   
9523  O O   . ASN C 338 ? 0.5490 0.8219 0.5639 -0.0723 -0.0112 0.0329  639 ASN C O   
9524  C CB  . ASN C 338 ? 0.4949 0.7532 0.5136 -0.0339 -0.0144 0.0381  639 ASN C CB  
9525  C CG  . ASN C 338 ? 0.4756 0.7092 0.4948 -0.0132 -0.0116 0.0414  639 ASN C CG  
9526  O OD1 . ASN C 338 ? 0.4512 0.6499 0.4649 -0.0128 -0.0091 0.0402  639 ASN C OD1 
9527  N ND2 . ASN C 338 ? 0.4467 0.6988 0.4715 0.0040  -0.0121 0.0459  639 ASN C ND2 
9528  N N   . ILE C 339 ? 0.5269 0.8677 0.5534 -0.0735 -0.0167 0.0342  640 ILE C N   
9529  C CA  . ILE C 339 ? 0.4846 0.8381 0.5060 -0.1001 -0.0175 0.0310  640 ILE C CA  
9530  C C   . ILE C 339 ? 0.5249 0.8982 0.5540 -0.1002 -0.0121 0.0325  640 ILE C C   
9531  O O   . ILE C 339 ? 0.5828 0.9389 0.6031 -0.1173 -0.0102 0.0308  640 ILE C O   
9532  C CB  . ILE C 339 ? 0.3701 0.7662 0.3941 -0.1132 -0.0227 0.0298  640 ILE C CB  
9533  C CG1 . ILE C 339 ? 0.4196 0.7893 0.4305 -0.1199 -0.0279 0.0267  640 ILE C CG1 
9534  C CG2 . ILE C 339 ? 0.3444 0.7638 0.3652 -0.1408 -0.0227 0.0274  640 ILE C CG2 
9535  C CD1 . ILE C 339 ? 0.3471 0.7590 0.3603 -0.1306 -0.0334 0.0255  640 ILE C CD1 
9536  N N   . ALA C 340 ? 0.5065 0.9155 0.5509 -0.0801 -0.0095 0.0356  641 ALA C N   
9537  C CA  . ALA C 340 ? 0.4795 0.9122 0.5318 -0.0776 -0.0039 0.0365  641 ALA C CA  
9538  C C   . ALA C 340 ? 0.4712 0.8580 0.5154 -0.0745 0.0006  0.0360  641 ALA C C   
9539  O O   . ALA C 340 ? 0.5060 0.8923 0.5463 -0.0889 0.0037  0.0351  641 ALA C O   
9540  C CB  . ALA C 340 ? 0.4021 0.8750 0.4701 -0.0513 -0.0020 0.0396  641 ALA C CB  
9541  N N   . VAL C 341 ? 0.4591 0.8081 0.5000 -0.0567 0.0007  0.0370  642 VAL C N   
9542  C CA  . VAL C 341 ? 0.4406 0.7486 0.4747 -0.0520 0.0045  0.0367  642 VAL C CA  
9543  C C   . VAL C 341 ? 0.5570 0.8349 0.5771 -0.0753 0.0033  0.0344  642 VAL C C   
9544  O O   . VAL C 341 ? 0.4793 0.7496 0.4953 -0.0825 0.0067  0.0342  642 VAL C O   
9545  C CB  . VAL C 341 ? 0.3447 0.6194 0.3767 -0.0323 0.0040  0.0380  642 VAL C CB  
9546  C CG1 . VAL C 341 ? 0.3018 0.5305 0.3238 -0.0344 0.0055  0.0368  642 VAL C CG1 
9547  C CG2 . VAL C 341 ? 0.3555 0.6493 0.3969 -0.0074 0.0071  0.0406  642 VAL C CG2 
9548  N N   . LEU C 342 ? 0.5225 0.7824 0.5334 -0.0870 -0.0018 0.0327  643 LEU C N   
9549  C CA  . LEU C 342 ? 0.5261 0.7534 0.5206 -0.1079 -0.0034 0.0305  643 LEU C CA  
9550  C C   . LEU C 342 ? 0.5399 0.7912 0.5318 -0.1297 -0.0020 0.0304  643 LEU C C   
9551  O O   . LEU C 342 ? 0.5807 0.8097 0.5621 -0.1401 0.0000  0.0307  643 LEU C O   
9552  C CB  . LEU C 342 ? 0.4248 0.6329 0.4090 -0.1162 -0.0089 0.0278  643 LEU C CB  
9553  C CG  . LEU C 342 ? 0.5227 0.7008 0.5052 -0.0994 -0.0104 0.0275  643 LEU C CG  
9554  C CD1 . LEU C 342 ? 0.3587 0.5336 0.3336 -0.1071 -0.0155 0.0245  643 LEU C CD1 
9555  C CD2 . LEU C 342 ? 0.5104 0.6436 0.4827 -0.0971 -0.0090 0.0270  643 LEU C CD2 
9556  N N   . TYR C 343 ? 0.5264 0.8245 0.5268 -0.1377 -0.0032 0.0302  644 TYR C N   
9557  C CA  . TYR C 343 ? 0.5435 0.8699 0.5415 -0.1614 -0.0019 0.0301  644 TYR C CA  
9558  C C   . TYR C 343 ? 0.5856 0.9271 0.5903 -0.1559 0.0047  0.0322  644 TYR C C   
9559  O O   . TYR C 343 ? 0.5452 0.8856 0.5407 -0.1762 0.0068  0.0325  644 TYR C O   
9560  C CB  . TYR C 343 ? 0.3826 0.7635 0.3915 -0.1682 -0.0046 0.0295  644 TYR C CB  
9561  C CG  . TYR C 343 ? 0.4188 0.8483 0.4331 -0.1867 -0.0019 0.0301  644 TYR C CG  
9562  C CD1 . TYR C 343 ? 0.4389 0.8655 0.4381 -0.2199 -0.0039 0.0285  644 TYR C CD1 
9563  C CD2 . TYR C 343 ? 0.4743 0.9537 0.5078 -0.1711 0.0028  0.0320  644 TYR C CD2 
9564  C CE1 . TYR C 343 ? 0.5208 0.9947 0.5248 -0.2390 -0.0011 0.0292  644 TYR C CE1 
9565  C CE2 . TYR C 343 ? 0.4216 0.9505 0.4611 -0.1877 0.0058  0.0323  644 TYR C CE2 
9566  C CZ  . TYR C 343 ? 0.5466 1.0742 0.5719 -0.2228 0.0039  0.0311  644 TYR C CZ  
9567  O OH  . TYR C 343 ? 0.6565 1.2362 0.6875 -0.2418 0.0072  0.0317  644 TYR C OH  
9568  N N   . SER C 344 ? 0.5807 0.9332 0.5990 -0.1291 0.0081  0.0335  645 SER C N   
9569  C CA  . SER C 344 ? 0.4981 0.8658 0.5219 -0.1221 0.0146  0.0345  645 SER C CA  
9570  C C   . SER C 344 ? 0.5114 0.8298 0.5209 -0.1257 0.0165  0.0347  645 SER C C   
9571  O O   . SER C 344 ? 0.5829 0.9055 0.5866 -0.1392 0.0200  0.0354  645 SER C O   
9572  C CB  . SER C 344 ? 0.3935 0.7822 0.4327 -0.0915 0.0175  0.0352  645 SER C CB  
9573  O OG  . SER C 344 ? 0.4736 0.9179 0.5267 -0.0885 0.0166  0.0356  645 SER C OG  
9574  N N   . PHE C 345 ? 0.4907 0.7641 0.4942 -0.1137 0.0141  0.0344  646 PHE C N   
9575  C CA  . PHE C 345 ? 0.5384 0.7657 0.5280 -0.1166 0.0147  0.0347  646 PHE C CA  
9576  C C   . PHE C 345 ? 0.6473 0.8563 0.6194 -0.1437 0.0125  0.0350  646 PHE C C   
9577  O O   . PHE C 345 ? 0.6549 0.8494 0.6172 -0.1521 0.0150  0.0365  646 PHE C O   
9578  C CB  . PHE C 345 ? 0.4311 0.6186 0.4176 -0.1014 0.0117  0.0341  646 PHE C CB  
9579  C CG  . PHE C 345 ? 0.3829 0.5689 0.3787 -0.0772 0.0150  0.0344  646 PHE C CG  
9580  C CD1 . PHE C 345 ? 0.3880 0.6077 0.3978 -0.0616 0.0171  0.0347  646 PHE C CD1 
9581  C CD2 . PHE C 345 ? 0.3473 0.4973 0.3361 -0.0702 0.0158  0.0344  646 PHE C CD2 
9582  C CE1 . PHE C 345 ? 0.3441 0.5566 0.3585 -0.0397 0.0202  0.0349  646 PHE C CE1 
9583  C CE2 . PHE C 345 ? 0.3903 0.5363 0.3851 -0.0505 0.0188  0.0342  646 PHE C CE2 
9584  C CZ  . PHE C 345 ? 0.4243 0.5989 0.4307 -0.0354 0.0211  0.0344  646 PHE C CZ  
9585  N N   . GLN C 346 ? 0.6691 0.8766 0.6350 -0.1582 0.0077  0.0338  647 GLN C N   
9586  C CA  . GLN C 346 ? 0.6278 0.8107 0.5729 -0.1844 0.0053  0.0339  647 GLN C CA  
9587  C C   . GLN C 346 ? 0.6221 0.8385 0.5662 -0.2049 0.0090  0.0356  647 GLN C C   
9588  O O   . GLN C 346 ? 0.6015 0.7929 0.5269 -0.2235 0.0092  0.0373  647 GLN C O   
9589  C CB  . GLN C 346 ? 0.6156 0.7881 0.5524 -0.1952 -0.0005 0.0311  647 GLN C CB  
9590  C CG  . GLN C 346 ? 0.6456 0.7739 0.5758 -0.1804 -0.0040 0.0294  647 GLN C CG  
9591  C CD  . GLN C 346 ? 0.6143 0.7421 0.5415 -0.1846 -0.0090 0.0260  647 GLN C CD  
9592  O OE1 . GLN C 346 ? 0.6102 0.7686 0.5385 -0.2006 -0.0105 0.0248  647 GLN C OE1 
9593  N NE2 . GLN C 346 ? 0.5497 0.6449 0.4729 -0.1705 -0.0114 0.0242  647 GLN C NE2 
9594  N N   . SER C 347 ? 0.5908 0.8641 0.5538 -0.2014 0.0119  0.0354  648 SER C N   
9595  C CA  . SER C 347 ? 0.5459 0.8588 0.5100 -0.2207 0.0160  0.0369  648 SER C CA  
9596  C C   . SER C 347 ? 0.6224 0.9279 0.5838 -0.2160 0.0219  0.0390  648 SER C C   
9597  O O   . SER C 347 ? 0.6904 1.0046 0.6419 -0.2378 0.0248  0.0410  648 SER C O   
9598  C CB  . SER C 347 ? 0.5583 0.9382 0.5451 -0.2139 0.0177  0.0359  648 SER C CB  
9599  O OG  . SER C 347 ? 0.6509 1.0426 0.6385 -0.2231 0.0119  0.0341  648 SER C OG  
9600  N N   . ASP C 348 ? 0.5299 0.8202 0.4989 -0.1891 0.0239  0.0387  649 ASP C N   
9601  C CA  . ASP C 348 ? 0.4056 0.6878 0.3720 -0.1820 0.0292  0.0399  649 ASP C CA  
9602  C C   . ASP C 348 ? 0.5069 0.7285 0.4534 -0.1848 0.0264  0.0415  649 ASP C C   
9603  O O   . ASP C 348 ? 0.5216 0.7289 0.4657 -0.1744 0.0296  0.0422  649 ASP C O   
9604  C CB  . ASP C 348 ? 0.3883 0.6891 0.3726 -0.1517 0.0329  0.0381  649 ASP C CB  
9605  C CG  . ASP C 348 ? 0.5008 0.8644 0.5035 -0.1461 0.0367  0.0371  649 ASP C CG  
9606  O OD1 . ASP C 348 ? 0.4847 0.8828 0.4876 -0.1678 0.0373  0.0378  649 ASP C OD1 
9607  O OD2 . ASP C 348 ? 0.5462 0.9249 0.5623 -0.1202 0.0391  0.0355  649 ASP C OD2 
9608  N N   . LYS C 349 ? 0.5497 0.7360 0.4811 -0.1976 0.0205  0.0417  650 LYS C N   
9609  C CA  . LYS C 349 ? 0.6368 0.7657 0.5482 -0.1991 0.0170  0.0433  650 LYS C CA  
9610  C C   . LYS C 349 ? 0.6990 0.8082 0.6171 -0.1731 0.0176  0.0426  650 LYS C C   
9611  O O   . LYS C 349 ? 0.7009 0.7830 0.6080 -0.1715 0.0182  0.0446  650 LYS C O   
9612  C CB  . LYS C 349 ? 0.6719 0.7866 0.5630 -0.2212 0.0186  0.0471  650 LYS C CB  
9613  C CG  . LYS C 349 ? 0.8450 0.9703 0.7240 -0.2513 0.0174  0.0481  650 LYS C CG  
9614  C CD  . LYS C 349 ? 0.9952 1.1808 0.8874 -0.2620 0.0236  0.0487  650 LYS C CD  
9615  C CE  . LYS C 349 ? 1.1259 1.3083 1.0034 -0.2777 0.0280  0.0530  650 LYS C CE  
9616  N NZ  . LYS C 349 ? 1.1953 1.3365 1.0425 -0.3059 0.0242  0.0565  650 LYS C NZ  
9617  N N   . VAL C 350 ? 0.6072 0.7304 0.5425 -0.1535 0.0174  0.0400  651 VAL C N   
9618  C CA  . VAL C 350 ? 0.5430 0.6449 0.4833 -0.1309 0.0173  0.0390  651 VAL C CA  
9619  C C   . VAL C 350 ? 0.6137 0.6863 0.5502 -0.1260 0.0115  0.0377  651 VAL C C   
9620  O O   . VAL C 350 ? 0.5741 0.6610 0.5164 -0.1277 0.0093  0.0362  651 VAL C O   
9621  C CB  . VAL C 350 ? 0.4915 0.6263 0.4509 -0.1114 0.0217  0.0374  651 VAL C CB  
9622  C CG1 . VAL C 350 ? 0.4319 0.5413 0.3934 -0.0915 0.0216  0.0364  651 VAL C CG1 
9623  C CG2 . VAL C 350 ? 0.3968 0.5647 0.3599 -0.1155 0.0279  0.0378  651 VAL C CG2 
9624  N N   . THR C 351 ? 0.5703 0.6042 0.4969 -0.1199 0.0091  0.0381  652 THR C N   
9625  C CA  . THR C 351 ? 0.5615 0.5673 0.4831 -0.1148 0.0041  0.0366  652 THR C CA  
9626  C C   . THR C 351 ? 0.5446 0.5687 0.4825 -0.1004 0.0041  0.0345  652 THR C C   
9627  O O   . THR C 351 ? 0.5866 0.6261 0.5372 -0.0861 0.0073  0.0345  652 THR C O   
9628  C CB  . THR C 351 ? 0.5517 0.5225 0.4647 -0.1057 0.0022  0.0374  652 THR C CB  
9629  O OG1 . THR C 351 ? 0.6491 0.6054 0.5472 -0.1170 0.0025  0.0403  652 THR C OG1 
9630  C CG2 . THR C 351 ? 0.5080 0.4495 0.4124 -0.1027 -0.0029 0.0357  652 THR C CG2 
9631  N N   . ILE C 352 ? 0.5167 0.5371 0.4518 -0.1050 0.0005  0.0328  653 ILE C N   
9632  C CA  . ILE C 352 ? 0.3876 0.4198 0.3345 -0.0923 -0.0004 0.0312  653 ILE C CA  
9633  C C   . ILE C 352 ? 0.5489 0.5596 0.4845 -0.0987 -0.0052 0.0288  653 ILE C C   
9634  O O   . ILE C 352 ? 0.5018 0.4956 0.4217 -0.1146 -0.0074 0.0282  653 ILE C O   
9635  C CB  . ILE C 352 ? 0.3464 0.4226 0.3079 -0.0912 0.0019  0.0317  653 ILE C CB  
9636  C CG1 . ILE C 352 ? 0.4859 0.5721 0.4593 -0.0738 0.0016  0.0315  653 ILE C CG1 
9637  C CG2 . ILE C 352 ? 0.3585 0.4518 0.3151 -0.1105 -0.0003 0.0308  653 ILE C CG2 
9638  C CD1 . ILE C 352 ? 0.4021 0.5306 0.3895 -0.0679 0.0038  0.0326  653 ILE C CD1 
9639  N N   . VAL C 353 ? 0.5855 0.5939 0.5270 -0.0864 -0.0066 0.0274  654 VAL C N   
9640  C CA  . VAL C 353 ? 0.5940 0.5827 0.5249 -0.0898 -0.0106 0.0242  654 VAL C CA  
9641  C C   . VAL C 353 ? 0.5000 0.5120 0.4417 -0.0831 -0.0112 0.0233  654 VAL C C   
9642  O O   . VAL C 353 ? 0.5563 0.5814 0.5110 -0.0685 -0.0090 0.0253  654 VAL C O   
9643  C CB  . VAL C 353 ? 0.6199 0.5736 0.5426 -0.0802 -0.0119 0.0232  654 VAL C CB  
9644  C CG1 . VAL C 353 ? 0.5369 0.4966 0.4732 -0.0626 -0.0097 0.0246  654 VAL C CG1 
9645  C CG2 . VAL C 353 ? 0.6871 0.6196 0.5968 -0.0826 -0.0157 0.0191  654 VAL C CG2 
9646  N N   . ASP C 354 ? 0.4535 0.4705 0.3883 -0.0946 -0.0143 0.0206  655 ASP C N   
9647  C CA  . ASP C 354 ? 0.4571 0.4963 0.4004 -0.0886 -0.0155 0.0200  655 ASP C CA  
9648  C C   . ASP C 354 ? 0.5609 0.5787 0.5020 -0.0754 -0.0163 0.0184  655 ASP C C   
9649  O O   . ASP C 354 ? 0.5940 0.5815 0.5264 -0.0721 -0.0164 0.0170  655 ASP C O   
9650  C CB  . ASP C 354 ? 0.4421 0.4946 0.3778 -0.1060 -0.0189 0.0170  655 ASP C CB  
9651  C CG  . ASP C 354 ? 0.5689 0.5846 0.4830 -0.1170 -0.0222 0.0121  655 ASP C CG  
9652  O OD1 . ASP C 354 ? 0.5931 0.5891 0.5021 -0.1074 -0.0233 0.0094  655 ASP C OD1 
9653  O OD2 . ASP C 354 ? 0.6833 0.6889 0.5837 -0.1354 -0.0234 0.0108  655 ASP C OD2 
9654  N N   . HIS C 355 ? 0.4947 0.5305 0.4432 -0.0676 -0.0168 0.0188  656 HIS C N   
9655  C CA  . HIS C 355 ? 0.4884 0.5085 0.4356 -0.0558 -0.0168 0.0177  656 HIS C CA  
9656  C C   . HIS C 355 ? 0.5853 0.5828 0.5163 -0.0624 -0.0198 0.0119  656 HIS C C   
9657  O O   . HIS C 355 ? 0.5732 0.5506 0.4999 -0.0536 -0.0194 0.0101  656 HIS C O   
9658  C CB  . HIS C 355 ? 0.4998 0.5441 0.4581 -0.0451 -0.0162 0.0210  656 HIS C CB  
9659  C CG  . HIS C 355 ? 0.4823 0.5559 0.4427 -0.0525 -0.0188 0.0211  656 HIS C CG  
9660  N ND1 . HIS C 355 ? 0.4734 0.5738 0.4419 -0.0570 -0.0183 0.0235  656 HIS C ND1 
9661  C CD2 . HIS C 355 ? 0.4661 0.5495 0.4219 -0.0560 -0.0219 0.0188  656 HIS C CD2 
9662  C CE1 . HIS C 355 ? 0.5208 0.6481 0.4904 -0.0630 -0.0213 0.0230  656 HIS C CE1 
9663  N NE2 . HIS C 355 ? 0.4529 0.5695 0.4144 -0.0630 -0.0238 0.0202  656 HIS C NE2 
9664  N N   . HIS C 356 ? 0.5139 0.5145 0.4349 -0.0780 -0.0228 0.0086  657 HIS C N   
9665  C CA  . HIS C 356 ? 0.5455 0.5190 0.4470 -0.0851 -0.0257 0.0022  657 HIS C CA  
9666  C C   . HIS C 356 ? 0.5727 0.5086 0.4610 -0.0849 -0.0254 0.0005  657 HIS C C   
9667  O O   . HIS C 356 ? 0.5222 0.4332 0.4007 -0.0767 -0.0259 -0.0032 657 HIS C O   
9668  C CB  . HIS C 356 ? 0.5225 0.5064 0.4144 -0.1047 -0.0290 -0.0009 657 HIS C CB  
9669  C CG  . HIS C 356 ? 0.5348 0.5598 0.4397 -0.1051 -0.0299 0.0012  657 HIS C CG  
9670  N ND1 . HIS C 356 ? 0.4504 0.4847 0.3578 -0.0958 -0.0308 0.0001  657 HIS C ND1 
9671  C CD2 . HIS C 356 ? 0.4631 0.5243 0.3794 -0.1123 -0.0301 0.0046  657 HIS C CD2 
9672  C CE1 . HIS C 356 ? 0.4978 0.5702 0.4165 -0.0970 -0.0320 0.0033  657 HIS C CE1 
9673  N NE2 . HIS C 356 ? 0.4865 0.5771 0.4114 -0.1062 -0.0317 0.0058  657 HIS C NE2 
9674  N N   . SER C 357 ? 0.6299 0.5626 0.5172 -0.0932 -0.0248 0.0034  658 SER C N   
9675  C CA  A SER C 357 ? 0.5943 0.4915 0.4678 -0.0931 -0.0251 0.0030  658 SER C CA  
9676  C CA  B SER C 357 ? 0.5940 0.4906 0.4671 -0.0929 -0.0251 0.0028  658 SER C CA  
9677  C C   . SER C 357 ? 0.4978 0.3881 0.3804 -0.0740 -0.0230 0.0050  658 SER C C   
9678  O O   . SER C 357 ? 0.4807 0.3422 0.3516 -0.0668 -0.0240 0.0026  658 SER C O   
9679  C CB  A SER C 357 ? 0.6351 0.5358 0.5068 -0.1068 -0.0244 0.0067  658 SER C CB  
9680  C CB  B SER C 357 ? 0.6394 0.5365 0.5086 -0.1075 -0.0247 0.0061  658 SER C CB  
9681  O OG  A SER C 357 ? 0.6504 0.5191 0.5098 -0.1053 -0.0246 0.0080  658 SER C OG  
9682  O OG  B SER C 357 ? 0.6854 0.5868 0.5433 -0.1277 -0.0270 0.0037  658 SER C OG  
9683  N N   . ALA C 358 ? 0.4643 0.3809 0.3668 -0.0654 -0.0201 0.0093  659 ALA C N   
9684  C CA  . ALA C 358 ? 0.5355 0.4470 0.4462 -0.0505 -0.0181 0.0113  659 ALA C CA  
9685  C C   . ALA C 358 ? 0.5935 0.4990 0.5033 -0.0392 -0.0183 0.0082  659 ALA C C   
9686  O O   . ALA C 358 ? 0.5153 0.4051 0.4224 -0.0298 -0.0182 0.0074  659 ALA C O   
9687  C CB  . ALA C 358 ? 0.5096 0.4473 0.4386 -0.0454 -0.0148 0.0162  659 ALA C CB  
9688  N N   . THR C 359 ? 0.5737 0.4941 0.4858 -0.0398 -0.0186 0.0064  660 THR C N   
9689  C CA  . THR C 359 ? 0.4967 0.4134 0.4071 -0.0298 -0.0183 0.0032  660 THR C CA  
9690  C C   . THR C 359 ? 0.4861 0.3736 0.3771 -0.0302 -0.0207 -0.0030 660 THR C C   
9691  O O   . THR C 359 ? 0.5509 0.4284 0.4396 -0.0186 -0.0200 -0.0054 660 THR C O   
9692  C CB  . THR C 359 ? 0.4494 0.3887 0.3649 -0.0307 -0.0183 0.0033  660 THR C CB  
9693  O OG1 . THR C 359 ? 0.4638 0.4068 0.3709 -0.0444 -0.0211 0.0009  660 THR C OG1 
9694  C CG2 . THR C 359 ? 0.4371 0.3999 0.3696 -0.0254 -0.0157 0.0097  660 THR C CG2 
9695  N N   . GLU C 360 ? 0.4955 0.3693 0.3715 -0.0435 -0.0234 -0.0059 661 GLU C N   
9696  C CA  . GLU C 360 ? 0.5368 0.3758 0.3900 -0.0441 -0.0258 -0.0119 661 GLU C CA  
9697  C C   . GLU C 360 ? 0.6395 0.4561 0.4883 -0.0348 -0.0258 -0.0104 661 GLU C C   
9698  O O   . GLU C 360 ? 0.6709 0.4659 0.5080 -0.0239 -0.0266 -0.0146 661 GLU C O   
9699  C CB  . GLU C 360 ? 0.7080 0.5346 0.5444 -0.0633 -0.0287 -0.0143 661 GLU C CB  
9700  C CG  . GLU C 360 ? 0.9579 0.7406 0.7663 -0.0656 -0.0313 -0.0198 661 GLU C CG  
9701  C CD  . GLU C 360 ? 1.1453 0.9123 0.9355 -0.0880 -0.0340 -0.0206 661 GLU C CD  
9702  O OE1 . GLU C 360 ? 1.1288 0.9214 0.9310 -0.1007 -0.0333 -0.0158 661 GLU C OE1 
9703  O OE2 . GLU C 360 ? 1.2114 0.9403 0.9743 -0.0932 -0.0365 -0.0261 661 GLU C OE2 
9704  N N   . SER C 361 ? 0.5163 0.3389 0.3738 -0.0381 -0.0250 -0.0045 662 SER C N   
9705  C CA  . SER C 361 ? 0.6117 0.4166 0.4660 -0.0293 -0.0254 -0.0023 662 SER C CA  
9706  C C   . SER C 361 ? 0.6872 0.5028 0.5535 -0.0116 -0.0237 -0.0026 662 SER C C   
9707  O O   . SER C 361 ? 0.7219 0.5200 0.5803 -0.0005 -0.0250 -0.0041 662 SER C O   
9708  C CB  . SER C 361 ? 0.7235 0.5380 0.5864 -0.0365 -0.0244 0.0040  662 SER C CB  
9709  O OG  . SER C 361 ? 0.8730 0.6771 0.7228 -0.0538 -0.0259 0.0044  662 SER C OG  
9710  N N   . PHE C 362 ? 0.5926 0.4375 0.4771 -0.0090 -0.0209 -0.0010 663 PHE C N   
9711  C CA  . PHE C 362 ? 0.5645 0.4219 0.4605 0.0047  -0.0189 -0.0007 663 PHE C CA  
9712  C C   . PHE C 362 ? 0.6621 0.5101 0.5481 0.0146  -0.0194 -0.0070 663 PHE C C   
9713  O O   . PHE C 362 ? 0.6644 0.5105 0.5514 0.0271  -0.0192 -0.0081 663 PHE C O   
9714  C CB  . PHE C 362 ? 0.4567 0.3433 0.3710 0.0038  -0.0157 0.0030  663 PHE C CB  
9715  C CG  . PHE C 362 ? 0.5006 0.4001 0.4259 0.0144  -0.0134 0.0041  663 PHE C CG  
9716  C CD1 . PHE C 362 ? 0.5342 0.4348 0.4662 0.0180  -0.0130 0.0072  663 PHE C CD1 
9717  C CD2 . PHE C 362 ? 0.5515 0.4622 0.4788 0.0198  -0.0117 0.0017  663 PHE C CD2 
9718  C CE1 . PHE C 362 ? 0.4574 0.3718 0.3988 0.0255  -0.0110 0.0079  663 PHE C CE1 
9719  C CE2 . PHE C 362 ? 0.5295 0.4540 0.4661 0.0274  -0.0093 0.0027  663 PHE C CE2 
9720  C CZ  . PHE C 362 ? 0.5589 0.4856 0.5027 0.0297  -0.0090 0.0058  663 PHE C CZ  
9721  N N   . ILE C 363 ? 0.7036 0.5469 0.5795 0.0095  -0.0200 -0.0116 664 ILE C N   
9722  C CA  . ILE C 363 ? 0.6811 0.5119 0.5439 0.0190  -0.0204 -0.0188 664 ILE C CA  
9723  C C   . ILE C 363 ? 0.7160 0.5155 0.5620 0.0275  -0.0229 -0.0214 664 ILE C C   
9724  O O   . ILE C 363 ? 0.6730 0.4709 0.5174 0.0432  -0.0223 -0.0245 664 ILE C O   
9725  C CB  . ILE C 363 ? 0.6573 0.4826 0.5074 0.0093  -0.0215 -0.0238 664 ILE C CB  
9726  C CG1 . ILE C 363 ? 0.6045 0.4622 0.4701 0.0036  -0.0194 -0.0209 664 ILE C CG1 
9727  C CG2 . ILE C 363 ? 0.4927 0.2986 0.3247 0.0194  -0.0219 -0.0324 664 ILE C CG2 
9728  C CD1 . ILE C 363 ? 0.5996 0.4793 0.4765 0.0151  -0.0160 -0.0210 664 ILE C CD1 
9729  N N   . LYS C 364 ? 0.6906 0.4656 0.5231 0.0173  -0.0258 -0.0199 665 LYS C N   
9730  C CA  . LYS C 364 ? 0.7349 0.4769 0.5494 0.0249  -0.0286 -0.0207 665 LYS C CA  
9731  C C   . LYS C 364 ? 0.7222 0.4769 0.5505 0.0385  -0.0281 -0.0164 665 LYS C C   
9732  O O   . LYS C 364 ? 0.7350 0.4754 0.5540 0.0543  -0.0296 -0.0188 665 LYS C O   
9733  C CB  . LYS C 364 ? 0.7720 0.4893 0.5711 0.0081  -0.0313 -0.0181 665 LYS C CB  
9734  C CG  . LYS C 364 ? 0.9695 0.6469 0.7455 0.0134  -0.0347 -0.0177 665 LYS C CG  
9735  C CD  . LYS C 364 ? 1.2386 0.9086 1.0116 -0.0026 -0.0359 -0.0109 665 LYS C CD  
9736  C CE  . LYS C 364 ? 1.3598 0.9844 1.1044 -0.0011 -0.0398 -0.0096 665 LYS C CE  
9737  N NZ  . LYS C 364 ? 1.3797 0.9682 1.0953 -0.0172 -0.0419 -0.0132 665 LYS C NZ  
9738  N N   . HIS C 365 ? 0.6227 0.4048 0.4724 0.0332  -0.0262 -0.0103 666 HIS C N   
9739  C CA  . HIS C 365 ? 0.6715 0.4678 0.5342 0.0438  -0.0258 -0.0067 666 HIS C CA  
9740  C C   . HIS C 365 ? 0.7663 0.5829 0.6385 0.0584  -0.0237 -0.0101 666 HIS C C   
9741  O O   . HIS C 365 ? 0.6796 0.4957 0.5507 0.0727  -0.0250 -0.0109 666 HIS C O   
9742  C CB  . HIS C 365 ? 0.5931 0.4115 0.4741 0.0337  -0.0239 -0.0004 666 HIS C CB  
9743  C CG  . HIS C 365 ? 0.6294 0.4661 0.5247 0.0418  -0.0232 0.0028  666 HIS C CG  
9744  N ND1 . HIS C 365 ? 0.6457 0.4715 0.5350 0.0500  -0.0261 0.0043  666 HIS C ND1 
9745  C CD2 . HIS C 365 ? 0.5915 0.4564 0.5056 0.0418  -0.0201 0.0049  666 HIS C CD2 
9746  C CE1 . HIS C 365 ? 0.4873 0.3365 0.3923 0.0541  -0.0250 0.0066  666 HIS C CE1 
9747  N NE2 . HIS C 365 ? 0.5218 0.3934 0.4412 0.0485  -0.0212 0.0070  666 HIS C NE2 
9748  N N   . MET C 366 ? 0.7039 0.5402 0.5849 0.0552  -0.0206 -0.0121 667 MET C N   
9749  C CA  . MET C 366 ? 0.5913 0.4467 0.4787 0.0674  -0.0180 -0.0159 667 MET C CA  
9750  C C   . MET C 366 ? 0.5751 0.4101 0.4451 0.0829  -0.0200 -0.0223 667 MET C C   
9751  O O   . MET C 366 ? 0.5564 0.4045 0.4317 0.0976  -0.0195 -0.0234 667 MET C O   
9752  C CB  . MET C 366 ? 0.6002 0.4707 0.4918 0.0607  -0.0150 -0.0178 667 MET C CB  
9753  C CG  . MET C 366 ? 0.6196 0.5185 0.5307 0.0530  -0.0119 -0.0119 667 MET C CG  
9754  S SD  . MET C 366 ? 0.6893 0.6110 0.6053 0.0516  -0.0081 -0.0137 667 MET C SD  
9755  C CE  . MET C 366 ? 0.6198 0.5549 0.5365 0.0678  -0.0057 -0.0188 667 MET C CE  
9756  N N   . GLU C 367 ? 0.6162 0.4193 0.4644 0.0800  -0.0221 -0.0268 668 GLU C N   
9757  C CA  . GLU C 367 ? 0.7003 0.4787 0.5281 0.0961  -0.0239 -0.0335 668 GLU C CA  
9758  C C   . GLU C 367 ? 0.7830 0.5513 0.6076 0.1092  -0.0269 -0.0306 668 GLU C C   
9759  O O   . GLU C 367 ? 0.7489 0.5230 0.5722 0.1288  -0.0269 -0.0340 668 GLU C O   
9760  C CB  . GLU C 367 ? 0.8034 0.5429 0.6047 0.0877  -0.0262 -0.0384 668 GLU C CB  
9761  C CG  . GLU C 367 ? 1.0652 0.8113 0.8622 0.0854  -0.0237 -0.0454 668 GLU C CG  
9762  C CD  . GLU C 367 ? 1.1304 0.8527 0.9105 0.0666  -0.0257 -0.0475 668 GLU C CD  
9763  O OE1 . GLU C 367 ? 1.2206 0.9045 0.9787 0.0620  -0.0293 -0.0480 668 GLU C OE1 
9764  O OE2 . GLU C 367 ? 1.0391 0.7818 0.8273 0.0557  -0.0238 -0.0482 668 GLU C OE2 
9765  N N   . ASN C 368 ? 0.7765 0.5326 0.6003 0.0990  -0.0296 -0.0241 669 ASN C N   
9766  C CA  . ASN C 368 ? 0.7013 0.4479 0.5211 0.1104  -0.0330 -0.0204 669 ASN C CA  
9767  C C   . ASN C 368 ? 0.6822 0.4687 0.5246 0.1229  -0.0314 -0.0189 669 ASN C C   
9768  O O   . ASN C 368 ? 0.7177 0.5042 0.5555 0.1421  -0.0334 -0.0206 669 ASN C O   
9769  C CB  . ASN C 368 ? 0.7521 0.4872 0.5710 0.0948  -0.0351 -0.0131 669 ASN C CB  
9770  C CG  . ASN C 368 ? 0.8041 0.4985 0.5980 0.0823  -0.0373 -0.0138 669 ASN C CG  
9771  O OD1 . ASN C 368 ? 0.8142 0.4778 0.5850 0.0891  -0.0389 -0.0195 669 ASN C OD1 
9772  N ND2 . ASN C 368 ? 0.7656 0.4596 0.5627 0.0632  -0.0373 -0.0084 669 ASN C ND2 
9773  N N   . GLU C 369 ? 0.6022 0.4231 0.4679 0.1119  -0.0279 -0.0158 670 GLU C N   
9774  C CA  . GLU C 369 ? 0.6043 0.4631 0.4908 0.1191  -0.0263 -0.0139 670 GLU C CA  
9775  C C   . GLU C 369 ? 0.6946 0.5715 0.5828 0.1362  -0.0243 -0.0201 670 GLU C C   
9776  O O   . GLU C 369 ? 0.6225 0.5171 0.5161 0.1511  -0.0255 -0.0203 670 GLU C O   
9777  C CB  . GLU C 369 ? 0.5077 0.3931 0.4145 0.1025  -0.0227 -0.0096 670 GLU C CB  
9778  C CG  . GLU C 369 ? 0.6187 0.4935 0.5267 0.0884  -0.0242 -0.0036 670 GLU C CG  
9779  C CD  . GLU C 369 ? 0.6524 0.5349 0.5657 0.0927  -0.0270 0.0005  670 GLU C CD  
9780  O OE1 . GLU C 369 ? 0.5714 0.4772 0.5006 0.0851  -0.0252 0.0039  670 GLU C OE1 
9781  O OE2 . GLU C 369 ? 0.5962 0.4601 0.4961 0.1037  -0.0312 0.0003  670 GLU C OE2 
9782  N N   . TYR C 370 ? 0.6974 0.5726 0.5807 0.1347  -0.0212 -0.0254 671 TYR C N   
9783  C CA  . TYR C 370 ? 0.5945 0.4879 0.4783 0.1512  -0.0185 -0.0319 671 TYR C CA  
9784  C C   . TYR C 370 ? 0.6258 0.4964 0.4910 0.1733  -0.0221 -0.0363 671 TYR C C   
9785  O O   . TYR C 370 ? 0.7880 0.6830 0.6595 0.1914  -0.0215 -0.0389 671 TYR C O   
9786  C CB  . TYR C 370 ? 0.5513 0.4436 0.4302 0.1449  -0.0147 -0.0371 671 TYR C CB  
9787  C CG  . TYR C 370 ? 0.5949 0.5248 0.4953 0.1325  -0.0100 -0.0336 671 TYR C CG  
9788  C CD1 . TYR C 370 ? 0.5928 0.5219 0.5005 0.1131  -0.0097 -0.0276 671 TYR C CD1 
9789  C CD2 . TYR C 370 ? 0.6596 0.6259 0.5719 0.1405  -0.0058 -0.0358 671 TYR C CD2 
9790  C CE1 . TYR C 370 ? 0.5364 0.4947 0.4605 0.1030  -0.0057 -0.0239 671 TYR C CE1 
9791  C CE2 . TYR C 370 ? 0.5246 0.5215 0.4535 0.1279  -0.0015 -0.0318 671 TYR C CE2 
9792  C CZ  . TYR C 370 ? 0.5167 0.5071 0.4504 0.1096  -0.0017 -0.0257 671 TYR C CZ  
9793  O OH  . TYR C 370 ? 0.5276 0.5434 0.4747 0.0983  0.0023  -0.0213 671 TYR C OH  
9794  N N   . ARG C 371 ? 0.6683 0.4922 0.5098 0.1722  -0.0261 -0.0368 672 ARG C N   
9795  C CA  . ARG C 371 ? 0.7738 0.5670 0.5924 0.1935  -0.0301 -0.0404 672 ARG C CA  
9796  C C   . ARG C 371 ? 0.8350 0.6439 0.6622 0.2067  -0.0335 -0.0352 672 ARG C C   
9797  O O   . ARG C 371 ? 0.8757 0.6907 0.6981 0.2310  -0.0348 -0.0387 672 ARG C O   
9798  C CB  . ARG C 371 ? 0.9471 0.6846 0.7372 0.1843  -0.0337 -0.0405 672 ARG C CB  
9799  C CG  . ARG C 371 ? 1.1188 0.8137 0.8798 0.2041  -0.0385 -0.0426 672 ARG C CG  
9800  C CD  . ARG C 371 ? 1.3024 0.9468 1.0393 0.1889  -0.0427 -0.0385 672 ARG C CD  
9801  N NE  . ARG C 371 ? 1.4185 1.0619 1.1597 0.1610  -0.0405 -0.0375 672 ARG C NE  
9802  C CZ  . ARG C 371 ? 1.5763 1.2010 1.3031 0.1525  -0.0388 -0.0442 672 ARG C CZ  
9803  N NH1 . ARG C 371 ? 1.6479 1.2503 1.3537 0.1695  -0.0387 -0.0531 672 ARG C NH1 
9804  N NH2 . ARG C 371 ? 1.5994 1.2292 1.3325 0.1276  -0.0373 -0.0424 672 ARG C NH2 
9805  N N   . CYS C 372 ? 0.7614 0.5783 0.6008 0.1921  -0.0353 -0.0271 673 CYS C N   
9806  C CA  . CYS C 372 ? 0.8419 0.6698 0.6861 0.2034  -0.0395 -0.0221 673 CYS C CA  
9807  C C   . CYS C 372 ? 0.7648 0.6484 0.6390 0.2014  -0.0372 -0.0195 673 CYS C C   
9808  O O   . CYS C 372 ? 0.8516 0.7548 0.7313 0.2159  -0.0404 -0.0177 673 CYS C O   
9809  C CB  . CYS C 372 ? 0.9485 0.7452 0.7819 0.1903  -0.0437 -0.0149 673 CYS C CB  
9810  S SG  . CYS C 372 ? 1.0614 0.8834 0.9186 0.1622  -0.0408 -0.0087 673 CYS C SG  
9811  N N   . ARG C 373 ? 0.7304 0.6395 0.6228 0.1839  -0.0322 -0.0192 674 ARG C N   
9812  C CA  . ARG C 373 ? 0.6834 0.6397 0.6014 0.1773  -0.0300 -0.0161 674 ARG C CA  
9813  C C   . ARG C 373 ? 0.7282 0.7212 0.6598 0.1796  -0.0242 -0.0206 674 ARG C C   
9814  O O   . ARG C 373 ? 0.6124 0.6470 0.5634 0.1764  -0.0224 -0.0188 674 ARG C O   
9815  C CB  . ARG C 373 ? 0.5929 0.5469 0.5197 0.1529  -0.0290 -0.0101 674 ARG C CB  
9816  C CG  . ARG C 373 ? 0.5807 0.5700 0.5272 0.1449  -0.0288 -0.0057 674 ARG C CG  
9817  C CD  . ARG C 373 ? 0.5673 0.5472 0.5182 0.1230  -0.0276 -0.0008 674 ARG C CD  
9818  N NE  . ARG C 373 ? 0.5666 0.5757 0.5332 0.1145  -0.0274 0.0027  674 ARG C NE  
9819  C CZ  . ARG C 373 ? 0.6064 0.6185 0.5807 0.0964  -0.0248 0.0059  674 ARG C CZ  
9820  N NH1 . ARG C 373 ? 0.6052 0.5965 0.5749 0.0860  -0.0222 0.0066  674 ARG C NH1 
9821  N NH2 . ARG C 373 ? 0.5913 0.6274 0.5770 0.0890  -0.0249 0.0082  674 ARG C NH2 
9822  N N   . GLY C 374 ? 0.7813 0.7603 0.7021 0.1837  -0.0213 -0.0266 675 GLY C N   
9823  C CA  . GLY C 374 ? 0.6357 0.6483 0.5675 0.1849  -0.0155 -0.0308 675 GLY C CA  
9824  C C   . GLY C 374 ? 0.6377 0.6627 0.5814 0.1621  -0.0111 -0.0275 675 GLY C C   
9825  O O   . GLY C 374 ? 0.5743 0.6342 0.5305 0.1596  -0.0062 -0.0287 675 GLY C O   
9826  N N   . GLY C 375 ? 0.5785 0.5772 0.5180 0.1458  -0.0125 -0.0232 676 GLY C N   
9827  C CA  . GLY C 375 ? 0.5485 0.5562 0.4974 0.1265  -0.0087 -0.0198 676 GLY C CA  
9828  C C   . GLY C 375 ? 0.6780 0.6675 0.6279 0.1110  -0.0109 -0.0136 676 GLY C C   
9829  O O   . GLY C 375 ? 0.6064 0.5788 0.5509 0.1133  -0.0152 -0.0114 676 GLY C O   
9830  N N   . CYS C 376 ? 0.6078 0.6016 0.5637 0.0957  -0.0078 -0.0105 677 CYS C N   
9831  C CA  . CYS C 376 ? 0.5682 0.5487 0.5260 0.0813  -0.0088 -0.0050 677 CYS C CA  
9832  C C   . CYS C 376 ? 0.5861 0.5825 0.5537 0.0686  -0.0046 -0.0014 677 CYS C C   
9833  O O   . CYS C 376 ? 0.5385 0.5334 0.5025 0.0660  -0.0025 -0.0028 677 CYS C O   
9834  C CB  . CYS C 376 ? 0.4354 0.3824 0.3780 0.0789  -0.0115 -0.0062 677 CYS C CB  
9835  S SG  . CYS C 376 ? 0.5154 0.4514 0.4606 0.0622  -0.0119 -0.0002 677 CYS C SG  
9836  N N   . PRO C 377 ? 0.5134 0.5237 0.4917 0.0607  -0.0036 0.0032  678 PRO C N   
9837  C CA  . PRO C 377 ? 0.4842 0.5043 0.4685 0.0492  0.0003  0.0072  678 PRO C CA  
9838  C C   . PRO C 377 ? 0.5454 0.5459 0.5248 0.0418  0.0000  0.0098  678 PRO C C   
9839  O O   . PRO C 377 ? 0.3896 0.3744 0.3664 0.0394  -0.0025 0.0112  678 PRO C O   
9840  C CB  . PRO C 377 ? 0.4916 0.5247 0.4847 0.0426  0.0007  0.0107  678 PRO C CB  
9841  C CG  . PRO C 377 ? 0.5557 0.5785 0.5466 0.0482  -0.0039 0.0098  678 PRO C CG  
9842  C CD  . PRO C 377 ? 0.5454 0.5632 0.5291 0.0623  -0.0059 0.0048  678 PRO C CD  
9843  N N   . ALA C 378 ? 0.5139 0.5182 0.4920 0.0383  0.0026  0.0106  679 ALA C N   
9844  C CA  . ALA C 378 ? 0.5503 0.5408 0.5241 0.0328  0.0020  0.0128  679 ALA C CA  
9845  C C   . ALA C 378 ? 0.5785 0.5785 0.5542 0.0274  0.0053  0.0169  679 ALA C C   
9846  O O   . ALA C 378 ? 0.5516 0.5645 0.5268 0.0290  0.0076  0.0157  679 ALA C O   
9847  C CB  . ALA C 378 ? 0.5543 0.5319 0.5181 0.0368  -0.0005 0.0079  679 ALA C CB  
9848  N N   . ASP C 379 ? 0.5054 0.4986 0.4821 0.0217  0.0054  0.0217  680 ASP C N   
9849  C CA  . ASP C 379 ? 0.5310 0.5285 0.5073 0.0176  0.0080  0.0269  680 ASP C CA  
9850  C C   . ASP C 379 ? 0.5330 0.5275 0.5046 0.0182  0.0065  0.0270  680 ASP C C   
9851  O O   . ASP C 379 ? 0.4818 0.4688 0.4533 0.0170  0.0047  0.0282  680 ASP C O   
9852  C CB  . ASP C 379 ? 0.4407 0.4314 0.4192 0.0130  0.0091  0.0318  680 ASP C CB  
9853  C CG  . ASP C 379 ? 0.5609 0.5514 0.5361 0.0097  0.0118  0.0378  680 ASP C CG  
9854  O OD1 . ASP C 379 ? 0.6705 0.6652 0.6420 0.0112  0.0120  0.0393  680 ASP C OD1 
9855  O OD2 . ASP C 379 ? 0.5991 0.5832 0.5735 0.0055  0.0135  0.0413  680 ASP C OD2 
9856  N N   . TRP C 380 ? 0.4961 0.4991 0.4637 0.0195  0.0073  0.0257  681 TRP C N   
9857  C CA  . TRP C 380 ? 0.4507 0.4534 0.4130 0.0194  0.0052  0.0247  681 TRP C CA  
9858  C C   . TRP C 380 ? 0.4124 0.4144 0.3758 0.0173  0.0047  0.0311  681 TRP C C   
9859  O O   . TRP C 380 ? 0.3712 0.3722 0.3336 0.0163  0.0021  0.0305  681 TRP C O   
9860  C CB  . TRP C 380 ? 0.3492 0.3625 0.3062 0.0208  0.0066  0.0227  681 TRP C CB  
9861  C CG  . TRP C 380 ? 0.4094 0.4231 0.3591 0.0203  0.0039  0.0195  681 TRP C CG  
9862  C CD1 . TRP C 380 ? 0.4630 0.4716 0.4055 0.0219  0.0022  0.0116  681 TRP C CD1 
9863  C CD2 . TRP C 380 ? 0.4654 0.4852 0.4128 0.0178  0.0025  0.0239  681 TRP C CD2 
9864  N NE1 . TRP C 380 ? 0.4571 0.4681 0.3928 0.0186  -0.0002 0.0103  681 TRP C NE1 
9865  C CE2 . TRP C 380 ? 0.4849 0.5052 0.4245 0.0163  -0.0002 0.0180  681 TRP C CE2 
9866  C CE3 . TRP C 380 ? 0.4708 0.4947 0.4205 0.0174  0.0031  0.0322  681 TRP C CE3 
9867  C CZ2 . TRP C 380 ? 0.5049 0.5342 0.4408 0.0134  -0.0028 0.0201  681 TRP C CZ2 
9868  C CZ3 . TRP C 380 ? 0.4185 0.4508 0.3646 0.0169  0.0006  0.0348  681 TRP C CZ3 
9869  C CH2 . TRP C 380 ? 0.4471 0.4842 0.3872 0.0144  -0.0024 0.0288  681 TRP C CH2 
9870  N N   . VAL C 381 ? 0.4043 0.4073 0.3685 0.0167  0.0074  0.0373  682 VAL C N   
9871  C CA  . VAL C 381 ? 0.4158 0.4159 0.3790 0.0175  0.0073  0.0438  682 VAL C CA  
9872  C C   . VAL C 381 ? 0.4765 0.4702 0.4438 0.0182  0.0056  0.0432  682 VAL C C   
9873  O O   . VAL C 381 ? 0.4960 0.4928 0.4631 0.0206  0.0044  0.0461  682 VAL C O   
9874  C CB  . VAL C 381 ? 0.4254 0.4203 0.3857 0.0161  0.0107  0.0499  682 VAL C CB  
9875  C CG1 . VAL C 381 ? 0.3255 0.3126 0.2823 0.0194  0.0106  0.0564  682 VAL C CG1 
9876  C CG2 . VAL C 381 ? 0.4316 0.4355 0.3869 0.0142  0.0127  0.0513  682 VAL C CG2 
9877  N N   . TRP C 382 ? 0.4827 0.4696 0.4534 0.0166  0.0056  0.0396  683 TRP C N   
9878  C CA  . TRP C 382 ? 0.4338 0.4147 0.4075 0.0164  0.0046  0.0391  683 TRP C CA  
9879  C C   . TRP C 382 ? 0.4706 0.4521 0.4442 0.0143  0.0017  0.0341  683 TRP C C   
9880  O O   . TRP C 382 ? 0.5251 0.5069 0.5002 0.0130  0.0007  0.0343  683 TRP C O   
9881  C CB  . TRP C 382 ? 0.4512 0.4230 0.4269 0.0150  0.0062  0.0389  683 TRP C CB  
9882  C CG  . TRP C 382 ? 0.5300 0.4952 0.5034 0.0153  0.0090  0.0440  683 TRP C CG  
9883  C CD1 . TRP C 382 ? 0.4965 0.4612 0.4655 0.0144  0.0111  0.0479  683 TRP C CD1 
9884  C CD2 . TRP C 382 ? 0.5305 0.4856 0.5029 0.0163  0.0101  0.0456  683 TRP C CD2 
9885  N NE1 . TRP C 382 ? 0.5291 0.4811 0.4932 0.0145  0.0132  0.0521  683 TRP C NE1 
9886  C CE2 . TRP C 382 ? 0.5779 0.5237 0.5441 0.0164  0.0126  0.0503  683 TRP C CE2 
9887  C CE3 . TRP C 382 ? 0.5754 0.5277 0.5502 0.0170  0.0094  0.0435  683 TRP C CE3 
9888  C CZ2 . TRP C 382 ? 0.6178 0.5493 0.5791 0.0180  0.0144  0.0522  683 TRP C CZ2 
9889  C CZ3 . TRP C 382 ? 0.6324 0.5742 0.6040 0.0189  0.0114  0.0453  683 TRP C CZ3 
9890  C CH2 . TRP C 382 ? 0.5456 0.4760 0.5101 0.0199  0.0139  0.0493  683 TRP C CH2 
9891  N N   . ILE C 383 ? 0.4651 0.4461 0.4354 0.0136  0.0004  0.0294  684 ILE C N   
9892  C CA  . ILE C 383 ? 0.4564 0.4316 0.4225 0.0108  -0.0025 0.0245  684 ILE C CA  
9893  C C   . ILE C 383 ? 0.5485 0.5318 0.5115 0.0073  -0.0045 0.0241  684 ILE C C   
9894  O O   . ILE C 383 ? 0.4832 0.4643 0.4438 0.0020  -0.0067 0.0223  684 ILE C O   
9895  C CB  . ILE C 383 ? 0.4273 0.3962 0.3887 0.0134  -0.0031 0.0192  684 ILE C CB  
9896  C CG1 . ILE C 383 ? 0.4320 0.3966 0.3972 0.0164  -0.0020 0.0195  684 ILE C CG1 
9897  C CG2 . ILE C 383 ? 0.3946 0.3524 0.3467 0.0103  -0.0063 0.0140  684 ILE C CG2 
9898  C CD1 . ILE C 383 ? 0.5651 0.5211 0.5318 0.0138  -0.0030 0.0207  684 ILE C CD1 
9899  N N   . VAL C 384 ? 0.5087 0.5028 0.4710 0.0092  -0.0040 0.0260  685 VAL C N   
9900  C CA  . VAL C 384 ? 0.4633 0.4686 0.4224 0.0058  -0.0065 0.0256  685 VAL C CA  
9901  C C   . VAL C 384 ? 0.4652 0.4810 0.4302 0.0056  -0.0069 0.0303  685 VAL C C   
9902  O O   . VAL C 384 ? 0.4979 0.5161 0.4673 0.0115  -0.0047 0.0359  685 VAL C O   
9903  C CB  . VAL C 384 ? 0.4137 0.4284 0.3695 0.0086  -0.0060 0.0270  685 VAL C CB  
9904  C CG1 . VAL C 384 ? 0.3214 0.3519 0.2754 0.0059  -0.0089 0.0283  685 VAL C CG1 
9905  C CG2 . VAL C 384 ? 0.4866 0.4945 0.4354 0.0089  -0.0056 0.0207  685 VAL C CG2 
9906  N N   . PRO C 385 ? 0.4432 0.4659 0.4075 -0.0008 -0.0095 0.0283  686 PRO C N   
9907  C CA  . PRO C 385 ? 0.4133 0.4490 0.3845 0.0000  -0.0092 0.0323  686 PRO C CA  
9908  C C   . PRO C 385 ? 0.5041 0.5582 0.4783 0.0068  -0.0095 0.0376  686 PRO C C   
9909  O O   . PRO C 385 ? 0.5359 0.5965 0.5059 0.0069  -0.0111 0.0376  686 PRO C O   
9910  C CB  . PRO C 385 ? 0.4284 0.4697 0.3967 -0.0113 -0.0120 0.0282  686 PRO C CB  
9911  C CG  . PRO C 385 ? 0.4659 0.4867 0.4241 -0.0168 -0.0132 0.0222  686 PRO C CG  
9912  C CD  . PRO C 385 ? 0.3466 0.3632 0.3024 -0.0098 -0.0123 0.0219  686 PRO C CD  
9913  N N   . PRO C 386 ? 0.5047 0.5669 0.4849 0.0136  -0.0080 0.0424  687 PRO C N   
9914  C CA  . PRO C 386 ? 0.4348 0.5107 0.4160 0.0232  -0.0083 0.0485  687 PRO C CA  
9915  C C   . PRO C 386 ? 0.4274 0.5319 0.4108 0.0215  -0.0121 0.0490  687 PRO C C   
9916  O O   . PRO C 386 ? 0.5175 0.6360 0.5017 0.0312  -0.0129 0.0546  687 PRO C O   
9917  C CB  . PRO C 386 ? 0.4233 0.4929 0.4080 0.0323  -0.0051 0.0523  687 PRO C CB  
9918  C CG  . PRO C 386 ? 0.4727 0.5428 0.4616 0.0251  -0.0045 0.0479  687 PRO C CG  
9919  C CD  . PRO C 386 ? 0.4230 0.4808 0.4077 0.0139  -0.0059 0.0423  687 PRO C CD  
9920  N N   . MET C 387 ? 0.4490 0.5624 0.4321 0.0091  -0.0146 0.0435  688 MET C N   
9921  C CA  . MET C 387 ? 0.4175 0.5574 0.4001 0.0038  -0.0189 0.0428  688 MET C CA  
9922  C C   . MET C 387 ? 0.5004 0.6300 0.4738 -0.0099 -0.0213 0.0356  688 MET C C   
9923  O O   . MET C 387 ? 0.4829 0.5884 0.4518 -0.0155 -0.0198 0.0312  688 MET C O   
9924  C CB  . MET C 387 ? 0.4268 0.5949 0.4174 0.0008  -0.0201 0.0433  688 MET C CB  
9925  C CG  . MET C 387 ? 0.5655 0.7288 0.5548 -0.0150 -0.0201 0.0375  688 MET C CG  
9926  S SD  . MET C 387 ? 0.6255 0.8266 0.6251 -0.0194 -0.0204 0.0386  688 MET C SD  
9927  C CE  . MET C 387 ? 0.6126 0.8466 0.6099 -0.0321 -0.0264 0.0363  688 MET C CE  
9928  N N   . SER C 388 ? 0.4184 0.5654 0.3874 -0.0142 -0.0251 0.0345  689 SER C N   
9929  C CA  . SER C 388 ? 0.4039 0.5431 0.3618 -0.0282 -0.0279 0.0268  689 SER C CA  
9930  C C   . SER C 388 ? 0.4172 0.5238 0.3664 -0.0268 -0.0255 0.0227  689 SER C C   
9931  O O   . SER C 388 ? 0.5109 0.5988 0.4506 -0.0362 -0.0262 0.0158  689 SER C O   
9932  C CB  . SER C 388 ? 0.4696 0.6125 0.4265 -0.0433 -0.0294 0.0224  689 SER C CB  
9933  O OG  . SER C 388 ? 0.5127 0.6919 0.4783 -0.0453 -0.0317 0.0257  689 SER C OG  
9934  N N   . GLY C 389 ? 0.3969 0.4967 0.3482 -0.0147 -0.0226 0.0271  690 GLY C N   
9935  C CA  . GLY C 389 ? 0.4099 0.4849 0.3557 -0.0118 -0.0198 0.0240  690 GLY C CA  
9936  C C   . GLY C 389 ? 0.5293 0.5921 0.4622 -0.0193 -0.0214 0.0154  690 GLY C C   
9937  O O   . GLY C 389 ? 0.4633 0.5045 0.3909 -0.0224 -0.0207 0.0101  690 GLY C O   
9938  N N   . SER C 390 ? 0.4945 0.5699 0.4203 -0.0216 -0.0238 0.0138  691 SER C N   
9939  C CA  . SER C 390 ? 0.4493 0.5105 0.3607 -0.0262 -0.0246 0.0051  691 SER C CA  
9940  C C   . SER C 390 ? 0.4657 0.5169 0.3667 -0.0399 -0.0280 -0.0026 691 SER C C   
9941  O O   . SER C 390 ? 0.5129 0.5444 0.3990 -0.0433 -0.0284 -0.0108 691 SER C O   
9942  C CB  . SER C 390 ? 0.4629 0.5399 0.3682 -0.0242 -0.0257 0.0055  691 SER C CB  
9943  O OG  . SER C 390 ? 0.4468 0.5474 0.3517 -0.0314 -0.0304 0.0067  691 SER C OG  
9944  N N   . ILE C 391 ? 0.5276 0.5903 0.4343 -0.0482 -0.0302 -0.0004 692 ILE C N   
9945  C CA  . ILE C 391 ? 0.6333 0.6819 0.5275 -0.0635 -0.0330 -0.0075 692 ILE C CA  
9946  C C   . ILE C 391 ? 0.5790 0.6007 0.4725 -0.0630 -0.0307 -0.0082 692 ILE C C   
9947  O O   . ILE C 391 ? 0.6197 0.6267 0.5027 -0.0759 -0.0326 -0.0123 692 ILE C O   
9948  C CB  . ILE C 391 ? 0.6502 0.7265 0.5473 -0.0772 -0.0370 -0.0063 692 ILE C CB  
9949  C CG1 . ILE C 391 ? 0.5604 0.6589 0.4762 -0.0723 -0.0355 0.0021  692 ILE C CG1 
9950  C CG2 . ILE C 391 ? 0.6411 0.7421 0.5340 -0.0803 -0.0407 -0.0074 692 ILE C CG2 
9951  C CD1 . ILE C 391 ? 0.4265 0.5530 0.3452 -0.0865 -0.0389 0.0024  692 ILE C CD1 
9952  N N   . THR C 392 ? 0.5969 0.6109 0.4998 -0.0492 -0.0268 -0.0041 693 THR C N   
9953  C CA  . THR C 392 ? 0.6425 0.6296 0.5424 -0.0473 -0.0250 -0.0056 693 THR C CA  
9954  C C   . THR C 392 ? 0.6179 0.5840 0.5093 -0.0374 -0.0233 -0.0103 693 THR C C   
9955  O O   . THR C 392 ? 0.6091 0.5863 0.5039 -0.0293 -0.0216 -0.0095 693 THR C O   
9956  C CB  . THR C 392 ? 0.5723 0.5661 0.4882 -0.0404 -0.0222 0.0017  693 THR C CB  
9957  O OG1 . THR C 392 ? 0.5588 0.5580 0.4838 -0.0271 -0.0191 0.0056  693 THR C OG1 
9958  C CG2 . THR C 392 ? 0.5798 0.6003 0.5063 -0.0462 -0.0231 0.0068  693 THR C CG2 
9959  N N   . PRO C 393 ? 0.6266 0.5634 0.5064 -0.0373 -0.0235 -0.0150 694 PRO C N   
9960  C CA  . PRO C 393 ? 0.6003 0.5193 0.4697 -0.0272 -0.0222 -0.0210 694 PRO C CA  
9961  C C   . PRO C 393 ? 0.5978 0.5274 0.4808 -0.0128 -0.0183 -0.0171 694 PRO C C   
9962  O O   . PRO C 393 ? 0.7306 0.6582 0.6086 -0.0042 -0.0165 -0.0213 694 PRO C O   
9963  C CB  . PRO C 393 ? 0.5628 0.4475 0.4167 -0.0293 -0.0238 -0.0254 694 PRO C CB  
9964  C CG  . PRO C 393 ? 0.4856 0.3739 0.3491 -0.0357 -0.0241 -0.0189 694 PRO C CG  
9965  C CD  . PRO C 393 ? 0.5592 0.4778 0.4336 -0.0453 -0.0248 -0.0148 694 PRO C CD  
9966  N N   . VAL C 394 ? 0.5692 0.5106 0.4683 -0.0104 -0.0166 -0.0096 695 VAL C N   
9967  C CA  . VAL C 394 ? 0.5290 0.4773 0.4388 0.0008  -0.0130 -0.0063 695 VAL C CA  
9968  C C   . VAL C 394 ? 0.4696 0.4396 0.3855 0.0038  -0.0109 -0.0032 695 VAL C C   
9969  O O   . VAL C 394 ? 0.4694 0.4450 0.3900 0.0116  -0.0077 -0.0021 695 VAL C O   
9970  C CB  . VAL C 394 ? 0.4663 0.4163 0.3885 0.0017  -0.0119 0.0000  695 VAL C CB  
9971  C CG1 . VAL C 394 ? 0.4856 0.4131 0.4005 0.0005  -0.0136 -0.0026 695 VAL C CG1 
9972  C CG2 . VAL C 394 ? 0.4211 0.3868 0.3517 -0.0046 -0.0123 0.0057  695 VAL C CG2 
9973  N N   . PHE C 395 ? 0.5694 0.5531 0.4850 -0.0025 -0.0127 -0.0013 696 PHE C N   
9974  C CA  . PHE C 395 ? 0.5646 0.5667 0.4824 0.0005  -0.0113 0.0019  696 PHE C CA  
9975  C C   . PHE C 395 ? 0.5563 0.5549 0.4643 0.0052  -0.0097 -0.0045 696 PHE C C   
9976  O O   . PHE C 395 ? 0.4299 0.4393 0.3416 0.0108  -0.0063 -0.0016 696 PHE C O   
9977  C CB  . PHE C 395 ? 0.5238 0.5414 0.4403 -0.0067 -0.0146 0.0038  696 PHE C CB  
9978  C CG  . PHE C 395 ? 0.5152 0.5511 0.4310 -0.0037 -0.0140 0.0073  696 PHE C CG  
9979  C CD1 . PHE C 395 ? 0.5453 0.5814 0.4494 -0.0038 -0.0141 0.0014  696 PHE C CD1 
9980  C CD2 . PHE C 395 ? 0.5063 0.5576 0.4311 -0.0003 -0.0136 0.0166  696 PHE C CD2 
9981  C CE1 . PHE C 395 ? 0.6653 0.7185 0.5675 -0.0016 -0.0136 0.0052  696 PHE C CE1 
9982  C CE2 . PHE C 395 ? 0.5919 0.6576 0.5137 0.0026  -0.0135 0.0209  696 PHE C CE2 
9983  C CZ  . PHE C 395 ? 0.6398 0.7074 0.5506 0.0013  -0.0135 0.0154  696 PHE C CZ  
9984  N N   . HIS C 396 ? 0.5504 0.5325 0.4446 0.0029  -0.0117 -0.0133 697 HIS C N   
9985  C CA  . HIS C 396 ? 0.5377 0.5138 0.4193 0.0081  -0.0103 -0.0214 697 HIS C CA  
9986  C C   . HIS C 396 ? 0.5496 0.5138 0.4311 0.0189  -0.0076 -0.0248 697 HIS C C   
9987  O O   . HIS C 396 ? 0.6269 0.5822 0.4960 0.0251  -0.0066 -0.0330 697 HIS C O   
9988  C CB  . HIS C 396 ? 0.5391 0.4997 0.4024 0.0000  -0.0142 -0.0298 697 HIS C CB  
9989  C CG  . HIS C 396 ? 0.5914 0.5669 0.4555 -0.0118 -0.0178 -0.0266 697 HIS C CG  
9990  N ND1 . HIS C 396 ? 0.5277 0.5215 0.3880 -0.0139 -0.0184 -0.0268 697 HIS C ND1 
9991  C CD2 . HIS C 396 ? 0.6078 0.5868 0.4773 -0.0215 -0.0208 -0.0226 697 HIS C CD2 
9992  C CE1 . HIS C 396 ? 0.5673 0.5754 0.4306 -0.0239 -0.0222 -0.0232 697 HIS C CE1 
9993  N NE2 . HIS C 396 ? 0.5975 0.5981 0.4669 -0.0286 -0.0235 -0.0208 697 HIS C NE2 
9994  N N   . GLN C 397 ? 0.5149 0.4799 0.4093 0.0219  -0.0064 -0.0191 698 GLN C N   
9995  C CA  . GLN C 397 ? 0.5338 0.4904 0.4294 0.0320  -0.0046 -0.0218 698 GLN C CA  
9996  C C   . GLN C 397 ? 0.5074 0.4857 0.4175 0.0369  -0.0004 -0.0161 698 GLN C C   
9997  O O   . GLN C 397 ? 0.6159 0.6023 0.5378 0.0325  0.0001  -0.0082 698 GLN C O   
9998  C CB  . GLN C 397 ? 0.4912 0.4289 0.3872 0.0300  -0.0074 -0.0205 698 GLN C CB  
9999  C CG  . GLN C 397 ? 0.4851 0.4173 0.3840 0.0409  -0.0062 -0.0216 698 GLN C CG  
10000 C CD  . GLN C 397 ? 0.5283 0.4419 0.4105 0.0506  -0.0070 -0.0307 698 GLN C CD  
10001 O OE1 . GLN C 397 ? 0.5411 0.4291 0.4066 0.0467  -0.0102 -0.0354 698 GLN C OE1 
10002 N NE2 . GLN C 397 ? 0.5549 0.4812 0.4401 0.0631  -0.0039 -0.0336 698 GLN C NE2 
10003 N N   . GLU C 398 ? 0.4523 0.4397 0.3604 0.0456  0.0028  -0.0204 699 GLU C N   
10004 C CA  . GLU C 398 ? 0.4572 0.4658 0.3779 0.0487  0.0070  -0.0156 699 GLU C CA  
10005 C C   . GLU C 398 ? 0.5672 0.5712 0.4969 0.0516  0.0062  -0.0133 699 GLU C C   
10006 O O   . GLU C 398 ? 0.5706 0.5574 0.4943 0.0573  0.0036  -0.0180 699 GLU C O   
10007 C CB  . GLU C 398 ? 0.4594 0.4824 0.3759 0.0574  0.0108  -0.0216 699 GLU C CB  
10008 C CG  . GLU C 398 ? 0.5841 0.6135 0.4906 0.0544  0.0119  -0.0240 699 GLU C CG  
10009 C CD  . GLU C 398 ? 0.6922 0.7393 0.5947 0.0630  0.0167  -0.0297 699 GLU C CD  
10010 O OE1 . GLU C 398 ? 0.5979 0.6578 0.4954 0.0593  0.0188  -0.0291 699 GLU C OE1 
10011 O OE2 . GLU C 398 ? 0.7739 0.8237 0.6780 0.0739  0.0182  -0.0345 699 GLU C OE2 
10012 N N   . MET C 399 ? 0.5428 0.5607 0.4849 0.0474  0.0083  -0.0061 700 MET C N   
10013 C CA  . MET C 399 ? 0.5182 0.5347 0.4689 0.0488  0.0076  -0.0037 700 MET C CA  
10014 C C   . MET C 399 ? 0.5934 0.6336 0.5539 0.0485  0.0117  -0.0006 700 MET C C   
10015 O O   . MET C 399 ? 0.7486 0.8021 0.7107 0.0428  0.0149  0.0034  700 MET C O   
10016 C CB  . MET C 399 ? 0.4426 0.4472 0.3971 0.0405  0.0053  0.0023  700 MET C CB  
10017 C CG  . MET C 399 ? 0.3937 0.3771 0.3395 0.0388  0.0013  -0.0004 700 MET C CG  
10018 S SD  . MET C 399 ? 0.4828 0.4630 0.4327 0.0285  0.0000  0.0065  700 MET C SD  
10019 C CE  . MET C 399 ? 0.4745 0.4364 0.4122 0.0249  -0.0043 0.0016  700 MET C CE  
10020 N N   . LEU C 400 ? 0.5174 0.5637 0.4835 0.0543  0.0113  -0.0023 701 LEU C N   
10021 C CA  . LEU C 400 ? 0.4262 0.4962 0.4027 0.0514  0.0144  0.0009  701 LEU C CA  
10022 C C   . LEU C 400 ? 0.5131 0.5761 0.4961 0.0437  0.0127  0.0065  701 LEU C C   
10023 O O   . LEU C 400 ? 0.5262 0.5731 0.5080 0.0467  0.0089  0.0055  701 LEU C O   
10024 C CB  . LEU C 400 ? 0.3606 0.4480 0.3397 0.0634  0.0150  -0.0049 701 LEU C CB  
10025 C CG  . LEU C 400 ? 0.5275 0.6288 0.5012 0.0722  0.0181  -0.0111 701 LEU C CG  
10026 C CD1 . LEU C 400 ? 0.5814 0.6981 0.5577 0.0875  0.0179  -0.0171 701 LEU C CD1 
10027 C CD2 . LEU C 400 ? 0.4883 0.6130 0.4660 0.0623  0.0234  -0.0069 701 LEU C CD2 
10028 N N   . ASN C 401 ? 0.5163 0.5895 0.5041 0.0332  0.0156  0.0123  702 ASN C N   
10029 C CA  . ASN C 401 ? 0.4895 0.5550 0.4815 0.0254  0.0145  0.0170  702 ASN C CA  
10030 C C   . ASN C 401 ? 0.5264 0.6146 0.5259 0.0212  0.0163  0.0176  702 ASN C C   
10031 O O   . ASN C 401 ? 0.4982 0.6065 0.4992 0.0165  0.0203  0.0187  702 ASN C O   
10032 C CB  . ASN C 401 ? 0.4642 0.5164 0.4524 0.0160  0.0158  0.0234  702 ASN C CB  
10033 C CG  . ASN C 401 ? 0.4598 0.4953 0.4489 0.0116  0.0137  0.0263  702 ASN C CG  
10034 O OD1 . ASN C 401 ? 0.4237 0.4554 0.4154 0.0153  0.0108  0.0235  702 ASN C OD1 
10035 N ND2 . ASN C 401 ? 0.4241 0.4492 0.4097 0.0047  0.0152  0.0318  702 ASN C ND2 
10036 N N   . TYR C 402 ? 0.4920 0.5788 0.4958 0.0222  0.0133  0.0168  703 TYR C N   
10037 C CA  . TYR C 402 ? 0.3303 0.4398 0.3416 0.0169  0.0140  0.0172  703 TYR C CA  
10038 C C   . TYR C 402 ? 0.4199 0.5155 0.4319 0.0136  0.0104  0.0185  703 TYR C C   
10039 O O   . TYR C 402 ? 0.4228 0.4946 0.4303 0.0176  0.0076  0.0184  703 TYR C O   
10040 C CB  . TYR C 402 ? 0.3861 0.5232 0.4029 0.0285  0.0139  0.0119  703 TYR C CB  
10041 C CG  . TYR C 402 ? 0.4611 0.5857 0.4737 0.0456  0.0102  0.0067  703 TYR C CG  
10042 C CD1 . TYR C 402 ? 0.4324 0.5463 0.4374 0.0532  0.0111  0.0035  703 TYR C CD1 
10043 C CD2 . TYR C 402 ? 0.4020 0.5241 0.4161 0.0538  0.0055  0.0049  703 TYR C CD2 
10044 C CE1 . TYR C 402 ? 0.4273 0.5252 0.4250 0.0675  0.0077  -0.0016 703 TYR C CE1 
10045 C CE2 . TYR C 402 ? 0.3705 0.4763 0.3772 0.0692  0.0020  0.0007  703 TYR C CE2 
10046 C CZ  . TYR C 402 ? 0.4849 0.5773 0.4828 0.0756  0.0033  -0.0028 703 TYR C CZ  
10047 O OH  . TYR C 402 ? 0.4488 0.5203 0.4359 0.0894  -0.0001 -0.0072 703 TYR C OH  
10048 N N   . ARG C 403 ? 0.4898 0.6016 0.5069 0.0047  0.0106  0.0198  704 ARG C N   
10049 C CA  . ARG C 403 ? 0.4818 0.5810 0.4979 -0.0021 0.0080  0.0213  704 ARG C CA  
10050 C C   . ARG C 403 ? 0.5259 0.6439 0.5484 0.0045  0.0039  0.0182  704 ARG C C   
10051 O O   . ARG C 403 ? 0.5407 0.6893 0.5701 0.0006  0.0046  0.0173  704 ARG C O   
10052 C CB  . ARG C 403 ? 0.4730 0.5710 0.4862 -0.0197 0.0111  0.0253  704 ARG C CB  
10053 C CG  . ARG C 403 ? 0.5389 0.6172 0.5439 -0.0254 0.0148  0.0295  704 ARG C CG  
10054 C CD  . ARG C 403 ? 0.7689 0.8151 0.7661 -0.0279 0.0140  0.0319  704 ARG C CD  
10055 N NE  . ARG C 403 ? 0.8712 0.9115 0.8658 -0.0381 0.0131  0.0321  704 ARG C NE  
10056 C CZ  . ARG C 403 ? 0.7834 0.8237 0.7726 -0.0531 0.0156  0.0345  704 ARG C CZ  
10057 N NH1 . ARG C 403 ? 0.7707 0.8175 0.7567 -0.0599 0.0194  0.0376  704 ARG C NH1 
10058 N NH2 . ARG C 403 ? 0.7535 0.7864 0.7388 -0.0622 0.0144  0.0337  704 ARG C NH2 
10059 N N   . LEU C 404 ? 0.6020 0.7030 0.6215 0.0141  -0.0004 0.0169  705 LEU C N   
10060 C CA  . LEU C 404 ? 0.5328 0.6455 0.5556 0.0220  -0.0052 0.0149  705 LEU C CA  
10061 C C   . LEU C 404 ? 0.5505 0.6517 0.5708 0.0124  -0.0076 0.0168  705 LEU C C   
10062 O O   . LEU C 404 ? 0.5220 0.5980 0.5361 0.0050  -0.0062 0.0189  705 LEU C O   
10063 C CB  . LEU C 404 ? 0.4486 0.5462 0.4660 0.0391  -0.0086 0.0125  705 LEU C CB  
10064 C CG  . LEU C 404 ? 0.5726 0.6761 0.5890 0.0511  -0.0068 0.0092  705 LEU C CG  
10065 C CD1 . LEU C 404 ? 0.4604 0.5435 0.4678 0.0672  -0.0110 0.0067  705 LEU C CD1 
10066 C CD2 . LEU C 404 ? 0.3044 0.4478 0.3305 0.0541  -0.0049 0.0071  705 LEU C CD2 
10067 N N   . THR C 405 ? 0.5543 0.6760 0.5791 0.0133  -0.0113 0.0159  706 THR C N   
10068 C CA  . THR C 405 ? 0.5236 0.6353 0.5448 0.0056  -0.0142 0.0170  706 THR C CA  
10069 C C   . THR C 405 ? 0.5251 0.6335 0.5438 0.0194  -0.0202 0.0164  706 THR C C   
10070 O O   . THR C 405 ? 0.4751 0.5990 0.4970 0.0340  -0.0225 0.0148  706 THR C O   
10071 C CB  . THR C 405 ? 0.5822 0.7196 0.6083 -0.0092 -0.0140 0.0168  706 THR C CB  
10072 O OG1 . THR C 405 ? 0.6437 0.7643 0.6632 -0.0197 -0.0155 0.0175  706 THR C OG1 
10073 C CG2 . THR C 405 ? 0.5209 0.6971 0.5563 -0.0010 -0.0179 0.0149  706 THR C CG2 
10074 N N   . PRO C 406 ? 0.4998 0.5858 0.5109 0.0165  -0.0226 0.0177  707 PRO C N   
10075 C CA  . PRO C 406 ? 0.4622 0.5252 0.4669 0.0034  -0.0201 0.0190  707 PRO C CA  
10076 C C   . PRO C 406 ? 0.4913 0.5316 0.4925 0.0015  -0.0153 0.0200  707 PRO C C   
10077 O O   . PRO C 406 ? 0.4847 0.5201 0.4858 0.0112  -0.0149 0.0197  707 PRO C O   
10078 C CB  . PRO C 406 ? 0.5465 0.5936 0.5436 0.0081  -0.0245 0.0198  707 PRO C CB  
10079 C CG  . PRO C 406 ? 0.5739 0.6422 0.5741 0.0194  -0.0301 0.0194  707 PRO C CG  
10080 C CD  . PRO C 406 ? 0.4788 0.5630 0.4859 0.0290  -0.0286 0.0180  707 PRO C CD  
10081 N N   . SER C 407 ? 0.3454 0.3716 0.3424 -0.0101 -0.0119 0.0209  708 SER C N   
10082 C CA  . SER C 407 ? 0.4946 0.5024 0.4883 -0.0110 -0.0077 0.0223  708 SER C CA  
10083 C C   . SER C 407 ? 0.4640 0.4504 0.4501 -0.0182 -0.0057 0.0230  708 SER C C   
10084 O O   . SER C 407 ? 0.5061 0.4918 0.4887 -0.0257 -0.0066 0.0220  708 SER C O   
10085 C CB  . SER C 407 ? 0.6497 0.6683 0.6469 -0.0161 -0.0038 0.0231  708 SER C CB  
10086 O OG  . SER C 407 ? 0.7582 0.7826 0.7539 -0.0295 -0.0024 0.0233  708 SER C OG  
10087 N N   . PHE C 408 ? 0.5147 0.4849 0.4978 -0.0152 -0.0030 0.0244  709 PHE C N   
10088 C CA  . PHE C 408 ? 0.4008 0.3527 0.3770 -0.0200 0.0003  0.0252  709 PHE C CA  
10089 C C   . PHE C 408 ? 0.5447 0.4944 0.5190 -0.0255 0.0040  0.0271  709 PHE C C   
10090 O O   . PHE C 408 ? 0.5999 0.5581 0.5784 -0.0227 0.0050  0.0284  709 PHE C O   
10091 C CB  . PHE C 408 ? 0.3181 0.2580 0.2924 -0.0131 0.0009  0.0261  709 PHE C CB  
10092 C CG  . PHE C 408 ? 0.4954 0.4332 0.4681 -0.0100 -0.0022 0.0250  709 PHE C CG  
10093 C CD1 . PHE C 408 ? 0.4479 0.3788 0.4150 -0.0141 -0.0023 0.0239  709 PHE C CD1 
10094 C CD2 . PHE C 408 ? 0.5078 0.4483 0.4823 -0.0036 -0.0050 0.0252  709 PHE C CD2 
10095 C CE1 . PHE C 408 ? 0.4310 0.3598 0.3951 -0.0119 -0.0051 0.0237  709 PHE C CE1 
10096 C CE2 . PHE C 408 ? 0.3980 0.3333 0.3682 -0.0017 -0.0079 0.0251  709 PHE C CE2 
10097 C CZ  . PHE C 408 ? 0.4548 0.3853 0.4202 -0.0060 -0.0080 0.0247  709 PHE C CZ  
10098 N N   . GLU C 409 ? 0.5538 0.4901 0.5198 -0.0336 0.0063  0.0271  710 GLU C N   
10099 C CA  . GLU C 409 ? 0.4939 0.4227 0.4540 -0.0405 0.0097  0.0294  710 GLU C CA  
10100 C C   . GLU C 409 ? 0.5524 0.4547 0.5011 -0.0389 0.0128  0.0306  710 GLU C C   
10101 O O   . GLU C 409 ? 0.5757 0.4675 0.5204 -0.0360 0.0126  0.0284  710 GLU C O   
10102 C CB  . GLU C 409 ? 0.5482 0.4850 0.5056 -0.0544 0.0095  0.0283  710 GLU C CB  
10103 C CG  . GLU C 409 ? 0.6351 0.6032 0.6043 -0.0552 0.0064  0.0269  710 GLU C CG  
10104 C CD  . GLU C 409 ? 0.7497 0.7343 0.7264 -0.0509 0.0077  0.0289  710 GLU C CD  
10105 O OE1 . GLU C 409 ? 0.8588 0.8310 0.8307 -0.0504 0.0110  0.0320  710 GLU C OE1 
10106 O OE2 . GLU C 409 ? 0.6049 0.6153 0.5915 -0.0473 0.0054  0.0273  710 GLU C OE2 
10107 N N   . TYR C 410 ? 0.5560 0.4476 0.4983 -0.0403 0.0158  0.0341  711 TYR C N   
10108 C CA  . TYR C 410 ? 0.5459 0.4099 0.4743 -0.0386 0.0187  0.0353  711 TYR C CA  
10109 C C   . TYR C 410 ? 0.5242 0.3724 0.4396 -0.0514 0.0196  0.0330  711 TYR C C   
10110 O O   . TYR C 410 ? 0.5096 0.3707 0.4271 -0.0635 0.0183  0.0318  711 TYR C O   
10111 C CB  . TYR C 410 ? 0.6662 0.5205 0.5888 -0.0352 0.0213  0.0406  711 TYR C CB  
10112 C CG  . TYR C 410 ? 0.7682 0.6381 0.7018 -0.0243 0.0203  0.0426  711 TYR C CG  
10113 C CD1 . TYR C 410 ? 0.8353 0.7074 0.7738 -0.0135 0.0194  0.0413  711 TYR C CD1 
10114 C CD2 . TYR C 410 ? 0.9224 0.8060 0.8605 -0.0260 0.0203  0.0455  711 TYR C CD2 
10115 C CE1 . TYR C 410 ? 0.9365 0.8227 0.8836 -0.0059 0.0182  0.0427  711 TYR C CE1 
10116 C CE2 . TYR C 410 ? 1.0131 0.9098 0.9594 -0.0170 0.0192  0.0466  711 TYR C CE2 
10117 C CZ  . TYR C 410 ? 1.0020 0.8994 0.9525 -0.0075 0.0179  0.0451  711 TYR C CZ  
10118 O OH  . TYR C 410 ? 0.9774 0.8876 0.9347 -0.0007 0.0166  0.0457  711 TYR C OH  
10119 N N   . GLN C 411 ? 0.5660 0.3871 0.4673 -0.0484 0.0218  0.0320  712 GLN C N   
10120 C CA  . GLN C 411 ? 0.5636 0.3625 0.4481 -0.0601 0.0230  0.0291  712 GLN C CA  
10121 C C   . GLN C 411 ? 0.6609 0.4249 0.5271 -0.0525 0.0266  0.0306  712 GLN C C   
10122 O O   . GLN C 411 ? 0.5957 0.3593 0.4657 -0.0367 0.0276  0.0322  712 GLN C O   
10123 C CB  . GLN C 411 ? 0.6226 0.4284 0.5092 -0.0635 0.0207  0.0231  712 GLN C CB  
10124 C CG  . GLN C 411 ? 0.5769 0.3755 0.4627 -0.0504 0.0214  0.0204  712 GLN C CG  
10125 C CD  . GLN C 411 ? 0.6093 0.4175 0.4970 -0.0548 0.0188  0.0152  712 GLN C CD  
10126 O OE1 . GLN C 411 ? 0.7316 0.5366 0.6116 -0.0681 0.0175  0.0119  712 GLN C OE1 
10127 N NE2 . GLN C 411 ? 0.5717 0.3924 0.4689 -0.0445 0.0178  0.0146  712 GLN C NE2 
10128 N N   . PRO C 412 ? 0.7579 0.4924 0.6032 -0.0631 0.0286  0.0303  713 PRO C N   
10129 C CA  . PRO C 412 ? 0.8156 0.5127 0.6404 -0.0537 0.0320  0.0320  713 PRO C CA  
10130 C C   . PRO C 412 ? 0.7922 0.4790 0.6129 -0.0411 0.0331  0.0266  713 PRO C C   
10131 O O   . PRO C 412 ? 0.7551 0.4528 0.5806 -0.0460 0.0316  0.0209  713 PRO C O   
10132 C CB  . PRO C 412 ? 0.8565 0.5228 0.6577 -0.0717 0.0335  0.0322  713 PRO C CB  
10133 C CG  . PRO C 412 ? 0.7841 0.4734 0.5936 -0.0906 0.0307  0.0278  713 PRO C CG  
10134 C CD  . PRO C 412 ? 0.7420 0.4762 0.5802 -0.0847 0.0278  0.0286  713 PRO C CD  
10135 N N   . ASP C 413 ? 0.8540 0.5225 0.6661 -0.0238 0.0357  0.0288  714 ASP C N   
10136 C CA  . ASP C 413 ? 0.9585 0.6166 0.7645 -0.0102 0.0378  0.0236  714 ASP C CA  
10137 C C   . ASP C 413 ? 0.9628 0.5904 0.7466 -0.0210 0.0391  0.0170  714 ASP C C   
10138 O O   . ASP C 413 ? 1.0166 0.6120 0.7791 -0.0314 0.0402  0.0181  714 ASP C O   
10139 C CB  . ASP C 413 ? 1.0716 0.7126 0.8684 0.0103  0.0405  0.0274  714 ASP C CB  
10140 C CG  . ASP C 413 ? 1.0762 0.7479 0.8935 0.0208  0.0389  0.0334  714 ASP C CG  
10141 O OD1 . ASP C 413 ? 1.0596 0.7665 0.8991 0.0189  0.0366  0.0322  714 ASP C OD1 
10142 O OD2 . ASP C 413 ? 1.1015 0.7605 0.9108 0.0309  0.0398  0.0393  714 ASP C OD2 
10143 N N   . PRO C 414 ? 0.9250 0.5600 0.7111 -0.0197 0.0392  0.0101  715 PRO C N   
10144 C CA  . PRO C 414 ? 0.8383 0.4473 0.6036 -0.0326 0.0399  0.0030  715 PRO C CA  
10145 C C   . PRO C 414 ? 0.9226 0.4815 0.6563 -0.0262 0.0440  0.0010  715 PRO C C   
10146 O O   . PRO C 414 ? 0.9893 0.5184 0.7006 -0.0417 0.0443  -0.0033 715 PRO C O   
10147 C CB  . PRO C 414 ? 0.7717 0.4024 0.5472 -0.0286 0.0393  -0.0031 715 PRO C CB  
10148 C CG  . PRO C 414 ? 0.8142 0.4685 0.6075 -0.0093 0.0403  0.0001  715 PRO C CG  
10149 C CD  . PRO C 414 ? 0.8625 0.5289 0.6682 -0.0075 0.0388  0.0085  715 PRO C CD  
10150 N N   . TRP C 415 ? 0.9791 0.5267 0.7086 -0.0042 0.0469  0.0039  716 TRP C N   
10151 C CA  . TRP C 415 ? 1.0587 0.5551 0.7553 0.0041  0.0507  0.0016  716 TRP C CA  
10152 C C   . TRP C 415 ? 1.1630 0.6250 0.8395 -0.0069 0.0505  0.0077  716 TRP C C   
10153 O O   . TRP C 415 ? 1.1980 0.6098 0.8420 -0.0040 0.0532  0.0059  716 TRP C O   
10154 C CB  . TRP C 415 ? 1.0238 0.5203 0.7211 0.0335  0.0538  0.0026  716 TRP C CB  
10155 C CG  . TRP C 415 ? 1.0541 0.5773 0.7714 0.0442  0.0522  0.0118  716 TRP C CG  
10156 C CD1 . TRP C 415 ? 1.1167 0.6199 0.8236 0.0486  0.0521  0.0199  716 TRP C CD1 
10157 C CD2 . TRP C 415 ? 1.0309 0.6049 0.7804 0.0507  0.0504  0.0140  716 TRP C CD2 
10158 N NE1 . TRP C 415 ? 1.0420 0.5828 0.7736 0.0579  0.0501  0.0265  716 TRP C NE1 
10159 C CE2 . TRP C 415 ? 1.0380 0.6216 0.7956 0.0589  0.0491  0.0228  716 TRP C CE2 
10160 C CE3 . TRP C 415 ? 0.9934 0.6039 0.7637 0.0495  0.0496  0.0096  716 TRP C CE3 
10161 C CZ2 . TRP C 415 ? 1.0342 0.6623 0.8197 0.0652  0.0470  0.0265  716 TRP C CZ2 
10162 C CZ3 . TRP C 415 ? 0.9798 0.6320 0.7767 0.0556  0.0477  0.0138  716 TRP C CZ3 
10163 C CH2 . TRP C 415 ? 1.0135 0.6742 0.8178 0.0630  0.0464  0.0217  716 TRP C CH2 
10164 N N   . ASN C 416 ? 1.2100 0.6962 0.9030 -0.0192 0.0476  0.0147  717 ASN C N   
10165 C CA  . ASN C 416 ? 1.2067 0.6643 0.8809 -0.0349 0.0475  0.0204  717 ASN C CA  
10166 C C   . ASN C 416 ? 1.3175 0.7630 0.9787 -0.0636 0.0464  0.0153  717 ASN C C   
10167 O O   . ASN C 416 ? 1.4043 0.8181 1.0429 -0.0797 0.0470  0.0186  717 ASN C O   
10168 C CB  . ASN C 416 ? 1.0582 0.5493 0.7548 -0.0373 0.0453  0.0294  717 ASN C CB  
10169 C CG  . ASN C 416 ? 1.0743 0.5818 0.7847 -0.0114 0.0456  0.0345  717 ASN C CG  
10170 O OD1 . ASN C 416 ? 1.1194 0.6013 0.8146 0.0087  0.0480  0.0343  717 ASN C OD1 
10171 N ND2 . ASN C 416 ? 1.0674 0.6187 0.8061 -0.0112 0.0431  0.0388  717 ASN C ND2 
10172 N N   . THR C 417 ? 1.2953 0.7658 0.9693 -0.0710 0.0447  0.0077  718 THR C N   
10173 C CA  . THR C 417 ? 1.2988 0.7721 0.9675 -0.0990 0.0424  0.0031  718 THR C CA  
10174 C C   . THR C 417 ? 1.3627 0.8203 1.0167 -0.1033 0.0428  -0.0076 718 THR C C   
10175 O O   . THR C 417 ? 1.4481 0.8968 1.0890 -0.1276 0.0412  -0.0120 718 THR C O   
10176 C CB  . THR C 417 ? 1.2009 0.7321 0.9041 -0.1085 0.0383  0.0056  718 THR C CB  
10177 O OG1 . THR C 417 ? 1.1389 0.7041 0.8682 -0.0882 0.0375  0.0058  718 THR C OG1 
10178 C CG2 . THR C 417 ? 1.1434 0.6846 0.8529 -0.1164 0.0379  0.0146  718 THR C CG2 
10179 N N   . HIS C 418 ? 1.3240 0.7789 0.9787 -0.0816 0.0449  -0.0122 719 HIS C N   
10180 C CA  . HIS C 418 ? 1.3340 0.7807 0.9774 -0.0848 0.0453  -0.0227 719 HIS C CA  
10181 C C   . HIS C 418 ? 1.3626 0.7466 0.9643 -0.0841 0.0492  -0.0285 719 HIS C C   
10182 O O   . HIS C 418 ? 1.3040 0.6578 0.8915 -0.0630 0.0529  -0.0264 719 HIS C O   
10183 C CB  . HIS C 418 ? 1.2386 0.7161 0.9029 -0.0629 0.0461  -0.0250 719 HIS C CB  
10184 C CG  . HIS C 418 ? 1.1918 0.6554 0.8404 -0.0611 0.0479  -0.0356 719 HIS C CG  
10185 N ND1 . HIS C 418 ? 1.1668 0.6513 0.8206 -0.0780 0.0445  -0.0413 719 HIS C ND1 
10186 C CD2 . HIS C 418 ? 1.2241 0.6556 0.8510 -0.0437 0.0528  -0.0418 719 HIS C CD2 
10187 C CE1 . HIS C 418 ? 1.2216 0.6869 0.8571 -0.0723 0.0473  -0.0505 719 HIS C CE1 
10188 N NE2 . HIS C 418 ? 1.2208 0.6538 0.8398 -0.0513 0.0526  -0.0513 719 HIS C NE2 
10189 N N   . VAL C 419 ? 1.4446 0.8088 1.0257 -0.1069 0.0480  -0.0361 720 VAL C N   
10190 C CA  . VAL C 419 ? 1.5338 0.8485 1.0784 -0.1069 0.0508  -0.0426 720 VAL C CA  
10191 C C   . VAL C 419 ? 1.6061 0.9171 1.1443 -0.0950 0.0530  -0.0534 720 VAL C C   
10192 O O   . VAL C 419 ? 1.6473 0.9787 1.1916 -0.1099 0.0504  -0.0599 720 VAL C O   
10193 C CB  . VAL C 419 ? 1.5125 0.8189 1.0418 -0.1379 0.0479  -0.0439 720 VAL C CB  
10194 C CG1 . VAL C 419 ? 1.5176 0.8031 1.0351 -0.1415 0.0485  -0.0351 720 VAL C CG1 
10195 C CG2 . VAL C 419 ? 1.4470 0.7964 0.9989 -0.1625 0.0430  -0.0442 720 VAL C CG2 
10196 N N   . TRP C 420 ? 1.6204 0.9086 1.1464 -0.0676 0.0576  -0.0552 721 TRP C N   
10197 C CA  . TRP C 420 ? 1.6168 0.9059 1.1389 -0.0520 0.0608  -0.0650 721 TRP C CA  
10198 C C   . TRP C 420 ? 1.6792 0.9493 1.1776 -0.0683 0.0603  -0.0752 721 TRP C C   
10199 O O   . TRP C 420 ? 1.7411 0.9852 1.2187 -0.0842 0.0590  -0.0749 721 TRP C O   
10200 C CB  . TRP C 420 ? 1.6295 0.9021 1.1444 -0.0181 0.0660  -0.0641 721 TRP C CB  
10201 C CG  . TRP C 420 ? 1.5861 0.8853 1.1268 0.0016  0.0668  -0.0558 721 TRP C CG  
10202 C CD1 . TRP C 420 ? 1.5590 0.8631 1.1106 0.0013  0.0648  -0.0444 721 TRP C CD1 
10203 C CD2 . TRP C 420 ? 1.5021 0.8449 1.0690 0.0234  0.0687  -0.0561 721 TRP C CD2 
10204 N NE1 . TRP C 420 ? 1.4674 0.8152 1.0504 0.0216  0.0650  -0.0381 721 TRP C NE1 
10205 C CE2 . TRP C 420 ? 1.4639 0.8360 1.0567 0.0348  0.0673  -0.0450 721 TRP C CE2 
10206 C CE3 . TRP C 420 ? 1.4172 0.7778 0.9871 0.0331  0.0715  -0.0647 721 TRP C CE3 
10207 C CZ2 . TRP C 420 ? 1.4118 0.8295 1.0329 0.0542  0.0684  -0.0425 721 TRP C CZ2 
10208 C CZ3 . TRP C 420 ? 1.4194 0.8259 1.0178 0.0524  0.0729  -0.0616 721 TRP C CZ3 
10209 C CH2 . TRP C 420 ? 1.4320 0.8664 1.0555 0.0621  0.0713  -0.0507 721 TRP C CH2 
10210 N N   . LYS C 421 ? 1.6729 0.9566 1.1732 -0.0646 0.0614  -0.0845 722 LYS C N   
10211 C CA  . LYS C 421 ? 1.6708 0.9383 1.1485 -0.0774 0.0612  -0.0948 722 LYS C CA  
10212 C C   . LYS C 421 ? 1.6489 0.8848 1.1038 -0.0525 0.0672  -0.1006 722 LYS C C   
10213 O O   . LYS C 421 ? 1.6348 0.8343 1.0623 -0.0571 0.0680  -0.1033 722 LYS C O   
10214 C CB  . LYS C 421 ? 1.6605 0.9611 1.1506 -0.0884 0.0588  -0.1019 722 LYS C CB  
10215 C CG  . LYS C 421 ? 1.6191 0.9722 1.1458 -0.1016 0.0528  -0.0932 722 LYS C CG  
10216 C CD  . LYS C 421 ? 1.5840 0.9413 1.1063 -0.1357 0.0467  -0.0940 722 LYS C CD  
10217 C CE  . LYS C 421 ? 1.4828 0.9048 1.0432 -0.1440 0.0404  -0.0884 722 LYS C CE  
10218 N NZ  . LYS C 421 ? 1.4364 0.8748 1.0057 -0.1695 0.0348  -0.0830 722 LYS C NZ  
10219 N N   . ARG D 3   ? 1.1258 1.1682 1.0851 -0.1995 -0.0218 -0.0505 304 ARG D N   
10220 C CA  . ARG D 3   ? 1.2135 1.2372 1.1627 -0.1940 -0.0226 -0.0538 304 ARG D CA  
10221 C C   . ARG D 3   ? 1.1774 1.1781 1.1256 -0.1756 -0.0218 -0.0479 304 ARG D C   
10222 O O   . ARG D 3   ? 1.1976 1.1831 1.1456 -0.1710 -0.0192 -0.0430 304 ARG D O   
10223 C CB  . ARG D 3   ? 1.3061 1.3610 1.2636 -0.1920 -0.0281 -0.0559 304 ARG D CB  
10224 C CG  . ARG D 3   ? 1.2946 1.3781 1.2702 -0.1767 -0.0328 -0.0484 304 ARG D CG  
10225 C CD  . ARG D 3   ? 1.3162 1.4323 1.3054 -0.1819 -0.0344 -0.0468 304 ARG D CD  
10226 N NE  . ARG D 3   ? 1.3388 1.4774 1.3435 -0.1660 -0.0387 -0.0395 304 ARG D NE  
10227 C CZ  . ARG D 3   ? 1.3624 1.4891 1.3716 -0.1528 -0.0375 -0.0326 304 ARG D CZ  
10228 N NH1 . ARG D 3   ? 1.4244 1.5189 1.4244 -0.1530 -0.0327 -0.0318 304 ARG D NH1 
10229 N NH2 . ARG D 3   ? 1.3021 1.4478 1.3237 -0.1393 -0.0414 -0.0265 304 ARG D NH2 
10230 N N   . PHE D 4   ? 1.0949 1.0946 1.0422 -0.1659 -0.0241 -0.0488 305 PHE D N   
10231 C CA  . PHE D 4   ? 0.9825 0.9619 0.9277 -0.1499 -0.0232 -0.0448 305 PHE D CA  
10232 C C   . PHE D 4   ? 0.8288 0.8307 0.7851 -0.1379 -0.0277 -0.0413 305 PHE D C   
10233 O O   . PHE D 4   ? 0.8289 0.8557 0.7900 -0.1422 -0.0313 -0.0433 305 PHE D O   
10234 C CB  . PHE D 4   ? 1.1062 1.0518 1.0328 -0.1513 -0.0198 -0.0511 305 PHE D CB  
10235 C CG  . PHE D 4   ? 1.2928 1.2103 1.2046 -0.1634 -0.0154 -0.0544 305 PHE D CG  
10236 C CD1 . PHE D 4   ? 1.3832 1.3021 1.2866 -0.1822 -0.0144 -0.0615 305 PHE D CD1 
10237 C CD2 . PHE D 4   ? 1.3114 1.2004 1.2163 -0.1566 -0.0122 -0.0505 305 PHE D CD2 
10238 C CE1 . PHE D 4   ? 1.3917 1.2821 1.2792 -0.1948 -0.0100 -0.0643 305 PHE D CE1 
10239 C CE2 . PHE D 4   ? 1.2963 1.1565 1.1852 -0.1678 -0.0082 -0.0528 305 PHE D CE2 
10240 C CZ  . PHE D 4   ? 1.3274 1.1872 1.2071 -0.1873 -0.0069 -0.0597 305 PHE D CZ  
10241 N N   . LEU D 5   ? 0.6643 0.6577 0.6240 -0.1233 -0.0276 -0.0357 306 LEU D N   
10242 C CA  . LEU D 5   ? 0.4976 0.5060 0.4643 -0.1124 -0.0310 -0.0324 306 LEU D CA  
10243 C C   . LEU D 5   ? 0.5712 0.5583 0.5315 -0.1018 -0.0287 -0.0321 306 LEU D C   
10244 O O   . LEU D 5   ? 0.7004 0.6680 0.6581 -0.0972 -0.0259 -0.0299 306 LEU D O   
10245 C CB  . LEU D 5   ? 0.4179 0.4469 0.3993 -0.1048 -0.0342 -0.0243 306 LEU D CB  
10246 C CG  . LEU D 5   ? 0.5019 0.5585 0.4917 -0.1121 -0.0374 -0.0244 306 LEU D CG  
10247 C CD1 . LEU D 5   ? 0.4962 0.5670 0.4988 -0.1034 -0.0396 -0.0169 306 LEU D CD1 
10248 C CD2 . LEU D 5   ? 0.6441 0.7195 0.6333 -0.1142 -0.0414 -0.0272 306 LEU D CD2 
10249 N N   . LYS D 6   ? 0.5969 0.5892 0.5547 -0.0979 -0.0299 -0.0343 307 LYS D N   
10250 C CA  . LYS D 6   ? 0.5970 0.5731 0.5490 -0.0881 -0.0275 -0.0352 307 LYS D CA  
10251 C C   . LYS D 6   ? 0.5630 0.5538 0.5245 -0.0774 -0.0299 -0.0285 307 LYS D C   
10252 O O   . LYS D 6   ? 0.5777 0.5901 0.5461 -0.0783 -0.0337 -0.0251 307 LYS D O   
10253 C CB  . LYS D 6   ? 0.6539 0.6219 0.5934 -0.0920 -0.0260 -0.0441 307 LYS D CB  
10254 C CG  . LYS D 6   ? 0.6998 0.6476 0.6271 -0.1029 -0.0231 -0.0511 307 LYS D CG  
10255 C CD  . LYS D 6   ? 0.8989 0.8291 0.8113 -0.1032 -0.0204 -0.0600 307 LYS D CD  
10256 C CE  . LYS D 6   ? 1.0405 0.9416 0.9381 -0.1120 -0.0169 -0.0661 307 LYS D CE  
10257 N NZ  . LYS D 6   ? 1.1209 1.0184 1.0060 -0.1234 -0.0163 -0.0760 307 LYS D NZ  
10258 N N   . VAL D 7   ? 0.5605 0.5391 0.5217 -0.0676 -0.0278 -0.0263 308 VAL D N   
10259 C CA  . VAL D 7   ? 0.5392 0.5286 0.5066 -0.0584 -0.0291 -0.0212 308 VAL D CA  
10260 C C   . VAL D 7   ? 0.5084 0.4883 0.4681 -0.0527 -0.0261 -0.0263 308 VAL D C   
10261 O O   . VAL D 7   ? 0.5837 0.5438 0.5355 -0.0509 -0.0230 -0.0310 308 VAL D O   
10262 C CB  . VAL D 7   ? 0.5251 0.5133 0.5011 -0.0517 -0.0295 -0.0136 308 VAL D CB  
10263 C CG1 . VAL D 7   ? 0.4746 0.4755 0.4587 -0.0558 -0.0324 -0.0089 308 VAL D CG1 
10264 C CG2 . VAL D 7   ? 0.5474 0.5136 0.5187 -0.0483 -0.0261 -0.0148 308 VAL D CG2 
10265 N N   . LYS D 8   ? 0.5557 0.5499 0.5169 -0.0496 -0.0271 -0.0254 309 LYS D N   
10266 C CA  . LYS D 8   ? 0.4366 0.4272 0.3915 -0.0441 -0.0242 -0.0306 309 LYS D CA  
10267 C C   . LYS D 8   ? 0.4927 0.4919 0.4543 -0.0357 -0.0240 -0.0252 309 LYS D C   
10268 O O   . LYS D 8   ? 0.6145 0.6268 0.5832 -0.0363 -0.0268 -0.0181 309 LYS D O   
10269 C CB  . LYS D 8   ? 0.5630 0.5645 0.5116 -0.0500 -0.0248 -0.0359 309 LYS D CB  
10270 C CG  . LYS D 8   ? 0.5368 0.5408 0.4798 -0.0446 -0.0218 -0.0411 309 LYS D CG  
10271 C CD  . LYS D 8   ? 0.5538 0.5655 0.4885 -0.0520 -0.0223 -0.0474 309 LYS D CD  
10272 C CE  . LYS D 8   ? 0.6270 0.6465 0.5566 -0.0475 -0.0195 -0.0521 309 LYS D CE  
10273 N NZ  . LYS D 8   ? 0.6680 0.6932 0.5879 -0.0551 -0.0196 -0.0593 309 LYS D NZ  
10274 N N   . ASN D 9   ? 0.5578 0.5493 0.5163 -0.0277 -0.0208 -0.0288 310 ASN D N   
10275 C CA  . ASN D 9   ? 0.5798 0.5833 0.5433 -0.0208 -0.0200 -0.0258 310 ASN D CA  
10276 C C   . ASN D 9   ? 0.6064 0.6218 0.5647 -0.0215 -0.0184 -0.0311 310 ASN D C   
10277 O O   . ASN D 9   ? 0.6296 0.6366 0.5797 -0.0196 -0.0157 -0.0395 310 ASN D O   
10278 C CB  . ASN D 9   ? 0.6078 0.6001 0.5720 -0.0108 -0.0177 -0.0267 310 ASN D CB  
10279 C CG  . ASN D 9   ? 0.6158 0.6235 0.5871 -0.0050 -0.0174 -0.0228 310 ASN D CG  
10280 O OD1 . ASN D 9   ? 0.5703 0.5918 0.5406 -0.0037 -0.0158 -0.0257 310 ASN D OD1 
10281 N ND2 . ASN D 9   ? 0.6182 0.6243 0.5963 -0.0021 -0.0187 -0.0166 310 ASN D ND2 
10282 N N   . TRP D 10  ? 0.6213 0.6549 0.5831 -0.0244 -0.0200 -0.0262 311 TRP D N   
10283 C CA  . TRP D 10  ? 0.6553 0.7022 0.6115 -0.0268 -0.0187 -0.0303 311 TRP D CA  
10284 C C   . TRP D 10  ? 0.6796 0.7350 0.6363 -0.0195 -0.0149 -0.0333 311 TRP D C   
10285 O O   . TRP D 10  ? 0.7813 0.8488 0.7331 -0.0210 -0.0129 -0.0376 311 TRP D O   
10286 C CB  . TRP D 10  ? 0.6124 0.6738 0.5698 -0.0339 -0.0223 -0.0233 311 TRP D CB  
10287 C CG  . TRP D 10  ? 0.5863 0.6442 0.5424 -0.0405 -0.0259 -0.0222 311 TRP D CG  
10288 C CD1 . TRP D 10  ? 0.5237 0.5768 0.4858 -0.0417 -0.0291 -0.0165 311 TRP D CD1 
10289 C CD2 . TRP D 10  ? 0.5151 0.5762 0.4635 -0.0468 -0.0267 -0.0277 311 TRP D CD2 
10290 N NE1 . TRP D 10  ? 0.5350 0.5898 0.4944 -0.0483 -0.0319 -0.0180 311 TRP D NE1 
10291 C CE2 . TRP D 10  ? 0.5050 0.5647 0.4559 -0.0519 -0.0307 -0.0248 311 TRP D CE2 
10292 C CE3 . TRP D 10  ? 0.6817 0.7482 0.6212 -0.0488 -0.0245 -0.0352 311 TRP D CE3 
10293 C CZ2 . TRP D 10  ? 0.6117 0.6760 0.5569 -0.0593 -0.0327 -0.0289 311 TRP D CZ2 
10294 C CZ3 . TRP D 10  ? 0.6524 0.7215 0.5852 -0.0563 -0.0265 -0.0394 311 TRP D CZ3 
10295 C CH2 . TRP D 10  ? 0.6579 0.7265 0.5938 -0.0617 -0.0307 -0.0361 311 TRP D CH2 
10296 N N   . GLU D 11  ? 0.6628 0.7142 0.6255 -0.0120 -0.0139 -0.0315 312 GLU D N   
10297 C CA  . GLU D 11  ? 0.6570 0.7166 0.6209 -0.0034 -0.0102 -0.0356 312 GLU D CA  
10298 C C   . GLU D 11  ? 0.6263 0.6699 0.5840 0.0053  -0.0074 -0.0446 312 GLU D C   
10299 O O   . GLU D 11  ? 0.6356 0.6859 0.5892 0.0108  -0.0039 -0.0521 312 GLU D O   
10300 C CB  . GLU D 11  ? 0.6897 0.7544 0.6630 0.0004  -0.0112 -0.0288 312 GLU D CB  
10301 C CG  . GLU D 11  ? 0.6889 0.7735 0.6659 0.0051  -0.0083 -0.0304 312 GLU D CG  
10302 C CD  . GLU D 11  ? 0.7612 0.8470 0.7462 0.0117  -0.0089 -0.0267 312 GLU D CD  
10303 O OE1 . GLU D 11  ? 0.7143 0.7923 0.7032 0.0085  -0.0119 -0.0195 312 GLU D OE1 
10304 O OE2 . GLU D 11  ? 0.7933 0.8888 0.7804 0.0206  -0.0062 -0.0314 312 GLU D OE2 
10305 N N   . THR D 12  ? 0.5555 0.5771 0.5114 0.0065  -0.0087 -0.0442 313 THR D N   
10306 C CA  . THR D 12  ? 0.5242 0.5254 0.4724 0.0151  -0.0063 -0.0514 313 THR D CA  
10307 C C   . THR D 12  ? 0.6488 0.6322 0.5857 0.0089  -0.0059 -0.0576 313 THR D C   
10308 O O   . THR D 12  ? 0.7119 0.6769 0.6391 0.0154  -0.0034 -0.0652 313 THR D O   
10309 C CB  . THR D 12  ? 0.5777 0.5638 0.5294 0.0210  -0.0077 -0.0465 313 THR D CB  
10310 O OG1 . THR D 12  ? 0.5806 0.5567 0.5334 0.0116  -0.0105 -0.0410 313 THR D OG1 
10311 C CG2 . THR D 12  ? 0.5543 0.5581 0.5169 0.0265  -0.0083 -0.0407 313 THR D CG2 
10312 N N   . GLU D 13  ? 0.6516 0.6397 0.5886 -0.0033 -0.0084 -0.0549 314 GLU D N   
10313 C CA  . GLU D 13  ? 0.6077 0.5821 0.5349 -0.0118 -0.0086 -0.0603 314 GLU D CA  
10314 C C   . GLU D 13  ? 0.7188 0.6677 0.6420 -0.0130 -0.0091 -0.0598 314 GLU D C   
10315 O O   . GLU D 13  ? 0.7035 0.6383 0.6171 -0.0206 -0.0088 -0.0651 314 GLU D O   
10316 C CB  . GLU D 13  ? 0.8003 0.7709 0.7159 -0.0095 -0.0052 -0.0714 314 GLU D CB  
10317 C CG  . GLU D 13  ? 0.8373 0.8322 0.7555 -0.0062 -0.0034 -0.0731 314 GLU D CG  
10318 C CD  . GLU D 13  ? 1.0417 1.0455 0.9521 -0.0150 -0.0032 -0.0786 314 GLU D CD  
10319 O OE1 . GLU D 13  ? 1.0869 1.0982 0.9991 -0.0259 -0.0068 -0.0739 314 GLU D OE1 
10320 O OE2 . GLU D 13  ? 1.1290 1.1330 1.0311 -0.0103 0.0005  -0.0879 314 GLU D OE2 
10321 N N   . VAL D 14  ? 0.7120 0.6550 0.6415 -0.0070 -0.0098 -0.0535 315 VAL D N   
10322 C CA  . VAL D 14  ? 0.7389 0.6586 0.6643 -0.0092 -0.0102 -0.0520 315 VAL D CA  
10323 C C   . VAL D 14  ? 0.7360 0.6607 0.6648 -0.0226 -0.0130 -0.0480 315 VAL D C   
10324 O O   . VAL D 14  ? 0.6986 0.6443 0.6378 -0.0260 -0.0157 -0.0418 315 VAL D O   
10325 C CB  . VAL D 14  ? 0.7773 0.6932 0.7092 0.0004  -0.0106 -0.0456 315 VAL D CB  
10326 C CG1 . VAL D 14  ? 0.7906 0.6839 0.7180 -0.0033 -0.0111 -0.0427 315 VAL D CG1 
10327 C CG2 . VAL D 14  ? 0.7443 0.6563 0.6726 0.0147  -0.0081 -0.0501 315 VAL D CG2 
10328 N N   . VAL D 15  ? 0.7545 0.6600 0.6741 -0.0302 -0.0124 -0.0515 316 VAL D N   
10329 C CA  . VAL D 15  ? 0.7456 0.6572 0.6688 -0.0429 -0.0149 -0.0484 316 VAL D CA  
10330 C C   . VAL D 15  ? 0.7079 0.6002 0.6289 -0.0450 -0.0144 -0.0453 316 VAL D C   
10331 O O   . VAL D 15  ? 0.7429 0.6089 0.6518 -0.0426 -0.0117 -0.0493 316 VAL D O   
10332 C CB  . VAL D 15  ? 0.7602 0.6724 0.6746 -0.0541 -0.0148 -0.0560 316 VAL D CB  
10333 C CG1 . VAL D 15  ? 0.6795 0.6043 0.5998 -0.0666 -0.0179 -0.0526 316 VAL D CG1 
10334 C CG2 . VAL D 15  ? 0.6865 0.6165 0.6012 -0.0514 -0.0149 -0.0595 316 VAL D CG2 
10335 N N   . LEU D 16  ? 0.6996 0.6044 0.6313 -0.0492 -0.0168 -0.0380 317 LEU D N   
10336 C CA  . LEU D 16  ? 0.6139 0.5053 0.5450 -0.0525 -0.0163 -0.0342 317 LEU D CA  
10337 C C   . LEU D 16  ? 0.6445 0.5469 0.5788 -0.0664 -0.0179 -0.0338 317 LEU D C   
10338 O O   . LEU D 16  ? 0.7167 0.6431 0.6594 -0.0697 -0.0207 -0.0326 317 LEU D O   
10339 C CB  . LEU D 16  ? 0.6041 0.5021 0.5459 -0.0437 -0.0175 -0.0258 317 LEU D CB  
10340 C CG  . LEU D 16  ? 0.6268 0.5256 0.5704 -0.0301 -0.0169 -0.0251 317 LEU D CG  
10341 C CD1 . LEU D 16  ? 0.5088 0.4193 0.4642 -0.0240 -0.0187 -0.0169 317 LEU D CD1 
10342 C CD2 . LEU D 16  ? 0.6817 0.5534 0.6120 -0.0236 -0.0141 -0.0297 317 LEU D CD2 
10343 N N   . THR D 17  ? 0.6503 0.5356 0.5772 -0.0744 -0.0162 -0.0348 318 THR D N   
10344 C CA  . THR D 17  ? 0.6944 0.5893 0.6226 -0.0890 -0.0170 -0.0359 318 THR D CA  
10345 C C   . THR D 17  ? 0.7111 0.6124 0.6484 -0.0899 -0.0175 -0.0287 318 THR D C   
10346 O O   . THR D 17  ? 0.7028 0.5838 0.6343 -0.0880 -0.0153 -0.0264 318 THR D O   
10347 C CB  . THR D 17  ? 0.7079 0.5787 0.6190 -0.1001 -0.0141 -0.0434 318 THR D CB  
10348 O OG1 . THR D 17  ? 0.6946 0.5560 0.5959 -0.0968 -0.0131 -0.0505 318 THR D OG1 
10349 C CG2 . THR D 17  ? 0.6418 0.5278 0.5548 -0.1168 -0.0150 -0.0458 318 THR D CG2 
10350 N N   . ASP D 18  ? 0.6811 0.6102 0.6318 -0.0923 -0.0205 -0.0253 319 ASP D N   
10351 C CA  . ASP D 18  ? 0.6000 0.5388 0.5606 -0.0917 -0.0212 -0.0188 319 ASP D CA  
10352 C C   . ASP D 18  ? 0.6856 0.6304 0.6452 -0.1064 -0.0203 -0.0212 319 ASP D C   
10353 O O   . ASP D 18  ? 0.6805 0.6464 0.6446 -0.1139 -0.0225 -0.0241 319 ASP D O   
10354 C CB  . ASP D 18  ? 0.5517 0.5159 0.5267 -0.0839 -0.0249 -0.0136 319 ASP D CB  
10355 C CG  . ASP D 18  ? 0.6051 0.5769 0.5895 -0.0808 -0.0254 -0.0073 319 ASP D CG  
10356 O OD1 . ASP D 18  ? 0.6358 0.6171 0.6233 -0.0893 -0.0251 -0.0076 319 ASP D OD1 
10357 O OD2 . ASP D 18  ? 0.6364 0.6056 0.6249 -0.0703 -0.0258 -0.0024 319 ASP D OD2 
10358 N N   . THR D 19  ? 0.6581 0.5849 0.6110 -0.1111 -0.0171 -0.0201 320 THR D N   
10359 C CA  . THR D 19  ? 0.6825 0.6179 0.6364 -0.1248 -0.0158 -0.0209 320 THR D CA  
10360 C C   . THR D 19  ? 0.7027 0.6534 0.6689 -0.1208 -0.0163 -0.0144 320 THR D C   
10361 O O   . THR D 19  ? 0.6514 0.6221 0.6241 -0.1299 -0.0163 -0.0149 320 THR D O   
10362 C CB  . THR D 19  ? 0.6439 0.5480 0.5799 -0.1350 -0.0115 -0.0239 320 THR D CB  
10363 O OG1 . THR D 19  ? 0.7130 0.5939 0.6438 -0.1245 -0.0098 -0.0190 320 THR D OG1 
10364 C CG2 . THR D 19  ? 0.5746 0.4614 0.4965 -0.1402 -0.0107 -0.0315 320 THR D CG2 
10365 N N   . LEU D 20  ? 0.5950 0.5382 0.5644 -0.1073 -0.0166 -0.0088 321 LEU D N   
10366 C CA  . LEU D 20  ? 0.5541 0.5061 0.5320 -0.1038 -0.0163 -0.0031 321 LEU D CA  
10367 C C   . LEU D 20  ? 0.6324 0.6180 0.6261 -0.1028 -0.0194 -0.0018 321 LEU D C   
10368 O O   . LEU D 20  ? 0.5085 0.5061 0.5088 -0.1046 -0.0186 0.0006  321 LEU D O   
10369 C CB  . LEU D 20  ? 0.4730 0.4115 0.4509 -0.0896 -0.0166 0.0019  321 LEU D CB  
10370 C CG  . LEU D 20  ? 0.5687 0.5135 0.5541 -0.0843 -0.0164 0.0077  321 LEU D CG  
10371 C CD1 . LEU D 20  ? 0.4732 0.4091 0.4519 -0.0944 -0.0126 0.0082  321 LEU D CD1 
10372 C CD2 . LEU D 20  ? 0.5067 0.4397 0.4916 -0.0710 -0.0172 0.0118  321 LEU D CD2 
10373 N N   . HIS D 21  ? 0.5712 0.5722 0.5701 -0.0996 -0.0230 -0.0034 322 HIS D N   
10374 C CA  . HIS D 21  ? 0.4808 0.5119 0.4933 -0.0965 -0.0266 -0.0016 322 HIS D CA  
10375 C C   . HIS D 21  ? 0.5011 0.5521 0.5178 -0.1083 -0.0259 -0.0046 322 HIS D C   
10376 O O   . HIS D 21  ? 0.4857 0.5617 0.5141 -0.1046 -0.0283 -0.0027 322 HIS D O   
10377 C CB  . HIS D 21  ? 0.5421 0.5841 0.5564 -0.0928 -0.0306 -0.0030 322 HIS D CB  
10378 C CG  . HIS D 21  ? 0.5372 0.5821 0.5450 -0.1047 -0.0305 -0.0097 322 HIS D CG  
10379 N ND1 . HIS D 21  ? 0.5662 0.5877 0.5609 -0.1092 -0.0280 -0.0141 322 HIS D ND1 
10380 C CD2 . HIS D 21  ? 0.5505 0.6191 0.5626 -0.1132 -0.0327 -0.0132 322 HIS D CD2 
10381 C CE1 . HIS D 21  ? 0.5776 0.6066 0.5680 -0.1208 -0.0284 -0.0202 322 HIS D CE1 
10382 N NE2 . HIS D 21  ? 0.5888 0.6475 0.5899 -0.1238 -0.0313 -0.0197 322 HIS D NE2 
10383 N N   . LEU D 22  ? 0.5863 0.6270 0.5933 -0.1223 -0.0228 -0.0095 323 LEU D N   
10384 C CA  . LEU D 22  ? 0.6403 0.7003 0.6505 -0.1358 -0.0214 -0.0127 323 LEU D CA  
10385 C C   . LEU D 22  ? 0.7062 0.7726 0.7224 -0.1349 -0.0189 -0.0090 323 LEU D C   
10386 O O   . LEU D 22  ? 0.6916 0.7841 0.7158 -0.1420 -0.0187 -0.0108 323 LEU D O   
10387 C CB  . LEU D 22  ? 0.6292 0.6705 0.6245 -0.1522 -0.0179 -0.0185 323 LEU D CB  
10388 C CG  . LEU D 22  ? 0.7071 0.7462 0.6964 -0.1552 -0.0201 -0.0237 323 LEU D CG  
10389 C CD1 . LEU D 22  ? 0.6970 0.7052 0.6675 -0.1677 -0.0162 -0.0288 323 LEU D CD1 
10390 C CD2 . LEU D 22  ? 0.6851 0.7611 0.6847 -0.1617 -0.0237 -0.0272 323 LEU D CD2 
10391 N N   . LYS D 23  ? 0.7214 0.7666 0.7341 -0.1262 -0.0172 -0.0042 324 LYS D N   
10392 C CA  . LYS D 23  ? 0.7207 0.7693 0.7370 -0.1257 -0.0145 -0.0009 324 LYS D CA  
10393 C C   . LYS D 23  ? 0.7542 0.8191 0.7836 -0.1106 -0.0174 0.0035  324 LYS D C   
10394 O O   . LYS D 23  ? 0.8519 0.9144 0.8831 -0.1068 -0.0153 0.0068  324 LYS D O   
10395 C CB  . LYS D 23  ? 0.7754 0.7898 0.7778 -0.1270 -0.0105 0.0015  324 LYS D CB  
10396 C CG  . LYS D 23  ? 0.9225 0.9214 0.9108 -0.1446 -0.0065 -0.0024 324 LYS D CG  
10397 C CD  . LYS D 23  ? 1.0642 1.0578 1.0475 -0.1527 -0.0019 -0.0002 324 LYS D CD  
10398 C CE  . LYS D 23  ? 1.2117 1.1688 1.1810 -0.1470 0.0000  0.0041  324 LYS D CE  
10399 N NZ  . LYS D 23  ? 1.2663 1.1984 1.2245 -0.1444 -0.0013 0.0018  324 LYS D NZ  
10400 N N   . SER D 24  ? 0.7246 0.8049 0.7620 -0.1022 -0.0221 0.0037  325 SER D N   
10401 C CA  . SER D 24  ? 0.7636 0.8584 0.8118 -0.0884 -0.0251 0.0076  325 SER D CA  
10402 C C   . SER D 24  ? 0.7860 0.9148 0.8456 -0.0903 -0.0266 0.0054  325 SER D C   
10403 O O   . SER D 24  ? 0.7956 0.9402 0.8564 -0.0997 -0.0275 0.0010  325 SER D O   
10404 C CB  . SER D 24  ? 0.7330 0.8228 0.7815 -0.0774 -0.0294 0.0099  325 SER D CB  
10405 O OG  . SER D 24  ? 0.7551 0.8622 0.8064 -0.0800 -0.0330 0.0071  325 SER D OG  
10406 N N   . THR D 25  ? 0.9104 1.0512 0.9783 -0.0812 -0.0268 0.0079  326 THR D N   
10407 C CA  . THR D 25  ? 1.0409 1.2159 1.1206 -0.0801 -0.0285 0.0058  326 THR D CA  
10408 C C   . THR D 25  ? 0.9933 1.1773 1.0809 -0.0628 -0.0321 0.0094  326 THR D C   
10409 O O   . THR D 25  ? 1.0433 1.2543 1.1406 -0.0587 -0.0331 0.0079  326 THR D O   
10410 C CB  . THR D 25  ? 1.1490 1.3361 1.2307 -0.0909 -0.0233 0.0030  326 THR D CB  
10411 O OG1 . THR D 25  ? 1.2411 1.3990 1.3113 -0.0978 -0.0185 0.0045  326 THR D OG1 
10412 C CG2 . THR D 25  ? 1.0885 1.3005 1.1732 -0.1053 -0.0231 -0.0027 326 THR D CG2 
10413 N N   . LEU D 26  ? 0.8880 1.0502 0.9710 -0.0527 -0.0339 0.0137  327 LEU D N   
10414 C CA  . LEU D 26  ? 0.8995 1.0654 0.9870 -0.0372 -0.0376 0.0172  327 LEU D CA  
10415 C C   . LEU D 26  ? 0.9244 1.0899 1.0102 -0.0316 -0.0431 0.0191  327 LEU D C   
10416 O O   . LEU D 26  ? 0.9902 1.1448 1.0698 -0.0383 -0.0433 0.0183  327 LEU D O   
10417 C CB  . LEU D 26  ? 0.8554 0.9976 0.9382 -0.0309 -0.0354 0.0209  327 LEU D CB  
10418 C CG  . LEU D 26  ? 0.7961 0.9358 0.8786 -0.0356 -0.0299 0.0199  327 LEU D CG  
10419 C CD1 . LEU D 26  ? 0.7885 0.9052 0.8657 -0.0288 -0.0287 0.0236  327 LEU D CD1 
10420 C CD2 . LEU D 26  ? 0.7239 0.8918 0.8161 -0.0333 -0.0292 0.0172  327 LEU D CD2 
10421 N N   . GLU D 27  ? 0.8444 1.0210 0.9348 -0.0191 -0.0474 0.0214  328 GLU D N   
10422 C CA  . GLU D 27  ? 0.7682 0.9480 0.8566 -0.0139 -0.0531 0.0234  328 GLU D CA  
10423 C C   . GLU D 27  ? 0.7952 0.9477 0.8745 -0.0100 -0.0539 0.0278  328 GLU D C   
10424 O O   . GLU D 27  ? 0.8559 0.9901 0.9321 -0.0061 -0.0517 0.0303  328 GLU D O   
10425 C CB  . GLU D 27  ? 0.7576 0.9568 0.8521 -0.0008 -0.0578 0.0249  328 GLU D CB  
10426 C CG  . GLU D 27  ? 0.8668 1.1003 0.9713 -0.0038 -0.0587 0.0203  328 GLU D CG  
10427 C CD  . GLU D 27  ? 1.0428 1.2957 1.1519 0.0107  -0.0649 0.0222  328 GLU D CD  
10428 O OE1 . GLU D 27  ? 1.1367 1.4204 1.2532 0.0088  -0.0674 0.0188  328 GLU D OE1 
10429 O OE2 . GLU D 27  ? 1.0863 1.3233 1.1907 0.0238  -0.0674 0.0270  328 GLU D OE2 
10430 N N   . THR D 28  ? 0.6949 0.8465 0.7696 -0.0119 -0.0571 0.0285  329 THR D N   
10431 C CA  . THR D 28  ? 0.5705 0.7022 0.6371 -0.0076 -0.0588 0.0328  329 THR D CA  
10432 C C   . THR D 28  ? 0.4882 0.6229 0.5534 0.0044  -0.0642 0.0376  329 THR D C   
10433 O O   . THR D 28  ? 0.6008 0.7173 0.6589 0.0089  -0.0651 0.0419  329 THR D O   
10434 C CB  . THR D 28  ? 0.5932 0.7215 0.6541 -0.0160 -0.0590 0.0310  329 THR D CB  
10435 O OG1 . THR D 28  ? 0.4758 0.6258 0.5391 -0.0173 -0.0632 0.0293  329 THR D OG1 
10436 C CG2 . THR D 28  ? 0.5945 0.7144 0.6539 -0.0271 -0.0538 0.0265  329 THR D CG2 
10437 N N   . GLY D 29  ? 0.4205 0.5777 0.4915 0.0095  -0.0679 0.0369  330 GLY D N   
10438 C CA  . GLY D 29  ? 0.5040 0.6639 0.5721 0.0215  -0.0737 0.0415  330 GLY D CA  
10439 C C   . GLY D 29  ? 0.6047 0.7733 0.6685 0.0195  -0.0784 0.0426  330 GLY D C   
10440 O O   . GLY D 29  ? 0.7323 0.9103 0.7947 0.0293  -0.0840 0.0459  330 GLY D O   
10441 N N   . CYS D 30  ? 0.4974 0.6627 0.5581 0.0078  -0.0762 0.0399  331 CYS D N   
10442 C CA  . CYS D 30  ? 0.4639 0.6405 0.5207 0.0045  -0.0803 0.0396  331 CYS D CA  
10443 C C   . CYS D 30  ? 0.4957 0.7034 0.5613 0.0020  -0.0827 0.0351  331 CYS D C   
10444 O O   . CYS D 30  ? 0.5414 0.7600 0.6153 -0.0030 -0.0793 0.0304  331 CYS D O   
10445 C CB  . CYS D 30  ? 0.3757 0.5401 0.4264 -0.0072 -0.0769 0.0369  331 CYS D CB  
10446 S SG  . CYS D 30  ? 0.4866 0.6201 0.5276 -0.0059 -0.0741 0.0413  331 CYS D SG  
10447 N N   . THR D 31  ? 0.5114 0.7346 0.5746 0.0050  -0.0887 0.0365  332 THR D N   
10448 C CA  . THR D 31  ? 0.5239 0.7791 0.5944 0.0005  -0.0914 0.0316  332 THR D CA  
10449 C C   . THR D 31  ? 0.4599 0.7166 0.5244 -0.0124 -0.0913 0.0280  332 THR D C   
10450 O O   . THR D 31  ? 0.5361 0.7701 0.5913 -0.0162 -0.0891 0.0293  332 THR D O   
10451 C CB  . THR D 31  ? 0.6201 0.8959 0.6930 0.0145  -0.0991 0.0355  332 THR D CB  
10452 O OG1 . THR D 31  ? 0.7341 1.0048 0.7962 0.0174  -0.1042 0.0401  332 THR D OG1 
10453 C CG2 . THR D 31  ? 0.5590 0.8245 0.6335 0.0298  -0.0994 0.0402  332 THR D CG2 
10454 N N   . GLU D 32  ? 0.4691 0.7539 0.5387 -0.0193 -0.0937 0.0228  333 GLU D N   
10455 C CA  . GLU D 32  ? 0.5921 0.8787 0.6548 -0.0317 -0.0938 0.0186  333 GLU D CA  
10456 C C   . GLU D 32  ? 0.5996 0.8821 0.6522 -0.0254 -0.0993 0.0240  333 GLU D C   
10457 O O   . GLU D 32  ? 0.5931 0.8676 0.6371 -0.0342 -0.0982 0.0216  333 GLU D O   
10458 C CB  . GLU D 32  ? 0.7452 1.0640 0.8153 -0.0419 -0.0952 0.0113  333 GLU D CB  
10459 C CG  . GLU D 32  ? 0.9102 1.2207 0.9780 -0.0602 -0.0887 0.0033  333 GLU D CG  
10460 C CD  . GLU D 32  ? 0.9631 1.3008 1.0405 -0.0706 -0.0874 -0.0035 333 GLU D CD  
10461 O OE1 . GLU D 32  ? 0.9710 1.3386 1.0582 -0.0634 -0.0919 -0.0026 333 GLU D OE1 
10462 O OE2 . GLU D 32  ? 0.9251 1.2537 0.9994 -0.0861 -0.0819 -0.0097 333 GLU D OE2 
10463 N N   . TYR D 33  ? 0.4990 0.7845 0.5508 -0.0103 -0.1049 0.0312  334 TYR D N   
10464 C CA  . TYR D 33  ? 0.4636 0.7444 0.5039 -0.0045 -0.1103 0.0373  334 TYR D CA  
10465 C C   . TYR D 33  ? 0.4521 0.7042 0.4839 0.0058  -0.1101 0.0456  334 TYR D C   
10466 O O   . TYR D 33  ? 0.4537 0.6994 0.4743 0.0102  -0.1144 0.0515  334 TYR D O   
10467 C CB  . TYR D 33  ? 0.4926 0.8038 0.5356 0.0039  -0.1189 0.0391  334 TYR D CB  
10468 C CG  . TYR D 33  ? 0.6300 0.9717 0.6785 -0.0081 -0.1202 0.0311  334 TYR D CG  
10469 C CD1 . TYR D 33  ? 0.6491 0.9929 0.6885 -0.0183 -0.1214 0.0285  334 TYR D CD1 
10470 C CD2 . TYR D 33  ? 0.6462 1.0152 0.7086 -0.0103 -0.1199 0.0255  334 TYR D CD2 
10471 C CE1 . TYR D 33  ? 0.7153 1.0859 0.7586 -0.0305 -0.1225 0.0205  334 TYR D CE1 
10472 C CE2 . TYR D 33  ? 0.6539 1.0510 0.7207 -0.0231 -0.1210 0.0177  334 TYR D CE2 
10473 C CZ  . TYR D 33  ? 0.7194 1.1165 0.7763 -0.0333 -0.1224 0.0151  334 TYR D CZ  
10474 O OH  . TYR D 33  ? 0.7366 1.1609 0.7969 -0.0472 -0.1234 0.0068  334 TYR D OH  
10475 N N   . ILE D 34  ? 0.5343 0.7689 0.5700 0.0089  -0.1054 0.0465  335 ILE D N   
10476 C CA  . ILE D 34  ? 0.4721 0.6780 0.4989 0.0161  -0.1045 0.0535  335 ILE D CA  
10477 C C   . ILE D 34  ? 0.5327 0.7187 0.5616 0.0087  -0.0967 0.0504  335 ILE D C   
10478 O O   . ILE D 34  ? 0.5431 0.7353 0.5819 0.0050  -0.0929 0.0453  335 ILE D O   
10479 C CB  . ILE D 34  ? 0.5372 0.7419 0.5650 0.0323  -0.1086 0.0593  335 ILE D CB  
10480 C CG1 . ILE D 34  ? 0.6909 0.9150 0.7155 0.0418  -0.1172 0.0631  335 ILE D CG1 
10481 C CG2 . ILE D 34  ? 0.5378 0.7106 0.5545 0.0376  -0.1074 0.0662  335 ILE D CG2 
10482 C CD1 . ILE D 34  ? 0.7658 1.0243 0.8040 0.0451  -0.1200 0.0582  335 ILE D CD1 
10483 N N   . CYS D 35  ? 0.4864 0.6497 0.5056 0.0061  -0.0943 0.0535  336 CYS D N   
10484 C CA  . CYS D 35  ? 0.4799 0.6237 0.5003 0.0017  -0.0876 0.0517  336 CYS D CA  
10485 C C   . CYS D 35  ? 0.5040 0.6289 0.5205 0.0109  -0.0878 0.0581  336 CYS D C   
10486 O O   . CYS D 35  ? 0.5198 0.6353 0.5261 0.0158  -0.0913 0.0645  336 CYS D O   
10487 C CB  . CYS D 35  ? 0.4716 0.6049 0.4850 -0.0078 -0.0840 0.0495  336 CYS D CB  
10488 S SG  . CYS D 35  ? 0.4787 0.5896 0.4934 -0.0116 -0.0764 0.0476  336 CYS D SG  
10489 N N   . MET D 36  ? 0.5272 0.6458 0.5507 0.0125  -0.0841 0.0563  337 MET D N   
10490 C CA  . MET D 36  ? 0.5413 0.6412 0.5615 0.0200  -0.0836 0.0610  337 MET D CA  
10491 C C   . MET D 36  ? 0.5128 0.5949 0.5320 0.0139  -0.0777 0.0597  337 MET D C   
10492 O O   . MET D 36  ? 0.4360 0.5045 0.4547 0.0183  -0.0762 0.0618  337 MET D O   
10493 C CB  . MET D 36  ? 0.5726 0.6816 0.6010 0.0290  -0.0848 0.0603  337 MET D CB  
10494 C CG  . MET D 36  ? 0.6833 0.8125 0.7131 0.0367  -0.0911 0.0616  337 MET D CG  
10495 S SD  . MET D 36  ? 0.7984 0.9358 0.8346 0.0519  -0.0937 0.0625  337 MET D SD  
10496 C CE  . MET D 36  ? 0.9413 1.0448 0.9633 0.0607  -0.0947 0.0700  337 MET D CE  
10497 N N   . GLY D 37  ? 0.4264 0.5084 0.4446 0.0045  -0.0746 0.0562  338 GLY D N   
10498 C CA  . GLY D 37  ? 0.4241 0.4923 0.4415 -0.0009 -0.0694 0.0544  338 GLY D CA  
10499 C C   . GLY D 37  ? 0.4549 0.5048 0.4654 0.0012  -0.0685 0.0592  338 GLY D C   
10500 O O   . GLY D 37  ? 0.5888 0.6300 0.6008 -0.0020 -0.0643 0.0573  338 GLY D O   
10501 N N   . SER D 38  ? 0.4165 0.4600 0.4187 0.0061  -0.0724 0.0652  339 SER D N   
10502 C CA  . SER D 38  ? 0.4426 0.4674 0.4368 0.0070  -0.0717 0.0698  339 SER D CA  
10503 C C   . SER D 38  ? 0.5097 0.5250 0.5022 0.0160  -0.0740 0.0733  339 SER D C   
10504 O O   . SER D 38  ? 0.5955 0.5933 0.5792 0.0166  -0.0739 0.0773  339 SER D O   
10505 C CB  . SER D 38  ? 0.5069 0.5263 0.4888 0.0036  -0.0735 0.0744  339 SER D CB  
10506 O OG  . SER D 38  ? 0.4776 0.5003 0.4531 0.0091  -0.0791 0.0788  339 SER D OG  
10507 N N   . ILE D 39  ? 0.4941 0.5208 0.4941 0.0228  -0.0760 0.0715  340 ILE D N   
10508 C CA  . ILE D 39  ? 0.5018 0.5206 0.5017 0.0322  -0.0772 0.0733  340 ILE D CA  
10509 C C   . ILE D 39  ? 0.5158 0.5275 0.5212 0.0296  -0.0722 0.0699  340 ILE D C   
10510 O O   . ILE D 39  ? 0.4623 0.4843 0.4770 0.0245  -0.0688 0.0650  340 ILE D O   
10511 C CB  . ILE D 39  ? 0.5319 0.5696 0.5395 0.0404  -0.0805 0.0716  340 ILE D CB  
10512 C CG1 . ILE D 39  ? 0.5812 0.6302 0.5845 0.0419  -0.0857 0.0742  340 ILE D CG1 
10513 C CG2 . ILE D 39  ? 0.5491 0.5791 0.5558 0.0521  -0.0820 0.0731  340 ILE D CG2 
10514 C CD1 . ILE D 39  ? 0.5450 0.5771 0.5330 0.0470  -0.0899 0.0816  340 ILE D CD1 
10515 N N   . MET D 40  ? 0.5169 0.5098 0.5152 0.0328  -0.0719 0.0727  341 MET D N   
10516 C CA  . MET D 40  ? 0.6108 0.5969 0.6129 0.0298  -0.0674 0.0698  341 MET D CA  
10517 C C   . MET D 40  ? 0.5844 0.5817 0.5972 0.0347  -0.0660 0.0655  341 MET D C   
10518 O O   . MET D 40  ? 0.5792 0.5820 0.5993 0.0296  -0.0621 0.0616  341 MET D O   
10519 C CB  . MET D 40  ? 0.7318 0.6954 0.7229 0.0307  -0.0675 0.0731  341 MET D CB  
10520 C CG  . MET D 40  ? 0.9011 0.8595 0.8955 0.0253  -0.0630 0.0701  341 MET D CG  
10521 S SD  . MET D 40  ? 1.0755 1.0100 1.0564 0.0212  -0.0625 0.0734  341 MET D SD  
10522 C CE  . MET D 40  ? 0.9555 0.8895 0.9284 0.0128  -0.0635 0.0771  341 MET D CE  
10523 N N   . HIS D 41  ? 0.6112 0.6122 0.6244 0.0449  -0.0690 0.0663  342 HIS D N   
10524 C CA  . HIS D 41  ? 0.6343 0.6494 0.6579 0.0499  -0.0675 0.0620  342 HIS D CA  
10525 C C   . HIS D 41  ? 0.6924 0.7291 0.7219 0.0555  -0.0711 0.0613  342 HIS D C   
10526 O O   . HIS D 41  ? 0.6927 0.7292 0.7188 0.0668  -0.0751 0.0635  342 HIS D O   
10527 C CB  . HIS D 41  ? 0.7805 0.7822 0.8001 0.0584  -0.0671 0.0622  342 HIS D CB  
10528 C CG  . HIS D 41  ? 0.9334 0.9139 0.9458 0.0532  -0.0643 0.0630  342 HIS D CG  
10529 N ND1 . HIS D 41  ? 0.9738 0.9327 0.9748 0.0584  -0.0656 0.0656  342 HIS D ND1 
10530 C CD2 . HIS D 41  ? 0.9696 0.9477 0.9841 0.0434  -0.0605 0.0613  342 HIS D CD2 
10531 C CE1 . HIS D 41  ? 0.9773 0.9232 0.9743 0.0508  -0.0626 0.0653  342 HIS D CE1 
10532 N NE2 . HIS D 41  ? 0.9488 0.9070 0.9544 0.0423  -0.0597 0.0628  342 HIS D NE2 
10533 N N   . PRO D 42  ? 0.7917 0.8473 0.8293 0.0482  -0.0701 0.0581  343 PRO D N   
10534 C CA  . PRO D 42  ? 0.8562 0.9358 0.9004 0.0527  -0.0736 0.0567  343 PRO D CA  
10535 C C   . PRO D 42  ? 0.9775 1.0739 1.0322 0.0574  -0.0717 0.0523  343 PRO D C   
10536 O O   . PRO D 42  ? 1.0023 1.0975 1.0615 0.0519  -0.0667 0.0490  343 PRO D O   
10537 C CB  . PRO D 42  ? 0.7814 0.8727 0.8289 0.0408  -0.0726 0.0542  343 PRO D CB  
10538 C CG  . PRO D 42  ? 0.7960 0.8673 0.8372 0.0324  -0.0693 0.0552  343 PRO D CG  
10539 C CD  . PRO D 42  ? 0.7487 0.8038 0.7881 0.0358  -0.0665 0.0559  343 PRO D CD  
10540 N N   . SER D 43  ? 1.0462 1.1590 1.1042 0.0682  -0.0759 0.0524  344 SER D N   
10541 C CA  . SER D 43  ? 1.1172 1.2502 1.1858 0.0737  -0.0742 0.0478  344 SER D CA  
10542 C C   . SER D 43  ? 1.1575 1.3219 1.2375 0.0660  -0.0738 0.0431  344 SER D C   
10543 O O   . SER D 43  ? 1.2088 1.3930 1.2986 0.0654  -0.0709 0.0384  344 SER D O   
10544 C CB  . SER D 43  ? 1.0865 1.2212 1.1528 0.0915  -0.0787 0.0497  344 SER D CB  
10545 O OG  . SER D 43  ? 1.0124 1.1677 1.0810 0.0974  -0.0845 0.0508  344 SER D OG  
10546 N N   . PRO D 49  ? 1.5602 1.6891 1.6360 0.1424  -0.0281 0.0008  350 PRO D N   
10547 C CA  . PRO D 49  ? 1.5931 1.7387 1.6731 0.1416  -0.0215 -0.0055 350 PRO D CA  
10548 C C   . PRO D 49  ? 1.6227 1.8089 1.7182 0.1335  -0.0179 -0.0085 350 PRO D C   
10549 O O   . PRO D 49  ? 1.5803 1.7715 1.6775 0.1176  -0.0131 -0.0084 350 PRO D O   
10550 C CB  . PRO D 49  ? 1.5733 1.7163 1.6492 0.1628  -0.0224 -0.0103 350 PRO D CB  
10551 C CG  . PRO D 49  ? 1.5632 1.6689 1.6250 0.1697  -0.0284 -0.0053 350 PRO D CG  
10552 C CD  . PRO D 49  ? 1.5491 1.6549 1.6141 0.1596  -0.0327 0.0016  350 PRO D CD  
10553 N N   . GLU D 50  ? 1.7071 1.9221 1.8130 0.1440  -0.0203 -0.0109 351 GLU D N   
10554 C CA  . GLU D 50  ? 1.7228 1.9784 1.8436 0.1352  -0.0175 -0.0137 351 GLU D CA  
10555 C C   . GLU D 50  ? 1.6743 1.9303 1.7978 0.1196  -0.0201 -0.0084 351 GLU D C   
10556 O O   . GLU D 50  ? 1.6220 1.9107 1.7571 0.1138  -0.0198 -0.0103 351 GLU D O   
10557 C CB  . GLU D 50  ? 1.7383 2.0278 1.8699 0.1524  -0.0196 -0.0186 351 GLU D CB  
10558 C CG  . GLU D 50  ? 1.7140 2.0246 1.8499 0.1619  -0.0139 -0.0267 351 GLU D CG  
10559 C CD  . GLU D 50  ? 1.6950 1.9764 1.8185 0.1799  -0.0150 -0.0283 351 GLU D CD  
10560 O OE1 . GLU D 50  ? 1.6806 1.9286 1.7916 0.1733  -0.0129 -0.0264 351 GLU D OE1 
10561 O OE2 . GLU D 50  ? 1.6875 1.9792 1.8131 0.2009  -0.0180 -0.0316 351 GLU D OE2 
10562 N N   . ASP D 51  ? 1.6797 1.9012 1.7925 0.1127  -0.0225 -0.0025 352 ASP D N   
10563 C CA  . ASP D 51  ? 1.6383 1.8567 1.7520 0.0968  -0.0239 0.0020  352 ASP D CA  
10564 C C   . ASP D 51  ? 1.5223 1.7428 1.6360 0.0786  -0.0174 0.0012  352 ASP D C   
10565 O O   . ASP D 51  ? 1.5687 1.7642 1.6743 0.0683  -0.0169 0.0052  352 ASP D O   
10566 C CB  . ASP D 51  ? 1.6818 1.8646 1.7842 0.0974  -0.0287 0.0082  352 ASP D CB  
10567 C CG  . ASP D 51  ? 1.7128 1.8819 1.8091 0.1161  -0.0339 0.0093  352 ASP D CG  
10568 O OD1 . ASP D 51  ? 1.7129 1.9003 1.8150 0.1265  -0.0381 0.0088  352 ASP D OD1 
10569 O OD2 . ASP D 51  ? 1.7171 1.8564 1.8017 0.1202  -0.0339 0.0106  352 ASP D OD2 
10570 N N   . VAL D 52  ? 1.2839 1.5354 1.4065 0.0750  -0.0126 -0.0039 353 VAL D N   
10571 C CA  . VAL D 52  ? 1.0440 1.2984 1.1652 0.0588  -0.0059 -0.0049 353 VAL D CA  
10572 C C   . VAL D 52  ? 0.8106 1.0989 0.9422 0.0468  -0.0035 -0.0076 353 VAL D C   
10573 O O   . VAL D 52  ? 0.7613 1.0832 0.9038 0.0539  -0.0034 -0.0124 353 VAL D O   
10574 C CB  . VAL D 52  ? 1.0378 1.2936 1.1562 0.0643  -0.0007 -0.0090 353 VAL D CB  
10575 C CG1 . VAL D 52  ? 0.9672 1.1849 1.0725 0.0689  -0.0020 -0.0059 353 VAL D CG1 
10576 C CG2 . VAL D 52  ? 1.0692 1.3527 1.1965 0.0812  -0.0010 -0.0150 353 VAL D CG2 
10577 N N   . ALA D 53  ? 0.6336 0.9131 0.7612 0.0287  -0.0015 -0.0047 354 ALA D N   
10578 C CA  . ALA D 53  ? 0.6201 0.9264 0.7552 0.0149  0.0002  -0.0068 354 ALA D CA  
10579 C C   . ALA D 53  ? 0.7109 1.0507 0.8532 0.0102  0.0066  -0.0126 354 ALA D C   
10580 O O   . ALA D 53  ? 0.8063 1.1407 0.9438 0.0099  0.0116  -0.0137 354 ALA D O   
10581 C CB  . ALA D 53  ? 0.5700 0.8535 0.6960 -0.0032 0.0014  -0.0026 354 ALA D CB  
10582 N N   . THR D 54  ? 0.7482 1.1249 0.9020 0.0061  0.0066  -0.0166 355 THR D N   
10583 C CA  . THR D 54  ? 0.7738 1.1866 0.9352 -0.0007 0.0131  -0.0225 355 THR D CA  
10584 C C   . THR D 54  ? 0.8435 1.2498 0.9973 -0.0251 0.0193  -0.0211 355 THR D C   
10585 O O   . THR D 54  ? 0.8751 1.2506 1.0186 -0.0356 0.0180  -0.0161 355 THR D O   
10586 C CB  . THR D 54  ? 0.7392 1.1973 0.9162 0.0032  0.0108  -0.0276 355 THR D CB  
10587 O OG1 . THR D 54  ? 0.8467 1.3076 1.0242 -0.0122 0.0085  -0.0261 355 THR D OG1 
10588 C CG2 . THR D 54  ? 0.7282 1.1894 0.9108 0.0285  0.0039  -0.0281 355 THR D CG2 
10589 N N   . LYS D 55  ? 0.8940 1.3297 1.0521 -0.0341 0.0262  -0.0259 356 LYS D N   
10590 C CA  . LYS D 55  ? 0.8713 1.3023 1.0208 -0.0584 0.0324  -0.0247 356 LYS D CA  
10591 C C   . LYS D 55  ? 0.8425 1.2745 0.9919 -0.0739 0.0300  -0.0235 356 LYS D C   
10592 O O   . LYS D 55  ? 0.7711 1.1725 0.9073 -0.0886 0.0312  -0.0191 356 LYS D O   
10593 C CB  . LYS D 55  ? 0.8308 1.3000 0.9865 -0.0660 0.0402  -0.0306 356 LYS D CB  
10594 C CG  . LYS D 55  ? 0.8038 1.2577 0.9491 -0.0675 0.0463  -0.0296 356 LYS D CG  
10595 C CD  . LYS D 55  ? 0.8024 1.2982 0.9545 -0.0758 0.0543  -0.0360 356 LYS D CD  
10596 C CE  . LYS D 55  ? 0.8532 1.3369 0.9958 -0.0732 0.0599  -0.0357 356 LYS D CE  
10597 N NZ  . LYS D 55  ? 0.9095 1.4368 1.0594 -0.0787 0.0679  -0.0427 356 LYS D NZ  
10598 N N   . ASP D 56  ? 0.9054 1.3720 1.0687 -0.0700 0.0265  -0.0278 357 ASP D N   
10599 C CA  . ASP D 56  ? 0.9492 1.4223 1.1130 -0.0860 0.0245  -0.0280 357 ASP D CA  
10600 C C   . ASP D 56  ? 0.8346 1.2715 0.9912 -0.0811 0.0176  -0.0227 357 ASP D C   
10601 O O   . ASP D 56  ? 0.8521 1.2779 1.0024 -0.0969 0.0171  -0.0215 357 ASP D O   
10602 C CB  . ASP D 56  ? 1.0256 1.5515 1.2071 -0.0834 0.0227  -0.0347 357 ASP D CB  
10603 C CG  . ASP D 56  ? 1.0537 1.6207 1.2432 -0.0908 0.0302  -0.0408 357 ASP D CG  
10604 O OD1 . ASP D 56  ? 1.0445 1.6012 1.2239 -0.1085 0.0375  -0.0400 357 ASP D OD1 
10605 O OD2 . ASP D 56  ? 1.0797 1.6898 1.2851 -0.0783 0.0287  -0.0464 357 ASP D OD2 
10606 N N   . GLN D 57  ? 0.6822 1.1006 0.8388 -0.0602 0.0125  -0.0197 358 GLN D N   
10607 C CA  . GLN D 57  ? 0.6245 1.0062 0.7725 -0.0570 0.0070  -0.0142 358 GLN D CA  
10608 C C   . GLN D 57  ? 0.6139 0.9545 0.7458 -0.0677 0.0104  -0.0094 358 GLN D C   
10609 O O   . GLN D 57  ? 0.5879 0.9029 0.7116 -0.0741 0.0079  -0.0061 358 GLN D O   
10610 C CB  . GLN D 57  ? 0.6660 1.0383 0.8169 -0.0331 0.0010  -0.0122 358 GLN D CB  
10611 C CG  . GLN D 57  ? 0.7421 1.1499 0.9070 -0.0194 -0.0040 -0.0158 358 GLN D CG  
10612 C CD  . GLN D 57  ? 0.7878 1.1795 0.9519 0.0037  -0.0101 -0.0129 358 GLN D CD  
10613 O OE1 . GLN D 57  ? 0.7646 1.1376 0.9236 0.0138  -0.0086 -0.0117 358 GLN D OE1 
10614 N NE2 . GLN D 57  ? 0.8387 1.2362 1.0065 0.0113  -0.0171 -0.0117 358 GLN D NE2 
10615 N N   . LEU D 58  ? 0.5214 0.8563 0.6482 -0.0695 0.0160  -0.0091 359 LEU D N   
10616 C CA  . LEU D 58  ? 0.5689 0.8635 0.6800 -0.0752 0.0181  -0.0039 359 LEU D CA  
10617 C C   . LEU D 58  ? 0.6229 0.9069 0.7235 -0.0977 0.0223  -0.0028 359 LEU D C   
10618 O O   . LEU D 58  ? 0.6167 0.8658 0.7051 -0.1021 0.0210  0.0017  359 LEU D O   
10619 C CB  . LEU D 58  ? 0.4875 0.7789 0.5957 -0.0682 0.0221  -0.0038 359 LEU D CB  
10620 C CG  . LEU D 58  ? 0.4797 0.7300 0.5731 -0.0678 0.0224  0.0020  359 LEU D CG  
10621 C CD1 . LEU D 58  ? 0.5134 0.7377 0.6045 -0.0567 0.0154  0.0058  359 LEU D CD1 
10622 C CD2 . LEU D 58  ? 0.4707 0.7197 0.5614 -0.0600 0.0258  0.0015  359 LEU D CD2 
10623 N N   . PHE D 59  ? 0.6329 0.9461 0.7374 -0.1122 0.0274  -0.0071 360 PHE D N   
10624 C CA  . PHE D 59  ? 0.6703 0.9732 0.7631 -0.1355 0.0319  -0.0064 360 PHE D CA  
10625 C C   . PHE D 59  ? 0.6556 0.9324 0.7408 -0.1411 0.0277  -0.0040 360 PHE D C   
10626 O O   . PHE D 59  ? 0.6804 0.9202 0.7495 -0.1481 0.0289  0.0004  360 PHE D O   
10627 C CB  . PHE D 59  ? 0.7611 1.1062 0.8623 -0.1503 0.0365  -0.0125 360 PHE D CB  
10628 C CG  . PHE D 59  ? 0.8730 1.2406 0.9769 -0.1521 0.0431  -0.0149 360 PHE D CG  
10629 C CD1 . PHE D 59  ? 0.8865 1.2295 0.9750 -0.1608 0.0486  -0.0110 360 PHE D CD1 
10630 C CD2 . PHE D 59  ? 0.8818 1.2974 1.0033 -0.1456 0.0440  -0.0213 360 PHE D CD2 
10631 C CE1 . PHE D 59  ? 0.8386 1.2039 0.9289 -0.1633 0.0550  -0.0134 360 PHE D CE1 
10632 C CE2 . PHE D 59  ? 0.8293 1.2682 0.9535 -0.1474 0.0505  -0.0242 360 PHE D CE2 
10633 C CZ  . PHE D 59  ? 0.7892 1.2029 0.8977 -0.1567 0.0563  -0.0204 360 PHE D CZ  
10634 N N   . PRO D 60  ? 0.5696 0.8638 0.6649 -0.1375 0.0226  -0.0069 361 PRO D N   
10635 C CA  . PRO D 60  ? 0.5679 0.8378 0.6545 -0.1449 0.0194  -0.0054 361 PRO D CA  
10636 C C   . PRO D 60  ? 0.6003 0.8306 0.6783 -0.1325 0.0156  0.0001  361 PRO D C   
10637 O O   . PRO D 60  ? 0.7479 0.9476 0.8127 -0.1406 0.0155  0.0025  361 PRO D O   
10638 C CB  . PRO D 60  ? 0.5479 0.8507 0.6488 -0.1416 0.0146  -0.0100 361 PRO D CB  
10639 C CG  . PRO D 60  ? 0.5869 0.9161 0.7024 -0.1226 0.0125  -0.0112 361 PRO D CG  
10640 C CD  . PRO D 60  ? 0.5315 0.8653 0.6452 -0.1248 0.0190  -0.0113 361 PRO D CD  
10641 N N   . LEU D 61  ? 0.5291 0.7589 0.6135 -0.1132 0.0125  0.0021  362 LEU D N   
10642 C CA  . LEU D 61  ? 0.5509 0.7455 0.6274 -0.1025 0.0092  0.0072  362 LEU D CA  
10643 C C   . LEU D 61  ? 0.5719 0.7362 0.6330 -0.1099 0.0134  0.0111  362 LEU D C   
10644 O O   . LEU D 61  ? 0.5242 0.6574 0.5740 -0.1116 0.0121  0.0143  362 LEU D O   
10645 C CB  . LEU D 61  ? 0.4773 0.6775 0.5622 -0.0824 0.0057  0.0082  362 LEU D CB  
10646 C CG  . LEU D 61  ? 0.5045 0.7288 0.6023 -0.0719 0.0004  0.0057  362 LEU D CG  
10647 C CD1 . LEU D 61  ? 0.5243 0.7489 0.6270 -0.0527 -0.0022 0.0069  362 LEU D CD1 
10648 C CD2 . LEU D 61  ? 0.4847 0.6945 0.5790 -0.0735 -0.0043 0.0070  362 LEU D CD2 
10649 N N   . ALA D 62  ? 0.5251 0.6987 0.5851 -0.1136 0.0185  0.0107  363 ALA D N   
10650 C CA  . ALA D 62  ? 0.4952 0.6411 0.5396 -0.1203 0.0224  0.0149  363 ALA D CA  
10651 C C   . ALA D 62  ? 0.4899 0.6176 0.5207 -0.1385 0.0248  0.0156  363 ALA D C   
10652 O O   . ALA D 62  ? 0.5289 0.6219 0.5452 -0.1397 0.0245  0.0200  363 ALA D O   
10653 C CB  . ALA D 62  ? 0.5240 0.6869 0.5698 -0.1221 0.0277  0.0138  363 ALA D CB  
10654 N N   . LYS D 63  ? 0.4991 0.6498 0.5341 -0.1525 0.0270  0.0110  364 LYS D N   
10655 C CA  . LYS D 63  ? 0.5691 0.7013 0.5899 -0.1711 0.0295  0.0110  364 LYS D CA  
10656 C C   . LYS D 63  ? 0.6145 0.7164 0.6280 -0.1661 0.0247  0.0130  364 LYS D C   
10657 O O   . LYS D 63  ? 0.6813 0.7480 0.6773 -0.1720 0.0260  0.0164  364 LYS D O   
10658 C CB  . LYS D 63  ? 0.5632 0.7287 0.5916 -0.1865 0.0317  0.0049  364 LYS D CB  
10659 C CG  . LYS D 63  ? 0.6375 0.7859 0.6484 -0.2106 0.0366  0.0045  364 LYS D CG  
10660 C CD  . LYS D 63  ? 0.8352 0.9954 0.8489 -0.2220 0.0347  -0.0007 364 LYS D CD  
10661 C CE  . LYS D 63  ? 0.9333 1.0798 0.9294 -0.2483 0.0402  -0.0022 364 LYS D CE  
10662 N NZ  . LYS D 63  ? 0.9958 1.0900 0.9690 -0.2521 0.0401  0.0020  364 LYS D NZ  
10663 N N   . GLU D 64  ? 0.6636 0.7782 0.6897 -0.1543 0.0192  0.0110  365 GLU D N   
10664 C CA  . GLU D 64  ? 0.6672 0.7569 0.6874 -0.1499 0.0149  0.0121  365 GLU D CA  
10665 C C   . GLU D 64  ? 0.5755 0.6299 0.5844 -0.1402 0.0141  0.0178  365 GLU D C   
10666 O O   . GLU D 64  ? 0.4972 0.5212 0.4919 -0.1443 0.0141  0.0194  365 GLU D O   
10667 C CB  . GLU D 64  ? 0.7696 0.8803 0.8051 -0.1375 0.0091  0.0099  365 GLU D CB  
10668 C CG  . GLU D 64  ? 0.9641 1.0699 0.9970 -0.1431 0.0062  0.0070  365 GLU D CG  
10669 C CD  . GLU D 64  ? 1.1259 1.1992 1.1502 -0.1340 0.0031  0.0101  365 GLU D CD  
10670 O OE1 . GLU D 64  ? 1.1668 1.2094 1.1774 -0.1354 0.0053  0.0135  365 GLU D OE1 
10671 O OE2 . GLU D 64  ? 1.1361 1.2156 1.1673 -0.1251 -0.0017 0.0093  365 GLU D OE2 
10672 N N   . PHE D 65  ? 0.5287 0.5869 0.5431 -0.1274 0.0135  0.0206  366 PHE D N   
10673 C CA  . PHE D 65  ? 0.5820 0.6108 0.5870 -0.1179 0.0123  0.0258  366 PHE D CA  
10674 C C   . PHE D 65  ? 0.5931 0.5962 0.5797 -0.1285 0.0166  0.0291  366 PHE D C   
10675 O O   . PHE D 65  ? 0.6006 0.5730 0.5745 -0.1263 0.0153  0.0322  366 PHE D O   
10676 C CB  . PHE D 65  ? 0.4475 0.4871 0.4615 -0.1036 0.0109  0.0274  366 PHE D CB  
10677 C CG  . PHE D 65  ? 0.4788 0.4923 0.4825 -0.0965 0.0104  0.0324  366 PHE D CG  
10678 C CD1 . PHE D 65  ? 0.4719 0.4673 0.4735 -0.0866 0.0061  0.0345  366 PHE D CD1 
10679 C CD2 . PHE D 65  ? 0.5377 0.5461 0.5335 -0.1003 0.0144  0.0348  366 PHE D CD2 
10680 C CE1 . PHE D 65  ? 0.5158 0.4902 0.5085 -0.0800 0.0054  0.0389  366 PHE D CE1 
10681 C CE2 . PHE D 65  ? 0.5539 0.5395 0.5398 -0.0937 0.0135  0.0395  366 PHE D CE2 
10682 C CZ  . PHE D 65  ? 0.6064 0.5759 0.5913 -0.0833 0.0088  0.0414  366 PHE D CZ  
10683 N N   . ILE D 66  ? 0.5360 0.5509 0.5204 -0.1394 0.0217  0.0286  367 ILE D N   
10684 C CA  . ILE D 66  ? 0.5975 0.5867 0.5624 -0.1504 0.0259  0.0324  367 ILE D CA  
10685 C C   . ILE D 66  ? 0.6572 0.6231 0.6081 -0.1627 0.0265  0.0317  367 ILE D C   
10686 O O   . ILE D 66  ? 0.5982 0.5292 0.5305 -0.1645 0.0271  0.0358  367 ILE D O   
10687 C CB  . ILE D 66  ? 0.5499 0.5598 0.5153 -0.1616 0.0318  0.0315  367 ILE D CB  
10688 C CG1 . ILE D 66  ? 0.4644 0.4943 0.4418 -0.1483 0.0313  0.0317  367 ILE D CG1 
10689 C CG2 . ILE D 66  ? 0.5116 0.4928 0.4543 -0.1744 0.0363  0.0361  367 ILE D CG2 
10690 C CD1 . ILE D 66  ? 0.5619 0.5664 0.5295 -0.1375 0.0298  0.0375  367 ILE D CD1 
10691 N N   . ASP D 67  ? 0.6966 0.6807 0.6554 -0.1707 0.0261  0.0262  368 ASP D N   
10692 C CA  . ASP D 67  ? 0.6533 0.6155 0.5987 -0.1825 0.0266  0.0244  368 ASP D CA  
10693 C C   . ASP D 67  ? 0.5926 0.5249 0.5312 -0.1697 0.0222  0.0266  368 ASP D C   
10694 O O   . ASP D 67  ? 0.6244 0.5219 0.5438 -0.1745 0.0232  0.0286  368 ASP D O   
10695 C CB  . ASP D 67  ? 0.6257 0.6173 0.5830 -0.1918 0.0261  0.0176  368 ASP D CB  
10696 C CG  . ASP D 67  ? 0.7243 0.7403 0.6828 -0.2102 0.0315  0.0147  368 ASP D CG  
10697 O OD1 . ASP D 67  ? 0.7835 0.7910 0.7318 -0.2173 0.0361  0.0181  368 ASP D OD1 
10698 O OD2 . ASP D 67  ? 0.6840 0.7290 0.6535 -0.2178 0.0310  0.0089  368 ASP D OD2 
10699 N N   . GLN D 68  ? 0.5688 0.5141 0.5223 -0.1531 0.0173  0.0263  369 GLN D N   
10700 C CA  . GLN D 68  ? 0.5917 0.5139 0.5407 -0.1413 0.0133  0.0276  369 GLN D CA  
10701 C C   . GLN D 68  ? 0.6921 0.5874 0.6295 -0.1322 0.0132  0.0336  369 GLN D C   
10702 O O   . GLN D 68  ? 0.6563 0.5231 0.5815 -0.1274 0.0117  0.0351  369 GLN D O   
10703 C CB  . GLN D 68  ? 0.6368 0.5817 0.6042 -0.1281 0.0084  0.0256  369 GLN D CB  
10704 C CG  . GLN D 68  ? 0.7414 0.6879 0.7158 -0.1115 0.0058  0.0295  369 GLN D CG  
10705 C CD  . GLN D 68  ? 0.7343 0.6958 0.7227 -0.0993 0.0009  0.0280  369 GLN D CD  
10706 O OE1 . GLN D 68  ? 0.7515 0.7003 0.7388 -0.0880 -0.0020 0.0303  369 GLN D OE1 
10707 N NE2 . GLN D 68  ? 0.6832 0.6725 0.6842 -0.1018 0.0000  0.0244  369 GLN D NE2 
10708 N N   . TYR D 69  ? 0.7096 0.6139 0.6498 -0.1295 0.0147  0.0369  370 TYR D N   
10709 C CA  . TYR D 69  ? 0.6761 0.5556 0.6037 -0.1223 0.0146  0.0427  370 TYR D CA  
10710 C C   . TYR D 69  ? 0.6639 0.5113 0.5684 -0.1339 0.0178  0.0452  370 TYR D C   
10711 O O   . TYR D 69  ? 0.7239 0.5413 0.6146 -0.1268 0.0161  0.0487  370 TYR D O   
10712 C CB  . TYR D 69  ? 0.5612 0.4570 0.4951 -0.1186 0.0159  0.0452  370 TYR D CB  
10713 C CG  . TYR D 69  ? 0.6483 0.5182 0.5662 -0.1147 0.0163  0.0514  370 TYR D CG  
10714 C CD1 . TYR D 69  ? 0.7555 0.6127 0.6725 -0.0994 0.0119  0.0542  370 TYR D CD1 
10715 C CD2 . TYR D 69  ? 0.6857 0.5443 0.5884 -0.1266 0.0209  0.0544  370 TYR D CD2 
10716 C CE1 . TYR D 69  ? 0.7320 0.5676 0.6347 -0.0949 0.0116  0.0599  370 TYR D CE1 
10717 C CE2 . TYR D 69  ? 0.7783 0.6123 0.6649 -0.1223 0.0207  0.0606  370 TYR D CE2 
10718 C CZ  . TYR D 69  ? 0.7606 0.5839 0.6478 -0.1058 0.0158  0.0632  370 TYR D CZ  
10719 O OH  . TYR D 69  ? 0.7962 0.5973 0.6681 -0.1002 0.0149  0.0694  370 TYR D OH  
10720 N N   . TYR D 70  ? 0.5850 0.4378 0.4843 -0.1516 0.0225  0.0432  371 TYR D N   
10721 C CA  . TYR D 70  ? 0.7121 0.5311 0.5869 -0.1639 0.0258  0.0460  371 TYR D CA  
10722 C C   . TYR D 70  ? 0.7776 0.5718 0.6420 -0.1657 0.0243  0.0432  371 TYR D C   
10723 O O   . TYR D 70  ? 0.7617 0.5182 0.6039 -0.1675 0.0250  0.0464  371 TYR D O   
10724 C CB  . TYR D 70  ? 0.7133 0.5456 0.5844 -0.1842 0.0318  0.0448  371 TYR D CB  
10725 C CG  . TYR D 70  ? 0.6773 0.5139 0.5454 -0.1830 0.0343  0.0499  371 TYR D CG  
10726 C CD1 . TYR D 70  ? 0.6619 0.4650 0.5063 -0.1872 0.0364  0.0562  371 TYR D CD1 
10727 C CD2 . TYR D 70  ? 0.6577 0.5299 0.5458 -0.1760 0.0340  0.0484  371 TYR D CD2 
10728 C CE1 . TYR D 70  ? 0.7785 0.5858 0.6194 -0.1860 0.0385  0.0609  371 TYR D CE1 
10729 C CE2 . TYR D 70  ? 0.6614 0.5375 0.5464 -0.1745 0.0363  0.0524  371 TYR D CE2 
10730 C CZ  . TYR D 70  ? 0.7570 0.6014 0.6185 -0.1799 0.0386  0.0587  371 TYR D CZ  
10731 O OH  . TYR D 70  ? 0.6813 0.5301 0.5387 -0.1788 0.0409  0.0628  371 TYR D OH  
10732 N N   . SER D 71  ? 0.7738 0.5872 0.6528 -0.1642 0.0219  0.0373  372 SER D N   
10733 C CA  . SER D 71  ? 0.8330 0.6235 0.7028 -0.1634 0.0201  0.0342  372 SER D CA  
10734 C C   . SER D 71  ? 0.7763 0.5440 0.6411 -0.1441 0.0162  0.0377  372 SER D C   
10735 O O   . SER D 71  ? 0.7899 0.5224 0.6357 -0.1430 0.0161  0.0385  372 SER D O   
10736 C CB  . SER D 71  ? 0.8831 0.7020 0.7702 -0.1651 0.0181  0.0274  372 SER D CB  
10737 O OG  . SER D 71  ? 1.0316 0.8307 0.9122 -0.1596 0.0156  0.0246  372 SER D OG  
10738 N N   . SER D 72  ? 0.6495 0.4367 0.5306 -0.1286 0.0128  0.0397  373 SER D N   
10739 C CA  . SER D 72  ? 0.6630 0.4344 0.5417 -0.1105 0.0089  0.0423  373 SER D CA  
10740 C C   . SER D 72  ? 0.9008 0.6368 0.7574 -0.1079 0.0098  0.0480  373 SER D C   
10741 O O   . SER D 72  ? 1.0049 0.7183 0.8524 -0.0965 0.0072  0.0489  373 SER D O   
10742 C CB  . SER D 72  ? 0.6233 0.4214 0.5212 -0.0974 0.0058  0.0440  373 SER D CB  
10743 O OG  . SER D 72  ? 0.8635 0.6656 0.7599 -0.0984 0.0075  0.0486  373 SER D OG  
10744 N N   . ILE D 73  ? 0.9271 0.6580 0.7741 -0.1181 0.0133  0.0520  374 ILE D N   
10745 C CA  . ILE D 73  ? 0.9336 0.6311 0.7583 -0.1157 0.0139  0.0584  374 ILE D CA  
10746 C C   . ILE D 73  ? 0.9668 0.6325 0.7674 -0.1322 0.0179  0.0585  374 ILE D C   
10747 O O   . ILE D 73  ? 0.9930 0.6333 0.7733 -0.1361 0.0199  0.0643  374 ILE D O   
10748 C CB  . ILE D 73  ? 0.8721 0.5821 0.6995 -0.1144 0.0148  0.0638  374 ILE D CB  
10749 C CG1 . ILE D 73  ? 0.8036 0.5315 0.6333 -0.1334 0.0200  0.0625  374 ILE D CG1 
10750 C CG2 . ILE D 73  ? 0.7441 0.4815 0.5929 -0.0984 0.0106  0.0636  374 ILE D CG2 
10751 C CD1 . ILE D 73  ? 0.7504 0.4893 0.5803 -0.1337 0.0218  0.0673  374 ILE D CD1 
10752 N N   . LYS D 74  ? 0.9754 0.6413 0.7764 -0.1426 0.0192  0.0520  375 LYS D N   
10753 C CA  . LYS D 74  ? 1.1174 0.7509 0.8943 -0.1592 0.0230  0.0509  375 LYS D CA  
10754 C C   . LYS D 74  ? 1.1059 0.7350 0.8702 -0.1770 0.0281  0.0551  375 LYS D C   
10755 O O   . LYS D 74  ? 1.1577 0.7483 0.8948 -0.1853 0.0306  0.0588  375 LYS D O   
10756 C CB  . LYS D 74  ? 1.2501 0.8378 1.0039 -0.1484 0.0210  0.0532  375 LYS D CB  
10757 C CG  . LYS D 74  ? 1.2986 0.8900 1.0635 -0.1248 0.0155  0.0521  375 LYS D CG  
10758 C CD  . LYS D 74  ? 1.3559 0.9626 1.1342 -0.1245 0.0143  0.0437  375 LYS D CD  
10759 C CE  . LYS D 74  ? 1.3751 0.9841 1.1622 -0.1019 0.0094  0.0429  375 LYS D CE  
10760 N NZ  . LYS D 74  ? 1.3109 0.9513 1.1199 -0.0999 0.0077  0.0362  375 LYS D NZ  
10761 N N   . ARG D 75  ? 1.0529 0.7211 0.8360 -0.1824 0.0298  0.0546  376 ARG D N   
10762 C CA  . ARG D 75  ? 0.9876 0.6602 0.7623 -0.2007 0.0353  0.0573  376 ARG D CA  
10763 C C   . ARG D 75  ? 0.9114 0.6242 0.7040 -0.2166 0.0383  0.0506  376 ARG D C   
10764 O O   . ARG D 75  ? 0.8695 0.6059 0.6678 -0.2261 0.0420  0.0516  376 ARG D O   
10765 C CB  . ARG D 75  ? 1.0222 0.7038 0.7999 -0.1914 0.0349  0.0639  376 ARG D CB  
10766 C CG  . ARG D 75  ? 1.0645 0.7085 0.8225 -0.1778 0.0322  0.0715  376 ARG D CG  
10767 C CD  . ARG D 75  ? 1.1647 0.7659 0.8899 -0.1921 0.0359  0.0760  376 ARG D CD  
10768 N NE  . ARG D 75  ? 1.1923 0.7640 0.8989 -0.1799 0.0338  0.0848  376 ARG D NE  
10769 C CZ  . ARG D 75  ? 1.1783 0.7219 0.8754 -0.1616 0.0288  0.0872  376 ARG D CZ  
10770 N NH1 . ARG D 75  ? 1.0823 0.6021 0.7625 -0.1510 0.0267  0.0954  376 ARG D NH1 
10771 N NH2 . ARG D 75  ? 1.1098 0.6506 0.8141 -0.1536 0.0260  0.0813  376 ARG D NH2 
10772 N N   . PHE D 76  ? 0.8894 0.6122 0.6913 -0.2190 0.0368  0.0436  377 PHE D N   
10773 C CA  . PHE D 76  ? 0.8452 0.6071 0.6637 -0.2337 0.0391  0.0370  377 PHE D CA  
10774 C C   . PHE D 76  ? 0.9138 0.6647 0.7136 -0.2602 0.0454  0.0364  377 PHE D C   
10775 O O   . PHE D 76  ? 0.9973 0.7064 0.7713 -0.2691 0.0470  0.0376  377 PHE D O   
10776 C CB  . PHE D 76  ? 0.8852 0.6584 0.7158 -0.2299 0.0355  0.0300  377 PHE D CB  
10777 C CG  . PHE D 76  ? 0.8831 0.7021 0.7343 -0.2407 0.0364  0.0234  377 PHE D CG  
10778 C CD1 . PHE D 76  ? 0.9253 0.7471 0.7685 -0.2640 0.0402  0.0184  377 PHE D CD1 
10779 C CD2 . PHE D 76  ? 0.7603 0.6191 0.6380 -0.2274 0.0333  0.0221  377 PHE D CD2 
10780 C CE1 . PHE D 76  ? 0.8368 0.7039 0.6996 -0.2731 0.0406  0.0122  377 PHE D CE1 
10781 C CE2 . PHE D 76  ? 0.7059 0.6068 0.6019 -0.2353 0.0336  0.0164  377 PHE D CE2 
10782 C CZ  . PHE D 76  ? 0.7383 0.6450 0.6277 -0.2578 0.0371  0.0114  377 PHE D CZ  
10783 N N   . GLY D 77  ? 0.8991 0.6873 0.7111 -0.2728 0.0492  0.0345  378 GLY D N   
10784 C CA  . GLY D 77  ? 0.8664 0.6492 0.6618 -0.2990 0.0558  0.0343  378 GLY D CA  
10785 C C   . GLY D 77  ? 0.9333 0.6872 0.7064 -0.3030 0.0594  0.0427  378 GLY D C   
10786 O O   . GLY D 77  ? 1.0555 0.8116 0.8175 -0.3200 0.0642  0.0421  378 GLY D O   
10787 N N   . SER D 78  ? 0.8896 0.6227 0.6586 -0.2823 0.0559  0.0493  379 SER D N   
10788 C CA  . SER D 78  ? 1.0210 0.7256 0.7675 -0.2848 0.0586  0.0579  379 SER D CA  
10789 C C   . SER D 78  ? 0.9735 0.7136 0.7293 -0.2944 0.0636  0.0588  379 SER D C   
10790 O O   . SER D 78  ? 0.8227 0.6106 0.6051 -0.2934 0.0638  0.0532  379 SER D O   
10791 C CB  . SER D 78  ? 1.0549 0.7370 0.7986 -0.2589 0.0530  0.0641  379 SER D CB  
10792 O OG  . SER D 78  ? 0.9425 0.6625 0.7143 -0.2413 0.0496  0.0625  379 SER D OG  
10793 N N   . LYS D 79  ? 1.0786 0.7979 0.8136 -0.2993 0.0664  0.0647  380 LYS D N   
10794 C CA  . LYS D 79  ? 1.0764 0.8261 0.8170 -0.3083 0.0715  0.0657  380 LYS D CA  
10795 C C   . LYS D 79  ? 0.9228 0.7043 0.6870 -0.2917 0.0694  0.0665  380 LYS D C   
10796 O O   . LYS D 79  ? 0.9818 0.8097 0.7678 -0.2949 0.0719  0.0614  380 LYS D O   
10797 C CB  . LYS D 79  ? 1.2115 0.9297 0.9251 -0.3112 0.0733  0.0724  380 LYS D CB  
10798 C CG  . LYS D 79  ? 1.2678 1.0045 0.9757 -0.3318 0.0794  0.0696  380 LYS D CG  
10799 C CD  . LYS D 79  ? 1.4135 1.1095 1.0903 -0.3355 0.0803  0.0760  380 LYS D CD  
10800 C CE  . LYS D 79  ? 1.5152 1.2193 1.1810 -0.3587 0.0857  0.0720  380 LYS D CE  
10801 N NZ  . LYS D 79  ? 1.5216 1.2693 1.2000 -0.3687 0.0911  0.0703  380 LYS D NZ  
10802 N N   . ALA D 80  ? 0.8445 0.6056 0.6073 -0.2691 0.0636  0.0713  381 ALA D N   
10803 C CA  . ALA D 80  ? 0.8425 0.6341 0.6291 -0.2489 0.0601  0.0704  381 ALA D CA  
10804 C C   . ALA D 80  ? 0.8177 0.6468 0.6340 -0.2415 0.0572  0.0620  381 ALA D C   
10805 O O   . ALA D 80  ? 0.7863 0.6508 0.6241 -0.2315 0.0564  0.0593  381 ALA D O   
10806 C CB  . ALA D 80  ? 0.7754 0.5373 0.5537 -0.2276 0.0541  0.0767  381 ALA D CB  
10807 N N   . HIS D 81  ? 0.7855 0.6066 0.6023 -0.2459 0.0554  0.0577  382 HIS D N   
10808 C CA  . HIS D 81  ? 0.7942 0.6519 0.6376 -0.2410 0.0529  0.0499  382 HIS D CA  
10809 C C   . HIS D 81  ? 0.7117 0.6133 0.5692 -0.2554 0.0580  0.0447  382 HIS D C   
10810 O O   . HIS D 81  ? 0.7442 0.6841 0.6255 -0.2451 0.0565  0.0409  382 HIS D O   
10811 C CB  . HIS D 81  ? 0.7751 0.6142 0.6135 -0.2449 0.0504  0.0463  382 HIS D CB  
10812 C CG  . HIS D 81  ? 0.7573 0.6310 0.6207 -0.2395 0.0472  0.0390  382 HIS D CG  
10813 N ND1 . HIS D 81  ? 0.7998 0.6655 0.6617 -0.2446 0.0453  0.0343  382 HIS D ND1 
10814 C CD2 . HIS D 81  ? 0.7508 0.6657 0.6400 -0.2287 0.0452  0.0356  382 HIS D CD2 
10815 C CE1 . HIS D 81  ? 0.7837 0.6853 0.6695 -0.2376 0.0422  0.0288  382 HIS D CE1 
10816 N NE2 . HIS D 81  ? 0.7820 0.7129 0.6844 -0.2275 0.0420  0.0297  382 HIS D NE2 
10817 N N   . MET D 82  ? 0.6977 0.5942 0.5398 -0.2792 0.0641  0.0444  383 MET D N   
10818 C CA  . MET D 82  ? 0.7585 0.6992 0.6135 -0.2947 0.0694  0.0390  383 MET D CA  
10819 C C   . MET D 82  ? 0.8189 0.7849 0.6827 -0.2881 0.0721  0.0407  383 MET D C   
10820 O O   . MET D 82  ? 0.7464 0.7583 0.6330 -0.2851 0.0730  0.0351  383 MET D O   
10821 C CB  . MET D 82  ? 0.7051 0.6310 0.5385 -0.3235 0.0757  0.0388  383 MET D CB  
10822 C CG  . MET D 82  ? 0.9428 0.8901 0.7853 -0.3379 0.0760  0.0306  383 MET D CG  
10823 S SD  . MET D 82  ? 1.0946 1.0404 0.9533 -0.3175 0.0672  0.0266  383 MET D SD  
10824 C CE  . MET D 82  ? 1.0566 1.0626 0.9419 -0.3274 0.0677  0.0162  383 MET D CE  
10825 N N   . GLU D 83  ? 0.9003 0.8369 0.7455 -0.2852 0.0732  0.0484  384 GLU D N   
10826 C CA  . GLU D 83  ? 0.8164 0.7748 0.6676 -0.2796 0.0760  0.0499  384 GLU D CA  
10827 C C   . GLU D 83  ? 0.7561 0.7369 0.6313 -0.2545 0.0705  0.0474  384 GLU D C   
10828 O O   . GLU D 83  ? 0.7690 0.7859 0.6599 -0.2500 0.0726  0.0440  384 GLU D O   
10829 C CB  . GLU D 83  ? 0.8350 0.7544 0.6590 -0.2818 0.0778  0.0591  384 GLU D CB  
10830 C CG  . GLU D 83  ? 1.0052 0.9156 0.8072 -0.3089 0.0856  0.0614  384 GLU D CG  
10831 C CD  . GLU D 83  ? 1.0808 0.9410 0.8503 -0.3121 0.0862  0.0714  384 GLU D CD  
10832 O OE1 . GLU D 83  ? 1.1242 0.9639 0.8903 -0.2922 0.0810  0.0766  384 GLU D OE1 
10833 O OE2 . GLU D 83  ? 1.0865 0.9310 0.8371 -0.3283 0.0896  0.0719  384 GLU D OE2 
10834 N N   . ARG D 84  ? 0.6889 0.6490 0.5668 -0.2382 0.0635  0.0487  385 ARG D N   
10835 C CA  . ARG D 84  ? 0.6679 0.6468 0.5670 -0.2157 0.0582  0.0464  385 ARG D CA  
10836 C C   . ARG D 84  ? 0.6901 0.7128 0.6140 -0.2150 0.0580  0.0383  385 ARG D C   
10837 O O   . ARG D 84  ? 0.6869 0.7395 0.6276 -0.2040 0.0577  0.0353  385 ARG D O   
10838 C CB  . ARG D 84  ? 0.6917 0.6391 0.5870 -0.2007 0.0512  0.0495  385 ARG D CB  
10839 C CG  . ARG D 84  ? 0.6738 0.6357 0.5880 -0.1788 0.0456  0.0479  385 ARG D CG  
10840 C CD  . ARG D 84  ? 0.6269 0.5984 0.5431 -0.1701 0.0467  0.0500  385 ARG D CD  
10841 N NE  . ARG D 84  ? 0.6176 0.6026 0.5513 -0.1508 0.0415  0.0478  385 ARG D NE  
10842 C CZ  . ARG D 84  ? 0.6278 0.6333 0.5714 -0.1418 0.0420  0.0461  385 ARG D CZ  
10843 N NH1 . ARG D 84  ? 0.6259 0.6433 0.5646 -0.1498 0.0477  0.0462  385 ARG D NH1 
10844 N NH2 . ARG D 84  ? 0.5222 0.5358 0.4797 -0.1252 0.0371  0.0441  385 ARG D NH2 
10845 N N   . LEU D 85  ? 0.7272 0.7540 0.6528 -0.2266 0.0580  0.0344  386 LEU D N   
10846 C CA  . LEU D 85  ? 0.6912 0.7615 0.6390 -0.2276 0.0578  0.0267  386 LEU D CA  
10847 C C   . LEU D 85  ? 0.7892 0.8978 0.7456 -0.2349 0.0638  0.0234  386 LEU D C   
10848 O O   . LEU D 85  ? 0.7496 0.8927 0.7263 -0.2222 0.0625  0.0191  386 LEU D O   
10849 C CB  . LEU D 85  ? 0.5899 0.6575 0.5337 -0.2440 0.0581  0.0233  386 LEU D CB  
10850 C CG  . LEU D 85  ? 0.6482 0.6982 0.5942 -0.2348 0.0515  0.0225  386 LEU D CG  
10851 C CD1 . LEU D 85  ? 0.6278 0.6828 0.5702 -0.2544 0.0531  0.0177  386 LEU D CD1 
10852 C CD2 . LEU D 85  ? 0.6974 0.7740 0.6669 -0.2139 0.0460  0.0196  386 LEU D CD2 
10853 N N   . GLU D 86  ? 0.8579 0.9607 0.7981 -0.2555 0.0706  0.0251  387 GLU D N   
10854 C CA  . GLU D 86  ? 0.8327 0.9723 0.7794 -0.2638 0.0772  0.0220  387 GLU D CA  
10855 C C   . GLU D 86  ? 0.6711 0.8189 0.6252 -0.2447 0.0764  0.0233  387 GLU D C   
10856 O O   . GLU D 86  ? 0.5945 0.7829 0.5672 -0.2376 0.0778  0.0177  387 GLU D O   
10857 C CB  . GLU D 86  ? 1.0511 1.1745 0.9745 -0.2892 0.0846  0.0253  387 GLU D CB  
10858 C CG  . GLU D 86  ? 1.2588 1.4174 1.1854 -0.2996 0.0924  0.0228  387 GLU D CG  
10859 C CD  . GLU D 86  ? 1.4207 1.6363 1.3721 -0.3029 0.0942  0.0133  387 GLU D CD  
10860 O OE1 . GLU D 86  ? 1.4296 1.6547 1.3890 -0.3080 0.0914  0.0091  387 GLU D OE1 
10861 O OE2 . GLU D 86  ? 1.4850 1.7366 1.4476 -0.2996 0.0983  0.0098  387 GLU D OE2 
10862 N N   . GLU D 87  ? 0.6301 0.7398 0.5698 -0.2351 0.0738  0.0303  388 GLU D N   
10863 C CA  . GLU D 87  ? 0.6013 0.7156 0.5458 -0.2180 0.0729  0.0315  388 GLU D CA  
10864 C C   . GLU D 87  ? 0.6840 0.8226 0.6524 -0.1971 0.0675  0.0264  388 GLU D C   
10865 O O   . GLU D 87  ? 0.7414 0.9069 0.7214 -0.1877 0.0691  0.0228  388 GLU D O   
10866 C CB  . GLU D 87  ? 0.5527 0.6214 0.4775 -0.2115 0.0699  0.0399  388 GLU D CB  
10867 C CG  . GLU D 87  ? 0.6022 0.6723 0.5290 -0.1954 0.0688  0.0416  388 GLU D CG  
10868 C CD  . GLU D 87  ? 0.7766 0.8043 0.6852 -0.1882 0.0649  0.0496  388 GLU D CD  
10869 O OE1 . GLU D 87  ? 0.8028 0.8038 0.7062 -0.1850 0.0601  0.0524  388 GLU D OE1 
10870 O OE2 . GLU D 87  ? 0.8398 0.8620 0.7390 -0.1853 0.0666  0.0530  388 GLU D OE2 
10871 N N   . VAL D 88  ? 0.6768 0.8055 0.6517 -0.1896 0.0613  0.0259  389 VAL D N   
10872 C CA  . VAL D 88  ? 0.5821 0.7308 0.5775 -0.1703 0.0559  0.0217  389 VAL D CA  
10873 C C   . VAL D 88  ? 0.6552 0.8515 0.6690 -0.1722 0.0587  0.0141  389 VAL D C   
10874 O O   . VAL D 88  ? 0.6687 0.8878 0.6959 -0.1575 0.0580  0.0106  389 VAL D O   
10875 C CB  . VAL D 88  ? 0.5386 0.6687 0.5361 -0.1644 0.0493  0.0227  389 VAL D CB  
10876 C CG1 . VAL D 88  ? 0.5724 0.7285 0.5910 -0.1486 0.0445  0.0179  389 VAL D CG1 
10877 C CG2 . VAL D 88  ? 0.4854 0.5741 0.4691 -0.1560 0.0455  0.0293  389 VAL D CG2 
10878 N N   . ASN D 89  ? 0.7046 0.9167 0.7187 -0.1903 0.0619  0.0112  390 ASN D N   
10879 C CA  . ASN D 89  ? 0.7164 0.9775 0.7480 -0.1940 0.0648  0.0037  390 ASN D CA  
10880 C C   . ASN D 89  ? 0.7235 1.0103 0.7590 -0.1918 0.0706  0.0011  390 ASN D C   
10881 O O   . ASN D 89  ? 0.6864 1.0092 0.7400 -0.1793 0.0701  -0.0047 390 ASN D O   
10882 C CB  . ASN D 89  ? 0.8725 1.1423 0.8989 -0.2185 0.0685  0.0016  390 ASN D CB  
10883 C CG  . ASN D 89  ? 0.9852 1.2592 1.0203 -0.2178 0.0629  -0.0011 390 ASN D CG  
10884 O OD1 . ASN D 89  ? 1.0396 1.3485 1.0852 -0.2282 0.0643  -0.0069 390 ASN D OD1 
10885 N ND2 . ASN D 89  ? 0.9645 1.2053 0.9955 -0.2056 0.0564  0.0029  390 ASN D ND2 
10886 N N   . LYS D 90  ? 0.6975 0.9668 0.7152 -0.2041 0.0763  0.0053  391 LYS D N   
10887 C CA  . LYS D 90  ? 0.7329 1.0229 0.7517 -0.2021 0.0821  0.0033  391 LYS D CA  
10888 C C   . LYS D 90  ? 0.6149 0.9087 0.6449 -0.1764 0.0778  0.0016  391 LYS D C   
10889 O O   . LYS D 90  ? 0.6413 0.9714 0.6860 -0.1672 0.0799  -0.0048 391 LYS D O   
10890 C CB  . LYS D 90  ? 0.8022 1.0607 0.7967 -0.2150 0.0868  0.0102  391 LYS D CB  
10891 C CG  . LYS D 90  ? 0.9096 1.1697 0.8903 -0.2428 0.0938  0.0112  391 LYS D CG  
10892 C CD  . LYS D 90  ? 1.0119 1.2370 0.9668 -0.2518 0.0976  0.0191  391 LYS D CD  
10893 C CE  . LYS D 90  ? 1.0498 1.2865 0.9918 -0.2787 0.1067  0.0192  391 LYS D CE  
10894 N NZ  . LYS D 90  ? 1.0801 1.3138 1.0183 -0.2981 0.1073  0.0183  391 LYS D NZ  
10895 N N   . GLU D 91  ? 0.4690 0.7246 0.4911 -0.1647 0.0720  0.0072  392 GLU D N   
10896 C CA  . GLU D 91  ? 0.4804 0.7328 0.5095 -0.1421 0.0678  0.0064  392 GLU D CA  
10897 C C   . GLU D 91  ? 0.5394 0.8205 0.5898 -0.1270 0.0637  0.0001  392 GLU D C   
10898 O O   . GLU D 91  ? 0.5661 0.8662 0.6260 -0.1123 0.0640  -0.0044 392 GLU D O   
10899 C CB  . GLU D 91  ? 0.4970 0.7047 0.5139 -0.1352 0.0621  0.0135  392 GLU D CB  
10900 C CG  . GLU D 91  ? 0.5065 0.6984 0.5165 -0.1233 0.0614  0.0157  392 GLU D CG  
10901 C CD  . GLU D 91  ? 0.6512 0.8008 0.6465 -0.1213 0.0568  0.0233  392 GLU D CD  
10902 O OE1 . GLU D 91  ? 0.7152 0.8518 0.7117 -0.1062 0.0522  0.0243  392 GLU D OE1 
10903 O OE2 . GLU D 91  ? 0.6949 0.8242 0.6770 -0.1350 0.0578  0.0281  392 GLU D OE2 
10904 N N   . ILE D 92  ? 0.5151 0.7988 0.5722 -0.1297 0.0596  -0.0004 393 ILE D N   
10905 C CA  . ILE D 92  ? 0.5933 0.9045 0.6695 -0.1153 0.0553  -0.0058 393 ILE D CA  
10906 C C   . ILE D 92  ? 0.7776 1.1368 0.8670 -0.1165 0.0605  -0.0133 393 ILE D C   
10907 O O   . ILE D 92  ? 0.7783 1.1603 0.8813 -0.0988 0.0584  -0.0182 393 ILE D O   
10908 C CB  . ILE D 92  ? 0.5379 0.8445 0.6176 -0.1200 0.0502  -0.0050 393 ILE D CB  
10909 C CG1 . ILE D 92  ? 0.5013 0.7614 0.5673 -0.1195 0.0459  0.0021  393 ILE D CG1 
10910 C CG2 . ILE D 92  ? 0.4707 0.8025 0.5686 -0.1030 0.0447  -0.0095 393 ILE D CG2 
10911 C CD1 . ILE D 92  ? 0.4800 0.7335 0.5493 -0.1207 0.0404  0.0025  393 ILE D CD1 
10912 N N   . ASP D 93  ? 0.8556 1.2308 0.9404 -0.1373 0.0675  -0.0145 394 ASP D N   
10913 C CA  . ASP D 93  ? 0.8407 1.2654 0.9384 -0.1404 0.0731  -0.0221 394 ASP D CA  
10914 C C   . ASP D 93  ? 0.8027 1.2367 0.9009 -0.1280 0.0769  -0.0248 394 ASP D C   
10915 O O   . ASP D 93  ? 0.8039 1.2738 0.9176 -0.1144 0.0774  -0.0318 394 ASP D O   
10916 C CB  . ASP D 93  ? 0.9249 1.3618 1.0151 -0.1682 0.0801  -0.0224 394 ASP D CB  
10917 C CG  . ASP D 93  ? 0.9837 1.4662 1.0902 -0.1756 0.0807  -0.0291 394 ASP D CG  
10918 O OD1 . ASP D 93  ? 1.0388 1.5310 1.1586 -0.1621 0.0737  -0.0312 394 ASP D OD1 
10919 O OD2 . ASP D 93  ? 0.9387 1.4478 1.0441 -0.1955 0.0880  -0.0322 394 ASP D OD2 
10920 N N   . THR D 94  ? 0.8178 1.2200 0.8987 -0.1322 0.0796  -0.0196 395 THR D N   
10921 C CA  . THR D 94  ? 0.8354 1.2457 0.9145 -0.1232 0.0839  -0.0223 395 THR D CA  
10922 C C   . THR D 94  ? 0.8482 1.2439 0.9315 -0.0977 0.0780  -0.0230 395 THR D C   
10923 O O   . THR D 94  ? 0.9264 1.3399 1.0144 -0.0855 0.0807  -0.0284 395 THR D O   
10924 C CB  . THR D 94  ? 0.8589 1.2419 0.9165 -0.1382 0.0890  -0.0163 395 THR D CB  
10925 O OG1 . THR D 94  ? 0.8979 1.2331 0.9423 -0.1365 0.0831  -0.0081 395 THR D OG1 
10926 C CG2 . THR D 94  ? 0.8859 1.2835 0.9372 -0.1646 0.0959  -0.0158 395 THR D CG2 
10927 N N   . THR D 95  ? 0.8118 1.1751 0.8926 -0.0898 0.0702  -0.0181 396 THR D N   
10928 C CA  . THR D 95  ? 0.7614 1.1047 0.8424 -0.0685 0.0648  -0.0178 396 THR D CA  
10929 C C   . THR D 95  ? 0.7694 1.1118 0.8619 -0.0541 0.0569  -0.0184 396 THR D C   
10930 O O   . THR D 95  ? 0.8523 1.1784 0.9447 -0.0367 0.0524  -0.0184 396 THR D O   
10931 C CB  . THR D 95  ? 0.6595 0.9580 0.7226 -0.0711 0.0629  -0.0102 396 THR D CB  
10932 O OG1 . THR D 95  ? 0.6422 0.9158 0.7016 -0.0766 0.0576  -0.0044 396 THR D OG1 
10933 C CG2 . THR D 95  ? 0.5582 0.8525 0.6068 -0.0871 0.0701  -0.0078 396 THR D CG2 
10934 N N   . SER D 96  ? 0.6629 1.0207 0.7637 -0.0615 0.0551  -0.0189 397 SER D N   
10935 C CA  . SER D 96  ? 0.6716 1.0273 0.7814 -0.0504 0.0474  -0.0185 397 SER D CA  
10936 C C   . SER D 96  ? 0.6180 0.9298 0.7173 -0.0482 0.0416  -0.0114 397 SER D C   
10937 O O   . SER D 96  ? 0.5557 0.8609 0.6605 -0.0365 0.0350  -0.0107 397 SER D O   
10938 C CB  . SER D 96  ? 0.7874 1.1629 0.9093 -0.0278 0.0446  -0.0241 397 SER D CB  
10939 O OG  . SER D 96  ? 0.8851 1.3020 1.0163 -0.0279 0.0506  -0.0312 397 SER D OG  
10940 N N   . THR D 97  ? 0.5968 0.8794 0.6809 -0.0586 0.0437  -0.0062 398 THR D N   
10941 C CA  . THR D 97  ? 0.5279 0.7714 0.6022 -0.0575 0.0385  0.0004  398 THR D CA  
10942 C C   . THR D 97  ? 0.6019 0.8232 0.6603 -0.0742 0.0422  0.0055  398 THR D C   
10943 O O   . THR D 97  ? 0.6343 0.8701 0.6893 -0.0876 0.0486  0.0042  398 THR D O   
10944 C CB  . THR D 97  ? 0.4967 0.7217 0.5690 -0.0398 0.0346  0.0011  398 THR D CB  
10945 O OG1 . THR D 97  ? 0.5460 0.7381 0.6108 -0.0390 0.0293  0.0069  398 THR D OG1 
10946 C CG2 . THR D 97  ? 0.4747 0.6958 0.5385 -0.0394 0.0393  0.0004  398 THR D CG2 
10947 N N   . TYR D 98  ? 0.5460 0.7323 0.5940 -0.0733 0.0383  0.0114  399 TYR D N   
10948 C CA  . TYR D 98  ? 0.4047 0.5664 0.4360 -0.0863 0.0409  0.0169  399 TYR D CA  
10949 C C   . TYR D 98  ? 0.4822 0.6109 0.5043 -0.0774 0.0363  0.0220  399 TYR D C   
10950 O O   . TYR D 98  ? 0.4811 0.6064 0.5097 -0.0632 0.0315  0.0211  399 TYR D O   
10951 C CB  . TYR D 98  ? 0.3938 0.5515 0.4210 -0.1024 0.0419  0.0185  399 TYR D CB  
10952 C CG  . TYR D 98  ? 0.4971 0.6373 0.5258 -0.0989 0.0356  0.0207  399 TYR D CG  
10953 C CD1 . TYR D 98  ? 0.4056 0.5628 0.4490 -0.0897 0.0314  0.0171  399 TYR D CD1 
10954 C CD2 . TYR D 98  ? 0.4903 0.5974 0.5047 -0.1048 0.0341  0.0262  399 TYR D CD2 
10955 C CE1 . TYR D 98  ? 0.3757 0.5178 0.4195 -0.0873 0.0260  0.0189  399 TYR D CE1 
10956 C CE2 . TYR D 98  ? 0.5477 0.6402 0.5631 -0.1017 0.0290  0.0275  399 TYR D CE2 
10957 C CZ  . TYR D 98  ? 0.4803 0.5907 0.5105 -0.0935 0.0251  0.0238  399 TYR D CZ  
10958 O OH  . TYR D 98  ? 0.5272 0.6236 0.5575 -0.0910 0.0203  0.0251  399 TYR D OH  
10959 N N   . GLN D 99  ? 0.5862 0.6908 0.5924 -0.0861 0.0377  0.0274  400 GLN D N   
10960 C CA  . GLN D 99  ? 0.5866 0.6626 0.5831 -0.0788 0.0338  0.0323  400 GLN D CA  
10961 C C   . GLN D 99  ? 0.5899 0.6399 0.5762 -0.0856 0.0315  0.0376  400 GLN D C   
10962 O O   . GLN D 99  ? 0.5837 0.6275 0.5598 -0.0994 0.0352  0.0397  400 GLN D O   
10963 C CB  . GLN D 99  ? 0.6005 0.6709 0.5853 -0.0803 0.0373  0.0342  400 GLN D CB  
10964 C CG  . GLN D 99  ? 0.5155 0.6076 0.5081 -0.0720 0.0395  0.0287  400 GLN D CG  
10965 C CD  . GLN D 99  ? 0.5957 0.6863 0.5977 -0.0559 0.0340  0.0263  400 GLN D CD  
10966 O OE1 . GLN D 99  ? 0.7432 0.8121 0.7394 -0.0499 0.0295  0.0297  400 GLN D OE1 
10967 N NE2 . GLN D 99  ? 0.4857 0.5993 0.5017 -0.0490 0.0340  0.0205  400 GLN D NE2 
10968 N N   . LEU D 100 ? 0.5193 0.5534 0.5071 -0.0761 0.0256  0.0394  401 LEU D N   
10969 C CA  . LEU D 100 ? 0.5274 0.5357 0.5048 -0.0801 0.0232  0.0441  401 LEU D CA  
10970 C C   . LEU D 100 ? 0.5925 0.5787 0.5529 -0.0820 0.0241  0.0497  401 LEU D C   
10971 O O   . LEU D 100 ? 0.5945 0.5807 0.5530 -0.0750 0.0235  0.0504  401 LEU D O   
10972 C CB  . LEU D 100 ? 0.3722 0.3725 0.3564 -0.0690 0.0170  0.0442  401 LEU D CB  
10973 C CG  . LEU D 100 ? 0.3925 0.4113 0.3914 -0.0672 0.0154  0.0397  401 LEU D CG  
10974 C CD1 . LEU D 100 ? 0.4434 0.4564 0.4488 -0.0551 0.0095  0.0398  401 LEU D CD1 
10975 C CD2 . LEU D 100 ? 0.4409 0.4575 0.4367 -0.0795 0.0170  0.0393  401 LEU D CD2 
10976 N N   . LYS D 101 ? 0.5933 0.5598 0.5399 -0.0917 0.0254  0.0536  402 LYS D N   
10977 C CA  . LYS D 101 ? 0.5031 0.4430 0.4324 -0.0904 0.0241  0.0600  402 LYS D CA  
10978 C C   . LYS D 101 ? 0.5814 0.5093 0.5136 -0.0767 0.0176  0.0614  402 LYS D C   
10979 O O   . LYS D 101 ? 0.6010 0.5352 0.5453 -0.0712 0.0145  0.0584  402 LYS D O   
10980 C CB  . LYS D 101 ? 0.5142 0.4321 0.4272 -0.1025 0.0264  0.0637  402 LYS D CB  
10981 C CG  . LYS D 101 ? 0.7126 0.6438 0.6241 -0.1188 0.0328  0.0614  402 LYS D CG  
10982 C CD  . LYS D 101 ? 0.8199 0.7622 0.7260 -0.1235 0.0376  0.0623  402 LYS D CD  
10983 C CE  . LYS D 101 ? 0.8718 0.7991 0.7580 -0.1404 0.0429  0.0664  402 LYS D CE  
10984 N NZ  . LYS D 101 ? 0.9636 0.9164 0.8519 -0.1503 0.0495  0.0637  402 LYS D NZ  
10985 N N   . ASP D 102 ? 0.5825 0.4939 0.5029 -0.0716 0.0156  0.0663  403 ASP D N   
10986 C CA  . ASP D 102 ? 0.5855 0.4876 0.5080 -0.0592 0.0096  0.0677  403 ASP D CA  
10987 C C   . ASP D 102 ? 0.5961 0.4839 0.5176 -0.0582 0.0070  0.0683  403 ASP D C   
10988 O O   . ASP D 102 ? 0.6749 0.5657 0.6061 -0.0497 0.0029  0.0664  403 ASP D O   
10989 C CB  . ASP D 102 ? 0.7138 0.6016 0.6221 -0.0550 0.0079  0.0731  403 ASP D CB  
10990 C CG  . ASP D 102 ? 0.8191 0.7203 0.7266 -0.0562 0.0106  0.0722  403 ASP D CG  
10991 O OD1 . ASP D 102 ? 0.7464 0.6681 0.6649 -0.0592 0.0138  0.0672  403 ASP D OD1 
10992 O OD2 . ASP D 102 ? 0.8837 0.7754 0.7792 -0.0536 0.0093  0.0765  403 ASP D OD2 
10993 N N   . THR D 103 ? 0.6474 0.5186 0.5562 -0.0675 0.0096  0.0706  404 THR D N   
10994 C CA  . THR D 103 ? 0.6319 0.4877 0.5380 -0.0670 0.0076  0.0705  404 THR D CA  
10995 C C   . THR D 103 ? 0.5844 0.4584 0.5076 -0.0677 0.0072  0.0646  404 THR D C   
10996 O O   . THR D 103 ? 0.6128 0.4829 0.5408 -0.0610 0.0036  0.0632  404 THR D O   
10997 C CB  . THR D 103 ? 0.6093 0.4432 0.4971 -0.0788 0.0111  0.0734  404 THR D CB  
10998 O OG1 . THR D 103 ? 0.6998 0.5480 0.5882 -0.0919 0.0167  0.0719  404 THR D OG1 
10999 C CG2 . THR D 103 ? 0.5797 0.3881 0.4481 -0.0745 0.0097  0.0802  404 THR D CG2 
11000 N N   . GLU D 104 ? 0.5758 0.4710 0.5077 -0.0756 0.0108  0.0609  405 GLU D N   
11001 C CA  . GLU D 104 ? 0.6165 0.5310 0.5641 -0.0761 0.0102  0.0556  405 GLU D CA  
11002 C C   . GLU D 104 ? 0.6410 0.5676 0.6023 -0.0631 0.0058  0.0539  405 GLU D C   
11003 O O   . GLU D 104 ? 0.6405 0.5707 0.6100 -0.0591 0.0029  0.0516  405 GLU D O   
11004 C CB  . GLU D 104 ? 0.5730 0.5099 0.5265 -0.0866 0.0150  0.0522  405 GLU D CB  
11005 C CG  . GLU D 104 ? 0.5331 0.4588 0.4719 -0.1020 0.0200  0.0540  405 GLU D CG  
11006 C CD  . GLU D 104 ? 0.5481 0.4971 0.4906 -0.1117 0.0254  0.0515  405 GLU D CD  
11007 O OE1 . GLU D 104 ? 0.6081 0.5554 0.5423 -0.1269 0.0298  0.0513  405 GLU D OE1 
11008 O OE2 . GLU D 104 ? 0.6599 0.6289 0.6130 -0.1046 0.0254  0.0496  405 GLU D OE2 
11009 N N   . LEU D 105 ? 0.6126 0.5442 0.5748 -0.0569 0.0054  0.0550  406 LEU D N   
11010 C CA  . LEU D 105 ? 0.6025 0.5431 0.5753 -0.0458 0.0015  0.0535  406 LEU D CA  
11011 C C   . LEU D 105 ? 0.5988 0.5256 0.5699 -0.0386 -0.0030 0.0553  406 LEU D C   
11012 O O   . LEU D 105 ? 0.5872 0.5209 0.5679 -0.0333 -0.0060 0.0531  406 LEU D O   
11013 C CB  . LEU D 105 ? 0.4983 0.4432 0.4691 -0.0421 0.0022  0.0543  406 LEU D CB  
11014 C CG  . LEU D 105 ? 0.4610 0.4151 0.4413 -0.0324 -0.0010 0.0521  406 LEU D CG  
11015 C CD1 . LEU D 105 ? 0.4115 0.3855 0.4038 -0.0318 0.0004  0.0473  406 LEU D CD1 
11016 C CD2 . LEU D 105 ? 0.4431 0.3932 0.4164 -0.0289 -0.0013 0.0538  406 LEU D CD2 
11017 N N   . ILE D 106 ? 0.6166 0.5244 0.5750 -0.0379 -0.0037 0.0593  407 ILE D N   
11018 C CA  . ILE D 106 ? 0.5151 0.4111 0.4714 -0.0304 -0.0078 0.0607  407 ILE D CA  
11019 C C   . ILE D 106 ? 0.5618 0.4557 0.5216 -0.0329 -0.0080 0.0582  407 ILE D C   
11020 O O   . ILE D 106 ? 0.5245 0.4224 0.4917 -0.0269 -0.0111 0.0565  407 ILE D O   
11021 C CB  . ILE D 106 ? 0.4996 0.3753 0.4401 -0.0285 -0.0083 0.0657  407 ILE D CB  
11022 C CG1 . ILE D 106 ? 0.5462 0.4257 0.4840 -0.0240 -0.0094 0.0680  407 ILE D CG1 
11023 C CG2 . ILE D 106 ? 0.4341 0.2966 0.3710 -0.0216 -0.0116 0.0665  407 ILE D CG2 
11024 C CD1 . ILE D 106 ? 0.4117 0.2729 0.3318 -0.0252 -0.0087 0.0734  407 ILE D CD1 
11025 N N   . TYR D 107 ? 0.5383 0.4261 0.4920 -0.0428 -0.0046 0.0577  408 TYR D N   
11026 C CA  . TYR D 107 ? 0.5758 0.4610 0.5310 -0.0469 -0.0046 0.0548  408 TYR D CA  
11027 C C   . TYR D 107 ? 0.5850 0.4926 0.5563 -0.0460 -0.0057 0.0506  408 TYR D C   
11028 O O   . TYR D 107 ? 0.5823 0.4905 0.5580 -0.0433 -0.0080 0.0485  408 TYR D O   
11029 C CB  . TYR D 107 ? 0.5507 0.4263 0.4954 -0.0598 -0.0003 0.0547  408 TYR D CB  
11030 C CG  . TYR D 107 ? 0.5174 0.3964 0.4657 -0.0667 0.0002  0.0504  408 TYR D CG  
11031 C CD1 . TYR D 107 ? 0.4995 0.4029 0.4604 -0.0723 0.0014  0.0465  408 TYR D CD1 
11032 C CD2 . TYR D 107 ? 0.4066 0.2649 0.3451 -0.0670 -0.0005 0.0500  408 TYR D CD2 
11033 C CE1 . TYR D 107 ? 0.5633 0.4718 0.5275 -0.0788 0.0015  0.0424  408 TYR D CE1 
11034 C CE2 . TYR D 107 ? 0.4083 0.2695 0.3491 -0.0740 0.0000  0.0455  408 TYR D CE2 
11035 C CZ  . TYR D 107 ? 0.5499 0.4368 0.5036 -0.0802 0.0008  0.0419  408 TYR D CZ  
11036 O OH  . TYR D 107 ? 0.6207 0.5117 0.5762 -0.0874 0.0009  0.0374  408 TYR D OH  
11037 N N   . GLY D 108 ? 0.5774 0.5035 0.5568 -0.0478 -0.0042 0.0493  409 GLY D N   
11038 C CA  . GLY D 108 ? 0.4830 0.4296 0.4764 -0.0458 -0.0056 0.0457  409 GLY D CA  
11039 C C   . GLY D 108 ? 0.4973 0.4457 0.4971 -0.0351 -0.0098 0.0460  409 GLY D C   
11040 O O   . GLY D 108 ? 0.5000 0.4554 0.5068 -0.0329 -0.0121 0.0441  409 GLY D O   
11041 N N   . ALA D 109 ? 0.3895 0.3319 0.3859 -0.0291 -0.0109 0.0486  410 ALA D N   
11042 C CA  . ALA D 109 ? 0.4443 0.3889 0.4458 -0.0207 -0.0147 0.0488  410 ALA D CA  
11043 C C   . ALA D 109 ? 0.4119 0.3471 0.4112 -0.0179 -0.0171 0.0492  410 ALA D C   
11044 O O   . ALA D 109 ? 0.4625 0.4034 0.4679 -0.0140 -0.0196 0.0481  410 ALA D O   
11045 C CB  . ALA D 109 ? 0.4431 0.3848 0.4409 -0.0164 -0.0152 0.0509  410 ALA D CB  
11046 N N   . LYS D 110 ? 0.4503 0.3705 0.4398 -0.0196 -0.0161 0.0507  411 LYS D N   
11047 C CA  . LYS D 110 ? 0.4132 0.3244 0.3999 -0.0162 -0.0180 0.0504  411 LYS D CA  
11048 C C   . LYS D 110 ? 0.5731 0.4898 0.5647 -0.0203 -0.0178 0.0470  411 LYS D C   
11049 O O   . LYS D 110 ? 0.5014 0.4208 0.4968 -0.0164 -0.0200 0.0456  411 LYS D O   
11050 C CB  . LYS D 110 ? 0.4155 0.3068 0.3888 -0.0163 -0.0170 0.0526  411 LYS D CB  
11051 C CG  . LYS D 110 ? 0.4872 0.3726 0.4544 -0.0103 -0.0183 0.0564  411 LYS D CG  
11052 C CD  . LYS D 110 ? 0.4482 0.3121 0.4010 -0.0079 -0.0182 0.0590  411 LYS D CD  
11053 C CE  . LYS D 110 ? 0.6038 0.4641 0.5506 -0.0016 -0.0200 0.0630  411 LYS D CE  
11054 N NZ  . LYS D 110 ? 0.6407 0.4821 0.5748 0.0052  -0.0215 0.0656  411 LYS D NZ  
11055 N N   . HIS D 111 ? 0.5573 0.4778 0.5491 -0.0286 -0.0152 0.0454  412 HIS D N   
11056 C CA  . HIS D 111 ? 0.5680 0.4949 0.5639 -0.0332 -0.0153 0.0420  412 HIS D CA  
11057 C C   . HIS D 111 ? 0.5564 0.5026 0.5645 -0.0302 -0.0176 0.0406  412 HIS D C   
11058 O O   . HIS D 111 ? 0.5289 0.4798 0.5404 -0.0301 -0.0192 0.0385  412 HIS D O   
11059 C CB  . HIS D 111 ? 0.5055 0.4306 0.4965 -0.0443 -0.0119 0.0405  412 HIS D CB  
11060 C CG  . HIS D 111 ? 0.5457 0.4479 0.5229 -0.0481 -0.0103 0.0408  412 HIS D CG  
11061 N ND1 . HIS D 111 ? 0.5630 0.4471 0.5288 -0.0460 -0.0094 0.0444  412 HIS D ND1 
11062 C CD2 . HIS D 111 ? 0.5069 0.3995 0.4784 -0.0527 -0.0099 0.0378  412 HIS D CD2 
11063 C CE1 . HIS D 111 ? 0.5902 0.4532 0.5435 -0.0486 -0.0085 0.0439  412 HIS D CE1 
11064 N NE2 . HIS D 111 ? 0.5604 0.4277 0.5168 -0.0530 -0.0086 0.0397  412 HIS D NE2 
11065 N N   . ALA D 112 ? 0.5632 0.5192 0.5766 -0.0272 -0.0177 0.0417  413 ALA D N   
11066 C CA  . ALA D 112 ? 0.5238 0.4932 0.5462 -0.0224 -0.0204 0.0411  413 ALA D CA  
11067 C C   . ALA D 112 ? 0.5043 0.4692 0.5268 -0.0167 -0.0234 0.0420  413 ALA D C   
11068 O O   . ALA D 112 ? 0.4384 0.4108 0.4655 -0.0151 -0.0255 0.0412  413 ALA D O   
11069 C CB  . ALA D 112 ? 0.4406 0.4164 0.4660 -0.0190 -0.0199 0.0420  413 ALA D CB  
11070 N N   . TRP D 113 ? 0.5252 0.4790 0.5422 -0.0135 -0.0236 0.0438  414 TRP D N   
11071 C CA  . TRP D 113 ? 0.4882 0.4401 0.5054 -0.0089 -0.0259 0.0441  414 TRP D CA  
11072 C C   . TRP D 113 ? 0.5006 0.4495 0.5159 -0.0110 -0.0259 0.0419  414 TRP D C   
11073 O O   . TRP D 113 ? 0.5184 0.4731 0.5369 -0.0096 -0.0276 0.0409  414 TRP D O   
11074 C CB  . TRP D 113 ? 0.4670 0.4110 0.4794 -0.0047 -0.0263 0.0461  414 TRP D CB  
11075 C CG  . TRP D 113 ? 0.4914 0.4371 0.5047 -0.0001 -0.0285 0.0462  414 TRP D CG  
11076 C CD1 . TRP D 113 ? 0.4452 0.3983 0.4628 0.0001  -0.0301 0.0451  414 TRP D CD1 
11077 C CD2 . TRP D 113 ? 0.5624 0.5041 0.5721 0.0047  -0.0295 0.0473  414 TRP D CD2 
11078 N NE1 . TRP D 113 ? 0.4175 0.3722 0.4346 0.0038  -0.0314 0.0452  414 TRP D NE1 
11079 C CE2 . TRP D 113 ? 0.5491 0.4979 0.5619 0.0071  -0.0312 0.0464  414 TRP D CE2 
11080 C CE3 . TRP D 113 ? 0.5116 0.4454 0.5151 0.0073  -0.0291 0.0492  414 TRP D CE3 
11081 C CZ2 . TRP D 113 ? 0.5032 0.4540 0.5148 0.0121  -0.0325 0.0467  414 TRP D CZ2 
11082 C CZ3 . TRP D 113 ? 0.4452 0.3798 0.4470 0.0131  -0.0309 0.0499  414 TRP D CZ3 
11083 C CH2 . TRP D 113 ? 0.4835 0.4278 0.4900 0.0155  -0.0326 0.0484  414 TRP D CH2 
11084 N N   . ARG D 114 ? 0.5119 0.4504 0.5206 -0.0147 -0.0237 0.0410  415 ARG D N   
11085 C CA  . ARG D 114 ? 0.4496 0.3826 0.4545 -0.0172 -0.0233 0.0381  415 ARG D CA  
11086 C C   . ARG D 114 ? 0.5477 0.4937 0.5589 -0.0213 -0.0242 0.0357  415 ARG D C   
11087 O O   . ARG D 114 ? 0.5355 0.4818 0.5459 -0.0212 -0.0250 0.0333  415 ARG D O   
11088 C CB  . ARG D 114 ? 0.4122 0.3303 0.4076 -0.0226 -0.0205 0.0376  415 ARG D CB  
11089 C CG  . ARG D 114 ? 0.4367 0.3417 0.4241 -0.0239 -0.0198 0.0346  415 ARG D CG  
11090 C CD  . ARG D 114 ? 0.4912 0.3789 0.4672 -0.0307 -0.0169 0.0345  415 ARG D CD  
11091 N NE  . ARG D 114 ? 0.5374 0.4075 0.5029 -0.0309 -0.0161 0.0315  415 ARG D NE  
11092 C CZ  . ARG D 114 ? 0.5619 0.4116 0.5141 -0.0370 -0.0136 0.0310  415 ARG D CZ  
11093 N NH1 . ARG D 114 ? 0.4558 0.2876 0.3975 -0.0362 -0.0130 0.0278  415 ARG D NH1 
11094 N NH2 . ARG D 114 ? 0.5719 0.4182 0.5203 -0.0439 -0.0115 0.0337  415 ARG D NH2 
11095 N N   . ASN D 115 ? 0.5056 0.4632 0.5225 -0.0242 -0.0241 0.0360  416 ASN D N   
11096 C CA  . ASN D 115 ? 0.4489 0.4204 0.4714 -0.0277 -0.0252 0.0339  416 ASN D CA  
11097 C C   . ASN D 115 ? 0.4071 0.3894 0.4360 -0.0221 -0.0284 0.0353  416 ASN D C   
11098 O O   . ASN D 115 ? 0.4819 0.4766 0.5153 -0.0234 -0.0300 0.0343  416 ASN D O   
11099 C CB  . ASN D 115 ? 0.4305 0.4115 0.4561 -0.0334 -0.0235 0.0330  416 ASN D CB  
11100 C CG  . ASN D 115 ? 0.3770 0.3474 0.3949 -0.0418 -0.0200 0.0315  416 ASN D CG  
11101 O OD1 . ASN D 115 ? 0.4646 0.4212 0.4748 -0.0440 -0.0194 0.0301  416 ASN D OD1 
11102 N ND2 . ASN D 115 ? 0.4416 0.4177 0.4605 -0.0466 -0.0176 0.0316  416 ASN D ND2 
11103 N N   . ALA D 116 ? 0.3743 0.3520 0.4027 -0.0162 -0.0295 0.0378  417 ALA D N   
11104 C CA  . ALA D 116 ? 0.4262 0.4106 0.4582 -0.0119 -0.0322 0.0397  417 ALA D CA  
11105 C C   . ALA D 116 ? 0.4477 0.4341 0.4786 -0.0121 -0.0338 0.0388  417 ALA D C   
11106 O O   . ALA D 116 ? 0.3970 0.3784 0.4252 -0.0102 -0.0338 0.0390  417 ALA D O   
11107 C CB  . ALA D 116 ? 0.4159 0.3947 0.4468 -0.0076 -0.0324 0.0422  417 ALA D CB  
11108 N N   . SER D 117 ? 0.4895 0.4852 0.5227 -0.0144 -0.0352 0.0375  418 SER D N   
11109 C CA  A SER D 117 ? 0.4416 0.4395 0.4726 -0.0158 -0.0364 0.0361  418 SER D CA  
11110 C CA  B SER D 117 ? 0.4557 0.4540 0.4869 -0.0158 -0.0364 0.0361  418 SER D CA  
11111 C C   . SER D 117 ? 0.4889 0.4864 0.5187 -0.0122 -0.0381 0.0387  418 SER D C   
11112 O O   . SER D 117 ? 0.5048 0.5023 0.5318 -0.0129 -0.0380 0.0374  418 SER D O   
11113 C CB  A SER D 117 ? 0.4444 0.4542 0.4779 -0.0188 -0.0381 0.0346  418 SER D CB  
11114 C CB  B SER D 117 ? 0.4292 0.4397 0.4631 -0.0184 -0.0384 0.0350  418 SER D CB  
11115 O OG  A SER D 117 ? 0.3769 0.3947 0.4139 -0.0149 -0.0409 0.0376  418 SER D OG  
11116 O OG  B SER D 117 ? 0.4171 0.4307 0.4524 -0.0234 -0.0367 0.0322  418 SER D OG  
11117 N N   . ARG D 118 ? 0.3740 0.3708 0.4050 -0.0089 -0.0393 0.0420  419 ARG D N   
11118 C CA  . ARG D 118 ? 0.3984 0.3939 0.4268 -0.0074 -0.0408 0.0446  419 ARG D CA  
11119 C C   . ARG D 118 ? 0.4104 0.4004 0.4371 -0.0066 -0.0392 0.0446  419 ARG D C   
11120 O O   . ARG D 118 ? 0.4398 0.4301 0.4643 -0.0067 -0.0400 0.0464  419 ARG D O   
11121 C CB  . ARG D 118 ? 0.4524 0.4473 0.4806 -0.0045 -0.0431 0.0480  419 ARG D CB  
11122 C CG  . ARG D 118 ? 0.4282 0.4304 0.4573 -0.0036 -0.0456 0.0486  419 ARG D CG  
11123 C CD  . ARG D 118 ? 0.4498 0.4490 0.4769 0.0010  -0.0482 0.0521  419 ARG D CD  
11124 N NE  . ARG D 118 ? 0.4700 0.4768 0.4967 0.0029  -0.0514 0.0532  419 ARG D NE  
11125 C CZ  . ARG D 118 ? 0.5588 0.5646 0.5837 0.0086  -0.0543 0.0560  419 ARG D CZ  
11126 N NH1 . ARG D 118 ? 0.6249 0.6208 0.6476 0.0124  -0.0541 0.0575  419 ARG D NH1 
11127 N NH2 . ARG D 118 ? 0.6214 0.6358 0.6459 0.0110  -0.0576 0.0570  419 ARG D NH2 
11128 N N   . CYS D 119 ? 0.4040 0.3895 0.4312 -0.0059 -0.0371 0.0429  420 CYS D N   
11129 C CA  . CYS D 119 ? 0.3864 0.3683 0.4122 -0.0039 -0.0362 0.0432  420 CYS D CA  
11130 C C   . CYS D 119 ? 0.3667 0.3490 0.3908 -0.0030 -0.0350 0.0405  420 CYS D C   
11131 O O   . CYS D 119 ? 0.3449 0.3225 0.3673 -0.0031 -0.0336 0.0380  420 CYS D O   
11132 C CB  . CYS D 119 ? 0.4651 0.4410 0.4911 -0.0024 -0.0350 0.0437  420 CYS D CB  
11133 S SG  . CYS D 119 ? 0.4627 0.4358 0.4866 0.0010  -0.0345 0.0441  420 CYS D SG  
11134 N N   . VAL D 120 ? 0.3527 0.3401 0.3764 -0.0021 -0.0353 0.0407  421 VAL D N   
11135 C CA  . VAL D 120 ? 0.3786 0.3687 0.4010 0.0002  -0.0340 0.0376  421 VAL D CA  
11136 C C   . VAL D 120 ? 0.4704 0.4563 0.4920 0.0053  -0.0332 0.0369  421 VAL D C   
11137 O O   . VAL D 120 ? 0.4276 0.4136 0.4474 0.0092  -0.0321 0.0339  421 VAL D O   
11138 C CB  . VAL D 120 ? 0.4550 0.4558 0.4776 -0.0017 -0.0345 0.0379  421 VAL D CB  
11139 C CG1 . VAL D 120 ? 0.3166 0.3212 0.3403 -0.0020 -0.0353 0.0403  421 VAL D CG1 
11140 C CG2 . VAL D 120 ? 0.3853 0.3918 0.4067 0.0006  -0.0329 0.0337  421 VAL D CG2 
11141 N N   . GLY D 121 ? 0.4164 0.3978 0.4383 0.0061  -0.0337 0.0394  422 GLY D N   
11142 C CA  . GLY D 121 ? 0.3384 0.3168 0.3587 0.0113  -0.0335 0.0394  422 GLY D CA  
11143 C C   . GLY D 121 ? 0.4799 0.4448 0.4958 0.0131  -0.0323 0.0391  422 GLY D C   
11144 O O   . GLY D 121 ? 0.5545 0.5144 0.5677 0.0172  -0.0325 0.0403  422 GLY D O   
11145 N N   . ARG D 122 ? 0.4134 0.3723 0.4276 0.0097  -0.0312 0.0376  423 ARG D N   
11146 C CA  . ARG D 122 ? 0.3939 0.3398 0.4033 0.0083  -0.0298 0.0377  423 ARG D CA  
11147 C C   . ARG D 122 ? 0.4903 0.4236 0.4921 0.0134  -0.0288 0.0362  423 ARG D C   
11148 O O   . ARG D 122 ? 0.4971 0.4169 0.4926 0.0121  -0.0275 0.0371  423 ARG D O   
11149 C CB  . ARG D 122 ? 0.3827 0.3282 0.3926 0.0017  -0.0289 0.0362  423 ARG D CB  
11150 C CG  . ARG D 122 ? 0.4041 0.3577 0.4196 -0.0020 -0.0298 0.0383  423 ARG D CG  
11151 C CD  . ARG D 122 ? 0.5253 0.4816 0.5418 -0.0077 -0.0293 0.0364  423 ARG D CD  
11152 N NE  . ARG D 122 ? 0.4760 0.4409 0.4948 -0.0085 -0.0307 0.0349  423 ARG D NE  
11153 C CZ  . ARG D 122 ? 0.5097 0.4780 0.5284 -0.0130 -0.0307 0.0324  423 ARG D CZ  
11154 N NH1 . ARG D 122 ? 0.4016 0.3656 0.4182 -0.0178 -0.0291 0.0308  423 ARG D NH1 
11155 N NH2 . ARG D 122 ? 0.4923 0.4688 0.5122 -0.0134 -0.0322 0.0316  423 ARG D NH2 
11156 N N   . ILE D 123 ? 0.4455 0.3826 0.4469 0.0194  -0.0292 0.0340  424 ILE D N   
11157 C CA  . ILE D 123 ? 0.4766 0.4003 0.4698 0.0265  -0.0285 0.0327  424 ILE D CA  
11158 C C   . ILE D 123 ? 0.5066 0.4230 0.4961 0.0302  -0.0294 0.0366  424 ILE D C   
11159 O O   . ILE D 123 ? 0.5424 0.4416 0.5222 0.0341  -0.0288 0.0370  424 ILE D O   
11160 C CB  . ILE D 123 ? 0.4688 0.4014 0.4633 0.0343  -0.0289 0.0295  424 ILE D CB  
11161 C CG1 . ILE D 123 ? 0.5613 0.4769 0.5456 0.0428  -0.0282 0.0274  424 ILE D CG1 
11162 C CG2 . ILE D 123 ? 0.4012 0.3502 0.4022 0.0383  -0.0309 0.0316  424 ILE D CG2 
11163 C CD1 . ILE D 123 ? 0.6543 0.5773 0.6388 0.0509  -0.0279 0.0226  424 ILE D CD1 
11164 N N   . GLN D 124 ? 0.5524 0.4801 0.5480 0.0287  -0.0308 0.0396  425 GLN D N   
11165 C CA  . GLN D 124 ? 0.6660 0.5901 0.6585 0.0317  -0.0318 0.0432  425 GLN D CA  
11166 C C   . GLN D 124 ? 0.6398 0.5535 0.6286 0.0251  -0.0304 0.0457  425 GLN D C   
11167 O O   . GLN D 124 ? 0.6183 0.5291 0.6041 0.0265  -0.0311 0.0488  425 GLN D O   
11168 C CB  . GLN D 124 ? 0.6616 0.6035 0.6618 0.0322  -0.0339 0.0444  425 GLN D CB  
11169 C CG  . GLN D 124 ? 0.6480 0.6039 0.6519 0.0384  -0.0353 0.0424  425 GLN D CG  
11170 C CD  . GLN D 124 ? 0.7222 0.6755 0.7212 0.0485  -0.0369 0.0432  425 GLN D CD  
11171 O OE1 . GLN D 124 ? 0.8050 0.7454 0.7970 0.0502  -0.0372 0.0461  425 GLN D OE1 
11172 N NE2 . GLN D 124 ? 0.8390 0.8053 0.8410 0.0554  -0.0379 0.0407  425 GLN D NE2 
11173 N N   . TRP D 125 ? 0.6071 0.5170 0.5962 0.0178  -0.0285 0.0441  426 TRP D N   
11174 C CA  . TRP D 125 ? 0.5247 0.4331 0.5141 0.0105  -0.0271 0.0458  426 TRP D CA  
11175 C C   . TRP D 125 ? 0.6524 0.5462 0.6321 0.0105  -0.0260 0.0487  426 TRP D C   
11176 O O   . TRP D 125 ? 0.6456 0.5417 0.6259 0.0067  -0.0252 0.0507  426 TRP D O   
11177 C CB  . TRP D 125 ? 0.4467 0.3548 0.4374 0.0030  -0.0254 0.0432  426 TRP D CB  
11178 C CG  . TRP D 125 ? 0.4556 0.3461 0.4360 0.0006  -0.0233 0.0417  426 TRP D CG  
11179 C CD1 . TRP D 125 ? 0.5490 0.4321 0.5250 0.0031  -0.0232 0.0385  426 TRP D CD1 
11180 C CD2 . TRP D 125 ? 0.4939 0.3714 0.4660 -0.0058 -0.0210 0.0429  426 TRP D CD2 
11181 N NE1 . TRP D 125 ? 0.5011 0.3649 0.4656 -0.0010 -0.0210 0.0376  426 TRP D NE1 
11182 C CE2 . TRP D 125 ? 0.5455 0.4056 0.5073 -0.0072 -0.0196 0.0406  426 TRP D CE2 
11183 C CE3 . TRP D 125 ? 0.4567 0.3352 0.4282 -0.0107 -0.0196 0.0456  426 TRP D CE3 
11184 C CZ2 . TRP D 125 ? 0.6308 0.4732 0.5810 -0.0145 -0.0169 0.0412  426 TRP D CZ2 
11185 C CZ3 . TRP D 125 ? 0.4276 0.2912 0.3886 -0.0179 -0.0168 0.0463  426 TRP D CZ3 
11186 C CH2 . TRP D 125 ? 0.5921 0.4371 0.5421 -0.0202 -0.0155 0.0443  426 TRP D CH2 
11187 N N   . SER D 126 ? 0.6128 0.4905 0.5823 0.0148  -0.0257 0.0489  427 SER D N   
11188 C CA  . SER D 126 ? 0.6034 0.4647 0.5614 0.0138  -0.0246 0.0523  427 SER D CA  
11189 C C   . SER D 126 ? 0.6503 0.5142 0.6065 0.0212  -0.0270 0.0560  427 SER D C   
11190 O O   . SER D 126 ? 0.5556 0.4074 0.5020 0.0205  -0.0263 0.0595  427 SER D O   
11191 C CB  . SER D 126 ? 0.5759 0.4143 0.5205 0.0150  -0.0234 0.0516  427 SER D CB  
11192 O OG  . SER D 126 ? 0.7087 0.5420 0.6490 0.0271  -0.0258 0.0518  427 SER D OG  
11193 N N   . LYS D 127 ? 0.6416 0.5216 0.6065 0.0273  -0.0297 0.0552  428 LYS D N   
11194 C CA  . LYS D 127 ? 0.6509 0.5373 0.6154 0.0335  -0.0323 0.0579  428 LYS D CA  
11195 C C   . LYS D 127 ? 0.7619 0.6642 0.7354 0.0281  -0.0325 0.0580  428 LYS D C   
11196 O O   . LYS D 127 ? 0.9725 0.8903 0.9548 0.0292  -0.0342 0.0563  428 LYS D O   
11197 C CB  . LYS D 127 ? 0.6893 0.5836 0.6561 0.0436  -0.0351 0.0565  428 LYS D CB  
11198 C CG  . LYS D 127 ? 0.8946 0.7718 0.8497 0.0529  -0.0358 0.0575  428 LYS D CG  
11199 C CD  . LYS D 127 ? 1.0797 0.9702 1.0384 0.0647  -0.0391 0.0563  428 LYS D CD  
11200 C CE  . LYS D 127 ? 1.1974 1.0741 1.1435 0.0762  -0.0414 0.0595  428 LYS D CE  
11201 N NZ  . LYS D 127 ? 1.1911 1.0666 1.1321 0.0753  -0.0430 0.0646  428 LYS D NZ  
11202 N N   . LEU D 128 ? 0.5212 0.4190 0.4918 0.0218  -0.0305 0.0597  429 LEU D N   
11203 C CA  . LEU D 128 ? 0.4853 0.3954 0.4631 0.0170  -0.0301 0.0591  429 LEU D CA  
11204 C C   . LEU D 128 ? 0.5399 0.4456 0.5107 0.0157  -0.0295 0.0621  429 LEU D C   
11205 O O   . LEU D 128 ? 0.5116 0.4047 0.4737 0.0126  -0.0272 0.0640  429 LEU D O   
11206 C CB  . LEU D 128 ? 0.3667 0.2796 0.3503 0.0099  -0.0276 0.0567  429 LEU D CB  
11207 C CG  . LEU D 128 ? 0.3846 0.3080 0.3743 0.0061  -0.0270 0.0559  429 LEU D CG  
11208 C CD1 . LEU D 128 ? 0.3734 0.3082 0.3701 0.0085  -0.0296 0.0547  429 LEU D CD1 
11209 C CD2 . LEU D 128 ? 0.3879 0.3139 0.3815 0.0000  -0.0244 0.0541  429 LEU D CD2 
11210 N N   . GLN D 129 ? 0.5276 0.4431 0.5008 0.0173  -0.0314 0.0623  430 GLN D N   
11211 C CA  . GLN D 129 ? 0.4628 0.3759 0.4291 0.0162  -0.0309 0.0647  430 GLN D CA  
11212 C C   . GLN D 129 ? 0.5197 0.4379 0.4902 0.0095  -0.0280 0.0628  430 GLN D C   
11213 O O   . GLN D 129 ? 0.5975 0.5258 0.5759 0.0087  -0.0287 0.0602  430 GLN D O   
11214 C CB  . GLN D 129 ? 0.5890 0.5109 0.5551 0.0211  -0.0346 0.0654  430 GLN D CB  
11215 C CG  . GLN D 129 ? 0.6458 0.5641 0.6024 0.0212  -0.0348 0.0684  430 GLN D CG  
11216 C CD  . GLN D 129 ? 0.7078 0.6092 0.6520 0.0227  -0.0337 0.0726  430 GLN D CD  
11217 O OE1 . GLN D 129 ? 0.6326 0.5266 0.5723 0.0292  -0.0358 0.0743  430 GLN D OE1 
11218 N NE2 . GLN D 129 ? 0.8048 0.6995 0.7425 0.0166  -0.0304 0.0740  430 GLN D NE2 
11219 N N   . VAL D 130 ? 0.4522 0.3634 0.4170 0.0047  -0.0247 0.0640  431 VAL D N   
11220 C CA  . VAL D 130 ? 0.4878 0.4059 0.4568 -0.0008 -0.0215 0.0618  431 VAL D CA  
11221 C C   . VAL D 130 ? 0.5860 0.5063 0.5494 -0.0011 -0.0210 0.0627  431 VAL D C   
11222 O O   . VAL D 130 ? 0.4728 0.3847 0.4255 -0.0015 -0.0206 0.0662  431 VAL D O   
11223 C CB  . VAL D 130 ? 0.5213 0.4345 0.4882 -0.0072 -0.0177 0.0617  431 VAL D CB  
11224 C CG1 . VAL D 130 ? 0.5519 0.4765 0.5246 -0.0116 -0.0146 0.0588  431 VAL D CG1 
11225 C CG2 . VAL D 130 ? 0.5831 0.4939 0.5545 -0.0071 -0.0184 0.0603  431 VAL D CG2 
11226 N N   . PHE D 131 ? 0.5407 0.4708 0.5099 -0.0009 -0.0212 0.0597  432 PHE D N   
11227 C CA  . PHE D 131 ? 0.4601 0.3930 0.4242 -0.0015 -0.0204 0.0594  432 PHE D CA  
11228 C C   . PHE D 131 ? 0.5004 0.4388 0.4671 -0.0056 -0.0160 0.0566  432 PHE D C   
11229 O O   . PHE D 131 ? 0.5841 0.5294 0.5593 -0.0048 -0.0157 0.0530  432 PHE D O   
11230 C CB  . PHE D 131 ? 0.3984 0.3370 0.3652 0.0015  -0.0237 0.0573  432 PHE D CB  
11231 C CG  . PHE D 131 ? 0.4503 0.3877 0.4140 0.0053  -0.0280 0.0598  432 PHE D CG  
11232 C CD1 . PHE D 131 ? 0.4291 0.3624 0.3828 0.0068  -0.0290 0.0633  432 PHE D CD1 
11233 C CD2 . PHE D 131 ? 0.5042 0.4457 0.4746 0.0076  -0.0309 0.0587  432 PHE D CD2 
11234 C CE1 . PHE D 131 ? 0.4312 0.3659 0.3826 0.0118  -0.0333 0.0655  432 PHE D CE1 
11235 C CE2 . PHE D 131 ? 0.4323 0.3765 0.4009 0.0116  -0.0347 0.0604  432 PHE D CE2 
11236 C CZ  . PHE D 131 ? 0.4754 0.4167 0.4350 0.0142  -0.0360 0.0637  432 PHE D CZ  
11237 N N   . ASP D 132 ? 0.4523 0.3881 0.4111 -0.0098 -0.0127 0.0584  433 ASP D N   
11238 C CA  . ASP D 132 ? 0.4405 0.3845 0.4015 -0.0141 -0.0079 0.0556  433 ASP D CA  
11239 C C   . ASP D 132 ? 0.5277 0.4789 0.4885 -0.0120 -0.0072 0.0522  433 ASP D C   
11240 O O   . ASP D 132 ? 0.6577 0.6063 0.6092 -0.0127 -0.0069 0.0537  433 ASP D O   
11241 C CB  . ASP D 132 ? 0.4298 0.3680 0.3809 -0.0208 -0.0042 0.0590  433 ASP D CB  
11242 C CG  . ASP D 132 ? 0.5336 0.4835 0.4881 -0.0267 0.0012  0.0559  433 ASP D CG  
11243 O OD1 . ASP D 132 ? 0.5408 0.5035 0.5044 -0.0239 0.0021  0.0510  433 ASP D OD1 
11244 O OD2 . ASP D 132 ? 0.5803 0.5262 0.5277 -0.0342 0.0047  0.0583  433 ASP D OD2 
11245 N N   . ALA D 133 ? 0.5088 0.4679 0.4785 -0.0091 -0.0070 0.0476  434 ALA D N   
11246 C CA  . ALA D 133 ? 0.4402 0.4041 0.4088 -0.0065 -0.0061 0.0436  434 ALA D CA  
11247 C C   . ALA D 133 ? 0.4280 0.4034 0.4011 -0.0069 -0.0015 0.0393  434 ALA D C   
11248 O O   . ALA D 133 ? 0.4881 0.4679 0.4637 -0.0025 -0.0009 0.0346  434 ALA D O   
11249 C CB  . ALA D 133 ? 0.4303 0.3911 0.4025 -0.0017 -0.0102 0.0414  434 ALA D CB  
11250 N N   . ARG D 134 ? 0.4169 0.3975 0.3907 -0.0123 0.0021  0.0407  435 ARG D N   
11251 C CA  . ARG D 134 ? 0.4700 0.4657 0.4489 -0.0135 0.0069  0.0366  435 ARG D CA  
11252 C C   . ARG D 134 ? 0.5768 0.5785 0.5491 -0.0141 0.0107  0.0338  435 ARG D C   
11253 O O   . ARG D 134 ? 0.5592 0.5758 0.5362 -0.0135 0.0149  0.0293  435 ARG D O   
11254 C CB  . ARG D 134 ? 0.4482 0.4484 0.4287 -0.0213 0.0096  0.0388  435 ARG D CB  
11255 C CG  . ARG D 134 ? 0.4542 0.4541 0.4438 -0.0200 0.0066  0.0391  435 ARG D CG  
11256 C CD  . ARG D 134 ? 0.4632 0.4662 0.4527 -0.0289 0.0094  0.0407  435 ARG D CD  
11257 N NE  . ARG D 134 ? 0.5087 0.4960 0.4854 -0.0349 0.0098  0.0460  435 ARG D NE  
11258 C CZ  . ARG D 134 ? 0.4980 0.4823 0.4687 -0.0445 0.0130  0.0482  435 ARG D CZ  
11259 N NH1 . ARG D 134 ? 0.5611 0.5601 0.5390 -0.0503 0.0161  0.0452  435 ARG D NH1 
11260 N NH2 . ARG D 134 ? 0.4910 0.4576 0.4479 -0.0485 0.0129  0.0535  435 ARG D NH2 
11261 N N   . ASP D 135 ? 0.5612 0.5533 0.5228 -0.0148 0.0095  0.0361  436 ASP D N   
11262 C CA  . ASP D 135 ? 0.5973 0.5949 0.5517 -0.0150 0.0130  0.0329  436 ASP D CA  
11263 C C   . ASP D 135 ? 0.6085 0.6049 0.5641 -0.0074 0.0111  0.0275  436 ASP D C   
11264 O O   . ASP D 135 ? 0.6283 0.6288 0.5778 -0.0066 0.0139  0.0236  436 ASP D O   
11265 C CB  . ASP D 135 ? 0.5763 0.5650 0.5167 -0.0203 0.0129  0.0380  436 ASP D CB  
11266 C CG  . ASP D 135 ? 0.6148 0.5907 0.5504 -0.0169 0.0068  0.0409  436 ASP D CG  
11267 O OD1 . ASP D 135 ? 0.6714 0.6437 0.6147 -0.0124 0.0027  0.0401  436 ASP D OD1 
11268 O OD2 . ASP D 135 ? 0.6694 0.6400 0.5933 -0.0192 0.0060  0.0441  436 ASP D OD2 
11269 N N   . CYS D 136 ? 0.5946 0.5849 0.5567 -0.0022 0.0067  0.0268  437 CYS D N   
11270 C CA  . CYS D 136 ? 0.5007 0.4855 0.4615 0.0039  0.0045  0.0222  437 CYS D CA  
11271 C C   . CYS D 136 ? 0.5226 0.5171 0.4875 0.0098  0.0082  0.0154  437 CYS D C   
11272 O O   . CYS D 136 ? 0.4533 0.4598 0.4270 0.0110  0.0106  0.0144  437 CYS D O   
11273 C CB  . CYS D 136 ? 0.4558 0.4313 0.4216 0.0066  -0.0008 0.0241  437 CYS D CB  
11274 S SG  . CYS D 136 ? 0.4827 0.4466 0.4435 0.0110  -0.0042 0.0199  437 CYS D SG  
11275 N N   . THR D 137 ? 0.4710 0.4613 0.4292 0.0136  0.0088  0.0101  438 THR D N   
11276 C CA  . THR D 137 ? 0.4331 0.4315 0.3940 0.0211  0.0123  0.0030  438 THR D CA  
11277 C C   . THR D 137 ? 0.5217 0.5066 0.4790 0.0288  0.0096  -0.0019 438 THR D C   
11278 O O   . THR D 137 ? 0.5633 0.5526 0.5236 0.0374  0.0117  -0.0076 438 THR D O   
11279 C CB  . THR D 137 ? 0.5617 0.5714 0.5163 0.0189  0.0182  -0.0007 438 THR D CB  
11280 O OG1 . THR D 137 ? 0.4746 0.4736 0.4170 0.0182  0.0173  -0.0031 438 THR D OG1 
11281 C CG2 . THR D 137 ? 0.5523 0.5716 0.5067 0.0094  0.0209  0.0048  438 THR D CG2 
11282 N N   . THR D 138 ? 0.5072 0.4758 0.4575 0.0262  0.0052  -0.0002 439 THR D N   
11283 C CA  . THR D 138 ? 0.5285 0.4817 0.4725 0.0315  0.0030  -0.0050 439 THR D CA  
11284 C C   . THR D 138 ? 0.5382 0.4777 0.4819 0.0282  -0.0027 -0.0006 439 THR D C   
11285 O O   . THR D 138 ? 0.6250 0.5669 0.5713 0.0218  -0.0050 0.0054  439 THR D O   
11286 C CB  . THR D 138 ? 0.4518 0.3988 0.3827 0.0299  0.0046  -0.0102 439 THR D CB  
11287 O OG1 . THR D 138 ? 0.4646 0.4076 0.3897 0.0210  0.0015  -0.0058 439 THR D OG1 
11288 C CG2 . THR D 138 ? 0.4748 0.4371 0.4046 0.0316  0.0107  -0.0144 439 THR D CG2 
11289 N N   . ALA D 139 ? 0.5842 0.5082 0.5232 0.0328  -0.0050 -0.0039 440 ALA D N   
11290 C CA  . ALA D 139 ? 0.5913 0.5025 0.5293 0.0291  -0.0100 -0.0002 440 ALA D CA  
11291 C C   . ALA D 139 ? 0.6274 0.5361 0.5591 0.0196  -0.0123 0.0020  440 ALA D C   
11292 O O   . ALA D 139 ? 0.4926 0.4024 0.4283 0.0147  -0.0156 0.0073  440 ALA D O   
11293 C CB  . ALA D 139 ? 0.5544 0.4468 0.4852 0.0347  -0.0115 -0.0043 440 ALA D CB  
11294 N N   . HIS D 140 ? 0.6278 0.5352 0.5497 0.0173  -0.0107 -0.0023 441 HIS D N   
11295 C CA  . HIS D 140 ? 0.5249 0.4343 0.4412 0.0088  -0.0130 -0.0001 441 HIS D CA  
11296 C C   . HIS D 140 ? 0.5628 0.4860 0.4869 0.0059  -0.0135 0.0069  441 HIS D C   
11297 O O   . HIS D 140 ? 0.5099 0.4343 0.4347 0.0010  -0.0173 0.0111  441 HIS D O   
11298 C CB  . HIS D 140 ? 0.5373 0.4461 0.4421 0.0074  -0.0107 -0.0058 441 HIS D CB  
11299 C CG  . HIS D 140 ? 0.5088 0.4004 0.4020 0.0065  -0.0118 -0.0122 441 HIS D CG  
11300 N ND1 . HIS D 140 ? 0.5611 0.4408 0.4504 0.0139  -0.0095 -0.0182 441 HIS D ND1 
11301 C CD2 . HIS D 140 ? 0.4590 0.3428 0.3431 -0.0014 -0.0152 -0.0136 441 HIS D CD2 
11302 C CE1 . HIS D 140 ? 0.5687 0.4308 0.4453 0.0104  -0.0112 -0.0230 441 HIS D CE1 
11303 N NE2 . HIS D 140 ? 0.4943 0.3594 0.3679 0.0003  -0.0147 -0.0204 441 HIS D NE2 
11304 N N   . GLY D 141 ? 0.5463 0.4800 0.4757 0.0088  -0.0097 0.0079  442 GLY D N   
11305 C CA  . GLY D 141 ? 0.5102 0.4533 0.4453 0.0059  -0.0099 0.0145  442 GLY D CA  
11306 C C   . GLY D 141 ? 0.5700 0.5112 0.5137 0.0059  -0.0133 0.0191  442 GLY D C   
11307 O O   . GLY D 141 ? 0.5079 0.4510 0.4525 0.0025  -0.0160 0.0241  442 GLY D O   
11308 N N   . MET D 142 ? 0.5457 0.4831 0.4952 0.0103  -0.0133 0.0174  443 MET D N   
11309 C CA  . MET D 142 ? 0.5233 0.4588 0.4801 0.0102  -0.0165 0.0213  443 MET D CA  
11310 C C   . MET D 142 ? 0.5198 0.4489 0.4727 0.0056  -0.0208 0.0228  443 MET D C   
11311 O O   . MET D 142 ? 0.4430 0.3754 0.4005 0.0033  -0.0233 0.0273  443 MET D O   
11312 C CB  . MET D 142 ? 0.4288 0.3601 0.3899 0.0161  -0.0162 0.0189  443 MET D CB  
11313 C CG  . MET D 142 ? 0.4241 0.3662 0.3914 0.0209  -0.0122 0.0173  443 MET D CG  
11314 S SD  . MET D 142 ? 0.5721 0.5104 0.5433 0.0302  -0.0124 0.0139  443 MET D SD  
11315 C CE  . MET D 142 ? 0.4497 0.3895 0.4299 0.0286  -0.0159 0.0198  443 MET D CE  
11316 N N   . PHE D 143 ? 0.4384 0.3590 0.3824 0.0040  -0.0217 0.0187  444 PHE D N   
11317 C CA  . PHE D 143 ? 0.4807 0.3975 0.4204 -0.0020 -0.0257 0.0194  444 PHE D CA  
11318 C C   . PHE D 143 ? 0.5703 0.4979 0.5102 -0.0056 -0.0274 0.0231  444 PHE D C   
11319 O O   . PHE D 143 ? 0.6259 0.5575 0.5692 -0.0082 -0.0306 0.0264  444 PHE D O   
11320 C CB  . PHE D 143 ? 0.5608 0.4660 0.4890 -0.0042 -0.0258 0.0135  444 PHE D CB  
11321 C CG  . PHE D 143 ? 0.5600 0.4635 0.4827 -0.0122 -0.0295 0.0133  444 PHE D CG  
11322 C CD1 . PHE D 143 ? 0.5131 0.4111 0.4373 -0.0156 -0.0321 0.0148  444 PHE D CD1 
11323 C CD2 . PHE D 143 ? 0.4889 0.3979 0.4047 -0.0169 -0.0304 0.0116  444 PHE D CD2 
11324 C CE1 . PHE D 143 ? 0.5297 0.4289 0.4492 -0.0242 -0.0352 0.0143  444 PHE D CE1 
11325 C CE2 . PHE D 143 ? 0.5438 0.4546 0.4552 -0.0248 -0.0341 0.0111  444 PHE D CE2 
11326 C CZ  . PHE D 143 ? 0.5965 0.5030 0.5100 -0.0288 -0.0363 0.0123  444 PHE D CZ  
11327 N N   . ASN D 144 ? 0.5200 0.4526 0.4555 -0.0052 -0.0253 0.0227  445 ASN D N   
11328 C CA  . ASN D 144 ? 0.5382 0.4795 0.4721 -0.0072 -0.0270 0.0270  445 ASN D CA  
11329 C C   . ASN D 144 ? 0.5189 0.4645 0.4614 -0.0051 -0.0277 0.0328  445 ASN D C   
11330 O O   . ASN D 144 ? 0.5289 0.4791 0.4725 -0.0060 -0.0311 0.0362  445 ASN D O   
11331 C CB  . ASN D 144 ? 0.5160 0.4604 0.4428 -0.0069 -0.0239 0.0260  445 ASN D CB  
11332 C CG  . ASN D 144 ? 0.5526 0.5038 0.4744 -0.0087 -0.0263 0.0305  445 ASN D CG  
11333 O OD1 . ASN D 144 ? 0.6213 0.5757 0.5406 -0.0111 -0.0306 0.0309  445 ASN D OD1 
11334 N ND2 . ASN D 144 ? 0.6272 0.5808 0.5471 -0.0076 -0.0237 0.0340  445 ASN D ND2 
11335 N N   . TYR D 145 ? 0.5254 0.4702 0.4737 -0.0022 -0.0246 0.0335  446 TYR D N   
11336 C CA  . TYR D 145 ? 0.5211 0.4682 0.4765 -0.0010 -0.0250 0.0382  446 TYR D CA  
11337 C C   . TYR D 145 ? 0.5124 0.4587 0.4736 -0.0011 -0.0284 0.0391  446 TYR D C   
11338 O O   . TYR D 145 ? 0.4930 0.4423 0.4572 -0.0007 -0.0305 0.0428  446 TYR D O   
11339 C CB  . TYR D 145 ? 0.5423 0.4903 0.5028 0.0009  -0.0210 0.0378  446 TYR D CB  
11340 C CG  . TYR D 145 ? 0.4736 0.4248 0.4300 -0.0004 -0.0176 0.0397  446 TYR D CG  
11341 C CD1 . TYR D 145 ? 0.4255 0.3760 0.3799 -0.0016 -0.0183 0.0449  446 TYR D CD1 
11342 C CD2 . TYR D 145 ? 0.4080 0.3625 0.3618 -0.0003 -0.0134 0.0360  446 TYR D CD2 
11343 C CE1 . TYR D 145 ? 0.4497 0.4007 0.3983 -0.0040 -0.0151 0.0472  446 TYR D CE1 
11344 C CE2 . TYR D 145 ? 0.3779 0.3362 0.3274 -0.0029 -0.0097 0.0379  446 TYR D CE2 
11345 C CZ  . TYR D 145 ? 0.4311 0.3866 0.3773 -0.0054 -0.0106 0.0438  446 TYR D CZ  
11346 O OH  . TYR D 145 ? 0.5300 0.4867 0.4696 -0.0091 -0.0070 0.0462  446 TYR D OH  
11347 N N   . ILE D 146 ? 0.4855 0.4270 0.4474 -0.0016 -0.0290 0.0358  447 ILE D N   
11348 C CA  . ILE D 146 ? 0.5007 0.4415 0.4675 -0.0027 -0.0317 0.0369  447 ILE D CA  
11349 C C   . ILE D 146 ? 0.4836 0.4291 0.4475 -0.0064 -0.0352 0.0376  447 ILE D C   
11350 O O   . ILE D 146 ? 0.3947 0.3454 0.3636 -0.0068 -0.0374 0.0400  447 ILE D O   
11351 C CB  . ILE D 146 ? 0.4402 0.3722 0.4067 -0.0021 -0.0312 0.0339  447 ILE D CB  
11352 C CG1 . ILE D 146 ? 0.4327 0.3647 0.4045 0.0029  -0.0283 0.0339  447 ILE D CG1 
11353 C CG2 . ILE D 146 ? 0.4974 0.4275 0.4658 -0.0050 -0.0340 0.0351  447 ILE D CG2 
11354 C CD1 . ILE D 146 ? 0.4723 0.3956 0.4427 0.0061  -0.0277 0.0307  447 ILE D CD1 
11355 N N   . CYS D 147 ? 0.5945 0.5405 0.5507 -0.0092 -0.0359 0.0351  448 CYS D N   
11356 C CA  . CYS D 147 ? 0.4611 0.4155 0.4150 -0.0129 -0.0396 0.0356  448 CYS D CA  
11357 C C   . CYS D 147 ? 0.4959 0.4599 0.4531 -0.0093 -0.0411 0.0402  448 CYS D C   
11358 O O   . CYS D 147 ? 0.5627 0.5354 0.5235 -0.0096 -0.0441 0.0417  448 CYS D O   
11359 C CB  . CYS D 147 ? 0.5302 0.4840 0.4744 -0.0167 -0.0400 0.0319  448 CYS D CB  
11360 S SG  . CYS D 147 ? 0.5127 0.4535 0.4502 -0.0220 -0.0393 0.0259  448 CYS D SG  
11361 N N   . ASN D 148 ? 0.4983 0.4603 0.4531 -0.0057 -0.0391 0.0423  449 ASN D N   
11362 C CA  . ASN D 148 ? 0.4395 0.4063 0.3947 -0.0017 -0.0406 0.0471  449 ASN D CA  
11363 C C   . ASN D 148 ? 0.4088 0.3751 0.3723 0.0010  -0.0406 0.0493  449 ASN D C   
11364 O O   . ASN D 148 ? 0.4525 0.4246 0.4179 0.0042  -0.0431 0.0519  449 ASN D O   
11365 C CB  . ASN D 148 ? 0.3492 0.3114 0.2982 0.0000  -0.0379 0.0493  449 ASN D CB  
11366 C CG  . ASN D 148 ? 0.5313 0.4954 0.4707 -0.0025 -0.0380 0.0472  449 ASN D CG  
11367 O OD1 . ASN D 148 ? 0.4504 0.4207 0.3871 -0.0050 -0.0412 0.0450  449 ASN D OD1 
11368 N ND2 . ASN D 148 ? 0.4773 0.4370 0.4111 -0.0025 -0.0345 0.0478  449 ASN D ND2 
11369 N N   . HIS D 149 ? 0.4805 0.4406 0.4487 0.0005  -0.0378 0.0480  450 HIS D N   
11370 C CA  . HIS D 149 ? 0.4330 0.3931 0.4086 0.0022  -0.0379 0.0494  450 HIS D CA  
11371 C C   . HIS D 149 ? 0.4104 0.3783 0.3893 0.0008  -0.0411 0.0488  450 HIS D C   
11372 O O   . HIS D 149 ? 0.4648 0.4382 0.4470 0.0039  -0.0428 0.0508  450 HIS D O   
11373 C CB  . HIS D 149 ? 0.4071 0.3614 0.3867 0.0014  -0.0351 0.0477  450 HIS D CB  
11374 C CG  . HIS D 149 ? 0.5196 0.4741 0.5061 0.0027  -0.0351 0.0489  450 HIS D CG  
11375 N ND1 . HIS D 149 ? 0.4678 0.4191 0.4575 0.0037  -0.0326 0.0494  450 HIS D ND1 
11376 C CD2 . HIS D 149 ? 0.4699 0.4286 0.4605 0.0024  -0.0373 0.0493  450 HIS D CD2 
11377 C CE1 . HIS D 149 ? 0.5603 0.5129 0.5553 0.0043  -0.0333 0.0500  450 HIS D CE1 
11378 N NE2 . HIS D 149 ? 0.4764 0.4332 0.4719 0.0037  -0.0360 0.0500  450 HIS D NE2 
11379 N N   . VAL D 150 ? 0.4375 0.4060 0.4150 -0.0040 -0.0420 0.0457  451 VAL D N   
11380 C CA  . VAL D 150 ? 0.3885 0.3649 0.3688 -0.0074 -0.0445 0.0449  451 VAL D CA  
11381 C C   . VAL D 150 ? 0.4885 0.4786 0.4689 -0.0057 -0.0476 0.0460  451 VAL D C   
11382 O O   . VAL D 150 ? 0.4734 0.4731 0.4590 -0.0040 -0.0491 0.0469  451 VAL D O   
11383 C CB  . VAL D 150 ? 0.4123 0.3839 0.3880 -0.0143 -0.0446 0.0414  451 VAL D CB  
11384 C CG1 . VAL D 150 ? 0.3720 0.3549 0.3485 -0.0200 -0.0474 0.0403  451 VAL D CG1 
11385 C CG2 . VAL D 150 ? 0.4255 0.3849 0.4023 -0.0144 -0.0424 0.0408  451 VAL D CG2 
11386 N N   . LYS D 151 ? 0.4932 0.4854 0.4675 -0.0054 -0.0486 0.0460  452 LYS D N   
11387 C CA  . LYS D 151 ? 0.4649 0.4714 0.4384 -0.0029 -0.0522 0.0471  452 LYS D CA  
11388 C C   . LYS D 151 ? 0.3989 0.4070 0.3755 0.0058  -0.0528 0.0509  452 LYS D C   
11389 O O   . LYS D 151 ? 0.4216 0.4429 0.4021 0.0092  -0.0555 0.0514  452 LYS D O   
11390 C CB  . LYS D 151 ? 0.4575 0.4643 0.4225 -0.0039 -0.0532 0.0466  452 LYS D CB  
11391 C CG  . LYS D 151 ? 0.4266 0.4492 0.3897 -0.0009 -0.0575 0.0479  452 LYS D CG  
11392 C CD  . LYS D 151 ? 0.4291 0.4527 0.3829 -0.0047 -0.0585 0.0462  452 LYS D CD  
11393 C CE  . LYS D 151 ? 0.4822 0.5250 0.4342 -0.0030 -0.0636 0.0468  452 LYS D CE  
11394 N NZ  . LYS D 151 ? 0.5127 0.5591 0.4562 -0.0096 -0.0649 0.0436  452 LYS D NZ  
11395 N N   . TYR D 152 ? 0.3834 0.3782 0.3576 0.0093  -0.0501 0.0534  453 TYR D N   
11396 C CA  . TYR D 152 ? 0.4834 0.4747 0.4581 0.0168  -0.0502 0.0569  453 TYR D CA  
11397 C C   . TYR D 152 ? 0.4518 0.4463 0.4346 0.0181  -0.0499 0.0560  453 TYR D C   
11398 O O   . TYR D 152 ? 0.4529 0.4534 0.4375 0.0245  -0.0518 0.0572  453 TYR D O   
11399 C CB  . TYR D 152 ? 0.4523 0.4280 0.4221 0.0175  -0.0467 0.0591  453 TYR D CB  
11400 C CG  . TYR D 152 ? 0.5342 0.5024 0.5034 0.0234  -0.0462 0.0621  453 TYR D CG  
11401 C CD1 . TYR D 152 ? 0.5622 0.5277 0.5239 0.0301  -0.0483 0.0658  453 TYR D CD1 
11402 C CD2 . TYR D 152 ? 0.5700 0.5331 0.5450 0.0227  -0.0439 0.0612  453 TYR D CD2 
11403 C CE1 . TYR D 152 ? 0.5702 0.5258 0.5294 0.0358  -0.0479 0.0683  453 TYR D CE1 
11404 C CE2 . TYR D 152 ? 0.5582 0.5132 0.5313 0.0276  -0.0434 0.0632  453 TYR D CE2 
11405 C CZ  . TYR D 152 ? 0.5727 0.5228 0.5376 0.0341  -0.0454 0.0667  453 TYR D CZ  
11406 O OH  . TYR D 152 ? 0.6266 0.5651 0.5875 0.0393  -0.0448 0.0686  453 TYR D OH  
11407 N N   . ALA D 153 ? 0.4779 0.4678 0.4650 0.0129  -0.0475 0.0539  454 ALA D N   
11408 C CA  . ALA D 153 ? 0.4847 0.4769 0.4785 0.0133  -0.0469 0.0532  454 ALA D CA  
11409 C C   . ALA D 153 ? 0.4684 0.4774 0.4665 0.0125  -0.0496 0.0515  454 ALA D C   
11410 O O   . ALA D 153 ? 0.5111 0.5266 0.5133 0.0171  -0.0501 0.0516  454 ALA D O   
11411 C CB  . ALA D 153 ? 0.2866 0.2711 0.2828 0.0079  -0.0444 0.0516  454 ALA D CB  
11412 N N   . THR D 154 ? 0.4985 0.5154 0.4952 0.0065  -0.0511 0.0496  455 THR D N   
11413 C CA  . THR D 154 ? 0.4034 0.4380 0.4041 0.0029  -0.0532 0.0475  455 THR D CA  
11414 C C   . THR D 154 ? 0.5336 0.5845 0.5363 0.0106  -0.0562 0.0482  455 THR D C   
11415 O O   . THR D 154 ? 0.6004 0.6662 0.6089 0.0121  -0.0570 0.0469  455 THR D O   
11416 C CB  . THR D 154 ? 0.4625 0.4995 0.4593 -0.0068 -0.0539 0.0450  455 THR D CB  
11417 O OG1 . THR D 154 ? 0.5085 0.5294 0.5029 -0.0124 -0.0513 0.0442  455 THR D OG1 
11418 C CG2 . THR D 154 ? 0.3964 0.4533 0.3967 -0.0125 -0.0559 0.0426  455 THR D CG2 
11419 N N   . ASN D 155 ? 0.5614 0.6104 0.5586 0.0161  -0.0579 0.0502  456 ASN D N   
11420 C CA  . ASN D 155 ? 0.3482 0.4088 0.3453 0.0262  -0.0612 0.0519  456 ASN D CA  
11421 C C   . ASN D 155 ? 0.4484 0.5358 0.4520 0.0256  -0.0640 0.0491  456 ASN D C   
11422 O O   . ASN D 155 ? 0.5029 0.6019 0.5104 0.0348  -0.0656 0.0493  456 ASN D O   
11423 C CB  . ASN D 155 ? 0.3455 0.3945 0.3425 0.0359  -0.0598 0.0543  456 ASN D CB  
11424 C CG  . ASN D 155 ? 0.4628 0.5153 0.4554 0.0480  -0.0631 0.0570  456 ASN D CG  
11425 O OD1 . ASN D 155 ? 0.5999 0.6539 0.5863 0.0496  -0.0655 0.0589  456 ASN D OD1 
11426 N ND2 . ASN D 155 ? 0.4378 0.4910 0.4326 0.0573  -0.0632 0.0572  456 ASN D ND2 
11427 N N   . LYS D 156 ? 0.4508 0.5485 0.4551 0.0145  -0.0646 0.0462  457 LYS D N   
11428 C CA  . LYS D 156 ? 0.3769 0.5023 0.3870 0.0108  -0.0670 0.0431  457 LYS D CA  
11429 C C   . LYS D 156 ? 0.4173 0.5522 0.4355 0.0114  -0.0653 0.0415  457 LYS D C   
11430 O O   . LYS D 156 ? 0.3843 0.5449 0.4086 0.0137  -0.0673 0.0394  457 LYS D O   
11431 C CB  . LYS D 156 ? 0.4230 0.5679 0.4328 0.0197  -0.0717 0.0438  457 LYS D CB  
11432 C CG  . LYS D 156 ? 0.5933 0.7376 0.5955 0.0150  -0.0740 0.0439  457 LYS D CG  
11433 C CD  . LYS D 156 ? 0.7676 0.9425 0.7722 0.0168  -0.0791 0.0422  457 LYS D CD  
11434 C CE  . LYS D 156 ? 0.9177 1.0963 0.9200 0.0336  -0.0827 0.0461  457 LYS D CE  
11435 N NZ  . LYS D 156 ? 0.9262 1.0872 0.9172 0.0359  -0.0837 0.0497  457 LYS D NZ  
11436 N N   . GLY D 157 ? 0.4286 0.5446 0.4469 0.0094  -0.0616 0.0422  458 GLY D N   
11437 C CA  . GLY D 157 ? 0.4643 0.5870 0.4888 0.0090  -0.0596 0.0408  458 GLY D CA  
11438 C C   . GLY D 157 ? 0.4927 0.6068 0.5187 0.0214  -0.0585 0.0424  458 GLY D C   
11439 O O   . GLY D 157 ? 0.4638 0.5774 0.4936 0.0208  -0.0562 0.0413  458 GLY D O   
11440 N N   . ASN D 158 ? 0.4514 0.5573 0.4733 0.0319  -0.0602 0.0449  459 ASN D N   
11441 C CA  . ASN D 158 ? 0.5405 0.6335 0.5612 0.0429  -0.0590 0.0464  459 ASN D CA  
11442 C C   . ASN D 158 ? 0.5859 0.6511 0.6011 0.0395  -0.0561 0.0487  459 ASN D C   
11443 O O   . ASN D 158 ? 0.6474 0.6977 0.6558 0.0436  -0.0564 0.0516  459 ASN D O   
11444 C CB  . ASN D 158 ? 0.5455 0.6431 0.5628 0.0564  -0.0624 0.0481  459 ASN D CB  
11445 C CG  . ASN D 158 ? 0.5890 0.6707 0.6030 0.0676  -0.0612 0.0494  459 ASN D CG  
11446 O OD1 . ASN D 158 ? 0.6511 0.7251 0.6675 0.0658  -0.0581 0.0478  459 ASN D OD1 
11447 N ND2 . ASN D 158 ? 0.5141 0.5891 0.5210 0.0792  -0.0638 0.0522  459 ASN D ND2 
11448 N N   . LEU D 159 ? 0.5401 0.5995 0.5581 0.0317  -0.0532 0.0474  460 LEU D N   
11449 C CA  . LEU D 159 ? 0.5273 0.5661 0.5416 0.0261  -0.0508 0.0489  460 LEU D CA  
11450 C C   . LEU D 159 ? 0.5234 0.5438 0.5334 0.0326  -0.0492 0.0510  460 LEU D C   
11451 O O   . LEU D 159 ? 0.4795 0.4989 0.4901 0.0397  -0.0489 0.0506  460 LEU D O   
11452 C CB  . LEU D 159 ? 0.4838 0.5217 0.5016 0.0176  -0.0487 0.0474  460 LEU D CB  
11453 C CG  . LEU D 159 ? 0.6267 0.6801 0.6468 0.0091  -0.0497 0.0454  460 LEU D CG  
11454 C CD1 . LEU D 159 ? 0.5790 0.6308 0.6010 0.0017  -0.0477 0.0444  460 LEU D CD1 
11455 C CD2 . LEU D 159 ? 0.5036 0.5532 0.5190 0.0033  -0.0508 0.0456  460 LEU D CD2 
11456 N N   . ARG D 160 ? 0.4279 0.4335 0.4331 0.0296  -0.0480 0.0529  461 ARG D N   
11457 C CA  . ARG D 160 ? 0.4615 0.4493 0.4612 0.0331  -0.0462 0.0550  461 ARG D CA  
11458 C C   . ARG D 160 ? 0.4904 0.4677 0.4905 0.0260  -0.0433 0.0548  461 ARG D C   
11459 O O   . ARG D 160 ? 0.4643 0.4430 0.4646 0.0204  -0.0431 0.0543  461 ARG D O   
11460 C CB  . ARG D 160 ? 0.4963 0.4783 0.4878 0.0375  -0.0476 0.0581  461 ARG D CB  
11461 C CG  . ARG D 160 ? 0.4605 0.4533 0.4507 0.0461  -0.0512 0.0587  461 ARG D CG  
11462 C CD  . ARG D 160 ? 0.5163 0.5014 0.4968 0.0504  -0.0528 0.0624  461 ARG D CD  
11463 N NE  . ARG D 160 ? 0.4738 0.4655 0.4530 0.0446  -0.0538 0.0625  461 ARG D NE  
11464 C CZ  . ARG D 160 ? 0.5585 0.5512 0.5302 0.0484  -0.0564 0.0651  461 ARG D CZ  
11465 N NH1 . ARG D 160 ? 0.5874 0.5740 0.5524 0.0585  -0.0584 0.0684  461 ARG D NH1 
11466 N NH2 . ARG D 160 ? 0.4819 0.4808 0.4518 0.0426  -0.0573 0.0646  461 ARG D NH2 
11467 N N   . SER D 161 ? 0.4512 0.4180 0.4508 0.0264  -0.0411 0.0549  462 SER D N   
11468 C CA  . SER D 161 ? 0.5365 0.4965 0.5375 0.0205  -0.0385 0.0544  462 SER D CA  
11469 C C   . SER D 161 ? 0.4666 0.4181 0.4622 0.0185  -0.0371 0.0561  462 SER D C   
11470 O O   . SER D 161 ? 0.4802 0.4239 0.4690 0.0215  -0.0369 0.0583  462 SER D O   
11471 C CB  . SER D 161 ? 0.6092 0.5628 0.6111 0.0208  -0.0368 0.0535  462 SER D CB  
11472 O OG  . SER D 161 ? 0.7529 0.7141 0.7581 0.0241  -0.0379 0.0519  462 SER D OG  
11473 N N   . ALA D 162 ? 0.4704 0.4228 0.4684 0.0137  -0.0358 0.0551  463 ALA D N   
11474 C CA  . ALA D 162 ? 0.4756 0.4229 0.4689 0.0117  -0.0341 0.0559  463 ALA D CA  
11475 C C   . ALA D 162 ? 0.4584 0.4063 0.4557 0.0078  -0.0321 0.0540  463 ALA D C   
11476 O O   . ALA D 162 ? 0.4927 0.4447 0.4949 0.0068  -0.0330 0.0525  463 ALA D O   
11477 C CB  . ALA D 162 ? 0.3930 0.3444 0.3824 0.0124  -0.0360 0.0564  463 ALA D CB  
11478 N N   . ILE D 163 ? 0.5480 0.4923 0.5425 0.0060  -0.0294 0.0543  464 ILE D N   
11479 C CA  . ILE D 163 ? 0.4957 0.4425 0.4937 0.0037  -0.0274 0.0522  464 ILE D CA  
11480 C C   . ILE D 163 ? 0.5456 0.4917 0.5385 0.0026  -0.0253 0.0521  464 ILE D C   
11481 O O   . ILE D 163 ? 0.5962 0.5382 0.5827 0.0020  -0.0244 0.0543  464 ILE D O   
11482 C CB  . ILE D 163 ? 0.3524 0.2994 0.3542 0.0017  -0.0255 0.0517  464 ILE D CB  
11483 C CG1 . ILE D 163 ? 0.3535 0.3066 0.3602 0.0010  -0.0240 0.0493  464 ILE D CG1 
11484 C CG2 . ILE D 163 ? 0.4125 0.3534 0.4086 -0.0006 -0.0232 0.0535  464 ILE D CG2 
11485 C CD1 . ILE D 163 ? 0.4276 0.3847 0.4394 -0.0011 -0.0228 0.0483  464 ILE D CD1 
11486 N N   . THR D 164 ? 0.5467 0.4960 0.5412 0.0028  -0.0247 0.0495  465 THR D N   
11487 C CA  . THR D 164 ? 0.4578 0.4080 0.4480 0.0020  -0.0222 0.0483  465 THR D CA  
11488 C C   . THR D 164 ? 0.4573 0.4128 0.4525 0.0019  -0.0194 0.0457  465 THR D C   
11489 O O   . THR D 164 ? 0.4797 0.4370 0.4795 0.0044  -0.0205 0.0436  465 THR D O   
11490 C CB  . THR D 164 ? 0.4613 0.4107 0.4476 0.0030  -0.0238 0.0466  465 THR D CB  
11491 O OG1 . THR D 164 ? 0.3707 0.3188 0.3531 0.0030  -0.0268 0.0488  465 THR D OG1 
11492 C CG2 . THR D 164 ? 0.3624 0.3132 0.3437 0.0023  -0.0208 0.0446  465 THR D CG2 
11493 N N   . ILE D 165 ? 0.4960 0.4546 0.4898 -0.0009 -0.0158 0.0459  466 ILE D N   
11494 C CA  . ILE D 165 ? 0.4569 0.4246 0.4565 -0.0016 -0.0129 0.0434  466 ILE D CA  
11495 C C   . ILE D 165 ? 0.6269 0.6002 0.6240 -0.0008 -0.0098 0.0404  466 ILE D C   
11496 O O   . ILE D 165 ? 0.5765 0.5486 0.5666 -0.0040 -0.0075 0.0415  466 ILE D O   
11497 C CB  . ILE D 165 ? 0.4488 0.4178 0.4486 -0.0071 -0.0107 0.0451  466 ILE D CB  
11498 C CG1 . ILE D 165 ? 0.4673 0.4295 0.4684 -0.0071 -0.0137 0.0473  466 ILE D CG1 
11499 C CG2 . ILE D 165 ? 0.4124 0.3949 0.4190 -0.0085 -0.0077 0.0420  466 ILE D CG2 
11500 C CD1 . ILE D 165 ? 0.4849 0.4437 0.4834 -0.0129 -0.0118 0.0490  466 ILE D CD1 
11501 N N   . PHE D 166 ? 0.6643 0.6434 0.6663 0.0039  -0.0097 0.0367  467 PHE D N   
11502 C CA  . PHE D 166 ? 0.4676 0.4522 0.4676 0.0066  -0.0068 0.0328  467 PHE D CA  
11503 C C   . PHE D 166 ? 0.4777 0.4778 0.4836 0.0056  -0.0027 0.0303  467 PHE D C   
11504 O O   . PHE D 166 ? 0.5461 0.5522 0.5578 0.0026  -0.0026 0.0316  467 PHE D O   
11505 C CB  . PHE D 166 ? 0.4467 0.4259 0.4466 0.0134  -0.0093 0.0298  467 PHE D CB  
11506 C CG  . PHE D 166 ? 0.4885 0.4553 0.4809 0.0125  -0.0121 0.0309  467 PHE D CG  
11507 C CD1 . PHE D 166 ? 0.4461 0.4110 0.4305 0.0108  -0.0106 0.0298  467 PHE D CD1 
11508 C CD2 . PHE D 166 ? 0.4668 0.4257 0.4598 0.0126  -0.0163 0.0331  467 PHE D CD2 
11509 C CE1 . PHE D 166 ? 0.4980 0.4540 0.4756 0.0093  -0.0135 0.0306  467 PHE D CE1 
11510 C CE2 . PHE D 166 ? 0.5720 0.5226 0.5585 0.0107  -0.0188 0.0338  467 PHE D CE2 
11511 C CZ  . PHE D 166 ? 0.5325 0.4820 0.5115 0.0091  -0.0176 0.0324  467 PHE D CZ  
11512 N N   . PRO D 167 ? 0.5087 0.5173 0.5132 0.0074  0.0010  0.0264  468 PRO D N   
11513 C CA  . PRO D 167 ? 0.4976 0.5246 0.5077 0.0050  0.0056  0.0240  468 PRO D CA  
11514 C C   . PRO D 167 ? 0.4741 0.5122 0.4952 0.0093  0.0041  0.0222  468 PRO D C   
11515 O O   . PRO D 167 ? 0.4520 0.4860 0.4757 0.0177  0.0008  0.0207  468 PRO D O   
11516 C CB  . PRO D 167 ? 0.5105 0.5445 0.5174 0.0092  0.0091  0.0190  468 PRO D CB  
11517 C CG  . PRO D 167 ? 0.4796 0.4970 0.4757 0.0086  0.0075  0.0206  468 PRO D CG  
11518 C CD  . PRO D 167 ? 0.5124 0.5151 0.5089 0.0102  0.0017  0.0240  468 PRO D CD  
11519 N N   . GLN D 168 ? 0.4240 0.4755 0.4503 0.0027  0.0065  0.0226  469 GLN D N   
11520 C CA  . GLN D 168 ? 0.4203 0.4847 0.4570 0.0053  0.0048  0.0212  469 GLN D CA  
11521 C C   . GLN D 168 ? 0.5310 0.6118 0.5745 0.0154  0.0057  0.0157  469 GLN D C   
11522 O O   . GLN D 168 ? 0.4384 0.5244 0.4792 0.0186  0.0091  0.0122  469 GLN D O   
11523 C CB  . GLN D 168 ? 0.4056 0.4824 0.4454 -0.0056 0.0077  0.0220  469 GLN D CB  
11524 C CG  . GLN D 168 ? 0.3696 0.4665 0.4106 -0.0104 0.0139  0.0184  469 GLN D CG  
11525 C CD  . GLN D 168 ? 0.4113 0.5066 0.4463 -0.0249 0.0175  0.0213  469 GLN D CD  
11526 O OE1 . GLN D 168 ? 0.4891 0.5631 0.5144 -0.0295 0.0163  0.0260  469 GLN D OE1 
11527 N NE2 . GLN D 168 ? 0.4585 0.5763 0.4987 -0.0323 0.0219  0.0184  469 GLN D NE2 
11528 N N   . ARG D 169 ? 0.5481 0.6377 0.5999 0.0209  0.0027  0.0148  470 ARG D N   
11529 C CA  . ARG D 169 ? 0.5422 0.6493 0.6010 0.0320  0.0029  0.0098  470 ARG D CA  
11530 C C   . ARG D 169 ? 0.4614 0.5949 0.5255 0.0277  0.0089  0.0056  470 ARG D C   
11531 O O   . ARG D 169 ? 0.4951 0.6358 0.5593 0.0149  0.0120  0.0071  470 ARG D O   
11532 C CB  . ARG D 169 ? 0.5629 0.6762 0.6294 0.0374  -0.0018 0.0105  470 ARG D CB  
11533 C CG  . ARG D 169 ? 0.6379 0.7698 0.7117 0.0506  -0.0024 0.0058  470 ARG D CG  
11534 C CD  . ARG D 169 ? 0.6656 0.7956 0.7430 0.0581  -0.0085 0.0078  470 ARG D CD  
11535 N NE  . ARG D 169 ? 0.6091 0.7098 0.6770 0.0636  -0.0126 0.0110  470 ARG D NE  
11536 C CZ  . ARG D 169 ? 0.6988 0.7895 0.7659 0.0655  -0.0178 0.0147  470 ARG D CZ  
11537 N NH1 . ARG D 169 ? 0.8504 0.9580 0.9256 0.0629  -0.0196 0.0155  470 ARG D NH1 
11538 N NH2 . ARG D 169 ? 0.6445 0.7091 0.7022 0.0690  -0.0210 0.0175  470 ARG D NH2 
11539 N N   . THR D 170 ? 0.3949 0.5419 0.4620 0.0383  0.0109  0.0001  471 THR D N   
11540 C CA  . THR D 170 ? 0.4419 0.6191 0.5156 0.0357  0.0166  -0.0048 471 THR D CA  
11541 C C   . THR D 170 ? 0.4808 0.6828 0.5663 0.0480  0.0150  -0.0095 471 THR D C   
11542 O O   . THR D 170 ? 0.4391 0.6601 0.5337 0.0436  0.0140  -0.0092 471 THR D O   
11543 C CB  . THR D 170 ? 0.4964 0.6729 0.5631 0.0369  0.0217  -0.0084 471 THR D CB  
11544 O OG1 . THR D 170 ? 0.6597 0.8272 0.7239 0.0530  0.0197  -0.0120 471 THR D OG1 
11545 C CG2 . THR D 170 ? 0.3841 0.5367 0.4383 0.0259  0.0227  -0.0035 471 THR D CG2 
11546 N N   . ASP D 171 ? 0.5879 0.7894 0.6727 0.0637  0.0145  -0.0138 472 ASP D N   
11547 C CA  . ASP D 171 ? 0.5882 0.8111 0.6830 0.0785  0.0121  -0.0180 472 ASP D CA  
11548 C C   . ASP D 171 ? 0.6746 0.8745 0.7657 0.0910  0.0048  -0.0151 472 ASP D C   
11549 O O   . ASP D 171 ? 0.7706 0.9823 0.8671 0.1060  0.0019  -0.0180 472 ASP D O   
11550 C CB  . ASP D 171 ? 0.6631 0.9047 0.7600 0.0894  0.0168  -0.0258 472 ASP D CB  
11551 C CG  . ASP D 171 ? 0.7085 0.9220 0.7924 0.0973  0.0172  -0.0273 472 ASP D CG  
11552 O OD1 . ASP D 171 ? 0.7274 0.9079 0.8009 0.0939  0.0139  -0.0222 472 ASP D OD1 
11553 O OD2 . ASP D 171 ? 0.7496 0.9754 0.8335 0.1070  0.0211  -0.0341 472 ASP D OD2 
11554 N N   . GLY D 172 ? 0.6848 0.8528 0.7663 0.0850  0.0016  -0.0093 473 GLY D N   
11555 C CA  . GLY D 172 ? 0.6202 0.7642 0.6960 0.0951  -0.0048 -0.0063 473 GLY D CA  
11556 C C   . GLY D 172 ? 0.6683 0.7936 0.7346 0.1088  -0.0052 -0.0095 473 GLY D C   
11557 O O   . GLY D 172 ? 0.6033 0.7044 0.6620 0.1161  -0.0103 -0.0067 473 GLY D O   
11558 N N   . LYS D 173 ? 0.6414 0.7761 0.7066 0.1120  0.0000  -0.0153 474 LYS D N   
11559 C CA  . LYS D 173 ? 0.6541 0.7697 0.7087 0.1241  0.0003  -0.0194 474 LYS D CA  
11560 C C   . LYS D 173 ? 0.6524 0.7468 0.6955 0.1140  0.0031  -0.0188 474 LYS D C   
11561 O O   . LYS D 173 ? 0.6691 0.7467 0.7020 0.1214  0.0040  -0.0227 474 LYS D O   
11562 C CB  . LYS D 173 ? 0.7088 0.8508 0.7697 0.1373  0.0041  -0.0276 474 LYS D CB  
11563 C CG  . LYS D 173 ? 0.8606 1.0351 0.9364 0.1441  0.0024  -0.0285 474 LYS D CG  
11564 C CD  . LYS D 173 ? 1.0106 1.1870 1.0863 0.1670  -0.0008 -0.0327 474 LYS D CD  
11565 C CE  . LYS D 173 ? 1.1300 1.3250 1.2073 0.1775  0.0050  -0.0419 474 LYS D CE  
11566 N NZ  . LYS D 173 ? 1.1618 1.4012 1.2540 0.1691  0.0108  -0.0455 474 LYS D NZ  
11567 N N   . HIS D 174 ? 0.6733 0.7675 0.7171 0.0975  0.0043  -0.0141 475 HIS D N   
11568 C CA  . HIS D 174 ? 0.6381 0.7147 0.6715 0.0875  0.0064  -0.0129 475 HIS D CA  
11569 C C   . HIS D 174 ? 0.6027 0.6622 0.6331 0.0760  0.0028  -0.0054 475 HIS D C   
11570 O O   . HIS D 174 ? 0.5101 0.5672 0.5373 0.0641  0.0048  -0.0027 475 HIS D O   
11571 C CB  . HIS D 174 ? 0.6403 0.7377 0.6760 0.0796  0.0131  -0.0158 475 HIS D CB  
11572 C CG  . HIS D 174 ? 0.7069 0.8232 0.7453 0.0908  0.0174  -0.0238 475 HIS D CG  
11573 N ND1 . HIS D 174 ? 0.7173 0.8630 0.7684 0.0979  0.0185  -0.0273 475 HIS D ND1 
11574 C CD2 . HIS D 174 ? 0.7466 0.8576 0.7767 0.0967  0.0207  -0.0297 475 HIS D CD2 
11575 C CE1 . HIS D 174 ? 0.7575 0.9160 0.8084 0.1084  0.0226  -0.0349 475 HIS D CE1 
11576 N NE2 . HIS D 174 ? 0.7703 0.9073 0.8082 0.1078  0.0241  -0.0366 475 HIS D NE2 
11577 N N   . ASP D 175 ? 0.6231 0.6709 0.6540 0.0800  -0.0027 -0.0019 476 ASP D N   
11578 C CA  . ASP D 175 ? 0.5797 0.6139 0.6088 0.0700  -0.0061 0.0046  476 ASP D CA  
11579 C C   . ASP D 175 ? 0.4892 0.4996 0.5063 0.0649  -0.0067 0.0060  476 ASP D C   
11580 O O   . ASP D 175 ? 0.6008 0.5963 0.6092 0.0713  -0.0072 0.0029  476 ASP D O   
11581 C CB  . ASP D 175 ? 0.7191 0.7467 0.7505 0.0758  -0.0116 0.0076  476 ASP D CB  
11582 C CG  . ASP D 175 ? 0.7261 0.7790 0.7699 0.0787  -0.0119 0.0072  476 ASP D CG  
11583 O OD1 . ASP D 175 ? 0.6931 0.7696 0.7444 0.0758  -0.0076 0.0042  476 ASP D OD1 
11584 O OD2 . ASP D 175 ? 0.7004 0.7500 0.7460 0.0833  -0.0165 0.0099  476 ASP D OD2 
11585 N N   . PHE D 176 ? 0.4461 0.4535 0.4624 0.0534  -0.0067 0.0104  477 PHE D N   
11586 C CA  . PHE D 176 ? 0.4654 0.4520 0.4725 0.0483  -0.0092 0.0132  477 PHE D CA  
11587 C C   . PHE D 176 ? 0.6301 0.6062 0.6381 0.0486  -0.0142 0.0173  477 PHE D C   
11588 O O   . PHE D 176 ? 0.5441 0.5300 0.5601 0.0471  -0.0153 0.0199  477 PHE D O   
11589 C CB  . PHE D 176 ? 0.3736 0.3623 0.3791 0.0375  -0.0074 0.0162  477 PHE D CB  
11590 C CG  . PHE D 176 ? 0.5255 0.5212 0.5269 0.0356  -0.0027 0.0130  477 PHE D CG  
11591 C CD1 . PHE D 176 ? 0.4978 0.5132 0.5051 0.0366  0.0018  0.0100  477 PHE D CD1 
11592 C CD2 . PHE D 176 ? 0.4710 0.4553 0.4624 0.0319  -0.0027 0.0130  477 PHE D CD2 
11593 C CE1 . PHE D 176 ? 0.5813 0.6036 0.5840 0.0339  0.0065  0.0073  477 PHE D CE1 
11594 C CE2 . PHE D 176 ? 0.5401 0.5310 0.5267 0.0297  0.0016  0.0103  477 PHE D CE2 
11595 C CZ  . PHE D 176 ? 0.5743 0.5837 0.5662 0.0307  0.0064  0.0075  477 PHE D CZ  
11596 N N   . ARG D 177 ? 0.6365 0.5929 0.6356 0.0497  -0.0171 0.0176  478 ARG D N   
11597 C CA  . ARG D 177 ? 0.5455 0.4906 0.5433 0.0492  -0.0215 0.0214  478 ARG D CA  
11598 C C   . ARG D 177 ? 0.4983 0.4258 0.4863 0.0431  -0.0233 0.0227  478 ARG D C   
11599 O O   . ARG D 177 ? 0.5543 0.4717 0.5335 0.0441  -0.0224 0.0192  478 ARG D O   
11600 C CB  . ARG D 177 ? 0.4267 0.3658 0.4229 0.0600  -0.0237 0.0200  478 ARG D CB  
11601 C CG  . ARG D 177 ? 0.4788 0.4379 0.4857 0.0668  -0.0229 0.0190  478 ARG D CG  
11602 C CD  . ARG D 177 ? 0.5363 0.5072 0.5521 0.0606  -0.0244 0.0233  478 ARG D CD  
11603 N NE  . ARG D 177 ? 0.5552 0.5131 0.5675 0.0591  -0.0288 0.0277  478 ARG D NE  
11604 C CZ  . ARG D 177 ? 0.5209 0.4761 0.5328 0.0665  -0.0321 0.0290  478 ARG D CZ  
11605 N NH1 . ARG D 177 ? 0.4510 0.4159 0.4663 0.0775  -0.0320 0.0260  478 ARG D NH1 
11606 N NH2 . ARG D 177 ? 0.4494 0.3928 0.4570 0.0634  -0.0357 0.0332  478 ARG D NH2 
11607 N N   . VAL D 178 ? 0.5401 0.4651 0.5293 0.0366  -0.0259 0.0270  479 VAL D N   
11608 C CA  . VAL D 178 ? 0.5234 0.4327 0.5038 0.0316  -0.0284 0.0283  479 VAL D CA  
11609 C C   . VAL D 178 ? 0.5893 0.4863 0.5657 0.0359  -0.0313 0.0295  479 VAL D C   
11610 O O   . VAL D 178 ? 0.6365 0.5391 0.6188 0.0365  -0.0330 0.0328  479 VAL D O   
11611 C CB  . VAL D 178 ? 0.5142 0.4285 0.4975 0.0231  -0.0295 0.0320  479 VAL D CB  
11612 C CG1 . VAL D 178 ? 0.5512 0.4530 0.5258 0.0172  -0.0318 0.0324  479 VAL D CG1 
11613 C CG2 . VAL D 178 ? 0.4936 0.4192 0.4803 0.0202  -0.0270 0.0317  479 VAL D CG2 
11614 N N   . TRP D 179 ? 0.5589 0.4379 0.5239 0.0385  -0.0320 0.0270  480 TRP D N   
11615 C CA  . TRP D 179 ? 0.5549 0.4187 0.5134 0.0431  -0.0349 0.0287  480 TRP D CA  
11616 C C   . TRP D 179 ? 0.5358 0.3926 0.4909 0.0341  -0.0377 0.0333  480 TRP D C   
11617 O O   . TRP D 179 ? 0.5600 0.4113 0.5137 0.0365  -0.0401 0.0365  480 TRP D O   
11618 C CB  . TRP D 179 ? 0.5902 0.4332 0.5351 0.0486  -0.0348 0.0247  480 TRP D CB  
11619 C CG  . TRP D 179 ? 0.5602 0.4103 0.5085 0.0611  -0.0326 0.0203  480 TRP D CG  
11620 C CD1 . TRP D 179 ? 0.4679 0.3412 0.4282 0.0633  -0.0294 0.0183  480 TRP D CD1 
11621 C CD2 . TRP D 179 ? 0.5209 0.3557 0.4604 0.0732  -0.0332 0.0173  480 TRP D CD2 
11622 N NE1 . TRP D 179 ? 0.4739 0.3503 0.4346 0.0755  -0.0279 0.0139  480 TRP D NE1 
11623 C CE2 . TRP D 179 ? 0.5307 0.3836 0.4789 0.0828  -0.0303 0.0131  480 TRP D CE2 
11624 C CE3 . TRP D 179 ? 0.5229 0.3299 0.4471 0.0769  -0.0359 0.0179  480 TRP D CE3 
11625 C CZ2 . TRP D 179 ? 0.5443 0.3904 0.4876 0.0974  -0.0301 0.0091  480 TRP D CZ2 
11626 C CZ3 . TRP D 179 ? 0.6412 0.4378 0.5590 0.0915  -0.0360 0.0143  480 TRP D CZ3 
11627 C CH2 . TRP D 179 ? 0.6386 0.4556 0.5664 0.1023  -0.0332 0.0097  480 TRP D CH2 
11628 N N   . ASN D 180 ? 0.4812 0.3397 0.4350 0.0240  -0.0374 0.0335  481 ASN D N   
11629 C CA  . ASN D 180 ? 0.4968 0.3553 0.4502 0.0151  -0.0393 0.0373  481 ASN D CA  
11630 C C   . ASN D 180 ? 0.4958 0.3698 0.4607 0.0162  -0.0399 0.0408  481 ASN D C   
11631 O O   . ASN D 180 ? 0.4769 0.3663 0.4519 0.0192  -0.0382 0.0402  481 ASN D O   
11632 C CB  . ASN D 180 ? 0.4726 0.3374 0.4258 0.0060  -0.0387 0.0363  481 ASN D CB  
11633 C CG  . ASN D 180 ? 0.5366 0.3892 0.4792 0.0042  -0.0379 0.0320  481 ASN D CG  
11634 O OD1 . ASN D 180 ? 0.5757 0.4287 0.5182 0.0102  -0.0359 0.0286  481 ASN D OD1 
11635 N ND2 . ASN D 180 ? 0.6051 0.4476 0.5382 -0.0049 -0.0393 0.0318  481 ASN D ND2 
11636 N N   . SER D 181 ? 0.4657 0.3354 0.4282 0.0127  -0.0421 0.0444  482 SER D N   
11637 C CA  . SER D 181 ? 0.3935 0.2778 0.3661 0.0130  -0.0426 0.0472  482 SER D CA  
11638 C C   . SER D 181 ? 0.4490 0.3465 0.4279 0.0061  -0.0417 0.0475  482 SER D C   
11639 O O   . SER D 181 ? 0.4503 0.3616 0.4388 0.0076  -0.0407 0.0479  482 SER D O   
11640 C CB  . SER D 181 ? 0.5354 0.4113 0.5025 0.0123  -0.0452 0.0509  482 SER D CB  
11641 O OG  . SER D 181 ? 0.4899 0.3543 0.4470 0.0035  -0.0462 0.0523  482 SER D OG  
11642 N N   . GLN D 182 ? 0.4864 0.3801 0.4597 -0.0014 -0.0420 0.0471  483 GLN D N   
11643 C CA  . GLN D 182 ? 0.5153 0.4218 0.4938 -0.0061 -0.0413 0.0467  483 GLN D CA  
11644 C C   . GLN D 182 ? 0.5576 0.4600 0.5303 -0.0088 -0.0407 0.0438  483 GLN D C   
11645 O O   . GLN D 182 ? 0.5399 0.4277 0.5030 -0.0098 -0.0410 0.0422  483 GLN D O   
11646 C CB  . GLN D 182 ? 0.5284 0.4404 0.5070 -0.0131 -0.0425 0.0487  483 GLN D CB  
11647 C CG  . GLN D 182 ? 0.5909 0.5102 0.5757 -0.0112 -0.0428 0.0511  483 GLN D CG  
11648 C CD  . GLN D 182 ? 0.6705 0.5918 0.6524 -0.0184 -0.0439 0.0529  483 GLN D CD  
11649 O OE1 . GLN D 182 ? 0.6319 0.5633 0.6156 -0.0235 -0.0437 0.0522  483 GLN D OE1 
11650 N NE2 . GLN D 182 ? 0.6877 0.6002 0.6643 -0.0187 -0.0450 0.0553  483 GLN D NE2 
11651 N N   . LEU D 183 ? 0.5155 0.4298 0.4930 -0.0099 -0.0400 0.0431  484 LEU D N   
11652 C CA  . LEU D 183 ? 0.5006 0.4131 0.4726 -0.0124 -0.0397 0.0404  484 LEU D CA  
11653 C C   . LEU D 183 ? 0.5196 0.4281 0.4840 -0.0213 -0.0414 0.0396  484 LEU D C   
11654 O O   . LEU D 183 ? 0.5107 0.4087 0.4659 -0.0244 -0.0414 0.0368  484 LEU D O   
11655 C CB  . LEU D 183 ? 0.4057 0.3314 0.3832 -0.0110 -0.0391 0.0406  484 LEU D CB  
11656 C CG  . LEU D 183 ? 0.3772 0.3076 0.3610 -0.0046 -0.0371 0.0414  484 LEU D CG  
11657 C CD1 . LEU D 183 ? 0.3004 0.2407 0.2868 -0.0043 -0.0369 0.0425  484 LEU D CD1 
11658 C CD2 . LEU D 183 ? 0.3386 0.2618 0.3195 -0.0004 -0.0351 0.0390  484 LEU D CD2 
11659 N N   . ILE D 184 ? 0.4512 0.3683 0.4187 -0.0261 -0.0426 0.0416  485 ILE D N   
11660 C CA  . ILE D 184 ? 0.5004 0.4164 0.4611 -0.0362 -0.0438 0.0408  485 ILE D CA  
11661 C C   . ILE D 184 ? 0.5439 0.4511 0.5009 -0.0393 -0.0443 0.0432  485 ILE D C   
11662 O O   . ILE D 184 ? 0.5178 0.4350 0.4819 -0.0380 -0.0443 0.0456  485 ILE D O   
11663 C CB  . ILE D 184 ? 0.4314 0.3682 0.3982 -0.0399 -0.0448 0.0407  485 ILE D CB  
11664 C CG1 . ILE D 184 ? 0.5829 0.5266 0.5513 -0.0364 -0.0448 0.0390  485 ILE D CG1 
11665 C CG2 . ILE D 184 ? 0.3708 0.3100 0.3314 -0.0516 -0.0459 0.0396  485 ILE D CG2 
11666 C CD1 . ILE D 184 ? 0.7149 0.6793 0.6893 -0.0373 -0.0463 0.0392  485 ILE D CD1 
11667 N N   . ARG D 185 ? 0.5753 0.4624 0.5200 -0.0431 -0.0445 0.0426  486 ARG D N   
11668 C CA  . ARG D 185 ? 0.6024 0.4774 0.5395 -0.0478 -0.0452 0.0453  486 ARG D CA  
11669 C C   . ARG D 185 ? 0.6777 0.5356 0.5992 -0.0584 -0.0456 0.0436  486 ARG D C   
11670 O O   . ARG D 185 ? 0.6578 0.5091 0.5736 -0.0598 -0.0454 0.0399  486 ARG D O   
11671 C CB  . ARG D 185 ? 0.5934 0.4541 0.5287 -0.0383 -0.0454 0.0474  486 ARG D CB  
11672 C CG  . ARG D 185 ? 0.6944 0.5698 0.6430 -0.0298 -0.0450 0.0493  486 ARG D CG  
11673 C CD  . ARG D 185 ? 0.7981 0.6621 0.7436 -0.0237 -0.0460 0.0521  486 ARG D CD  
11674 N NE  . ARG D 185 ? 0.8725 0.7371 0.8151 -0.0299 -0.0469 0.0556  486 ARG D NE  
11675 C CZ  . ARG D 185 ? 0.8706 0.7312 0.8124 -0.0254 -0.0481 0.0588  486 ARG D CZ  
11676 N NH1 . ARG D 185 ? 0.8349 0.6920 0.7795 -0.0144 -0.0486 0.0588  486 ARG D NH1 
11677 N NH2 . ARG D 185 ? 0.8239 0.6856 0.7621 -0.0320 -0.0487 0.0620  486 ARG D NH2 
11678 N N   . TYR D 186 ? 0.5865 0.4358 0.4998 -0.0664 -0.0461 0.0463  487 TYR D N   
11679 C CA  . TYR D 186 ? 0.5290 0.3595 0.4252 -0.0786 -0.0464 0.0451  487 TYR D CA  
11680 C C   . TYR D 186 ? 0.6250 0.4226 0.5058 -0.0743 -0.0469 0.0465  487 TYR D C   
11681 O O   . TYR D 186 ? 0.7001 0.4921 0.5831 -0.0644 -0.0475 0.0499  487 TYR D O   
11682 C CB  . TYR D 186 ? 0.5847 0.4258 0.4790 -0.0924 -0.0463 0.0470  487 TYR D CB  
11683 C CG  . TYR D 186 ? 0.5896 0.4632 0.4974 -0.0968 -0.0460 0.0449  487 TYR D CG  
11684 C CD1 . TYR D 186 ? 0.6258 0.5080 0.5342 -0.1007 -0.0463 0.0405  487 TYR D CD1 
11685 C CD2 . TYR D 186 ? 0.6187 0.5148 0.5379 -0.0965 -0.0457 0.0471  487 TYR D CD2 
11686 C CE1 . TYR D 186 ? 0.6173 0.5300 0.5376 -0.1034 -0.0466 0.0388  487 TYR D CE1 
11687 C CE2 . TYR D 186 ? 0.6260 0.5517 0.5570 -0.0989 -0.0456 0.0450  487 TYR D CE2 
11688 C CZ  . TYR D 186 ? 0.5937 0.5279 0.5253 -0.1019 -0.0463 0.0411  487 TYR D CZ  
11689 O OH  . TYR D 186 ? 0.5974 0.5620 0.5405 -0.1028 -0.0468 0.0392  487 TYR D OH  
11690 N N   . ALA D 187 ? 0.6239 0.3994 0.4882 -0.0815 -0.0469 0.0437  488 ALA D N   
11691 C CA  . ALA D 187 ? 0.7083 0.4493 0.5557 -0.0763 -0.0474 0.0443  488 ALA D CA  
11692 C C   . ALA D 187 ? 0.6996 0.4239 0.5345 -0.0825 -0.0484 0.0498  488 ALA D C   
11693 O O   . ALA D 187 ? 0.6652 0.4014 0.5006 -0.0955 -0.0481 0.0519  488 ALA D O   
11694 C CB  . ALA D 187 ? 0.6583 0.3782 0.4897 -0.0828 -0.0469 0.0390  488 ALA D CB  
11695 N N   . GLY D 188 ? 0.7993 0.4965 0.6228 -0.0725 -0.0496 0.0521  489 GLY D N   
11696 C CA  . GLY D 188 ? 0.8382 0.5121 0.6450 -0.0773 -0.0509 0.0577  489 GLY D CA  
11697 C C   . GLY D 188 ? 0.9265 0.5584 0.7087 -0.0762 -0.0516 0.0566  489 GLY D C   
11698 O O   . GLY D 188 ? 0.9119 0.5322 0.6932 -0.0616 -0.0519 0.0537  489 GLY D O   
11699 N N   . TYR D 189 ? 0.9492 0.5576 0.7105 -0.0919 -0.0516 0.0587  490 TYR D N   
11700 C CA  . TYR D 189 ? 0.8590 0.4224 0.5930 -0.0926 -0.0523 0.0579  490 TYR D CA  
11701 C C   . TYR D 189 ? 0.9756 0.5129 0.6904 -0.0971 -0.0539 0.0657  490 TYR D C   
11702 O O   . TYR D 189 ? 1.0067 0.5465 0.7145 -0.1160 -0.0530 0.0685  490 TYR D O   
11703 C CB  . TYR D 189 ? 0.7898 0.3443 0.5119 -0.1105 -0.0505 0.0521  490 TYR D CB  
11704 C CG  . TYR D 189 ? 0.8767 0.4623 0.6177 -0.1104 -0.0490 0.0452  490 TYR D CG  
11705 C CD1 . TYR D 189 ? 0.9288 0.5057 0.6698 -0.0981 -0.0486 0.0393  490 TYR D CD1 
11706 C CD2 . TYR D 189 ? 0.8445 0.4676 0.6021 -0.1224 -0.0480 0.0445  490 TYR D CD2 
11707 C CE1 . TYR D 189 ? 0.8552 0.4595 0.6116 -0.0984 -0.0474 0.0334  490 TYR D CE1 
11708 C CE2 . TYR D 189 ? 0.9097 0.5598 0.6829 -0.1216 -0.0471 0.0387  490 TYR D CE2 
11709 C CZ  . TYR D 189 ? 0.8854 0.5252 0.6574 -0.1101 -0.0468 0.0334  490 TYR D CZ  
11710 O OH  . TYR D 189 ? 0.9069 0.5724 0.6927 -0.1096 -0.0461 0.0283  490 TYR D OH  
11711 N N   . LYS D 190 ? 0.9114 0.4241 0.6167 -0.0802 -0.0563 0.0691  491 LYS D N   
11712 C CA  . LYS D 190 ? 1.0313 0.5121 0.7133 -0.0841 -0.0582 0.0768  491 LYS D CA  
11713 C C   . LYS D 190 ? 1.0527 0.4895 0.7037 -0.0964 -0.0576 0.0750  491 LYS D C   
11714 O O   . LYS D 190 ? 1.0947 0.5145 0.7392 -0.0894 -0.0570 0.0685  491 LYS D O   
11715 C CB  . LYS D 190 ? 1.1468 0.6174 0.8286 -0.0609 -0.0616 0.0814  491 LYS D CB  
11716 C CG  . LYS D 190 ? 1.3327 0.8089 1.0131 -0.0634 -0.0635 0.0904  491 LYS D CG  
11717 C CD  . LYS D 190 ? 1.4381 0.9018 1.1151 -0.0411 -0.0675 0.0954  491 LYS D CD  
11718 C CE  . LYS D 190 ? 1.4286 0.8924 1.0985 -0.0456 -0.0690 0.1037  491 LYS D CE  
11719 N NZ  . LYS D 190 ? 1.4194 0.8664 1.0804 -0.0262 -0.0722 0.1071  491 LYS D NZ  
11720 N N   . GLN D 191 ? 0.9872 0.4179 0.6247 -0.1138 -0.0564 0.0784  492 GLN D N   
11721 C CA  . GLN D 191 ? 0.9784 0.3818 0.5921 -0.1271 -0.0547 0.0752  492 GLN D CA  
11722 C C   . GLN D 191 ? 1.0032 0.3726 0.5967 -0.1146 -0.0564 0.0786  492 GLN D C   
11723 O O   . GLN D 191 ? 1.0615 0.4325 0.6594 -0.0995 -0.0589 0.0845  492 GLN D O   
11724 C CB  . GLN D 191 ? 1.1392 0.5570 0.7493 -0.1535 -0.0524 0.0768  492 GLN D CB  
11725 C CG  . GLN D 191 ? 1.1860 0.6439 0.8188 -0.1651 -0.0511 0.0753  492 GLN D CG  
11726 C CD  . GLN D 191 ? 1.1984 0.6618 0.8321 -0.1776 -0.0492 0.0670  492 GLN D CD  
11727 O OE1 . GLN D 191 ? 1.2144 0.6616 0.8446 -0.1674 -0.0496 0.0615  492 GLN D OE1 
11728 N NE2 . GLN D 191 ? 1.2053 0.6938 0.8437 -0.1998 -0.0471 0.0655  492 GLN D NE2 
11729 N N   . PRO D 192 ? 1.0460 0.3838 0.6163 -0.1204 -0.0553 0.0748  493 PRO D N   
11730 C CA  . PRO D 192 ? 1.0828 0.3864 0.6322 -0.1085 -0.0572 0.0783  493 PRO D CA  
11731 C C   . PRO D 192 ? 1.1282 0.4313 0.6700 -0.1155 -0.0582 0.0869  493 PRO D C   
11732 O O   . PRO D 192 ? 1.2318 0.5157 0.7634 -0.1010 -0.0608 0.0918  493 PRO D O   
11733 C CB  . PRO D 192 ? 1.0861 0.3582 0.6114 -0.1190 -0.0553 0.0723  493 PRO D CB  
11734 C CG  . PRO D 192 ? 1.0528 0.3426 0.5905 -0.1268 -0.0531 0.0642  493 PRO D CG  
11735 C CD  . PRO D 192 ? 1.0627 0.3939 0.6250 -0.1355 -0.0527 0.0668  493 PRO D CD  
11736 N N   . ASP D 193 ? 1.0558 0.3807 0.6023 -0.1374 -0.0562 0.0888  494 ASP D N   
11737 C CA  . ASP D 193 ? 1.1245 0.4497 0.6623 -0.1470 -0.0565 0.0963  494 ASP D CA  
11738 C C   . ASP D 193 ? 1.1029 0.4556 0.6608 -0.1365 -0.0585 0.1026  494 ASP D C   
11739 O O   . ASP D 193 ? 1.1784 0.5363 0.7316 -0.1446 -0.0586 0.1089  494 ASP D O   
11740 C CB  . ASP D 193 ? 1.1389 0.4759 0.6709 -0.1763 -0.0531 0.0947  494 ASP D CB  
11741 C CG  . ASP D 193 ? 1.1669 0.5483 0.7252 -0.1859 -0.0514 0.0930  494 ASP D CG  
11742 O OD1 . ASP D 193 ? 1.1809 0.5790 0.7595 -0.1728 -0.0523 0.0905  494 ASP D OD1 
11743 O OD2 . ASP D 193 ? 1.2186 0.6187 0.7768 -0.2068 -0.0491 0.0939  494 ASP D OD2 
11744 N N   . GLY D 194 ? 1.0835 0.4535 0.6625 -0.1189 -0.0600 0.1009  495 GLY D N   
11745 C CA  . GLY D 194 ? 1.0388 0.4354 0.6372 -0.1083 -0.0620 0.1061  495 GLY D CA  
11746 C C   . GLY D 194 ? 1.0115 0.4463 0.6319 -0.1202 -0.0601 0.1049  495 GLY D C   
11747 O O   . GLY D 194 ? 0.9712 0.4291 0.6110 -0.1087 -0.0618 0.1071  495 GLY D O   
11748 N N   . SER D 195 ? 0.9919 0.4347 0.6095 -0.1429 -0.0568 0.1015  496 SER D N   
11749 C CA  . SER D 195 ? 0.9580 0.4387 0.5965 -0.1544 -0.0550 0.1003  496 SER D CA  
11750 C C   . SER D 195 ? 1.0054 0.4981 0.6620 -0.1430 -0.0557 0.0952  496 SER D C   
11751 O O   . SER D 195 ? 0.9741 0.4461 0.6259 -0.1294 -0.0568 0.0913  496 SER D O   
11752 C CB  . SER D 195 ? 0.9379 0.4273 0.5697 -0.1810 -0.0514 0.0971  496 SER D CB  
11753 O OG  . SER D 195 ? 1.0546 0.5328 0.6810 -0.1862 -0.0502 0.0896  496 SER D OG  
11754 N N   . THR D 196 ? 0.9937 0.5308 0.6770 -0.1453 -0.0542 0.0930  497 THR D N   
11755 C CA  . THR D 196 ? 0.9740 0.5379 0.6822 -0.1321 -0.0539 0.0860  497 THR D CA  
11756 C C   . THR D 196 ? 0.9883 0.5841 0.7103 -0.1479 -0.0509 0.0801  497 THR D C   
11757 O O   . THR D 196 ? 0.9762 0.5943 0.7027 -0.1626 -0.0492 0.0817  497 THR D O   
11758 C CB  . THR D 196 ? 0.9867 0.5783 0.7180 -0.1138 -0.0554 0.0882  497 THR D CB  
11759 O OG1 . THR D 196 ? 1.0442 0.6080 0.7624 -0.0990 -0.0586 0.0938  497 THR D OG1 
11760 C CG2 . THR D 196 ? 0.9673 0.5838 0.7222 -0.1009 -0.0548 0.0813  497 THR D CG2 
11761 N N   . LEU D 197 ? 1.0059 0.6039 0.7334 -0.1446 -0.0503 0.0730  498 LEU D N   
11762 C CA  . LEU D 197 ? 0.8990 0.5278 0.6400 -0.1567 -0.0482 0.0669  498 LEU D CA  
11763 C C   . LEU D 197 ? 0.8063 0.4693 0.5757 -0.1405 -0.0484 0.0635  498 LEU D C   
11764 O O   . LEU D 197 ? 0.8316 0.4852 0.6048 -0.1225 -0.0496 0.0625  498 LEU D O   
11765 C CB  . LEU D 197 ? 0.9553 0.5603 0.6790 -0.1675 -0.0476 0.0613  498 LEU D CB  
11766 C CG  . LEU D 197 ? 0.9717 0.6075 0.7074 -0.1800 -0.0460 0.0546  498 LEU D CG  
11767 C CD1 . LEU D 197 ? 0.9025 0.5701 0.6463 -0.1967 -0.0445 0.0564  498 LEU D CD1 
11768 C CD2 . LEU D 197 ? 0.9639 0.5707 0.6780 -0.1922 -0.0455 0.0492  498 LEU D CD2 
11769 N N   . GLY D 198 ? 0.7559 0.4585 0.5445 -0.1466 -0.0471 0.0618  499 GLY D N   
11770 C CA  . GLY D 198 ? 0.7197 0.4535 0.5338 -0.1317 -0.0472 0.0597  499 GLY D CA  
11771 C C   . GLY D 198 ? 0.7844 0.5262 0.6089 -0.1182 -0.0481 0.0646  499 GLY D C   
11772 O O   . GLY D 198 ? 0.8716 0.6104 0.6899 -0.1234 -0.0483 0.0697  499 GLY D O   
11773 N N   . ASP D 199 ? 0.7829 0.5350 0.6225 -0.1014 -0.0487 0.0629  500 ASP D N   
11774 C CA  . ASP D 199 ? 0.7257 0.4923 0.5788 -0.0891 -0.0495 0.0662  500 ASP D CA  
11775 C C   . ASP D 199 ? 0.7426 0.4818 0.5849 -0.0768 -0.0515 0.0697  500 ASP D C   
11776 O O   . ASP D 199 ? 0.7710 0.4993 0.6133 -0.0653 -0.0521 0.0670  500 ASP D O   
11777 C CB  . ASP D 199 ? 0.6785 0.4723 0.5534 -0.0789 -0.0488 0.0624  500 ASP D CB  
11778 C CG  . ASP D 199 ? 0.7239 0.5359 0.6134 -0.0690 -0.0491 0.0649  500 ASP D CG  
11779 O OD1 . ASP D 199 ? 0.7677 0.5671 0.6517 -0.0627 -0.0506 0.0690  500 ASP D OD1 
11780 O OD2 . ASP D 199 ? 0.6485 0.4871 0.5543 -0.0674 -0.0481 0.0627  500 ASP D OD2 
11781 N N   . PRO D 200 ? 0.8179 0.5467 0.6509 -0.0781 -0.0528 0.0756  501 PRO D N   
11782 C CA  . PRO D 200 ? 0.7741 0.4765 0.5956 -0.0653 -0.0554 0.0792  501 PRO D CA  
11783 C C   . PRO D 200 ? 0.7687 0.4850 0.6068 -0.0465 -0.0565 0.0778  501 PRO D C   
11784 O O   . PRO D 200 ? 0.7798 0.4767 0.6105 -0.0337 -0.0584 0.0784  501 PRO D O   
11785 C CB  . PRO D 200 ? 0.7080 0.4041 0.5189 -0.0719 -0.0566 0.0861  501 PRO D CB  
11786 C CG  . PRO D 200 ? 0.6173 0.3235 0.4252 -0.0924 -0.0540 0.0853  501 PRO D CG  
11787 C CD  . PRO D 200 ? 0.6678 0.4061 0.4974 -0.0922 -0.0520 0.0791  501 PRO D CD  
11788 N N   . ALA D 201 ? 0.7726 0.5219 0.6322 -0.0445 -0.0552 0.0756  502 ALA D N   
11789 C CA  . ALA D 201 ? 0.7761 0.5404 0.6517 -0.0291 -0.0557 0.0738  502 ALA D CA  
11790 C C   . ALA D 201 ? 0.7864 0.5433 0.6629 -0.0211 -0.0550 0.0688  502 ALA D C   
11791 O O   . ALA D 201 ? 0.8180 0.5779 0.7012 -0.0072 -0.0557 0.0678  502 ALA D O   
11792 C CB  . ALA D 201 ? 0.6814 0.4791 0.5773 -0.0309 -0.0540 0.0721  502 ALA D CB  
11793 N N   . ASN D 202 ? 0.7530 0.5018 0.6227 -0.0299 -0.0534 0.0654  503 ASN D N   
11794 C CA  . ASN D 202 ? 0.7232 0.4697 0.5955 -0.0234 -0.0522 0.0599  503 ASN D CA  
11795 C C   . ASN D 202 ? 0.7843 0.4964 0.6361 -0.0213 -0.0530 0.0587  503 ASN D C   
11796 O O   . ASN D 202 ? 0.8474 0.5538 0.6971 -0.0192 -0.0517 0.0535  503 ASN D O   
11797 C CB  . ASN D 202 ? 0.6031 0.3686 0.4842 -0.0331 -0.0501 0.0559  503 ASN D CB  
11798 C CG  . ASN D 202 ? 0.6042 0.4014 0.5050 -0.0323 -0.0493 0.0566  503 ASN D CG  
11799 O OD1 . ASN D 202 ? 0.6574 0.4644 0.5684 -0.0218 -0.0497 0.0577  503 ASN D OD1 
11800 N ND2 . ASN D 202 ? 0.5863 0.4001 0.4923 -0.0431 -0.0483 0.0554  503 ASN D ND2 
11801 N N   . VAL D 203 ? 0.8062 0.4938 0.6414 -0.0215 -0.0551 0.0635  504 VAL D N   
11802 C CA  . VAL D 203 ? 0.7317 0.3816 0.5438 -0.0207 -0.0559 0.0627  504 VAL D CA  
11803 C C   . VAL D 203 ? 0.8645 0.5071 0.6779 -0.0023 -0.0562 0.0589  504 VAL D C   
11804 O O   . VAL D 203 ? 0.9163 0.5396 0.7186 -0.0014 -0.0552 0.0540  504 VAL D O   
11805 C CB  . VAL D 203 ? 0.7460 0.3704 0.5390 -0.0242 -0.0584 0.0697  504 VAL D CB  
11806 C CG1 . VAL D 203 ? 0.7218 0.3053 0.4916 -0.0153 -0.0601 0.0697  504 VAL D CG1 
11807 C CG2 . VAL D 203 ? 0.7444 0.3676 0.5290 -0.0459 -0.0571 0.0715  504 VAL D CG2 
11808 N N   . GLN D 204 ? 0.8000 0.4600 0.6275 0.0123  -0.0574 0.0605  505 GLN D N   
11809 C CA  . GLN D 204 ? 0.8763 0.5327 0.7059 0.0302  -0.0576 0.0567  505 GLN D CA  
11810 C C   . GLN D 204 ? 0.8268 0.4991 0.6675 0.0300  -0.0542 0.0494  505 GLN D C   
11811 O O   . GLN D 204 ? 0.6628 0.3190 0.4949 0.0369  -0.0532 0.0444  505 GLN D O   
11812 C CB  . GLN D 204 ? 0.9467 0.6230 0.7902 0.0442  -0.0596 0.0596  505 GLN D CB  
11813 C CG  . GLN D 204 ? 1.1210 0.7808 0.9564 0.0635  -0.0618 0.0589  505 GLN D CG  
11814 C CD  . GLN D 204 ? 1.1319 0.8222 0.9878 0.0781  -0.0615 0.0563  505 GLN D CD  
11815 O OE1 . GLN D 204 ? 1.0198 0.7388 0.8928 0.0758  -0.0616 0.0583  505 GLN D OE1 
11816 N NE2 . GLN D 204 ? 1.1862 0.8703 1.0399 0.0929  -0.0610 0.0514  505 GLN D NE2 
11817 N N   . PHE D 205 ? 0.7409 0.4438 0.5997 0.0225  -0.0524 0.0488  506 PHE D N   
11818 C CA  . PHE D 205 ? 0.7219 0.4403 0.5904 0.0214  -0.0494 0.0429  506 PHE D CA  
11819 C C   . PHE D 205 ? 0.7366 0.4358 0.5902 0.0105  -0.0483 0.0391  506 PHE D C   
11820 O O   . PHE D 205 ? 0.7468 0.4434 0.5988 0.0142  -0.0464 0.0332  506 PHE D O   
11821 C CB  . PHE D 205 ? 0.6557 0.4071 0.5438 0.0153  -0.0482 0.0440  506 PHE D CB  
11822 C CG  . PHE D 205 ? 0.6734 0.4408 0.5708 0.0146  -0.0455 0.0390  506 PHE D CG  
11823 C CD1 . PHE D 205 ? 0.7541 0.5334 0.6611 0.0266  -0.0440 0.0360  506 PHE D CD1 
11824 C CD2 . PHE D 205 ? 0.6930 0.4642 0.5888 0.0020  -0.0445 0.0371  506 PHE D CD2 
11825 C CE1 . PHE D 205 ? 0.6066 0.3998 0.5205 0.0254  -0.0412 0.0317  506 PHE D CE1 
11826 C CE2 . PHE D 205 ? 0.5886 0.3740 0.4916 0.0019  -0.0423 0.0329  506 PHE D CE2 
11827 C CZ  . PHE D 205 ? 0.5977 0.3930 0.5092 0.0134  -0.0406 0.0304  506 PHE D CZ  
11828 N N   . THR D 206 ? 0.7249 0.4115 0.5670 -0.0036 -0.0492 0.0420  507 THR D N   
11829 C CA  . THR D 206 ? 0.7419 0.4080 0.5674 -0.0157 -0.0484 0.0384  507 THR D CA  
11830 C C   . THR D 206 ? 0.9258 0.5581 0.7325 -0.0066 -0.0486 0.0348  507 THR D C   
11831 O O   . THR D 206 ? 0.9725 0.5959 0.7719 -0.0092 -0.0469 0.0286  507 THR D O   
11832 C CB  . THR D 206 ? 0.6728 0.3307 0.4881 -0.0324 -0.0495 0.0427  507 THR D CB  
11833 O OG1 . THR D 206 ? 0.6002 0.2915 0.4336 -0.0396 -0.0490 0.0449  507 THR D OG1 
11834 C CG2 . THR D 206 ? 0.6425 0.2802 0.4400 -0.0469 -0.0487 0.0388  507 THR D CG2 
11835 N N   . GLU D 207 ? 0.9761 0.5893 0.7743 0.0051  -0.0507 0.0385  508 GLU D N   
11836 C CA  . GLU D 207 ? 0.9817 0.5622 0.7619 0.0168  -0.0511 0.0350  508 GLU D CA  
11837 C C   . GLU D 207 ? 0.9224 0.5178 0.7141 0.0306  -0.0488 0.0282  508 GLU D C   
11838 O O   . GLU D 207 ? 0.8962 0.4708 0.6746 0.0342  -0.0475 0.0220  508 GLU D O   
11839 C CB  . GLU D 207 ? 1.0711 0.6324 0.8419 0.0292  -0.0543 0.0409  508 GLU D CB  
11840 C CG  . GLU D 207 ? 1.1274 0.6585 0.8764 0.0173  -0.0564 0.0468  508 GLU D CG  
11841 C CD  . GLU D 207 ? 1.3243 0.8478 1.0698 0.0287  -0.0601 0.0543  508 GLU D CD  
11842 O OE1 . GLU D 207 ? 1.3635 0.9065 1.1242 0.0461  -0.0611 0.0544  508 GLU D OE1 
11843 O OE2 . GLU D 207 ? 1.3626 0.8615 1.0897 0.0196  -0.0619 0.0602  508 GLU D OE2 
11844 N N   . ILE D 208 ? 0.8675 0.4981 0.6826 0.0380  -0.0482 0.0290  509 ILE D N   
11845 C CA  . ILE D 208 ? 0.7699 0.4174 0.5964 0.0500  -0.0457 0.0230  509 ILE D CA  
11846 C C   . ILE D 208 ? 0.7615 0.4130 0.5869 0.0396  -0.0427 0.0170  509 ILE D C   
11847 O O   . ILE D 208 ? 0.7286 0.3707 0.5473 0.0464  -0.0407 0.0103  509 ILE D O   
11848 C CB  . ILE D 208 ? 0.7747 0.4594 0.6257 0.0564  -0.0454 0.0255  509 ILE D CB  
11849 C CG1 . ILE D 208 ? 0.9268 0.6093 0.7788 0.0676  -0.0486 0.0309  509 ILE D CG1 
11850 C CG2 . ILE D 208 ? 0.6647 0.3676 0.5266 0.0665  -0.0423 0.0193  509 ILE D CG2 
11851 C CD1 . ILE D 208 ? 0.9299 0.6485 0.8049 0.0723  -0.0484 0.0330  509 ILE D CD1 
11852 N N   . CYS D 209 ? 0.7408 0.4073 0.5725 0.0234  -0.0426 0.0190  510 CYS D N   
11853 C CA  . CYS D 209 ? 0.7901 0.4625 0.6206 0.0126  -0.0405 0.0139  510 CYS D CA  
11854 C C   . CYS D 209 ? 0.8563 0.4942 0.6629 0.0077  -0.0403 0.0090  510 CYS D C   
11855 O O   . CYS D 209 ? 0.8817 0.5162 0.6835 0.0098  -0.0382 0.0021  510 CYS D O   
11856 C CB  . CYS D 209 ? 0.8226 0.5146 0.6617 -0.0035 -0.0412 0.0174  510 CYS D CB  
11857 S SG  . CYS D 209 ? 0.7576 0.4891 0.6231 0.0002  -0.0410 0.0219  510 CYS D SG  
11858 N N   . ILE D 210 ? 0.8922 0.5033 0.6821 0.0000  -0.0424 0.0123  511 ILE D N   
11859 C CA  . ILE D 210 ? 0.9040 0.4786 0.6685 -0.0066 -0.0422 0.0078  511 ILE D CA  
11860 C C   . ILE D 210 ? 0.8949 0.4496 0.6500 0.0109  -0.0410 0.0019  511 ILE D C   
11861 O O   . ILE D 210 ? 0.9745 0.5154 0.7177 0.0087  -0.0391 -0.0056 511 ILE D O   
11862 C CB  . ILE D 210 ? 0.8798 0.4265 0.6266 -0.0162 -0.0446 0.0134  511 ILE D CB  
11863 C CG1 . ILE D 210 ? 0.8300 0.3987 0.5855 -0.0352 -0.0451 0.0176  511 ILE D CG1 
11864 C CG2 . ILE D 210 ? 0.7507 0.2543 0.4685 -0.0217 -0.0444 0.0087  511 ILE D CG2 
11865 C CD1 . ILE D 210 ? 0.8627 0.4065 0.6002 -0.0481 -0.0469 0.0229  511 ILE D CD1 
11866 N N   . GLN D 211 ? 0.8750 0.4310 0.6362 0.0290  -0.0420 0.0048  512 GLN D N   
11867 C CA  . GLN D 211 ? 0.9800 0.5203 0.7337 0.0480  -0.0409 -0.0009 512 GLN D CA  
11868 C C   . GLN D 211 ? 0.9979 0.5620 0.7635 0.0522  -0.0373 -0.0084 512 GLN D C   
11869 O O   . GLN D 211 ? 0.9738 0.5205 0.7273 0.0601  -0.0353 -0.0160 512 GLN D O   
11870 C CB  . GLN D 211 ? 1.0728 0.6187 0.8347 0.0665  -0.0430 0.0040  512 GLN D CB  
11871 C CG  . GLN D 211 ? 1.2291 0.7623 0.9848 0.0881  -0.0422 -0.0017 512 GLN D CG  
11872 C CD  . GLN D 211 ? 1.4135 0.9570 1.1789 0.1059  -0.0448 0.0032  512 GLN D CD  
11873 O OE1 . GLN D 211 ? 1.4602 1.0191 1.2363 0.1012  -0.0472 0.0109  512 GLN D OE1 
11874 N NE2 . GLN D 211 ? 1.4775 1.0140 1.2392 0.1268  -0.0444 -0.0015 512 GLN D NE2 
11875 N N   . GLN D 212 ? 0.8897 0.4927 0.6781 0.0471  -0.0362 -0.0064 513 GLN D N   
11876 C CA  . GLN D 212 ? 0.9202 0.5482 0.7204 0.0494  -0.0328 -0.0122 513 GLN D CA  
11877 C C   . GLN D 212 ? 0.8713 0.4939 0.6616 0.0342  -0.0314 -0.0173 513 GLN D C   
11878 O O   . GLN D 212 ? 0.8313 0.4748 0.6301 0.0342  -0.0287 -0.0216 513 GLN D O   
11879 C CB  . GLN D 212 ? 0.9054 0.5738 0.7312 0.0487  -0.0324 -0.0074 513 GLN D CB  
11880 C CG  . GLN D 212 ? 0.8885 0.5708 0.7273 0.0643  -0.0330 -0.0041 513 GLN D CG  
11881 C CD  . GLN D 212 ? 1.0685 0.7439 0.9030 0.0824  -0.0310 -0.0104 513 GLN D CD  
11882 O OE1 . GLN D 212 ? 1.1854 0.8512 1.0174 0.0960  -0.0329 -0.0087 513 GLN D OE1 
11883 N NE2 . GLN D 212 ? 1.0873 0.7689 0.9209 0.0832  -0.0274 -0.0178 513 GLN D NE2 
11884 N N   . GLY D 213 ? 0.8556 0.4526 0.6283 0.0203  -0.0332 -0.0168 514 GLY D N   
11885 C CA  . GLY D 213 ? 0.8208 0.4125 0.5829 0.0049  -0.0323 -0.0222 514 GLY D CA  
11886 C C   . GLY D 213 ? 0.8635 0.4673 0.6289 -0.0152 -0.0342 -0.0179 514 GLY D C   
11887 O O   . GLY D 213 ? 0.9148 0.5111 0.6685 -0.0296 -0.0341 -0.0222 514 GLY D O   
11888 N N   . TRP D 214 ? 0.9068 0.5299 0.6873 -0.0169 -0.0359 -0.0099 515 TRP D N   
11889 C CA  . TRP D 214 ? 0.9004 0.5384 0.6852 -0.0349 -0.0375 -0.0063 515 TRP D CA  
11890 C C   . TRP D 214 ? 0.9988 0.6061 0.7612 -0.0499 -0.0388 -0.0069 515 TRP D C   
11891 O O   . TRP D 214 ? 0.9110 0.4886 0.6593 -0.0463 -0.0398 -0.0046 515 TRP D O   
11892 C CB  . TRP D 214 ? 0.8878 0.5492 0.6913 -0.0326 -0.0389 0.0018  515 TRP D CB  
11893 C CG  . TRP D 214 ? 0.8487 0.5336 0.6610 -0.0479 -0.0400 0.0046  515 TRP D CG  
11894 C CD1 . TRP D 214 ? 0.8241 0.5329 0.6446 -0.0544 -0.0396 0.0018  515 TRP D CD1 
11895 C CD2 . TRP D 214 ? 0.7851 0.4733 0.5986 -0.0580 -0.0418 0.0104  515 TRP D CD2 
11896 N NE1 . TRP D 214 ? 0.8028 0.5303 0.6302 -0.0669 -0.0412 0.0054  515 TRP D NE1 
11897 C CE2 . TRP D 214 ? 0.7977 0.5136 0.6214 -0.0696 -0.0423 0.0105  515 TRP D CE2 
11898 C CE3 . TRP D 214 ? 0.7498 0.4210 0.5566 -0.0579 -0.0431 0.0157  515 TRP D CE3 
11899 C CZ2 . TRP D 214 ? 0.8117 0.5401 0.6396 -0.0809 -0.0436 0.0149  515 TRP D CZ2 
11900 C CZ3 . TRP D 214 ? 0.8634 0.5464 0.6739 -0.0701 -0.0443 0.0204  515 TRP D CZ3 
11901 C CH2 . TRP D 214 ? 0.7603 0.4723 0.5817 -0.0814 -0.0443 0.0197  515 TRP D CH2 
11902 N N   . LYS D 215 ? 1.0012 0.6163 0.7596 -0.0670 -0.0390 -0.0099 516 LYS D N   
11903 C CA  . LYS D 215 ? 0.9652 0.5565 0.7034 -0.0852 -0.0400 -0.0107 516 LYS D CA  
11904 C C   . LYS D 215 ? 0.9171 0.5320 0.6667 -0.0978 -0.0417 -0.0042 516 LYS D C   
11905 O O   . LYS D 215 ? 0.8874 0.5350 0.6508 -0.1054 -0.0420 -0.0047 516 LYS D O   
11906 C CB  . LYS D 215 ? 1.1075 0.6942 0.8335 -0.0971 -0.0393 -0.0191 516 LYS D CB  
11907 C CG  . LYS D 215 ? 1.2127 0.7805 0.9290 -0.0839 -0.0372 -0.0265 516 LYS D CG  
11908 C CD  . LYS D 215 ? 1.3004 0.8188 0.9890 -0.0831 -0.0369 -0.0295 516 LYS D CD  
11909 C CE  . LYS D 215 ? 1.3294 0.8311 1.0128 -0.0626 -0.0348 -0.0349 516 LYS D CE  
11910 N NZ  . LYS D 215 ? 1.2841 0.7879 0.9789 -0.0430 -0.0352 -0.0288 516 LYS D NZ  
11911 N N   . PRO D 216 ? 1.0013 0.6014 0.7450 -0.1000 -0.0427 0.0019  517 PRO D N   
11912 C CA  . PRO D 216 ? 0.8515 0.4775 0.6087 -0.1088 -0.0438 0.0082  517 PRO D CA  
11913 C C   . PRO D 216 ? 0.8442 0.4689 0.5897 -0.1326 -0.0442 0.0070  517 PRO D C   
11914 O O   . PRO D 216 ? 0.8576 0.4483 0.5790 -0.1428 -0.0439 0.0040  517 PRO D O   
11915 C CB  . PRO D 216 ? 0.8625 0.4700 0.6159 -0.0996 -0.0446 0.0149  517 PRO D CB  
11916 C CG  . PRO D 216 ? 0.9820 0.5435 0.7091 -0.0973 -0.0444 0.0121  517 PRO D CG  
11917 C CD  . PRO D 216 ? 1.0057 0.5647 0.7302 -0.0921 -0.0430 0.0035  517 PRO D CD  
11918 N N   . PRO D 217 ? 0.8321 0.4932 0.5937 -0.1421 -0.0447 0.0090  518 PRO D N   
11919 C CA  . PRO D 217 ? 0.8616 0.5254 0.6134 -0.1654 -0.0450 0.0084  518 PRO D CA  
11920 C C   . PRO D 217 ? 0.9149 0.5540 0.6518 -0.1736 -0.0450 0.0140  518 PRO D C   
11921 O O   . PRO D 217 ? 0.9984 0.6287 0.7203 -0.1944 -0.0447 0.0129  518 PRO D O   
11922 C CB  . PRO D 217 ? 0.7952 0.5078 0.5712 -0.1683 -0.0457 0.0098  518 PRO D CB  
11923 C CG  . PRO D 217 ? 0.6837 0.4138 0.4771 -0.1496 -0.0457 0.0089  518 PRO D CG  
11924 C CD  . PRO D 217 ? 0.6559 0.3579 0.4441 -0.1327 -0.0450 0.0108  518 PRO D CD  
11925 N N   . ARG D 218 ? 1.0020 0.6296 0.7416 -0.1588 -0.0453 0.0199  519 ARG D N   
11926 C CA  . ARG D 218 ? 1.0102 0.6196 0.7383 -0.1648 -0.0455 0.0266  519 ARG D CA  
11927 C C   . ARG D 218 ? 1.0631 0.7017 0.7984 -0.1838 -0.0451 0.0287  519 ARG D C   
11928 O O   . ARG D 218 ? 1.2032 0.8285 0.9209 -0.2041 -0.0445 0.0283  519 ARG D O   
11929 C CB  . ARG D 218 ? 1.0384 0.5959 0.7345 -0.1710 -0.0455 0.0258  519 ARG D CB  
11930 C CG  . ARG D 218 ? 1.1014 0.6303 0.7890 -0.1524 -0.0456 0.0221  519 ARG D CG  
11931 C CD  . ARG D 218 ? 1.1469 0.6226 0.8047 -0.1511 -0.0462 0.0244  519 ARG D CD  
11932 N NE  . ARG D 218 ? 1.2496 0.7200 0.9118 -0.1347 -0.0477 0.0322  519 ARG D NE  
11933 C CZ  . ARG D 218 ? 1.2496 0.7108 0.9158 -0.1110 -0.0486 0.0321  519 ARG D CZ  
11934 N NH1 . ARG D 218 ? 1.2286 0.6880 0.8990 -0.0974 -0.0503 0.0392  519 ARG D NH1 
11935 N NH2 . ARG D 218 ? 1.2296 0.6846 0.8951 -0.1012 -0.0476 0.0246  519 ARG D NH2 
11936 N N   . GLY D 219 ? 0.9735 0.6535 0.7350 -0.1766 -0.0453 0.0304  520 GLY D N   
11937 C CA  . GLY D 219 ? 0.8966 0.6090 0.6686 -0.1897 -0.0449 0.0327  520 GLY D CA  
11938 C C   . GLY D 219 ? 0.8919 0.6216 0.6805 -0.1769 -0.0451 0.0388  520 GLY D C   
11939 O O   . GLY D 219 ? 0.8785 0.5943 0.6694 -0.1593 -0.0458 0.0415  520 GLY D O   
11940 N N   . ARG D 220 ? 0.8836 0.6457 0.6840 -0.1860 -0.0445 0.0404  521 ARG D N   
11941 C CA  . ARG D 220 ? 0.7862 0.5644 0.6005 -0.1761 -0.0444 0.0458  521 ARG D CA  
11942 C C   . ARG D 220 ? 0.7840 0.5894 0.6224 -0.1579 -0.0450 0.0447  521 ARG D C   
11943 O O   . ARG D 220 ? 0.8248 0.6329 0.6721 -0.1449 -0.0453 0.0486  521 ARG D O   
11944 C CB  . ARG D 220 ? 0.8246 0.6271 0.6418 -0.1920 -0.0431 0.0475  521 ARG D CB  
11945 C CG  . ARG D 220 ? 0.8618 0.6771 0.6897 -0.1833 -0.0428 0.0529  521 ARG D CG  
11946 C CD  . ARG D 220 ? 1.0364 0.8348 0.8468 -0.1970 -0.0418 0.0580  521 ARG D CD  
11947 N NE  . ARG D 220 ? 1.1259 0.9582 0.9441 -0.2111 -0.0398 0.0576  521 ARG D NE  
11948 C CZ  . ARG D 220 ? 1.2164 1.0658 1.0425 -0.2090 -0.0389 0.0613  521 ARG D CZ  
11949 N NH1 . ARG D 220 ? 1.2503 1.0857 1.0772 -0.1942 -0.0400 0.0660  521 ARG D NH1 
11950 N NH2 . ARG D 220 ? 1.2550 1.1370 1.0882 -0.2218 -0.0368 0.0600  521 ARG D NH2 
11951 N N   . PHE D 221 ? 0.6593 0.4847 0.5076 -0.1572 -0.0453 0.0396  522 PHE D N   
11952 C CA  . PHE D 221 ? 0.6416 0.4939 0.5115 -0.1421 -0.0458 0.0389  522 PHE D CA  
11953 C C   . PHE D 221 ? 0.7162 0.5647 0.5866 -0.1357 -0.0464 0.0342  522 PHE D C   
11954 O O   . PHE D 221 ? 0.7205 0.5948 0.6026 -0.1344 -0.0470 0.0314  522 PHE D O   
11955 C CB  . PHE D 221 ? 0.6317 0.5235 0.5170 -0.1474 -0.0456 0.0384  522 PHE D CB  
11956 C CG  . PHE D 221 ? 0.7080 0.6073 0.5939 -0.1533 -0.0445 0.0424  522 PHE D CG  
11957 C CD1 . PHE D 221 ? 0.7799 0.6762 0.6721 -0.1412 -0.0443 0.0467  522 PHE D CD1 
11958 C CD2 . PHE D 221 ? 0.7473 0.6584 0.6274 -0.1718 -0.0436 0.0416  522 PHE D CD2 
11959 C CE1 . PHE D 221 ? 0.7589 0.6625 0.6509 -0.1468 -0.0433 0.0503  522 PHE D CE1 
11960 C CE2 . PHE D 221 ? 0.8033 0.7226 0.6835 -0.1777 -0.0422 0.0452  522 PHE D CE2 
11961 C CZ  . PHE D 221 ? 0.7809 0.6958 0.6668 -0.1649 -0.0420 0.0496  522 PHE D CZ  
11962 N N   . ASP D 222 ? 0.6514 0.4672 0.5081 -0.1309 -0.0463 0.0335  523 ASP D N   
11963 C CA  . ASP D 222 ? 0.6972 0.5079 0.5544 -0.1224 -0.0464 0.0292  523 ASP D CA  
11964 C C   . ASP D 222 ? 0.7099 0.5339 0.5841 -0.1041 -0.0463 0.0310  523 ASP D C   
11965 O O   . ASP D 222 ? 0.7531 0.5653 0.6281 -0.0941 -0.0461 0.0345  523 ASP D O   
11966 C CB  . ASP D 222 ? 0.6978 0.4690 0.5345 -0.1219 -0.0461 0.0273  523 ASP D CB  
11967 C CG  . ASP D 222 ? 0.7991 0.5499 0.6155 -0.1404 -0.0460 0.0265  523 ASP D CG  
11968 O OD1 . ASP D 222 ? 0.8694 0.6407 0.6882 -0.1555 -0.0461 0.0260  523 ASP D OD1 
11969 O OD2 . ASP D 222 ? 0.8878 0.6017 0.6850 -0.1399 -0.0459 0.0262  523 ASP D OD2 
11970 N N   . VAL D 223 ? 0.6281 0.4767 0.5151 -0.1002 -0.0466 0.0288  524 VAL D N   
11971 C CA  . VAL D 223 ? 0.5862 0.4433 0.4862 -0.0842 -0.0461 0.0300  524 VAL D CA  
11972 C C   . VAL D 223 ? 0.6339 0.4662 0.5252 -0.0755 -0.0452 0.0279  524 VAL D C   
11973 O O   . VAL D 223 ? 0.6446 0.4646 0.5248 -0.0796 -0.0450 0.0234  524 VAL D O   
11974 C CB  . VAL D 223 ? 0.4971 0.3818 0.4091 -0.0825 -0.0467 0.0283  524 VAL D CB  
11975 C CG1 . VAL D 223 ? 0.4613 0.3495 0.3827 -0.0678 -0.0459 0.0291  524 VAL D CG1 
11976 C CG2 . VAL D 223 ? 0.4709 0.3819 0.3933 -0.0876 -0.0476 0.0304  524 VAL D CG2 
11977 N N   . LEU D 224 ? 0.5176 0.3429 0.4132 -0.0635 -0.0447 0.0308  525 LEU D N   
11978 C CA  . LEU D 224 ? 0.5683 0.3722 0.4563 -0.0539 -0.0438 0.0287  525 LEU D CA  
11979 C C   . LEU D 224 ? 0.5703 0.3850 0.4645 -0.0473 -0.0425 0.0249  525 LEU D C   
11980 O O   . LEU D 224 ? 0.5269 0.3651 0.4329 -0.0474 -0.0426 0.0256  525 LEU D O   
11981 C CB  . LEU D 224 ? 0.5497 0.3488 0.4427 -0.0424 -0.0438 0.0326  525 LEU D CB  
11982 C CG  . LEU D 224 ? 0.5981 0.3765 0.4800 -0.0446 -0.0451 0.0362  525 LEU D CG  
11983 C CD1 . LEU D 224 ? 0.5489 0.3392 0.4430 -0.0357 -0.0455 0.0407  525 LEU D CD1 
11984 C CD2 . LEU D 224 ? 0.5154 0.2617 0.3800 -0.0395 -0.0451 0.0339  525 LEU D CD2 
11985 N N   . PRO D 225 ? 0.5850 0.3822 0.4704 -0.0410 -0.0414 0.0211  526 PRO D N   
11986 C CA  . PRO D 225 ? 0.6499 0.4578 0.5409 -0.0341 -0.0397 0.0178  526 PRO D CA  
11987 C C   . PRO D 225 ? 0.6207 0.4401 0.5252 -0.0215 -0.0385 0.0203  526 PRO D C   
11988 O O   . PRO D 225 ? 0.6207 0.4352 0.5279 -0.0160 -0.0390 0.0236  526 PRO D O   
11989 C CB  . PRO D 225 ? 0.6774 0.4609 0.5525 -0.0323 -0.0386 0.0121  526 PRO D CB  
11990 C CG  . PRO D 225 ? 0.6694 0.4282 0.5343 -0.0304 -0.0394 0.0140  526 PRO D CG  
11991 C CD  . PRO D 225 ? 0.6242 0.3898 0.4919 -0.0406 -0.0414 0.0191  526 PRO D CD  
11992 N N   . LEU D 226 ? 0.4422 0.2772 0.3543 -0.0175 -0.0369 0.0189  527 LEU D N   
11993 C CA  . LEU D 226 ? 0.5306 0.3755 0.4536 -0.0067 -0.0352 0.0203  527 LEU D CA  
11994 C C   . LEU D 226 ? 0.6607 0.4917 0.5774 0.0026  -0.0333 0.0163  527 LEU D C   
11995 O O   . LEU D 226 ? 0.7539 0.5728 0.6594 0.0016  -0.0324 0.0113  527 LEU D O   
11996 C CB  . LEU D 226 ? 0.5184 0.3836 0.4502 -0.0067 -0.0340 0.0207  527 LEU D CB  
11997 C CG  . LEU D 226 ? 0.6140 0.4945 0.5541 -0.0121 -0.0359 0.0251  527 LEU D CG  
11998 C CD1 . LEU D 226 ? 0.5955 0.4922 0.5412 -0.0115 -0.0350 0.0257  527 LEU D CD1 
11999 C CD2 . LEU D 226 ? 0.4791 0.3628 0.4278 -0.0083 -0.0363 0.0292  527 LEU D CD2 
12000 N N   . LEU D 227 ? 0.6173 0.4507 0.5409 0.0120  -0.0328 0.0181  528 LEU D N   
12001 C CA  . LEU D 227 ? 0.5690 0.3940 0.4893 0.0234  -0.0311 0.0145  528 LEU D CA  
12002 C C   . LEU D 227 ? 0.6102 0.4574 0.5447 0.0301  -0.0288 0.0151  528 LEU D C   
12003 O O   . LEU D 227 ? 0.5574 0.4144 0.5017 0.0330  -0.0297 0.0189  528 LEU D O   
12004 C CB  . LEU D 227 ? 0.5190 0.3265 0.4333 0.0288  -0.0333 0.0164  528 LEU D CB  
12005 C CG  . LEU D 227 ? 0.6480 0.4308 0.5476 0.0364  -0.0331 0.0120  528 LEU D CG  
12006 C CD1 . LEU D 227 ? 0.4696 0.2490 0.3717 0.0486  -0.0345 0.0144  528 LEU D CD1 
12007 C CD2 . LEU D 227 ? 0.4727 0.2563 0.3686 0.0410  -0.0297 0.0048  528 LEU D CD2 
12008 N N   . LEU D 228 ? 0.4577 0.3128 0.3925 0.0318  -0.0257 0.0110  529 LEU D N   
12009 C CA  . LEU D 228 ? 0.5308 0.4081 0.4777 0.0338  -0.0232 0.0120  529 LEU D CA  
12010 C C   . LEU D 228 ? 0.5551 0.4377 0.5034 0.0439  -0.0198 0.0072  529 LEU D C   
12011 O O   . LEU D 228 ? 0.5509 0.4239 0.4897 0.0471  -0.0181 0.0017  529 LEU D O   
12012 C CB  . LEU D 228 ? 0.6139 0.5005 0.5609 0.0255  -0.0223 0.0126  529 LEU D CB  
12013 C CG  . LEU D 228 ? 0.5827 0.4678 0.5290 0.0163  -0.0256 0.0167  529 LEU D CG  
12014 C CD1 . LEU D 228 ? 0.5382 0.4336 0.4842 0.0102  -0.0251 0.0172  529 LEU D CD1 
12015 C CD2 . LEU D 228 ? 0.5318 0.4237 0.4880 0.0166  -0.0272 0.0218  529 LEU D CD2 
12016 N N   . GLN D 229 ? 0.5260 0.4255 0.4861 0.0486  -0.0186 0.0088  530 GLN D N   
12017 C CA  . GLN D 229 ? 0.5710 0.4812 0.5351 0.0585  -0.0153 0.0044  530 GLN D CA  
12018 C C   . GLN D 229 ? 0.5303 0.4634 0.5036 0.0545  -0.0116 0.0049  530 GLN D C   
12019 O O   . GLN D 229 ? 0.5170 0.4608 0.4989 0.0496  -0.0124 0.0096  530 GLN D O   
12020 C CB  . GLN D 229 ? 0.6244 0.5353 0.5937 0.0679  -0.0174 0.0055  530 GLN D CB  
12021 C CG  . GLN D 229 ? 0.5905 0.5227 0.5697 0.0766  -0.0145 0.0025  530 GLN D CG  
12022 C CD  . GLN D 229 ? 0.6501 0.5814 0.6322 0.0876  -0.0174 0.0032  530 GLN D CD  
12023 O OE1 . GLN D 229 ? 0.7236 0.6503 0.7076 0.0853  -0.0212 0.0083  530 GLN D OE1 
12024 N NE2 . GLN D 229 ? 0.6847 0.6210 0.6668 0.1004  -0.0158 -0.0022 530 GLN D NE2 
12025 N N   . ALA D 230 ? 0.4961 0.4354 0.4663 0.0564  -0.0075 0.0000  531 ALA D N   
12026 C CA  . ALA D 230 ? 0.5219 0.4820 0.4985 0.0525  -0.0033 -0.0001 531 ALA D CA  
12027 C C   . ALA D 230 ? 0.5721 0.5477 0.5537 0.0620  0.0006  -0.0056 531 ALA D C   
12028 O O   . ALA D 230 ? 0.6861 0.6544 0.6614 0.0707  0.0016  -0.0115 531 ALA D O   
12029 C CB  . ALA D 230 ? 0.5582 0.5152 0.5259 0.0452  -0.0014 -0.0010 531 ALA D CB  
12030 N N   . ASN D 231 ? 0.5335 0.5310 0.5263 0.0601  0.0029  -0.0042 532 ASN D N   
12031 C CA  . ASN D 231 ? 0.5500 0.5693 0.5493 0.0667  0.0074  -0.0095 532 ASN D CA  
12032 C C   . ASN D 231 ? 0.5492 0.5668 0.5499 0.0818  0.0059  -0.0140 532 ASN D C   
12033 O O   . ASN D 231 ? 0.5444 0.5740 0.5460 0.0905  0.0095  -0.0205 532 ASN D O   
12034 C CB  . ASN D 231 ? 0.6190 0.6440 0.6117 0.0640  0.0127  -0.0138 532 ASN D CB  
12035 C CG  . ASN D 231 ? 0.6668 0.7205 0.6681 0.0622  0.0183  -0.0162 532 ASN D CG  
12036 O OD1 . ASN D 231 ? 0.7096 0.7767 0.7195 0.0557  0.0185  -0.0122 532 ASN D OD1 
12037 N ND2 . ASN D 231 ? 0.8144 0.8781 0.8127 0.0676  0.0232  -0.0232 532 ASN D ND2 
12038 N N   . GLY D 232 ? 0.5972 0.6004 0.5976 0.0857  0.0005  -0.0106 533 GLY D N   
12039 C CA  . GLY D 232 ? 0.4585 0.4579 0.4588 0.1008  -0.0016 -0.0139 533 GLY D CA  
12040 C C   . GLY D 232 ? 0.5432 0.5192 0.5293 0.1089  -0.0017 -0.0189 533 GLY D C   
12041 O O   . GLY D 232 ? 0.6068 0.5785 0.5909 0.1234  -0.0029 -0.0226 533 GLY D O   
12042 N N   . ASN D 233 ? 0.6537 0.6145 0.6292 0.1006  -0.0007 -0.0195 534 ASN D N   
12043 C CA  . ASN D 233 ? 0.6657 0.6018 0.6261 0.1068  -0.0010 -0.0246 534 ASN D CA  
12044 C C   . ASN D 233 ? 0.6325 0.5400 0.5840 0.1057  -0.0068 -0.0203 534 ASN D C   
12045 O O   . ASN D 233 ? 0.6231 0.5314 0.5802 0.0993  -0.0101 -0.0135 534 ASN D O   
12046 C CB  . ASN D 233 ? 0.6097 0.5431 0.5619 0.0978  0.0024  -0.0276 534 ASN D CB  
12047 C CG  . ASN D 233 ? 0.6599 0.6199 0.6184 0.0996  0.0086  -0.0324 534 ASN D CG  
12048 O OD1 . ASN D 233 ? 0.6793 0.6517 0.6422 0.1120  0.0110  -0.0377 534 ASN D OD1 
12049 N ND2 . ASN D 233 ? 0.6197 0.5896 0.5786 0.0873  0.0112  -0.0304 534 ASN D ND2 
12050 N N   . ASP D 234 ? 0.6593 0.5408 0.5957 0.1120  -0.0076 -0.0247 535 ASP D N   
12051 C CA  . ASP D 234 ? 0.6894 0.5416 0.6146 0.1090  -0.0126 -0.0209 535 ASP D CA  
12052 C C   . ASP D 234 ? 0.6902 0.5398 0.6145 0.0915  -0.0139 -0.0159 535 ASP D C   
12053 O O   . ASP D 234 ? 0.6691 0.5283 0.5937 0.0836  -0.0110 -0.0178 535 ASP D O   
12054 C CB  . ASP D 234 ? 0.7075 0.5293 0.6136 0.1162  -0.0127 -0.0270 535 ASP D CB  
12055 C CG  . ASP D 234 ? 0.7142 0.5358 0.6195 0.1360  -0.0119 -0.0321 535 ASP D CG  
12056 O OD1 . ASP D 234 ? 0.6657 0.5087 0.5849 0.1443  -0.0125 -0.0298 535 ASP D OD1 
12057 O OD2 . ASP D 234 ? 0.7725 0.5724 0.6627 0.1437  -0.0108 -0.0388 535 ASP D OD2 
12058 N N   . PRO D 235 ? 0.6707 0.5096 0.5941 0.0854  -0.0181 -0.0096 536 PRO D N   
12059 C CA  . PRO D 235 ? 0.6051 0.4444 0.5287 0.0700  -0.0194 -0.0053 536 PRO D CA  
12060 C C   . PRO D 235 ? 0.5976 0.4161 0.5053 0.0629  -0.0195 -0.0090 536 PRO D C   
12061 O O   . PRO D 235 ? 0.6077 0.4050 0.5020 0.0691  -0.0193 -0.0140 536 PRO D O   
12062 C CB  . PRO D 235 ? 0.6541 0.4871 0.5801 0.0675  -0.0237 0.0014  536 PRO D CB  
12063 C CG  . PRO D 235 ? 0.6457 0.4601 0.5632 0.0797  -0.0254 -0.0002 536 PRO D CG  
12064 C CD  . PRO D 235 ? 0.6812 0.5075 0.6027 0.0929  -0.0220 -0.0062 536 PRO D CD  
12065 N N   . GLU D 236 ? 0.6341 0.4585 0.5425 0.0500  -0.0199 -0.0067 537 GLU D N   
12066 C CA  . GLU D 236 ? 0.6526 0.4620 0.5469 0.0415  -0.0201 -0.0104 537 GLU D CA  
12067 C C   . GLU D 236 ? 0.6864 0.4926 0.5796 0.0284  -0.0237 -0.0053 537 GLU D C   
12068 O O   . GLU D 236 ? 0.7007 0.5229 0.6060 0.0249  -0.0249 0.0005  537 GLU D O   
12069 C CB  . GLU D 236 ? 0.6407 0.4650 0.5359 0.0395  -0.0166 -0.0145 537 GLU D CB  
12070 C CG  . GLU D 236 ? 0.6845 0.5174 0.5826 0.0521  -0.0123 -0.0197 537 GLU D CG  
12071 C CD  . GLU D 236 ? 0.7246 0.5765 0.6254 0.0492  -0.0084 -0.0223 537 GLU D CD  
12072 O OE1 . GLU D 236 ? 0.7165 0.5653 0.6094 0.0399  -0.0088 -0.0234 537 GLU D OE1 
12073 O OE2 . GLU D 236 ? 0.7165 0.5874 0.6269 0.0556  -0.0049 -0.0231 537 GLU D OE2 
12074 N N   . LEU D 237 ? 0.6163 0.4023 0.4945 0.0208  -0.0252 -0.0080 538 LEU D N   
12075 C CA  . LEU D 237 ? 0.6098 0.3944 0.4865 0.0078  -0.0283 -0.0039 538 LEU D CA  
12076 C C   . LEU D 237 ? 0.7314 0.5332 0.6108 -0.0018 -0.0283 -0.0043 538 LEU D C   
12077 O O   . LEU D 237 ? 0.7353 0.5398 0.6102 -0.0012 -0.0262 -0.0092 538 LEU D O   
12078 C CB  . LEU D 237 ? 0.5968 0.3520 0.4555 0.0022  -0.0301 -0.0061 538 LEU D CB  
12079 C CG  . LEU D 237 ? 0.6758 0.4112 0.5296 0.0107  -0.0312 -0.0040 538 LEU D CG  
12080 C CD1 . LEU D 237 ? 0.7150 0.4168 0.5470 0.0059  -0.0322 -0.0075 538 LEU D CD1 
12081 C CD2 . LEU D 237 ? 0.6892 0.4347 0.5536 0.0078  -0.0336 0.0038  538 LEU D CD2 
12082 N N   . PHE D 238 ? 0.7818 0.5960 0.6686 -0.0100 -0.0308 0.0010  539 PHE D N   
12083 C CA  . PHE D 238 ? 0.6985 0.5290 0.5874 -0.0190 -0.0318 0.0014  539 PHE D CA  
12084 C C   . PHE D 238 ? 0.6882 0.5221 0.5786 -0.0290 -0.0351 0.0052  539 PHE D C   
12085 O O   . PHE D 238 ? 0.6873 0.5237 0.5854 -0.0272 -0.0360 0.0100  539 PHE D O   
12086 C CB  . PHE D 238 ? 0.6643 0.5177 0.5665 -0.0142 -0.0306 0.0046  539 PHE D CB  
12087 C CG  . PHE D 238 ? 0.6420 0.4968 0.5449 -0.0049 -0.0269 0.0015  539 PHE D CG  
12088 C CD1 . PHE D 238 ? 0.6949 0.5512 0.5903 -0.0059 -0.0250 -0.0033 539 PHE D CD1 
12089 C CD2 . PHE D 238 ? 0.6775 0.5343 0.5887 0.0045  -0.0252 0.0032  539 PHE D CD2 
12090 C CE1 . PHE D 238 ? 0.6666 0.5263 0.5628 0.0023  -0.0211 -0.0065 539 PHE D CE1 
12091 C CE2 . PHE D 238 ? 0.6975 0.5588 0.6102 0.0126  -0.0215 -0.0001 539 PHE D CE2 
12092 C CZ  . PHE D 238 ? 0.6837 0.5467 0.5890 0.0116  -0.0192 -0.0049 539 PHE D CZ  
12093 N N   . GLN D 239 ? 0.6392 0.4756 0.5226 -0.0399 -0.0368 0.0029  540 GLN D N   
12094 C CA  . GLN D 239 ? 0.7228 0.5679 0.6085 -0.0503 -0.0397 0.0059  540 GLN D CA  
12095 C C   . GLN D 239 ? 0.7001 0.5729 0.5992 -0.0496 -0.0409 0.0097  540 GLN D C   
12096 O O   . GLN D 239 ? 0.5718 0.4555 0.4698 -0.0505 -0.0412 0.0078  540 GLN D O   
12097 C CB  . GLN D 239 ? 0.8187 0.6548 0.6901 -0.0635 -0.0411 0.0011  540 GLN D CB  
12098 C CG  . GLN D 239 ? 0.9336 0.7839 0.8080 -0.0757 -0.0439 0.0035  540 GLN D CG  
12099 C CD  . GLN D 239 ? 1.0611 0.9225 0.9291 -0.0871 -0.0457 -0.0008 540 GLN D CD  
12100 O OE1 . GLN D 239 ? 1.1434 1.0219 1.0161 -0.0837 -0.0462 -0.0015 540 GLN D OE1 
12101 N NE2 . GLN D 239 ? 1.0286 0.8807 0.8853 -0.1010 -0.0468 -0.0036 540 GLN D NE2 
12102 N N   . ILE D 240 ? 0.5773 0.4601 0.4876 -0.0473 -0.0417 0.0150  541 ILE D N   
12103 C CA  . ILE D 240 ? 0.5937 0.5006 0.5151 -0.0467 -0.0433 0.0185  541 ILE D CA  
12104 C C   . ILE D 240 ? 0.6369 0.5553 0.5540 -0.0572 -0.0460 0.0164  541 ILE D C   
12105 O O   . ILE D 240 ? 0.6467 0.5586 0.5570 -0.0671 -0.0470 0.0145  541 ILE D O   
12106 C CB  . ILE D 240 ? 0.5474 0.4614 0.4796 -0.0440 -0.0438 0.0235  541 ILE D CB  
12107 C CG1 . ILE D 240 ? 0.5754 0.4790 0.5114 -0.0348 -0.0415 0.0253  541 ILE D CG1 
12108 C CG2 . ILE D 240 ? 0.4397 0.3759 0.3820 -0.0414 -0.0452 0.0267  541 ILE D CG2 
12109 C CD1 . ILE D 240 ? 0.5352 0.4478 0.4822 -0.0316 -0.0418 0.0299  541 ILE D CD1 
12110 N N   . PRO D 241 ? 0.6671 0.6028 0.5870 -0.0560 -0.0474 0.0166  542 PRO D N   
12111 C CA  . PRO D 241 ? 0.6246 0.5754 0.5415 -0.0655 -0.0505 0.0145  542 PRO D CA  
12112 C C   . PRO D 241 ? 0.5952 0.5591 0.5192 -0.0708 -0.0524 0.0168  542 PRO D C   
12113 O O   . PRO D 241 ? 0.5595 0.5334 0.4945 -0.0638 -0.0525 0.0212  542 PRO D O   
12114 C CB  . PRO D 241 ? 0.5466 0.5143 0.4673 -0.0593 -0.0519 0.0162  542 PRO D CB  
12115 C CG  . PRO D 241 ? 0.5319 0.4871 0.4521 -0.0499 -0.0486 0.0171  542 PRO D CG  
12116 C CD  . PRO D 241 ? 0.6541 0.5961 0.5788 -0.0462 -0.0463 0.0188  542 PRO D CD  
12117 N N   . PRO D 242 ? 0.5148 0.4791 0.4319 -0.0836 -0.0537 0.0136  543 PRO D N   
12118 C CA  . PRO D 242 ? 0.6042 0.5811 0.5272 -0.0901 -0.0548 0.0154  543 PRO D CA  
12119 C C   . PRO D 242 ? 0.6345 0.6409 0.5708 -0.0845 -0.0570 0.0184  543 PRO D C   
12120 O O   . PRO D 242 ? 0.5478 0.5625 0.4925 -0.0828 -0.0568 0.0213  543 PRO D O   
12121 C CB  . PRO D 242 ? 0.6247 0.6000 0.5362 -0.1065 -0.0559 0.0104  543 PRO D CB  
12122 C CG  . PRO D 242 ? 0.6791 0.6285 0.5767 -0.1075 -0.0543 0.0064  543 PRO D CG  
12123 C CD  . PRO D 242 ? 0.5782 0.5298 0.4807 -0.0937 -0.0537 0.0077  543 PRO D CD  
12124 N N   . GLU D 243 ? 0.5233 0.5450 0.4609 -0.0807 -0.0593 0.0179  544 GLU D N   
12125 C CA  . GLU D 243 ? 0.4180 0.4665 0.3667 -0.0738 -0.0619 0.0208  544 GLU D CA  
12126 C C   . GLU D 243 ? 0.4773 0.5217 0.4344 -0.0597 -0.0604 0.0259  544 GLU D C   
12127 O O   . GLU D 243 ? 0.5122 0.5750 0.4778 -0.0527 -0.0623 0.0285  544 GLU D O   
12128 C CB  . GLU D 243 ? 0.5294 0.5938 0.4752 -0.0729 -0.0652 0.0194  544 GLU D CB  
12129 C CG  . GLU D 243 ? 0.4409 0.4915 0.3813 -0.0643 -0.0642 0.0205  544 GLU D CG  
12130 C CD  . GLU D 243 ? 0.5746 0.6058 0.5020 -0.0720 -0.0624 0.0157  544 GLU D CD  
12131 O OE1 . GLU D 243 ? 0.6065 0.6296 0.5280 -0.0835 -0.0618 0.0118  544 GLU D OE1 
12132 O OE2 . GLU D 243 ? 0.6635 0.6869 0.5854 -0.0668 -0.0615 0.0155  544 GLU D OE2 
12133 N N   . LEU D 244 ? 0.4855 0.5067 0.4400 -0.0554 -0.0572 0.0270  545 LEU D N   
12134 C CA  . LEU D 244 ? 0.4449 0.4619 0.4070 -0.0443 -0.0556 0.0312  545 LEU D CA  
12135 C C   . LEU D 244 ? 0.5194 0.5320 0.4867 -0.0454 -0.0540 0.0326  545 LEU D C   
12136 O O   . LEU D 244 ? 0.4776 0.4893 0.4517 -0.0372 -0.0529 0.0358  545 LEU D O   
12137 C CB  . LEU D 244 ? 0.4294 0.4277 0.3870 -0.0386 -0.0529 0.0317  545 LEU D CB  
12138 C CG  . LEU D 244 ? 0.5082 0.5082 0.4607 -0.0348 -0.0534 0.0316  545 LEU D CG  
12139 C CD1 . LEU D 244 ? 0.4587 0.4417 0.4090 -0.0294 -0.0497 0.0322  545 LEU D CD1 
12140 C CD2 . LEU D 244 ? 0.5303 0.5472 0.4875 -0.0279 -0.0561 0.0351  545 LEU D CD2 
12141 N N   . VAL D 245 ? 0.4701 0.4793 0.4334 -0.0559 -0.0538 0.0304  546 VAL D N   
12142 C CA  . VAL D 245 ? 0.5155 0.5192 0.4816 -0.0581 -0.0524 0.0319  546 VAL D CA  
12143 C C   . VAL D 245 ? 0.4746 0.5025 0.4474 -0.0624 -0.0540 0.0319  546 VAL D C   
12144 O O   . VAL D 245 ? 0.4329 0.4685 0.4016 -0.0741 -0.0549 0.0293  546 VAL D O   
12145 C CB  . VAL D 245 ? 0.5024 0.4844 0.4578 -0.0669 -0.0510 0.0301  546 VAL D CB  
12146 C CG1 . VAL D 245 ? 0.5680 0.5445 0.5252 -0.0688 -0.0498 0.0325  546 VAL D CG1 
12147 C CG2 . VAL D 245 ? 0.4553 0.4158 0.4045 -0.0612 -0.0494 0.0293  546 VAL D CG2 
12148 N N   . LEU D 246 ? 0.3947 0.4351 0.3773 -0.0534 -0.0541 0.0344  547 LEU D N   
12149 C CA  . LEU D 246 ? 0.4247 0.4896 0.4143 -0.0558 -0.0553 0.0339  547 LEU D CA  
12150 C C   . LEU D 246 ? 0.4527 0.5122 0.4417 -0.0633 -0.0533 0.0343  547 LEU D C   
12151 O O   . LEU D 246 ? 0.5254 0.5675 0.5139 -0.0593 -0.0514 0.0365  547 LEU D O   
12152 C CB  . LEU D 246 ? 0.4231 0.5010 0.4219 -0.0425 -0.0561 0.0360  547 LEU D CB  
12153 C CG  . LEU D 246 ? 0.4656 0.5682 0.4730 -0.0412 -0.0567 0.0353  547 LEU D CG  
12154 C CD1 . LEU D 246 ? 0.4568 0.5863 0.4661 -0.0448 -0.0598 0.0327  547 LEU D CD1 
12155 C CD2 . LEU D 246 ? 0.4430 0.5462 0.4566 -0.0269 -0.0564 0.0376  547 LEU D CD2 
12156 N N   . GLU D 247 ? 0.4356 0.5103 0.4237 -0.0749 -0.0538 0.0322  548 GLU D N   
12157 C CA  . GLU D 247 ? 0.4728 0.5428 0.4579 -0.0843 -0.0518 0.0327  548 GLU D CA  
12158 C C   . GLU D 247 ? 0.4760 0.5771 0.4694 -0.0878 -0.0520 0.0314  548 GLU D C   
12159 O O   . GLU D 247 ? 0.4862 0.6127 0.4855 -0.0864 -0.0541 0.0292  548 GLU D O   
12160 C CB  . GLU D 247 ? 0.4000 0.4523 0.3714 -0.0990 -0.0514 0.0312  548 GLU D CB  
12161 C CG  . GLU D 247 ? 0.5116 0.5308 0.4738 -0.0956 -0.0505 0.0324  548 GLU D CG  
12162 C CD  . GLU D 247 ? 0.6425 0.6432 0.5895 -0.1093 -0.0504 0.0301  548 GLU D CD  
12163 O OE1 . GLU D 247 ? 0.7249 0.7380 0.6690 -0.1186 -0.0517 0.0266  548 GLU D OE1 
12164 O OE2 . GLU D 247 ? 0.7190 0.6926 0.6563 -0.1109 -0.0491 0.0317  548 GLU D OE2 
12165 N N   . VAL D 248 ? 0.4400 0.5401 0.4335 -0.0921 -0.0499 0.0328  549 VAL D N   
12166 C CA  . VAL D 248 ? 0.3997 0.5294 0.4012 -0.0948 -0.0493 0.0313  549 VAL D CA  
12167 C C   . VAL D 248 ? 0.4888 0.6161 0.4819 -0.1126 -0.0474 0.0311  549 VAL D C   
12168 O O   . VAL D 248 ? 0.3818 0.4864 0.3679 -0.1150 -0.0456 0.0341  549 VAL D O   
12169 C CB  . VAL D 248 ? 0.4096 0.5433 0.4200 -0.0815 -0.0481 0.0330  549 VAL D CB  
12170 C CG1 . VAL D 248 ? 0.4306 0.5963 0.4490 -0.0840 -0.0470 0.0307  549 VAL D CG1 
12171 C CG2 . VAL D 248 ? 0.3147 0.4460 0.3309 -0.0649 -0.0497 0.0337  549 VAL D CG2 
12172 N N   . PRO D 249 ? 0.3303 0.4802 0.3228 -0.1257 -0.0478 0.0280  550 PRO D N   
12173 C CA  . PRO D 249 ? 0.5205 0.6694 0.5042 -0.1441 -0.0455 0.0280  550 PRO D CA  
12174 C C   . PRO D 249 ? 0.5554 0.7236 0.5468 -0.1423 -0.0431 0.0286  550 PRO D C   
12175 O O   . PRO D 249 ? 0.5241 0.7230 0.5289 -0.1332 -0.0435 0.0263  550 PRO D O   
12176 C CB  . PRO D 249 ? 0.4266 0.5989 0.4091 -0.1580 -0.0468 0.0236  550 PRO D CB  
12177 C CG  . PRO D 249 ? 0.3355 0.5380 0.3330 -0.1435 -0.0494 0.0212  550 PRO D CG  
12178 C CD  . PRO D 249 ? 0.3729 0.5535 0.3733 -0.1241 -0.0503 0.0242  550 PRO D CD  
12179 N N   . ILE D 250 ? 0.5145 0.6640 0.4966 -0.1503 -0.0407 0.0317  551 ILE D N   
12180 C CA  . ILE D 250 ? 0.4950 0.6579 0.4830 -0.1472 -0.0383 0.0327  551 ILE D CA  
12181 C C   . ILE D 250 ? 0.4653 0.6582 0.4536 -0.1636 -0.0362 0.0301  551 ILE D C   
12182 O O   . ILE D 250 ? 0.5715 0.7533 0.5462 -0.1823 -0.0350 0.0309  551 ILE D O   
12183 C CB  . ILE D 250 ? 0.4794 0.6088 0.4574 -0.1461 -0.0371 0.0377  551 ILE D CB  
12184 C CG1 . ILE D 250 ? 0.4805 0.5833 0.4586 -0.1312 -0.0391 0.0396  551 ILE D CG1 
12185 C CG2 . ILE D 250 ? 0.4434 0.5873 0.4280 -0.1412 -0.0348 0.0384  551 ILE D CG2 
12186 C CD1 . ILE D 250 ? 0.3617 0.4811 0.3547 -0.1138 -0.0405 0.0376  551 ILE D CD1 
12187 N N   . ARG D 251 ? 0.4156 0.6461 0.4184 -0.1568 -0.0355 0.0266  552 ARG D N   
12188 C CA  . ARG D 251 ? 0.4768 0.7410 0.4821 -0.1705 -0.0328 0.0237  552 ARG D CA  
12189 C C   . ARG D 251 ? 0.4810 0.7607 0.4948 -0.1607 -0.0302 0.0235  552 ARG D C   
12190 O O   . ARG D 251 ? 0.4464 0.7134 0.4652 -0.1430 -0.0309 0.0249  552 ARG D O   
12191 C CB  . ARG D 251 ? 0.4006 0.7038 0.4157 -0.1733 -0.0345 0.0182  552 ARG D CB  
12192 C CG  . ARG D 251 ? 0.4680 0.7908 0.4988 -0.1509 -0.0374 0.0157  552 ARG D CG  
12193 C CD  . ARG D 251 ? 0.4607 0.7579 0.4888 -0.1412 -0.0413 0.0174  552 ARG D CD  
12194 N NE  . ARG D 251 ? 0.4313 0.7523 0.4725 -0.1235 -0.0444 0.0148  552 ARG D NE  
12195 C CZ  . ARG D 251 ? 0.4729 0.7774 0.5146 -0.1098 -0.0475 0.0163  552 ARG D CZ  
12196 N NH1 . ARG D 251 ? 0.4788 0.8065 0.5311 -0.0943 -0.0503 0.0143  552 ARG D NH1 
12197 N NH2 . ARG D 251 ? 0.4714 0.7371 0.5026 -0.1110 -0.0480 0.0198  552 ARG D NH2 
12198 N N   . HIS D 252 ? 0.4875 0.7952 0.5023 -0.1732 -0.0269 0.0213  553 HIS D N   
12199 C CA  . HIS D 252 ? 0.4756 0.8002 0.4972 -0.1660 -0.0238 0.0203  553 HIS D CA  
12200 C C   . HIS D 252 ? 0.4548 0.8308 0.4919 -0.1625 -0.0227 0.0137  553 HIS D C   
12201 O O   . HIS D 252 ? 0.4914 0.8936 0.5294 -0.1767 -0.0225 0.0106  553 HIS D O   
12202 C CB  . HIS D 252 ? 0.4004 0.7121 0.4081 -0.1835 -0.0201 0.0239  553 HIS D CB  
12203 C CG  . HIS D 252 ? 0.4703 0.7901 0.4818 -0.1757 -0.0171 0.0238  553 HIS D CG  
12204 N ND1 . HIS D 252 ? 0.4686 0.8306 0.4902 -0.1761 -0.0138 0.0187  553 HIS D ND1 
12205 C CD2 . HIS D 252 ? 0.4981 0.7902 0.5041 -0.1677 -0.0168 0.0278  553 HIS D CD2 
12206 C CE1 . HIS D 252 ? 0.4569 0.8154 0.4786 -0.1686 -0.0115 0.0194  553 HIS D CE1 
12207 N NE2 . HIS D 252 ? 0.4478 0.7643 0.4601 -0.1637 -0.0134 0.0250  553 HIS D NE2 
12208 N N   . PRO D 253 ? 0.4465 0.8384 0.4952 -0.1439 -0.0221 0.0110  554 PRO D N   
12209 C CA  . PRO D 253 ? 0.3604 0.8017 0.4243 -0.1371 -0.0214 0.0043  554 PRO D CA  
12210 C C   . PRO D 253 ? 0.4969 0.9731 0.5609 -0.1552 -0.0169 0.0012  554 PRO D C   
12211 O O   . PRO D 253 ? 0.6219 1.1429 0.6974 -0.1552 -0.0166 -0.0046 554 PRO D O   
12212 C CB  . PRO D 253 ? 0.3689 0.8085 0.4410 -0.1132 -0.0213 0.0029  554 PRO D CB  
12213 C CG  . PRO D 253 ? 0.3947 0.7974 0.4553 -0.1167 -0.0192 0.0079  554 PRO D CG  
12214 C CD  . PRO D 253 ? 0.4599 0.8267 0.5076 -0.1291 -0.0215 0.0136  554 PRO D CD  
12215 N N   . LYS D 254 ? 0.3985 0.8569 0.4499 -0.1707 -0.0133 0.0048  555 LYS D N   
12216 C CA  . LYS D 254 ? 0.5282 1.0174 0.5776 -0.1895 -0.0083 0.0024  555 LYS D CA  
12217 C C   . LYS D 254 ? 0.5400 1.0135 0.5727 -0.2173 -0.0073 0.0062  555 LYS D C   
12218 O O   . LYS D 254 ? 0.6013 1.1081 0.6349 -0.2351 -0.0050 0.0027  555 LYS D O   
12219 C CB  . LYS D 254 ? 0.6628 1.1479 0.7096 -0.1854 -0.0042 0.0033  555 LYS D CB  
12220 C CG  . LYS D 254 ? 0.7451 1.2473 0.8066 -0.1596 -0.0043 -0.0014 555 LYS D CG  
12221 C CD  . LYS D 254 ? 0.8468 1.4034 0.9249 -0.1536 -0.0036 -0.0095 555 LYS D CD  
12222 C CE  . LYS D 254 ? 0.9469 1.5251 1.0353 -0.1345 -0.0010 -0.0149 555 LYS D CE  
12223 N NZ  . LYS D 254 ? 0.9404 1.4789 1.0262 -0.1150 -0.0032 -0.0119 555 LYS D NZ  
12224 N N   . PHE D 255 ? 0.5759 0.9993 0.5928 -0.2216 -0.0089 0.0131  556 PHE D N   
12225 C CA  . PHE D 255 ? 0.6201 1.0207 0.6179 -0.2469 -0.0080 0.0172  556 PHE D CA  
12226 C C   . PHE D 255 ? 0.7198 1.1170 0.7173 -0.2515 -0.0119 0.0156  556 PHE D C   
12227 O O   . PHE D 255 ? 0.7297 1.0963 0.7260 -0.2390 -0.0159 0.0179  556 PHE D O   
12228 C CB  . PHE D 255 ? 0.6557 1.0039 0.6361 -0.2473 -0.0084 0.0250  556 PHE D CB  
12229 C CG  . PHE D 255 ? 0.6629 1.0128 0.6413 -0.2447 -0.0048 0.0269  556 PHE D CG  
12230 C CD1 . PHE D 255 ? 0.6824 1.0655 0.6603 -0.2596 0.0002  0.0245  556 PHE D CD1 
12231 C CD2 . PHE D 255 ? 0.6329 0.9523 0.6095 -0.2281 -0.0064 0.0308  556 PHE D CD2 
12232 C CE1 . PHE D 255 ? 0.6653 1.0501 0.6405 -0.2573 0.0036  0.0260  556 PHE D CE1 
12233 C CE2 . PHE D 255 ? 0.6028 0.9240 0.5769 -0.2260 -0.0034 0.0323  556 PHE D CE2 
12234 C CZ  . PHE D 255 ? 0.6391 0.9922 0.6120 -0.2404 0.0016  0.0299  556 PHE D CZ  
12235 N N   . GLU D 256 ? 0.6848 1.1154 0.6835 -0.2700 -0.0105 0.0113  557 GLU D N   
12236 C CA  . GLU D 256 ? 0.7265 1.1557 0.7237 -0.2767 -0.0142 0.0094  557 GLU D CA  
12237 C C   . GLU D 256 ? 0.7362 1.1125 0.7103 -0.2911 -0.0151 0.0150  557 GLU D C   
12238 O O   . GLU D 256 ? 0.7199 1.0781 0.6910 -0.2890 -0.0189 0.0147  557 GLU D O   
12239 C CB  . GLU D 256 ? 0.7962 1.2720 0.7978 -0.2914 -0.0122 0.0030  557 GLU D CB  
12240 C CG  . GLU D 256 ? 0.9026 1.4294 0.9256 -0.2740 -0.0111 -0.0030 557 GLU D CG  
12241 C CD  . GLU D 256 ? 1.0455 1.6058 1.0640 -0.2854 -0.0062 -0.0079 557 GLU D CD  
12242 O OE1 . GLU D 256 ? 1.1509 1.7095 1.1565 -0.3022 -0.0058 -0.0093 557 GLU D OE1 
12243 O OE2 . GLU D 256 ? 1.0218 1.6101 1.0488 -0.2778 -0.0028 -0.0107 557 GLU D OE2 
12244 N N   . TRP D 257 ? 0.7098 1.0596 0.6665 -0.3049 -0.0118 0.0202  558 TRP D N   
12245 C CA  . TRP D 257 ? 0.7212 1.0179 0.6544 -0.3168 -0.0130 0.0257  558 TRP D CA  
12246 C C   . TRP D 257 ? 0.7477 1.0037 0.6802 -0.2948 -0.0169 0.0295  558 TRP D C   
12247 O O   . TRP D 257 ? 0.8434 1.0573 0.7590 -0.3004 -0.0187 0.0328  558 TRP D O   
12248 C CB  . TRP D 257 ? 0.7913 1.0669 0.7047 -0.3345 -0.0089 0.0313  558 TRP D CB  
12249 C CG  . TRP D 257 ? 0.7902 1.0759 0.7106 -0.3225 -0.0064 0.0334  558 TRP D CG  
12250 C CD1 . TRP D 257 ? 0.6926 1.0226 0.6230 -0.3275 -0.0022 0.0300  558 TRP D CD1 
12251 C CD2 . TRP D 257 ? 0.7774 1.0295 0.6950 -0.3042 -0.0079 0.0389  558 TRP D CD2 
12252 N NE1 . TRP D 257 ? 0.6296 0.9542 0.5629 -0.3134 -0.0009 0.0328  558 TRP D NE1 
12253 C CE2 . TRP D 257 ? 0.6985 0.9760 0.6241 -0.2995 -0.0045 0.0384  558 TRP D CE2 
12254 C CE3 . TRP D 257 ? 0.7613 0.9667 0.6709 -0.2914 -0.0117 0.0437  558 TRP D CE3 
12255 C CZ2 . TRP D 257 ? 0.6425 0.8992 0.5676 -0.2832 -0.0050 0.0425  558 TRP D CZ2 
12256 C CZ3 . TRP D 257 ? 0.7271 0.9139 0.6372 -0.2751 -0.0122 0.0479  558 TRP D CZ3 
12257 C CH2 . TRP D 257 ? 0.6463 0.8584 0.5639 -0.2716 -0.0090 0.0473  558 TRP D CH2 
12258 N N   . PHE D 258 ? 0.6499 0.9174 0.5996 -0.2703 -0.0181 0.0288  559 PHE D N   
12259 C CA  . PHE D 258 ? 0.6255 0.8537 0.5730 -0.2514 -0.0210 0.0330  559 PHE D CA  
12260 C C   . PHE D 258 ? 0.5901 0.7980 0.5349 -0.2477 -0.0249 0.0321  559 PHE D C   
12261 O O   . PHE D 258 ? 0.5560 0.7205 0.4874 -0.2455 -0.0264 0.0364  559 PHE D O   
12262 C CB  . PHE D 258 ? 0.5735 0.8193 0.5394 -0.2275 -0.0213 0.0317  559 PHE D CB  
12263 C CG  . PHE D 258 ? 0.5995 0.8072 0.5607 -0.2126 -0.0228 0.0369  559 PHE D CG  
12264 C CD1 . PHE D 258 ? 0.5206 0.7020 0.4819 -0.1999 -0.0264 0.0381  559 PHE D CD1 
12265 C CD2 . PHE D 258 ? 0.6303 0.8303 0.5868 -0.2119 -0.0204 0.0404  559 PHE D CD2 
12266 C CE1 . PHE D 258 ? 0.5447 0.6944 0.5023 -0.1868 -0.0276 0.0424  559 PHE D CE1 
12267 C CE2 . PHE D 258 ? 0.5868 0.7546 0.5392 -0.1986 -0.0220 0.0450  559 PHE D CE2 
12268 C CZ  . PHE D 258 ? 0.6127 0.7560 0.5662 -0.1862 -0.0256 0.0459  559 PHE D CZ  
12269 N N   . LYS D 259 ? 0.5161 0.7558 0.4730 -0.2469 -0.0265 0.0265  560 LYS D N   
12270 C CA  . LYS D 259 ? 0.6057 0.8294 0.5593 -0.2453 -0.0301 0.0251  560 LYS D CA  
12271 C C   . LYS D 259 ? 0.6363 0.8234 0.5665 -0.2656 -0.0297 0.0272  560 LYS D C   
12272 O O   . LYS D 259 ? 0.5340 0.6906 0.4565 -0.2613 -0.0323 0.0278  560 LYS D O   
12273 C CB  . LYS D 259 ? 0.5970 0.8652 0.5654 -0.2451 -0.0319 0.0186  560 LYS D CB  
12274 C CG  . LYS D 259 ? 0.6679 0.9720 0.6354 -0.2681 -0.0295 0.0146  560 LYS D CG  
12275 C CD  . LYS D 259 ? 0.7312 1.0759 0.7120 -0.2671 -0.0324 0.0082  560 LYS D CD  
12276 C CE  . LYS D 259 ? 0.7527 1.1357 0.7326 -0.2918 -0.0302 0.0035  560 LYS D CE  
12277 N NZ  . LYS D 259 ? 0.7834 1.1974 0.7707 -0.2953 -0.0258 0.0029  560 LYS D NZ  
12278 N N   . ASP D 260 ? 0.6342 0.8216 0.5515 -0.2873 -0.0264 0.0284  561 ASP D N   
12279 C CA  . ASP D 260 ? 0.7317 0.8808 0.6239 -0.3074 -0.0259 0.0307  561 ASP D CA  
12280 C C   . ASP D 260 ? 0.7019 0.7980 0.5784 -0.2993 -0.0265 0.0374  561 ASP D C   
12281 O O   . ASP D 260 ? 0.7214 0.7787 0.5758 -0.3116 -0.0267 0.0395  561 ASP D O   
12282 C CB  . ASP D 260 ? 0.8346 1.0002 0.7166 -0.3343 -0.0219 0.0303  561 ASP D CB  
12283 C CG  . ASP D 260 ? 0.9435 1.1660 0.8418 -0.3426 -0.0213 0.0231  561 ASP D CG  
12284 O OD1 . ASP D 260 ? 0.9902 1.2343 0.9053 -0.3278 -0.0245 0.0189  561 ASP D OD1 
12285 O OD2 . ASP D 260 ? 0.9259 1.1678 0.8179 -0.3565 -0.0174 0.0216  561 ASP D OD2 
12286 N N   . LEU D 261 ? 0.6312 0.7245 0.5180 -0.2787 -0.0269 0.0406  562 LEU D N   
12287 C CA  . LEU D 261 ? 0.6738 0.7199 0.5479 -0.2685 -0.0283 0.0464  562 LEU D CA  
12288 C C   . LEU D 261 ? 0.7214 0.7440 0.5943 -0.2577 -0.0316 0.0448  562 LEU D C   
12289 O O   . LEU D 261 ? 0.7274 0.7076 0.5854 -0.2534 -0.0328 0.0485  562 LEU D O   
12290 C CB  . LEU D 261 ? 0.6237 0.6761 0.5097 -0.2503 -0.0280 0.0495  562 LEU D CB  
12291 C CG  . LEU D 261 ? 0.6407 0.7144 0.5259 -0.2613 -0.0243 0.0511  562 LEU D CG  
12292 C CD1 . LEU D 261 ? 0.5124 0.6019 0.4129 -0.2430 -0.0239 0.0521  562 LEU D CD1 
12293 C CD2 . LEU D 261 ? 0.6617 0.7000 0.5207 -0.2782 -0.0229 0.0571  562 LEU D CD2 
12294 N N   . GLY D 262 ? 0.6988 0.7487 0.5862 -0.2532 -0.0331 0.0392  563 GLY D N   
12295 C CA  . GLY D 262 ? 0.6472 0.6790 0.5337 -0.2441 -0.0360 0.0371  563 GLY D CA  
12296 C C   . GLY D 262 ? 0.7085 0.7286 0.6052 -0.2193 -0.0378 0.0392  563 GLY D C   
12297 O O   . GLY D 262 ? 0.7636 0.7579 0.6547 -0.2118 -0.0396 0.0389  563 GLY D O   
12298 N N   . LEU D 263 ? 0.6332 0.6713 0.5440 -0.2068 -0.0371 0.0410  564 LEU D N   
12299 C CA  . LEU D 263 ? 0.6075 0.6321 0.5259 -0.1855 -0.0384 0.0433  564 LEU D CA  
12300 C C   . LEU D 263 ? 0.5550 0.6018 0.4905 -0.1714 -0.0402 0.0396  564 LEU D C   
12301 O O   . LEU D 263 ? 0.5143 0.5963 0.4613 -0.1733 -0.0403 0.0360  564 LEU D O   
12302 C CB  . LEU D 263 ? 0.5936 0.6234 0.5172 -0.1788 -0.0369 0.0469  564 LEU D CB  
12303 C CG  . LEU D 263 ? 0.7515 0.7612 0.6585 -0.1910 -0.0352 0.0516  564 LEU D CG  
12304 C CD1 . LEU D 263 ? 0.6722 0.7041 0.5879 -0.1882 -0.0331 0.0530  564 LEU D CD1 
12305 C CD2 . LEU D 263 ? 0.7576 0.7241 0.6507 -0.1844 -0.0367 0.0562  564 LEU D CD2 
12306 N N   . LYS D 264 ? 0.5608 0.5869 0.4972 -0.1570 -0.0418 0.0407  565 LYS D N   
12307 C CA  . LYS D 264 ? 0.5656 0.6076 0.5168 -0.1414 -0.0433 0.0386  565 LYS D CA  
12308 C C   . LYS D 264 ? 0.5223 0.5425 0.4753 -0.1255 -0.0436 0.0417  565 LYS D C   
12309 O O   . LYS D 264 ? 0.6411 0.6350 0.5839 -0.1263 -0.0431 0.0450  565 LYS D O   
12310 C CB  . LYS D 264 ? 0.6103 0.6544 0.5594 -0.1445 -0.0452 0.0349  565 LYS D CB  
12311 C CG  . LYS D 264 ? 0.6601 0.6679 0.5938 -0.1473 -0.0456 0.0353  565 LYS D CG  
12312 C CD  . LYS D 264 ? 0.6608 0.6738 0.5926 -0.1509 -0.0474 0.0309  565 LYS D CD  
12313 C CE  . LYS D 264 ? 0.7248 0.7054 0.6374 -0.1613 -0.0472 0.0297  565 LYS D CE  
12314 N NZ  . LYS D 264 ? 0.7294 0.6990 0.6413 -0.1518 -0.0486 0.0274  565 LYS D NZ  
12315 N N   . TRP D 265 ? 0.4499 0.4823 0.4156 -0.1110 -0.0445 0.0408  566 TRP D N   
12316 C CA  . TRP D 265 ? 0.5193 0.5334 0.4871 -0.0969 -0.0448 0.0430  566 TRP D CA  
12317 C C   . TRP D 265 ? 0.6289 0.6503 0.6041 -0.0869 -0.0461 0.0410  566 TRP D C   
12318 O O   . TRP D 265 ? 0.6028 0.6457 0.5830 -0.0887 -0.0472 0.0383  566 TRP D O   
12319 C CB  . TRP D 265 ? 0.4248 0.4437 0.3997 -0.0892 -0.0437 0.0454  566 TRP D CB  
12320 C CG  . TRP D 265 ? 0.3648 0.3597 0.3369 -0.0804 -0.0437 0.0482  566 TRP D CG  
12321 C CD1 . TRP D 265 ? 0.5285 0.5225 0.5086 -0.0671 -0.0439 0.0485  566 TRP D CD1 
12322 C CD2 . TRP D 265 ? 0.3978 0.3665 0.3573 -0.0842 -0.0438 0.0509  566 TRP D CD2 
12323 N NE1 . TRP D 265 ? 0.4667 0.4389 0.4416 -0.0627 -0.0439 0.0510  566 TRP D NE1 
12324 C CE2 . TRP D 265 ? 0.4179 0.3741 0.3802 -0.0720 -0.0441 0.0525  566 TRP D CE2 
12325 C CE3 . TRP D 265 ? 0.4825 0.4364 0.4277 -0.0968 -0.0436 0.0522  566 TRP D CE3 
12326 C CZ2 . TRP D 265 ? 0.4686 0.4005 0.4212 -0.0705 -0.0446 0.0553  566 TRP D CZ2 
12327 C CZ3 . TRP D 265 ? 0.4219 0.3476 0.3557 -0.0952 -0.0442 0.0554  566 TRP D CZ3 
12328 C CH2 . TRP D 265 ? 0.4796 0.3957 0.4178 -0.0812 -0.0448 0.0568  566 TRP D CH2 
12329 N N   . TYR D 266 ? 0.5744 0.5785 0.5498 -0.0764 -0.0462 0.0424  567 TYR D N   
12330 C CA  . TYR D 266 ? 0.5389 0.5473 0.5197 -0.0669 -0.0471 0.0412  567 TYR D CA  
12331 C C   . TYR D 266 ? 0.5663 0.5885 0.5586 -0.0556 -0.0469 0.0421  567 TYR D C   
12332 O O   . TYR D 266 ? 0.6028 0.6249 0.5982 -0.0532 -0.0458 0.0437  567 TYR D O   
12333 C CB  . TYR D 266 ? 0.4310 0.4149 0.4054 -0.0624 -0.0469 0.0417  567 TYR D CB  
12334 C CG  . TYR D 266 ? 0.5351 0.5019 0.5077 -0.0581 -0.0458 0.0444  567 TYR D CG  
12335 C CD1 . TYR D 266 ? 0.5090 0.4768 0.4894 -0.0473 -0.0452 0.0459  567 TYR D CD1 
12336 C CD2 . TYR D 266 ? 0.5156 0.4645 0.4775 -0.0650 -0.0456 0.0456  567 TYR D CD2 
12337 C CE1 . TYR D 266 ? 0.4106 0.3657 0.3899 -0.0433 -0.0446 0.0480  567 TYR D CE1 
12338 C CE2 . TYR D 266 ? 0.5279 0.4622 0.4879 -0.0597 -0.0452 0.0483  567 TYR D CE2 
12339 C CZ  . TYR D 266 ? 0.4725 0.4119 0.4421 -0.0489 -0.0448 0.0494  567 TYR D CZ  
12340 O OH  . TYR D 266 ? 0.6737 0.6020 0.6423 -0.0436 -0.0447 0.0517  567 TYR D OH  
12341 N N   . GLY D 267 ? 0.4720 0.5049 0.4692 -0.0488 -0.0481 0.0411  568 GLY D N   
12342 C CA  . GLY D 267 ? 0.4078 0.4528 0.4139 -0.0385 -0.0480 0.0418  568 GLY D CA  
12343 C C   . GLY D 267 ? 0.4190 0.4490 0.4265 -0.0289 -0.0470 0.0437  568 GLY D C   
12344 O O   . GLY D 267 ? 0.4424 0.4775 0.4554 -0.0219 -0.0464 0.0443  568 GLY D O   
12345 N N   . LEU D 268 ? 0.3861 0.3981 0.3883 -0.0287 -0.0465 0.0444  569 LEU D N   
12346 C CA  . LEU D 268 ? 0.4334 0.4348 0.4371 -0.0203 -0.0455 0.0457  569 LEU D CA  
12347 C C   . LEU D 268 ? 0.5131 0.4991 0.5148 -0.0206 -0.0441 0.0468  569 LEU D C   
12348 O O   . LEU D 268 ? 0.5546 0.5282 0.5504 -0.0235 -0.0439 0.0464  569 LEU D O   
12349 C CB  . LEU D 268 ? 0.4770 0.4740 0.4769 -0.0183 -0.0460 0.0452  569 LEU D CB  
12350 C CG  . LEU D 268 ? 0.4838 0.4721 0.4847 -0.0108 -0.0446 0.0466  569 LEU D CG  
12351 C CD1 . LEU D 268 ? 0.5003 0.4971 0.5054 -0.0040 -0.0451 0.0478  569 LEU D CD1 
12352 C CD2 . LEU D 268 ? 0.5008 0.4821 0.4963 -0.0106 -0.0444 0.0460  569 LEU D CD2 
12353 N N   . PRO D 269 ? 0.4225 0.4088 0.4285 -0.0170 -0.0432 0.0479  570 PRO D N   
12354 C CA  . PRO D 269 ? 0.4052 0.3790 0.4097 -0.0163 -0.0423 0.0490  570 PRO D CA  
12355 C C   . PRO D 269 ? 0.3650 0.3319 0.3706 -0.0104 -0.0413 0.0491  570 PRO D C   
12356 O O   . PRO D 269 ? 0.4994 0.4702 0.5088 -0.0060 -0.0406 0.0493  570 PRO D O   
12357 C CB  . PRO D 269 ? 0.3672 0.3473 0.3759 -0.0155 -0.0419 0.0497  570 PRO D CB  
12358 C CG  . PRO D 269 ? 0.3386 0.3308 0.3522 -0.0113 -0.0419 0.0487  570 PRO D CG  
12359 C CD  . PRO D 269 ? 0.4096 0.4082 0.4215 -0.0133 -0.0431 0.0478  570 PRO D CD  
12360 N N   . ALA D 270 ? 0.4345 0.3906 0.4360 -0.0104 -0.0410 0.0488  571 ALA D N   
12361 C CA  . ALA D 270 ? 0.3874 0.3394 0.3894 -0.0059 -0.0396 0.0483  571 ALA D CA  
12362 C C   . ALA D 270 ? 0.4640 0.4072 0.4647 -0.0037 -0.0390 0.0481  571 ALA D C   
12363 O O   . ALA D 270 ? 0.4519 0.3864 0.4469 -0.0043 -0.0393 0.0471  571 ALA D O   
12364 C CB  . ALA D 270 ? 0.4073 0.3587 0.4048 -0.0073 -0.0398 0.0469  571 ALA D CB  
12365 N N   . VAL D 271 ? 0.4969 0.4428 0.5027 -0.0006 -0.0383 0.0489  572 VAL D N   
12366 C CA  . VAL D 271 ? 0.3993 0.3405 0.4050 0.0025  -0.0384 0.0489  572 VAL D CA  
12367 C C   . VAL D 271 ? 0.4425 0.3825 0.4484 0.0063  -0.0366 0.0471  572 VAL D C   
12368 O O   . VAL D 271 ? 0.4901 0.4359 0.4994 0.0068  -0.0348 0.0466  572 VAL D O   
12369 C CB  . VAL D 271 ? 0.4998 0.4471 0.5109 0.0036  -0.0385 0.0499  572 VAL D CB  
12370 C CG1 . VAL D 271 ? 0.3938 0.3410 0.4069 0.0082  -0.0384 0.0494  572 VAL D CG1 
12371 C CG2 . VAL D 271 ? 0.2949 0.2424 0.3043 0.0002  -0.0403 0.0516  572 VAL D CG2 
12372 N N   . SER D 272 ? 0.4366 0.3687 0.4381 0.0090  -0.0369 0.0459  573 SER D N   
12373 C CA  . SER D 272 ? 0.5080 0.4397 0.5087 0.0127  -0.0348 0.0434  573 SER D CA  
12374 C C   . SER D 272 ? 0.5439 0.4756 0.5462 0.0193  -0.0346 0.0422  573 SER D C   
12375 O O   . SER D 272 ? 0.5942 0.5269 0.5960 0.0231  -0.0327 0.0395  573 SER D O   
12376 C CB  . SER D 272 ? 0.4206 0.3433 0.4131 0.0106  -0.0349 0.0416  573 SER D CB  
12377 O OG  . SER D 272 ? 0.4108 0.3216 0.3961 0.0088  -0.0370 0.0421  573 SER D OG  
12378 N N   . ASN D 273 ? 0.5221 0.4540 0.5261 0.0214  -0.0366 0.0440  574 ASN D N   
12379 C CA  . ASN D 273 ? 0.5378 0.4701 0.5426 0.0292  -0.0372 0.0430  574 ASN D CA  
12380 C C   . ASN D 273 ? 0.4835 0.4319 0.4980 0.0310  -0.0368 0.0432  574 ASN D C   
12381 O O   . ASN D 273 ? 0.5179 0.4703 0.5343 0.0378  -0.0379 0.0426  574 ASN D O   
12382 C CB  . ASN D 273 ? 0.4391 0.3572 0.4358 0.0314  -0.0404 0.0451  574 ASN D CB  
12383 C CG  . ASN D 273 ? 0.5585 0.4779 0.5559 0.0265  -0.0425 0.0487  574 ASN D CG  
12384 O OD1 . ASN D 273 ? 0.5870 0.5179 0.5914 0.0223  -0.0416 0.0492  574 ASN D OD1 
12385 N ND2 . ASN D 273 ? 0.5464 0.4527 0.5353 0.0269  -0.0451 0.0511  574 ASN D ND2 
12386 N N   . MET D 274 ? 0.4130 0.3704 0.4328 0.0254  -0.0352 0.0436  575 MET D N   
12387 C CA  . MET D 274 ? 0.4119 0.3834 0.4395 0.0251  -0.0347 0.0433  575 MET D CA  
12388 C C   . MET D 274 ? 0.5263 0.5085 0.5583 0.0248  -0.0312 0.0406  575 MET D C   
12389 O O   . MET D 274 ? 0.6789 0.6574 0.7078 0.0244  -0.0290 0.0393  575 MET D O   
12390 C CB  . MET D 274 ? 0.3180 0.2909 0.3471 0.0188  -0.0352 0.0452  575 MET D CB  
12391 C CG  . MET D 274 ? 0.4897 0.4558 0.5151 0.0186  -0.0385 0.0477  575 MET D CG  
12392 S SD  . MET D 274 ? 0.5331 0.5044 0.5613 0.0127  -0.0387 0.0487  575 MET D SD  
12393 C CE  . MET D 274 ? 0.4512 0.4365 0.4862 0.0143  -0.0388 0.0473  575 MET D CE  
12394 N N   . LEU D 275 ? 0.4938 0.4902 0.5328 0.0240  -0.0305 0.0397  576 LEU D N   
12395 C CA  . LEU D 275 ? 0.4504 0.4596 0.4937 0.0224  -0.0269 0.0370  576 LEU D CA  
12396 C C   . LEU D 275 ? 0.4875 0.5003 0.5324 0.0135  -0.0251 0.0377  576 LEU D C   
12397 O O   . LEU D 275 ? 0.4417 0.4564 0.4886 0.0110  -0.0269 0.0386  576 LEU D O   
12398 C CB  . LEU D 275 ? 0.5044 0.5297 0.5542 0.0285  -0.0273 0.0346  576 LEU D CB  
12399 C CG  . LEU D 275 ? 0.4788 0.5203 0.5334 0.0282  -0.0232 0.0310  576 LEU D CG  
12400 C CD1 . LEU D 275 ? 0.4235 0.4736 0.4808 0.0394  -0.0241 0.0282  576 LEU D CD1 
12401 C CD2 . LEU D 275 ? 0.3660 0.4240 0.4270 0.0205  -0.0216 0.0301  576 LEU D CD2 
12402 N N   . LEU D 276 ? 0.4729 0.4850 0.5156 0.0088  -0.0216 0.0372  577 LEU D N   
12403 C CA  . LEU D 276 ? 0.4183 0.4301 0.4598 0.0005  -0.0196 0.0379  577 LEU D CA  
12404 C C   . LEU D 276 ? 0.4907 0.5190 0.5370 -0.0036 -0.0164 0.0353  577 LEU D C   
12405 O O   . LEU D 276 ? 0.5914 0.6268 0.6382 -0.0025 -0.0136 0.0335  577 LEU D O   
12406 C CB  . LEU D 276 ? 0.4578 0.4566 0.4917 -0.0023 -0.0180 0.0398  577 LEU D CB  
12407 C CG  . LEU D 276 ? 0.5054 0.5012 0.5352 -0.0103 -0.0151 0.0406  577 LEU D CG  
12408 C CD1 . LEU D 276 ? 0.3552 0.3475 0.3853 -0.0138 -0.0166 0.0412  577 LEU D CD1 
12409 C CD2 . LEU D 276 ? 0.4410 0.4242 0.4623 -0.0110 -0.0141 0.0430  577 LEU D CD2 
12410 N N   . GLU D 277 ? 0.5005 0.5364 0.5503 -0.0087 -0.0167 0.0346  578 GLU D N   
12411 C CA  . GLU D 277 ? 0.5200 0.5739 0.5746 -0.0145 -0.0138 0.0317  578 GLU D CA  
12412 C C   . GLU D 277 ? 0.5313 0.5782 0.5800 -0.0261 -0.0108 0.0323  578 GLU D C   
12413 O O   . GLU D 277 ? 0.4740 0.5113 0.5197 -0.0297 -0.0123 0.0333  578 GLU D O   
12414 C CB  . GLU D 277 ? 0.3861 0.4570 0.4489 -0.0119 -0.0166 0.0297  578 GLU D CB  
12415 C CG  . GLU D 277 ? 0.4816 0.5766 0.5513 -0.0171 -0.0139 0.0261  578 GLU D CG  
12416 C CD  . GLU D 277 ? 0.7584 0.8560 0.8269 -0.0292 -0.0128 0.0252  578 GLU D CD  
12417 O OE1 . GLU D 277 ? 0.8996 0.9861 0.9653 -0.0300 -0.0157 0.0266  578 GLU D OE1 
12418 O OE2 . GLU D 277 ? 0.8176 0.9280 0.8873 -0.0387 -0.0089 0.0227  578 GLU D OE2 
12419 N N   . ILE D 278 ? 0.4620 0.5125 0.5079 -0.0320 -0.0063 0.0316  579 ILE D N   
12420 C CA  . ILE D 278 ? 0.5083 0.5497 0.5459 -0.0438 -0.0030 0.0326  579 ILE D CA  
12421 C C   . ILE D 278 ? 0.5169 0.5788 0.5581 -0.0524 0.0013  0.0294  579 ILE D C   
12422 O O   . ILE D 278 ? 0.5708 0.6437 0.6140 -0.0505 0.0040  0.0282  579 ILE D O   
12423 C CB  . ILE D 278 ? 0.4287 0.4500 0.4552 -0.0440 -0.0014 0.0361  579 ILE D CB  
12424 C CG1 . ILE D 278 ? 0.4407 0.4452 0.4644 -0.0357 -0.0055 0.0389  579 ILE D CG1 
12425 C CG2 . ILE D 278 ? 0.4172 0.4270 0.4335 -0.0557 0.0018  0.0375  579 ILE D CG2 
12426 C CD1 . ILE D 278 ? 0.5930 0.5822 0.6073 -0.0341 -0.0048 0.0420  579 ILE D CD1 
12427 N N   . GLY D 279 ? 0.4171 0.4848 0.4587 -0.0624 0.0021  0.0276  580 GLY D N   
12428 C CA  . GLY D 279 ? 0.4430 0.5306 0.4870 -0.0736 0.0066  0.0245  580 GLY D CA  
12429 C C   . GLY D 279 ? 0.5179 0.6361 0.5748 -0.0674 0.0070  0.0208  580 GLY D C   
12430 O O   . GLY D 279 ? 0.5257 0.6600 0.5837 -0.0737 0.0117  0.0186  580 GLY D O   
12431 N N   . GLY D 280 ? 0.4473 0.5737 0.5131 -0.0547 0.0023  0.0199  581 GLY D N   
12432 C CA  . GLY D 280 ? 0.4614 0.6139 0.5384 -0.0455 0.0020  0.0166  581 GLY D CA  
12433 C C   . GLY D 280 ? 0.4766 0.6229 0.5521 -0.0344 0.0026  0.0173  581 GLY D C   
12434 O O   . GLY D 280 ? 0.5455 0.7086 0.6291 -0.0234 0.0014  0.0146  581 GLY D O   
12435 N N   . LEU D 281 ? 0.4760 0.5990 0.5410 -0.0365 0.0043  0.0206  582 LEU D N   
12436 C CA  . LEU D 281 ? 0.5015 0.6171 0.5641 -0.0264 0.0044  0.0210  582 LEU D CA  
12437 C C   . LEU D 281 ? 0.5270 0.6259 0.5888 -0.0155 -0.0013 0.0233  582 LEU D C   
12438 O O   . LEU D 281 ? 0.6412 0.7257 0.6998 -0.0180 -0.0042 0.0261  582 LEU D O   
12439 C CB  . LEU D 281 ? 0.3510 0.4503 0.4021 -0.0334 0.0081  0.0236  582 LEU D CB  
12440 C CG  . LEU D 281 ? 0.4553 0.5661 0.5036 -0.0471 0.0140  0.0225  582 LEU D CG  
12441 C CD1 . LEU D 281 ? 0.4972 0.5863 0.5313 -0.0540 0.0167  0.0266  582 LEU D CD1 
12442 C CD2 . LEU D 281 ? 0.4031 0.5431 0.4600 -0.0444 0.0176  0.0174  582 LEU D CD2 
12443 N N   . GLU D 282 ? 0.4989 0.5990 0.5625 -0.0039 -0.0025 0.0219  583 GLU D N   
12444 C CA  . GLU D 282 ? 0.5337 0.6187 0.5957 0.0059  -0.0075 0.0238  583 GLU D CA  
12445 C C   . GLU D 282 ? 0.5747 0.6413 0.6282 0.0090  -0.0071 0.0251  583 GLU D C   
12446 O O   . GLU D 282 ? 0.4868 0.5588 0.5396 0.0133  -0.0045 0.0224  583 GLU D O   
12447 C CB  . GLU D 282 ? 0.4952 0.5946 0.5648 0.0174  -0.0102 0.0211  583 GLU D CB  
12448 C CG  . GLU D 282 ? 0.5979 0.7210 0.6769 0.0147  -0.0107 0.0190  583 GLU D CG  
12449 C CD  . GLU D 282 ? 0.6519 0.7890 0.7377 0.0280  -0.0141 0.0168  583 GLU D CD  
12450 O OE1 . GLU D 282 ? 0.6637 0.8049 0.7530 0.0300  -0.0183 0.0180  583 GLU D OE1 
12451 O OE2 . GLU D 282 ? 0.6172 0.7608 0.7042 0.0372  -0.0126 0.0138  583 GLU D OE2 
12452 N N   . PHE D 283 ? 0.5424 0.5890 0.5895 0.0070  -0.0095 0.0289  584 PHE D N   
12453 C CA  . PHE D 283 ? 0.3997 0.4300 0.4387 0.0093  -0.0097 0.0301  584 PHE D CA  
12454 C C   . PHE D 283 ? 0.4215 0.4417 0.4596 0.0176  -0.0141 0.0306  584 PHE D C   
12455 O O   . PHE D 283 ? 0.4039 0.4132 0.4400 0.0165  -0.0173 0.0335  584 PHE D O   
12456 C CB  . PHE D 283 ? 0.3260 0.3431 0.3581 0.0016  -0.0093 0.0338  584 PHE D CB  
12457 C CG  . PHE D 283 ? 0.3928 0.4155 0.4225 -0.0071 -0.0049 0.0339  584 PHE D CG  
12458 C CD1 . PHE D 283 ? 0.4491 0.4725 0.4734 -0.0085 -0.0013 0.0332  584 PHE D CD1 
12459 C CD2 . PHE D 283 ? 0.3708 0.3977 0.4024 -0.0146 -0.0039 0.0346  584 PHE D CD2 
12460 C CE1 . PHE D 283 ? 0.4228 0.4504 0.4432 -0.0176 0.0030  0.0338  584 PHE D CE1 
12461 C CE2 . PHE D 283 ? 0.4300 0.4600 0.4574 -0.0240 0.0004  0.0348  584 PHE D CE2 
12462 C CZ  . PHE D 283 ? 0.5003 0.5304 0.5219 -0.0257 0.0039  0.0348  584 PHE D CZ  
12463 N N   . SER D 284 ? 0.4710 0.4946 0.5098 0.0260  -0.0141 0.0275  585 SER D N   
12464 C CA  . SER D 284 ? 0.4980 0.5108 0.5344 0.0340  -0.0181 0.0278  585 SER D CA  
12465 C C   . SER D 284 ? 0.4896 0.4823 0.5170 0.0326  -0.0198 0.0297  585 SER D C   
12466 O O   . SER D 284 ? 0.4565 0.4377 0.4802 0.0368  -0.0231 0.0306  585 SER D O   
12467 C CB  . SER D 284 ? 0.5046 0.5243 0.5425 0.0444  -0.0175 0.0237  585 SER D CB  
12468 O OG  . SER D 284 ? 0.5899 0.6119 0.6247 0.0445  -0.0134 0.0204  585 SER D OG  
12469 N N   . ALA D 285 ? 0.4595 0.4479 0.4824 0.0265  -0.0178 0.0305  586 ALA D N   
12470 C CA  . ALA D 285 ? 0.4917 0.4646 0.5068 0.0244  -0.0196 0.0321  586 ALA D CA  
12471 C C   . ALA D 285 ? 0.5563 0.5283 0.5703 0.0170  -0.0192 0.0353  586 ALA D C   
12472 O O   . ALA D 285 ? 0.5006 0.4760 0.5124 0.0136  -0.0163 0.0351  586 ALA D O   
12473 C CB  . ALA D 285 ? 0.4703 0.4375 0.4785 0.0272  -0.0181 0.0289  586 ALA D CB  
12474 N N   . CYS D 286 ? 0.3851 0.3520 0.3998 0.0148  -0.0222 0.0382  587 CYS D N   
12475 C CA  . CYS D 286 ? 0.3432 0.3092 0.3573 0.0096  -0.0221 0.0410  587 CYS D CA  
12476 C C   . CYS D 286 ? 0.5067 0.4654 0.5187 0.0086  -0.0254 0.0431  587 CYS D C   
12477 O O   . CYS D 286 ? 0.5165 0.4762 0.5312 0.0069  -0.0264 0.0448  587 CYS D O   
12478 C CB  . CYS D 286 ? 0.4620 0.4359 0.4819 0.0072  -0.0210 0.0414  587 CYS D CB  
12479 S SG  . CYS D 286 ? 0.4912 0.4691 0.5174 0.0102  -0.0240 0.0413  587 CYS D SG  
12480 N N   . PRO D 287 ? 0.5356 0.4880 0.5424 0.0090  -0.0269 0.0427  588 PRO D N   
12481 C CA  . PRO D 287 ? 0.4157 0.3642 0.4212 0.0073  -0.0299 0.0443  588 PRO D CA  
12482 C C   . PRO D 287 ? 0.4967 0.4477 0.5032 0.0053  -0.0303 0.0466  588 PRO D C   
12483 O O   . PRO D 287 ? 0.4653 0.4166 0.4693 0.0047  -0.0290 0.0473  588 PRO D O   
12484 C CB  . PRO D 287 ? 0.4297 0.3728 0.4286 0.0064  -0.0307 0.0430  588 PRO D CB  
12485 C CG  . PRO D 287 ? 0.5160 0.4600 0.5123 0.0076  -0.0281 0.0411  588 PRO D CG  
12486 C CD  . PRO D 287 ? 0.5776 0.5268 0.5792 0.0103  -0.0258 0.0403  588 PRO D CD  
12487 N N   . PHE D 288 ? 0.4895 0.4416 0.4988 0.0047  -0.0321 0.0477  589 PHE D N   
12488 C CA  . PHE D 288 ? 0.4302 0.3842 0.4402 0.0042  -0.0326 0.0492  589 PHE D CA  
12489 C C   . PHE D 288 ? 0.4010 0.3572 0.4111 0.0032  -0.0350 0.0495  589 PHE D C   
12490 O O   . PHE D 288 ? 0.3420 0.2972 0.3518 0.0017  -0.0362 0.0491  589 PHE D O   
12491 C CB  . PHE D 288 ? 0.4547 0.4101 0.4684 0.0040  -0.0314 0.0494  589 PHE D CB  
12492 C CG  . PHE D 288 ? 0.5235 0.4814 0.5413 0.0040  -0.0322 0.0487  589 PHE D CG  
12493 C CD1 . PHE D 288 ? 0.4471 0.4065 0.4660 0.0034  -0.0340 0.0492  589 PHE D CD1 
12494 C CD2 . PHE D 288 ? 0.4886 0.4488 0.5088 0.0048  -0.0312 0.0477  589 PHE D CD2 
12495 C CE1 . PHE D 288 ? 0.4387 0.4000 0.4600 0.0032  -0.0350 0.0491  589 PHE D CE1 
12496 C CE2 . PHE D 288 ? 0.5289 0.4920 0.5523 0.0057  -0.0325 0.0475  589 PHE D CE2 
12497 C CZ  . PHE D 288 ? 0.4351 0.3979 0.4585 0.0047  -0.0345 0.0485  589 PHE D CZ  
12498 N N   . SER D 289 ? 0.4508 0.4101 0.4606 0.0041  -0.0358 0.0503  590 SER D N   
12499 C CA  . SER D 289 ? 0.4353 0.4004 0.4455 0.0030  -0.0378 0.0502  590 SER D CA  
12500 C C   . SER D 289 ? 0.4414 0.4107 0.4533 0.0060  -0.0381 0.0506  590 SER D C   
12501 O O   . SER D 289 ? 0.4611 0.4262 0.4713 0.0091  -0.0372 0.0514  590 SER D O   
12502 C CB  . SER D 289 ? 0.4142 0.3816 0.4206 0.0015  -0.0391 0.0498  590 SER D CB  
12503 O OG  . SER D 289 ? 0.4967 0.4642 0.5006 0.0047  -0.0390 0.0508  590 SER D OG  
12504 N N   . GLY D 290 ? 0.4544 0.4315 0.4687 0.0051  -0.0393 0.0500  591 GLY D N   
12505 C CA  . GLY D 290 ? 0.4106 0.3936 0.4264 0.0092  -0.0397 0.0496  591 GLY D CA  
12506 C C   . GLY D 290 ? 0.5408 0.5369 0.5583 0.0076  -0.0414 0.0486  591 GLY D C   
12507 O O   . GLY D 290 ? 0.5546 0.5559 0.5705 0.0067  -0.0428 0.0487  591 GLY D O   
12508 N N   . TRP D 291 ? 0.4243 0.4273 0.4448 0.0064  -0.0411 0.0475  592 TRP D N   
12509 C CA  . TRP D 291 ? 0.3313 0.3489 0.3537 0.0030  -0.0422 0.0463  592 TRP D CA  
12510 C C   . TRP D 291 ? 0.4619 0.4814 0.4855 -0.0016 -0.0412 0.0458  592 TRP D C   
12511 O O   . TRP D 291 ? 0.3804 0.3929 0.4044 0.0001  -0.0400 0.0459  592 TRP D O   
12512 C CB  . TRP D 291 ? 0.3023 0.3332 0.3272 0.0095  -0.0431 0.0450  592 TRP D CB  
12513 C CG  . TRP D 291 ? 0.4512 0.4796 0.4770 0.0167  -0.0420 0.0440  592 TRP D CG  
12514 C CD1 . TRP D 291 ? 0.4790 0.5131 0.5074 0.0164  -0.0407 0.0421  592 TRP D CD1 
12515 C CD2 . TRP D 291 ? 0.4907 0.5086 0.5135 0.0247  -0.0419 0.0447  592 TRP D CD2 
12516 N NE1 . TRP D 291 ? 0.4808 0.5083 0.5080 0.0240  -0.0398 0.0410  592 TRP D NE1 
12517 C CE2 . TRP D 291 ? 0.5099 0.5264 0.5333 0.0290  -0.0406 0.0427  592 TRP D CE2 
12518 C CE3 . TRP D 291 ? 0.5181 0.5267 0.5365 0.0282  -0.0427 0.0468  592 TRP D CE3 
12519 C CZ2 . TRP D 291 ? 0.6494 0.6533 0.6681 0.0364  -0.0400 0.0428  592 TRP D CZ2 
12520 C CZ3 . TRP D 291 ? 0.5246 0.5214 0.5385 0.0353  -0.0422 0.0475  592 TRP D CZ3 
12521 C CH2 . TRP D 291 ? 0.6328 0.6264 0.6466 0.0393  -0.0409 0.0454  592 TRP D CH2 
12522 N N   . TYR D 292 ? 0.4817 0.5109 0.5050 -0.0083 -0.0416 0.0454  593 TYR D N   
12523 C CA  . TYR D 292 ? 0.4669 0.4967 0.4892 -0.0141 -0.0408 0.0457  593 TYR D CA  
12524 C C   . TYR D 292 ? 0.3904 0.4316 0.4164 -0.0110 -0.0396 0.0438  593 TYR D C   
12525 O O   . TYR D 292 ? 0.4081 0.4635 0.4378 -0.0066 -0.0396 0.0416  593 TYR D O   
12526 C CB  . TYR D 292 ? 0.3746 0.4101 0.3934 -0.0238 -0.0413 0.0459  593 TYR D CB  
12527 C CG  . TYR D 292 ? 0.5146 0.5335 0.5267 -0.0290 -0.0420 0.0478  593 TYR D CG  
12528 C CD1 . TYR D 292 ? 0.3940 0.3989 0.4023 -0.0299 -0.0417 0.0499  593 TYR D CD1 
12529 C CD2 . TYR D 292 ? 0.4377 0.4548 0.4464 -0.0327 -0.0430 0.0473  593 TYR D CD2 
12530 C CE1 . TYR D 292 ? 0.4650 0.4540 0.4664 -0.0331 -0.0424 0.0515  593 TYR D CE1 
12531 C CE2 . TYR D 292 ? 0.4329 0.4330 0.4341 -0.0368 -0.0434 0.0485  593 TYR D CE2 
12532 C CZ  . TYR D 292 ? 0.5315 0.5171 0.5290 -0.0364 -0.0431 0.0506  593 TYR D CZ  
12533 O OH  . TYR D 292 ? 0.5165 0.4842 0.5058 -0.0388 -0.0436 0.0515  593 TYR D OH  
12534 N N   . MET D 293 ? 0.4328 0.4683 0.4574 -0.0128 -0.0387 0.0444  594 MET D N   
12535 C CA  . MET D 293 ? 0.3570 0.4045 0.3829 -0.0145 -0.0374 0.0427  594 MET D CA  
12536 C C   . MET D 293 ? 0.3707 0.4249 0.3931 -0.0249 -0.0374 0.0439  594 MET D C   
12537 O O   . MET D 293 ? 0.3499 0.3914 0.3667 -0.0306 -0.0383 0.0467  594 MET D O   
12538 C CB  . MET D 293 ? 0.4155 0.4542 0.4402 -0.0129 -0.0367 0.0430  594 MET D CB  
12539 C CG  . MET D 293 ? 0.4222 0.4723 0.4472 -0.0145 -0.0352 0.0410  594 MET D CG  
12540 S SD  . MET D 293 ? 0.4484 0.4881 0.4722 -0.0109 -0.0347 0.0402  594 MET D SD  
12541 C CE  . MET D 293 ? 0.5033 0.5337 0.5215 -0.0186 -0.0361 0.0447  594 MET D CE  
12542 N N   . GLY D 294 ? 0.3710 0.4447 0.3959 -0.0274 -0.0363 0.0416  595 GLY D N   
12543 C CA  . GLY D 294 ? 0.4137 0.4955 0.4347 -0.0390 -0.0360 0.0424  595 GLY D CA  
12544 C C   . GLY D 294 ? 0.5674 0.6348 0.5798 -0.0473 -0.0360 0.0461  595 GLY D C   
12545 O O   . GLY D 294 ? 0.5630 0.6236 0.5685 -0.0565 -0.0366 0.0483  595 GLY D O   
12546 N N   . THR D 295 ? 0.4706 0.5318 0.4821 -0.0441 -0.0355 0.0468  596 THR D N   
12547 C CA  . THR D 295 ? 0.4678 0.5177 0.4705 -0.0512 -0.0358 0.0505  596 THR D CA  
12548 C C   . THR D 295 ? 0.4709 0.4980 0.4673 -0.0517 -0.0379 0.0542  596 THR D C   
12549 O O   . THR D 295 ? 0.4321 0.4479 0.4187 -0.0586 -0.0386 0.0578  596 THR D O   
12550 C CB  . THR D 295 ? 0.4022 0.4520 0.4052 -0.0472 -0.0352 0.0503  596 THR D CB  
12551 O OG1 . THR D 295 ? 0.3986 0.4410 0.4069 -0.0372 -0.0359 0.0489  596 THR D OG1 
12552 C CG2 . THR D 295 ? 0.3840 0.4552 0.3904 -0.0483 -0.0326 0.0467  596 THR D CG2 
12553 N N   . GLU D 296 ? 0.4893 0.5090 0.4901 -0.0439 -0.0389 0.0534  597 GLU D N   
12554 C CA  . GLU D 296 ? 0.4311 0.4313 0.4264 -0.0434 -0.0407 0.0560  597 GLU D CA  
12555 C C   . GLU D 296 ? 0.4879 0.4822 0.4749 -0.0529 -0.0411 0.0574  597 GLU D C   
12556 O O   . GLU D 296 ? 0.5591 0.5355 0.5363 -0.0559 -0.0422 0.0606  597 GLU D O   
12557 C CB  . GLU D 296 ? 0.5096 0.5071 0.5112 -0.0352 -0.0410 0.0542  597 GLU D CB  
12558 C CG  . GLU D 296 ? 0.5382 0.5374 0.5463 -0.0269 -0.0406 0.0529  597 GLU D CG  
12559 C CD  . GLU D 296 ? 0.5056 0.4993 0.5172 -0.0207 -0.0407 0.0520  597 GLU D CD  
12560 O OE1 . GLU D 296 ? 0.4735 0.4552 0.4823 -0.0195 -0.0415 0.0534  597 GLU D OE1 
12561 O OE2 . GLU D 296 ? 0.3711 0.3725 0.3874 -0.0169 -0.0400 0.0498  597 GLU D OE2 
12562 N N   . ILE D 297 ? 0.5069 0.5154 0.4967 -0.0573 -0.0402 0.0549  598 ILE D N   
12563 C CA  . ILE D 297 ? 0.5076 0.5131 0.4892 -0.0685 -0.0404 0.0555  598 ILE D CA  
12564 C C   . ILE D 297 ? 0.5063 0.5168 0.4811 -0.0791 -0.0391 0.0572  598 ILE D C   
12565 O O   . ILE D 297 ? 0.4877 0.4813 0.4499 -0.0875 -0.0396 0.0604  598 ILE D O   
12566 C CB  . ILE D 297 ? 0.4199 0.4428 0.4077 -0.0699 -0.0402 0.0518  598 ILE D CB  
12567 C CG1 . ILE D 297 ? 0.3550 0.3754 0.3494 -0.0591 -0.0412 0.0503  598 ILE D CG1 
12568 C CG2 . ILE D 297 ? 0.3608 0.3796 0.3392 -0.0828 -0.0404 0.0519  598 ILE D CG2 
12569 C CD1 . ILE D 297 ? 0.3182 0.3605 0.3209 -0.0566 -0.0413 0.0470  598 ILE D CD1 
12570 N N   . GLY D 298 ? 0.5287 0.5620 0.5110 -0.0789 -0.0374 0.0549  599 GLY D N   
12571 C CA  . GLY D 298 ? 0.6288 0.6728 0.6056 -0.0905 -0.0356 0.0556  599 GLY D CA  
12572 C C   . GLY D 298 ? 0.6311 0.6582 0.5972 -0.0935 -0.0358 0.0603  599 GLY D C   
12573 O O   . GLY D 298 ? 0.6202 0.6400 0.5741 -0.1058 -0.0353 0.0632  599 GLY D O   
12574 N N   . VAL D 299 ? 0.6284 0.6486 0.5978 -0.0830 -0.0368 0.0612  600 VAL D N   
12575 C CA  . VAL D 299 ? 0.6246 0.6318 0.5845 -0.0845 -0.0376 0.0656  600 VAL D CA  
12576 C C   . VAL D 299 ? 0.6162 0.5952 0.5662 -0.0825 -0.0404 0.0698  600 VAL D C   
12577 O O   . VAL D 299 ? 0.4503 0.4134 0.3860 -0.0901 -0.0411 0.0743  600 VAL D O   
12578 C CB  . VAL D 299 ? 0.5261 0.5428 0.4941 -0.0753 -0.0373 0.0639  600 VAL D CB  
12579 C CG1 . VAL D 299 ? 0.5540 0.5593 0.5119 -0.0771 -0.0385 0.0684  600 VAL D CG1 
12580 C CG2 . VAL D 299 ? 0.4316 0.4750 0.4081 -0.0761 -0.0343 0.0591  600 VAL D CG2 
12581 N N   . ARG D 300 ? 0.5524 0.5244 0.5091 -0.0720 -0.0418 0.0684  601 ARG D N   
12582 C CA  . ARG D 300 ? 0.6048 0.5526 0.5537 -0.0672 -0.0444 0.0718  601 ARG D CA  
12583 C C   . ARG D 300 ? 0.6613 0.5930 0.6009 -0.0730 -0.0449 0.0723  601 ARG D C   
12584 O O   . ARG D 300 ? 0.6224 0.5333 0.5471 -0.0777 -0.0461 0.0763  601 ARG D O   
12585 C CB  . ARG D 300 ? 0.4627 0.4116 0.4224 -0.0542 -0.0454 0.0697  601 ARG D CB  
12586 C CG  . ARG D 300 ? 0.4675 0.4309 0.4359 -0.0487 -0.0449 0.0684  601 ARG D CG  
12587 C CD  . ARG D 300 ? 0.4961 0.4546 0.4558 -0.0507 -0.0463 0.0724  601 ARG D CD  
12588 N NE  . ARG D 300 ? 0.5287 0.4664 0.4791 -0.0471 -0.0492 0.0766  601 ARG D NE  
12589 C CZ  . ARG D 300 ? 0.4829 0.4166 0.4378 -0.0371 -0.0511 0.0764  601 ARG D CZ  
12590 N NH1 . ARG D 300 ? 0.4619 0.4095 0.4295 -0.0315 -0.0502 0.0726  601 ARG D NH1 
12591 N NH2 . ARG D 300 ? 0.4733 0.3893 0.4195 -0.0328 -0.0539 0.0799  601 ARG D NH2 
12592 N N   . ASP D 301 ? 0.6444 0.5843 0.5912 -0.0729 -0.0440 0.0684  602 ASP D N   
12593 C CA  . ASP D 301 ? 0.6784 0.6034 0.6165 -0.0783 -0.0444 0.0680  602 ASP D CA  
12594 C C   . ASP D 301 ? 0.6691 0.5878 0.5933 -0.0935 -0.0437 0.0700  602 ASP D C   
12595 O O   . ASP D 301 ? 0.6357 0.5291 0.5446 -0.0979 -0.0448 0.0725  602 ASP D O   
12596 C CB  . ASP D 301 ? 0.5312 0.4706 0.4799 -0.0764 -0.0437 0.0632  602 ASP D CB  
12597 C CG  . ASP D 301 ? 0.5806 0.5190 0.5387 -0.0630 -0.0444 0.0618  602 ASP D CG  
12598 O OD1 . ASP D 301 ? 0.5809 0.5021 0.5344 -0.0567 -0.0457 0.0638  602 ASP D OD1 
12599 O OD2 . ASP D 301 ? 0.6026 0.5577 0.5720 -0.0586 -0.0436 0.0587  602 ASP D OD2 
12600 N N   . TYR D 302 ? 0.7005 0.6412 0.6286 -0.1019 -0.0417 0.0688  603 TYR D N   
12601 C CA  . TYR D 302 ? 0.7503 0.6887 0.6657 -0.1186 -0.0404 0.0702  603 TYR D CA  
12602 C C   . TYR D 302 ? 0.6734 0.5976 0.5748 -0.1241 -0.0406 0.0758  603 TYR D C   
12603 O O   . TYR D 302 ? 0.7236 0.6305 0.6079 -0.1368 -0.0404 0.0787  603 TYR D O   
12604 C CB  . TYR D 302 ? 0.7518 0.7232 0.6774 -0.1260 -0.0380 0.0662  603 TYR D CB  
12605 C CG  . TYR D 302 ? 0.6183 0.6010 0.5515 -0.1261 -0.0382 0.0614  603 TYR D CG  
12606 C CD1 . TYR D 302 ? 0.5959 0.5583 0.5251 -0.1217 -0.0400 0.0610  603 TYR D CD1 
12607 C CD2 . TYR D 302 ? 0.5478 0.5626 0.4918 -0.1302 -0.0366 0.0573  603 TYR D CD2 
12608 C CE1 . TYR D 302 ? 0.6792 0.6523 0.6144 -0.1221 -0.0403 0.0568  603 TYR D CE1 
12609 C CE2 . TYR D 302 ? 0.6587 0.6850 0.6091 -0.1298 -0.0373 0.0532  603 TYR D CE2 
12610 C CZ  . TYR D 302 ? 0.6761 0.6812 0.6218 -0.1262 -0.0392 0.0531  603 TYR D CZ  
12611 O OH  . TYR D 302 ? 0.6591 0.6763 0.6103 -0.1263 -0.0401 0.0492  603 TYR D OH  
12612 N N   . CYS D 303 ? 0.7233 0.6536 0.6301 -0.1156 -0.0410 0.0776  604 CYS D N   
12613 C CA  . CYS D 303 ? 0.7186 0.6423 0.6132 -0.1222 -0.0408 0.0826  604 CYS D CA  
12614 C C   . CYS D 303 ? 0.7021 0.6022 0.5881 -0.1125 -0.0440 0.0877  604 CYS D C   
12615 O O   . CYS D 303 ? 0.7518 0.6412 0.6237 -0.1184 -0.0444 0.0930  604 CYS D O   
12616 C CB  . CYS D 303 ? 0.6937 0.6480 0.5989 -0.1237 -0.0382 0.0803  604 CYS D CB  
12617 S SG  . CYS D 303 ? 0.6440 0.6296 0.5563 -0.1370 -0.0344 0.0750  604 CYS D SG  
12618 N N   . ASP D 304 ? 0.7008 0.5934 0.5941 -0.0982 -0.0462 0.0866  605 ASP D N   
12619 C CA  . ASP D 304 ? 0.7069 0.5770 0.5910 -0.0891 -0.0496 0.0913  605 ASP D CA  
12620 C C   . ASP D 304 ? 0.7699 0.6084 0.6314 -0.0966 -0.0509 0.0962  605 ASP D C   
12621 O O   . ASP D 304 ? 0.8207 0.6486 0.6769 -0.1026 -0.0501 0.0942  605 ASP D O   
12622 C CB  . ASP D 304 ? 0.6721 0.5407 0.5677 -0.0739 -0.0513 0.0885  605 ASP D CB  
12623 C CG  . ASP D 304 ? 0.7136 0.6044 0.6259 -0.0647 -0.0512 0.0860  605 ASP D CG  
12624 O OD1 . ASP D 304 ? 0.7237 0.6334 0.6409 -0.0695 -0.0494 0.0851  605 ASP D OD1 
12625 O OD2 . ASP D 304 ? 0.7069 0.5961 0.6267 -0.0529 -0.0527 0.0846  605 ASP D OD2 
12626 N N   . ASN D 305 ? 0.7550 0.5774 0.6018 -0.0964 -0.0531 0.1026  606 ASN D N   
12627 C CA  . ASN D 305 ? 0.8004 0.5880 0.6225 -0.1025 -0.0547 0.1081  606 ASN D CA  
12628 C C   . ASN D 305 ? 0.8135 0.5779 0.6319 -0.0933 -0.0566 0.1065  606 ASN D C   
12629 O O   . ASN D 305 ? 0.7962 0.5357 0.5978 -0.1016 -0.0563 0.1074  606 ASN D O   
12630 C CB  . ASN D 305 ? 0.9475 0.7211 0.7553 -0.0993 -0.0577 0.1156  606 ASN D CB  
12631 C CG  . ASN D 305 ? 1.0301 0.8194 0.8338 -0.1127 -0.0553 0.1182  606 ASN D CG  
12632 O OD1 . ASN D 305 ? 1.0188 0.8124 0.8168 -0.1293 -0.0519 0.1173  606 ASN D OD1 
12633 N ND2 . ASN D 305 ? 1.0207 0.8198 0.8269 -0.1059 -0.0571 0.1210  606 ASN D ND2 
12634 N N   . SER D 306 ? 0.7517 0.5239 0.5849 -0.0768 -0.0582 0.1037  607 SER D N   
12635 C CA  . SER D 306 ? 0.8145 0.5689 0.6462 -0.0669 -0.0596 0.1012  607 SER D CA  
12636 C C   . SER D 306 ? 0.8270 0.5922 0.6690 -0.0718 -0.0567 0.0945  607 SER D C   
12637 O O   . SER D 306 ? 0.7588 0.5106 0.5996 -0.0646 -0.0573 0.0917  607 SER D O   
12638 C CB  . SER D 306 ? 0.8739 0.6355 0.7178 -0.0481 -0.0622 0.1005  607 SER D CB  
12639 O OG  . SER D 306 ? 1.0420 0.7871 0.8730 -0.0407 -0.0660 0.1068  607 SER D OG  
12640 N N   . ARG D 307 ? 0.8206 0.6104 0.6724 -0.0829 -0.0537 0.0917  608 ARG D N   
12641 C CA  . ARG D 307 ? 0.8404 0.6436 0.7029 -0.0863 -0.0515 0.0855  608 ARG D CA  
12642 C C   . ARG D 307 ? 0.8499 0.6489 0.7009 -0.1048 -0.0495 0.0849  608 ARG D C   
12643 O O   . ARG D 307 ? 0.9207 0.6906 0.7506 -0.1120 -0.0503 0.0882  608 ARG D O   
12644 C CB  . ARG D 307 ? 0.8107 0.6482 0.6960 -0.0815 -0.0500 0.0818  608 ARG D CB  
12645 C CG  . ARG D 307 ? 0.8041 0.6458 0.7005 -0.0650 -0.0517 0.0816  608 ARG D CG  
12646 C CD  . ARG D 307 ? 0.8573 0.6861 0.7545 -0.0552 -0.0526 0.0790  608 ARG D CD  
12647 N NE  . ARG D 307 ? 0.7803 0.6199 0.6855 -0.0587 -0.0506 0.0738  608 ARG D NE  
12648 C CZ  . ARG D 307 ? 0.7255 0.5894 0.6477 -0.0552 -0.0493 0.0704  608 ARG D CZ  
12649 N NH1 . ARG D 307 ? 0.5939 0.4731 0.5269 -0.0490 -0.0494 0.0710  608 ARG D NH1 
12650 N NH2 . ARG D 307 ? 0.6813 0.5533 0.6086 -0.0581 -0.0480 0.0664  608 ARG D NH2 
12651 N N   . TYR D 308 ? 0.7148 0.5420 0.5782 -0.1126 -0.0471 0.0808  609 TYR D N   
12652 C CA  . TYR D 308 ? 0.6870 0.5134 0.5405 -0.1307 -0.0453 0.0795  609 TYR D CA  
12653 C C   . TYR D 308 ? 0.7481 0.5728 0.5888 -0.1449 -0.0441 0.0840  609 TYR D C   
12654 O O   . TYR D 308 ? 0.7485 0.5641 0.5749 -0.1616 -0.0427 0.0842  609 TYR D O   
12655 C CB  . TYR D 308 ? 0.7147 0.5737 0.5856 -0.1338 -0.0434 0.0734  609 TYR D CB  
12656 C CG  . TYR D 308 ? 0.7816 0.6337 0.6548 -0.1292 -0.0442 0.0690  609 TYR D CG  
12657 C CD1 . TYR D 308 ? 0.7122 0.5690 0.5988 -0.1126 -0.0452 0.0670  609 TYR D CD1 
12658 C CD2 . TYR D 308 ? 0.7954 0.6358 0.6561 -0.1424 -0.0437 0.0668  609 TYR D CD2 
12659 C CE1 . TYR D 308 ? 0.7457 0.5966 0.6335 -0.1087 -0.0457 0.0630  609 TYR D CE1 
12660 C CE2 . TYR D 308 ? 0.7365 0.5706 0.5982 -0.1385 -0.0444 0.0624  609 TYR D CE2 
12661 C CZ  . TYR D 308 ? 0.8293 0.6688 0.7045 -0.1214 -0.0453 0.0607  609 TYR D CZ  
12662 O OH  . TYR D 308 ? 0.9101 0.7441 0.7856 -0.1180 -0.0457 0.0564  609 TYR D OH  
12663 N N   . ASN D 309 ? 0.7266 0.5605 0.5716 -0.1394 -0.0444 0.0874  610 ASN D N   
12664 C CA  . ASN D 309 ? 0.7494 0.5769 0.5797 -0.1502 -0.0437 0.0930  610 ASN D CA  
12665 C C   . ASN D 309 ? 0.7877 0.6280 0.6119 -0.1715 -0.0403 0.0916  610 ASN D C   
12666 O O   . ASN D 309 ? 0.7891 0.6070 0.5915 -0.1860 -0.0398 0.0956  610 ASN D O   
12667 C CB  . ASN D 309 ? 0.7276 0.5138 0.5350 -0.1476 -0.0466 0.0995  610 ASN D CB  
12668 C CG  . ASN D 309 ? 0.6932 0.4721 0.4852 -0.1560 -0.0465 0.1063  610 ASN D CG  
12669 O OD1 . ASN D 309 ? 0.7957 0.6010 0.5982 -0.1564 -0.0451 0.1063  610 ASN D OD1 
12670 N ND2 . ASN D 309 ? 0.6180 0.3602 0.3839 -0.1631 -0.0478 0.1120  610 ASN D ND2 
12671 N N   . ILE D 310 ? 0.8191 0.6965 0.6626 -0.1732 -0.0380 0.0860  611 ILE D N   
12672 C CA  . ILE D 310 ? 0.8337 0.7313 0.6756 -0.1922 -0.0348 0.0832  611 ILE D CA  
12673 C C   . ILE D 310 ? 0.7785 0.6995 0.6222 -0.1998 -0.0321 0.0848  611 ILE D C   
12674 O O   . ILE D 310 ? 0.7595 0.7065 0.6064 -0.2138 -0.0290 0.0816  611 ILE D O   
12675 C CB  . ILE D 310 ? 0.7813 0.7079 0.6425 -0.1895 -0.0341 0.0758  611 ILE D CB  
12676 C CG1 . ILE D 310 ? 0.7938 0.7501 0.6777 -0.1740 -0.0339 0.0730  611 ILE D CG1 
12677 C CG2 . ILE D 310 ? 0.7746 0.6792 0.6334 -0.1829 -0.0365 0.0739  611 ILE D CG2 
12678 C CD1 . ILE D 310 ? 0.8085 0.8027 0.7101 -0.1751 -0.0322 0.0664  611 ILE D CD1 
12679 N N   . LEU D 311 ? 0.7488 0.6637 0.5911 -0.1906 -0.0332 0.0891  612 LEU D N   
12680 C CA  . LEU D 311 ? 0.7202 0.6577 0.5637 -0.1974 -0.0304 0.0901  612 LEU D CA  
12681 C C   . LEU D 311 ? 0.6770 0.6088 0.5007 -0.2206 -0.0276 0.0933  612 LEU D C   
12682 O O   . LEU D 311 ? 0.7376 0.7012 0.5676 -0.2325 -0.0238 0.0898  612 LEU D O   
12683 C CB  . LEU D 311 ? 0.6569 0.5840 0.4982 -0.1851 -0.0325 0.0948  612 LEU D CB  
12684 C CG  . LEU D 311 ? 0.5310 0.4821 0.3954 -0.1675 -0.0329 0.0901  612 LEU D CG  
12685 C CD1 . LEU D 311 ? 0.5227 0.4644 0.3838 -0.1572 -0.0351 0.0944  612 LEU D CD1 
12686 C CD2 . LEU D 311 ? 0.4429 0.4346 0.3233 -0.1714 -0.0290 0.0838  612 LEU D CD2 
12687 N N   . GLU D 312 ? 0.7081 0.5996 0.5074 -0.2277 -0.0294 0.0996  613 GLU D N   
12688 C CA  . GLU D 312 ? 0.8570 0.7385 0.6340 -0.2511 -0.0268 0.1036  613 GLU D CA  
12689 C C   . GLU D 312 ? 0.8500 0.7548 0.6316 -0.2684 -0.0234 0.0975  613 GLU D C   
12690 O O   . GLU D 312 ? 0.9054 0.8311 0.6827 -0.2865 -0.0194 0.0972  613 GLU D O   
12691 C CB  . GLU D 312 ? 1.0727 0.9019 0.8212 -0.2544 -0.0297 0.1109  613 GLU D CB  
12692 C CG  . GLU D 312 ? 1.2283 1.0358 0.9602 -0.2509 -0.0315 0.1196  613 GLU D CG  
12693 C CD  . GLU D 312 ? 1.3754 1.1330 1.0738 -0.2610 -0.0332 0.1273  613 GLU D CD  
12694 O OE1 . GLU D 312 ? 1.3128 1.0656 0.9985 -0.2799 -0.0305 0.1253  613 GLU D OE1 
12695 O OE2 . GLU D 312 ? 1.4943 1.2206 1.1812 -0.2470 -0.0374 0.1333  613 GLU D OE2 
12696 N N   . GLU D 313 ? 0.8076 0.7106 0.5974 -0.2637 -0.0249 0.0925  614 GLU D N   
12697 C CA  . GLU D 313 ? 0.8764 0.8005 0.6690 -0.2806 -0.0224 0.0868  614 GLU D CA  
12698 C C   . GLU D 313 ? 0.7807 0.7589 0.5971 -0.2807 -0.0193 0.0807  614 GLU D C   
12699 O O   . GLU D 313 ? 0.8469 0.8498 0.6620 -0.2998 -0.0158 0.0780  614 GLU D O   
12700 C CB  . GLU D 313 ? 0.8594 0.7700 0.6556 -0.2741 -0.0250 0.0827  614 GLU D CB  
12701 C CG  . GLU D 313 ? 0.9910 0.9208 0.7879 -0.2925 -0.0230 0.0768  614 GLU D CG  
12702 C CD  . GLU D 313 ? 1.1811 1.0932 0.9778 -0.2871 -0.0258 0.0731  614 GLU D CD  
12703 O OE1 . GLU D 313 ? 1.2238 1.1535 1.0231 -0.3000 -0.0249 0.0676  614 GLU D OE1 
12704 O OE2 . GLU D 313 ? 1.2255 1.1076 1.0194 -0.2702 -0.0289 0.0754  614 GLU D OE2 
12705 N N   . VAL D 314 ? 0.7340 0.7313 0.5718 -0.2595 -0.0205 0.0781  615 VAL D N   
12706 C CA  . VAL D 314 ? 0.6391 0.6856 0.4992 -0.2566 -0.0178 0.0719  615 VAL D CA  
12707 C C   . VAL D 314 ? 0.6568 0.7211 0.5116 -0.2680 -0.0139 0.0739  615 VAL D C   
12708 O O   . VAL D 314 ? 0.6730 0.7752 0.5357 -0.2792 -0.0102 0.0692  615 VAL D O   
12709 C CB  . VAL D 314 ? 0.6110 0.6674 0.4921 -0.2311 -0.0202 0.0690  615 VAL D CB  
12710 C CG1 . VAL D 314 ? 0.4756 0.5793 0.3775 -0.2262 -0.0174 0.0629  615 VAL D CG1 
12711 C CG2 . VAL D 314 ? 0.7074 0.7513 0.5944 -0.2216 -0.0235 0.0664  615 VAL D CG2 
12712 N N   . ALA D 315 ? 0.6574 0.6963 0.4987 -0.2653 -0.0146 0.0807  616 ALA D N   
12713 C CA  . ALA D 315 ? 0.6364 0.6889 0.4698 -0.2768 -0.0109 0.0833  616 ALA D CA  
12714 C C   . ALA D 315 ? 0.7562 0.8092 0.5718 -0.3045 -0.0075 0.0848  616 ALA D C   
12715 O O   . ALA D 315 ? 0.7217 0.8091 0.5408 -0.3171 -0.0029 0.0821  616 ALA D O   
12716 C CB  . ALA D 315 ? 0.6113 0.6317 0.4308 -0.2687 -0.0133 0.0911  616 ALA D CB  
12717 N N   . LYS D 316 ? 0.8198 0.8359 0.6163 -0.3147 -0.0094 0.0883  617 LYS D N   
12718 C CA  . LYS D 316 ? 0.8432 0.8564 0.6204 -0.3430 -0.0060 0.0897  617 LYS D CA  
12719 C C   . LYS D 316 ? 0.7781 0.8398 0.5734 -0.3515 -0.0031 0.0802  617 LYS D C   
12720 O O   . LYS D 316 ? 0.7076 0.7976 0.5017 -0.3631 0.0004  0.0767  617 LYS D O   
12721 C CB  . LYS D 316 ? 0.9026 0.8652 0.6572 -0.3457 -0.0098 0.0924  617 LYS D CB  
12722 C CG  . LYS D 316 ? 1.0437 0.9586 0.7747 -0.3402 -0.0126 0.1011  617 LYS D CG  
12723 C CD  . LYS D 316 ? 1.1836 1.0501 0.8945 -0.3396 -0.0162 0.1025  617 LYS D CD  
12724 C CE  . LYS D 316 ? 1.2506 1.0712 0.9383 -0.3323 -0.0194 0.1108  617 LYS D CE  
12725 N NZ  . LYS D 316 ? 1.3147 1.0894 0.9853 -0.3280 -0.0229 0.1114  617 LYS D NZ  
12726 N N   . LYS D 317 ? 0.8109 0.8841 0.6236 -0.3415 -0.0053 0.0747  618 LYS D N   
12727 C CA  . LYS D 317 ? 0.8127 0.9362 0.6451 -0.3471 -0.0030 0.0660  618 LYS D CA  
12728 C C   . LYS D 317 ? 0.8040 0.9746 0.6552 -0.3406 0.0004  0.0622  618 LYS D C   
12729 O O   . LYS D 317 ? 0.8447 1.0599 0.7073 -0.3502 0.0036  0.0558  618 LYS D O   
12730 C CB  . LYS D 317 ? 0.8155 0.9427 0.6648 -0.3307 -0.0070 0.0607  618 LYS D CB  
12731 C CG  . LYS D 317 ? 0.8787 0.9693 0.7115 -0.3401 -0.0096 0.0618  618 LYS D CG  
12732 C CD  . LYS D 317 ? 0.9007 1.0222 0.7475 -0.3440 -0.0102 0.0538  618 LYS D CD  
12733 C CE  . LYS D 317 ? 0.9988 1.1214 0.8285 -0.3668 -0.0083 0.0510  618 LYS D CE  
12734 N NZ  . LYS D 317 ? 1.0992 1.1650 0.9007 -0.3732 -0.0103 0.0552  618 LYS D NZ  
12735 N N   . MET D 318 ? 0.6871 0.8496 0.5415 -0.3240 -0.0002 0.0653  619 MET D N   
12736 C CA  . MET D 318 ? 0.5700 0.7741 0.4407 -0.3168 0.0031  0.0613  619 MET D CA  
12737 C C   . MET D 318 ? 0.6597 0.8712 0.5150 -0.3364 0.0081  0.0648  619 MET D C   
12738 O O   . MET D 318 ? 0.6576 0.9056 0.5247 -0.3330 0.0117  0.0610  619 MET D O   
12739 C CB  . MET D 318 ? 0.5400 0.7343 0.4219 -0.2899 0.0003  0.0620  619 MET D CB  
12740 C CG  . MET D 318 ? 0.5098 0.7168 0.4140 -0.2690 -0.0029 0.0560  619 MET D CG  
12741 S SD  . MET D 318 ? 0.5956 0.7896 0.5113 -0.2400 -0.0060 0.0566  619 MET D SD  
12742 C CE  . MET D 318 ? 0.5551 0.7850 0.4765 -0.2406 -0.0009 0.0537  619 MET D CE  
12743 N N   . ASN D 319 ? 0.7325 0.9082 0.5608 -0.3541 0.0079  0.0710  620 ASN D N   
12744 C CA  . ASN D 319 ? 0.8505 1.0233 0.6601 -0.3668 0.0103  0.0732  620 ASN D CA  
12745 C C   . ASN D 319 ? 0.7515 0.9206 0.5600 -0.3581 0.0115  0.0786  620 ASN D C   
12746 O O   . ASN D 319 ? 0.7906 0.9825 0.5970 -0.3640 0.0149  0.0770  620 ASN D O   
12747 C CB  . ASN D 319 ? 0.9311 1.1521 0.7487 -0.3778 0.0143  0.0645  620 ASN D CB  
12748 C CG  . ASN D 319 ? 1.0591 1.2668 0.8578 -0.3963 0.0136  0.0630  620 ASN D CG  
12749 O OD1 . ASN D 319 ? 1.1631 1.3526 0.9392 -0.4103 0.0144  0.0663  620 ASN D OD1 
12750 N ND2 . ASN D 319 ? 0.9543 1.1701 0.7614 -0.3968 0.0121  0.0581  620 ASN D ND2 
12751 N N   . LEU D 320 ? 0.7373 0.8779 0.5468 -0.3422 0.0079  0.0841  621 LEU D N   
12752 C CA  . LEU D 320 ? 0.7582 0.8929 0.5663 -0.3294 0.0074  0.0876  621 LEU D CA  
12753 C C   . LEU D 320 ? 0.8305 0.9240 0.6072 -0.3424 0.0067  0.0985  621 LEU D C   
12754 O O   . LEU D 320 ? 0.8317 0.8891 0.5902 -0.3494 0.0036  0.1014  621 LEU D O   
12755 C CB  . LEU D 320 ? 0.7624 0.8844 0.5860 -0.3013 0.0021  0.0861  621 LEU D CB  
12756 C CG  . LEU D 320 ? 0.6671 0.8243 0.5196 -0.2870 0.0022  0.0762  621 LEU D CG  
12757 C CD1 . LEU D 320 ? 0.5925 0.7334 0.4570 -0.2614 -0.0027 0.0757  621 LEU D CD1 
12758 C CD2 . LEU D 320 ? 0.6667 0.8742 0.5343 -0.2880 0.0074  0.0691  621 LEU D CD2 
12759 N N   . ASP D 321 ? 0.8699 0.9682 0.6413 -0.3401 0.0082  0.1017  622 ASP D N   
12760 C CA  . ASP D 321 ? 0.8653 0.9242 0.6094 -0.3446 0.0054  0.1101  622 ASP D CA  
12761 C C   . ASP D 321 ? 0.8607 0.8786 0.5979 -0.3289 -0.0002 0.1181  622 ASP D C   
12762 O O   . ASP D 321 ? 0.9340 0.9586 0.6836 -0.3095 -0.0025 0.1169  622 ASP D O   
12763 C CB  . ASP D 321 ? 1.0130 1.0933 0.7538 -0.3478 0.0087  0.1105  622 ASP D CB  
12764 C CG  . ASP D 321 ? 1.1330 1.1722 0.8468 -0.3494 0.0051  0.1198  622 ASP D CG  
12765 O OD1 . ASP D 321 ? 1.0543 1.0527 0.7493 -0.3538 0.0013  0.1244  622 ASP D OD1 
12766 O OD2 . ASP D 321 ? 1.2351 1.2828 0.9462 -0.3456 0.0060  0.1224  622 ASP D OD2 
12767 N N   . MET D 322 ? 0.8770 0.8529 0.5987 -0.3298 -0.0045 0.1217  623 MET D N   
12768 C CA  . MET D 322 ? 0.9407 0.8779 0.6564 -0.3133 -0.0104 0.1282  623 MET D CA  
12769 C C   . MET D 322 ? 1.0565 0.9559 0.7470 -0.3113 -0.0141 0.1367  623 MET D C   
12770 O O   . MET D 322 ? 1.1198 0.9816 0.8008 -0.2986 -0.0196 0.1421  623 MET D O   
12771 C CB  . MET D 322 ? 0.8441 0.7591 0.5600 -0.3119 -0.0129 0.1263  623 MET D CB  
12772 C CG  . MET D 322 ? 0.9077 0.8614 0.6533 -0.3061 -0.0111 0.1154  623 MET D CG  
12773 S SD  . MET D 322 ? 0.9872 0.9207 0.7309 -0.3107 -0.0129 0.1124  623 MET D SD  
12774 C CE  . MET D 322 ? 1.0123 0.8900 0.7411 -0.2927 -0.0198 0.1197  623 MET D CE  
12775 N N   . ARG D 323 ? 1.0317 0.9419 0.7118 -0.3226 -0.0114 0.1377  624 ARG D N   
12776 C CA  . ARG D 323 ? 1.1650 1.0408 0.8208 -0.3213 -0.0149 0.1458  624 ARG D CA  
12777 C C   . ARG D 323 ? 1.1763 1.0529 0.8350 -0.3051 -0.0178 0.1510  624 ARG D C   
12778 O O   . ARG D 323 ? 1.3555 1.1969 0.9985 -0.2951 -0.0232 0.1583  624 ARG D O   
12779 C CB  . ARG D 323 ? 1.2461 1.1318 0.8881 -0.3407 -0.0112 0.1450  624 ARG D CB  
12780 C CG  . ARG D 323 ? 1.3048 1.1761 0.9344 -0.3570 -0.0101 0.1420  624 ARG D CG  
12781 C CD  . ARG D 323 ? 1.3970 1.2871 1.0165 -0.3770 -0.0058 0.1401  624 ARG D CD  
12782 N NE  . ARG D 323 ? 1.4453 1.3881 1.0860 -0.3788 -0.0008 0.1343  624 ARG D NE  
12783 C CZ  . ARG D 323 ? 1.4724 1.4417 1.1097 -0.3928 0.0034  0.1318  624 ARG D CZ  
12784 N NH1 . ARG D 323 ? 1.5161 1.4639 1.1290 -0.4080 0.0032  0.1351  624 ARG D NH1 
12785 N NH2 . ARG D 323 ? 1.4179 1.4355 1.0761 -0.3914 0.0079  0.1256  624 ARG D NH2 
12786 N N   . LYS D 324 ? 1.0418 0.9585 0.7201 -0.3016 -0.0144 0.1471  625 LYS D N   
12787 C CA  . LYS D 324 ? 1.0353 0.9558 0.7173 -0.2860 -0.0173 0.1503  625 LYS D CA  
12788 C C   . LYS D 324 ? 0.9435 0.8881 0.6582 -0.2653 -0.0186 0.1403  625 LYS D C   
12789 O O   . LYS D 324 ? 0.9791 0.9563 0.7143 -0.2676 -0.0144 0.1311  625 LYS D O   
12790 C CB  . LYS D 324 ? 1.0211 0.9685 0.6986 -0.2953 -0.0131 0.1504  625 LYS D CB  
12791 C CG  . LYS D 324 ? 1.0717 1.0683 0.7685 -0.3049 -0.0055 0.1404  625 LYS D CG  
12792 C CD  . LYS D 324 ? 1.1307 1.1401 0.8154 -0.3231 -0.0012 0.1393  625 LYS D CD  
12793 C CE  . LYS D 324 ? 1.1340 1.1968 0.8388 -0.3299 0.0063  0.1292  625 LYS D CE  
12794 N NZ  . LYS D 324 ? 1.1176 1.2081 0.8359 -0.3173 0.0079  0.1261  625 LYS D NZ  
12795 N N   . THR D 325 ? 0.8671 0.7955 0.5857 -0.2451 -0.0246 0.1424  626 THR D N   
12796 C CA  . THR D 325 ? 0.7679 0.7159 0.5152 -0.2256 -0.0261 0.1337  626 THR D CA  
12797 C C   . THR D 325 ? 0.7512 0.7432 0.5175 -0.2248 -0.0212 0.1251  626 THR D C   
12798 O O   . THR D 325 ? 0.5911 0.6065 0.3812 -0.2163 -0.0196 0.1160  626 THR D O   
12799 C CB  . THR D 325 ? 0.7933 0.7199 0.5396 -0.2063 -0.0329 0.1378  626 THR D CB  
12800 O OG1 . THR D 325 ? 0.9274 0.8582 0.6633 -0.2063 -0.0339 0.1421  626 THR D OG1 
12801 C CG2 . THR D 325 ? 0.7708 0.6537 0.4980 -0.2049 -0.0378 0.1459  626 THR D CG2 
12802 N N   . SER D 326 ? 0.7197 0.7226 0.4747 -0.2329 -0.0190 0.1278  627 SER D N   
12803 C CA  . SER D 326 ? 0.7357 0.7785 0.5068 -0.2305 -0.0145 0.1194  627 SER D CA  
12804 C C   . SER D 326 ? 0.7176 0.7934 0.5018 -0.2409 -0.0078 0.1112  627 SER D C   
12805 O O   . SER D 326 ? 0.8036 0.9141 0.6034 -0.2369 -0.0039 0.1028  627 SER D O   
12806 C CB  . SER D 326 ? 0.7233 0.7693 0.4770 -0.2376 -0.0136 0.1244  627 SER D CB  
12807 O OG  . SER D 326 ? 0.8813 0.9039 0.6073 -0.2554 -0.0132 0.1344  627 SER D OG  
12808 N N   . SER D 327 ? 0.5795 0.6463 0.3573 -0.2540 -0.0065 0.1130  628 SER D N   
12809 C CA  . SER D 327 ? 0.6864 0.7866 0.4808 -0.2606 -0.0013 0.1043  628 SER D CA  
12810 C C   . SER D 327 ? 0.6169 0.7286 0.4376 -0.2417 -0.0032 0.0959  628 SER D C   
12811 O O   . SER D 327 ? 0.6192 0.7639 0.4572 -0.2420 0.0007  0.0874  628 SER D O   
12812 C CB  . SER D 327 ? 0.7819 0.8689 0.5619 -0.2805 0.0002  0.1082  628 SER D CB  
12813 O OG  . SER D 327 ? 0.8346 0.8978 0.6189 -0.2728 -0.0041 0.1086  628 SER D OG  
12814 N N   . LEU D 328 ? 0.5365 0.6223 0.3599 -0.2253 -0.0090 0.0983  629 LEU D N   
12815 C CA  . LEU D 328 ? 0.6027 0.6939 0.4483 -0.2077 -0.0113 0.0917  629 LEU D CA  
12816 C C   . LEU D 328 ? 0.6386 0.7338 0.4916 -0.2129 -0.0103 0.0885  629 LEU D C   
12817 O O   . LEU D 328 ? 0.6542 0.7699 0.5275 -0.2031 -0.0096 0.0808  629 LEU D O   
12818 C CB  . LEU D 328 ? 0.5537 0.6776 0.4187 -0.1958 -0.0088 0.0828  629 LEU D CB  
12819 C CG  . LEU D 328 ? 0.5833 0.7039 0.4428 -0.1889 -0.0101 0.0846  629 LEU D CG  
12820 C CD1 . LEU D 328 ? 0.5014 0.6443 0.3806 -0.1733 -0.0091 0.0753  629 LEU D CD1 
12821 C CD2 . LEU D 328 ? 0.4906 0.5738 0.3374 -0.1831 -0.0165 0.0931  629 LEU D CD2 
12822 N N   . TRP D 329 ? 0.7332 0.8069 0.5684 -0.2282 -0.0106 0.0945  630 TRP D N   
12823 C CA  . TRP D 329 ? 0.7097 0.7856 0.5502 -0.2343 -0.0100 0.0914  630 TRP D CA  
12824 C C   . TRP D 329 ? 0.7383 0.7989 0.5910 -0.2168 -0.0146 0.0894  630 TRP D C   
12825 O O   . TRP D 329 ? 0.7702 0.8484 0.6389 -0.2131 -0.0139 0.0830  630 TRP D O   
12826 C CB  . TRP D 329 ? 0.7048 0.7556 0.5208 -0.2550 -0.0096 0.0983  630 TRP D CB  
12827 C CG  . TRP D 329 ? 0.7101 0.7130 0.5050 -0.2522 -0.0146 0.1077  630 TRP D CG  
12828 C CD1 . TRP D 329 ? 0.7570 0.7397 0.5319 -0.2555 -0.0158 0.1158  630 TRP D CD1 
12829 C CD2 . TRP D 329 ? 0.7265 0.6963 0.5173 -0.2450 -0.0191 0.1099  630 TRP D CD2 
12830 N NE1 . TRP D 329 ? 0.7329 0.6719 0.4919 -0.2496 -0.0211 0.1230  630 TRP D NE1 
12831 C CE2 . TRP D 329 ? 0.8065 0.7372 0.5751 -0.2431 -0.0229 0.1192  630 TRP D CE2 
12832 C CE3 . TRP D 329 ? 0.7915 0.7614 0.5949 -0.2393 -0.0203 0.1048  630 TRP D CE3 
12833 C CZ2 . TRP D 329 ? 0.7528 0.6452 0.5120 -0.2351 -0.0277 0.1230  630 TRP D CZ2 
12834 C CZ3 . TRP D 329 ? 0.7672 0.6993 0.5611 -0.2325 -0.0247 0.1084  630 TRP D CZ3 
12835 C CH2 . TRP D 329 ? 0.7687 0.6628 0.5411 -0.2300 -0.0282 0.1172  630 TRP D CH2 
12836 N N   . LYS D 330 ? 0.7298 0.7591 0.5751 -0.2057 -0.0193 0.0948  631 LYS D N   
12837 C CA  . LYS D 330 ? 0.6417 0.6583 0.4988 -0.1889 -0.0233 0.0927  631 LYS D CA  
12838 C C   . LYS D 330 ? 0.7027 0.7497 0.5843 -0.1753 -0.0220 0.0843  631 LYS D C   
12839 O O   . LYS D 330 ? 0.7278 0.7819 0.6226 -0.1695 -0.0224 0.0795  631 LYS D O   
12840 C CB  . LYS D 330 ? 0.5610 0.5463 0.4081 -0.1779 -0.0281 0.0991  631 LYS D CB  
12841 C CG  . LYS D 330 ? 0.7071 0.6549 0.5307 -0.1863 -0.0306 0.1070  631 LYS D CG  
12842 C CD  . LYS D 330 ? 0.6838 0.6030 0.5005 -0.1719 -0.0360 0.1124  631 LYS D CD  
12843 C CE  . LYS D 330 ? 0.7014 0.5812 0.4933 -0.1792 -0.0385 0.1200  631 LYS D CE  
12844 N NZ  . LYS D 330 ? 0.7927 0.6449 0.5780 -0.1636 -0.0441 0.1250  631 LYS D NZ  
12845 N N   . ASP D 331 ? 0.6878 0.7517 0.5744 -0.1701 -0.0206 0.0824  632 ASP D N   
12846 C CA  . ASP D 331 ? 0.6355 0.7253 0.5429 -0.1569 -0.0194 0.0744  632 ASP D CA  
12847 C C   . ASP D 331 ? 0.5766 0.6958 0.4961 -0.1614 -0.0158 0.0677  632 ASP D C   
12848 O O   . ASP D 331 ? 0.5735 0.7030 0.5088 -0.1499 -0.0164 0.0622  632 ASP D O   
12849 C CB  . ASP D 331 ? 0.6403 0.7436 0.5471 -0.1544 -0.0176 0.0733  632 ASP D CB  
12850 C CG  . ASP D 331 ? 0.5387 0.6155 0.4307 -0.1527 -0.0213 0.0808  632 ASP D CG  
12851 O OD1 . ASP D 331 ? 0.5443 0.6077 0.4176 -0.1653 -0.0213 0.0877  632 ASP D OD1 
12852 O OD2 . ASP D 331 ? 0.4573 0.5266 0.3555 -0.1389 -0.0244 0.0800  632 ASP D OD2 
12853 N N   . GLN D 332 ? 0.6001 0.7340 0.5119 -0.1783 -0.0121 0.0682  633 GLN D N   
12854 C CA  . GLN D 332 ? 0.5923 0.7600 0.5158 -0.1834 -0.0085 0.0614  633 GLN D CA  
12855 C C   . GLN D 332 ? 0.6004 0.7608 0.5277 -0.1845 -0.0107 0.0607  633 GLN D C   
12856 O O   . GLN D 332 ? 0.4933 0.6763 0.4367 -0.1773 -0.0102 0.0543  633 GLN D O   
12857 C CB  . GLN D 332 ? 0.6507 0.8348 0.5631 -0.2034 -0.0040 0.0627  633 GLN D CB  
12858 C CG  . GLN D 332 ? 0.7205 0.9485 0.6454 -0.2041 0.0010  0.0549  633 GLN D CG  
12859 C CD  . GLN D 332 ? 0.7717 1.0126 0.6826 -0.2251 0.0056  0.0573  633 GLN D CD  
12860 O OE1 . GLN D 332 ? 0.6926 0.9069 0.5835 -0.2396 0.0048  0.0652  633 GLN D OE1 
12861 N NE2 . GLN D 332 ? 0.9697 1.2507 0.8900 -0.2265 0.0106  0.0506  633 GLN D NE2 
12862 N N   . ALA D 333 ? 0.5960 0.7243 0.5074 -0.1933 -0.0130 0.0672  634 ALA D N   
12863 C CA  . ALA D 333 ? 0.5686 0.6861 0.4808 -0.1953 -0.0151 0.0667  634 ALA D CA  
12864 C C   . ALA D 333 ? 0.5940 0.7020 0.5192 -0.1754 -0.0188 0.0645  634 ALA D C   
12865 O O   . ALA D 333 ? 0.5147 0.6294 0.4488 -0.1726 -0.0197 0.0609  634 ALA D O   
12866 C CB  . ALA D 333 ? 0.4577 0.5395 0.3469 -0.2094 -0.0166 0.0740  634 ALA D CB  
12867 N N   . LEU D 334 ? 0.5653 0.6597 0.4916 -0.1621 -0.0207 0.0665  635 LEU D N   
12868 C CA  . LEU D 334 ? 0.5091 0.5954 0.4472 -0.1443 -0.0237 0.0644  635 LEU D CA  
12869 C C   . LEU D 334 ? 0.6106 0.7274 0.5678 -0.1343 -0.0222 0.0569  635 LEU D C   
12870 O O   . LEU D 334 ? 0.5276 0.6430 0.4941 -0.1250 -0.0240 0.0544  635 LEU D O   
12871 C CB  . LEU D 334 ? 0.4883 0.5553 0.4224 -0.1344 -0.0260 0.0681  635 LEU D CB  
12872 C CG  . LEU D 334 ? 0.4400 0.5006 0.3857 -0.1167 -0.0285 0.0660  635 LEU D CG  
12873 C CD1 . LEU D 334 ? 0.4200 0.4561 0.3631 -0.1127 -0.0318 0.0683  635 LEU D CD1 
12874 C CD2 . LEU D 334 ? 0.4648 0.5193 0.4080 -0.1100 -0.0296 0.0680  635 LEU D CD2 
12875 N N   . VAL D 335 ? 0.6042 0.7482 0.5668 -0.1352 -0.0188 0.0532  636 VAL D N   
12876 C CA  . VAL D 335 ? 0.5082 0.6802 0.4877 -0.1242 -0.0174 0.0459  636 VAL D CA  
12877 C C   . VAL D 335 ? 0.4915 0.6804 0.4772 -0.1289 -0.0173 0.0428  636 VAL D C   
12878 O O   . VAL D 335 ? 0.4261 0.6211 0.4231 -0.1172 -0.0189 0.0393  636 VAL D O   
12879 C CB  . VAL D 335 ? 0.5177 0.7163 0.5005 -0.1245 -0.0135 0.0418  636 VAL D CB  
12880 C CG1 . VAL D 335 ? 0.3275 0.5536 0.3269 -0.1112 -0.0122 0.0340  636 VAL D CG1 
12881 C CG2 . VAL D 335 ? 0.3295 0.5129 0.3062 -0.1196 -0.0139 0.0443  636 VAL D CG2 
12882 N N   . GLU D 336 ? 0.5472 0.7436 0.5245 -0.1468 -0.0155 0.0442  637 GLU D N   
12883 C CA  . GLU D 336 ? 0.5796 0.7955 0.5622 -0.1537 -0.0153 0.0409  637 GLU D CA  
12884 C C   . GLU D 336 ? 0.5746 0.7679 0.5570 -0.1490 -0.0193 0.0425  637 GLU D C   
12885 O O   . GLU D 336 ? 0.4591 0.6690 0.4517 -0.1443 -0.0204 0.0384  637 GLU D O   
12886 C CB  . GLU D 336 ? 0.5589 0.7824 0.5297 -0.1765 -0.0126 0.0427  637 GLU D CB  
12887 C CG  . GLU D 336 ? 0.5861 0.8379 0.5572 -0.1839 -0.0079 0.0406  637 GLU D CG  
12888 C CD  . GLU D 336 ? 0.5469 0.8421 0.5365 -0.1748 -0.0059 0.0323  637 GLU D CD  
12889 O OE1 . GLU D 336 ? 0.5182 0.8233 0.5195 -0.1651 -0.0082 0.0287  637 GLU D OE1 
12890 O OE2 . GLU D 336 ? 0.5253 0.8451 0.5174 -0.1767 -0.0020 0.0294  637 GLU D OE2 
12891 N N   . ILE D 337 ? 0.6307 0.7870 0.6008 -0.1500 -0.0215 0.0483  638 ILE D N   
12892 C CA  . ILE D 337 ? 0.4920 0.6256 0.4611 -0.1448 -0.0250 0.0495  638 ILE D CA  
12893 C C   . ILE D 337 ? 0.5764 0.7158 0.5602 -0.1255 -0.0267 0.0462  638 ILE D C   
12894 O O   . ILE D 337 ? 0.5914 0.7329 0.5809 -0.1211 -0.0285 0.0441  638 ILE D O   
12895 C CB  . ILE D 337 ? 0.4618 0.5560 0.4151 -0.1472 -0.0269 0.0560  638 ILE D CB  
12896 C CG1 . ILE D 337 ? 0.5487 0.6330 0.4846 -0.1674 -0.0255 0.0595  638 ILE D CG1 
12897 C CG2 . ILE D 337 ? 0.4526 0.5236 0.4063 -0.1381 -0.0302 0.0567  638 ILE D CG2 
12898 C CD1 . ILE D 337 ? 0.6055 0.6541 0.5243 -0.1693 -0.0270 0.0664  638 ILE D CD1 
12899 N N   . ASN D 338 ? 0.5167 0.6584 0.5059 -0.1144 -0.0260 0.0456  639 ASN D N   
12900 C CA  . ASN D 338 ? 0.4799 0.6221 0.4804 -0.0969 -0.0275 0.0430  639 ASN D CA  
12901 C C   . ASN D 338 ? 0.4663 0.6404 0.4797 -0.0907 -0.0266 0.0371  639 ASN D C   
12902 O O   . ASN D 338 ? 0.4189 0.5925 0.4399 -0.0785 -0.0284 0.0353  639 ASN D O   
12903 C CB  . ASN D 338 ? 0.3624 0.4946 0.3625 -0.0886 -0.0271 0.0441  639 ASN D CB  
12904 C CG  . ASN D 338 ? 0.4769 0.5768 0.4683 -0.0873 -0.0296 0.0493  639 ASN D CG  
12905 O OD1 . ASN D 338 ? 0.5982 0.6855 0.5938 -0.0769 -0.0316 0.0492  639 ASN D OD1 
12906 N ND2 . ASN D 338 ? 0.5145 0.6010 0.4933 -0.0980 -0.0295 0.0538  639 ASN D ND2 
12907 N N   . ILE D 339 ? 0.4447 0.6466 0.4601 -0.0988 -0.0237 0.0342  640 ILE D N   
12908 C CA  . ILE D 339 ? 0.4249 0.6605 0.4521 -0.0939 -0.0231 0.0285  640 ILE D CA  
12909 C C   . ILE D 339 ? 0.5092 0.7471 0.5373 -0.0982 -0.0256 0.0284  640 ILE D C   
12910 O O   . ILE D 339 ? 0.5465 0.7972 0.5840 -0.0870 -0.0274 0.0253  640 ILE D O   
12911 C CB  . ILE D 339 ? 0.3974 0.6644 0.4259 -0.1037 -0.0192 0.0254  640 ILE D CB  
12912 C CG1 . ILE D 339 ? 0.3801 0.6503 0.4104 -0.0950 -0.0167 0.0236  640 ILE D CG1 
12913 C CG2 . ILE D 339 ? 0.2892 0.5945 0.3290 -0.1023 -0.0188 0.0196  640 ILE D CG2 
12914 C CD1 . ILE D 339 ? 0.3751 0.6681 0.4024 -0.1071 -0.0124 0.0220  640 ILE D CD1 
12915 N N   . ALA D 340 ? 0.4923 0.7159 0.5094 -0.1143 -0.0259 0.0318  641 ALA D N   
12916 C CA  . ALA D 340 ? 0.5511 0.7761 0.5671 -0.1208 -0.0280 0.0312  641 ALA D CA  
12917 C C   . ALA D 340 ? 0.5392 0.7438 0.5577 -0.1072 -0.0315 0.0322  641 ALA D C   
12918 O O   . ALA D 340 ? 0.4546 0.6731 0.4799 -0.1022 -0.0335 0.0295  641 ALA D O   
12919 C CB  . ALA D 340 ? 0.4824 0.6896 0.4830 -0.1409 -0.0274 0.0348  641 ALA D CB  
12920 N N   . VAL D 341 ? 0.4245 0.5976 0.4373 -0.1013 -0.0322 0.0361  642 VAL D N   
12921 C CA  . VAL D 341 ? 0.4711 0.6243 0.4855 -0.0893 -0.0349 0.0372  642 VAL D CA  
12922 C C   . VAL D 341 ? 0.4493 0.6203 0.4761 -0.0734 -0.0357 0.0338  642 VAL D C   
12923 O O   . VAL D 341 ? 0.4032 0.5765 0.4334 -0.0678 -0.0380 0.0328  642 VAL D O   
12924 C CB  . VAL D 341 ? 0.4903 0.6123 0.4980 -0.0853 -0.0351 0.0414  642 VAL D CB  
12925 C CG1 . VAL D 341 ? 0.4526 0.5574 0.4627 -0.0732 -0.0372 0.0421  642 VAL D CG1 
12926 C CG2 . VAL D 341 ? 0.4289 0.5302 0.4224 -0.0994 -0.0349 0.0452  642 VAL D CG2 
12927 N N   . LEU D 342 ? 0.4367 0.6197 0.4692 -0.0659 -0.0338 0.0320  643 LEU D N   
12928 C CA  . LEU D 342 ? 0.4564 0.6524 0.4986 -0.0496 -0.0346 0.0288  643 LEU D CA  
12929 C C   . LEU D 342 ? 0.4919 0.7193 0.5413 -0.0489 -0.0355 0.0250  643 LEU D C   
12930 O O   . LEU D 342 ? 0.4360 0.6674 0.4904 -0.0371 -0.0379 0.0239  643 LEU D O   
12931 C CB  . LEU D 342 ? 0.3915 0.5930 0.4366 -0.0424 -0.0321 0.0268  643 LEU D CB  
12932 C CG  . LEU D 342 ? 0.4170 0.5900 0.4564 -0.0399 -0.0317 0.0299  643 LEU D CG  
12933 C CD1 . LEU D 342 ? 0.5343 0.7148 0.5735 -0.0400 -0.0287 0.0281  643 LEU D CD1 
12934 C CD2 . LEU D 342 ? 0.2618 0.4178 0.3031 -0.0264 -0.0335 0.0304  643 LEU D CD2 
12935 N N   . TYR D 343 ? 0.4820 0.7329 0.5318 -0.0618 -0.0338 0.0231  644 TYR D N   
12936 C CA  . TYR D 343 ? 0.4012 0.6868 0.4588 -0.0622 -0.0348 0.0190  644 TYR D CA  
12937 C C   . TYR D 343 ? 0.4731 0.7529 0.5282 -0.0661 -0.0382 0.0202  644 TYR D C   
12938 O O   . TYR D 343 ? 0.4801 0.7796 0.5422 -0.0578 -0.0408 0.0177  644 TYR D O   
12939 C CB  . TYR D 343 ? 0.3386 0.6505 0.3961 -0.0779 -0.0317 0.0167  644 TYR D CB  
12940 C CG  . TYR D 343 ? 0.3190 0.6681 0.3832 -0.0837 -0.0327 0.0126  644 TYR D CG  
12941 C CD1 . TYR D 343 ? 0.3364 0.7197 0.4129 -0.0702 -0.0333 0.0077  644 TYR D CD1 
12942 C CD2 . TYR D 343 ? 0.4152 0.7659 0.4728 -0.1031 -0.0331 0.0134  644 TYR D CD2 
12943 C CE1 . TYR D 343 ? 0.4084 0.8296 0.4919 -0.0752 -0.0345 0.0037  644 TYR D CE1 
12944 C CE2 . TYR D 343 ? 0.4813 0.8685 0.5450 -0.1100 -0.0340 0.0092  644 TYR D CE2 
12945 C CZ  . TYR D 343 ? 0.5179 0.9421 0.5954 -0.0958 -0.0349 0.0043  644 TYR D CZ  
12946 O OH  . TYR D 343 ? 0.5574 1.0219 0.6421 -0.1018 -0.0362 -0.0001 644 TYR D OH  
12947 N N   . SER D 344 ? 0.4954 0.7485 0.5399 -0.0782 -0.0384 0.0237  645 SER D N   
12948 C CA  . SER D 344 ? 0.4336 0.6799 0.4740 -0.0837 -0.0412 0.0242  645 SER D CA  
12949 C C   . SER D 344 ? 0.4864 0.7196 0.5296 -0.0673 -0.0441 0.0253  645 SER D C   
12950 O O   . SER D 344 ? 0.4496 0.6976 0.4965 -0.0634 -0.0469 0.0236  645 SER D O   
12951 C CB  . SER D 344 ? 0.3855 0.6026 0.4124 -0.0990 -0.0404 0.0276  645 SER D CB  
12952 O OG  . SER D 344 ? 0.5033 0.7353 0.5260 -0.1168 -0.0382 0.0264  645 SER D OG  
12953 N N   . PHE D 345 ? 0.4139 0.6203 0.4548 -0.0580 -0.0435 0.0282  646 PHE D N   
12954 C CA  . PHE D 345 ? 0.4304 0.6231 0.4727 -0.0434 -0.0457 0.0295  646 PHE D CA  
12955 C C   . PHE D 345 ? 0.5022 0.7190 0.5536 -0.0292 -0.0472 0.0268  646 PHE D C   
12956 O O   . PHE D 345 ? 0.4731 0.6916 0.5254 -0.0215 -0.0502 0.0270  646 PHE D O   
12957 C CB  . PHE D 345 ? 0.3712 0.5351 0.4101 -0.0372 -0.0443 0.0324  646 PHE D CB  
12958 C CG  . PHE D 345 ? 0.3825 0.5177 0.4124 -0.0445 -0.0444 0.0356  646 PHE D CG  
12959 C CD1 . PHE D 345 ? 0.3530 0.4829 0.3757 -0.0595 -0.0435 0.0363  646 PHE D CD1 
12960 C CD2 . PHE D 345 ? 0.3675 0.4806 0.3953 -0.0362 -0.0452 0.0377  646 PHE D CD2 
12961 C CE1 . PHE D 345 ? 0.4044 0.5068 0.4180 -0.0644 -0.0437 0.0389  646 PHE D CE1 
12962 C CE2 . PHE D 345 ? 0.3826 0.4715 0.4027 -0.0414 -0.0451 0.0400  646 PHE D CE2 
12963 C CZ  . PHE D 345 ? 0.4660 0.5490 0.4789 -0.0547 -0.0445 0.0405  646 PHE D CZ  
12964 N N   . GLN D 346 ? 0.4980 0.7334 0.5554 -0.0249 -0.0453 0.0242  647 GLN D N   
12965 C CA  . GLN D 346 ? 0.4897 0.7455 0.5547 -0.0090 -0.0466 0.0215  647 GLN D CA  
12966 C C   . GLN D 346 ? 0.4944 0.7815 0.5645 -0.0103 -0.0495 0.0189  647 GLN D C   
12967 O O   . GLN D 346 ? 0.5200 0.8143 0.5930 0.0034  -0.0526 0.0186  647 GLN D O   
12968 C CB  . GLN D 346 ? 0.4440 0.7134 0.5137 -0.0043 -0.0435 0.0185  647 GLN D CB  
12969 C CG  . GLN D 346 ? 0.5171 0.7581 0.5830 0.0041  -0.0419 0.0202  647 GLN D CG  
12970 C CD  . GLN D 346 ? 0.5816 0.8317 0.6495 0.0034  -0.0382 0.0174  647 GLN D CD  
12971 O OE1 . GLN D 346 ? 0.5569 0.8354 0.6292 -0.0029 -0.0365 0.0142  647 GLN D OE1 
12972 N NE2 . GLN D 346 ? 0.6263 0.8530 0.6904 0.0092  -0.0368 0.0184  647 GLN D NE2 
12973 N N   . SER D 347 ? 0.3968 0.7021 0.4670 -0.0271 -0.0486 0.0172  648 SER D N   
12974 C CA  . SER D 347 ? 0.3479 0.6861 0.4231 -0.0307 -0.0513 0.0142  648 SER D CA  
12975 C C   . SER D 347 ? 0.4974 0.8227 0.5678 -0.0300 -0.0552 0.0164  648 SER D C   
12976 O O   . SER D 347 ? 0.4779 0.8250 0.5531 -0.0216 -0.0589 0.0149  648 SER D O   
12977 C CB  . SER D 347 ? 0.4325 0.7901 0.5069 -0.0518 -0.0489 0.0119  648 SER D CB  
12978 O OG  . SER D 347 ? 0.5304 0.9011 0.6086 -0.0529 -0.0450 0.0100  648 SER D OG  
12979 N N   . ASP D 348 ? 0.4526 0.7434 0.5133 -0.0379 -0.0547 0.0199  649 ASP D N   
12980 C CA  . ASP D 348 ? 0.4637 0.7384 0.5187 -0.0363 -0.0578 0.0219  649 ASP D CA  
12981 C C   . ASP D 348 ? 0.5038 0.7589 0.5582 -0.0178 -0.0591 0.0249  649 ASP D C   
12982 O O   . ASP D 348 ? 0.4611 0.6957 0.5092 -0.0171 -0.0607 0.0273  649 ASP D O   
12983 C CB  . ASP D 348 ? 0.4058 0.6519 0.4502 -0.0515 -0.0563 0.0238  649 ASP D CB  
12984 C CG  . ASP D 348 ? 0.4675 0.7284 0.5090 -0.0713 -0.0554 0.0212  649 ASP D CG  
12985 O OD1 . ASP D 348 ? 0.3150 0.6120 0.3638 -0.0742 -0.0562 0.0177  649 ASP D OD1 
12986 O OD2 . ASP D 348 ? 0.6010 0.8375 0.6324 -0.0841 -0.0539 0.0226  649 ASP D OD2 
12987 N N   . LYS D 349 ? 0.4430 0.7029 0.5028 -0.0039 -0.0583 0.0245  650 LYS D N   
12988 C CA  . LYS D 349 ? 0.4019 0.6415 0.4596 0.0128  -0.0592 0.0272  650 LYS D CA  
12989 C C   . LYS D 349 ? 0.4487 0.6513 0.4977 0.0096  -0.0582 0.0312  650 LYS D C   
12990 O O   . LYS D 349 ? 0.4338 0.6220 0.4785 0.0177  -0.0601 0.0337  650 LYS D O   
12991 C CB  . LYS D 349 ? 0.4564 0.7126 0.5161 0.0259  -0.0636 0.0271  650 LYS D CB  
12992 C CG  . LYS D 349 ? 0.4109 0.7048 0.4801 0.0329  -0.0646 0.0229  650 LYS D CG  
12993 C CD  . LYS D 349 ? 0.5410 0.8573 0.6121 0.0421  -0.0699 0.0226  650 LYS D CD  
12994 C CE  . LYS D 349 ? 0.7208 1.0661 0.8000 0.0588  -0.0714 0.0194  650 LYS D CE  
12995 N NZ  . LYS D 349 ? 0.8659 1.2209 0.9437 0.0736  -0.0772 0.0210  650 LYS D NZ  
12996 N N   . VAL D 350 ? 0.5197 0.7073 0.5659 -0.0016 -0.0551 0.0317  651 VAL D N   
12997 C CA  . VAL D 350 ? 0.4883 0.6430 0.5276 -0.0037 -0.0537 0.0348  651 VAL D CA  
12998 C C   . VAL D 350 ? 0.4951 0.6371 0.5356 0.0021  -0.0510 0.0355  651 VAL D C   
12999 O O   . VAL D 350 ? 0.4703 0.6212 0.5136 -0.0026 -0.0489 0.0339  651 VAL D O   
13000 C CB  . VAL D 350 ? 0.2945 0.4400 0.3284 -0.0196 -0.0527 0.0350  651 VAL D CB  
13001 C CG1 . VAL D 350 ? 0.3031 0.4170 0.3308 -0.0201 -0.0511 0.0378  651 VAL D CG1 
13002 C CG2 . VAL D 350 ? 0.3516 0.5077 0.3830 -0.0258 -0.0554 0.0338  651 VAL D CG2 
13003 N N   . THR D 351 ? 0.4352 0.5565 0.4726 0.0111  -0.0508 0.0378  652 THR D N   
13004 C CA  . THR D 351 ? 0.4225 0.5314 0.4602 0.0172  -0.0486 0.0380  652 THR D CA  
13005 C C   . THR D 351 ? 0.4699 0.5711 0.5069 0.0075  -0.0460 0.0381  652 THR D C   
13006 O O   . THR D 351 ? 0.4293 0.5166 0.4621 -0.0005 -0.0457 0.0399  652 THR D O   
13007 C CB  . THR D 351 ? 0.4175 0.5027 0.4500 0.0242  -0.0487 0.0407  652 THR D CB  
13008 O OG1 . THR D 351 ? 0.5222 0.6114 0.5530 0.0328  -0.0513 0.0416  652 THR D OG1 
13009 C CG2 . THR D 351 ? 0.3631 0.4370 0.3955 0.0302  -0.0465 0.0403  652 THR D CG2 
13010 N N   . ILE D 352 ? 0.4229 0.5320 0.4631 0.0094  -0.0443 0.0361  653 ILE D N   
13011 C CA  . ILE D 352 ? 0.3398 0.4412 0.3785 0.0019  -0.0420 0.0365  653 ILE D CA  
13012 C C   . ILE D 352 ? 0.4572 0.5613 0.4982 0.0095  -0.0402 0.0342  653 ILE D C   
13013 O O   . ILE D 352 ? 0.4256 0.5428 0.4699 0.0188  -0.0406 0.0316  653 ILE D O   
13014 C CB  . ILE D 352 ? 0.3920 0.5075 0.4306 -0.0108 -0.0416 0.0359  653 ILE D CB  
13015 C CG1 . ILE D 352 ? 0.3307 0.4318 0.3644 -0.0196 -0.0400 0.0379  653 ILE D CG1 
13016 C CG2 . ILE D 352 ? 0.3434 0.4876 0.3880 -0.0092 -0.0409 0.0322  653 ILE D CG2 
13017 C CD1 . ILE D 352 ? 0.2664 0.3710 0.2957 -0.0334 -0.0399 0.0388  653 ILE D CD1 
13018 N N   . VAL D 353 ? 0.4589 0.5503 0.4974 0.0060  -0.0385 0.0350  654 VAL D N   
13019 C CA  . VAL D 353 ? 0.4471 0.5398 0.4866 0.0112  -0.0366 0.0324  654 VAL D CA  
13020 C C   . VAL D 353 ? 0.4803 0.5783 0.5187 0.0016  -0.0349 0.0323  654 VAL D C   
13021 O O   . VAL D 353 ? 0.3945 0.4813 0.4291 -0.0068 -0.0353 0.0355  654 VAL D O   
13022 C CB  . VAL D 353 ? 0.5092 0.5797 0.5453 0.0171  -0.0363 0.0332  654 VAL D CB  
13023 C CG1 . VAL D 353 ? 0.4485 0.5027 0.4813 0.0097  -0.0364 0.0364  654 VAL D CG1 
13024 C CG2 . VAL D 353 ? 0.4702 0.5418 0.5061 0.0230  -0.0344 0.0295  654 VAL D CG2 
13025 N N   . ASP D 354 ? 0.4000 0.5155 0.4411 0.0031  -0.0331 0.0287  655 ASP D N   
13026 C CA  . ASP D 354 ? 0.4638 0.5847 0.5027 -0.0059 -0.0313 0.0287  655 ASP D CA  
13027 C C   . ASP D 354 ? 0.4462 0.5510 0.4817 -0.0039 -0.0304 0.0288  655 ASP D C   
13028 O O   . ASP D 354 ? 0.3966 0.4900 0.4321 0.0049  -0.0306 0.0275  655 ASP D O   
13029 C CB  . ASP D 354 ? 0.4442 0.5926 0.4873 -0.0058 -0.0293 0.0245  655 ASP D CB  
13030 C CG  . ASP D 354 ? 0.5513 0.7047 0.5972 0.0072  -0.0280 0.0196  655 ASP D CG  
13031 O OD1 . ASP D 354 ? 0.4071 0.5536 0.4501 0.0079  -0.0263 0.0181  655 ASP D OD1 
13032 O OD2 . ASP D 354 ? 0.6922 0.8548 0.7422 0.0172  -0.0290 0.0173  655 ASP D OD2 
13033 N N   . HIS D 355 ? 0.4982 0.6013 0.5297 -0.0127 -0.0297 0.0306  656 HIS D N   
13034 C CA  . HIS D 355 ? 0.4849 0.5728 0.5127 -0.0119 -0.0296 0.0312  656 HIS D CA  
13035 C C   . HIS D 355 ? 0.3835 0.4755 0.4124 -0.0041 -0.0277 0.0261  656 HIS D C   
13036 O O   . HIS D 355 ? 0.4926 0.5702 0.5196 -0.0003 -0.0279 0.0255  656 HIS D O   
13037 C CB  . HIS D 355 ? 0.4389 0.5243 0.4609 -0.0221 -0.0297 0.0346  656 HIS D CB  
13038 C CG  . HIS D 355 ? 0.4631 0.5674 0.4839 -0.0292 -0.0277 0.0336  656 HIS D CG  
13039 N ND1 . HIS D 355 ? 0.4481 0.5620 0.4686 -0.0367 -0.0277 0.0351  656 HIS D ND1 
13040 C CD2 . HIS D 355 ? 0.4006 0.5159 0.4195 -0.0314 -0.0255 0.0312  656 HIS D CD2 
13041 C CE1 . HIS D 355 ? 0.3977 0.5288 0.4165 -0.0435 -0.0254 0.0337  656 HIS D CE1 
13042 N NE2 . HIS D 355 ? 0.4219 0.5545 0.4398 -0.0400 -0.0239 0.0314  656 HIS D NE2 
13043 N N   . HIS D 356 ? 0.3527 0.4644 0.3845 -0.0015 -0.0257 0.0219  657 HIS D N   
13044 C CA  . HIS D 356 ? 0.4556 0.5700 0.4875 0.0073  -0.0238 0.0162  657 HIS D CA  
13045 C C   . HIS D 356 ? 0.4898 0.5904 0.5221 0.0185  -0.0248 0.0148  657 HIS D C   
13046 O O   . HIS D 356 ? 0.5285 0.6131 0.5569 0.0222  -0.0244 0.0132  657 HIS D O   
13047 C CB  . HIS D 356 ? 0.3560 0.4967 0.3914 0.0087  -0.0214 0.0117  657 HIS D CB  
13048 C CG  . HIS D 356 ? 0.4277 0.5814 0.4610 -0.0036 -0.0199 0.0133  657 HIS D CG  
13049 N ND1 . HIS D 356 ? 0.4037 0.5530 0.4315 -0.0086 -0.0187 0.0132  657 HIS D ND1 
13050 C CD2 . HIS D 356 ? 0.4227 0.5919 0.4571 -0.0131 -0.0197 0.0156  657 HIS D CD2 
13051 C CE1 . HIS D 356 ? 0.4358 0.5968 0.4609 -0.0199 -0.0177 0.0156  657 HIS D CE1 
13052 N NE2 . HIS D 356 ? 0.4420 0.6147 0.4708 -0.0234 -0.0181 0.0170  657 HIS D NE2 
13053 N N   . SER D 357 ? 0.3964 0.5029 0.4325 0.0234  -0.0261 0.0155  658 SER D N   
13054 C CA  . SER D 357 ? 0.4317 0.5239 0.4665 0.0341  -0.0273 0.0150  658 SER D CA  
13055 C C   . SER D 357 ? 0.4308 0.4980 0.4613 0.0308  -0.0285 0.0188  658 SER D C   
13056 O O   . SER D 357 ? 0.4091 0.4596 0.4353 0.0369  -0.0282 0.0174  658 SER D O   
13057 C CB  . SER D 357 ? 0.4785 0.5825 0.5176 0.0385  -0.0292 0.0162  658 SER D CB  
13058 O OG  . SER D 357 ? 0.6284 0.7178 0.6646 0.0494  -0.0304 0.0162  658 SER D OG  
13059 N N   . ALA D 358 ? 0.4172 0.4814 0.4481 0.0212  -0.0296 0.0233  659 ALA D N   
13060 C CA  . ALA D 358 ? 0.2988 0.3429 0.3267 0.0186  -0.0307 0.0265  659 ALA D CA  
13061 C C   . ALA D 358 ? 0.4323 0.4665 0.4566 0.0172  -0.0295 0.0245  659 ALA D C   
13062 O O   . ALA D 358 ? 0.4249 0.4431 0.4461 0.0187  -0.0296 0.0247  659 ALA D O   
13063 C CB  . ALA D 358 ? 0.3290 0.3728 0.3577 0.0099  -0.0321 0.0311  659 ALA D CB  
13064 N N   . THR D 359 ? 0.4260 0.4701 0.4498 0.0133  -0.0283 0.0225  660 THR D N   
13065 C CA  . THR D 359 ? 0.3370 0.3728 0.3569 0.0109  -0.0276 0.0206  660 THR D CA  
13066 C C   . THR D 359 ? 0.3691 0.3989 0.3856 0.0184  -0.0258 0.0150  660 THR D C   
13067 O O   . THR D 359 ? 0.4326 0.4484 0.4448 0.0176  -0.0255 0.0134  660 THR D O   
13068 C CB  . THR D 359 ? 0.3837 0.4309 0.4027 0.0039  -0.0272 0.0209  660 THR D CB  
13069 O OG1 . THR D 359 ? 0.4536 0.5182 0.4743 0.0056  -0.0254 0.0180  660 THR D OG1 
13070 C CG2 . THR D 359 ? 0.3357 0.3822 0.3551 -0.0034 -0.0293 0.0268  660 THR D CG2 
13071 N N   . GLU D 360 ? 0.4440 0.4842 0.4618 0.0257  -0.0245 0.0115  661 GLU D N   
13072 C CA  . GLU D 360 ? 0.5185 0.5497 0.5317 0.0351  -0.0230 0.0061  661 GLU D CA  
13073 C C   . GLU D 360 ? 0.5521 0.5616 0.5613 0.0389  -0.0241 0.0081  661 GLU D C   
13074 O O   . GLU D 360 ? 0.5560 0.5480 0.5581 0.0407  -0.0231 0.0052  661 GLU D O   
13075 C CB  . GLU D 360 ? 0.5159 0.5642 0.5322 0.0441  -0.0220 0.0025  661 GLU D CB  
13076 C CG  . GLU D 360 ? 0.6641 0.7026 0.6745 0.0560  -0.0204 -0.0034 661 GLU D CG  
13077 C CD  . GLU D 360 ? 0.9604 1.0185 0.9749 0.0669  -0.0198 -0.0069 661 GLU D CD  
13078 O OE1 . GLU D 360 ? 1.0676 1.1496 1.0898 0.0630  -0.0201 -0.0053 661 GLU D OE1 
13079 O OE2 . GLU D 360 ? 1.0294 1.0789 1.0388 0.0794  -0.0191 -0.0115 661 GLU D OE2 
13080 N N   . SER D 361 ? 0.5302 0.5398 0.5427 0.0392  -0.0260 0.0129  662 SER D N   
13081 C CA  A SER D 361 ? 0.5103 0.5000 0.5181 0.0423  -0.0268 0.0151  662 SER D CA  
13082 C CA  B SER D 361 ? 0.5093 0.4991 0.5172 0.0422  -0.0268 0.0152  662 SER D CA  
13083 C C   . SER D 361 ? 0.5240 0.4992 0.5285 0.0337  -0.0265 0.0165  662 SER D C   
13084 O O   . SER D 361 ? 0.5100 0.4664 0.5074 0.0348  -0.0258 0.0154  662 SER D O   
13085 C CB  A SER D 361 ? 0.4840 0.4787 0.4957 0.0440  -0.0288 0.0197  662 SER D CB  
13086 C CB  B SER D 361 ? 0.4869 0.4819 0.4988 0.0433  -0.0289 0.0200  662 SER D CB  
13087 O OG  A SER D 361 ? 0.4738 0.4808 0.4874 0.0535  -0.0293 0.0179  662 SER D OG  
13088 O OG  B SER D 361 ? 0.4707 0.4648 0.4855 0.0339  -0.0298 0.0243  662 SER D OG  
13089 N N   . PHE D 362 ? 0.4917 0.4759 0.5009 0.0249  -0.0272 0.0188  663 PHE D N   
13090 C CA  . PHE D 362 ? 0.4347 0.4095 0.4421 0.0175  -0.0273 0.0198  663 PHE D CA  
13091 C C   . PHE D 362 ? 0.4815 0.4485 0.4828 0.0163  -0.0257 0.0146  663 PHE D C   
13092 O O   . PHE D 362 ? 0.4783 0.4316 0.4750 0.0125  -0.0252 0.0141  663 PHE D O   
13093 C CB  . PHE D 362 ? 0.5143 0.5005 0.5268 0.0103  -0.0288 0.0231  663 PHE D CB  
13094 C CG  . PHE D 362 ? 0.5259 0.5064 0.5376 0.0039  -0.0293 0.0238  663 PHE D CG  
13095 C CD1 . PHE D 362 ? 0.4356 0.4082 0.4479 0.0022  -0.0298 0.0267  663 PHE D CD1 
13096 C CD2 . PHE D 362 ? 0.4316 0.4161 0.4417 -0.0005 -0.0292 0.0213  663 PHE D CD2 
13097 C CE1 . PHE D 362 ? 0.4692 0.4399 0.4817 -0.0035 -0.0301 0.0269  663 PHE D CE1 
13098 C CE2 . PHE D 362 ? 0.4352 0.4174 0.4451 -0.0061 -0.0300 0.0217  663 PHE D CE2 
13099 C CZ  . PHE D 362 ? 0.5738 0.5499 0.5853 -0.0076 -0.0304 0.0244  663 PHE D CZ  
13100 N N   . ILE D 363 ? 0.4190 0.3948 0.4195 0.0189  -0.0246 0.0104  664 ILE D N   
13101 C CA  . ILE D 363 ? 0.4767 0.4441 0.4702 0.0179  -0.0228 0.0046  664 ILE D CA  
13102 C C   . ILE D 363 ? 0.5073 0.4531 0.4922 0.0237  -0.0216 0.0020  664 ILE D C   
13103 O O   . ILE D 363 ? 0.5192 0.4497 0.4971 0.0188  -0.0208 -0.0002 664 ILE D O   
13104 C CB  . ILE D 363 ? 0.4953 0.4769 0.4889 0.0203  -0.0215 0.0000  664 ILE D CB  
13105 C CG1 . ILE D 363 ? 0.4945 0.4928 0.4930 0.0122  -0.0227 0.0027  664 ILE D CG1 
13106 C CG2 . ILE D 363 ? 0.3440 0.3142 0.3287 0.0209  -0.0194 -0.0071 664 ILE D CG2 
13107 C CD1 . ILE D 363 ? 0.4037 0.3977 0.3992 0.0039  -0.0234 0.0021  664 ILE D CD1 
13108 N N   . LYS D 364 ? 0.5342 0.4783 0.5187 0.0338  -0.0216 0.0025  665 LYS D N   
13109 C CA  . LYS D 364 ? 0.5884 0.5094 0.5633 0.0403  -0.0210 0.0016  665 LYS D CA  
13110 C C   . LYS D 364 ? 0.5384 0.4442 0.5101 0.0326  -0.0215 0.0058  665 LYS D C   
13111 O O   . LYS D 364 ? 0.4938 0.3782 0.4551 0.0302  -0.0202 0.0038  665 LYS D O   
13112 C CB  . LYS D 364 ? 0.6051 0.5302 0.5815 0.0525  -0.0220 0.0031  665 LYS D CB  
13113 C CG  . LYS D 364 ? 0.6796 0.6233 0.6600 0.0610  -0.0213 -0.0012 665 LYS D CG  
13114 C CD  . LYS D 364 ? 0.7919 0.7215 0.7619 0.0703  -0.0193 -0.0081 665 LYS D CD  
13115 C CE  . LYS D 364 ? 0.8916 0.8262 0.8614 0.0864  -0.0200 -0.0095 665 LYS D CE  
13116 N NZ  . LYS D 364 ? 0.8280 0.7954 0.8109 0.0886  -0.0209 -0.0083 665 LYS D NZ  
13117 N N   . HIS D 365 ? 0.5716 0.4884 0.5517 0.0282  -0.0231 0.0113  666 HIS D N   
13118 C CA  . HIS D 365 ? 0.5541 0.4601 0.5323 0.0212  -0.0233 0.0151  666 HIS D CA  
13119 C C   . HIS D 365 ? 0.6018 0.5044 0.5779 0.0106  -0.0223 0.0126  666 HIS D C   
13120 O O   . HIS D 365 ? 0.4772 0.3635 0.4458 0.0054  -0.0211 0.0123  666 HIS D O   
13121 C CB  . HIS D 365 ? 0.4771 0.3975 0.4650 0.0193  -0.0251 0.0205  666 HIS D CB  
13122 C CG  . HIS D 365 ? 0.4938 0.4093 0.4821 0.0114  -0.0251 0.0237  666 HIS D CG  
13123 N ND1 . HIS D 365 ? 0.5137 0.4131 0.4952 0.0113  -0.0243 0.0258  666 HIS D ND1 
13124 C CD2 . HIS D 365 ? 0.4652 0.3912 0.4599 0.0039  -0.0257 0.0251  666 HIS D CD2 
13125 C CE1 . HIS D 365 ? 0.4635 0.3653 0.4478 0.0033  -0.0240 0.0280  666 HIS D CE1 
13126 N NE2 . HIS D 365 ? 0.4997 0.4177 0.4923 -0.0006 -0.0250 0.0275  666 HIS D NE2 
13127 N N   . MET D 366 ? 0.6086 0.5271 0.5904 0.0069  -0.0228 0.0107  667 MET D N   
13128 C CA  . MET D 366 ? 0.5369 0.4557 0.5173 -0.0029 -0.0225 0.0082  667 MET D CA  
13129 C C   . MET D 366 ? 0.5679 0.4671 0.5361 -0.0047 -0.0203 0.0026  667 MET D C   
13130 O O   . MET D 366 ? 0.5176 0.4066 0.4809 -0.0130 -0.0195 0.0020  667 MET D O   
13131 C CB  . MET D 366 ? 0.6116 0.5498 0.5981 -0.0051 -0.0237 0.0072  667 MET D CB  
13132 C CG  . MET D 366 ? 0.6679 0.6124 0.6558 -0.0148 -0.0246 0.0065  667 MET D CG  
13133 S SD  . MET D 366 ? 0.6677 0.6345 0.6621 -0.0163 -0.0268 0.0075  667 MET D SD  
13134 C CE  . MET D 366 ? 0.7286 0.6977 0.7193 -0.0261 -0.0273 0.0033  667 MET D CE  
13135 N N   . GLU D 367 ? 0.6424 0.5357 0.6048 0.0029  -0.0191 -0.0019 668 GLU D N   
13136 C CA  . GLU D 367 ? 0.7837 0.6554 0.7326 0.0013  -0.0170 -0.0078 668 GLU D CA  
13137 C C   . GLU D 367 ? 0.7174 0.5642 0.6563 0.0011  -0.0160 -0.0057 668 GLU D C   
13138 O O   . GLU D 367 ? 0.6953 0.5248 0.6240 -0.0074 -0.0144 -0.0085 668 GLU D O   
13139 C CB  . GLU D 367 ? 0.8952 0.7642 0.8388 0.0113  -0.0157 -0.0136 668 GLU D CB  
13140 C CG  . GLU D 367 ? 0.9511 0.8414 0.9046 0.0206  -0.0167 -0.0122 668 GLU D CG  
13141 C CD  . GLU D 367 ? 0.9988 0.9013 0.9521 0.0223  -0.0155 -0.0185 668 GLU D CD  
13142 O OE1 . GLU D 367 ? 0.9707 0.8754 0.9218 0.0132  -0.0151 -0.0217 668 GLU D OE1 
13143 O OE2 . GLU D 367 ? 1.0194 0.9308 0.9748 0.0327  -0.0149 -0.0204 668 GLU D OE2 
13144 N N   . ASN D 368 ? 0.7673 0.6120 0.7083 0.0093  -0.0169 -0.0006 669 ASN D N   
13145 C CA  . ASN D 368 ? 0.6507 0.4717 0.5812 0.0087  -0.0161 0.0024  669 ASN D CA  
13146 C C   . ASN D 368 ? 0.5822 0.4042 0.5144 -0.0053 -0.0156 0.0050  669 ASN D C   
13147 O O   . ASN D 368 ? 0.6212 0.4219 0.5412 -0.0125 -0.0138 0.0041  669 ASN D O   
13148 C CB  . ASN D 368 ? 0.7625 0.5852 0.6960 0.0198  -0.0177 0.0077  669 ASN D CB  
13149 C CG  . ASN D 368 ? 0.7997 0.5974 0.7209 0.0195  -0.0171 0.0115  669 ASN D CG  
13150 O OD1 . ASN D 368 ? 0.8686 0.6394 0.7740 0.0215  -0.0156 0.0089  669 ASN D OD1 
13151 N ND2 . ASN D 368 ? 0.7034 0.5084 0.6305 0.0165  -0.0180 0.0176  669 ASN D ND2 
13152 N N   . GLU D 369 ? 0.5750 0.4218 0.5216 -0.0094 -0.0172 0.0079  670 GLU D N   
13153 C CA  . GLU D 369 ? 0.5516 0.4039 0.5015 -0.0214 -0.0169 0.0099  670 GLU D CA  
13154 C C   . GLU D 369 ? 0.5975 0.4464 0.5420 -0.0329 -0.0155 0.0044  670 GLU D C   
13155 O O   . GLU D 369 ? 0.5970 0.4391 0.5368 -0.0435 -0.0140 0.0045  670 GLU D O   
13156 C CB  . GLU D 369 ? 0.5466 0.4253 0.5121 -0.0214 -0.0191 0.0135  670 GLU D CB  
13157 C CG  . GLU D 369 ? 0.5608 0.4421 0.5307 -0.0139 -0.0202 0.0189  670 GLU D CG  
13158 C CD  . GLU D 369 ? 0.6152 0.4862 0.5807 -0.0186 -0.0189 0.0223  670 GLU D CD  
13159 O OE1 . GLU D 369 ? 0.6142 0.4987 0.5877 -0.0233 -0.0193 0.0249  670 GLU D OE1 
13160 O OE2 . GLU D 369 ? 0.6528 0.5018 0.6060 -0.0174 -0.0173 0.0224  670 GLU D OE2 
13161 N N   . TYR D 370 ? 0.6093 0.4643 0.5541 -0.0318 -0.0159 -0.0006 671 TYR D N   
13162 C CA  . TYR D 370 ? 0.7405 0.5904 0.6781 -0.0429 -0.0147 -0.0064 671 TYR D CA  
13163 C C   . TYR D 370 ? 0.7119 0.5293 0.6313 -0.0456 -0.0119 -0.0094 671 TYR D C   
13164 O O   . TYR D 370 ? 0.6562 0.4650 0.5684 -0.0586 -0.0103 -0.0115 671 TYR D O   
13165 C CB  . TYR D 370 ? 0.7118 0.5741 0.6519 -0.0411 -0.0156 -0.0114 671 TYR D CB  
13166 C CG  . TYR D 370 ? 0.7641 0.6557 0.7180 -0.0450 -0.0183 -0.0095 671 TYR D CG  
13167 C CD1 . TYR D 370 ? 0.7442 0.6529 0.7098 -0.0374 -0.0204 -0.0043 671 TYR D CD1 
13168 C CD2 . TYR D 370 ? 0.7255 0.6272 0.6798 -0.0563 -0.0189 -0.0129 671 TYR D CD2 
13169 C CE1 . TYR D 370 ? 0.6727 0.6047 0.6487 -0.0403 -0.0230 -0.0021 671 TYR D CE1 
13170 C CE2 . TYR D 370 ? 0.5883 0.5161 0.5542 -0.0584 -0.0218 -0.0107 671 TYR D CE2 
13171 C CZ  . TYR D 370 ? 0.6340 0.5753 0.6101 -0.0499 -0.0239 -0.0051 671 TYR D CZ  
13172 O OH  . TYR D 370 ? 0.5755 0.5392 0.5609 -0.0511 -0.0270 -0.0025 671 TYR D OH  
13173 N N   . ARG D 371 ? 0.6832 0.4821 0.5943 -0.0336 -0.0113 -0.0095 672 ARG D N   
13174 C CA  . ARG D 371 ? 0.7969 0.5610 0.6881 -0.0344 -0.0089 -0.0123 672 ARG D CA  
13175 C C   . ARG D 371 ? 0.8143 0.5637 0.6987 -0.0430 -0.0076 -0.0075 672 ARG D C   
13176 O O   . ARG D 371 ? 0.8861 0.6165 0.7572 -0.0552 -0.0053 -0.0103 672 ARG D O   
13177 C CB  . ARG D 371 ? 1.0316 0.7816 0.9165 -0.0170 -0.0091 -0.0126 672 ARG D CB  
13178 C CG  . ARG D 371 ? 1.2504 0.9665 1.1143 -0.0149 -0.0069 -0.0188 672 ARG D CG  
13179 C CD  . ARG D 371 ? 1.3969 1.1046 1.2567 0.0047  -0.0074 -0.0202 672 ARG D CD  
13180 N NE  . ARG D 371 ? 1.4428 1.1825 1.3193 0.0131  -0.0090 -0.0213 672 ARG D NE  
13181 C CZ  . ARG D 371 ? 1.4090 1.1647 1.2962 0.0256  -0.0109 -0.0169 672 ARG D CZ  
13182 N NH1 . ARG D 371 ? 1.3624 1.1057 1.2455 0.0322  -0.0119 -0.0110 672 ARG D NH1 
13183 N NH2 . ARG D 371 ? 1.3646 1.1490 1.2656 0.0307  -0.0119 -0.0183 672 ARG D NH2 
13184 N N   . CYS D 372 ? 0.7418 0.5003 0.6345 -0.0379 -0.0088 -0.0004 673 CYS D N   
13185 C CA  . CYS D 372 ? 0.8070 0.5494 0.6910 -0.0444 -0.0073 0.0043  673 CYS D CA  
13186 C C   . CYS D 372 ? 0.7334 0.4973 0.6283 -0.0578 -0.0069 0.0066  673 CYS D C   
13187 O O   . CYS D 372 ? 0.7044 0.4561 0.5908 -0.0672 -0.0048 0.0090  673 CYS D O   
13188 C CB  . CYS D 372 ? 0.8479 0.5836 0.7312 -0.0306 -0.0087 0.0105  673 CYS D CB  
13189 S SG  . CYS D 372 ? 0.8454 0.6169 0.7514 -0.0255 -0.0114 0.0160  673 CYS D SG  
13190 N N   . ARG D 373 ? 0.7223 0.5176 0.6347 -0.0586 -0.0088 0.0058  674 ARG D N   
13191 C CA  . ARG D 373 ? 0.5485 0.3669 0.4723 -0.0687 -0.0089 0.0075  674 ARG D CA  
13192 C C   . ARG D 373 ? 0.6796 0.5165 0.6095 -0.0785 -0.0094 0.0022  674 ARG D C   
13193 O O   . ARG D 373 ? 0.6948 0.5498 0.6321 -0.0883 -0.0092 0.0025  674 ARG D O   
13194 C CB  . ARG D 373 ? 0.5253 0.3657 0.4648 -0.0594 -0.0113 0.0128  674 ARG D CB  
13195 C CG  . ARG D 373 ? 0.4837 0.3433 0.4329 -0.0667 -0.0109 0.0156  674 ARG D CG  
13196 C CD  . ARG D 373 ? 0.4592 0.3385 0.4226 -0.0568 -0.0135 0.0197  674 ARG D CD  
13197 N NE  . ARG D 373 ? 0.5360 0.4300 0.5069 -0.0615 -0.0129 0.0225  674 ARG D NE  
13198 C CZ  . ARG D 373 ? 0.5894 0.5039 0.5732 -0.0561 -0.0149 0.0248  674 ARG D CZ  
13199 N NH1 . ARG D 373 ? 0.5780 0.5002 0.5683 -0.0472 -0.0178 0.0251  674 ARG D NH1 
13200 N NH2 . ARG D 373 ? 0.4766 0.4032 0.4659 -0.0598 -0.0139 0.0265  674 ARG D NH2 
13201 N N   . GLY D 374 ? 0.6430 0.4778 0.5702 -0.0758 -0.0102 -0.0029 675 GLY D N   
13202 C CA  . GLY D 374 ? 0.6804 0.5325 0.6120 -0.0853 -0.0111 -0.0080 675 GLY D CA  
13203 C C   . GLY D 374 ? 0.7065 0.5901 0.6553 -0.0802 -0.0145 -0.0062 675 GLY D C   
13204 O O   . GLY D 374 ? 0.7152 0.6183 0.6700 -0.0882 -0.0158 -0.0089 675 GLY D O   
13205 N N   . GLY D 375 ? 0.6355 0.5244 0.5918 -0.0675 -0.0161 -0.0018 676 GLY D N   
13206 C CA  . GLY D 375 ? 0.6848 0.5991 0.6547 -0.0625 -0.0193 0.0002  676 GLY D CA  
13207 C C   . GLY D 375 ? 0.6818 0.6002 0.6592 -0.0521 -0.0203 0.0063  676 GLY D C   
13208 O O   . GLY D 375 ? 0.6136 0.5172 0.5864 -0.0486 -0.0189 0.0090  676 GLY D O   
13209 N N   . CYS D 376 ? 0.6262 0.5641 0.6140 -0.0477 -0.0231 0.0085  677 CYS D N   
13210 C CA  . CYS D 376 ? 0.5333 0.4767 0.5281 -0.0391 -0.0244 0.0139  677 CYS D CA  
13211 C C   . CYS D 376 ? 0.5643 0.5288 0.5688 -0.0380 -0.0275 0.0159  677 CYS D C   
13212 O O   . CYS D 376 ? 0.6299 0.6006 0.6348 -0.0356 -0.0289 0.0148  677 CYS D O   
13213 C CB  . CYS D 376 ? 0.5046 0.4376 0.4954 -0.0301 -0.0240 0.0140  677 CYS D CB  
13214 S SG  . CYS D 376 ? 0.5267 0.4694 0.5259 -0.0212 -0.0259 0.0197  677 CYS D SG  
13215 N N   . PRO D 377 ? 0.5353 0.5110 0.5468 -0.0393 -0.0285 0.0188  678 PRO D N   
13216 C CA  . PRO D 377 ? 0.4496 0.4432 0.4685 -0.0374 -0.0318 0.0208  678 PRO D CA  
13217 C C   . PRO D 377 ? 0.5264 0.5199 0.5471 -0.0294 -0.0333 0.0244  678 PRO D C   
13218 O O   . PRO D 377 ? 0.5262 0.5117 0.5467 -0.0251 -0.0323 0.0268  678 PRO D O   
13219 C CB  . PRO D 377 ? 0.4809 0.4842 0.5060 -0.0392 -0.0320 0.0226  678 PRO D CB  
13220 C CG  . PRO D 377 ? 0.4548 0.4440 0.4767 -0.0387 -0.0290 0.0239  678 PRO D CG  
13221 C CD  . PRO D 377 ? 0.4051 0.3764 0.4174 -0.0403 -0.0268 0.0212  678 PRO D CD  
13222 N N   . ALA D 378 ? 0.5421 0.5447 0.5637 -0.0283 -0.0357 0.0248  679 ALA D N   
13223 C CA  . ALA D 378 ? 0.5343 0.5364 0.5557 -0.0229 -0.0366 0.0276  679 ALA D CA  
13224 C C   . ALA D 378 ? 0.5043 0.5179 0.5274 -0.0223 -0.0400 0.0303  679 ALA D C   
13225 O O   . ALA D 378 ? 0.4171 0.4391 0.4397 -0.0256 -0.0416 0.0285  679 ALA D O   
13226 C CB  . ALA D 378 ? 0.4864 0.4823 0.5025 -0.0222 -0.0348 0.0243  679 ALA D CB  
13227 N N   . ASP D 379 ? 0.4217 0.4348 0.4458 -0.0182 -0.0413 0.0347  680 ASP D N   
13228 C CA  . ASP D 379 ? 0.4147 0.4344 0.4382 -0.0168 -0.0446 0.0385  680 ASP D CA  
13229 C C   . ASP D 379 ? 0.4720 0.4903 0.4910 -0.0168 -0.0444 0.0397  680 ASP D C   
13230 O O   . ASP D 379 ? 0.4655 0.4788 0.4839 -0.0150 -0.0439 0.0422  680 ASP D O   
13231 C CB  . ASP D 379 ? 0.4834 0.5016 0.5098 -0.0128 -0.0461 0.0424  680 ASP D CB  
13232 C CG  . ASP D 379 ? 0.5697 0.5922 0.5938 -0.0103 -0.0500 0.0464  680 ASP D CG  
13233 O OD1 . ASP D 379 ? 0.5958 0.6211 0.6152 -0.0121 -0.0514 0.0473  680 ASP D OD1 
13234 O OD2 . ASP D 379 ? 0.5158 0.5383 0.5420 -0.0061 -0.0516 0.0487  680 ASP D OD2 
13235 N N   . TRP D 380 ? 0.4036 0.4276 0.4191 -0.0197 -0.0448 0.0375  681 TRP D N   
13236 C CA  . TRP D 380 ? 0.3477 0.3735 0.3585 -0.0208 -0.0441 0.0378  681 TRP D CA  
13237 C C   . TRP D 380 ? 0.2779 0.3022 0.2860 -0.0200 -0.0460 0.0438  681 TRP D C   
13238 O O   . TRP D 380 ? 0.3158 0.3389 0.3219 -0.0208 -0.0443 0.0446  681 TRP D O   
13239 C CB  . TRP D 380 ? 0.3731 0.4069 0.3800 -0.0243 -0.0450 0.0352  681 TRP D CB  
13240 C CG  . TRP D 380 ? 0.3959 0.4335 0.3977 -0.0262 -0.0433 0.0334  681 TRP D CG  
13241 C CD1 . TRP D 380 ? 0.2889 0.3271 0.2891 -0.0269 -0.0402 0.0272  681 TRP D CD1 
13242 C CD2 . TRP D 380 ? 0.3758 0.4172 0.3725 -0.0278 -0.0444 0.0376  681 TRP D CD2 
13243 N NE1 . TRP D 380 ? 0.4754 0.5200 0.4711 -0.0284 -0.0391 0.0269  681 TRP D NE1 
13244 C CE2 . TRP D 380 ? 0.3696 0.4166 0.3629 -0.0299 -0.0415 0.0334  681 TRP D CE2 
13245 C CE3 . TRP D 380 ? 0.3506 0.3900 0.3441 -0.0279 -0.0473 0.0444  681 TRP D CE3 
13246 C CZ2 . TRP D 380 ? 0.3893 0.4422 0.3768 -0.0330 -0.0412 0.0359  681 TRP D CZ2 
13247 C CZ3 . TRP D 380 ? 0.4058 0.4481 0.3919 -0.0315 -0.0472 0.0474  681 TRP D CZ3 
13248 C CH2 . TRP D 380 ? 0.4625 0.5126 0.4461 -0.0345 -0.0440 0.0431  681 TRP D CH2 
13249 N N   . VAL D 381 ? 0.4117 0.4362 0.4187 -0.0186 -0.0494 0.0478  682 VAL D N   
13250 C CA  . VAL D 381 ? 0.3990 0.4178 0.4009 -0.0177 -0.0515 0.0537  682 VAL D CA  
13251 C C   . VAL D 381 ? 0.4351 0.4457 0.4386 -0.0168 -0.0496 0.0547  682 VAL D C   
13252 O O   . VAL D 381 ? 0.4702 0.4760 0.4682 -0.0189 -0.0497 0.0581  682 VAL D O   
13253 C CB  . VAL D 381 ? 0.3799 0.3988 0.3813 -0.0137 -0.0556 0.0572  682 VAL D CB  
13254 C CG1 . VAL D 381 ? 0.3921 0.4009 0.3860 -0.0120 -0.0579 0.0633  682 VAL D CG1 
13255 C CG2 . VAL D 381 ? 0.3681 0.3976 0.3678 -0.0150 -0.0579 0.0560  682 VAL D CG2 
13256 N N   . TRP D 382 ? 0.4996 0.5084 0.5096 -0.0145 -0.0479 0.0519  683 TRP D N   
13257 C CA  . TRP D 382 ? 0.4675 0.4700 0.4791 -0.0135 -0.0462 0.0523  683 TRP D CA  
13258 C C   . TRP D 382 ? 0.3844 0.3897 0.3980 -0.0147 -0.0431 0.0487  683 TRP D C   
13259 O O   . TRP D 382 ? 0.4196 0.4233 0.4326 -0.0153 -0.0421 0.0495  683 TRP D O   
13260 C CB  . TRP D 382 ? 0.4603 0.4588 0.4766 -0.0098 -0.0463 0.0520  683 TRP D CB  
13261 C CG  . TRP D 382 ? 0.4789 0.4729 0.4928 -0.0068 -0.0490 0.0557  683 TRP D CG  
13262 C CD1 . TRP D 382 ? 0.5056 0.5025 0.5173 -0.0050 -0.0521 0.0578  683 TRP D CD1 
13263 C CD2 . TRP D 382 ? 0.5552 0.5402 0.5678 -0.0044 -0.0492 0.0578  683 TRP D CD2 
13264 N NE1 . TRP D 382 ? 0.5120 0.5014 0.5207 -0.0006 -0.0542 0.0611  683 TRP D NE1 
13265 C CE2 . TRP D 382 ? 0.6297 0.6110 0.6387 -0.0005 -0.0523 0.0608  683 TRP D CE2 
13266 C CE3 . TRP D 382 ? 0.5905 0.5702 0.6038 -0.0049 -0.0473 0.0570  683 TRP D CE3 
13267 C CZ2 . TRP D 382 ? 0.7088 0.6796 0.7145 0.0031  -0.0531 0.0628  683 TRP D CZ2 
13268 C CZ3 . TRP D 382 ? 0.6290 0.5994 0.6393 -0.0025 -0.0481 0.0589  683 TRP D CZ3 
13269 C CH2 . TRP D 382 ? 0.6143 0.5796 0.6206 0.0016  -0.0508 0.0615  683 TRP D CH2 
13270 N N   . ILE D 383 ? 0.3752 0.3846 0.3904 -0.0147 -0.0416 0.0444  684 ILE D N   
13271 C CA  . ILE D 383 ? 0.3979 0.4085 0.4143 -0.0137 -0.0388 0.0407  684 ILE D CA  
13272 C C   . ILE D 383 ? 0.4869 0.5051 0.5003 -0.0160 -0.0379 0.0406  684 ILE D C   
13273 O O   . ILE D 383 ? 0.5193 0.5405 0.5341 -0.0147 -0.0363 0.0393  684 ILE D O   
13274 C CB  . ILE D 383 ? 0.3721 0.3816 0.3890 -0.0130 -0.0374 0.0359  684 ILE D CB  
13275 C CG1 . ILE D 383 ? 0.4161 0.4193 0.4357 -0.0123 -0.0376 0.0360  684 ILE D CG1 
13276 C CG2 . ILE D 383 ? 0.3844 0.3934 0.4008 -0.0102 -0.0347 0.0320  684 ILE D CG2 
13277 C CD1 . ILE D 383 ? 0.4657 0.4624 0.4873 -0.0093 -0.0366 0.0374  684 ILE D CD1 
13278 N N   . VAL D 384 ? 0.4851 0.5080 0.4943 -0.0195 -0.0390 0.0419  685 VAL D N   
13279 C CA  . VAL D 384 ? 0.4754 0.5069 0.4810 -0.0229 -0.0377 0.0416  685 VAL D CA  
13280 C C   . VAL D 384 ? 0.3778 0.4081 0.3819 -0.0256 -0.0381 0.0458  685 VAL D C   
13281 O O   . VAL D 384 ? 0.4351 0.4569 0.4361 -0.0268 -0.0405 0.0504  685 VAL D O   
13282 C CB  . VAL D 384 ? 0.5289 0.5650 0.5288 -0.0266 -0.0389 0.0425  685 VAL D CB  
13283 C CG1 . VAL D 384 ? 0.2866 0.3316 0.2814 -0.0316 -0.0374 0.0433  685 VAL D CG1 
13284 C CG2 . VAL D 384 ? 0.5371 0.5758 0.5379 -0.0251 -0.0380 0.0371  685 VAL D CG2 
13285 N N   . PRO D 385 ? 0.4242 0.4625 0.4297 -0.0266 -0.0359 0.0439  686 PRO D N   
13286 C CA  . PRO D 385 ? 0.4189 0.4567 0.4227 -0.0307 -0.0362 0.0472  686 PRO D CA  
13287 C C   . PRO D 385 ? 0.5191 0.5541 0.5140 -0.0380 -0.0374 0.0520  686 PRO D C   
13288 O O   . PRO D 385 ? 0.5382 0.5776 0.5288 -0.0404 -0.0373 0.0522  686 PRO D O   
13289 C CB  . PRO D 385 ? 0.3157 0.3682 0.3233 -0.0304 -0.0334 0.0432  686 PRO D CB  
13290 C CG  . PRO D 385 ? 0.4724 0.5268 0.4847 -0.0228 -0.0321 0.0380  686 PRO D CG  
13291 C CD  . PRO D 385 ? 0.4698 0.5173 0.4793 -0.0227 -0.0332 0.0381  686 PRO D CD  
13292 N N   . PRO D 386 ? 0.5224 0.5492 0.5129 -0.0420 -0.0386 0.0560  687 PRO D N   
13293 C CA  . PRO D 386 ? 0.4868 0.5059 0.4662 -0.0489 -0.0400 0.0614  687 PRO D CA  
13294 C C   . PRO D 386 ? 0.4854 0.5161 0.4594 -0.0580 -0.0377 0.0616  687 PRO D C   
13295 O O   . PRO D 386 ? 0.4679 0.4904 0.4304 -0.0652 -0.0387 0.0666  687 PRO D O   
13296 C CB  . PRO D 386 ? 0.4883 0.4926 0.4643 -0.0498 -0.0416 0.0645  687 PRO D CB  
13297 C CG  . PRO D 386 ? 0.4609 0.4744 0.4455 -0.0486 -0.0397 0.0604  687 PRO D CG  
13298 C CD  . PRO D 386 ? 0.4235 0.4467 0.4176 -0.0408 -0.0385 0.0557  687 PRO D CD  
13299 N N   . MET D 387 ? 0.5060 0.5550 0.4869 -0.0579 -0.0346 0.0564  688 MET D N   
13300 C CA  . MET D 387 ? 0.4499 0.5146 0.4269 -0.0659 -0.0318 0.0554  688 MET D CA  
13301 C C   . MET D 387 ? 0.5412 0.6231 0.5260 -0.0601 -0.0293 0.0488  688 MET D C   
13302 O O   . MET D 387 ? 0.4659 0.5473 0.4591 -0.0508 -0.0294 0.0450  688 MET D O   
13303 C CB  . MET D 387 ? 0.4489 0.5217 0.4256 -0.0738 -0.0302 0.0554  688 MET D CB  
13304 C CG  . MET D 387 ? 0.5299 0.6163 0.5188 -0.0674 -0.0289 0.0498  688 MET D CG  
13305 S SD  . MET D 387 ? 0.5597 0.6635 0.5493 -0.0774 -0.0269 0.0486  688 MET D SD  
13306 C CE  . MET D 387 ? 0.5736 0.7030 0.5617 -0.0844 -0.0228 0.0458  688 MET D CE  
13307 N N   . SER D 388 ? 0.5153 0.6113 0.4960 -0.0656 -0.0268 0.0475  689 SER D N   
13308 C CA  . SER D 388 ? 0.4130 0.5266 0.3999 -0.0603 -0.0238 0.0404  689 SER D CA  
13309 C C   . SER D 388 ? 0.4212 0.5258 0.4117 -0.0504 -0.0251 0.0374  689 SER D C   
13310 O O   . SER D 388 ? 0.4925 0.6039 0.4897 -0.0425 -0.0233 0.0312  689 SER D O   
13311 C CB  . SER D 388 ? 0.4098 0.5402 0.4058 -0.0570 -0.0214 0.0354  689 SER D CB  
13312 O OG  . SER D 388 ? 0.5011 0.6411 0.4944 -0.0673 -0.0202 0.0378  689 SER D OG  
13313 N N   . GLY D 389 ? 0.4032 0.4923 0.3884 -0.0510 -0.0282 0.0417  690 GLY D N   
13314 C CA  . GLY D 389 ? 0.3828 0.4631 0.3715 -0.0434 -0.0298 0.0393  690 GLY D CA  
13315 C C   . GLY D 389 ? 0.5059 0.5958 0.4964 -0.0392 -0.0272 0.0320  690 GLY D C   
13316 O O   . GLY D 389 ? 0.4387 0.5259 0.4350 -0.0318 -0.0264 0.0273  690 GLY D O   
13317 N N   . SER D 390 ? 0.4092 0.5091 0.3935 -0.0440 -0.0257 0.0310  691 SER D N   
13318 C CA  . SER D 390 ? 0.4118 0.5181 0.3964 -0.0399 -0.0235 0.0236  691 SER D CA  
13319 C C   . SER D 390 ? 0.4433 0.5630 0.4334 -0.0346 -0.0194 0.0166  691 SER D C   
13320 O O   . SER D 390 ? 0.5114 0.6331 0.5017 -0.0290 -0.0174 0.0096  691 SER D O   
13321 C CB  . SER D 390 ? 0.4411 0.5542 0.4166 -0.0462 -0.0233 0.0240  691 SER D CB  
13322 O OG  . SER D 390 ? 0.3662 0.4943 0.3382 -0.0525 -0.0204 0.0246  691 SER D OG  
13323 N N   . ILE D 391 ? 0.5149 0.6437 0.5091 -0.0356 -0.0182 0.0179  692 ILE D N   
13324 C CA  . ILE D 391 ? 0.5070 0.6493 0.5075 -0.0281 -0.0150 0.0110  692 ILE D CA  
13325 C C   . ILE D 391 ? 0.3923 0.5225 0.3992 -0.0188 -0.0165 0.0101  692 ILE D C   
13326 O O   . ILE D 391 ? 0.4019 0.5410 0.4140 -0.0110 -0.0148 0.0055  692 ILE D O   
13327 C CB  . ILE D 391 ? 0.5444 0.7084 0.5467 -0.0335 -0.0125 0.0111  692 ILE D CB  
13328 C CG1 . ILE D 391 ? 0.5390 0.6981 0.5435 -0.0382 -0.0148 0.0175  692 ILE D CG1 
13329 C CG2 . ILE D 391 ? 0.5197 0.6962 0.5142 -0.0432 -0.0103 0.0117  692 ILE D CG2 
13330 C CD1 . ILE D 391 ? 0.4918 0.6733 0.5011 -0.0409 -0.0125 0.0158  692 ILE D CD1 
13331 N N   . THR D 392 ? 0.4027 0.5133 0.4087 -0.0190 -0.0198 0.0143  693 THR D N   
13332 C CA  . THR D 392 ? 0.5108 0.6087 0.5212 -0.0107 -0.0209 0.0132  693 THR D CA  
13333 C C   . THR D 392 ? 0.4964 0.5803 0.5035 -0.0073 -0.0212 0.0098  693 THR D C   
13334 O O   . THR D 392 ? 0.4856 0.5670 0.4880 -0.0128 -0.0220 0.0107  693 THR D O   
13335 C CB  . THR D 392 ? 0.4768 0.5641 0.4894 -0.0130 -0.0239 0.0197  693 THR D CB  
13336 O OG1 . THR D 392 ? 0.5063 0.5811 0.5151 -0.0176 -0.0264 0.0238  693 THR D OG1 
13337 C CG2 . THR D 392 ? 0.4224 0.5217 0.4360 -0.0191 -0.0237 0.0231  693 THR D CG2 
13338 N N   . PRO D 393 ? 0.4569 0.5313 0.4652 0.0012  -0.0205 0.0059  694 PRO D N   
13339 C CA  . PRO D 393 ? 0.4859 0.5475 0.4892 0.0032  -0.0200 0.0013  694 PRO D CA  
13340 C C   . PRO D 393 ? 0.5159 0.5643 0.5177 -0.0025 -0.0227 0.0051  694 PRO D C   
13341 O O   . PRO D 393 ? 0.4963 0.5396 0.4933 -0.0048 -0.0225 0.0018  694 PRO D O   
13342 C CB  . PRO D 393 ? 0.4229 0.4751 0.4264 0.0136  -0.0188 -0.0028 694 PRO D CB  
13343 C CG  . PRO D 393 ? 0.4900 0.5463 0.4997 0.0160  -0.0201 0.0019  694 PRO D CG  
13344 C CD  . PRO D 393 ? 0.4121 0.4878 0.4249 0.0094  -0.0201 0.0048  694 PRO D CD  
13345 N N   . VAL D 394 ? 0.5335 0.5776 0.5388 -0.0048 -0.0252 0.0115  695 VAL D N   
13346 C CA  . VAL D 394 ? 0.5039 0.5385 0.5085 -0.0092 -0.0276 0.0147  695 VAL D CA  
13347 C C   . VAL D 394 ? 0.4699 0.5117 0.4712 -0.0158 -0.0292 0.0164  695 VAL D C   
13348 O O   . VAL D 394 ? 0.3359 0.3731 0.3356 -0.0188 -0.0310 0.0167  695 VAL D O   
13349 C CB  . VAL D 394 ? 0.5336 0.5629 0.5425 -0.0092 -0.0297 0.0206  695 VAL D CB  
13350 C CG1 . VAL D 394 ? 0.4248 0.4442 0.4356 -0.0031 -0.0288 0.0193  695 VAL D CG1 
13351 C CG2 . VAL D 394 ? 0.2790 0.3177 0.2894 -0.0116 -0.0303 0.0249  695 VAL D CG2 
13352 N N   . PHE D 395 ? 0.4255 0.4794 0.4251 -0.0186 -0.0286 0.0177  696 PHE D N   
13353 C CA  . PHE D 395 ? 0.3692 0.4288 0.3637 -0.0248 -0.0303 0.0201  696 PHE D CA  
13354 C C   . PHE D 395 ? 0.4645 0.5239 0.4547 -0.0258 -0.0298 0.0146  696 PHE D C   
13355 O O   . PHE D 395 ? 0.4993 0.5588 0.4866 -0.0298 -0.0326 0.0167  696 PHE D O   
13356 C CB  . PHE D 395 ? 0.3990 0.4712 0.3906 -0.0285 -0.0288 0.0218  696 PHE D CB  
13357 C CG  . PHE D 395 ? 0.4779 0.5547 0.4622 -0.0349 -0.0306 0.0252  696 PHE D CG  
13358 C CD1 . PHE D 395 ? 0.4875 0.5714 0.4666 -0.0368 -0.0295 0.0206  696 PHE D CD1 
13359 C CD2 . PHE D 395 ? 0.4156 0.4887 0.3969 -0.0389 -0.0336 0.0330  696 PHE D CD2 
13360 C CE1 . PHE D 395 ? 0.4654 0.5537 0.4367 -0.0427 -0.0315 0.0242  696 PHE D CE1 
13361 C CE2 . PHE D 395 ? 0.4723 0.5479 0.4451 -0.0442 -0.0357 0.0370  696 PHE D CE2 
13362 C CZ  . PHE D 395 ? 0.4497 0.5337 0.4178 -0.0461 -0.0347 0.0328  696 PHE D CZ  
13363 N N   . HIS D 396 ? 0.5083 0.5674 0.4975 -0.0219 -0.0266 0.0073  697 HIS D N   
13364 C CA  . HIS D 396 ? 0.4526 0.5107 0.4361 -0.0234 -0.0257 0.0009  697 HIS D CA  
13365 C C   . HIS D 396 ? 0.5139 0.5574 0.4972 -0.0225 -0.0262 -0.0022 697 HIS D C   
13366 O O   . HIS D 396 ? 0.3864 0.4265 0.3640 -0.0242 -0.0251 -0.0085 697 HIS D O   
13367 C CB  . HIS D 396 ? 0.4512 0.5162 0.4319 -0.0196 -0.0216 -0.0061 697 HIS D CB  
13368 C CG  . HIS D 396 ? 0.4704 0.5510 0.4524 -0.0206 -0.0203 -0.0033 697 HIS D CG  
13369 N ND1 . HIS D 396 ? 0.4783 0.5715 0.4550 -0.0267 -0.0201 -0.0026 697 HIS D ND1 
13370 C CD2 . HIS D 396 ? 0.4965 0.5827 0.4840 -0.0176 -0.0194 -0.0008 697 HIS D CD2 
13371 C CE1 . HIS D 396 ? 0.5248 0.6303 0.5034 -0.0279 -0.0186 0.0002  697 HIS D CE1 
13372 N NE2 . HIS D 396 ? 0.4420 0.5441 0.4275 -0.0226 -0.0182 0.0011  697 HIS D NE2 
13373 N N   . GLN D 397 ? 0.4537 0.4886 0.4422 -0.0207 -0.0275 0.0019  698 GLN D N   
13374 C CA  . GLN D 397 ? 0.4436 0.4646 0.4316 -0.0209 -0.0276 -0.0002 698 GLN D CA  
13375 C C   . GLN D 397 ? 0.4639 0.4871 0.4538 -0.0268 -0.0311 0.0035  698 GLN D C   
13376 O O   . GLN D 397 ? 0.5414 0.5676 0.5363 -0.0266 -0.0334 0.0100  698 GLN D O   
13377 C CB  . GLN D 397 ? 0.4879 0.4991 0.4799 -0.0152 -0.0268 0.0019  698 GLN D CB  
13378 C CG  . GLN D 397 ? 0.5119 0.5085 0.5025 -0.0167 -0.0268 0.0008  698 GLN D CG  
13379 C CD  . GLN D 397 ? 0.4857 0.4703 0.4680 -0.0163 -0.0242 -0.0069 698 GLN D CD  
13380 O OE1 . GLN D 397 ? 0.5326 0.5133 0.5116 -0.0096 -0.0219 -0.0107 698 GLN D OE1 
13381 N NE2 . GLN D 397 ? 0.4524 0.4310 0.4308 -0.0233 -0.0247 -0.0095 698 GLN D NE2 
13382 N N   . GLU D 398 ? 0.4206 0.4424 0.4062 -0.0319 -0.0314 -0.0010 699 GLU D N   
13383 C CA  . GLU D 398 ? 0.4122 0.4375 0.4004 -0.0370 -0.0345 0.0014  699 GLU D CA  
13384 C C   . GLU D 398 ? 0.4966 0.5121 0.4893 -0.0359 -0.0341 0.0035  699 GLU D C   
13385 O O   . GLU D 398 ? 0.3894 0.3911 0.3795 -0.0339 -0.0313 0.0004  699 GLU D O   
13386 C CB  . GLU D 398 ? 0.4072 0.4341 0.3894 -0.0437 -0.0346 -0.0049 699 GLU D CB  
13387 C CG  . GLU D 398 ? 0.4133 0.4548 0.3921 -0.0466 -0.0368 -0.0050 699 GLU D CG  
13388 C CD  . GLU D 398 ? 0.5439 0.5872 0.5159 -0.0535 -0.0368 -0.0122 699 GLU D CD  
13389 O OE1 . GLU D 398 ? 0.6081 0.6641 0.5764 -0.0566 -0.0389 -0.0125 699 GLU D OE1 
13390 O OE2 . GLU D 398 ? 0.5310 0.5621 0.5001 -0.0565 -0.0347 -0.0177 699 GLU D OE2 
13391 N N   . MET D 399 ? 0.5276 0.5499 0.5262 -0.0369 -0.0371 0.0087  700 MET D N   
13392 C CA  . MET D 399 ? 0.4829 0.4988 0.4863 -0.0358 -0.0368 0.0114  700 MET D CA  
13393 C C   . MET D 399 ? 0.5013 0.5267 0.5086 -0.0403 -0.0393 0.0123  700 MET D C   
13394 O O   . MET D 399 ? 0.6065 0.6449 0.6156 -0.0404 -0.0427 0.0150  700 MET D O   
13395 C CB  . MET D 399 ? 0.4008 0.4165 0.4087 -0.0298 -0.0374 0.0175  700 MET D CB  
13396 C CG  . MET D 399 ? 0.3879 0.3966 0.3939 -0.0250 -0.0349 0.0168  700 MET D CG  
13397 S SD  . MET D 399 ? 0.4739 0.4870 0.4842 -0.0210 -0.0365 0.0237  700 MET D SD  
13398 C CE  . MET D 399 ? 0.3830 0.3956 0.3909 -0.0170 -0.0337 0.0213  700 MET D CE  
13399 N N   . LEU D 400 ? 0.4291 0.4486 0.4371 -0.0440 -0.0377 0.0103  701 LEU D N   
13400 C CA  . LEU D 400 ? 0.5121 0.5432 0.5251 -0.0482 -0.0396 0.0109  701 LEU D CA  
13401 C C   . LEU D 400 ? 0.5193 0.5505 0.5389 -0.0434 -0.0399 0.0161  701 LEU D C   
13402 O O   . LEU D 400 ? 0.3781 0.3962 0.3967 -0.0414 -0.0371 0.0168  701 LEU D O   
13403 C CB  . LEU D 400 ? 0.5024 0.5289 0.5114 -0.0573 -0.0373 0.0051  701 LEU D CB  
13404 C CG  . LEU D 400 ? 0.4912 0.5206 0.4938 -0.0637 -0.0377 -0.0008 701 LEU D CG  
13405 C CD1 . LEU D 400 ? 0.5619 0.5830 0.5592 -0.0736 -0.0350 -0.0063 701 LEU D CD1 
13406 C CD2 . LEU D 400 ? 0.4161 0.4679 0.4231 -0.0644 -0.0423 0.0007  701 LEU D CD2 
13407 N N   . ASN D 401 ? 0.5491 0.5949 0.5747 -0.0411 -0.0432 0.0194  702 ASN D N   
13408 C CA  . ASN D 401 ? 0.5143 0.5610 0.5456 -0.0358 -0.0436 0.0238  702 ASN D CA  
13409 C C   . ASN D 401 ? 0.5533 0.6127 0.5902 -0.0395 -0.0439 0.0223  702 ASN D C   
13410 O O   . ASN D 401 ? 0.4495 0.5250 0.4886 -0.0423 -0.0466 0.0206  702 ASN D O   
13411 C CB  . ASN D 401 ? 0.3752 0.4264 0.4078 -0.0285 -0.0472 0.0291  702 ASN D CB  
13412 C CG  . ASN D 401 ? 0.4939 0.5408 0.5301 -0.0226 -0.0470 0.0330  702 ASN D CG  
13413 O OD1 . ASN D 401 ? 0.5612 0.5996 0.5981 -0.0233 -0.0438 0.0322  702 ASN D OD1 
13414 N ND2 . ASN D 401 ? 0.4824 0.5337 0.5196 -0.0166 -0.0503 0.0373  702 ASN D ND2 
13415 N N   . TYR D 402 ? 0.4740 0.5277 0.5131 -0.0398 -0.0411 0.0227  703 TYR D N   
13416 C CA  . TYR D 402 ? 0.3731 0.4400 0.4179 -0.0435 -0.0405 0.0212  703 TYR D CA  
13417 C C   . TYR D 402 ? 0.5157 0.5739 0.5619 -0.0406 -0.0377 0.0235  703 TYR D C   
13418 O O   . TYR D 402 ? 0.5049 0.5461 0.5469 -0.0373 -0.0361 0.0254  703 TYR D O   
13419 C CB  . TYR D 402 ? 0.4028 0.4725 0.4446 -0.0553 -0.0384 0.0156  703 TYR D CB  
13420 C CG  . TYR D 402 ? 0.4869 0.5340 0.5192 -0.0601 -0.0348 0.0133  703 TYR D CG  
13421 C CD1 . TYR D 402 ? 0.4171 0.4505 0.4460 -0.0631 -0.0308 0.0134  703 TYR D CD1 
13422 C CD2 . TYR D 402 ? 0.4242 0.4632 0.4499 -0.0609 -0.0353 0.0110  703 TYR D CD2 
13423 C CE1 . TYR D 402 ? 0.4716 0.4823 0.4903 -0.0660 -0.0279 0.0117  703 TYR D CE1 
13424 C CE2 . TYR D 402 ? 0.4660 0.4837 0.4824 -0.0635 -0.0320 0.0085  703 TYR D CE2 
13425 C CZ  . TYR D 402 ? 0.5457 0.5484 0.5583 -0.0655 -0.0285 0.0090  703 TYR D CZ  
13426 O OH  . TYR D 402 ? 0.4649 0.4447 0.4669 -0.0666 -0.0257 0.0069  703 TYR D OH  
13427 N N   . ARG D 403 ? 0.4412 0.5133 0.4936 -0.0415 -0.0371 0.0230  704 ARG D N   
13428 C CA  . ARG D 403 ? 0.4933 0.5619 0.5483 -0.0368 -0.0353 0.0254  704 ARG D CA  
13429 C C   . ARG D 403 ? 0.5014 0.5681 0.5547 -0.0459 -0.0308 0.0229  704 ARG D C   
13430 O O   . ARG D 403 ? 0.4931 0.5773 0.5509 -0.0520 -0.0300 0.0200  704 ARG D O   
13431 C CB  . ARG D 403 ? 0.5078 0.5938 0.5705 -0.0286 -0.0382 0.0270  704 ARG D CB  
13432 C CG  . ARG D 403 ? 0.7676 0.8502 0.8324 -0.0227 -0.0365 0.0290  704 ARG D CG  
13433 C CD  . ARG D 403 ? 0.8889 0.9825 0.9587 -0.0116 -0.0400 0.0309  704 ARG D CD  
13434 N NE  . ARG D 403 ? 1.0491 1.1281 1.1140 -0.0044 -0.0428 0.0349  704 ARG D NE  
13435 C CZ  . ARG D 403 ? 1.1266 1.1883 1.1872 -0.0014 -0.0415 0.0372  704 ARG D CZ  
13436 N NH1 . ARG D 403 ? 1.1558 1.2120 1.2160 -0.0041 -0.0376 0.0363  704 ARG D NH1 
13437 N NH2 . ARG D 403 ? 1.1552 1.2055 1.2109 0.0035  -0.0440 0.0405  704 ARG D NH2 
13438 N N   . LEU D 404 ? 0.4275 0.4734 0.4737 -0.0472 -0.0278 0.0241  705 LEU D N   
13439 C CA  . LEU D 404 ? 0.4049 0.4444 0.4470 -0.0551 -0.0234 0.0230  705 LEU D CA  
13440 C C   . LEU D 404 ? 0.4610 0.5006 0.5057 -0.0495 -0.0220 0.0258  705 LEU D C   
13441 O O   . LEU D 404 ? 0.4154 0.4526 0.4624 -0.0397 -0.0241 0.0286  705 LEU D O   
13442 C CB  . LEU D 404 ? 0.3420 0.3568 0.3726 -0.0593 -0.0212 0.0227  705 LEU D CB  
13443 C CG  . LEU D 404 ? 0.4994 0.5075 0.5243 -0.0641 -0.0220 0.0195  705 LEU D CG  
13444 C CD1 . LEU D 404 ? 0.5025 0.4839 0.5160 -0.0634 -0.0201 0.0200  705 LEU D CD1 
13445 C CD2 . LEU D 404 ? 0.5730 0.5923 0.5976 -0.0767 -0.0206 0.0150  705 LEU D CD2 
13446 N N   . THR D 405 ? 0.5042 0.5453 0.5471 -0.0567 -0.0182 0.0249  706 THR D N   
13447 C CA  . THR D 405 ? 0.4917 0.5319 0.5354 -0.0528 -0.0162 0.0271  706 THR D CA  
13448 C C   . THR D 405 ? 0.4415 0.4616 0.4742 -0.0592 -0.0123 0.0284  706 THR D C   
13449 O O   . THR D 405 ? 0.3356 0.3471 0.3610 -0.0691 -0.0104 0.0268  706 THR D O   
13450 C CB  . THR D 405 ? 0.4880 0.5538 0.5407 -0.0540 -0.0151 0.0248  706 THR D CB  
13451 O OG1 . THR D 405 ? 0.6015 0.6666 0.6545 -0.0495 -0.0130 0.0265  706 THR D OG1 
13452 C CG2 . THR D 405 ? 0.2939 0.3697 0.3454 -0.0681 -0.0119 0.0213  706 THR D CG2 
13453 N N   . PRO D 406 ? 0.5240 0.5340 0.5535 -0.0537 -0.0114 0.0316  707 PRO D N   
13454 C CA  . PRO D 406 ? 0.4655 0.4792 0.5000 -0.0428 -0.0133 0.0335  707 PRO D CA  
13455 C C   . PRO D 406 ? 0.4841 0.4957 0.5217 -0.0345 -0.0177 0.0344  707 PRO D C   
13456 O O   . PRO D 406 ? 0.4949 0.4959 0.5283 -0.0357 -0.0189 0.0345  707 PRO D O   
13457 C CB  . PRO D 406 ? 0.4845 0.4804 0.5101 -0.0419 -0.0114 0.0366  707 PRO D CB  
13458 C CG  . PRO D 406 ? 0.5514 0.5400 0.5689 -0.0527 -0.0076 0.0363  707 PRO D CG  
13459 C CD  . PRO D 406 ? 0.5018 0.4925 0.5194 -0.0596 -0.0080 0.0334  707 PRO D CD  
13460 N N   . SER D 407 ? 0.5088 0.5297 0.5527 -0.0264 -0.0199 0.0349  708 SER D N   
13461 C CA  . SER D 407 ? 0.5899 0.6076 0.6351 -0.0195 -0.0239 0.0363  708 SER D CA  
13462 C C   . SER D 407 ? 0.5291 0.5449 0.5752 -0.0113 -0.0250 0.0380  708 SER D C   
13463 O O   . SER D 407 ? 0.6115 0.6335 0.6595 -0.0099 -0.0231 0.0373  708 SER D O   
13464 C CB  . SER D 407 ? 0.6148 0.6471 0.6659 -0.0190 -0.0266 0.0347  708 SER D CB  
13465 O OG  . SER D 407 ? 0.6477 0.6962 0.7055 -0.0147 -0.0271 0.0336  708 SER D OG  
13466 N N   . PHE D 408 ? 0.4441 0.4512 0.4880 -0.0067 -0.0277 0.0400  709 PHE D N   
13467 C CA  . PHE D 408 ? 0.3431 0.3479 0.3870 0.0003  -0.0295 0.0413  709 PHE D CA  
13468 C C   . PHE D 408 ? 0.4389 0.4530 0.4868 0.0049  -0.0326 0.0412  709 PHE D C   
13469 O O   . PHE D 408 ? 0.4859 0.5048 0.5353 0.0030  -0.0343 0.0410  709 PHE D O   
13470 C CB  . PHE D 408 ? 0.3165 0.3080 0.3552 0.0016  -0.0309 0.0435  709 PHE D CB  
13471 C CG  . PHE D 408 ? 0.4003 0.3834 0.4346 -0.0004 -0.0286 0.0441  709 PHE D CG  
13472 C CD1 . PHE D 408 ? 0.4689 0.4505 0.5016 0.0014  -0.0272 0.0440  709 PHE D CD1 
13473 C CD2 . PHE D 408 ? 0.3466 0.3232 0.3776 -0.0036 -0.0280 0.0446  709 PHE D CD2 
13474 C CE1 . PHE D 408 ? 0.4833 0.4577 0.5111 -0.0004 -0.0255 0.0449  709 PHE D CE1 
13475 C CE2 . PHE D 408 ? 0.4230 0.3916 0.4490 -0.0043 -0.0265 0.0456  709 PHE D CE2 
13476 C CZ  . PHE D 408 ? 0.4528 0.4207 0.4772 -0.0029 -0.0254 0.0460  709 PHE D CZ  
13477 N N   . GLU D 409 ? 0.4633 0.4799 0.5123 0.0115  -0.0332 0.0410  710 GLU D N   
13478 C CA  . GLU D 409 ? 0.4325 0.4583 0.4847 0.0179  -0.0361 0.0408  710 GLU D CA  
13479 C C   . GLU D 409 ? 0.5217 0.5355 0.5687 0.0254  -0.0382 0.0425  710 GLU D C   
13480 O O   . GLU D 409 ? 0.5691 0.5730 0.6121 0.0258  -0.0365 0.0424  710 GLU D O   
13481 C CB  . GLU D 409 ? 0.3883 0.4327 0.4475 0.0196  -0.0345 0.0377  710 GLU D CB  
13482 C CG  . GLU D 409 ? 0.5105 0.5677 0.5741 0.0106  -0.0321 0.0354  710 GLU D CG  
13483 C CD  . GLU D 409 ? 0.6972 0.7625 0.7631 0.0080  -0.0350 0.0354  710 GLU D CD  
13484 O OE1 . GLU D 409 ? 0.6766 0.7435 0.7426 0.0149  -0.0391 0.0370  710 GLU D OE1 
13485 O OE2 . GLU D 409 ? 0.6885 0.7574 0.7549 -0.0011 -0.0331 0.0339  710 GLU D OE2 
13486 N N   . TYR D 410 ? 0.5200 0.5339 0.5657 0.0310  -0.0420 0.0442  711 TYR D N   
13487 C CA  . TYR D 410 ? 0.5692 0.5704 0.6084 0.0387  -0.0440 0.0456  711 TYR D CA  
13488 C C   . TYR D 410 ? 0.4937 0.5034 0.5362 0.0471  -0.0431 0.0427  711 TYR D C   
13489 O O   . TYR D 410 ? 0.4947 0.5239 0.5454 0.0483  -0.0424 0.0403  711 TYR D O   
13490 C CB  . TYR D 410 ? 0.5652 0.5608 0.5995 0.0422  -0.0484 0.0490  711 TYR D CB  
13491 C CG  . TYR D 410 ? 0.6979 0.6884 0.7294 0.0344  -0.0492 0.0514  711 TYR D CG  
13492 C CD1 . TYR D 410 ? 0.7868 0.7623 0.8116 0.0298  -0.0485 0.0530  711 TYR D CD1 
13493 C CD2 . TYR D 410 ? 0.8444 0.8467 0.8796 0.0316  -0.0507 0.0517  711 TYR D CD2 
13494 C CE1 . TYR D 410 ? 0.9081 0.8815 0.9308 0.0233  -0.0489 0.0547  711 TYR D CE1 
13495 C CE2 . TYR D 410 ? 0.9627 0.9611 0.9950 0.0251  -0.0511 0.0533  711 TYR D CE2 
13496 C CZ  . TYR D 410 ? 0.9658 0.9503 0.9921 0.0213  -0.0501 0.0548  711 TYR D CZ  
13497 O OH  . TYR D 410 ? 1.0214 1.0046 1.0453 0.0154  -0.0502 0.0558  711 TYR D OH  
13498 N N   . GLN D 411 ? 0.5010 0.4966 0.5368 0.0527  -0.0431 0.0425  712 GLN D N   
13499 C CA  . GLN D 411 ? 0.5963 0.5975 0.6335 0.0628  -0.0425 0.0394  712 GLN D CA  
13500 C C   . GLN D 411 ? 0.5336 0.5141 0.5598 0.0712  -0.0456 0.0412  712 GLN D C   
13501 O O   . GLN D 411 ? 0.5629 0.5241 0.5800 0.0665  -0.0468 0.0442  712 GLN D O   
13502 C CB  . GLN D 411 ? 0.5403 0.5448 0.5794 0.0601  -0.0376 0.0358  712 GLN D CB  
13503 C CG  . GLN D 411 ? 0.5873 0.5724 0.6180 0.0545  -0.0363 0.0367  712 GLN D CG  
13504 C CD  . GLN D 411 ? 0.5224 0.5123 0.5546 0.0513  -0.0318 0.0335  712 GLN D CD  
13505 O OE1 . GLN D 411 ? 0.4303 0.4348 0.4678 0.0553  -0.0293 0.0301  712 GLN D OE1 
13506 N NE2 . GLN D 411 ? 0.4361 0.4150 0.4633 0.0439  -0.0307 0.0347  712 GLN D NE2 
13507 N N   . PRO D 412 ? 0.5696 0.5533 0.5954 0.0837  -0.0469 0.0394  713 PRO D N   
13508 C CA  . PRO D 412 ? 0.6464 0.6060 0.6590 0.0923  -0.0498 0.0410  713 PRO D CA  
13509 C C   . PRO D 412 ? 0.6175 0.5564 0.6208 0.0879  -0.0472 0.0396  713 PRO D C   
13510 O O   . PRO D 412 ? 0.6051 0.5513 0.6130 0.0825  -0.0431 0.0364  713 PRO D O   
13511 C CB  . PRO D 412 ? 0.6848 0.6555 0.7005 0.1078  -0.0508 0.0379  713 PRO D CB  
13512 C CG  . PRO D 412 ? 0.6566 0.6579 0.6874 0.1055  -0.0471 0.0336  713 PRO D CG  
13513 C CD  . PRO D 412 ? 0.6133 0.6232 0.6502 0.0908  -0.0461 0.0357  713 PRO D CD  
13514 N N   . ASP D 413 ? 0.6653 0.5778 0.6544 0.0892  -0.0497 0.0423  714 ASP D N   
13515 C CA  . ASP D 413 ? 0.6672 0.5582 0.6453 0.0854  -0.0479 0.0406  714 ASP D CA  
13516 C C   . ASP D 413 ? 0.7702 0.6623 0.7479 0.0953  -0.0454 0.0348  714 ASP D C   
13517 O O   . ASP D 413 ? 0.7516 0.6483 0.7302 0.1088  -0.0468 0.0333  714 ASP D O   
13518 C CB  . ASP D 413 ? 0.7061 0.5680 0.6675 0.0851  -0.0513 0.0445  714 ASP D CB  
13519 C CG  . ASP D 413 ? 0.8093 0.6700 0.7699 0.0736  -0.0529 0.0497  714 ASP D CG  
13520 O OD1 . ASP D 413 ? 0.7905 0.6643 0.7596 0.0634  -0.0507 0.0493  714 ASP D OD1 
13521 O OD2 . ASP D 413 ? 0.9045 0.7509 0.8554 0.0752  -0.0565 0.0541  714 ASP D OD2 
13522 N N   . PRO D 414 ? 0.7178 0.6061 0.6935 0.0895  -0.0417 0.0313  715 PRO D N   
13523 C CA  . PRO D 414 ? 0.7090 0.6035 0.6861 0.0980  -0.0385 0.0252  715 PRO D CA  
13524 C C   . PRO D 414 ? 0.7246 0.5979 0.6888 0.1111  -0.0402 0.0230  715 PRO D C   
13525 O O   . PRO D 414 ? 0.6812 0.5641 0.6485 0.1232  -0.0386 0.0181  715 PRO D O   
13526 C CB  . PRO D 414 ? 0.6127 0.5043 0.5876 0.0871  -0.0349 0.0229  715 PRO D CB  
13527 C CG  . PRO D 414 ? 0.5826 0.4718 0.5582 0.0738  -0.0363 0.0279  715 PRO D CG  
13528 C CD  . PRO D 414 ? 0.6533 0.5313 0.6240 0.0759  -0.0407 0.0326  715 PRO D CD  
13529 N N   . TRP D 415 ? 0.7388 0.5828 0.6876 0.1091  -0.0432 0.0261  716 TRP D N   
13530 C CA  . TRP D 415 ? 0.7548 0.5729 0.6880 0.1213  -0.0450 0.0243  716 TRP D CA  
13531 C C   . TRP D 415 ? 0.8441 0.6656 0.7784 0.1363  -0.0490 0.0268  716 TRP D C   
13532 O O   . TRP D 415 ? 0.8784 0.6782 0.7994 0.1493  -0.0510 0.0256  716 TRP D O   
13533 C CB  . TRP D 415 ? 0.7715 0.5556 0.6860 0.1121  -0.0467 0.0271  716 TRP D CB  
13534 C CG  . TRP D 415 ? 0.7958 0.5766 0.7093 0.1026  -0.0499 0.0344  716 TRP D CG  
13535 C CD1 . TRP D 415 ? 0.8150 0.5837 0.7211 0.1086  -0.0543 0.0396  716 TRP D CD1 
13536 C CD2 . TRP D 415 ? 0.7636 0.5535 0.6829 0.0859  -0.0490 0.0372  716 TRP D CD2 
13537 N NE1 . TRP D 415 ? 0.7867 0.5570 0.6937 0.0958  -0.0558 0.0453  716 TRP D NE1 
13538 C CE2 . TRP D 415 ? 0.8124 0.5961 0.7279 0.0822  -0.0525 0.0437  716 TRP D CE2 
13539 C CE3 . TRP D 415 ? 0.8098 0.6126 0.7366 0.0746  -0.0457 0.0349  716 TRP D CE3 
13540 C CZ2 . TRP D 415 ? 0.8167 0.6079 0.7364 0.0677  -0.0525 0.0472  716 TRP D CZ2 
13541 C CZ3 . TRP D 415 ? 0.8285 0.6381 0.7594 0.0612  -0.0461 0.0387  716 TRP D CZ3 
13542 C CH2 . TRP D 415 ? 0.8397 0.6440 0.7674 0.0579  -0.0492 0.0444  716 TRP D CH2 
13543 N N   . ASN D 416 ? 0.8504 0.6977 0.7992 0.1351  -0.0504 0.0301  717 ASN D N   
13544 C CA  . ASN D 416 ? 0.8474 0.7059 0.8003 0.1502  -0.0540 0.0314  717 ASN D CA  
13545 C C   . ASN D 416 ? 0.8085 0.6982 0.7763 0.1607  -0.0513 0.0253  717 ASN D C   
13546 O O   . ASN D 416 ? 0.8674 0.7651 0.8368 0.1770  -0.0539 0.0244  717 ASN D O   
13547 C CB  . ASN D 416 ? 0.7762 0.6471 0.7360 0.1434  -0.0573 0.0378  717 ASN D CB  
13548 C CG  . ASN D 416 ? 0.7457 0.5870 0.6897 0.1348  -0.0603 0.0441  717 ASN D CG  
13549 O OD1 . ASN D 416 ? 0.7546 0.5639 0.6804 0.1388  -0.0617 0.0448  717 ASN D OD1 
13550 N ND2 . ASN D 416 ? 0.7337 0.5851 0.6838 0.1225  -0.0611 0.0484  717 ASN D ND2 
13551 N N   . THR D 417 ? 0.7708 0.6786 0.7489 0.1519  -0.0461 0.0211  718 THR D N   
13552 C CA  . THR D 417 ? 0.8023 0.7419 0.7946 0.1590  -0.0426 0.0152  718 THR D CA  
13553 C C   . THR D 417 ? 0.8133 0.7471 0.8007 0.1634  -0.0380 0.0081  718 THR D C   
13554 O O   . THR D 417 ? 0.8720 0.8246 0.8657 0.1761  -0.0361 0.0026  718 THR D O   
13555 C CB  . THR D 417 ? 0.8417 0.8106 0.8502 0.1449  -0.0398 0.0159  718 THR D CB  
13556 O OG1 . THR D 417 ? 0.9453 0.9164 0.9565 0.1392  -0.0439 0.0221  718 THR D OG1 
13557 C CG2 . THR D 417 ? 0.8760 0.8809 0.8995 0.1517  -0.0370 0.0107  718 THR D CG2 
13558 N N   . HIS D 418 ? 0.7932 0.7033 0.7694 0.1534  -0.0361 0.0078  719 HIS D N   
13559 C CA  . HIS D 418 ? 0.8467 0.7543 0.8189 0.1549  -0.0313 0.0009  719 HIS D CA  
13560 C C   . HIS D 418 ? 0.8671 0.7584 0.8280 0.1736  -0.0320 -0.0041 719 HIS D C   
13561 O O   . HIS D 418 ? 0.9728 0.8340 0.9189 0.1797  -0.0362 -0.0014 719 HIS D O   
13562 C CB  . HIS D 418 ? 0.8246 0.7103 0.7864 0.1397  -0.0299 0.0019  719 HIS D CB  
13563 C CG  . HIS D 418 ? 0.8213 0.7050 0.7783 0.1397  -0.0251 -0.0051 719 HIS D CG  
13564 N ND1 . HIS D 418 ? 0.8186 0.7300 0.7873 0.1353  -0.0202 -0.0084 719 HIS D ND1 
13565 C CD2 . HIS D 418 ? 0.8540 0.7112 0.7946 0.1436  -0.0243 -0.0096 719 HIS D CD2 
13566 C CE1 . HIS D 418 ? 0.8404 0.7436 0.8007 0.1365  -0.0166 -0.0146 719 HIS D CE1 
13567 N NE2 . HIS D 418 ? 0.8388 0.7094 0.7823 0.1416  -0.0190 -0.0157 719 HIS D NE2 
13568 N N   . VAL D 419 ? 0.8911 0.8018 0.8582 0.1828  -0.0278 -0.0114 720 VAL D N   
13569 C CA  . VAL D 419 ? 0.9810 0.8760 0.9366 0.2008  -0.0274 -0.0178 720 VAL D CA  
13570 C C   . VAL D 419 ? 0.9416 0.8222 0.8871 0.1946  -0.0226 -0.0237 720 VAL D C   
13571 O O   . VAL D 419 ? 0.8786 0.7818 0.8336 0.1851  -0.0176 -0.0266 720 VAL D O   
13572 C CB  . VAL D 419 ? 0.9975 0.9261 0.9667 0.2183  -0.0263 -0.0228 720 VAL D CB  
13573 C CG1 . VAL D 419 ? 0.9333 0.8696 0.9080 0.2271  -0.0324 -0.0170 720 VAL D CG1 
13574 C CG2 . VAL D 419 ? 0.9380 0.9078 0.9258 0.2090  -0.0205 -0.0261 720 VAL D CG2 
13575 N N   . TRP D 420 ? 0.9526 0.7941 0.8774 0.1990  -0.0241 -0.0254 721 TRP D N   
13576 C CA  . TRP D 420 ? 0.9882 0.8098 0.9000 0.1900  -0.0207 -0.0300 721 TRP D CA  
13577 C C   . TRP D 420 ? 1.0916 0.9210 1.0015 0.2028  -0.0157 -0.0404 721 TRP D C   
13578 O O   . TRP D 420 ? 1.1237 0.9558 1.0331 0.2228  -0.0163 -0.0444 721 TRP D O   
13579 C CB  . TRP D 420 ? 0.9510 0.7260 0.8398 0.1872  -0.0245 -0.0276 721 TRP D CB  
13580 C CG  . TRP D 420 ? 0.8376 0.6052 0.7270 0.1717  -0.0284 -0.0183 721 TRP D CG  
13581 C CD1 . TRP D 420 ? 0.8104 0.5805 0.7045 0.1745  -0.0330 -0.0109 721 TRP D CD1 
13582 C CD2 . TRP D 420 ? 0.7420 0.5008 0.6273 0.1512  -0.0279 -0.0157 721 TRP D CD2 
13583 N NE1 . TRP D 420 ? 0.6423 0.4052 0.5353 0.1568  -0.0351 -0.0042 721 TRP D NE1 
13584 C CE2 . TRP D 420 ? 0.7133 0.4699 0.6014 0.1426  -0.0320 -0.0069 721 TRP D CE2 
13585 C CE3 . TRP D 420 ? 0.7571 0.5111 0.6365 0.1395  -0.0245 -0.0200 721 TRP D CE3 
13586 C CZ2 . TRP D 420 ? 0.7502 0.5011 0.6362 0.1236  -0.0326 -0.0027 721 TRP D CZ2 
13587 C CZ3 . TRP D 420 ? 0.8326 0.5813 0.7101 0.1207  -0.0256 -0.0155 721 TRP D CZ3 
13588 C CH2 . TRP D 420 ? 0.8044 0.5520 0.6855 0.1132  -0.0295 -0.0070 721 TRP D CH2 
13589 N N   . LYS D 421 ? 1.1335 0.9666 1.0416 0.1915  -0.0110 -0.0447 722 LYS D N   
13590 C CA  . LYS D 421 ? 1.1512 0.9925 1.0567 0.2007  -0.0055 -0.0549 722 LYS D CA  
13591 C C   . LYS D 421 ? 1.0675 0.8721 0.9504 0.1974  -0.0044 -0.0603 722 LYS D C   
13592 O O   . LYS D 421 ? 0.9947 0.7689 0.8644 0.1860  -0.0077 -0.0561 722 LYS D O   
13593 C CB  . LYS D 421 ? 1.2062 1.0870 1.1286 0.1906  -0.0001 -0.0561 722 LYS D CB  
13594 C CG  . LYS D 421 ? 1.2276 1.1092 1.1526 0.1679  -0.0006 -0.0494 722 LYS D CG  
13595 C CD  . LYS D 421 ? 1.2117 1.1335 1.1564 0.1595  0.0026  -0.0469 722 LYS D CD  
13596 C CE  . LYS D 421 ? 1.1625 1.1035 1.1223 0.1645  -0.0005 -0.0415 722 LYS D CE  
13597 N NZ  . LYS D 421 ? 1.0810 1.0627 1.0588 0.1597  0.0035  -0.0416 722 LYS D NZ  
# 
